accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
P31232 | TAGL_RAT | Smooth muscle protein 22-alpha | Rattus | MANKGPSYGMSREVQSKIEKKYDEELEERLVEWIVMQCGPDVGRPDRGRLGFQVWLKNGVILSKLVNSLYPEGSKPVKVPENPPSMVFKQMEQVAQFLKAAEDYGVTKTDMFQTVDLFEGKDMAAVQRTVMALGSLAVTKNDGHYRGDPNWFMKKAQEHKREFTDSQLQEGKHVIGLQMGSNRGASQAGMTGYGRPRQIIS | Actin cross-linking/gelling protein. | P31232 |
Q6N223 | UREG_RHOPA | Urease accessory protein UreG | Rhodopseudomonas | MSDHHGPLRVGIGGPVGSGKTALMDLLCKSMRERYDIAAITNDIYTKWDAEFLVRSGSLTPDRIAGVETGGCPHTAIREDASMNLAAVAEMRSKFPGLDLVLIESGGDNLAATFSPELADITIYVIDVAAGDKIPSKGGPGITRSDLLVINKIDLAPYVGASLEKMDTDAKRMRGARPFVMTNLKKSEGLDRIIGFIEEKGGLTPRRSA | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | Q6N223 |
A8G909 | TRUB_SERP5 | tRNA-uridine isomerase | Serratia | MSRPRRRGRDIHGVLLLDKPQGLSSNDALQKVKRLYNANRAGHTGALDPLATGMLPICLGEATKFSQFLLDSDKRYRVIARLGQRTDTSDADGQIVQERPVSFTQAQLDAALDSFRGDIKQVPSMYSALKYQGKKLYEYARQGIEVPREARSITVYELQFIRWEGDELELEIHCSKGTYIRTITDDLGELLGCGAHVIYLRRLQVATYPTERMVTLEQLNELLEQAHRQEIAPAELLDPLLMPMDSPVENYPEVNLLPVVAGYVKQGQPVQVAGAPASGMVRITEGEERKFIGVGDIADDGRVAPRRLVVEYFD | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A8G909 |
A9BJC5 | YIDD_PETMO | Putative membrane protein insertion efficiency factor | Petrotoga | MKKLVLKSIDFYRKHISPATPPKCIYLPTCSSYTYEAVEKFGVFKGLYLGFRRFIRCNPLHKGGYDPVPEKFSFFVHKQGKNKQHRRSV | Could be involved in insertion of integral membrane proteins into the membrane. | A9BJC5 |
Q98PL5 | THIO_MYCPU | Thioredoxin | Mycoplasmopsis | METLLWKDAREKIKKGVNFVEFAAPWCPDCVMMKPVIEQVEQEIKNLNLPVNFYHVNADESGMFRKADAEVAVLRIPTHYIVKDGKQVFIGYEYFPKHILVEKIKELFK | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Q98PL5 |
A6KZL6 | YIDD_PHOV8 | Putative membrane protein insertion efficiency factor | Phocaeicola | MKKILSYLLLLPVYFYRGYISPMTPPSCRFVPTCSEYAIEAIKKHGPFKGLYLAVRRILRCHPWGGSGYDPVP | Could be involved in insertion of integral membrane proteins into the membrane. | A6KZL6 |
P82960 | TXH22_CYRSC | Huwentoxin-II | Cyriopagopus | LFECSFSCEQEKEGDKPCKKKKCKGGWKCKFNMCVKV | Lethal neurotoxin that blocks neuromuscular transmission. Acts cooperatively to potentiate the activity of huwentoxin-I. | P82960 |
Q8T6L5 | TPM_PERFU | Tropomyosin | Periplaneta | MDAIKKKMQAMKLEKDNAMDRALLCEQQARDANLRAEKAEEEARSLQKKIQQIENDLDQTMEQLMQVNAKLDEKDKALQNAESEVAALNRRIQLLEEDLERSEERLATATAKLAEASQAADESERARKILESKGLADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAESGESKIVELEEELRVVGNNLKSLEVSEEKANLREEAYKQQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVHEKEKYKFICDDLDMTFTELIGN | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | Q8T6L5 |
Q96K75 | ZN514_HUMAN | Zinc finger protein 514 | Homo | MTFEDVAVEFSQWEWGQLNPAQKDLYREVMLENFRNLAILGLLVSKPYVICQLEEGGEPFMVEREISTGAHSDWKRRSKSKESMPSWGISKEELFQVVSVEKHIQDVLQFSKLKAACGCDGQLEMQQIKQERHLKQMSTIHKSATTLSRDYKWNGFGRSLGLRSVLVNQHSILMGEGSYKCDTEFRQTLGGNNSQRTHPEKKSCKCNECGKSFHFQSELRRHQRCHTGEKPYECSDCGRAFGHISSLIKHQRTHTGEKPYECSECGRAFSQSSSLVLHYRFHTGEKPYKCNECGRAFGHTSSLIKHQRTHTGEKPYECRECGRTFSQSSSLIVHYRFHTGEKPYKCNKCGRAFSQSSSLTQHYRFHTGEKPYKCNECGRAFAHTASLIKHQRSHAGKKTL | May be involved in transcriptional regulation. | Q96K75 |
Q5XA89 | UVRA_STRP6 | Excinuclease ABC subunit A | Streptococcus | MQNKIIIHGARAHNLKNIDVEIPRDKLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGNMEKPDVDSIDGLSPAISIDQKTTSKNPRSTVGTVTEINDYLRLLYARVGTPYCINGHGAITASSAEQIVEQVLALPERTRMQILAPIVRRKKGQHKTIFEKIQKDGYVRVRVDGDIFDVTEVPELSKSKMHNIEVVIDRLVNKDGIRSRLFDSVEAALRLGDGYLMIDTMDGNELLFSEHYSCPVCGFTVPELEPRLFSFNAPFGSCPTCDGLGIKLEVDLDLVVPDPSKSLKEGALAPWNPISSNYYPTMLEQAMASFGVDMDTPFEALTEEERDLVLYGSGDREFHFHYVNDFGGERNIDIPFEGVVTNVNRRYHETNSDYTRNVMRGYMNELTCATCHGYRLNDQALCVHVGGEEGPHIGQISELSIADHLQLLEELELTENESTIAKPIVKEIHDRLTFLNNVGLNYLTLSRAAGTLSGGESQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNDRLIESLKKMRDLGNTLIVVEHDEDTMMQADWLIDVGPGAGEFGGEIIASGTPKQVAKNKKSITGQYLSGKKFIPVPLERRSGNGRFIEIKGAAQNNLQSLDVRFPLGKFIAVTGVSGSGKSTLVNSILKKAVAQKLNRNADKPGKYHSISGIEHIERLIDIDQSPIGRTPRSNPATYTGVFDDIRDLFARTNEAKIRGYKKGRFSFNVKGGRCEACSGDGIIKIEMHFLPDVYVPCEVCHGRRYNSETLEVHYKEKNIAEVLDMTVDDALVFFSAIPKIARKIQTIKDVGLGYVTLGQPATTLSGGEAQRMKLASELHKRSTGKSLYILDEPTTGLHTDDIARLLKVLERFVDDGNTVLVIEHNLDVIKSADHIIDLGPEGGVGGGQIVATGTPEEVAQVKESYTGHYLKVKLQQ | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | Q5XA89 |
Q8C176 | TAF2_MOUSE | Transcription initiation factor TFIID 150 kDa subunit | Mus | MNRKKGDKGFESPRPYKLTHQVVCINNINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFSNAYAAAVSAVDPDAGNGELCIKVPSELWKHVDELKVLKIHINFSLDQPKGGLHFVVPSVEGSMAERGAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKKTFHYMLTIPTAASNISLAIGPFEILVDPYMHEVTHFCLPQLLPLLKHTTSYIHEVFEFYEEILTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQALAQQFFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFGVNEYHHWIKEELDKIVAYELKTGGVLLHPIFGGGKEKDNPASHLHFSIKHPHTLSWEYYTMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTASSQKFQSHMWSQMLVSTYGFLKSISNVSGKDIQPLIKQWLDQSGVVKFYGSFAFNRKRNVLELEIKQDYTSPGTQKYVGPLKVTVQELDGSFNHTLQIEENSLKHDIPCHSKSRRNKKKKIPLMNGEEVDMDLSAMEADSPLLWIRIDPDMSVLRKVEFEQADFMWQYELRYERDVVAQQESILALEKFPTPASRLALTDILEQEQCFYRVRMSACFCLAKIANSMVSTWTGPPAMKSLFTRMFCCKTCPNIVKTNNFMSFQSYFLQKTMPVAMALLRDVHNLCPKEVLTFILDLIKYNDNRKNKFSDNYYRAEMIDALANSVTPAVSVNNEVRTLDNLNPDVRLILEEITRFLNMEKLLPSYRHTITVSCLRAIRVLQKNGHVPSDASLFKSYAEYGHFVDIRIAALEAVVDYTKVDRSYEELQWLLNMIQTDPVPYVRHKILNMLTKNPPFTKNMESPLCNEALVDQLWKLMNSGTAHDWRLRCGAVDLYFTLFGLSRPSCLPLPELGLVLNLKEKKAVLNPTIIPEAGVGNQFSSSQDEEEVDMDTVHDSQAFISHHLNMLERPSTPGLSKYRPHHHHHHHEHKKKKKKHKHKHKHKHKHDSKDKDREPFAFSSPASGRSVRSPSLSD | The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF2 forms a promoter DNA binding subcomplex of TFIID, together with TAF7 and TAF1. | Q8C176 |
Q5N829 | ZIP4L_ORYSJ | Protein ZIP4 homolog | Oryza sativa | MKISELSPEYREPPSHAGLIADLSKAVSDVESFAASATAPEKLAADLRRILTSLASAASSSSFTESLSVQIWRLGTRLWNAVVDRANSAALAGGPAALAVEAEIRQAAPELLLLAGIPNGVPSAAAKVASFFHRSGLAWLDLGRVDLASACFEKATPLVSAAATEDRGVLLELNLARARAASDAGDQALAVALLSRSKPLAAASPEGAKSLAQGYLSIGEATLAAKHSNPAVEASTLFTEALDLCEKAASPSSSSPRTPPYGGATPKTPNLEGLKRRCLRFLALERLQAQDYEGVLRCIRVSRASMGLEEEHPSIGVMAMRAWIGSGNMAEADKELERLMANALATENLCVSAAEAYLAAAGPEAARKVLIALAARCRAGGAAAAVRVVKQVIDGGGGGIGRARAIAELVSDERVVALFDGPGNTHERGTMHALLWNCGTEHFRAKNYDTSADLIERSMLYVSRDEESRSRRADCFRVLSICHIALQHLDRALEFVNEAYKVEPNIKCAFLKVKINLQKGEEDEAFKQMKTMVGCVDFNPEFLTLTAHEAMSCKSFGVAVASLSYLLGLYSAERPMPMPEVAVLRNLIELLSREPGTEAEILKYSRRAKQRMADLGVESFFGSGIVGGRELNWFADLSWNMGLRASKEKKYNFGAEFFELAAEFFSSRNAECDENRSKVCKALIMAVTIMLNAEELNNSPLSDSDIKKGVEMLSRAGKLLPLISPSVPVASDQLEANNFLYLHTFNSYQLMGRMGTPAHPQQLQLIKNFASSKACTPANLLTLGVTASKGALPNMLAAEFSLKACITTALASQSPNYRVISCALRKLACLAGLQDLNGSKSDAAYDVFQQAYQIVVGLKEGEYPVEEGQWLVATAWNMSCLPLRLHQAKVARKWMKMGLDLARHLEGMKERIASMQTTFENFERVSGDEPDECSQEEAPKASISGSMSQPVLV | Required for crossover formation, complete synapsis of homologous chromosomes and bivalent formation during meiosis. Is specific to recombination events resulting in interference-sensitive crossovers (class I meiotic crossover) and works cooperatively with MER3 to promote crossovers. | Q5N829 |
Q92B94 | TRMB_LISIN | tRNA(m7G46)-methyltransferase | Listeria | MRVKHKPWAKDRLEEFPAIYIKNPEDFKGRWQEVFGNNNPIHIEIGSGKGQFISGMAKANPEINYIGIEMIESVLVSALDKAIEAEVPNLRLVARDAKLLEESFEKGEIAQIYLNFSDPWPKKRHTKRRLTNPTFLTIYERLLPKAGEIHFKTDNRSLFEYSLVAFSEYNMLLTFVSLDLHNSDYEGNIKTEYEEKFSAKGFPIYRLEAKFDRD | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q92B94 |
P18736 | ZG71_XENLA | Gastrula zinc finger protein XlCGF71.1 | Xenopus | TGEKPFSCSTCGKCFLDRSHLTRHQRIHTREKPFSCSVCKKCFLDQSSLTRHQLIHTADKNFSCLECEKCFSKQSSLVSHQRTHTGEKPFSCSECDKCFAFSSELIVHQRTHTGEKPFSCSECEKCFSKQSSLTRHQMIH | May be involved in transcriptional regulation. | P18736 |
Q1QVW0 | TIG_CHRSD | PPIase | Chromohalobacter | MQVSVESTSQIERRVTVQVPAAEVDQAVATRLQETAKNVRLNGFRRGKIPLTVVRQRFGREVRNEVVGEMMRQHYVQAITQESLNPAGSPQVEPTVDEDGKDLEFVATLEVYPEFELNSIENTEIERPQAEVTEADVDQMIETLRTQHAEWEAVDRAAANGDQVTIDFEGYLGDEPFEGGAAEGHELELGSNSFIPGFEEQLVGAKAGDELEIKVTFPEDYQAAHLAGQEATFKVKVHKVAGKQLPEVDDEFIKRFGVEEGGVAAFRADVQKNMEHELSQAVTNRVKQQALEALQQANDIPVPQSLIQQETQGLKRQAAQQFGLGEDFDVSQLPDELFADQAKKRVQVGLLLAEVVKVNELDASDDEIKARVEELAQQYQQPEQVIEYYLKNDEMKNQIKSSVLEDKAVDKLLEQAQVKDVEMSYEQALQAAQQQEGAEEEAQEETSA | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | Q1QVW0 |
B1HZE8 | URED_LYSSC | Urease accessory protein UreD | Lysinibacillus | MVNPQKINHFGKLEMAFEPRRGYTRLVHVYQQPPLKASRELYEGSDPTATVFLMESSGGMVAGDRNEINVKLASGSRVRLKQQSALKIYPSHTGDHCTQAITVEMADEARLEWLPEVTIPFERAKFQADTTIRMKESSTLIWGEIVAPGREMRGEVFDYQAYQSKYKVYVEEQLIAFDSIHFKPQEMNFAALGLLEKALYIGSLWIVSPLVKNLNMRDLQDLIQQEQSLQASVTKLTDQAIHCRWLAKEQRTLHKEINRMFEQMTALL | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | B1HZE8 |
A0KTZ8 | TRUB_SHESA | tRNA-uridine isomerase | Shewanella | MARRSKGRFIDGIVLLDKATGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPVCLGEATKFSQHLLDSDKRYLVTAKLGQRTDTSDSDGEVVQTRPLEFTEAQLMSALEHFRGDTQQVPSMYSALKYQGQPLYKYAREGIEVPREARPITVFELNFIGLEGDELTLDIHCSKGTYIRTIIDDLGEMLGCGAHVIMLRRTQVAHYPYDKMVTLEQLEALVAKAQEEQLDPSSLLDSLLLPMDTAVADFPEVNVPDASAAYLMQGQAVRVSGLVADTLVRITLGTERRFVGIGEMNQDGLLAPKRLVVLHDQAKAS | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A0KTZ8 |
Q4KF90 | TAL_PSEF5 | Transaldolase | Pseudomonas | MTSKLEQLKKITTVVADTGDFDAIARVKPVDATTNPSLLLKAAAIPGYADLLNACVNDCKGDVGLASDRFGVAVGQEILKVIPGRISTEVDARLSFDTEAMLKRAHRLIELYDKAGIGRDRVLIKIASTWEGIRAAEKLEREGIQTNLTLLFSFAQAVACAEAGVFLISPFVGRIYDWYKKATGNDYQGADDPGVQSVTRIYNYYKANDYKTVVMGASFRNLNQIEQLAGCDRLTISPDLIEKLAADTGKLERKLSPGKTGEARQSLNEAQFRWASNEDAMATEKLAEGIRQFARDQEKLEALLAAKL | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q4KF90 |
C5YHI2 | TPS2_SORBI | Beta-sesquiphellandrene synthase | Sorghum | MALTPSVCSISDVQGLQKDRTFHPSLWGDFFLTYQPPTAPKHAYMAERAEVLKEEVRKMVKSANEIQNILDLILTLQRLGLDNHYENEINELLSFVHDSDYDDKDLNLVSLRFYLLRKHGYDVSSDVFKCFQDKEGNFVVKDTKSLLSLYNAAHLRIHGEEVLDEAIIFTRGKLESVLDSLETTLADEVTLALQTPLFRRVRILETRNYIPIYEKEVARNEVILEFAKLNFNLLQLLYCEELKMITLWWKQLNVETNLSFIRDRIVEMHFWMTGACSEKKYSLTRTITTKMTAYITILDDIMDTHSTTEEAMLLAEAIYRCEENAAELLPEYMKDFYLYLLKTFDSVKHELGPNRSFRVFYLKELLKILVRGYSQEIKWRDEHYVPETIDEHLEVSKATVGAFQVACSSFVGMGDIITKEILDWLLSYPKLLKSMTTFVRLSNDIASTKREQTGGHHASTVQCYMMQHGTTIHDACEKIKELTEDTWKDMMKLYLTPTEQPKVIIQTVLDFARTAEFMYKKTDAFTFSHTIKDTIALLFVEPTLV | Sesquiterpene synthase converting farnesyl diphosphate into beta-sesquiphellandrene and six minor products, zingiberene, 7-epi-sesquithujene, sesquisabinene A, (E)-alpha-bergamotene, (E)-beta-farnesene and beta-bisabolene. Can also accept geranyl diphosphate as substrate, producing nine monoterpenes, with myrcene and limonene as the major products. | C5YHI2 |
Q8LG88 | TDT_ARATH | Vacuolar malate transporter | Arabidopsis | MNGGDVTVAGSDDLKSPLLPVVHNDEPFERQTVGQQLRTIFTPKNCYIALGPLLCAVVCLCVDLGGDETTTARNMLGVLVWMFAWWLTEAVPMPITSMTPLFLFPLFGISAADDVANSYMDDVISLVLGSFILALAVEHYNIHRRLALNITLVFCVEPLNAPLLLLGICATTAFVSMWMHNVAAAVMMMPVATGILQRLPSSSSTTEVVHPAVGKFSRAVVLGVIYSAAVGGMSTLTGTGVNLILVGMWKSYFPEADPISFSQWFFFGFPLALCIFVVLWCVLCVMYCPKGAGQALSPYLHKSHLRRELDLLGPMNFAEKMVLAVFGGLVVLWMTRNITDDIPGWGRIFAGRAGDGTVSVMMATLLFIIPSNIKKGEKLMDWNKCKKLPWNIVLLLGAGFAIADGVRTSGLAEVLSKGLVFLETAPYWAIAPTVCLIAATITEFTSNNATTTLLVPLLIEIAKNMGIHPLLLMVPGAIGAQFAFLLPTGTPSNVVGFTTGHIEIKDMIKTGLPLKIAGTIFLSILMPTLGAYVFASMGGV | Putative carrier protein indirectly involved in the uptake of malate and fumarate to the vacuole, probably by regulating the energization across the tonoplast. Uptake of malate to vacuoles is inhibited by citrate and by the uncoupler carbonyl-cyanide m-chlorophenylhydrazone, but seems to be not affected by sodium. Critical for pH homeostasis. | Q8LG88 |
Q4K5I7 | THIE_PSEF5 | Thiamine-phosphate pyrophosphorylase | Pseudomonas | MKLRGLYAITDSQLLAGKFLKYVEAALEGGVTLLQYRDKSDDQARRLREAETLLALCERYKTRLIINDDAELAARIGAGVHLGQTDGPLTPARALLGRQAIIGATCHSQLPLAEQAAKEGASYVAFGRFFNSTTKPGAPAASLELLDQARASLHLPICVIGGITLDNAAPLVNHGADLLAVVHGLFGAESAEEVTRRARAFNALFNS | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | Q4K5I7 |
Q6FJV1 | VAC8_CANGA | Vacuolar protein 8 | Nakaseomyces/Candida clade | MGGCCSCFRDSSDDVSVLPITDNEREAVTLLLGYLEDKDRLDFYSGGPLKALTTLVYSDNLNLQRSAALAFAEVTEKYVRQVSRDVLEPILILLQSQDPQIQVAACAALGNLAVNNENKLLIVDMGGLEPLINQMMGTNVEVQCNAVGCITNLATRDDNKHKIATSGALVPLTKLAKSKHIRVQRNATGALLNMTHSEENRRELVNAGAVPVLVSLLSSNDPDVQYYCTTALSNIAVDEANRKKLAQTEPRLVSKLVSLMDSPSSRVKCQATLALRNLASDTSYQLEIVRAGGLPHLVNLIQSESVPLILASVACIRNISIHPLNEGLIVDAGFLPPLVKLLDYRDSEEIQCHAVSTLRNLAASSEKNRKEFFESGAVKKCKELALDSPVSVQSEISACFAILALADVSKQDLLDADILQALIPMTFSTNQEVSGNAAAALANLCSRIDNYSKIISSWDQPKEGIRGFLKRFLQSNYATFEHIALWAILQLSESHNDKVIYLIKNDKEIINSVRKMADVTYDRLQKSGVDVNKNGNSEERGDNEDHQSNNDRNLANSTSSDQYEDASMELYNITQQILQFLD | Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. | Q6FJV1 |
A7NRF7 | THIE_ROSCS | Thiamine-phosphate pyrophosphorylase | Roseiflexus | MAWSTLVDPSPSVLTNPIPFPSGRGIVYVITDRRAAGERSLIDIVHAALRGGANAIQLRDKDVPARAMIALGEALLPLTRAAGVPLIVNDRVDVALALDADGVHVGQDDIPADMVRRIIGPARILGVSVATVEQAQQAARDGATYVSVGDLFGTPSKPDAGPPIGLTPLTEIARAVDLPVLGIGGITVANAASVVRAGAVGVAVISAVIGAPDPEAATRALCDVAAQR | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | A7NRF7 |
Q9HM63 | VATD_THEAC | V-ATPase subunit D | Thermoplasma | MEEGVNMDIRPTRIELIRTRRRIRLAKKGLDLLKMKRSALIYEFLQISRTIRGMKENLRKEVVEALNIIKVASVLEGSLALERIANMSSDSRINVNSRNVMGVNIPTLEVSYNLSILSDVYRTVSVPVAIDDSIRRFQKLFYDLILIVEKENSLRNLLMEIDRTKRRSNAIENILIPRLEYQAKMIKMTLDERERDTFTTLKTIKKKIEAEND | Produces ATP from ADP in the presence of a proton gradient across the membrane. | Q9HM63 |
B0KHA7 | TAL_PSEPG | Transaldolase | Pseudomonas | MTSKLEQLKQFTTVVADTGDLDAITRLKPVDATTNPSLLLKAAAIPGYADLLKQVKADAKGDVDLACDKFAVAVGSGILKVIPGRISTEVDARLSFDEPALLNKARQLIALYEAAGVPKDRVLIKLASTWEGIRAAEKLEKEGIQTNLTLLFSFAQAQACADAGVFLISPFVGRIYDWYKKSTGKDYVGAEDPGVQSVTRIYNYYKANGYNTVVMGASFRNIGQIEQLAGCDRLTISPELLQQLSDDQGELPQVLKPGNAGEAKQPLNESQFRWAMNEDAMGTEKLAEGIRQFARDQEKLEKLMAEKA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | B0KHA7 |
Q48A93 | THIG_COLP3 | Thiazole synthase | Colwellia | MVALNIYGQQLDSRLLIGSALYPSPHVMKQAILASGSQVVTLSLKRQNPAEKAGQQIWRYLQEVVTEVNGHLLPNTAGCKTAKEAVTLAKMSREIFQTDWIKLEVIGDDYNLQPDPIELLHATEQLINDGFKVLPYCTDDLVLCQRLYDLGCQVIMPWASPIGTGKGLMNPYNLETIRLRLPNATLILDAGIGKPSDACLAMEMGYDGVLLNSAVALADNPVLMAKAFGQALQAGEQGYVAGIMDQRQTAHPSTPTLDTPFWHQN | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | Q48A93 |
A3D465 | THIG_SHEB5 | Thiazole synthase | Shewanella | MLTIADVEFESRLFTGTGKFSNSQVMLEAITASKSQLVTVAMKRIDFKMGLDDLLTPLRQAGVRLLPNTSGARNAKEAVFAAELAREMLGTHWIKLEIHPDPKYLMPDAIETLEAARILCEKGFIVMPYVHADPVLCRRLEEVGCAAVMPLASPIGSNQGLVTESFLKIIIEQARVPVVIDAGIGAPSQAARAMELGADAVLVNTAIASSASPIVMAECFKEAVQCGRRAFEAGLGRVQTGAVHTSPLTGFLNQ | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | A3D465 |
Q9RW63 | TATC_DEIRA | Sec-independent protein translocase protein TatC | Deinococcus | MTQLPPPEQTVLKPAPPELASAPLFDHLEELRRRLILSVVFLAVGMVIAFTYRVQLIELVKVPLTYSELYTTGKVQLVTTKLASQLLLSFNLAFWAGLTLALPFIVWQIWAFIAPGLYPQERRWGLPFILGAGFAFAAGVVFGYKLVLPTMVPFLIEFLAGTVTQMQDLQEYIGTVVTFLVAFGVAFELPILAVILTRLGIVNHTMLRQGWRFALIGIMILAAVITPTPDPANMALVAVPLYALYELGVVLSRVFRVIAPEEQERPAPMS | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. | Q9RW63 |
Q1WUP5 | TRMB_LIGS1 | tRNA(m7G46)-methyltransferase | Ligilactobacillus | MRLRNKPWAKPLIEENPDFVVTEPTKLKGKWHTRFQNNNPIFVEIGMGKGRFIVEMAKKNPEKNYIGLELQTVAVGIALKKQLEEKLPNLQLICANGSGLGEYFEKGEIAGIYLNFSDPWPKKRQTKRRLTYKTFLEQYKEVLDSNGHIEFKTDNQGLFEYSLVSMNNFGMKFDGVWLDLHSSPEAEDNVMTEYEEKFSKKGQPIFKLEAHF | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q1WUP5 |
Q9VN97 | TI17D_DROME | Probable mitochondrial import inner membrane translocase subunit Tim17 4 | Sophophora | MEYNRQPCPIRIVEDCGCAFMMGTMGGSLFQYLKGFRNAPSGLRRGLHGGIESVRLRTPAIAGSFAIWGATFSTVDCVMVSYRQREDSWNAIVSGAATGGILAARNGIRAMANSAFVGCLVLAMLEGAGAAVATIYASDGGVKAEESLITVDQQMQRPQWETSVADSNLTGAELERVLDECRAYRAHNKMQQPMRSDAVEGKELGQLMKPMHSLVDLVKLAEIV | Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. | Q9VN97 |
Q92750 | TAF4B_HUMAN | Transcription initiation factor TFIID 105 kDa subunit | Homo | MPAGLTEPAGAAPPAAVSASGTVTMAPAGALPVRVESTPVALGAVTKAPVSVCVEPTASQPLRSPVGTLVTKVAPVSAPPKVSSGPRLPAPQIVAVKAPNTTTIQFPANLQLPPGTVLIKSNSGPLMLVSPQQTVTRAETTSNITSRPAVPANPQTVKICTVPNSSSQLIKKVAVTPVKKLAQIGTTVVTTVPKPSSVQSVAVPTSVVTVTPGKPLNTVTTLKPSSLGASSTPSNEPNLKAENSAAVQINLSPTMLENVKKCKNFLAMLIKLACSGSQSPEMGQNVKKLVEQLLDAKIEAEEFTRKLYVELKSSPQPHLVPFLKKSVVALRQLLPNSQSFIQQCVQQTSSDMVIATCTTTVTTSPVVTTTVSSSQSEKSIIVSGATAPRTVSVQTLNPLAGPVGAKAGVVTLHSVGPTAATGGTTAGTGLLQTSKPLVTSVANTVTTVSLQPEKPVVSGTAVTLSLPAVTFGETSGAAICLPSVKPVVSSAGTTSDKPVIGTPVQIKLAQPGPVLSQPAGIPQAVQVKQLVVQQPSGGNEKQVTTISHSSTLTIQKCGQKTMPVNTIIPTSQFPPASILKQITLPGNKILSLQASPTQKNRIKENVTSCFRDEDDINDVTSMAGVNLNEENACILATNSELVGTLIQSCKDEPFLFIGALQKRILDIGKKHDITELNSDAVNLISQATQERLRGLLEKLTAIAQHRMTTYKASENYILCSDTRSQLKFLEKLDQLEKQRKDLEEREMLLKAAKSRSNKEDPEQLRLKQKAKELQQLELAQIQHRDANLTALAAIGPRKKRPLESGIEGLKDNLLASGTSSLTATKQLHRPRITRICLRDLIFCMEQEREMKYSRALYLALLK | Cell type-specific subunit of the general transcription factor TFIID that may function as a gene-selective coactivator in certain cells. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TAF4B is a transcriptional coactivator of the p65/RELA NF-kappa-B subunit. Involved in the activation of a subset of antiapoptotic genes including TNFAIP3. May be involved in regulating folliculogenesis. Through interaction with OCBA/POU2AF1, acts as a coactivator of B-cell-specific transcription. Plays a role in spermiogenesis and oogenesis. | Q92750 |
Q0C197 | TPIS_HYPNA | Triose-phosphate isomerase | Hyphomonas | MPRTLIAGNWKMNGLMANLAEVERVAAEVPASSEGAETLLCLPATLIHAGSAKSEGSGLKIGGETCHANEKGAHTGDLAAEMLKDAGASYVIVGHSERRADHGETDAVVAAQASAALRAGITPIICVGETLDQRDAGEVLTVITTQMAESIPEGAEAAAIVIAYEPVWAIGTGRVATSEQIAEVHTSIRNLLVRRFGDAGRTTRILYGGSMNPGNAAEILAVAEVNGGLIGGASLKAADFLAIYRLAAQ | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q0C197 |
Q9Y320 | TMX2_HUMAN | Thioredoxin domain-containing protein 14 | Homo | MAVLAPLIALVYSVPRLSRWLAQPYYLLSALLSAAFLLVRKLPPLCHGLPTQREDGNPCDFDWREVEILMFLSAIVMMKNRRSITVEQHIGNIFMFSKVANTILFFRLDIRMGLLYITLCIVFLMTCKPPLYMGPEYIKYFNDKTIDEELERDKRVTWIVEFFANWSNDCQSFAPIYADLSLKYNCTGLNFGKVDVGRYTDVSTRYKVSTSPLTKQLPTLILFQGGKEAMRRPQIDKKGRAVSWTFSEENVIREFNLNELYQRAKKLSKAGDNIPEEQPVASTPTTVSDGENKKDK | Endoplasmic reticulum and mitochondria-associated protein that probably functions as a regulator of cellular redox state and thereby regulates protein post-translational modification, protein folding and mitochondrial activity. Indirectly regulates neuronal proliferation, migration, and organization in the developing brain. | Q9Y320 |
Q32L57 | TUSC3_BOVIN | Magnesium uptake/transporter TUSC3 | Bos | MGARGAPSRRRQAGRRPRYLPTGSFPFLLLLLLLCIQLGGGQKKKENLLAEKVEQLMEWSSRRSVFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSVCRLANEEYQILANSWRYSSAFCNKLFFSKVDYDEGTDIFQQLNINSAPTFMHFPPKGRPKRADTFDLQRIGFGAEQLAKWIADRTDVHIRVFRPPNYSGTIALALLVSLVGGLLYLRRNNLEFIYNKTGWAMVSLCIVFAMTSGQMWNHIRGPPYAHKNPHNGQVSYIHGSSQVQFVAESHIILVLNAAITMGMDLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPYSFLIK | Magnesium transporter. | Q32L57 |
Q94IP1 | TCMO_SORBI | Cytochrome P450C4H | Sorghum | MDLVLLEKALLGLFAAAVLAVAVAKLTGKRYRLPPGPAGAPVVGNWLQVGDDLNHRNLMSLAKRFGDIFLLRMGVRNLVVVSTPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGDHWRKMRRIMTVPFFTNKVVAQNRVGWEEEARLVVEDVRKDPRAAAEGVVIRRRLQLMMYNDMFRIMFDTRFESEQDPLFNKLKALNAERSRLSQSFEYNYGDFIPVLRPFLRGYLNRCHDLKTRRMKVFEDNFVQERKKVMAQTGEIRCAMDHILEAERKGEINHDNVLYIVENINVAAIETTLWSIEWGIAELVNHPAIQSKLREEMDSVLGAGVPVTEPDLERLPYLQAIVKETLRLRMAIPLLVPHMNLNDGKLAGYDIPAESKILVNAWFLANDPKRWVRPDEFRPERFLEEEKTVEAHGNDFRFVPFGVGRRSCPGIILALPIIGITLGRLVQNFQLLPPPGQDKIDTTEKPGQFSNQIAKHATIVCKPLEA | Catalyzes the first oxidative step of the phenylpropanoid pathway in higher plants by transforming trans-cinnamate into p-coumarate . The compounds formed by this pathway are essential components for lignification, pollination, and defense against ultraviolet light, predators and pathogens . Can also use 2-naphthoic acid as substrate . | Q94IP1 |
Q3ASF7 | TRMD_CHLCH | tRNA [GM37] methyltransferase | Chlorobium | MRFDVISVIPYFFDSVLTSGLLNIARKKGEVEIYIHNLHDYGLGRYKQVDDAPYGGGAGMVIRPEPVFACIEALQAERHYDAVIFLTPDGELLEQPLANRLSRLENLLLLCGHYKAIDERIREQLITMEISVGDVVLSGGEIPALMLMDAIVRLIPGVLGDSESALTDSFQNGLLDAAYYTRPADFRGMKVPEVLLSGHQAHIEQWRTASALERTKIRRPDLLERAWREEF | Specifically methylates guanosine-37 in various tRNAs. | Q3ASF7 |
A5VKZ3 | TRMB_LIMRD | tRNA(m7G46)-methyltransferase | Limosilactobacillus | MRVKHKKWADPLIAAHPELMIDDATQFKGKWQSRFAKEQPLHLEVGMGKGQFIIGMAKDHPEINFIGLEIQRTVAAIALKKALEEDLPNLQLICGDGEDLQEYFEDGEVAKMYLNFSDPWPKKRHAKRRLTYKTFLATYQQILQDQGAIELKTDNMGLFEFSLESMNNYGMIFDGVWLDLHHSEENEHNVETEYEQKFAAKGQPIYKLIANFK | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | A5VKZ3 |
P59873 | TRUB_BACAN | tRNA-uridine isomerase | Bacillus cereus group | MEGVVLLHKPKGMTSHDCVFKLRKILREKRIGHTGTLDPDVTGVLPICVGRATKIAQFLTSETKTYEGEVTLGFSTTTEDASGEVVETKYVDRVITRKEVEEALATLTGTIEQMPPMFSAVKVNGKKLYEYARAGQEVERPVRTITIHEFVLLDDREVFEGENISFRFRVTCSKGTYVRTLAVMIGEKLGFPSHMSHLVRTASGEFLLEDCISFEEIEENVQNGTVESIFISIDEALSKFPKMVVDEKQAEKIKNGMFLKNELQITAPFITVFDKNDRCLAIYEHHPKHPGMLKPMKVLVNNQELKL | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | P59873 |
Q97TX6 | TRPB2_SACS2 | Tryptophan synthase beta chain 2 | Saccharolobus | MAMRIRIDLPQDEIPAQWYNILPDLPEELPPPQDPTGKSLELLKEVLPSKVLELEFAKERYVKIPDEVLERYLQVGRPTPIIRAKRLEEYLGNNIKIYLKMESYTYTGSHKINSALAHVYYAKLDNAKFVTTETGAGQWGSSVALASALFRMKAHIFMVRTSYYAKPYRKYMMQMYGAEVHPSPSDLTEFGRQLLAKDSNHPGSLGIAISDAVEYAHKNGGKYVVGSVVNSDIMFKTIAGMEAKKQMELIGEDPDYIIGVVGGGSNYAALAYPFLGDELRSGKVRRKYIASGSSEVPKMTKGVYKYDYPDTAKLLPMLKMYTIGSDFVPPPVYAGGLRYHGVAPTLSLLISKGIVQARDYSQEESFKWAKLFSELEGYIPAPETSHALPILAEIAEEAKKSGERKTVLVSFSGHGLLDLGNYASVLFKE | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | Q97TX6 |
O13548 | YP099_YEAST | Mitochondrial protein YPR099C | Saccharomyces | MSPSESFNSFSLFSTLSMFKFLTQITFSRPFVYSALNKGCPDFLITSNCIHGNSWPHLSNLFEVKNFLMPSEDPPQLQNCKVIFLHGNTNAPTPLRPMEFRAIAFTTISPYIRVCVST | Essential for the functional mitochondria and respiratory growth. | O13548 |
Q8G3S4 | TILS_BIFLO | tRNA(Ile)-lysidine synthetase | Bifidobacterium | MAYSARLRKAVGAVRATLSAVELCDVQAPEFAQHGDHAVAADAPLVLVACSGGRDSMALAAVSHIVCTSMGVRCGAVIVDHGLQAGSERVASEAADRCRALGLGPVIMRNATVQARGEGLEAAARQARYDELCAAAHESGAIAVLLAHTMDDQAETVLIGLLRSRGVDALAGMPQVFTRSGATFARPLLTLTRAETTGICEDLGVEYWDDPTNGDAVDGELPNDYPLRSRVRHDLLPAIERFAGFNVTRHFAESARLARMDKEYLDQRSDEVMGEAVAAVDRPASSAAVSTDAPRACVAGDTNDSGHGIGLMIGVKRIAREPEAIRLRVIAHALSQAGVNASAAQIAAIDRLVVDWHGQGGVSLPRGYSANRKKHVIRVCQDGAHANR | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | Q8G3S4 |
P49021 | TIM_DROME | Protein timeless | Sophophora | MDWLLATPQLYSAFSSLGCLEGDTYVVNPNALAILEEINYKLTYEDQTLRTFRRAIGFGQNVRSDLIPLLENAKDDAVLESVIRILVNLTVPVECLFSVDVMYRTDVGRHTIFELNKLLYTSKEAFTEARSTKSVVEYMKHILESDPKLSPHKCDQINNCLLLLRNILHIPETHAHCVMPMMQSMPHGISMQNTILWNLFIQSIDKLLLYLMTCPQRAFWGVTMVQLIALIYKDQHVSTLQKLLSLWFEASLSESSEDNESNTSPPKQGSGDSSPMLTSDPTSDSSDNGSNGRGMGGGMREGTAATLQEVSRKGQEYQNAMARVPADKPDGSEEASDMTGNDSEQPGSPEQSQPAGESMDDGDYEDQRHRQLNEHGEEDEDEDEVEEEEYLQLGPASEPLNLTQQPADKVNNTTNPTSSAPQGCLGNEPFKPPPPLPVRASTSAHAQMQKFNESSYASHVSAVKLGQKSPHAGQLQLTKGKCCPQKRECPSSQSELSDCGYGTQVENQESISTSSNDDDGPQGKPQHQKPPCNTKPRNKPRTIMSPMDKKELRRKKLVKRSKSSLINMKGLVQHTPTDDDISNLLKEFTVDFLLKGYSYLVEELHMQLLSNAKVPIDTSHFFWLVTYFLKFAAQLELDMEHIDTILTYDVLSYLTYEGVSLCEQLELNARQEGSDLKPYLRRMHLVVTAIREFLQAIDTYNKVTHLNEDDKAHLRQLQLQISEMSDLRCLFVLLLRRFNPSIHSKQYLQDLVVTNHILLLILDSSAKLGGCQTIRLSEHITQFATLEVMHYYGILLEDFNNNGEFVNDCIFTMMHHIGGDLGQIGVLFQPIILKTYSRIWEADYELCDDWSDLIEYVIHKFMNTPPKSPLTIPTTSLTEMTKEHNQEHTVCSWSQEEMDTLYWYYVQSKKNNDIVGKIVKLFSNNGNKLKTRISIIQQLLQQDIITLLEYDDLMKFEDAEYQRTLLTTPTSATTESGIEIKECAYGKPSDDVQILLDLIIKENKAQHLLWLQRILIECCFVKLTLRSGLKVPEGDHIMEPVAYHCICKQKSIPVVQWNNEQSTTMLYQPFVLLLHKLGIQLPADAGSIFARIPDYWTPETMYGLAKKLGPLDKLNLKFDASELEDATASSPSRYHHTGPRNSLSSVSSLDVDLGDTEELALIPEVDAAVEKAHAMASTPSPSEIFAVPKTKHCNSIIRYTPDPTPPVPNWLQLVMRSKCNHRTGPSGDPSDCIGSSSTTVDDEGFGKSISAATSQAASTSMSTVNPTTTLSLNMLNTFMGSHNENSSSSGCGGTVSSLSMVALMSTGAAGGGGNTSGLEMDVDASMKSSFERLEVNGSHFSRANNLDQEYSAMVASVYEKEKELNSDNVSLASDLTRMYVSDEDDRLERTEIRVPHYH | Required for the production of circadian rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition. | P49021 |
A0LSX9 | UPPP_ACIC1 | Undecaprenyl pyrophosphate phosphatase | Acidothermus | MNGVSAVVLGVIEGVTEFLPVSSTAHLTIAEALMGMKTDAPAVTAFTAVIQMGAILAAIVYFRRDIRTVVTAWFRGLVRADERRSPDALLGWYVIAGTIPIGLAGYLGRNVIKHDLRSLWYVVAGLVLWSIAIVYAERTAAQRRDLRDMRLPDAVFIGVIQVLALVPGVSRSGATISAGLRQGFDRVAATRFSFLLAIPALLAAGIFELKDAVGTSGVSMASLVVGTGMAFLTAYASIAWLLRFVAHHSLTNFVWYRVTVAVFVVAALTTGLVHAV | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A0LSX9 |
A8H615 | TIG_SHEPA | PPIase | Shewanella | MQVSVETTQGLERRLTISVPAEQIENTVKEALKSEAKRARIPGFRPGKVPVSVINKRYGSAIRQDIMGEVMQRNFVEAIIAEKLNPAGAPTLTPGSTEGENFEFVATFEIYPEVELKGLESITVEQPTAEVTEADVDAMIETLRNQHATFEVADRAAAEGDKAKINFVGSIDGEEFEGGKADDFELQLGSGRMIPGFESGVEGHKAGEEFNIEVTFPEDYHAENLKGKVATFAITLNEVQAANLPEVNDEFATLFGITEGGIDALRAEISKNMSRELEQALKANVKEQVLNGLVEQNDIELPTALINGEVEVLRKQAMQRFGDQAANMPELPADLFTEQAARRVKVGLLLGEVIKTNELKAEDERVQGLIASMASAYEDPSEVVAYYNGNEELMQNMRNVALEEQAVEALLKTATLTEKAVNFEEFMNKATGRA | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | A8H615 |
Q0HLF9 | TRUB_SHESM | tRNA-uridine isomerase | Shewanella | MARRSKGRFIDGIVLLDKATGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDSDKRYLVTAKLGQRTDTSDSDGEVVQTRPIEFTEAQLMSALEHFRGDTLQVPSMYSALKYQGQPLYKYAREGIEVPREARPITVFELNFISLEGDELTLDIHCSKGTYIRTIIDDLGEMLGCGAHVIMLRRTQVAHYPYDKMVTLEQLEALVAKAQEEQLDPSSLLDSLLLPMDTAVADFPEVNVPDASAAYLMQGQAVRVSGLVADKLVRITLGTERRFVGIGEMNEDGLLAPKRLVVIHDQAKAS | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q0HLF9 |
C1DK47 | UBIA_AZOVD | 4-HB polyprenyltransferase | Azotobacter | MYTALLQSMNRLHPRAWDFIQLVRLDRPIGIYLLLWPTLWAVWIAADGSPSLKHVLIFTCGVILMRSAGCVINDFADRNFDGHVARTRQRPLATGRIRTREAWALFAVLVALSFGLVLLTDPFTVALSFGALAVASLYPFMKRYTHLPQLVLGAAYSWGIPMAFTAATGRLPLEAWLIFAANLAWTVAYDTYYAMTDREDDLKIGVKSTAILFGAADRAIILALQGLTLGLLLVVGMRLGLGPYFHLGLLVAALCFAWEFVTTRRREPQACFRAFLHNHWAGLAILVGLILDYGI | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. | C1DK47 |
Q02322 | UVRD_HAEIN | DNA helicase II | Haemophilus | MMDISELLDGLNDKQRERVAAPLGNHLVLAGAGSGKTRVLTHRIAWLIAVENISEGSIMAVTFTNKAAAEMRHRIQSTLAKHAQHQLFGMWIGTFHSIAHRLLRAHHLDVGLPQDFQILDSEDQLRLIKRLLKLHNFDEKAFPPKQACWYINNKKDEGLRPNDIEDFNDRQEREWIKIYQIYQDTCDRAGLVDFAELLIRVYELFEKKPLILQRYQQRFQHILVDEFQDTNKIQYKWIKILAGKTGQVMIVGDDDQSIYGWRGAQIENIQKFLKDFKAETIRLEQNYRSTANILNSANELIANNSDRLGKNLWTEGEKGDPVGIYSAFNELDEAKFVASQIQDWVEHGGKLDDCAVLYRSNSQSRVIEEALIRCQIPYRIYGGMRFFERQEIKDALAYLRLINNRQDDAAFERVINTPTRGIGDRTLDILRNLTRERQITLWQAVQVATQENMLAGRASTALLRFQELINSLQLDTAEMPLFAQTDFVIKHSGLYEMYQQEKGEKGEVRIENLEELVTATREFIKPDNAEEMTELTAFLTHASLEAGEEQASPHQSCVEMMTLHSAKGLEFPRVFMVGVEEGLFPSFRSFEEPGRLEEERRLAYVGITRAKKKLTISYAESRRLYAKEERHLPSRFIAELPRECIQEIRLRGTVTRAMNLAKVGSLSNTSAVENEWKMGQKVKHEKFGFGTVINVEGSENNTRLQIAFQAQGIKWLIAHLAKLEKVR | May process damage occurring in non-replicating regions of DNA to produce recombinational intermediates for sister strand recombinational exchange. | Q02322 |
Q0TUS0 | TACY_CLOP1 | Thiol-activated cytolysin | Clostridium | MIRFKKTKLIASIAMALCLFSQPVISFSKDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKAGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN | A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A conformation change leads to insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host cell membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation. | Q0TUS0 |
A9I0N5 | Y443_BORPD | Nucleotide-binding protein Bpet0443 | Bordetella | MLKVVLITGISGSGKSVALRMLEDAGYTCIDNLPVRFLSEFVAGARDDGLERVAIAIDVRSPGELAELPGVITAMRAMGTSLRVVFLDANTHTLAQRYSESRRRHPLTDRLSRGGQTPSLLDCIALERDLLAPLRDQEHVIDTSDLTPGQLRAWIRDLVQADRPPLVLTFESFAYKRGVPSDADLVFDVRCLPNPYYDRTLRPLTGRDEPVATWLAGFEIVGQMIDDIAGYLRRWLPQYTQDTRNYLTVAIGCTGGQHRSVYVVEQLALRFAEHDPLLVRHRTQLPDEST | Displays ATPase and GTPase activities. | A9I0N5 |
P31292 | WNT10_XENLA | Protein Wnt-10 | Xenopus | QECKCHGTSGSCQFKTCWYVTPDFRAVSTLMRDKLQRAVFVNSRNKNSGAFHPRLNKKRLQRELVYFEKSPDFCEKDPRVDSLGTQGRVCNKTSQQMDNCASLCCGRGHNVLMQTRRERCNCRFHWCC | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. | P31292 |
B1J1Y7 | THIE_PSEPW | Thiamine-phosphate pyrophosphorylase | Pseudomonas | MKLRGLYAITDSQLLAGRFLTHVEAALEGGVRLLQYRDKSDDAARRLREAQALQKLCERYGTELVINDDAELAARLGVGVHLGQTDGPLTPARALLGRQAIIGSTCHASLDLAAQAASEGASYVAFGRFFNSVTKPGAPAADVGLLAQARGQVKLPIAVIGGITLDNAAPLVAHGADLLAVIHGLFGADSAQEVTRRARAFNALFAS | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | B1J1Y7 |
Q9HXY2 | UPPS_PSEAE | Undecaprenyl pyrophosphate synthase | Pseudomonas | MEKTRKDVCVPRHVAIIMDGNNRWAKKRLLPGVAGHKAGVDAVRAVIEVCAEAGVEVLTLFAFSSENWQRPADEVSALMELFLVALRREVRKLDENGIRLRIIGDRTRFHPELQAAMREAEAATAGNTRFLLQVAANYGGQWDIVQAAQRLAREVQGGHLAADDISAELLQGCLVTGDQPLPDLCIRTGGEHRISNFLLWQLAYAELYFSDLFWPDFKHAAMRAALADFSKRQRRFGKTSEQVEAEARPSC | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. | Q9HXY2 |
Q9I2Q0 | TSI1_PSEAE | Immune protein Tsi1 | Pseudomonas | MKLLAGSFAALFLSLSAQAADCTFTQLEIVPQFGSPNMFGGEDEHVRVMFSNEDPNDDNPDAFPEPPVYLADRDSGNDCRIEDGGIWSRGGVFLSQDGRRVLMHEFSGSSAELVSYDSATCKVVHREDISGQRWAVDKDGLRLGQKCSGESVDSCAKIVKRSLAPFCQTAKK | Immunity protein that plays a role in preventing early activation of toxin Tse1. Binds to a large surface of Tse1 and thereby occludes the active site to specifically inhibits enzyme activity by forming a hydrogen bond with the catalytic diad. | Q9I2Q0 |
A6MFL2 | VKT2_DEMVE | Kunitz-type serine protease inhibitor vestiginin-2 | Demansia | MSSGGLLLLLGLLTLWAELTPVSSKDRPEFCELPPDRGTCMGYSQAFYYNPSQNKCLPFMFGGCKANPNNFKTLEECKRTCAA | Serine protease inhibitor. | A6MFL2 |
A3CLI1 | TRHO_STRSV | tRNA hydroxylation protein O | Streptococcus | MAKDIRVLLYYKYVPIENAEKFAADHLAFCKSIGLKGRILVADEGINGTVSGDYETTQKYMDYVHSLPGMEDLWFKIDEENEQAFKKMFVRYKKEIVHLGLEDNDFDNDINPLETTGAYLSPKEFKEALLDEDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDNKEKFMDKRVIVYCTGGVRCEKFSGWMVREGYKDVGQLHGGIATYGKDPEVQGELWDGKMYVFDERISVDINHVNPVVIGKDWFDGTPCERYVNCGNPECNRRILTSEENEDKYLRGCSHECRVHPRNRYVAENGLSQAEVVERLAAIGESLETLVAQ | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | A3CLI1 |
Q12667 | XYNA_PIRSP | Xylanase A | unclassified Piromyces | MKLFQIFPLLLSLTSVTLAADDFCNATGFQGQSVVSTGHDVKKIGNIDYEQWADGGNNSATFYSDGSFKCNFSNTKDYLCRSGVAFSQAKYPSEIGHIEAEYRLVKKSASNVGYSYVGVYGWTLQSGISGVYEYYIVDNWLSQWRPGDWVGNTKFGDFTIDGGVYTVYKNVNGNLTQYFSLRKSERTCGTIDVTAHFAQWEKLGLKMPKITEIKVLAEAGNTGGGCSGSVEIPYAKIYINGKDQDGKSKGGSSSGGSNGQGLGNGQGNGQGQGNGQGQSATGSGKCPSTITSQGYKCCSSNCDIIYRDQSGDWGVENDEWCGCGSRVPKTTNCPSSIKNQGYKCCSDSCEIVLTDSDGDWGIENDEWCGCGIKNTTPTTTTKKSNNSQPTQGQSNNNSSTNTNFCSTSKHSGQSVTETSNKVGSIGGVGYELWADSGNNSATFYSDGSFSCSFRNAKDYLCRSGLSFDSTKTYQQLGHMYADFKLVKQNIQNVDYSYVGIYGWTRNPLVEFYVVDNWLSQWRPGDWVGNKKHGDFTIDGAKYTVYENTRTGPSIDGNTTFKQYFSIRQQARDCGTIDITAHFEQWEKLGMRMGKMHEAKVLGEAGSTGSGTSGTADFPYAKVYIK | Hydrolyzes 1,4-beta linked polysaccharide backbones of xylans, one of the major hemicellulose components in hardwoods and softwoods. It is more active against xylopentaose than xylotetraose, has trace activity against xylotriose. The major products released from hydrolysis of xylooligosaccharides are xylobiose and xylotriose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex. | Q12667 |
Q9YGJ2 | VSP1_GLOHA | Snake venom serine protease pallabin | Gloydius | MVLIRVLANLLILQLSYAQKSSKLVIGGDECNINEHRFLVALYTSRTLFCGGTLINQEWVLTAAHCNMEDIQIKLGMHSKKVPNEDEQKRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSAHIAPLSLPSSPPSVGSDCRTMGWGRISSTKETYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCVGDSGGPLICNGQSQGIASWGDDPCAQPHRPAAYTKVFDHLDWIENIIAGNTDASCPP | Snake venom serine protease that may act in the hemostasis system of the prey. | Q9YGJ2 |
A4F9T1 | YBEY_SACEN | Endoribonuclease YbeY | Saccharopolyspora | MSIEIANESGVEVPEPSIVSVARFALDKMSVSQLAELSIVLVELDVMSDLHERWMDLPGPTDVMAFPMDEYDSSRRPDSAGAGPALLGDIVLCPAFAKDQARKAGHSLLDELHLLTVHGVLHLLGYDHAEPEEEREMFGLQNQILADFRAAKAAAEREQAQRSADSAVLGAVGLEEQDGPGTH | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A4F9T1 |
A9N0K2 | THIG_SALPB | Thiazole synthase | Salmonella | MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLIEAGVTLLPNTSGAKTAEEAIFAAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQGLETKAMLEIIIQQSTVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVMMATAFRLAVEAGVLARQAVPGSKSSQASATSPLTGFLEALA | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | A9N0K2 |
Q6IVA4 | UBA5_CHICK | Ubiquitin activating enzyme-like protein | Gallus | MAERVELLERRVRELERELELARGGRASARARIETMSPEVTDSNPYSRLMALKRMGIVKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLDNFEHFMDRISNGALEEGKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSENAVSGHIQLIIPGESACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKYLLNFGTVSYYLGYNAMQDFFPTMAMKPNPQCSDQNCRKQQENYKIKEAAQPKQEEIHQEEEIVHEDNDWGIELVSETTEDELKAASGPVPDLPVGITVAYTIPNKEENLTAEETVAESEESLEDLMAKMRNL | E1-like enzyme which specifically catalyzes the first step in ufmylation. Activates UFM1 by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a UFM1-E1 thioester and free AMP. Activates UFM1 via a trans-binding mechanism, in which UFM1 interacts with distinct sites in both subunits of the UBA5 homodimer. Trans-binding also promotes stabilization of the UBA5 homodimer, and enhances ATP-binding. Transfer of UFM1 from UBA5 to the E2-like enzyme UFC1 also takes place using a trans mechanism. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. | Q6IVA4 |
Q9D709 | TMM79_MOUSE | Mattrin | Mus | MTEPETLALLDMKEPETPEKSPPQALVLQSEEEGGTESPGTESLRVGSSVGSPIVREGPEDGPDSTISEAATLPWGTDPHPSAPLPDPPGWRDIEPEPLESEAPTKSEEPFKEDANLLPEKTVRAFVPIDLQCIERKPQEERILHRDAGPGELRNFLPARLSHPEPPERKWAEAVVRPPGRSCGGCGSCGGREALRAVASVVAALIFFPCLLYGAYAFLPFDAPRLPTMSSRLVYTLRCGVFATFPIVLGLLVYGLSLLCFSALRPFGEPRREVEIHRQYVAQSVQLFILYFFNLAVLSTYLPQDTLKLLPLLTGLFAISRLIYWLTFAVGRSFRGFGYGLTFLPLLAMLVWNLYYMFVVEPERMLTASESRLDYPDHARSVSDYRPRSWG | Contributes to the epidermal integrity and skin barrier function. Plays a role in the lamellar granule (LG) secretory system and in the stratum corneum (SC) epithelial cell formation. | Q9D709 |
P21939 | XYLB_LACPE | Xylulose kinase | Lactiplantibacillus | MSAVVLGIDLGTSAVKVSAIDKQGNVVAQASAKYALQQPHPGYSEQDPEDWVTQTTQAIRELLQQSEVTADQIEGLSYSGQMHGLVLLDESATVLRPAILWNDTRTTSQCRELESQFGDDFIKITGNRPLEGFTLPKLLWVKENEPNIWKRARTFLLPKDYLRYRMTGKLAMDKSDATGTVLLDITTSQWSETLCNQLDIPLTLCPPLIESTAYVGHINQTYAQLSGLSVNTKVFGGAADNAAGAVGAGILSSDKALVSIGTSGVVLKYEDNAQTDYRGVLQYERHAFPGKYYSMGVTLAAGYSLNWFKQTFAPDEDFGTVVASAEQSTIGANGLLFAPYIVGERAPYADATIRGSFIGVDGSHQRADFVRAVLEGIIFSFEDLIKLYQHNGAEFKTIVSIGGGAKSALWLQIQADIFNCKVVSLKNEQGPGMGAAMIAATGLGWFKTLADCAQTFVHYGKAYYPVTAHVAQYQEMYRLYQQIYVQTQPITAGLLEQRKQH | Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate. | P21939 |
B2GBZ2 | YBEY_LIMF3 | Endoribonuclease YbeY | Limosilactobacillus | MELQLRDHTEGKLQPSQERLAEKALAQAAERLDVPEQAEMSLTFVLNPEIRELNRDYRGIDRATDVISFAIEDDDDLANLPAEIRAELPVELGDLVISIDKVTEQALFLNHSADRELGYLLVHGFLHLNGYDHEEPADEEKMFTLQEEILDGLGLSR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | B2GBZ2 |
Q2EF88 | YSL3_ARATH | Protein YELLOW STRIPE LIKE 3 | Arabidopsis | MRSMMMEREGRNEIEREVIDDLEETQNEGDDFKSIPPWKEQITFRGIVASLIIGIIYSVIVMKLNLTTGLVPNLNVSAALLAFVFLRSWTKLLTKAGIVTKPFTKQENTVVQTCAVACYSIAVGGGFGSYLLGLNRITYEQSGGTHTDGNYPEGTKEPGIGWMTAFLFFTCFVGLLALVPLRKIMIIDYKLTYPSGTATAVLINGFHTPKGNKMAKKQVFGFVKYFSFSFIWAFFQWFFSGGTECGFIQFPTFGLEALKNTFYFDFSMTYVGAGMICPHIVNISLLFGAVLSWGIMWPLIKGLKGDWFPSTLPENSMKSLNGYKVFISISLILGDGLYQFIKILFKTGINMYVKLNNRNSGKSNSEKDKQSIADLKRDEIFVRDSIPLWVAAVGYAAFSVVSIIAIPIMFPELKWYFIVVAYMLAPSLGFSNAYGAGLTDMNMAYNYGKVALFILAAMAGKQNGVVAGLVGCGLIKSIVSISSDLMHDFKTGHLTLTSPRSMLVSQAIGTAIGCVVAPLTFFLFYKAFDVGNQEGEYKAPYALVYRNMAILGVEGFSALPQHCLQLCYGFFAFAVAANLVRDRLPDKIGNWVPLPMAMAVPFLVGGYFAIDMCVGSLIVFAWNMRDRVKAGLMVPAVASGLICGDGLWILPSSVLALAGVRPPICMGFMPSKYSS | May be involved in the lateral transport of nicotianamine-chelated metals in the vasculature. | Q2EF88 |
A7HKC0 | UVRB_FERNB | Excinuclease ABC subunit B | Fervidobacterium | MPYELISDYEPMGDQPQAIESLVNGLNKGYRFQTLLGVTGSGKTFTMANVIKEVNRPVLIISPNKTLAAQLYSEFKAFFPNNKVEFFISYYDYYQPEAYVPTKDLYIEKSADINDVIARMRMSAIKSIMTRRDVIVVASVSAIYACGDPRDFDTLNIKLEVGQRINLSEFVKKLVKIGYERKEDIGLTGSFRLRGDTLEIFPSYQDEGIRIELFGDEIDRMYTFDRMNRDVIERLDRLTIYPTKEYVTTEEKIERAVKSIRAELDEQVKKLRSEGKELEAQRLWQRTMNDIELLSTLGYCTGIENYSRHFDGRQPGEPPYSLLDYYDEDFIVFIDESHITIPQLRAMYHGEMSRKKSLVEYGFRLPCAYDNRPLKFDEFMQKVNQVIFVSATPGPYELEVSEQVVEQIIRPTGLIDPQVEVRPTRYQVDDLVNEIVQVKKRGEKALVTVLTKKTAEMLAEYLVEFNIRALYLHSELDAIKRVEVLKKLRAGEIDVVVGVNLLREGLDLPEVSLVAILDADTEGFLRSETTLIQIIGRTARNENGKVIMYADRITPAMQRAIDETNRRRKIQMEYNEKHGIKPKTIIKPLMEDIFAPFRDKEEEMYKVYEDSILQMKESLSLEEYAALLEEEMYKAASELRYEDAARLRDELFKIKEELNRN | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage. | A7HKC0 |
Q47692 | TSH_ECOLX | Temperature-sensitive hemagglutinin tsh translocator | Escherichia | MNRIYSLRYSAVARGFIAVSEFARKCVHKSVRRLCFPVLLLIPVLFSAGSLAGTVNNELGYQLFRDFAENKGMFRPGATNIAIYNKQGEFVGTLDKAAMPDFSAVDSEIGVATLINPQYIASVKHNGGYTNVSFGDGENRYNIVDRNNAPSLDFHAPRLDKLVTEVAPTAVTAQGAVAGAYLDKERYPVFYRLGSGTQYIKDSNGQLTQMGGAYSWLTGGTVGSLSSYQNGEMISTSSGLVFDYKLNGAMPIYGEAGDSGSPLFAFDTVQNKWVLVGVLTAGNGAGGRGNNWAVIPLDFIGQKFNEDNDAPVTFRTSEGGALEWSFNSSTGAGALTQGTTTYAMHGQQGNDLNAGKNLIFQGQNGQINLKDSVSQGAGSLTFRDNYTVTTSNGSTWTGAGIVVDNGVSVNWQVNGVKGDNLHKIGEGTLTVQGTGINEGGLKVGDGKVVLNQQADNKGQVQAFSSVNIASGRPTVVLTDERQVNPDTVSWGYRGGTLDVNGNSLTFHQLKAADYGAVLANNVDKRATITLDYALRADKVALNGWSESGKGTAGNLYKYNNPYTNTTDYFILKQSTYGYFPTDQSSNATWEFVGHSQGDAQKLVADRFNTAGYLFHGQLKGNLNVDNRLPEGVTGALVMDGAADISGTFTQENGRLTLQGHPVIHAYNTQSVADKLAASGDHSVLTQPTSFSQEDWENRSFTFDRLSLKNTDFGLGRNATLNTTIQADNSSVTLGDSRVFIDKNDGQGTAFTLEEGTSVATKDADKSVFNGTVNLDNQSVLNINDIFNGGIQANNSTVNISSDSAVLGNSTLTSTALNLNKGANALASQSFVSDGPVNISDAALSLNSRPDEVSHTLLPVYDYAGSWNLKGDDARLNVGPYSMLSGNINVQDKGTVTLGGEGELSPDLTLQNQMLYSLFNGYRNIWSGSLNAPDATVSMTDTQWSMNGNSTAGNMKLNRTIVGFNGGTSPFTTLTTDNLDAVQSAFVMRTDLNKADKLVINKSATGHDNSIWVNFLKKPSNKDTLDIPLVSAPEATADNLFRASTRVVGFSDVTPILSVRKEDGKKEWVLDGYQVARNDGQGKAAATFMHISYNNFITEVNNLNKRMGDLRDINGEAGTWVRLLNGSGSADGGFTDHYTLLQMGADRKHELGSMDLFTGVMATYTDTDASADLYSGKTKSWGGGFYASGLFRSGAYFDVIAKYIHNENKYDLNFAGAGKQNFRSHSLYAGAEVGYRYHLTDTTFVEPQAELVWGRLQGQTFNWNDSGMDVSMRRNSVNPLVGRTGVVSGKTFSGKDWSLTARAGLHYEFDLTDSADVHLKDAAGEHQINGRKDSRMLYGVGLNARFGDNTRLGLEVERSAFGKYNTDDAINANIRYSF | Contributes to the development of lesions and deposition of fibrin in the avian air sacs. It can act both as an adhesin and as a serine protease. Agglutinates erythrocytes while in contact with the extracellular surface of the bacterial cells. Can adhere to purified hemoglobin and bind with great efficiency to extracellular matrix proteins. Cleaves casein and exhibits mucinolytic activity. | Q47692 |
Q498E2 | TDRP_RAT | Testis development-related protein | Rattus | MWKLSRSRVLLDEPPEEEDVLRGASPASAAAQAPGASLRGWKEATSLFNKDDEERLLETSRSSKSKGTNVRLKEELKAEKKSGFWDALVLKQNVQPKKPDQMEGWEPPKLTAEDVATDHTEDGISSLPPWSAWEDDTKGSTKYTSLASSASSSRWSLRSAGKLVSIRRQSKGHLTETCEEVE | Contributes to normal sperm motility, but not essential for male fertility. | Q498E2 |
P07529 | XYNA_NAGAL | 1,4-beta-D-xylan xylanohydrolase | Naganishia | MLSSTTLLAILSALALTSVQAAPADKNSLDYLANKAGKRYLGTAVQSPQLVPGSQYVQILESQFDAITPENEMKWEVVEPTEGNFDFTGTDKIVAEAKKTGSLLRGHNICWDSQLRYAHEVAPKMKLCINDYNIETVNAKSQAMAKVAAGLLAKGAPLHCIGMFKNAKRRSSGLLIRTASSGLESHFIGGSTPKDIPAAMNLFSDQGLEVPMTELDVRIPVNGNDMPANATVAKEQVDDYYTSVSACLGNDLCPGVSIWQFADPTSWIPGVFKGKLIAVSCTFSGCLLQYCVGYGAALLYDAQYQPKSTYYVVQQALKDGKNSGSKFHGIKL | Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose. | P07529 |
Q0KEP0 | Y381_CUPNH | Nucleotide-binding protein H16_A0381 | Cupriavidus | MRIILITGISGSGKSVALNVLEDAGYYCVDNLPAQFIPELTRYLDSQGYTHLGVATDIRSRESLDQLPDTVRALAAEHQVEVVFLTASTDALVQRYSETRRRHPLSVRTDGVPGPGGEPAFNDTALMEAIEMERALLSPLAEAAHRIDTSNVRTNTLRSWIKELIRDDSQRLTLLFESFGFKHGVPSDADMVFDVRSLPNPYYDLALRPLTGRDTPVIDFLQAQPMVLAMAEDIRAYVEKWLPSFIADNRSYLTVAIGCTGGQHRSVYIAERLANYFRAHGNVLVRHRELAPAG | Displays ATPase and GTPase activities. | Q0KEP0 |
A5G9V4 | YIDC_GEOUR | Membrane protein YidC | Geotalea | MEKRVVIAVILSIAVLYAYSMIFPPPQKKDVVKPGPVPQSQTAPVQAVSSTSVLPAIMQQGNVSVRDLVVETDLFTAVFSTRGAGLKKLVLKRYKETSGPGGREVVLVNEEAAEKFSLLTEGKSFGIEPTVVYNSISNGLKLAGNEKGTLEFTSTSPTGIVFKKSYIFTGNDYRIDLHQELLNNSPTKFDGSLHLIGNNRIEAKPGDGRFEVYGPVTLADDKINTEKVADFSKGPKQYDKNILWTAFADKYFMNAILSDNNSIAAVRLAKVNTNYLQDDVSSPPLALNPGQSAAVNYRIFYGPKDLEILKGQGSRLEEAIDFGWFSALAKPLLRTLKFFYSYTHNYGIAIIIITVILKLLFFPLTHKSYKSMKEMQKLQPKMAELKEKFKNDRDAMNRAVMDLYKTHKVNPMGGCLPMIVQIPVFFALYKALMFSIELRHAPFMLWIMDLSAKDPYYVTPVIMGVTMFVQQKMTPSNMDPVQAKMMLALPVVFTFMFLNFPSGLVLYWLVNNILTIAQQTYINKSLPS | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. | A5G9V4 |
Q8I3Z5 | TCTP_PLAF7 | Translationally-controlled tumor protein homolog | Plasmodium (Laverania) | MKVFKDVFTNDEVCSDSYVQQDPFEVPEFREIAFEVKSNKRIKGNEDYGIADNSEDAVEGMGADVEHVIDIVDSFQLTSTAFSKKEYSAYIKNYMQKVAKYLEEKKPDRVEIFKTKAQPFIKHILTNFDDFEFYMGESLDMEAGIIYSYYKGEEITPRFVYISDGLFEEKY | Involved in calcium binding and microtubule stabilization. | Q8I3Z5 |
Q01WE6 | UPPP_SOLUE | Undecaprenyl pyrophosphate phosphatase | Candidatus Solibacter | MPILQVIVLAVVQGLTEFLPISSTAHLYLTSWLLGWQIEGLDFDIALHIGTLLAVLIFFARDWLQIIAQGFGIRREGDRELNHNHMLLWLLLIGTVPVGIAGLLFNKQAEGAWRNPFVMGFMLIVVGVLMWIAENAGRQQRDLSSLDLADTLAIGTAQALAVVPGTSRSGVTITAGLFRSLTRESAARFSFLLSTPAIGAAAAKAIWDMHKKGGGLHGMLHADFLVGVAVSAITGCIVIAWFLHYLRRNGLRPFVYYRILFGIIVLALAFIRRPA | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q01WE6 |
Q91V04 | TRAM1_MOUSE | Translocating chain-associated membrane protein 1 | Mus | MAIRKKSNKNPPLLSHEFLLQNHADIVSCLAMLFLLGLMFEVTAKGAIIFVALQYNVTRPATEEQATESASLYHYGIKDLATVLFYMLVAIIIHAIIQEYVLDKINRRMHFSKTKHSKFNESGQLSAFYLFACVWGTFILISENYISDPTILWRAYPHNLMTFQTKFFYISQLAYWLHAFPELYFQKTKKEDIPRQLVYIGLYLFHIAGAYLLNLNHLGLVLLVLHYFVEFLFHISRLFYFSDEKYQKGFSLWAVLFVLGRLLTLILSVLTVGFGLARAENQKLDFSTGNFNVLAVRIAVLASICITQAFMMWKFINFQLRRWREHSAFQAPPVKRKPAVTKGRSSRKGTENGVNGTVTSNGADSPRNRKEKSS | Involved in the translocation of nascent protein chains into or through the endoplasmic reticulum (ER) membrane by facilitating the proper chain positioning at the SEC61 channel. Regulates the exposure of nascent secretory protein chain to the cytosol during translocation into the ER. May affect the phospholipid bilayer in the vicinity of the lateral gate of the SEC61 channel, thereby facilitating ER protein transport. Intimately associates with transmembrane (TM) domain of nascent membrane proteins during the entire integration process into the ER membrane. Associates with the second TM domain of G-protein-coupled receptor opsin/OPSD nascent chain in the ER membrane, which may facilitate its integration into the membrane. Under conditions of ER stress, participates in the disposal of misfolded ER membrane proteins during the unfolded protein response (UPR), an integrated stress response (ISR) pathway, by selectively retrotranslocating misfolded ER-membrane proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome. | Q91V04 |
P39301 | ULAA_ECOLI | Ascorbate-specific permease IIC component UlaA | Escherichia | MEILYNIFTVFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIDRMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVTLFIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVHWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSILIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWAVKLTGMSAWMGMADWSILAPPMMQGFFSIGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA | The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. | P39301 |
Q8KGG3 | YIDD_CHLTE | Putative membrane protein insertion efficiency factor | Chlorobaculum | MNIVPILLIRFYQSFISPLLGPSCKYHPTCSNYAIEAFRQHNFFYASWLTVWRVLRCNPFSKGGYDPVPPKSVKSAGNSKDSK | Could be involved in insertion of integral membrane proteins into the membrane. | Q8KGG3 |
F1Q7H8 | ZD20A_DANRE | Zinc finger DHHC domain-containing protein 20-A | Danio | MAPSHAVRCCQRGLSWIPVIFINLVVCWSYYAYVVELCIYTIPNVNEQVIYLVVFHAFFFMFMWSYWKTISSKPTNPSKEFCLPKAEKELYEKEERPEAQQDILKRVARELPIYTFTGSGAIRYCDRCQLIKPDRCHHCSTCDKCVLKMDHHCPWVNNCVGFSNYKFFVLFLAYSMLYCVYIAATVLQYFIKFWTNQLPDTHAKFHVLFLFFVAAMFFISILSLFSYHLWLVGKNRTTIEAFRAPVFRNGPDKNGFTLGFRKNITQVFGDQKKYWCLPIFSSLGDGYTFPTRLVTVDVEHGNIEHQTIKCTVDGQTNARPLSESQNHLLCNDEGQKDSSMAAIEVCQPVCVTLENES | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues on protein substrates and has a preference for acyl-CoA with C16 fatty acid chains but may also utilize acyl-CoA with C14 and C18 fatty acid chains. | F1Q7H8 |
B7UTC1 | YEGS_ECO27 | Probable lipid kinase YegS | Escherichia | MAEFPASLLILNGKSTDNLPLREAIMLLREEGMTIHVRVTWEKGDAVRFVEEARKLGVATVIAGGGDGTINEVSTALIQCEGDDIPALGILPLGTANDFATSVGIPEALDKALKLAIAGNAIAIDMAQVNKQTCFINMATGGFGTRITTETPEKLKAALGGVSYIIHGLMRMDTLQPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEIIPTLVSTLKSDEDNPNIIEGASSWFDIQAPHEITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR | Probably phosphorylates lipids; the in vivo substrate is unknown. | B7UTC1 |
P56811 | TFX_METTM | DNA-binding protein Tfx | Methanothermobacter | MSKKTFLTERQKTVLEMRERGWSQKKIARELKTTRQNVSAIERKAMENIEKSRNTLDFVKFLKSPVRILCRRGDTLDEIIKRLLEESNKEGIHVIHDSITLAFLIREKASHRIVHRVVKSDFEIGVTRDGEIIVDLNS | Transcriptional activator of the fmdECB operon. | P56811 |
Q9NFZ4 | TPM_LEPDS | Tropomyosin | Lepidoglyphus | MEAIKNKMQAMKLEKDNAIDRAEIAEQKSRDANLRAEKSEEEVRGLQKKIQQIENELDQVQESLTQANTKLEEKEKSLQTAEGDVAALNRRIQLIEEDLERSEGRLKIATSKLEEASQSADESERMRKMLEHRSITDEERMEGLESQLKEARMMAEDADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAQQREEAYEQQIRIMTTKLKEAEARAEFAERSVQKLQKEVDRLEDELVHEKEKYKSISDELDQTFAELTGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | Q9NFZ4 |
Q3BMF4 | TTCA_XANC5 | tRNA 2-thiocytidine biosynthesis protein TtcA | Xanthomonas | MTAVLPLPQPLADPAPRDPRQRLQREQLRLGKRLQRQVGQAIADFGMIAPGDKVMVCLSGGKDSYTLLDMLLQLQRKAPVPFSLVAVNLDQKQPDFPAHVLPAYLRGLGVPFDIVEQDTYSVVSRVIPAGKTMCSLCSRLRRGALYAYAQTHGVTKIALGHHRDDIVATFFMNLFHHARLAAMAPKLRSDDGAHVVIRPLAYVREADIAAYAQARQFPIIPCNLCGSQENLQRQQVGKLLQQWDREFPGRVEQIARALGDVRPEQLADRTLFDFLALGRSGDAPSDVDPDPSAWLSASHAPHDSD | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | Q3BMF4 |
A4IRT9 | THII_GEOTN | tRNA 4-thiouridine synthase | Geobacillus | MKYDRILIRYGEMTTKGKNRNIFVRRLKNNIARKLQAFPRIKIEYMRDRMYILLNGEPHEPIIDKLKTVFGIHSFSLAMKCENDLAAIKETALAAVRQLPYKGKTFKVSARRVDKQFPYRSDELNHEVGAHILRQTEDLTVNVRQPDIDVRIEVRQDGTYVTCHDIFGAGGLPVGTSGKAMLMLSGGIDSPVAGYLAMKRGLEIEAVHFFSPPFTSERAKQKVIDLVRKLTAYGGKIKLHIVPFTEVQQAIYQGVPNEYSLISTRRAMLKITDALRRRQRGLAIVTGESLGQVASQTLESMYVINEVTNTPVLRPLISMDKMEIIEIAKQIDTHDISILPYEDCCTIFTPRAPKTKPKKEKVLQHESQLDLAPLLEKAINETETIVIDEEAGQADEFTALF | Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. | A4IRT9 |
Q9ZMZ5 | UREE_HELPJ | Urease accessory protein UreE | Helicobacter | MIIERLVGNLRDLNPLDFNVDHVDLEWFETRKKIARFKTRQGKDIAIRLKDAPKLGLSQGDILFKEEKEIIAVNILDSEVIHIQAKSVAEVAKICYEIGNRHAALYYGESQFEFKTPFEKPTLALLEKLGVQNRVLSSKLDSKERLTVSMPHSEPNFKVSLASDFKVVVK | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | Q9ZMZ5 |
P45142 | TRUB_HAEIN | tRNA-uridine isomerase | Haemophilus | MSRPRKRWRDVDGVFLLDKPQGMSSNDIMQKVKRLFQANKAGHTGALDPLATGMLPICLGEATKFSQFLLDADKRYLVTAKLGERTDTSDAEGQVVETREVNLETQQILTALEQFRGDILQVPTMFSALKHNGKPLYEYARQGITVEREARPITIFELNFIEYNAPFLTLEVHCSKGTYIRTLVDDLGEVLGCGAHVTMLRRTAVADYPVAEMMPINELQLLAESFPLSELDRLLLPTDTAVSKLPALHLDAEQSKAIGFGQRVKFANEQQLSGQVRLFSAENLFLGVLNRREYYSPTTINYTIRITSLPFL | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | P45142 |
P9WGC8 | TSAC_MYCTO | tRNA threonylcarbamoyladenosine biosynthesis protein MT1340 | Mycobacterium tuberculosis complex | MTETFDCADPEQRSRGIVSAVGAIKAGQLVVMPTDTVYGIGADAFDSSAVAALLSAKGRGRDMPVGVLVGSWHTIEGLVYSMPDGARELIRAFWPGALSLVVVQAPSLQWDLGDAHGTVMLRMPLHPVAIELLREVGPMAVSSANISGHPPPVDAEQARSQLGDHVAVYLDAGPSEQQAGSTIVDLTGATPRVLRPGPVSTERIAEVLGVDAASLFG | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. | P9WGC8 |
Q6MP18 | TPIS_BDEBA | Triose-phosphate isomerase | Bdellovibrio | MKKIFAANWKLFKSPKETREFFGQFKELAGKATGEVVFFPSAISLEAASESLKGTSIKFGAQNCYFQAQGAFTGENSAQVVKDLGGSYVLIGHSERRAIFGEGDALVADKVAFVQGLGLTPMLCIGETLQERESAKTFRVLETQLNLGLAKADKTKPVVVAYEPVWAIGTGKVATPEQVAETHTDVFNILKALGFETAPILYGGSVKPDNAAGLIKQPHVNGFLVGGASLEAKSFSEIASV | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q6MP18 |
A3P8N2 | TYPH_BURP0 | TdRPase | pseudomallei group | MTFLPQEFIRKVRDRAPLDTADVARFVQGVTAGDVTEGQIAAFAMAVYFNELPLSARIALTLAQRDSGDVLDWRGARLNGPVVDKHSTGGVGDLTSLVIGPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYDVAPSVDMLRRVVRDAGLAIVGQTAQLAPADKRIYAVRDVTATVESISLITASILSKKLAAGVSALAMDVKVGSGAFMPSAEQSAELARSIVDVGNGAGMRTAATLTDMNQALAPCAGNAIEVRCAIDFLTGAARPARLEAVSFALAAQMLTMGGLAADAHDARRRLRAVLESGAAAERFARMVAALGGPADLVERPERHLPRAAAAAPVAAARAGWIERIDARALGLAVVGLGGGRAKIGDTLDYSVGLSALAELGERVEAGQPLATVHARDADSAAQATDAVRRAYRIGAEPPAQTRVVHAVIE | The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | A3P8N2 |
Q4KL14 | TPC3L_MOUSE | BET3-like protein | Mus | MSRPAHKRPEYHKINKDLFVLTYGALVAQLCKDYEKDEDVNKYLDKMGYNIGTRLVEDFLARSCVRRCHSYSEIINIIAQVAFKMYLGITPSVTCHNSSRNEFSLILHKNPLAEFVEELPAGRSALCYCNLLCGIIRGALEMVHLAANVTFLQDRLKGDSVTEIGITFLKKLDEKKYRRKK | May play a role in vesicular transport from endoplasmic reticulum to Golgi. | Q4KL14 |
P15620 | ZN271_MOUSE | Zinc finger protein 35 | Mus | MEIQFSYESQDHHFLSDGETKIKIGEPATEEEMTGKIGTVTEESGSLEEDVPHDSRGKEFREFGEELNDQMLFRRRQYNCDECDQSFAWSTGLIRHQRTHWKPYECEECGKAFRMSSALVLHQRIHTGEKPYPCSWCIKSFSRSSDLIKHQRVHTGEKPYKCDECGKAFSQSSDLMIHQRIHTGEKPYQCSHCSKSFSQHSGMVKHLRIHTGEKPYMCNHCYKHFSQSSDLIKHQRIHTGEKPYKCDVCGKAFSQSSDRILHQRIHTGEKPYPCAQCNKSFSQNSDLIKHRRIHTGEKPYKCSECGKAFNQSSVLILHQRIHTGEKPYPCNQCTKSFSRLSDLINHQRIHTGEKPYPCSQCSKMFSRRSDLVKHYRIHTGEKPYECDKCGKTFSQSSNLILHQRIHTGEKPYPCNSCSKSFSRGSDLIKHQRVHTGEKPYTCNLCSKSFSQSSDLTKHQRVHSGEKPYHCSSCNKAFRQSSDLILHHRVHTGERPYACTQCPRSFSQKSDLIKHQRIHTGEKPYKCMCGKAFSQCSAFTLHQRIHTGEKPYPCAQCGKSFSQRSDLVNHQRVHADQKLQM | May act to control gene activity during the pachytene stage of meiotic prophase. May function as a transcription activator. | P15620 |
B5EI26 | TIG_CITBB | PPIase | Citrifermentans | MQISVESVNSIKKKLNFEIPADKVSAEVDKAYAEIRKHAAIKGFRKGKVPMSLIEKHYGEKMAEDVVKNLVQESYFSAVSEQGLNPVGYPAIESNPLKKGESFKYSATVEVFPEVEVKDYTGLAVVKEKLEIDDSVVAARLKEMQERMSQLGPAPEGHAAAMGDFVTFDFKGAMDGVYFEGGSAEDFQLELGSGRFIPGFEEQMVGMTVGTNSTIKVNFPEGYGNADLAGKPADFEVSIKEIKVKELPELNDDFAKEFGEEFETLDLLKAKLAEMNEAQEVSRINAELRDRLIKALIEKNELEVPEALVDRQAQMMLESTKQRLASQRLSLEMMGMTDDSYKAQFRDNAREQVKGSLLLDAVAEKEKIEPTEEEFEAQLSVIAEQTRQDLEKVTQLYKTNERAKDNLMAQMREDKAVQFILDRAKVTEVPKAEIK | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | B5EI26 |
Q8REL0 | UVRC_FUSNN | Excinuclease ABC subunit C | Fusobacterium | MDIGKIDIPESSGVYLMKKNNKVIYVGKAKNLKNRVSSYFNRVHESEKTNELVKNIEDIEFFLTNTEIDALLLENNLIKKYSPKYNILLKDEKTYPFIKISKEDFSSIKIVRTTKALDIKSGEYFGPYPYGAWRLKNILMKLFKIRDCNRDMKKTSPRPCLKYYMKSCTGPCVYKDIKEEYNKDVENLKQVLKGNTSKLINELTALMNKASQDMDFEKSIIYREQIKELKSIASSQIIQYERELDEDIFVFKTILDKAFICVLNMRDGKILGKSSTSIDLKNKITDNIYEAIFMSYYSKHILPKSLVLDAEYENELSVVVKALTIEDSKKKEFHFPKIKSRRKELLDMAYKNLERDIESYFSKKDTIEKGIKDLHDILGLKRFPRKIECFDISNIQGKDAVASMSVSIEGRAARKEYRKFKIRCKDTPDDFSMMREVIERRYSKLPDIEFPDVILIDGGLGQINSAGEVLKRLGKIHLSELLSLAERNEEIYKYGESIPYVLSKDMEALKIFQRVRDEAHRFGITYHRKIRSKRIISSELDKIDGIGEVRRRKLLTKFGSISAIKKASIEELKEIIPEKVALEIKNKIR | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q8REL0 |
Q7UM42 | TSAD_RHOBA | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Rhodopirellula | MTPTAASELLLSIESTCDETAAAVIRRDGTVLGQCIATQETLHEQFGGVVPEIAARAHLERILPVIDTALTQAKVRGEDLTAIAVADRPGLAGSLLVGVVAAKTLALAWNKPLISLNHLHAHLYACQLIEGAPANIYPAIGLIVSGGHTSLYVCRTAIDLEYLGGTIDDAAGEAFDKVAAMLSLPFPGGIEVAKLASQGNDKAYSFPRSMIHDPGDDFSFSGLKTAVRYAIVGPGRQDFASLDISDQVKRDVCASFEAAVVDVLVSKCRRAIKRHRNRNNDPQNSINRLIVGGGVAANQRLRRDLQAAADKDGFELWIAPPHLCTDNAVMGAIAWKKFEAEQFASLDLDITPGLQRGF | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | Q7UM42 |
A4XTM7 | TAL_PSEMY | Transaldolase | Pseudomonas | MTSKLEQLKQFTTVVADTGDLDAIARLKPVDATTNPSLLLKAASLPGYADLLKQAVSTGKGDPGLACDHFAVAVGQEILKVIPGRISTEVDARLSFDTGATLLRAERLIGLYEQAGIGRERVLIKIASTWEGIRAAEQLEKSGVQTNLTLLFSFAQAQACADAGVFLISPFVGRIYDWYKKTEGRDFVGSEDPGVQSVSRIYDYYKANGYDTVVMGASFRNLGQIEALAGCDRLTISPELLQKLAEDEGELSRKLAPGGAGEARQTLDESAFRWALNEDAMATEKLAEGIRLFARDQEKLEALLAAKA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | A4XTM7 |
A0Q1Q3 | YBEY_CLONN | Endoribonuclease YbeY | Clostridium | MIYIDNRQDKIKIDEKTLNTLDEIIKYALKEEEVYVNTEVSVILIDNDTIKEINKETRDIDKVTDVLSFPMLDYPKGKTYKEVYKDYEFDASYLDEGELVLGDIVLSLERAEEQSKEFGHSFLREVCYLTIHSVLHLLGYDHMEDDEKAIMRKREEEILNKFSIKR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A0Q1Q3 |
Q6GJG2 | TILS_STAAR | tRNA(Ile)-lysidine synthetase | Staphylococcus | MQLNSNGWHVDDHIVVAVSTGIDSMCLLYQLLNDYKDSYRKLTCLHVNHGVRSASIEEARFLEAYCERHHIDLHIKKLDLSHSLNRNNSIQNEARIKRYEWFDEMMNVLEADVLLTAHHLDDQLETIMYRIFNGKSTRNKLGFDELSKRNGYQIYRPLLAVSKKEIKQFQERYHIPYFEDESNKDNKYVRNDIRNRIIPAIDENNQLKVSHLLKLKQWHDEQYDILQYSAKQFIQEFVKFDEQSKYLEVSRQAFNNLPNSLKMVVLDCLLSKYYELFNISAKTYEEWFKQFSSKKAQFSINLTDKWIIQIAYGKLIIMAKNNGDTYFRVQTIEKPGNYIFNKYRLEIHSNLPKCLFPLTVRTRQSGDTFKLNGRDGYKKVNRLFIDCKVQQWVRDQMPIVLDKQQRIIAVGDLYQQQTIKQWIIISKNGDE | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | Q6GJG2 |
A4WG70 | ZAPB_ENT38 | Cell division protein ZapB | Enterobacter | MTMSLEVFEKLESKVQQAIDTITLLQMEIEELKEKNNALAQEVHSAQNGREELERENQQLREQQNGWQDRLQALLGRMEEV | Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA. | A4WG70 |
P95508 | YIHI_MANHA | Der GTPase-activating protein YihI | Mannheimia | MSRTKKTRRITDIMPARKTDKPKQPMPKLGGGKNRKLTRYELDAQAREEKRKRKHKGLPTGSRNADPAEQKKAVVKEVKDPRIGSRKKVPLMVEFVNQPEKGRTIKAVPVEPIKPTLSPEQELEQLENNECLNQLLDDLEAGKTLSAEDQKFMNECLDRIDELMTELGIEYEDEEGDNGDALLRQFETMDINKFR | A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis. | P95508 |
Q5Y4U2 | TXAG1_AGEOR | AgorTX_B7b | Agelena | MCVATCLCTFAYVLAKSDEGENLISKVEETQRGCIEIGGDCDGYLDKSYCQCCRNNGFCSCYKVPEWFGYKVGCKCSVDWNFVGWCRLKQFCPGGSQNPSLCKDPNPRRRRHGK | Inhibits voltage-gated calcium channels (Cav). | Q5Y4U2 |
Q9ZQZ9 | TI204_ARATH | Translocon at the inner envelope membrane of chloroplasts 20-IV | Arabidopsis | MQGLAATTTNRGSLTFLAPRNHSPISKKFVNPRVFFPNVDSSAKLRLSASSISRRCPREIAPLSATASVDFAAAATSSNQLFANGLPPLAPGLRRHRRPIEPARVAKDDFFKIKLPKIAERPEWWWRTLACVPYLISLQISDVGFYVQPFLEKHDAIGDMIYFIPGAINRWPTWFFMVYCYLGYMWVVKNKELPHYLRFHMMMGMLLETALQVIWCTSNFFPLIHFKGRFGMYYWMAIGFTYICLLLECIRCALAGVYAQIPFMTDAASIHTLFNLGGFQRPLR | Involved in protein precursor import into chloroplasts. Partially redundant with TIC20-I, but not with TIC20-II or TIC20-V. | Q9ZQZ9 |
Q732R2 | TRUB_BACC1 | tRNA-uridine isomerase | Bacillus cereus group | MEGVVLLHKPKGMTSHDCIFKLRKILREKRIGHTGTLDPDVTGVLPICVGRATKIAQFLTSETKTYEGEVTLGFSTTTEDASGEVVETKHVDRVITRKEVEEVLAALTGTIEQMPPMFSAVKVNGKKLYEYARAGQEVERPVRTITIHEFVLLDEREVFEGENISFRFRVTCSKGTYVRTLAVMIGEKLGFPSHMSHLVRTASGEFVLEDCISFEEIEENVQNGTVESIFISIDEALSKFPKMVVDEKQAEKIKNGMFLKNELQITAPFITVFDKNDRCLAIYEHHPKHPGMLKPMKVLVNNQELKL | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q732R2 |
Q7VKR6 | THII_HAEDU | tRNA 4-thiouridine synthase | Haemophilus | MKFIIKLFPEIMIKSDSVRKRFIKILTSNIRNVLLRETEQVAVVRNWDFIEVRAKVAEEIPLILDLLKRTPGIHHILEVQEMPFTSLHDIFEHTFAKYQNQLVDKTFCVRVRRKGKHEFSSLDVEKYVGGGLNQRIESARVKLTKPDVTVRIDINGDKMLLVEARHEGLGGYPIGTQEDVLSLISGGFDSGVSSYMFIRRGSRVHYCFFNLGGASHEIGVKQMAYHIWSRYSTSHKVRFVAINFESVVGEILEKVDNGQMGVVLKRMMVRAASQIAERFAIQAIVTGEALGQVSSQTLTNLRLIDKAADSLVLRPLITHDKEKIIALAKQIGTDDIAKSMPEFCGVISKNPTVKAIESKIVEEEGHFDFDVLEKAVQNATYLDIREIALQTEKDVVAVEATSALTEKDIILDIRSPEEMDEKPLVLAQAQVIELPFYKLSTQFAHLDQSKNYLLYCERGVMSKLQALYLKEKGYQNVKVFNLPK | Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. | Q7VKR6 |
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