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
|
|---|---|---|---|---|---|---|
B5FDT8 | UBIG_ALIFM | 3-demethylubiquinone 3-O-methyltransferase | Aliivibrio | MTQQLNVDPAEIKKFEDMASRWWDLEGEFKPLHQINPLRLNYVLENANGLFGKKVLDVGCGGGILAESMAKQGADVVGLDMGKEPLTVARLHALETGTKLEYVQSTAEQHAEENPETYDVVTCMEMLEHVPDPLSVIRSCAKMVKPGGHVFFSTLNRNIKSYLFAIVGAEQLLKLVPKGTHDHNKFIRPSELLKMLDQTALQERGITGLHYNPLTDTYSLGKNVDVNYIVHTTL | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | B5FDT8 |
O95670 | VATG2_HUMAN | Vacuolar proton pump subunit G 2 | Homo | MASQSQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREHEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCDVRPQVHPNYRISA | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. | O95670 |
A5VYH8 | UPP_PSEP1 | UPRTase | Pseudomonas | MPTREIRHPLIRHKLGLMRRADISTKNFRELAQEVGALLTYEATQDLPLETYEIDGWCGKVSVEKIAGKKITVVPILRAGIGMLDGVLSLIPGAKVSAVGVARNEETLEAHTYLEKLAPDINQRLALIIDPMLATGGSMVATIDLLKKAGCKEIRAMVLVAAPEGIEVVEKAHPDVKIYTASIDQRLNEHGYIVPGLGDAGDKIFGTKQKDA | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | A5VYH8 |
Q9WYV0 | UVRA_THEMA | Excinuclease ABC subunit A | Thermotoga | MNEIVVKGARVHNLKNITVRIPKNRLVVITGVSGSGKSSLAMDTIYAEGQRRYLESLSTYARQFLGNLKKPDVDEIEGLSPAIAIDQKTVSHNPRSTVGTVTEIYDYLRVLYARIGKAHCPECGRPLEKKSIDEILQDLFNSFKEGSRIYILAPVATEKKGTFKKEIEEFISKGFARIEIDGEIYRLEEVPELDKNKRHTVKLVVDRLILETRNEHRILDSLELAMREGKGFVEIRNVDTGESKIFSENLMCPVCGIGFPEITPKLFSFNSPYGACPNCHGLGFTFEVDPSLVIDEEKSVLEGAIIPYRWDRRLSRWVAREIEKRGVSPHLPFKDLPEDVKEFILYGDDRFEGVVPKVQRWHRETESPEMKEWLEKNFIVQRTCSVCGGRRLNREALSVKINGLNIHEFTELSISEELEFLKNLNLTEREREIVGELLKEIEKRLEFLVDVGLEYLTLSRSATTLSGGESQRIRLATQIGSGLTGVIYVLDEPTIGLHPRDTERLIKTLKKLRDLGNTVIVVEHDEEVIRNADHIIDIGPGGGTNGGRVVFQGTVDELLKNPDSSLTGEYLSGKRKITVNKTRRLPYASLKIKGVRHNNLKNIDVEIPLGVFVCVTGVSGSGKSSLVMETLYPALMNLLHKTKLPAGEFDSIEGHENIDKMIAIDQSPIGRTPRSNPATYTKVFDEIRSLFAMTPAAKARGYNKSRFSFNLKGGRCEACQGQGYVKIEMLFLPDVYVECDVCKGKRYNRETLEITYKGKNISDILDMTVDEALEFFKNIPSIKRTLQVLHDVGLGYVKLGQPATTLSGGEAQRIKLASELRKRDTGRTLYILDEPTVGLHFEDVRKLVEVLHRLVDRGNTVIVIEHNLDVIKNADHIIDLGPEGGKEGGYIVATGTPEEIAKNPHSYTGRFLKNVL | 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. | Q9WYV0 |
Q8NZU4 | TRMB_STRP8 | tRNA(m7G46)-methyltransferase | Streptococcus | MRVRKRKGAEKHLANNPHYVILNPEDAKGRWHDVFGNDRPIHIEVGSGKGGFITGMALKNPDINYIGIDIQLSVLSYALDKVLASEVPNVKLLRVDGSSLTNYFEDGEVDMMYLNFSDPWPKTKHEKRRLTYKDFLDTYKRILPEHGEIHFKTDNRGLFEYSLASFSQYGMTLRQIWLDLHASNYEGNVMTEYEEKFSNKGQVIYRVEANF | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q8NZU4 |
Q7VRS7 | UREF_BLOFL | Urease accessory protein UreF | Candidatus Blochmannia | MNIHRECRSLLSLIQIVSGNLPTGGFSYSKGLESAIEYGWVKSLEDFLNWQKQWIHEQLIYIDWPMLKRCYYYTKINDSKNFKKCALQILSYRDTYELRLEEQRRGKAMEKLISQWYDPISDSWAVAFKCSGLASMAWLGYEWNIPIKNLALGYAYNALESSIMVGLKLLPFGQRTAQKLLRYLVEFLPNAWDKADLVKDHEVGGNFLLQSIASACHEDQYSRLFSS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q7VRS7 |
Q9NZ09 | UBAP1_HUMAN | Nasopharyngeal carcinoma-associated gene 20 protein | Homo | MASKKLGADFHGTFSYLDDVPFKTGDKFKTPAKVGLPIGFSLPDCLQVVREVQYDFSLEKKTIEWAEEIKKIEEAEREAECKIAEAEAKVNSKSGPEGDSKMSFSKTHSTATMPPPINPILASLQHNSILTPTRVSSSATKQKVLSPPHIKADFNLADFECEEDPFDNLELKTIDEKEELRNILVGTTGPIMAQLLDNNLPRGGSGSVLQDEEVLASLERATLDFKPLHKPNGFITLPQLGNCEKMSLSSKVSLPPIPAVSNIKSLSFPKLDSDDSNQKTAKLASTFHSTSCLRNGTFQNSLKPSTQSSASELNGHHTLGLSALNLDSGTEMPALTSSQMPSLSVLSVCTEESSPPNTGPTVTPPNFSVSQVPNMPSCPQAYSELQMLSPSERQCVETVVNMGYSYECVLRAMKKKGENIEQILDYLFAHGQLCEKGFDPLLVEEALEMHQCSEEKMMEFLQLMSKFKEMGFELKDIKEVLLLHNNDQDNALEDLMARAGAS | Component of the ESCRT-I complex, a regulator of vesicular trafficking process . Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) . Plays a role in the proteasomal degradation of ubiquitinated cell-surface proteins, such as EGFR and BST2 . | Q9NZ09 |
A1VJ15 | TGT_POLNA | tRNA-guanine transglycosylase | Polaromonas | MLEFEVLKTDPATVDSEGAYLGSYARRGQLTLNHGVVQTPIFMPVGTYGTVKGVTPQSLHDMNAQIILGNTFHLWMRPGLDVVAQFGGLHKFESWHKPILTDSGGFQVWSLGEMRKISEEGVKFASPVNGDKLFLTPEISMQIQTLLNSDIVMQFDECTPYDTKGHITTEGEARSSMELSRRWAKRCEIEFDKLENPNALFGIVQGGMFENLRQESLDALVEMDFPGYAVGGVSVGEPKEEMLRIMAHTPHRLPAHKPRYLMGVGTPEDLVEGVASGVDMFDCVMPTRNARNGHMFTRFGDLKIRNARYKSEEAPVDSTCGCYTCRNFSRAYMHHLDRCGEMLGPMLSSIHNLHYYLNLMQEVRGALDAGRFGEFVRQFKADRQRGV | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). | A1VJ15 |
Q5VY80 | ULBP6_HUMAN | Retinoic acid early transcript 1L protein | Homo | MAAAAIPALLLCLPLLFLLFGWSRARRDDPHSLCYDITVIPKFRPGPRWCAVQGQVDEKTFLHYDCGNKTVTPVSPLGKKLNVTMAWKAQNPVLREVVDILTEQLLDIQLENYTPKEPLTLQARMSCEQKAEGHSSGSWQFSIDGQTFLLFDSEKRMWTTVHPGARKMKEKWENDKDVAMSFHYISMGDCIGWLEDFLMGMDSTLEPSAGAPLAMSSGTTQLRATATTLILCCLLIILPCFILPGI | Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity. | Q5VY80 |
Q95WA2 | TCTP_SCHMA | Histamine-releasing factor | Schistosoma | MIVYKDMITEDEMFTDSHCPRVVADFFYEVDSRFTTVSSNVDGRLIGANPSGEGGEDENVDDTSKRVIDLVHANGFISVPFDQKSYKAHLNLYLKTIIERLQKTDPDKVPLLKSQVNKYMKNVLDNFDQYEFYMGPPSNPDAMIVLMNFREDGMTPYFVFFKDGLT | Involved in calcium binding and microtubule stabilization. | Q95WA2 |
Q5R5J8 | ZDHC9_PONAB | Zinc finger DHHC domain-containing protein 9 | Pongo | MSVMVVRKKVTRKWEKLPGRNTFCCDGRVMMARQKGIFYLTLFLILGTCTLFFAFECRYLAVQQSPAIPVFAAMLFLFSMATLLRASFSDPGVIPRALPDEAAFIEMEIEATNGAVPQGQRPPPRIKNSQINNQIVKLKYCYTCKIFRPPRASHCSICDNCVERFDHHCPWVGNCVGKRNYRYFYLFILSLSLLTIYVFAFNIVYVALKSLKIGFLETLKETPGTVLEVLICFFTLWSVVGLTGFHTFLVALNQTTNEDIKGSWTGKNRVQNPYSHGNIVKNCCEVLCGPLPPSVLDRRGILPLEESGSRPPSTQETSSSLLPQSPAPTEHLNSNEMPDDSSTPEEMPPPEPPEPPQEAAEAEK | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS. May have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and therefore regulate G protein-coupled receptor signaling. | Q5R5J8 |
Q813X6 | TOX1_BACCR | Ribonuclease BC_0920 | Bacillus cereus group | MSLNMYLGEVQGQTQSMNAVCNATIQGMEQVIQSIDAFAIDTVLQGQTYSSAKSFFVQTFRPLAQGIIYLCEELIRQNDAFPSQFQSQVASTDVIEQEILEQIREIDRMKASMEAISQAMPIPGMDAMANLFTVMRKKLQEKLDHLYQFNQTSSNNYSTALQLAASIAAGLAEVQSGKGFSPASGTFSTQGLNMEWTTSIQAITEERARQAANSIEEGEMCGKLPEKSTGEKIWDGIVEGTGQAVSDTIDGIKALGDWETWENMGNAALHPIDTLSTMYNTLSDSFINDVINGDAESRAKWGSYALTQVGLGLIGDKGLSKASKLGQAGKVTKLAKNKIPQAVSHITSNLQMGDRFAFAGGNSLRFRFDTPDFKKAEEKLSTYQFARGESNYGGSNFVNENHRSSLSNREIISNLQHTEKFRPNTLKHILEGEINWRGDAMGYHTEVLENTPGKIISGTEEILNDQGIYKARVEVNGTPKTGNRGFSTFFPKDWSPQKIVDNINEAYNNRTYEFGNTYSGIGSEGIRISMYIDGNGKIISAFPAE | Toxic component of an LXG toxin-immunity module. The C-terminus (residues 322-545) has RNase activity in E.coli which is neutralized by cognate immunity protein BC_0921, but not by immunity proteins specific to other toxins with the LXG domain . Degrades 5S rRNA and several tRNAs in vitro; cleavage is endonucleolytic within the anticodon loop for tRNA(GAU-Ile) and tRNA(UUC-Glu) but total for 5S rRNA and at least one other tRNA. RNase activity is suppressed by cognate immunity protein BC_0921 . | Q813X6 |
A1U6H0 | TRPD_MARN8 | Anthranilate phosphoribosyltransferase | Marinobacter | MDMKQALNRIASNLDLSRDEMKDVMRIVMNGEATDAQIGAFLMGLRLKSETIDEITGATEVMRELATGVTVNAEPLVDIVGTGGDGANLFNVSSAASFVVAAAGGYVAKHGNRGVSSKSGSADLIEKAGINLNMKPEEVARCVEQIGVGFMFAPAHHGAMKHAIGPRRELGCRTIFNILGPMTNPAGVTRQLIGVFTRELCRPMAEVLQRLGAEHIMVVCSKDGLDEISLATVTHVAELKDGEITEYDLTPEDLGIKSQSLVGLSVDGADESLALIKAAFGRSHDETTEKARDMIALNAGAAIYVAGLARTAKEGVDMALDAMGSGLAAGKMSELADFSQCF | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A1U6H0 |
B1JX27 | UREF_BURCC | Urease accessory protein UreF | Burkholderia cepacia complex | MTTTELVVLLHLASPALPIGAYSYSQGLEAALDANLIRDADSARDWIASGLTDVLAHGELPFLAHQLARWQTHDTHALAAENAWFVASRESAELRRETEQMGWSLAQLCASLEWGDAARRATLASLSPIALPTAFAYAAAAHDAGADATLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVALRGAIDAAVRRALATPPDAVNTFAPQLGILSARHETQYSRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | B1JX27 |
B1Z8R3 | UREG2_METPB | Urease accessory protein UreG 2 | Methylorubrum | MKKITRIGIGGPVGSGKTAVIETITPRLIERGIKPLIITNDVVTTEDAKQVRRTLNGVLIEEKIVGVETGACPHTAVREDPSMNIAAVEELEDKYPDSDVILIESGGDNLTLTFSPALADFYIYVIDVAAGDKIPRKNGAGVCQSDILVINKRDLAPYVGASLEVMARDSKIMRGKKPFLFTNCKTGEGIDDLLRLILDMALFDVTTNRPLAASA | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | B1Z8R3 |
Q73FE5 | TILS_BACC1 | tRNA(Ile)-lysidine synthetase | Bacillus cereus group | MKDTFVEKVDDFVKQHDVLKERSTIVVGVSGGPDSVALLYYLLEKRAAKQFEIVVAHVDHMFRGDESHEDLQFVQDLCKELGVICETIRINVSQYQQQYGMNAQVAARECRYAFLERIMKKYDARYVALGHHGDDQVETILMRLVRGSTPKGYAGIAVKRPFHNGYLIRPLLGVTKEEIVDYCHKLKIIPRIDPSNKKEVYTRNRLRKYVLPHLKEENPQVHEKFQKFSMQMQEDEAYLQELAFEKMNKVITKKSDKQISLSIPAFESMSMPLQRRGIQLILNYLYEYKIPSSLSSIHIDKVIEFFKRTQPSGSLDFPGDLKIVRAYEECSFGFKQEIVSPFLQDLSVPGTITLSNGDKLVTEVSEDIPSNMNETVFVAKYNDISYPLRIRSRENGDRMSIQGMNGTKKIKAIFIEAKVPREKREEWPVVCDARGNVIWLPLLKRSAFAISKETAKKDKYMIIHYKSKESSGRIMK | 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. | Q73FE5 |
A1K668 | YCIB_AZOSB | Inner membrane-spanning protein YciB | Azoarcus | MKFFLDLLPVILFFVAYKFAGAAPDDSHALVAQFLGAGISPSQAPILIATAVAIAATLAQVLIVWLRHGKVDKMLWVSLAIITLFGGATLVFHNPTFIKWKPTVFYWTFAGALAVSALLFRRNLVQKMLEAQIRLPAPVWQRLNLAWIGFFTLMGFLNLYVAYGYSEEAWVNFKLFGAMGLMLAFFLGQGFYLSRHLEEDAK | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | A1K668 |
B1YUF7 | UREF_BURA4 | Urease accessory protein UreF | Burkholderia cepacia complex | MTTTELVALLHLASPALPIGAFSYSQGFEAALDANLIRDADTARDWIASGLTDVLAHGELPFLAHQLARWHAHDADALARENAWFIASRESAELRRETEQMGWSLAQLCTSLEWGDAARRATLATISPIALPTAFTYAAAAHDASADAVLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVALRGAIDAAVRRALATPPDAVNTFAPQLGILSARHETQYSRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | B1YUF7 |
Q5C8T6 | TRIM5_GORGO | TRIM5alpha | Gorilla | MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHEKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAQECQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDILKRLTKSETEMVQQTQSVRELISDLEHRLQGSVMELLQGVDGVIKRMENVTLKKPETFPKNRRRVFRAPDLKGMLEVFRELTDVRRYWVDVTVAPNNISCAVISEDMRQVSSPKPQIIYGAQGTRYQTFMNFNYCTGILGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDATCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDGSFHTPSAPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCRVPMTLCSPSS | Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. | Q5C8T6 |
A6RIB9 | TVP38_BOTFB | Golgi apparatus membrane protein tvp38 | Botrytis | MPADYSSTARALALPISPLETPSSPDQHVERPPWSRRISSNVRRANNSASPYSNQPTTSFKDQILRKAEKLQRKFVSTWQKLSPLQKCLAVGAAVLNIILIALFLVYQHQIFASLAPFAERWRDMRGGWMILWAMTFVAAFPPLIGYSSTITIAGFVYGVPKGWAIVASATVAGSLCSFLASRTILSSYVHRLVGKDKRFEALALTLKHDGIKILCMIRLCPLPYSLSNAAVATFPTVHPLNYALATALVTPKLFIHVFIGSRLGSLAGDEEMDASTKLINYASIIIGAGLGATVGYVIYQRTMARAKELEIEELEAANGDVAAGRRVAAEYSDANNDDAALMNDDDISLWDNEDAQTGYTDFVDEDEADVFASGDLDEEGNIGGKGKTAGT | Golgi membrane protein involved in vesicular trafficking and spindle migration. | A6RIB9 |
Q6ZCX1 | YSL17_ORYSJ | Protein YELLOW STRIPE LIKE 17 | Oryza sativa | MAEEARGGQRVVVDDDREDASSVASSTERAFEGEPLPSLGETVTARSAAVSGVLGAVVSVVAMRLNLTSGLLPSLGVPAGLLGFFLARVWIRALDVVGVSHLPFTRQENTLIQIAVVSCSTIAFSGGFGTYILGMSGKSANEGHIGSHGRNVEEPNIGRVIAFLFLVNFSGLFIIVPLRKMMIIRHRLTFPSGTATAHLINSFHTPHGAKQARLQVVTLFKSLGATVLWPIFQWFFAGGKNCGFQIFPTFGMAAYRRGFYFDFSTTNVGIGMICPPMITASMLAGSIVSWGILWPYIETKAGRWFPENLDANDLGGIMGYRVFVGVSMILADGLFTILSALVRTACAMRKRRRGASTVTAAVPPFQCLSATERTMQSFDDRRRAQVFLRDSFPTWVAVASYAALAALSVVAVPLLYPQLGHRHVAAAYVAAPVFAFCNAYGVGVTDMNLSATYGKIAMMVFSSWVGMDGGGVVAGLAACGIIVSAVSGSSDFMQDFKTGYLTLTSPRAMLVGQVAGTALGCVVNPAIFWVFYKVYNMGGGGGDGADVAPYARAYRGIAVLSVGRHGLPDHSVLLCKLFFAMALALSAAREVAERRRWRALRYIPSTIGVAVAFFVPPRIPVGMAVGCLALHVWRRHVDAGGARLLLPAVASGLICGDGLGSLASSMLTLLRARPPICIKFVSRFENQKLDAFLATRHA | May be involved in the transport of nicotianamine-chelated metals. | Q6ZCX1 |
Q8Y6U8 | TPX_LISMO | Thioredoxin-dependent peroxiredoxin | Listeria | MTQVTFKHNPVTLVGTERKVGDKAPNFTVVNRDLEEVTLHDYDGKVRLISVVPSIDTSVCSTQTRKFNEEASNLDNTVVLTISVDLPFAQKKWCAAEGLPNAITLSDHRDLSFGEAYGVIMKELRLLARSVFVVNAVGEIVYTEVVPEGSDHPNYEAAIEAAKKA | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | Q8Y6U8 |
Q3IZ05 | TRMD_CERS4 | tRNA [GM37] methyltransferase | Cereibacter | MLKGAWQARIVTLFPEAFPGTLGLSLTGKALEMGLWSLETIDLRPFGEGRHRNVDDNPAGGGAGMVLRADIVARALDAASVGTPPERSRWPVVYLSPRGKPFSQAMARDWAGAEGLTLLCGRFEGVDQRVLDAYAVEEVSLGDFVLTGGEIAAQALIDATVRLIPRVLGNHASTEEESFSEGLLEFPQYTRPTVWQDRTIPEVLLSGHHANIARWRRAEAERLTKERRPDLWRAYCAARGRDPDEDREL | Specifically methylates guanosine-37 in various tRNAs. | Q3IZ05 |
P41352 | TBB_TETTH | Beta-tubulin | Tetrahymena | MREIVHIQGGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGRYVPRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPDRIMETFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVIDNEALYDICFRTLKLTTPTYGDLNHLVSAAMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMIGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSICDIPPKGLKMAVTFVGNSTAIQEMFKRVAEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFEEEEGEN | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | P41352 |
Q6IQC7 | TMX2B_DANRE | Thioredoxin domain-containing protein 14 | Danio | MALLTPLFAFLYHLPQVYKWLLKPYYIASLFMSIAFVMIRKMPGVCEHLSTQREDGNSCDFDWREVEILMFLSAIVMMKNRRAITIEQHVGNIILFCKVANVILFFRLDIRLGLLYLTLCIVFLMTCKPPLYMGPEYIKYFSDKTIDEELEKDHRVTWIVEFFANWSPECQSFASVYADLSLKYNCAGLKFGKVDIGRYGEVSKKYRVSTSPLSKQLPSLVLFQGGKEVMRRPQVDKKGRAVSWTFTEENIIREFNLNELYQKSKKLGKTKEKLERPSELVFSTVPEEEEPEAETISAMDTESKKDK | 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. | Q6IQC7 |
B1KNS7 | TILS_SHEWM | tRNA(Ile)-lysidine synthetase | Shewanella | MTEPSFNTSALIEESIKSAKINVGAKLVLAYSGGVDSEVLAQGLSLYAKSHPEFRYLLVHVHHGLSRNADAWVTHCQKQALDYQLPIEVVQVQVKTGPRLSIEAEARRARYKAITSLMDSADVLLTAHHLDDQLETVLLALKRGLGPKGLSAMGALQVFDGDKQLLRPLLNVSREQIEAKAASLSLPHIEDESNTDDKYDRNFLRLQIIPKLKSRWSAIATTASRSAALCAQQQAVIDDEVSARLPNFIELVPYGEGTALNLDLLSHQTPNWQALLLRGYIESSGFAPVSQIQLEQLLSQLLTAKPDANLEVRIADMLVRRFREKAYLSSYRPHKPKSLESIELTLESEVHFVQEINIPLLSNIRVEVLEDDGGERVRLPLIEEKVSVRFSAVGSLRCHPHNRQKGRELKKLWQEYGVPPWERERVPLIFYNEKLVCAVGYWVEHSFQSAEHETGLRFSIAIVSNECESI | 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. | B1KNS7 |
P57515 | TYSY_BUCAI | Thymidylate synthase | Buchnera | MKQYIKLIKKIIRVGNQKKDRTGTGTLSIFGYNMKFDLKKGFPLLTTKKCHIASIIYELLWFLKGDTNISYLNENKISIWNNWANESGDVGPIYGKQWRNWSTPEGHEIDQIKNVLIQLKKNPDSRRMLVSSWNVGDIDKMRLPPCHVLFQFYVFNNTLSCQLYQRSCDVFLGLPFNIASYSILIHMIAQQCDLKVGDFLWTGGDVHLYNNHIELAKKQILRIPRTLPKLTILKKPQSLFQYCFEDFKIIGYHPYPAIKGEISI | Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | P57515 |
C0HL49 | TP1A_RANIT | Temporin-1ITa | Rana | FLGAIAQALTSLLGKL | Antimicrobial peptide active against Gram-positive bacterium S.epidermidis ATCC 12228 (MIC=8 uM) and against yeast C.parapsilosis ATCC 22019 (MIC=64 uM) but not against Gram-negative bacterium E.coli ATCC 25922. Has hemolytic and cytotoxic activity. | C0HL49 |
Q9I744 | TSSF1_PSEAE | Type VI secretion system component TssF1 | Pseudomonas | MNPRLLEYYNQELQHIRESAAEFAEEFPKIAGRLSLSGFECADPYVERLLEGFAYLTARVQLKLDAEYPTFTHNLLEIAYPHYLAPTPSMTVVQLRPDPNEGALSSGFSIERGASLRGQLGPDDQTACEYRTAHPVTLWPLEVAQADYFGNPAAVLGRLAASEPRAKAGLRIRLRSGAGIPFDSLSLDALPLYLHGADEQPYRLYEQLLGNACAVFVRAPDNAWVERLPTSSLRARGFDDEDALLPVVPRAFQGYRLLQEYFALPARFLFVEFSGLNRALRRCHGEELELVVLFGKHDQRLEGTVDAEQLVPFCTPAINLFPRRCDRIHLSDRVNEHHVIVDRTRPLDFEVHSLQQVSGHGSGPEQPFQPFYAVRDPARYGREQAYFRVRREPRVLSSKQRRKGPRSTYVGSETFVALVDANQAPYRHDLRQLGIAALCTNRDLPLFMPIGAHKSDFTLEDSAPVMQVRCLAGPSRPRASRAHDASAWRLISQLSLNYLSLAERGQGAAALRELLRLYGDSGDPALQLQIEGLREVSSKPCTRRLPMPGPIVFGRGLEITLDFDENAFRGTGVFLLGAVFERFLARYVSINSFTETVLRTGERGEVMRWQAKPGSRPNL | Core component of the H1 type VI (H1-T6SS) secretion system that plays a role in the release of toxins targeting both eukaryotic and prokaryotic species. | Q9I744 |
Q8VBT0 | TMX1_MOUSE | Thioredoxin domain-containing protein 1 | Mus | MAHLGRLMVPLAALVLLLWAVPGAHGRRNNVRVLTDENWTSLLEGEWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVKVAKVDVTEQTGLSGRFIITALPSIYHCKDGEFRRYVGPRTKKDFINFVSDKEWKNIEPISSWFGPSSVLMTMMSALFQLSVYIRTSHSYFVHDLGIPAWGSYLVFAFATVLSGLLLGLCMIFVADCLCPSKRRKPQQQYAKKTSPEFSQPLKKVEEEQEADEEDVSEEEAEDREGASKATSQSSIRQRCVGLPSATDTS | May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. | Q8VBT0 |
C3K7T2 | UVRC_PSEFS | Excinuclease ABC subunit C | Pseudomonas | MTTPFDPSAFLSTCSGRPGVYRMFDSEARLLYVGKAKNLKNRLASYFRKSGLAPKTAALVARIAQVETTITANETEALLLEQTLIKEWRPPYNILLRDDKSYPYVFLSDGNFPRLSIHRGAKKQKGKYFGPYPSAGAIRESLSLLQKTFFVRQCEDSFYKNRTRPCLQYQIKRCKAPCVGLVDPAEYAEDVRHSVMFLEGRSNALTDELSGAMEQAASTLDFERAAELRDQISLLRRVQDQQSMEGGTGDVDVIAAFVNPGGACVHLISVRGGRVLGSKNFFPQTGIDEEVAEVMAAFLGQYYVSSPERDLPSELIVNVVHEDFPTLIEAIHELRGRELDISHRVRGTRARWQQLAVTNAEQALGARLANRQHVAARFDALAEVLNLDEPPQRLECYDISHSSGEATVASCVVFGPEGPIKSDYRRYNIEGVTAGDDYAAMHQALTRRFSKLKDGEGKLPDILLVDGGKGQLSMARDVLNELAVPDLILLGVAKGATRKAGFETLYLNDSAHEFTLKGDSPALHLIQQIRDEAHRFAITGHRARRGKTRRTSTLEGVAGVGPTRRRDLLKHFGGLQELSRASIDEIAKAPGISKKLAELIYANLHSE | 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. | C3K7T2 |
Q9JME7 | TPC2L_MOUSE | Trafficking protein particle complex subunit 2-like protein | Mus | MAVCIAVIAKENYPLYIRSTPTESELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKFVMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSRAFDTMVTSMMIQVC | May play a role in vesicular transport from endoplasmic reticulum to Golgi. | Q9JME7 |
C1DEK7 | Y1984_AZOVD | Nucleoid-associated protein Avin_19840 | Azotobacter | MMKGGMAGLMKQAQLMQEKMQKLQEEIANAEVTGQSGAGLVSVVMTGRHDVRRVTLDDSLMQEDKEVLEDLIAAAVNDAVRKIEQNNQEKMAGMTAGMGLPPGFKMPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | C1DEK7 |
P0DJ50 | VKT31_MESMA | Delta-KTx 3.1 | Mesobuthus | MMNVITVVGIILSVVCTISDAEGVDCTLPSDTGRCKAYFIRYFYNQKAGECQKFVYGGCEGNSNNFLTKSDCCKQCSPGKC | Dual-function toxin that completely inhibits trypsin activity at a molar ratio of 1:1 (dissociation constant of 420 nM) and that inhibits mKv1.3/KCNA3 potassium channel currents with an IC(50) of 371.3 nM. | P0DJ50 |
Q8TZV9 | XERA_PYRFU | Tyrosine recombinase XerA | Pyrococcus | MREKTLRSEVLEEFATYLELEGKSKNTIRMYTYFLSKFLEEGYSPTARDALRFLAKLRAKGYSIRSINLVVQALKAYFKFEGLNEEAERLRNPKIPKTLPKSLTEEEVKKLIEVIPKDKIRDRLIVLLLYGTGLRVSELCNLKIEDINFEKGFLTVRGGKGGKDRTIPIPQPLLTEIKNYLRRRTDDSPYLFVESRRKNKEKLSPKTVWRILKEYGRKAGIKVTPHQLRHSFATHMLERGIDIRIIQELLGHASLSTTQIYTRVTAKHLKEAVERANLLENLIGGE | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. | Q8TZV9 |
A1URT5 | UBIG_BARBK | 3-demethylubiquinone 3-O-methyltransferase | Bartonella | MINKTRTTVDQSEIDHFSRIAAEWWNPQGKFRPLHKFNPTRLAYIKEKICLAFDRDPFSLAPFAGLKILDIGCGGGLLCEPMVRLGATVIGADAAQNNIEVAKIHATQSGLSIDYRATTAEKLADKGEKFDIILNMEIVEHVADVDLFISATAKMLKPQGLMFIATLNRTWKSWGLAIVGAEYILRWLPKGTHDYKKFLKPQELKKLLLTNSLKVIDELGITYNPLNDSWNRSKDMDVNYMLLVKRLQ | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | A1URT5 |
Q2M2T2 | TKTI1_BOVIN | Uncharacterized protein C19orf71 homolog | Bos | MQTLRRQAAWPCVPRGTLEVDFPPPLYSDDYLSQEGPRWTPAIKQATRWKYTPMGRDAAGQLWYTGLTNSDSREAWYTLPRAPDSPYREAYARWHGCYGHRERSLPSAYTQRLRETAWYDPIIPAQYTDPSTRWGSVLWKDRPIRGKEFAINRHRFGVEALWRASDYVRYLSAPQRPRYTAQNYRQWGLEPYCPATNQRPPPVYTPSH | Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Located at the center of the tektin bundle where may function to recruit tektins or stabilize the bundle. | Q2M2T2 |
A9HZS2 | UBID_BORPD | Polyprenyl p-hydroxybenzoate decarboxylase | Bordetella | MKYRDLRDFLQQLELRGELKRIATPVSTHLEMTEIADRVLRAQGPALLFEHAVHNGARAAMPVLANLFGTPRRVAWGMGADEVSALRDTGELLASLREPEAPRGLRDALGKVAMLKSALWDMAPKRVRGPACQEIVWEGADVDLARLPIQTCWPGDVAPLLTWGLVITRGPNARRQNLGIYRQQPIAPNKLIMRWLSHRGGALDFREHARAHPGTPFPVAVALGADPATILGAVTPVPDSLSEYQFAGLLRGSRTEVGQALGSDLSVPAWAEIVLEGHLLPANDPRAVAPVVPEGAPPPPDTGYEMALEGPYGDHTGYYNEQDWFPVFTVDRITMRRDPVYHSTYTGKPPDEPAVLGVALNEVFVPLLRRQLPEIVDFYLPPEGCSYRLAVVSIRKQYAGHAKRVMFGLWSVLRQFMYTKFIVVVDDDIDPRNWNEVVWAITTRMDPVRDTVLVERTPIDYLDFASPVSGLGGKMGMDATNKWPGETDREWGRPIAMDDAVKQRVDAMWGELGL | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | A9HZS2 |
Q1CV84 | UREE_HELPH | Urease accessory protein UreE | Helicobacter | MIIERLVGNLRDLNPLDFNVDHVDLEWFETRKKIARFKTRQGKDIAIRLKDAPKLGLSQGDILFKEEKEIIAVNILDSEVIHIQAKSVAEVAKICYEIGNRHAALYYGESQFEFKTPFEKPTLALLEKLGVQNRVLSSKLDSKERLTVSMPHSEPNFKVSLASDFKVVMK | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | Q1CV84 |
Q500M2 | XPT_PSEU2 | Xanthine phosphoribosyltransferase | Pseudomonas syringae | MEALHKKIREEGIVLSDQVLKVDAFLNHQIDPALMKEIGDEFARLFADAGVTKIVTIEASGIAPAVMAGLNMGVPVIFARKHQSLTLTENLLTASVYSFTKQVESTVAISPRHLSSDDNVLIIDDFLANGKASQALISIIKQAGATVAGLGIVIEKSFQGGRAELDAQGYRVESLARVESLAGGVVTFK | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | Q500M2 |
Q13BD7 | UREG_RHOPS | Urease accessory protein UreG | Rhodopseudomonas | MSTHHGPLRVGIGGPVGSGKTALMDLLCKSMRERYDIAAITNDIYTKWDAEFLVRSGSLTPDRIAGVETGGCPHTAIREDASMNLAAVAEMRSKFPGLDLVLIESGGDNLAATFSPELADLTIYVIDVSAGDKIPSKGGPGITRSDLLVINKIDLAPYVGASLDKMDADARRMRGERPFVMTNLKTREGLERILSFIETKGGLKPKADTA | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | Q13BD7 |
Q6L1R1 | TBP_PICTO | TATA-box factor | Picrophilus | MSEMEKITIENIVASTSLAEHLDLSKIALALEGSEYEPEQFPGLIYRLQEPKTAVLIFRSGKVNCTGAKNLDDVKKTIDIIIDKLKKADIEVYDNPDIIVQNIVAVYDLESNLNLTDIAMSLGLENVEYEPEQFPGLVYRVEEPKVVLLLFGSGKVVCTGAKEENEIEQAVIKVKKDLQKVGLI | General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation. | Q6L1R1 |
P49339 | WNT11_CHICK | Protein Wnt-11 | Gallus | MKPSPQFFLAAFLSLILQTGICYGIKWIALSKTPSSLALNQTQHCKQLEGLVVSQVQLCRSNLELMQTIIQAAREVIKTCRKTFSDMRWNCSSIELAPNYLLDLERGTRESAFVYALSAAAISHTIARACTTGDLPGCSCGPIPGETPGPGYRWGGCADNLNYGLIMGSKFSDAPMKMKKSGSQANKLMHLHNSEVGRQVLKASLEMKCKCHGVSGSCSIKTCWKGLQELRDIALDLKNKYLSATKVVHRPMGTRKYLVPKDIDIRPVKETELIYLQSSPDFCMKNEKVGSHGTQDRQCNKTSNGSDSCDLMCCGRGYNPYMDKVVERCHCKYHWCCYVTCKKCERTVERYVCK | Ligand for members of the frizzled family of seven transmembrane receptors. May play a role in the formation of dermal structure, both limb and feather buds. Is likely to signal over only few cell diameters. | P49339 |
O31562 | YFIT_BACSU | Putative metal-dependent hydrolase YfiT | Bacillus | MTSVNLSYPIGEYKPRESISKEQKDKWIQVLEEVPAKLKQAVEVMTDSQLDTPYRDGGWTVRQVVHHLADSHMNSYIRFKLSLTEETPAIRPYDEKAWSELKDSKTADPSGSLALLQELHGRWTALLRTLTDQQFKRGFYHPDTKEIITLENALGLYVWHSHHHIAHITELSRRMGWS | Possible metal-dependent hydrolase. | O31562 |
P47683 | TRMD_MYCGE | tRNA [GM37] methyltransferase | Mycoplasma | MKITVLTLFENTIWPYLNSSIMLQAQKANLVQFEVVNWRNFCNDKHKTVDDMAYGGGSGMVLKAEPIINCLNFYKAPNSHVVLLSPEGEQFSQNCAKKLTKYEHLILLSGHYEGFDQRIYKYIDQIVSLGDFVLSGGELVALSVIDATVRLIKGVINDQSLICESFNDNLLDFPVYTRPYDLKGDKVPEVLLSGDHQKIESFRKEQQILKTAKYRPDLYKKYLENKNEKNK | Specifically methylates guanosine-37 in various tRNAs. | P47683 |
A7X1M7 | XERC_STAA1 | Tyrosine recombinase XerC | Staphylococcus | MNHIQEAFLNTLKVERNFSEHTLKSYQDDLIQFNQFLEQEHLQLKTFEYRDARNYLSYLYSNHLKRTSVSRKISTLRTFYEYWMTLDENIINPFVQLVHPKKEKYLPQFFYEEEMEALFKTVEEDTSKNLRDRVILELLYATGIRVSELVNIKKQDIDFYANGVTVLGKGSKERFVPFGAYCRQSIENYLEHFKPIQSCNHDFLILNMKGEAITERGVRYVLNDIVKRTAGVSEIHPHKLRHTFATHLLNQGADLRTVQSLLGHVNLSTTGKYTHVSNQQLRKVYLNAHPRAKKENET | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | A7X1M7 |
X1WER2 | UBA5_DANRE | UFM1-activating enzyme | Danio | MATVEELKLRIRELENELIKSKQKQSDAEHNIRPKIEQMSAEVVDSNPYSRLMALKRMGIVQDYEKIRSFAVAVVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVEAAQHTLRNINPDVAFETHNYNITTMDNFTHFMDRVSHGGLEEGKPVDLILSCVDNFEARMAINTACNELGQIWMESGVSENAVSGHIQLIIPGETACFACAPPLVVAANIDEKTLKRDGVCAASLPTTMGVVAGLLVQNVLKYLLGFGTVSYYLGYNAMQDFFPSMAMKANPQCDDRHCRRQQDEYKKKEAERPKQEVVQEEEEVVHEDNEWGIELVSEVTEAELQDASGPIPDLPEGITVAYTIPEKDGGSGETVEETEQSLEELMAQMKKI | 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. | X1WER2 |
Q6QDC9 | TBB_ZYMTR | Beta-tubulin | Zymoseptoria | MREIVHLQTGQCGNQIGAAFWQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVLDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVMPSPKVSDTVVEPYNATLSVHQLVENSDATFCIDNEALYDICMRTLKLNNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAHSFRAVTVPELTQQIFDPKNMMAASDFRNGRYLTCSAIYRGKVSMKEVEDQIRNVQNKNTAYFVEWIPNNVQTALCSIPPRGLKMSSTFVGNSTSIQELFKRVGDQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEASVSDAEEEYDEEAPLEGEE | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Q6QDC9 |
B5KL33 | VKT2_TROCA | Kunitz-type serine protease inhibitor carinatin-2 | Tropidechis | MSSGGLLLLLGLLTLWEILTPVSSKDHPEFCELPADSGPCRGILHAFYYHPVHRTCLEFIYGGCYGNANNFKTIDECKRTCAA | Serine protease inhibitor. | B5KL33 |
B4R1Q1 | TOTZ_DROSI | Protein Turandot Z | Sophophora | MYFAIRLSFVLAVLFCLTGNGSARMLDADRNRLQQLQIRSQQSADANTQVDIAYEVIGIYDKYKGQGGSNVLREAQLNSQVNDFKRKTMVIDGVPAQGGVWGILGAIKKAADAVPDNVKKDAENLVKSSTKVLVRGIYDYLMGKMKQH | A humoral factor that may play a role in stress tolerance. | B4R1Q1 |
P39849 | XYLB_PSEPU | Benzyl alcohol dehydrogenase | Pseudomonas | MEIKAAIVRQKNGPFLLEHVALNEPAEDQVLVRLVATGLCHTDLVCRDQHYPVPLPMVFGHEGAGVVERVGSAVKKVQPGDHVVLTFYTCGSCDACLSGDPTSCANSFGPNFMGRSVTGECTIHDHQGAEVGASFFGQSSFATYALSYERNTVKVTKDVPLELLGPLGCGIQTGAGSVLNALNPPAGSAIAIFGAGAVGLSAVMAAVVAGCTTIIAVDVKENRLELASELGATHIINPAANDPIEAIKEIFADGVPYVLETSGLPAVLTQAILSSAIGGEIGIVGAPPMGATVPVDINFLLFNRKLRGIVEGQSISDIFIPRLVELYRQGKFPFDKLIKFYPFDEINRAAEDSEKGVTLKPVLRIG | Oxidizes primary alcohols with an aromatic or cyclohex-1-ene ring. It is highly specific for benzyl alcohol. | P39849 |
C1A4H0 | UVRB_GEMAT | Excinuclease ABC subunit B | Gemmatimonas | MTAPFRLHAPFAPAGDQPRAITELSSGLHRGDRIQTLLGVTGSGKTMTMANVIADWGRPTLVLSHNKTLAAQLYGELKSFFPNNAVEYFISYYDYYQPEAYVPSSDTYIEKDASINEDIDRLRLRATSSLMERDDVVIVSTVSAIYGLGDPVQYRERMVALSRGQQIARDDILRALVGIQYLRNDVAFERGTFRVRGDTVEILPAYEEQAVRIELWGDEIERISKIDPVTGETIAALERMAIYPAKHFITNRPTIERASMAIRDELATRLAELRMAGKLLEAQRLEQRTQFDLEMLMEIGTCAGIENYSRHISGREAGERPACLLDYFPDDYLVVVDESHVTLPQIRAMYNGDRARKLTLVDYGFRLPSALDNRPLVFDEFMSLVPRLVNVSATPGELELQLSEGVVVEQVIRPTGLLDPVLEVRPVKGQVDDLLHEIRARERRGERVLVTTLTKRMSEDLTDYLQQMGVRVRYMHSDIDAIERMEIVRGLRLGEFDVLVGINLLREGLDMPEVSLVAILDADQEGFLRSDRSLIQTIGRAARNLHGMAILYGDRITGSMQRAIDETTRRRTIQREHNEAHGIVPRGVTKSVDEVRFITRVADARVEREGEAPAPRRLASESAPRSREELETLVGELEIAMREAAVALDFEAAARLRDQLFEVRTALGQAPSEARGNAQAPKRPPGSAPQRRAGGGRRGR | 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. | C1A4H0 |
P91800 | TCTP_SCHJA | Translationally-controlled tumor protein homolog | Schistosoma | MRVFKDAISGDEMFSDSHSPQLINDVVYEVDANFITVSNGLDSKLIAANPSGEEGQEEVSDSTERVIDLVHASRLVSTSFDKKSYRAYLKGYLKAIKERLQKENPERVSIFESRINEYMVNVFKNFDDYEHYIGESMNPDGMVALMNFRENGVTPYFVFLKDGLIEEKY | Involved in calcium binding and microtubule stabilization. | P91800 |
P32610 | VATD_YEAST | Vacuolar proton pump subunit D | Saccharomyces | MSGNREQVFPTRMTLGLMKTKLKGANQGYSLLKRKSEALTKRFRDITKRIDDAKQKMGRVMQTAAFSLAEVSYATGENIGYQVQESVSTARFKVRARQENVSGVYLSQFESYIDPEINDFRLTGLGRGGQQVQRAKEIYSRAVETLVELASLQTAFIILDEVIKVTNRRVNAIEHVIIPRTENTIAYINSELDELDREEFYRLKKVQEKKQNETAKLDAEMKLKRDRAEQDASEVAADEEPQGETLVADQEDDVIF | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments . | P32610 |
Q9CR76 | TM186_MOUSE | Transmembrane protein 186 | Mus | MAFLLRVVPRLQGPTAWRRPLQGLWCCSGQGDSKRWVGSRSPHSREKSPGTETETFHTIYRFRAIRAIGFLSRLKLAQTAVTVVALPPGFYCYSQGLMTLSSLCLLGGVASFALAMLCWMSHFFRRLVGILYVNESGTLLRVAHLTFWGWRQDTYCAVSDMIPLSESQERVQDVFVRIQQYSGKQTFYLTLRYGRILDRERFAQVFGTLATLKNSK | As part of the MCIA complex, required for efficient assembly of the mitochondrial complex I. | Q9CR76 |
Q9FTU1 | YSL1_ORYSJ | Protein YELLOW STRIPE LIKE 1 | Oryza sativa | MADPAGAGGEQEAPSVEAAFAGQPPPPWWQQVTVRAVAVSVVLGTLFSFMAMRTGLTAGFVPSFNMSASLLSFFIIKSWTRLMARCGVASQPFTRQENVVVQTCVISCATLSIYGGFTSYLLAMNETVAKAAGGGTDGRNVYTLHTGKIVAFLFLVTFSSLFCTLPLRNTMIVDYKLIYPSGSAVAGIVNSFHTPKGATKAKLQVNAMFKSVAGSFAWAFFQWFYTGGDGCGFHAFPLFGLEAYKEKFYFDFSASLVGVGMICPHLINFSMLLGSISSSGFIWPALQAKQGEWYTDPSPTSFKGINGYKVPMGVSMVLGDCLFQLGAITVKAVQHYRKGRQEQKLAVDGAADDGGGGCVPDDDDENKWHATYDERRRNQVFLSDGIPDQFAVAGYVALAALSTALVPRIFPQIRYHHVAVCYAVAPLLAFCNSYTSGLMDWSLATVYGKLAIFVVGASVGAASGGVIAGLAACGVMMVVIGDAAELMHDFKTAYLTLTSPVSMFASQAIGTALGCVVNPAVFLAFRWLAGAEHPPGDPRSAYAAPMAVAYRGIAVLGVEGVGTLPRHAIALCAACFAAAVFLDTAGAAARAARWRVGGWVPNPMAMAIPFFVGPTFAIDMCVGSLLLMAWRRADRQGAATLAVVVASGLICGEGLWTLPSAVLAMLKVQPPICMKFLSRSQIQEVRQHFVLGAADIQPAVTLTHHHHQ | May be involved in the transport of nicotianamine-chelated metals. | Q9FTU1 |
Q554C5 | WRKY1_DICDI | WRKY domain-containing protein 1 | Dictyostelium | MGAQYSTELNKYNNNNNNNNNNNNNNNNNNNNHTISGNENLNNNNNNNNNNNNYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNNGNSNSNSNNNNNNNGINKYSNYFESLINNTNKDTNIPNNSNSNNNNSDRDFIQNMIKSANQIKPGEKELVLFHKLHQSLKENQSFSIEELRNSSILSISPDKSFLTNINEINVNNNNNNNNNNNENNKVGVNGSSTTTTTTTTTTTNNNSNNNNNNNNNNNNNNNNNNNNNEDDEDDYGDDDTIENNEPTFVDKPNKSAKLQKPKLKSNLNDTNGGNSPQQNGKISKYMAKKLLALQQKQLEQEQEQKQQQKQQQQQQQQQQQQQQQQQQQQQKDAIENINNNNNNKLQPIVKNSVNKTTKQKKNKTTTHNVKQQITFLTKSDNEDEYDASDEYIDDDDDDDEKYDDDDDEYFEGNNNNNYKKNNISNKSKNKNNNDESDSFSESEIFKQKKLNHDKNQSNPKQQLTSHSEFDNSLLNKNQSRTNSKIQKLQIKEENYHQIQQEHGEKQQQQQQQQQQPQQQQQQQQQQQQQQQQEMQVDKEQTEKIINTNKKEEQKPNDYFPPIPTNPFKRDNETAFGKNNENNNNNNNNNNNNNNNNNNNNNNNNNNYRNNKPNGEGFLSNLKIIPPMISSSPYYSKKSSNVVPTSPKSNLSDQQPPFSPVQISPQKQSPATTTTTTTTTTPTPLKKQKKNKTNNNINNNNINNNNNNNNNNNNNNNNNNNNNNNNNNYSINNINNEEDEENNSTQNNNNNNNNNNNSPQNSNTNSNNSNNSNNSNNISNIVSDGYQWRKYGQKNVKGSLHPRHYYKCTFQGCNVRKQVERIGDTNQNSTVYKGEHCHGFPQTTRVVSDQQAFRNSVMFEGLDGNNNNNNNNNNNNNNYSSNSNSNGNGNGNGNGNGNGNGNGNGNSNGNQDQNGNSFNDQNGDSPTQHGQISPMNSPKNTIPTTTTTTTSISTYVNTNSTNKKNNSKQEKKISVKNETTDDDEFQEDIDQLSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNDDNNNNNNNNNNNNNNNRFNGTSESKGSKKLVIETGSSIDHLDDGFFWRKYGQKSVKGSPFPKSYFKCAELTCPVKKQVIQQDSKYINTYRGKHNHDPPESEAIEKRKKHFNGLYNNNNNNNNNNNNNNNNNNNNNNINNINNNNINNLNSLNNINNINNNNNSNQINNFSGSIQNNLKNILKEQLKEAGKLHNEIENNLIDD | Probable transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. | Q554C5 |
Q6AUG0 | U2AFB_ORYSJ | Zinc finger CCCH domain-containing protein 38 | Oryza sativa | MAEHLASIFGTEKDRVNCPFYFKIGACRHGDRCSRLHNRPTVSPTIVLANMYQRPDMITPGVDAQGQPIDPEKMQEHFEDFYEDIYEELSKFGEVETLNVCDNLADHMIGNVYVQFREEEQAVAAHNALQGRFYSGRPIIVEYSPVTDFREATCRQFEENSCNRGGYCNFMHVKQIGRELRRKLYGGRSRRSHGRSRSPSPRHRRGNRDRDDFRRERDGYRGGGDGYRGGGGGGGGDGYRGGDSYRGGGGGGRRGGGSRYDRYDDGGRRRHGSPPRRARSPVRESSEERRAKIEQWNREREEKP | Necessary for the splicing of pre-mRNA. | Q6AUG0 |
Q9VWB9 | THADA_DROME | Thyroid adenoma-associated protein homolog | Sophophora | MNDLNLRVAALKVCAHPKRFAELRDALVPLPNTWIAAPHDFVLQFAAAKSSAEQVQVVKDVFYGEQAQDHEDVAHFLADLLLASPLKHAVRNQLTKLFSDNALAKQNASPHRRHSKEHLLEALQQSLGEMANSLAVITPPVSHERTNDVFVSANACLQNFPFGREALGKQVHRFAPLLTTALERYWADICDPTLELSPTRRNELYLYVQNALRFLVSLLAEWSDKLRLFEDQRFPGTSNAVAQKVARYYDTPWDVRSIAALLIGHLARFSGTFKAYVEDCSRPKAEQDVPIQMAALLVLRPVDYTENATLALAILKRIVAVSELKSTVTNLLVFLSKHLFIYSKSLGEMHAHLPDDQKLLYQRILAQLQVFALQNISSDTDSVRHMSSALLHQVLQHAQAAGQEELFQVVYRQFEDRAAYLNASCMALEQLVAVAGVSKSIENCPSLFGVIFPRHLGCEDCVDALFKAMMVSAHKTEPFAEWQSRWFGLLLAAIRVPEKRRQVIEELIAQAVQLEPTRLAQVLLPDDRLPLSCKLAAILGVRQLSARRQNLLRGMKEEVEQALIGLDDHTRLLALRFLVETPRPSELLNADQMGAIELYVRHNANNPSAHLRQLGYGLLQKALKRVHFGLVEYRKSRTPASQEVLQFLIRLIRTLAQNLFPTANYGRRWLSLRLLRDCLELSEMVGITFSELGIELPTEALMACLGDSYEHNKVLAAQLLERFQSHSLFKPDEMIELLLSLRPSDSATGAFQLQVYCKASRVQSEMPTPTHGGTIHEPLTFRALQWCLQHLREGLRLAQLDLGEAAKLNPLYGLLFASRHLLQQLKLKELAKEPQWRQYIDELVTMCLAVSSVVLPVVSSASPEGHLPETCDQETDQPLTNVLDRQLSREELLQVRTTPQMILLCAWRSSKEVCLILGELVQRAPLEEEEDEEQQQQQGDFLLSRAQLEAIGEHFLQLLAETKHRGAFEQAYVGFTMLCRRFWHSESVRLNQLPGQWVDEAMAMVSGQEEWAGKGARLCATRRSAGMPFMLQALVGTELKLGTHATLYRCMNRLLEVCERRTGGAAGITARSHALNIMRALFRSSELAELVTEFMARGIQCALDGLLLAEEWAERNSATLLLAALIVRVFGVERARLETGELHVRNRMTGRIFFTRYPQLFDYFHAALQRESEQMDAGGGGSENASGKRRQAVQLEAMLLMLSRLYPSSLEGAESTLNLSEFVPFLIRICHSHDLMTREMAALVVANFVTQEQALAEIRRIVVELKALQLRLKNTEAANTKLNTNVLHGQLLLLLHLHRLVRWTRPSLTRMQLHTLAELAAPLLQHDACAFSALVAVMVAAMEDAVEPGLLDFQLLEQIGVVYLLNHKEVQSRCQQLGISNRFYQIFGLHLHRLRGISQGIVLHIVEDLAETIWALDELKVELWLYILLQRSLSEQNSLVSEQDIEHFEFSRDIRRYFETLSREQREEVGQELYESPAVRSSVLHMMHMIKSSKNSCWSLQLAGRLAALQTLLRDPGLELNQLVQRCSEEHSTHQEAGLLLGLRRLIGESKMLERKHWLPMLNYAQRLVHPGQPVYLRHQAAELCDSLARNHLRDQLVAGTTDVDIGLVGRFSGLVLLLLHDDAEWVRHRAVQLVCGAGLRTRSGAGQEQEQSAMAPLILPSALIPPFLDTMIGKLTFDDFNMVQRLVDIIAEPFTTADAMELFDKQENNHYCERNHVLTELWDARGRADPRARTPTIPTGYQIFK | Plays a key role in energy homeostasis by regulating the balance between energy storage and heat production. Functions by negatively regulating Ca(2+) signaling pathways that are involved in heat production and maintaining correct lipid storage in the fat body. Regulates Ca(2+) signaling pathways by reducing the activity of the calcium-transporting ATPase SERCA possibly by promoting uncoupling of SERCA ATP hydrolysis from calcium pumping. May also function in the nervous system to control feeding behavior. | Q9VWB9 |
P9WFZ0 | TRMI_MYCTO | tRNA(m1A58)-methyltransferase | Mycobacterium tuberculosis complex | MSATGPFSIGERVQLTDAKGRRYTMSLTPGAEFHTHRGSIAHDAVIGLEQGSVVKSSNGALFLVLRPLLVDYVMSMPRGPQVIYPKDAAQIVHEGDIFPGARVLEAGAGSGALTLSLLRAVGPAGQVISYEQRADHAEHARRNVSGCYGQPPDNWRLVVSDLADSELPDGSVDRAVLDMLAPWEVLDAVSRLLVAGGVLMVYVATVTQLSRIVEALRAKQCWTEPRAWETLQRGWNVVGLAVRPQHSMRGHTAFLVATRRLAPGAVAPAPLGRKREGRDG | Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA. | P9WFZ0 |
Q70Y02 | YCF3_AMBTC | Photosystem I assembly protein Ycf3 | Amborella | MPRSRINGNFIDKTSSIVANILLRIIPTTSGEKEAFTYYRDGMSAQSEGNYAEALQNYYEATRPEIDPYDRSYILYNIGLIHTSNGEHTKALEYYFRALERNPFLPQASNNMAVICHYRGEQAIRQGDSEIAETWSDQAAEYWKQAIALTPGNYIEAQNWLKITRRFE | Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits. | Q70Y02 |
I1S2K3 | XYNA_GIBZE | 1,4-beta-D-xylan xylanohydrolase A | Fusarium | MVSFKSLLVAVSALTGALARPFDFLDERDDGNATSVLEARQVTGNSEGYHNGYFYSWWSDGGGYAQYRMGEGSHYQVDWRNTGNFVGGKGWNPGTGRTINYGGSFNPQGNGYLCVYGWTRGPLVEYYVIESYGSYNPGSQAQHRGTVYTDGDTYDLYMSTRYQQPSIDGVQTFNQYWSIRRNKRTSGSVNMQNHFNAWRSAGMNLGNHYYQILATEGYQSSGSSSIYVQTS | Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Plays an important role in causing fusarium head blight (FHB) on cereal crops. | I1S2K3 |
Q46GQ7 | TAL_PROMT | Transaldolase | Prochlorococcus | MESLLSQLSSMTVVVADTGDLEAIKKYHPRDATTNPSLILAAAQMPAYQSLIDQALTTSREMLGTSAAKADVVKEALDELCVVFGKEILKLIPGRVSTEVDARLSFDTDATIEKARKIIAKYNADGISNDRVLIKIASTWEGIKAAEVLEKENIHCNLTLLFNFYQAVACAEAGVTLISPFVGRILDWYKSATGRDSYPATEDPGVVSVTKIFNFFKSNGYKTEVMGASFRNIEEITELAGCDLLTISPKLLQQLNETHMDLPIKLNAQKPLVIEEKIHLDQTSFELMMAGDKMATEKLDDGISGFSKAIDKLENQLNERLELIEGEVALTH | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q46GQ7 |
O59947 | TRI5_STACH | Sesquiterpene cyclase | Stachybotrys | MEAFPTEYFLGTAVRLLENVKYRDSNYTREERVENLQYAYNKAAAHFAQERQQQILKVSPKRLEASLRTIVGMVVYSWAKVSKELMADLSIHYTYTLILDDSEDDPHPQMLTYFDDLQSGNPQKHPWWMLVNEHFPNVLRHFGPFCSLNLIRSTLDFFEGCWIEQYNFHGFPGSFDYPGFLRRMNGLGHCVGGSLWPKENFNEQEHFLEITSAIAQMENWMVWVNDLMSFYKEFDDPRDQTSLVKNYVVSEGITLNQALEKLTQDTLQSSEQMMVVFSQKDPKIMDTIECFMHGYITWHLCDNRYRLKEIYDRTKDIQTEDAMKFRKFYEQAFKVGAIEATEWAYPTVVERLEQRKAEEQAERDEQAALANPEKAQVAQVVLA | TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway. | O59947 |
A2SDR5 | URED_METPP | Urease accessory protein UreD | Methylibium | MAWLGSLDLHYRPDPDAPAAALPRTIGRGVHSGPLRVLQSLYPEGPGICHHVLVHPPGGIVGGDELALTAQVDTGAHALLTTPGATRFYRSGGDAALQTLTARVADGARLEWLPLETLVHDGARARNALRFELAPGAEMLGWDLLALGLPAAGERYASGCFEQSIEVRSAAHPLPWLERGVLDFDDPRHAPVTQRLLASPLGWAGHTVLATLWFASGTALASARRDALIDAARAPDSAAQPGAEPLGVTAPHDHVVVLRMLGARVEPLMQRLRAVRGRWRRLAWDCAGAEPRVWRT | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A2SDR5 |
Q9D3D0 | TTPAL_MOUSE | Alpha-tocopherol transfer protein-like | Mus | MSEESDSLRTSPSVASLSENELPLPPPDPPGYVCSLTEDLVTKAREELQEKPEWRLRDVQALRDMVRKEYPYLSTSLDDAFLLRFLRARKFDYDRALQLLVNYHGCRRSWPEVFSNLRPSALKDVLNSGFLTVLPHTDPRGCHVLCIRPDRWIPSNYPITENIRAVYLTLEKLIQSEETQVNGIVILADYKGVSLSKASHFGPFIAKKVIGILQDGFPIRIKAVHIVNEPRIFKGIFAIIKPFLKEKIANRFFLHGSDLNSLHTNLPRNILPKEYGGTAGELDTASWNAVLLASEEDFVKEFCQPMPACDNLLGQPLLPEGLISDAQCDDSMRAMKSQLYSCY | May act as a protein that binds a hydrophobic ligand. | Q9D3D0 |
A9WDP2 | YIDD_CHLAA | Putative membrane protein insertion efficiency factor | Chloroflexus | MLRWLLLKLIRFYQVAISPWTPPSCIYTPTCSHYGYEAIKKYGALRGGWMTVKRIARCHPFARGGYDPVP | Could be involved in insertion of integral membrane proteins into the membrane. | A9WDP2 |
Q1H4G9 | TSAC_METFK | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Methylobacillus | MRARALQHFLRSGGVIAYPTESCFGLGCDPTNHRALKRLLRIKGRPQRKGLIVIAQHFSQLQKLIAPVTPEQKQRMFTRWPGPHTWLVPASRRCPALLRGRHTSLAVRVTANPLAANLCRHAGMALVSTSANHNGRVPAKTARECHRLFGGRVKVLPGRTGGASKPSTIQDLITGAIVRP | 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. | Q1H4G9 |
Q9KA80 | TRUB_HALH5 | tRNA-uridine isomerase | Halalkalibacterium (ex Joshi et al. 2022) | MDMTGILPLAKPRGMTSHDCVAKLRRLLKTKKVGHTGTLDPDVYGVLPVCIGHATKVAQYMSDYPKAYEGEVTVGFSTTTEDRSGDTVETKTIQQPFVEAVVDQVLATFVGEIKQIPPMYSAVKVRGKRLYEYARAGITVERPERTVTIFSLERMSDIVYEEGVCRFRFNVSCSKGTYVRTLAVDIGKALGYPAHMSDLVRTKSGPFSLEECFTFTELEERLEQGEGSSLLLPIETAILDIPRVQVNKEIEEKIRHGAVLPQKWFNHPRFTVYNEEGALLAIYKAHPSKDGFVKPEKMLANDQQ | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q9KA80 |
Q8SSC5 | UGPA1_ENCCU | UDP-glucose pyrophosphorylase | Encephalitozoon | MQESRSKESTLSGDEDKDVHRFLDEFDDKCTCKLLKEMKETLEGLKKSHPNPTNLDEFYRLFERYLRTRHEKIVWEKIRSPKDRIVQYNEIPEPTEKSKELLRKLAILKLNGGLGTTMGCVGPKSAITIKDGKNFIDLVVKQIRYLNSKYKIDVPLILMNSFNTEGMTDKIIFRYDGIKKFSQSKFPRISSETLLPVSPSHGDKGMYPPGHGDLFYSMKNSGMLEELLEGGYEYLFVSNIDNLASTVDLKLLEYFATNELGFLMEVTDKTRADVKGGTLIEYKGALRLLEIAQVPSNKKSEFTSFKKFTIFNTNNLWINLKEMKKKLEEGFFDLDIIENKKALDDETVIQLETAIGSAIKYFPNSCGVVVPRSRFLPVKTCSDLFLVESNLFVEKNGTLQLHPSRVPETCPTVKLIGENFSKIEKYEKCFKGIPDILELEVLTVSGNVLFGKNVVLKGTVIILADEKSKICVPDGSVLEDNIIYGNLPIIDH | Plays a central role as a glucosyl donor in cellular metabolic pathways. | Q8SSC5 |
Q664P8 | TAUB_YERPS | Taurine import ATP-binding protein TauB | Yersinia | MLNVSGLWAEYQGKPALQDVSLQIASGQLVVVLGPSGCGKTTLLNLIAGFMTPSAGVITLDNIPVSGPSAERGVVFQNEGLLPWRDVVSNVEFGLQLAGMSKEQRRVTALKMLNRVGLAGFEHHFIWQLSGGMRQRVGIARALAVDPRLLLLDEPFGALDAFTREQMQELLLTIWRDTGKQILLITHDIEEAVFLASELLLLSPGPGQVVERLSLNFGQRYAEGEPCRAIKSDPEFIARREYVLGKVFQQREVLI | Part of the ABC transporter complex TauABC involved in taurine import. Responsible for energy coupling to the transport system. | Q664P8 |
C4XNJ6 | YIDC_SOLM1 | Membrane protein YidC | Solidesulfovibrio | MENKRVILAVALSLAVLVGWNFLFPPAKQAPKPDAAVSQQDAPAQSSPAAPAAKAETLAAFAPTPGKRITIDTPLYTAVLNSTGGVLEQFALKNYRETIKPDSPLVNLIDDKAKAKAPLGIILNGSPTWQNVDWSAEGGDLKLEAGAAGTVVLAGRMGDVVVKRELTFSGDSYIIDEKFSLSNNGGAPLRNRLSLTVAVDRLSAADDSYNPTQAAFYGASGLDLESGDKKLAEGVAPEKPMEWGAVMSNYFLVGIVPEAADLRGKAKLEDGVFRVALDKDGLEVPAGGRSDLSIAYFLGPKVPKYLEMAPHKLVASIDYGWFDFVAKPLIKLLHFFYDYVGNYGVAIILLTILIKLIFWPLSQKSYKSMDQMKKLQPLLTQLREKYKDDRQKMNEEMMQLYKTYKVNPAGGCLPMIVQIPVFFGLYQALLHSIELRHASFITHLPFTNMIWLADLSAKDPFYITPLIMGATMFLQQKMTPAPGDPTQAKVMLFMPVIFTFMFLNFPSGLVVYWLVNNVISIAQQGWMLNKKS | 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. | C4XNJ6 |
A7FT29 | XPT2_CLOB1 | Xanthine phosphoribosyltransferase 2 | Clostridium | MKLLEDKILKEGILLEGNILKVDSFLNHQMDVKLFNEIGKEFKRRFEGCSINKILTIEASGIGIATIVSQYFDFCPVVFAKKVDAANMDKDTYESKVHSFTKNKTYNVRVSKKYINKGDKILLIDDFLANGCAALGLIDIIKQGGAELIGVGIAIEKGFQKGRKELEKVGAKVESLAILDKIENDKVYFK | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | A7FT29 |
A1AZC8 | YQGF_PARDP | Putative pre-16S rRNA nuclease | Paracoccus | MICENVETFAEALPRTGAVAGLDLGTKTIGVAVSDGLRGVASPLTVIRRTKFTADAQALLKIVQDRALVGLVLGLPRNMDGSEGPRAQSTRAFARNLERLTPLPITFWDERLSTVAAERALLEGDTSRKRRAEVIDQVAAGYILQGALDRLRFLGRTE | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | A1AZC8 |
A3QFX7 | TIG_SHELP | PPIase | Shewanella | MQVSVETTQGLERRLTISVPAEQIEKAVSDSLKNEAKRARIPGFRPGKVPVSVINKRYGKAIRQEITGEVMQRNFIEAIIAEKLNPAGAPTFVPGETDAENFQFVATFEIYPEVELKGLDAIEVEQPTAEVTDADVDAMIETLRKQHATFEAVEREAAEGDKAKIDFVGSIDGEEFEGGKAEDFELQLGSGRMIPGFESGVEGHKAGEAFDIDVTFPEDYHAENLKGKVAKFAITLKEVQAANLPEVNDEFAKLFGVADGGLEALKVEIRKNMSRELEQALKANVKDQVLNGLLEQNEIELPKALIDGEVNVLRQQAMQRFGNQAANMPELPADLFTEQAERRVKVGLLLGEVIKTNELKADDERVQALIASMASAYEDPQEVIEYYNNNQEMMQNMRNVALEEQAVEALLKTAKVTEKAVQFEEFMNKATGRA | 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. | A3QFX7 |
Q62590 | TSHB_PHOSU | Thyrotropin beta chain | Phodopus | YCLTINTTICAGYCMTRDINGKLFLPKSALSQDVCTYRDFTYRTVEIPGCPHHVAPYFSYPVAMSCKCGKCNTDYSDCIHEAVKTNYCTKPQTFYLGGFSV | Indispensable for the control of thyroid structure and metabolism. | Q62590 |
A6VTV5 | URED_MARMS | Urease accessory protein UreD | Marinomonas | MNNKHNLALAEQYDQKPLIKTSMLPEVGASQWHAFLTLGFSKTARGTVLKTSDHKGPLYVQKPFYPEGRDTAHIYLLHPPGGLVSGDRLTITANLAENTHVLITTPGAGRVYRARKDKTLQHQITQLNVAENSLMEWLPQETILYPNAHTRLENRIHLANNAKFIGWEITCFGLPANQEDFAQGHAEQGFEIRQNGRLKVRERLVIDDSSRTIFAAKAGLAGKPINGLMIAGPFDLTNASHSASHDELIDSLRKHCAQHNSVSGVSLVGEYIFVRSLHHDSEQVKQLFIQCWREIRPALINKESNEPRIWAT | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A6VTV5 |
B7UHL4 | XNI_ECO27 | Flap endonuclease Xni | Escherichia | MAVHLLIVDALNLIRRIHAVQGSPCVETCQHALDQLIMHSQPTHAVAVFDDENRSSGWRHQRLPDYKAGRPPMPEELHDEMPALRAAFEQRGVPCWSASGNEADDLAATLAVKVTQAGHQATIVSTDKGYCQLLSPTLRIRDYFQKRWLDAPFIDKEFGVQPQQLPDYWGLAGISSSKVPGVAGIGPKSATQLLVEFKSLEGIYENLNAVAEKWRKKLETHKEMAFLCRDIARLQTDLHIDGNLQQLRLVR | Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. | B7UHL4 |
Q98CN6 | TRPA_RHILO | Tryptophan synthase alpha chain | Mesorhizobium | MTTRIDRRMAKLKTEGRPALVTYFMGGDPDYDTSLSIMKALPGAGSDIIELGMPFSDPMADGPAIQAAGLRALKGGQTLVKTLKMASEFRAGDNETPIVLMGYYNPIYIYGVDRFLKDALASGIDGLIVVDLPPEMDEELCIPALKAGINFIRLATPTTDDKRLPKVLQNTSGFVYYVSMTGITGSALADTGKVAAAVNRIKGHTDLPVCVGFGVKTAEQARVIGANADGVVVGTAIVNAVANVLGPKGEKTADPAEAVATLVSGLAQGVRSARLAAAE | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q98CN6 |
Q9XTQ6 | TBH1_CAEEL | Tyramine beta-hydroxylase | Caenorhabditis | MEPTASQGIQYLRGGVEWILKLLNLHILNVKHENKPLLFRLIDLKVYIPSSVSTVRWSSGASSYVILGEYRKMRSAVALLFLLVAYCGGVVHAGEIVAELYHTNVTVKWHTDYERQLVDFSIWFGASTPDVLFLGFSDFGDTNNSDVLMYYNSKKEIKDAYTNRDFKITSDLQQDFQLLRKRKDHIVVRRKLTTCDSRDYAFLPGTTQFYIAASWGSTNLVDIRDKRWVVDKKFGKVIEGPTDQPNIEEEPAALEKDVKVVIVNSNSPDPIPNVETTYKCIIRKMPFDTVNNMYHVVRMEPYVTPGNEHLVHHMEIFMCRDEVEEWSGSCNDPKKPPKSKSCSHVIAAWAMGEGPIHYPKEAGLPIGGKGKNAYVMVEIHYNNPELHKGVIDSSGFQFFVTGQLRKYDAGIMELGLIYSDANSVPPNQKAWAMNGYCPSQCTKNLPEEGINIFASQLHAHLTGRKLFTSQYRSGVRIGDVNRDEHYSPHWQHLQQLRPVVKVMPGDTLVTTCVYDTRKRSKVTFGGYRIVDEMCVNYIYYYPASDVEVCKSAISNSTLRAYFSERHGMDGKRMQISDMYSNVKDWGNGVDEEFYNVLNVGNMNMNCLKSNGEPFEFESKDSRQSWENMARPTFVSGSFITTRDRFQCPAINDMINFE | Required for the conversion of tyramine to octopamine, a precursor of octapamine but probably itself a neurotransmitter . Involved in the regulation of egg laying, which is inhibited by tyramine . Due to its involvement in octopamine biosynthesis, also required for crtc-1-dependent regulation of AMPK-mediated longevity . | Q9XTQ6 |
A8FHJ2 | TPIS_BACP2 | Triose-phosphate isomerase | Bacillus | MRKPIIAGNWKMNKTLGEAVSFVEEVKSSIPYPDKVEAIVCAPALFLEKLNSLSNGTDLKIGAQNMHFEENGAFTGEISPAALKDLGIGYSVIGHSERREFFAETDETVNKKAHAAFKHGIVPIICVGETLEEREAGKTNELVADQVKKALAGFTTQQVAESVIAYEPIWAIGTGKSSTAKDANDVCAHIRQTVASEYGQEAADSLRIQYGGSVKPANIKEYMAESDIDGALVGGASLEPQSFVQLLEEGQYE | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A8FHJ2 |
A0A063C1W0 | USTZ_USTVR | Ustilaginoidins biosynthesis cluster protein Z | Ustilaginoidea | MASHHQLLCLNILGFRKPGISTEDYRNYMVNVHAPLVAGLMEKYGFLHFTMSHASEQSPQLMDQLYDAQFANTASYDCCVQIVFPSIECFVNMKADPYFKQTVGPDHEKFADTKRSQMMIGWFSPLLINGQQTDSLSAAE | Dehydratase; part of the gene cluster that mediates the biosynthesis of ustilaginoidins, dimeric gamma-naphthopyrones isolated from different fungal species . The first step in the biosynthesis of ustilaginoidins is the production of gamma-naphthopyrone precursor YWA1 by the non-reducing polyketide synthase ustP, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units . YWA1 is then probably substrate of the ustZ to yield norrubrofusarin via a dehydration reaction (Probable). A key enzyme in the biosynthetic pathway is the laccase ustL, which catalyzes the oxidative dimerization of norrubrofusarin to ustilaginoidin A . It can produce the M- and P-atropisomers in varying amounts, depending on the reaction conditions . For the biosynthesis of 3-methylustilaginoid in derivatives such as chaetochromin A, a methylated derivative of YWA1 is required (Probable). The C-methylation is considered to be catalyzed by ustM, the phosphopantetheine attachment site of which indicates that it acts on the growing polyketide chain before release of the product (Probable). For the biosynthesis of chaetochromin A, it is assumed that saturation of the D2 double bond takes place before dimerization, and is probably catalyzed by an external reductase because no candidate gene was identified within the cluster (Probable). | A0A063C1W0 |
P0AAA7 | WZXE_ECOLI | Lipid III flippase | Escherichia | MSLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRVVGTSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIGVLAYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMRKLLAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAIWLLLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYIVYFSLCCGVFLLWRRRA | Mediates the transbilayer movement of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (lipid III) from the inner to the outer leaflet of the cytoplasmic membrane during the assembly of enterobacterial common antigen (ECA). Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)). Could also mediate the translocation of Und-PP-GlcNAc. | P0AAA7 |
Q0JBY9 | TR120_ORYSJ | Trafficking protein particle complex II-specific subunit 120 homolog | Oryza sativa | MEPGVSIESGSAIRVAVLPVGGPISPARLRDYAALVARHARVDLASLRPYYSEHQKSPFAHQPWGGGCLRLKFVLGGCVPSPWEDFQSSRKVLAVVGICHLPSSPDLGRVAADFVDAARSYPSALASRCFAFCPTDAQLVQKKRDNIIMFPPSDQQSLELHMLTMIQDLSASLLMEFEKWVLRAESTGTILKTPLDSQSSLGSEEVIKAKKRRLGRAQKIIGDYCLLAGSPADANAHYATAIELARLTGDVFWHAGALEGSVCALVVDRMAESDPVLEDEVKFRYYTIIQLYRRATLQDNAQRVSPVSFELEAALKLARYLCRRQCAKEVSDLLMGAADGAKALIDASDRLILYIEIARLFGTLGYKRKAAFFSRQVAQLYLQQDNAYAAMSAMQVLTTTTTAYHVQSRKTSKMDHGLLKSVVSLFESQWSTLQMVVLREILMSSIRAADPLSSWSAAARLLRSFYPLITPAGQSGLASSLSNSADKLPSGTRCADPCLPFIRLHSFPLHPSQREIVKRNPNKKEWWTGGGPSGPFIYTPFTKGGTSGTSKQEVNWIVGEPVQVMVELANPCSFDLIVESIYLSVHSGNFDAFPVSVNLPPNTSKLVLLSGIPTQVGQVSIPGCIVHCFGVITEHLFKEVDCLLLGAAQGLVLSDPFRCCGSSKFKSVNFPSISVVPPLPLLVANVVGGDGSILLYEGEIRDVLITLTNAGTVPVEEANVALSGKNQDSVISIAHSTWKSALPIKPGGEVTFAVTLRAWHLSPTDLEADGSRSPANSRRIAREGSNPFLDIHYAGPSGNSESNDVSLPPGRRLVVPLNICVVQGMRLVRARLLSMELPARFTDAHLRSVSSKDNLSNGSDAIRNDISLLKIDPYKGSWDLRLLELELFNPTDVVFDVDVSVHLDGTSVEQKILPEDKTASSACHKTRIDRDYSARVLIPLEHFKLPVLDTSFFVKENGSDEPLGSRAATLAEKNAKAELNASINNLISKIKVKWHSGRNSSGELNIKDAIQTALQASIMDILLPDPLTFSFRHAKDGTTAKTDSSKEPGDGSSRSADESVLRCKDPIFANEMTHMEVQIRNNTKETIRMNLSISCKDVAGENCFDENSATVLWAGVLSDIYLEVQPLQEVVHPFSIYFLVPGDYSLQAASVIIDATDVLRARAKAESPDEPILCRGSPFHIHVVGTA | Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that is required for the proper transport of proteins in post-Golgi trafficking pathways to the growing cell plate in mitotic active cells. | Q0JBY9 |
O34294 | THIE_RHIEC | Thiamine-phosphate pyrophosphorylase | Rhizobium | MRLDPFYLIVDSADWVERLVPLGVKLVQLRIKDRPEPVLREEIRRAKAACAAAACQLIINDYWRLAIDEGCDFIHLGQEDLMAADLAAIRRAGLKLGLSTHDPSELETALAAAPDYVALGPVWPTILKEMKWAPQGVERLADWRRRVGPMPLVAIGGITAERAPLVLENGADSAAVVTDITRNPDPEARTRQWLAATAPWRSVG | 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). | O34294 |
Q6FYQ5 | TILS_BARQU | tRNA(Ile)-lysidine synthetase | Bartonella | MCVKLAGNLFKTSDFIQCRKVILAVSGGSDSLALLFLVKDHLKTFSIPTEIIVVTVDHQLRRESACEAESVAEICRAHHIQHVIVRWEGKKPKTHIISSARTVRYNLLFKEAQKQGATLIMTGHTLNDQVETYQMRCQRLQKSADVLQREAFEDMRDGVCSTETRANIAEKSYGLMYERGLSCIPREALLNQTVRLIRPLLGVKRKTLRAYLRLKGKTWIDDPTNENPNFERVRVRQSLHPKKFAGIAQKVHEATLQRRKQAQNVANLILALDVSVEHGRCFIAKPVSFLQQHSGFPFVVGLFAVLMGGGFYLLPTKKLNTLVSKLCLHSLEKRRFTLAGSVIESNRSGLAFWRESRNIKEGAVEPGKTFLWDGRYQITNRGDETIKVGAAGLQQLKSLFKNNNFDLENAHFPSLQSLLMISNDKGYDIPELTNHTTSQQSIIIKRIMAPFDWLLSCEDVPFVNVLEPFFDIKVER | 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. | Q6FYQ5 |
A8H5P7 | TOLB_SHEPA | Tol-Pal system protein TolB | Shewanella | MKNLGKWLLTSLLICSMPVKAALDIIITEGVDAARPIAVIPFVWQGTGPMPSQISDVVMSDLARSGTFSPADELSLPQRGISTLAQFNASAWMAQPAEAVVMGSIKPYGGDKYLVSFELIDLVKAQLQSDSMSTKDLVIDSRETVISAAQFRQYGHRISDVVYEKLTGIRGAFLTRVAYVVVNHGEKSPYKLMIADYDGYNEQMLLRSPEPLMSPSWSPDGQSLAYVSFENRKAEVFVQNIYTQQRTKITSFDGINGAPVFSPDGKKLAVTLSKDGQPEVYVVDIATKAIKRVTNHYAIDTEPSWFPDGKSLLITSERGGRPQLYRVFLDSGKISRLTFEGEWNLGGSISPDGRSIIFVNRINGKFNIARMDLETRFMQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSMDGRFKARLPAGQGEVKSPSWSPFL | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | A8H5P7 |
Q944T2 | TCTP_SOYBN | Translationally-controlled tumor protein homolog | Glycine subgen. Soja | MLVYQDLLTGDELLSDSFRYKEIENGMLWEVEGKWVVKGAVDVDIGANPSAEGGGEDEGVDDAAVKVVDIVDTFRLQEQPAFDKKQFVTFMKRFIKNLTPKLDAEQQELFKKHIEGATKYLLSKIKDFQFFVGESMGDDACLVFAYYKDGAADPTFLYFAYALKEVKC | Involved in calcium binding and microtubule stabilization. | Q944T2 |
A6VTV9 | UREE_MARMS | Urease accessory protein UreE | Marinomonas | MLDIYERLGTHCHDPVYTTVTLTHEQRDRGRLKLVGENNEEVRVFLERGKPLLVGEFLKSECGKIVQVAGAVEDVAHASCEDWEAFSKACYHLGNRHTKIQIGERWLRIKPDHVLEDMLHMLGLIVTHEEAVFVPESGAYSHGHSHH | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | A6VTV9 |
Q9PFT8 | TTCA_XYLFA | tRNA 2-thiocytidine biosynthesis protein TtcA | Xylella | MDATFPPQRNITARPAPDRIRREQCKLAKRLRRQVGQAIADFGMIEANDKIMVCLSGGKDSYTLLDMLLQLRAKAPVPFELTAVNLDQKQPGFPKHVLPEYLSSIGMPHHIIEQDTYSVVTRVVPEGKTLCALCSRMRRGALYAYAETQGFTKIALGHHRDDMVATFFMNLFHHAKLSGMPPKLRSDNGKHVVIRPLAYVSETDIIAYADAREFPIIPCNLCGSQENLQRKQVGVILKAWEKEYPGRIEQIARALGNIRPSQLADQSLFDFQALGRHSNTPLPNAHAWLAGDLANDTAP | 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. | Q9PFT8 |
Q21U86 | TATA_ALBFT | Sec-independent protein translocase protein TatA | Rhodoferax | MGFSTTHLLIFLVIIIVIFGTKKLRNIGSDLGGAVKGFKDGMKEGSDKAADAPAAAPQQVASSATAAKETIDVEAKTKA | 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. TatA could form the protein-conducting channel of the Tat system. | Q21U86 |
Q8Z9A5 | UPPS_SALTI | Undecaprenyl pyrophosphate synthase | Salmonella | MLSATQPVSENLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANNGIDALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDISRFNSRLQERIRKSEALTAHNTGLTLNIAANYGGRWDIVQGVRQLAELVQAGVLRPDQIDEERLGQQICMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALHAFANRERRFGGTEPGDDKA | 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. | Q8Z9A5 |
Q2YIT8 | VIRB4_BRUA2 | Type IV secretion system protein virB4 | Brucella | MGAQSKYAQQLNNERSLAPFIPFRSQVGPTTVITRDGDFVRTWRIAGLAFETQDKEKLLIRKDQLNTLFRAIASNNVALWSHNVRRRTWDHLKSFFSNPFCDALDKKYYGSFSGYRMMSNELYLTVIYRPVPAKISRLFNVAVHRSHAEILQEQQLAIRKLDEIGNQIETSLRRYGGDDGRGIEVLSTYEDKHGALCSQQLEFYNFLLSGEWQKVRVPSCPLDEYLGTGWVYAGTETIEIRTANATRYARGIDFKDYANHTEPGILNGLMYSDYEYVITQSFSFMTKRDGKEFLTRQKQRLQNTEDGSASQIMEMDIAIDQLGRGDFVMGEYHYSLLVFAEDMETVRHNTSHAMNILQDNGFLATVIATATDAAFYAQLPCNWRYRPRVAGLTSLNFAGLSCFHNFRAGKRDGNPWGQALTLLKTPSGQPAYLNFHYSKGDEDNFDKKLLGNTRIIGQSGAGKTVLMNFCLAQAQKYLHNAPMGMCNVFFDKDQGAKGTILAIGGKYLAIRNGEPTGFNPFQMEPTAGNILFLEKLVQVLVSRDGQHVTTTDESRISHAIRTVMRMRPELRRLSTVLQNVTEGSDRQDRENSVAKRLAKWCFDDGTGKRGTFWWVLDCPQDQIDFNTHSNYGFDGTDFLDNADVRTPISMYLLHRMELAIDGRRFIYWMDEAWKWVDDEAFSEFANNKQLTIRKQNGLGVFATQMPSSLLNSKVASALVQQVATEIYLPNPKADYHEYTDGFKVTNEEFDIIRSMSEESRMFLVKQGHHSMICRLELNGFDDELAILSGSSDNNELLDQVIAEVGDDPSVWLPVFQERRKARIASSKSTGR | The virB operon is essential for intracellular survival and is not involved in the invasion process. Constitutes a major determinant of virulence in mice. | Q2YIT8 |
A9MKB9 | YBEY_SALAR | Endoribonuclease YbeY | Salmonella | MSQVILDLQLACENHSGLPDEAQFQRWLDGVIPQFQEASEVTIRLVDEAESHDLNLTYRGKDKPTNVLSFPFEAPPGIEMPLLGDLIICRQVVEQEAQEQDKPLEAHWAHMVVHGSLHLLGYDHIDDDEAEEMESLETEIMLAMGYEDPYIAEKE | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A9MKB9 |
P32779 | VLP25_BORHE | Variable major outer membrane lipoprotein 25 | Borrelia | MRKRISAIINKLNISIMMMIVVLMIGCGQQAVEAGKDGAAAATGGRSLSEVLMEVGKSAENAFYSFMALVPDTLGLRVTKDTKKNEVGGYFNSLGGKLGKASDELEEVAKKSEVEGAKDGPIAVAIRAAVDTAKTTLSTLKEHLESLKGIGDDDKVGEATSNQNGVAASTDELKGAFKALKGIVDTAGKEGVAKPKAGDTAVKIGNADNKDGAKVLAAAANAGRAVGDKAAAIVSAVSGEEMLASIVASQEGDADAALAADATAQTSALKFARGGGNAGQLAKEAAKAAAVAGGIALRSLVKGGKLAANNNDDDKVVQSAGVTAVNKLLVAVEGIIKKTVKNVLEKAKGEIDKARAPKATGQ | The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. | P32779 |
V9QFG7 | TXA2_LATGE | Latrodectin-2 | Latrodectus | MLKLICIVFLVTVLTFVVGEDTLDPAEYGCPSDVDMAELTEKNEVCLRCEDFHKEGVAFTLCKTNCFTTEYYKNCVKDLEEAGKETEE | May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana. | V9QFG7 |
Q8NCN2 | ZBT34_HUMAN | Zinc finger and BTB domain-containing protein 34 | Homo | MDSSSFIQFDVPEYSSTVLSQLNELRLQGKLCDIIVHIQGQPFRAHKAVLAASSPYFRDHSALSTMSGLSISVIKNPNVFEQLLSFCYTGRMSLQLKDVVSFLTAASFLQMQCVIDKCTQILESIHSKISVGDVDSVTVGAEENPESRNGVKDSSFFANPVEISPPYCSQGRQPTASSDLRMETTPSKALRSRLQEEGHSDRGSSGSVSEYEIQIEGDHEQGDLLVRESQITEVKVKMEKSDRPSCSDSSSLGDDGYHTEMVDGEQVVAVNVGSYGSVLQHAYSYSQAASQPTNVSEAFGSLSNSSPSRSMLSCFRGGRARQKRALSVHLHSDLQGLVQGSDSEAMMNNPGYESSPRERSARGHWYPYNERLICIYCGKSFNQKGSLDRHMRLHMGITPFVCKFCGKKYTRKDQLEYHIRGHTDDKPFRCEICGKCFPFQGTLNQHLRKNHPGVAEVRSRIESPERTDVYVEQKLENDASASEMGLDSRMEIHTVSDAPD | May be a transcriptional repressor. | Q8NCN2 |
Q831N0 | TSAD_ENTFA | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Enterococcus | MTIFTKERKLLLAVESSCDETSVAVIEDGDKILSNIVASQIKSHQRFGGVVPEVASRHHVEQVTICIEEALTEAKVTPEELSGVAVTYGPGLVGALLIGLSAAKAFAWAHQLPLIPVNHMAGHIYAARFVAPLEFPLMALLVSGGHTELVYMKEDGSFEIVGETRDDAAGEAYDKVGRVLGLPYPSGKEIDALAHEGTDTYQFPRAMLKEDNYDFSFSGLKSAFINTVHNAEQRGEALSTKDLAASFQASVVEVLVTKTIRACQEYPVKQLLIAGGVAANQGLREAMRHAISEQLPAVTLLIPPLKLCGDNAAMIGAAAFIEAEKNHFASYNLNAEPGVSFMTISEEG | 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. | Q831N0 |
B2SXA0 | UBIA_PARPJ | 4-HB polyprenyltransferase | Paraburkholderia | MFARLPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGHPTWPLLVIFTVGTVLMRSAGCAINDYADRDFDRYVKRTENRPITSGKIKAWEAVALAAALSLLAFLLILPLNTLTKELSVAALFVAGSYPFTKRFFAIPQAYLGIAFGFGIPMAFAAIQGHVPLLAWVMLLANVFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAIMICYAATLGIYVGIGVLLGFGVLYWLGWAAAAGCAIYHYTLIRNRERMACFAAFRHNNWLGGALFVGIAAHYAAGSF | 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. | B2SXA0 |
P36195 | TDT_CHICK | Terminal deoxynucleotidyltransferase | Gallus | MERIRPPTVVSQRKRQKGMYSPKLSCGYEIKFNKLVIFIMQRKMGMTRRTFLMELARSKGFRVESELSDSVTHIVAENNSYPEVLDWLKGQAVGDSSRFEILDISWLTACMEMGRPVDLEKKYHLVEQAGQYPTLKTPESEVSSFTASKVSQYSCQRKTTLNNCNKKFTDAFEIMAENYEFKENEIFCLEFLRAASVLKSLPFPVTRMKDIQGLPCMGDRVRDVIEEIIEEGESSRAKDVLNDERYKSFKEFTSVFGVGVKTSEKWFRMGLRTVEEVKADKTLKLSKMQRAGFLYYEDLVSCVSKAEADAVSSIVKNTVCTFLPDALVTITGGFRRGKKIGHDIDFLITSPGQREDDELLHKGLLLYCDIIESTFVKEQIPSRHVDAMDHFQKCFAILKLYQPRVDNSSYNMSKKCDMAEVKDWKAIRVDLVITPFEQYAYALLGWTGSRQFGRDLRRYATHERKMMLDNHALYDKRKRVFLKAGSEEEIFAHLGLDYVEPWERNA | Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. | P36195 |