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
|
|---|---|---|---|---|---|---|
B7LWL0
|
TRUD_ESCF3
|
tRNA-uridine isomerase D
|
Escherichia
|
MIEFDNLTYLHGKPQGTGLLKANPEDFVVVEDLGFEPDGEGEHILVRILKNGCNTRFVADALAKFLKIHAREVSFAGQKDKHAVTEQWFCARVPGKEMPDLSAFQLEGCQVLEYARHKRKLRLGALKGNAFTLVLRDVSNRDDVEQRLIDICVKGVPNYFGAQRFGIGGSNLQGALRWAQTNTPVRDRNKRSFWLSAARSALFNQIVAERLKKADVNQVVDGDALQLAGRGSWFVATTEELAELQRRVNDKELMITAALPGSGEWGTQREALAFEQAAVAEETELQTLLVREKVEAARRAMLLYPQQLSWNWWDDVTVEIRFWLPAGSFATSVVRELINTTGEYAHIAE
|
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
|
B7LWL0
|
Q9ZJG8
|
YIDC_HELPJ
|
Membrane protein YidC
|
Helicobacter
|
MDKNNNNNLRLILAIALSFLFIALYSYFFQEPNKTTTETTKQETTNNHTATSPTASNTITQDFSVTQTIPQESLLSTISFEHAKIEIDSLGRIKQVYLKDKKYLTPKEKGFLEHVSHLFSSKENSQPSLKELPLLAADKLKPLEVRFLDPTLNNKAFNTPYSASKTTLGPNEQLVLTQDLGTLSIIKTLTFYDDLHYDLKIAFKSPNNLIPSYVITNGYRPVADLDSYTFSGVLLENTDKKIEKIEDKDAKEIKRFSNTLFLSSVDRYFTTLLFTKDPQGFEALIDSEIGTKNPLGFISLKNEANLHGYIGPKDYRSLKAISPMLTDVIEYGLITFFAKGVFVLLDYLYQFVGNWGWAIILLTIIVRIILYPLSYKGMVSMQKLKELAPKMKELQEKYKGEPQKLQAHMMQLYKKHGANPLGGCLPLILQIPVFFAIYRVLYNAVELKSSEWVLWIHDLSIMDPYFILPLLMGASMYWHQSVTPNTMTDPMQAKIFKLLPLLFTIFLITFPAGLVLYWTTHNILSVLQQLIINKVLENKKRAHAQNIKE
|
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.
|
Q9ZJG8
|
P77315
|
YPHD_ECOLI
|
Probable ABC transporter permease protein YphD
|
Escherichia
|
MSASSLPLPQGKSVSLKQFVSRHINEIGLLVVIAILYLVFSLNAPGFISLNNQMNVLRDAATIGIAAWAMTLIIISGEIDVSVGPMVAFVSVCLAFLLQFEVPLAVACLLVLLLGALMGTLAGVLRGVFNVPSFVATLGLWSALRGMGLFMTNALPVPIDENEVLDWLGGQFLGVPVSALIMIVLFALFVFISRKTAFGRSVFAVGGNATAAQLCGINVRRVRILIFTLSGLLAAVTGILLAARLGSGNAGAANGLEFDVIAAVVVGGTALSGGRGSLFGTLLGVLVITLIGNGLVLLGINSFFQQVVRGVIIVVAVLANILLTQRSSKAKR
|
Probably part of the binding-protein-dependent transport system YphDEF. Probably responsible for the translocation of the substrate across the membrane.
|
P77315
|
Q20745
|
UNC84_CAEEL
|
Uncoordinated protein 84
|
Caenorhabditis
|
MAPATEADNNFDTHEWKSEFASTRSGRNSPNIFAKVRRKLLLTPPVRNARSPRLTEEELDALTGDLPYATNYTYAYSKIYDPSLPDHWEVPNLGGTTSGSLSEQEHWSAASLSRQLLYILRFPVYLVLHVITYILEAFYHVIKITSFTIWDYLLYLVKLAKTRYYAYQDHRRRTALIRNRQEPFSTKAARSIRRFFEILVYVVLTPYRMLTRSNNGVEQYQYRSIKDQLENERASRMTTRSQTLERSRKFDGLSKSPARRAAPAFVKTSTITRITAKVFSSSPFGEGTSENITPTVVTTRTVKQRSVTPRFRQTRATREAITRALDTPELEIDTPLSTYGLRSRGLSHLNTPEPTFDIGHAAATSTPLFPQETYNYQYEEATGNKIKTAFTWLGYLILFPFFAARHVWYTFYDYGKSAYMKLTNYQQAPMETIHVRDINEPAPSSSDVHDAVGVSWRIRIADFLSSFVATIVEAHQVVFAMFKGGIVETVSYFGGLFAGLTDKKSSKFSWCQILGLLLALLFAIFLLGFLTSDNTAIRVKEITKDKNASKKSEGSLPAVPIWISAANHVKHYTWMVKEFVVDIAFDTYNYGKSTIGRLGTTPRYAWDLIASGCGAVGNGLKSVLSSSFRFIDFCAGKLFYYGSDGFLSANKSIGTFFNGCYETLYNGCTAIVGHTKSFIYNASNAVYNFFSTIFAGLLNFSTSSQNSILSLLKSFGTGITNIFYNFIYAPIAGVFNFAGDNYMYFFNEVAAVFGKVYNSVVSVLKTVINWILFLIAYPFSLCTRAWIRISQYAPEDVVQVIPIPQAITPTPDVERIVEEPLRKVTDVEDEELVIIPAPAPKPIPVPAPTPAPVIIHQTNVVETVDKDAIIKEVTEKLRAELSAQFQQELSAKFEQNYNTIIEQLKMENTNIQYDKNHLEAIIRQMIYEYDTDKTGKVDYALESSGGAVVSTRCSETYKSYTRLEKFWDIPIYYFHYSPRVVIQRNSKSLFPGECWCFKESRGYIAVELSHFIDVSSISYEHIGSEVAPEGNRSSAPKGVLVWAYKQIDDLNSRVLIGDYTYDLDGPPLQFFLAKHKPDFPVKFVELEVTSNYGAPFTCLYRLRVHGKVVQV
|
Involved in nuclear migration and anchoring in hypodermal precursor cells . Most likely recruits anc-1 to the nuclear envelope where anc-1 functions to tether the nucleus to the actin cytoskeleton . Component of the unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton) complex where it recruits and interacts with unc-83 to form a bridge connecting the nuclear envelope to the cytoskeleton which allows for nuclear transport along microtubules . Its role in nuclear migration may be in association with lamin, lmn-1 . Regulates nuclear migrations in one-cell embryos, controlling the posterior migration of the male pronucleus following fertilization . Not required for centrosome attachment to the nucleus . Plays a role in the maintenance of the nuclear envelope architecture in body wall muscle cells . May be involved in DNA damage repair through an association with zyg-12 . Potentially has roles in homologous recombination, double strand break repair and meiotic recombination . Specifically, may in part inhibit non-homologous end joining repair, most likely through recruiting fan-1 to the nucleoplasm, to facilitate the repair of DNA cross-links .
|
Q20745
|
Q7TTX7
|
TGT_PARMW
|
tRNA-guanine transglycosylase
|
Parasynechococcus marenigrum
|
MFGFEISAHCANTAARCGCFHTPHGPVHTPRFMPVGTLATVKGISTDQLARTGAQMVLSNTYHLHLQPGEEIVAAAGGLHGFMGWDGPMLTDSGGFQVFSLGDLNKIDDRGVVFRNPRDGRIIDMTPEHATQIQMALGADVAMAFDQCPPYPATENDVIDACRRTHAWLARCVEAHSRDNQALFGIVQGGCFPHLRRESARAVADFDLPGIAVGGVSVGEPVEEMHRIVRDVTPLLPTHKPRYLMGIGTLREMAVAVANGIDLFDCVLPTRLGRHGTALVGGERWNLRNARFRHDHTPLDPSCPCPTCSGGHTRAYLNHLIRSEELLGLTLLSLHNITHLLRFTTAMSQAIRDGCFSEDFAPWEPDSPAHHTW
|
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).
|
Q7TTX7
|
A7Z0S0
|
TRUA_BACVZ
|
tRNA-uridine isomerase I
|
Bacillus amyloliquefaciens group
|
MRVKCTIAYDGHLFNGYQVQPGKRTVQSELEKALAVIHKTDGRVPVYSSGRTDSDVHAAGQVIHFDTPLSIPGEKWPFALNALLPDDIAVKTAEIADDGFHARFSAVQKEYRYFVYTEKHPDVFKRHYAYHFAYPLNVQKMREASRHLVGTHDFTSFCAADTAVQDKVRTIYELDWTETVDGLQMRITGNGFLYNMVRIIAGTLLDTGAGKFSPDDVKAMLEAKDREAAGRTAPGHGLYLWSVCYDN
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
A7Z0S0
|
Q9A6H0
|
TYSY_CAUVC
|
Thymidylate synthase
|
Caulobacter
|
MSTAVLDAPKAATDHPERQYLTLLADILENGVQRGDRTGTGTLGVFGRQIRFDLAKGFPVLTTKKLHLRSIIIELLWFLKGDTNIAYLKDNGVRIWDEWADENGDLGPVYGKQWRSWATPDGRVIDQISALVENLKANPNSRRHIVTAWNPADVDDMALPPCHCLFQFFVADGKLSCQLYQRSADVFLGVPFNIASYALLTLMVAKVVGLEPGEFVHTFGDAHLYLNHLDQAREQLTREPFDFPTMKIADKRDLFGFEYEDFTLEGYQAHPHIKAEVSV
|
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.
|
Q9A6H0
|
P23669
|
THRC_CORGL
|
Threonine synthase
|
Corynebacterium
|
MDYISTRDASRTPARFSDILLGGLAPDGGLYLPATYPQLDDAQLSKWREVLANEGYAALAAEVISLFVDDIPVEDIKAITARAYTYPKFNSEDIVPVTELEDNIYLGHLSEGPTAAFKDMAMQLLGELFEYELRRRNETINILGATSGDTGSSAEYAMRGREGIRVFMLTPAGRMTPFQQAQMFGLDDPNIFNIALDGVFDDCQDVVKAVSADAEFKKDNRIGAVNSINWARLMAQVVYYVSSWIRTTTSNDQKVSFSVPTGNFGDICAGHIARQMGLPIDRLIVATNENDVLDEFFRTGDYRVRSSADTHETSSPSMDISRASNFERFIFDLLGRDATRVNDLFGTQVRQGGFSLADDANFEKAAAEYGFASGRSTHADRVATIADVHSRLDVLIDPHTADGVHVARQWRDEVNTPIIVLETALPVKFADTIVEAIGEAPQTPERFAAIMDAPFKVSDLPNDTDAVKQYIVDAIANTSVK
|
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
|
P23669
|
P38987
|
TEM1_YEAST
|
Protein TEM1
|
Saccharomyces
|
MATPSTGANNSIPAVRNQVEVQVGLVGDAQVGKTSLMVKYVQNIYDKEYTQTLGVNFLKRKVSIRSTDIIFSIMDLGGQREFINMLPIATVGSSVIIFLFDLTRPETLSSIKEWYRQAYGLNDSAIPILVGTKYDLLIDLDPEYQEQISRTSMKYAQVMNAPLIFCSTAKSINIQKIFKIALAKIFNLTLTIPEINEIGDPLLIYKHLGGQQHRHHNKSQDRKSHNIRKPSSSPSSKAPSPGVNT
|
GTP-binding protein involved in termination of M phase. May play a role in triggering the degradation of G2 cyclin to inactivate M-phase promoting factor at the termination of mitosis. Acts upstream of CDC15 kinase and may be required to activate the CDC15 protein kinase pathway.
|
P38987
|
Q7WY78
|
TAGT_BACSU
|
Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagT
|
Bacillus
|
MEERSQRRKKKRKLKKWVKVVAGLMAFLVIAAGSVGAYAFVKLNNASKEAHVSLARGEQSVKRIKEFDPGKDSFSVLLLGIDAREKNGETVDQARSDANVLVTFNRKEKTAKMLSIPRDAYVNIPGHGYDKFTHAHAYGGVDLTVKTVEEMLDIPVDYVVESNFTAFEDVVNELNGVKVTVKSDKVIQQIKKDTKGKVVLQKGTHTLDGEEALAYVRTRKADSDLLRGQRQMEVLSAIIDKSKSLSSIPAYDDIVDTMGQNLKMNLSLKDAIGLFPFITSLKSVESIQLTGYDYEPAGVYYFKLNQQKLQEVKKELQNDLGV
|
May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG).
|
Q7WY78
|
A7LAC6
|
VSP1_TRIAB
|
Snake venom serine protease
|
Trimeresurus
|
MVLITVLANLLILQLSYAQKSSELVIGGDECNINEHRFLVALYDVWSGDFLCGGTLINKEYVLTAAHCETRNMYIYLGMHNKNVQFDDEQRRYPKKKYFFRCSNNFTRWDKDIMLIRLNRPVRNSEHIAPLSLPSSPPSVGSVCRVMGWGTITSPNETLPDVPRCANINLLNYTVCRGVFPRLPARSRTLCAGVLQGGIDTCKRDSGGPLICNGQLQGVVFWGPKPCAQPRKPALYTKVFNHLDWIQSIIAGNTTVTCPP
|
Thrombin-like snake venom serine protease.
|
A7LAC6
|
Q8ZK90
|
ULAA_SALTY
|
Ascorbate-specific permease IIC component UlaA
|
Salmonella
|
MEILYNIFTIFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIERMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVSFYIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKTHWTIYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSILIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWAVKLTGMSAWMGMADWSILAPPMMQGFFSLGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA
|
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.
|
Q8ZK90
|
O14273
|
YET4_SCHPO
|
Meiotically up-regulated protein C8C9.04
|
Schizosaccharomyces
|
MTTNPDIVKQTKNEIHQVTSRVQEKLDSKSTNAVEQNNNSSQASVTKDNKKKAAKRAKKKAAKKKKQSAAASASSTPVEEAQHAQEEQQEQTILQEPGFTQTIVEKDADQVDEPLEPIASSALGTVEPPTDNKPSASTSTAVPTTEARNTSITEPANSPSSSSSSASTKSTATTQSADYVVAEHFAPQRNDEQLGNSPASITSKPATTSAAQPSSKVEENMAKATSQPITTAEKEIPELKPIEPEAIMISKEINTTHDQAAATTTAAVASASTTATAESHAVADGIMNDNVLESIGENVQQETVFEDASDIPHADVIPHTTTVTVEEESPIALGQGGVTHEATTSARASASGIPGAFEEVQQTVQEDLPHPTAETVEIARFAEQPVRAQQPEQYESSVVQEATETVTDVGKGVSSTVKNEVNVPSTIPTESENPVAVGGTTAEHPVQEAVTAPTETAHDFSKETTTASKRVSKHDKASAEKHKVARKPSSTGQEPTTPSTPAKSAQSSKHARRPSKQASAPSSPGTTSAAVPGGKKSAIEAAAPIPTSADTVESKHAAGSGSATTIPSPGSATTKPTPGSATTKPTPVSATEEHAAGTTKPAPAAGATATAENETADGKAQTATDGEAAPKKSWFKRMKKSFGKLFH
|
Has a role in meiosis and sporulation.
|
O14273
|
Q5FWF6
|
ZN789_HUMAN
|
Zinc finger protein 789
|
Homo
|
MFPPARGKELLSFEDVAMYFTREEWGHLNWGQKDLYRDVMLENYRNMVLLGFQFPKPEMICQLENWDEQWILDLPRTGNRKASGSACPGSEARHKMKKLTPKQKFSEDLESYKISVVMQESAEKLSEKLHKCKEFVDSCRLTFPTSGDEYSRGFLQNLNLIQDQNAQTRWKQGRYDEDGKPFNQRSLLLGHERILTRAKSYECSECGKVIRRKAWFDQHQRIHFLENPFECKVCGQAFRQRSALTVHKQCHLQNKPYRCHDCGKCFRQLAYLVEHKRIHTKEKPYKCSKCEKTFSQNSTLIRHQVIHSGEKRHKCLECGKAFGRHSTLLCHQQIHSKPNTHKCSECGQSFGRNVDLIQHQRIHTKEEFFQCGECGKTFSFKRNLFRHQVIHTGSQPYQCVICGKSFKWHTSFIKHQGTHKGQIST
|
May be involved in transcriptional regulation.
|
Q5FWF6
|
A1K8Q1
|
UBIG_AZOSB
|
3-demethylubiquinone 3-O-methyltransferase
|
Azoarcus
|
MNTNADPAEVQKFSDLAHRWWDPASEFKPLHEINPLRLDWIDGHCGLAGKKVLDVGCGGGLLSEGMAQRGAEVSGIDLSEKALGVARLHLYESGLQVDYQLTSAEAHAATHPAQFDVVTCMEMLEHVPNPESTVHACAQMAKPGGAVFFSTLNRNFKAYLFAVVGAEYLLNLLPRGTHDYAKFIKPSELSRYCRNAGLELVSLSGMTYNPITKVYALSRDTDVNYMVHARKLG
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
A1K8Q1
|
Q0TEV3
|
TRMJ_ECOL5
|
tRNA Cm32/Um32 methyltransferase
|
Escherichia
|
MLQNIRIVLVETSHTGNMGSVARAMKTMGLTNLWLVNPLVKPDSQAIALAAGASDVIGNAHIVDTLDEALAGCSLVVGTSARSRTLPWPILDPRECGLKSVAEAANTPVALVFGRERVGLTNEELQKCHYHVAIAANPEYSSLNLAMAVQVIAYEVRMAWLATQENGEQVEHEETPYPLVDDLERFYGHLEQTLLATGFIRENHPGQVMNKLRRLFTRARPESQELNILRGILASIEQQNKGNKAE
|
Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
|
Q0TEV3
|
P07911
|
UROM_HUMAN
|
Uromodulin, secreted form
|
Homo
|
MGQPSLTWMLMVVVASWFITTAATDTSEARWCSECHSNATCTEDEAVTTCTCQEGFTGDGLTCVDLDECAIPGAHNCSANSSCVNTPGSFSCVCPEGFRLSPGLGCTDVDECAEPGLSHCHALATCVNVVGSYLCVCPAGYRGDGWHCECSPGSCGPGLDCVPEGDALVCADPCQAHRTLDEYWRSTEYGEGYACDTDLRGWYRFVGQGGARMAETCVPVLRCNTAAPMWLNGTHPSSDEGIVSRKACAHWSGHCCLWDASVQVKACAGGYYVYNLTAPPECHLAYCTDPSSVEGTCEECSIDEDCKSNNGRWHCQCKQDFNITDISLLEHRLECGANDMKVSLGKCQLKSLGFDKVFMYLSDSRCSGFNDRDNRDWVSVVTPARDGPCGTVLTRNETHATYSNTLYLADEIIIRDLNIKINFACSYPLDMKVSLKTALQPMVSALNIRVGGTGMFTVRMALFQTPSYTQPYQGSSVTLSTEAFLYVGTMLDGGDLSRFALLMTNCYATPSSNATDPLKYFIIQDRCPHTRDSTIQVVENGESSQGRFSVQMFRFAGNYDLVYLHCEVYLCDTMNEKCKPTCSGTRFRSGSVIDQSRVLNLGPITRKGVQATVSRAFSSLGLLKVWLPLLLSATLTLTFQ
|
In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals.
|
P07911
|
Q81GG4
|
TRPA_BACCR
|
Tryptophan synthase alpha chain
|
Bacillus cereus group
|
MGVEKIKAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREVNIALIPLVTVTSPIERIEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKVIELLENEKREEICELIYATKQKEEA
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
Q81GG4
|
Q31910
|
YCF4_BRAOL
|
Photosystem I assembly protein Ycf4
|
Brassica
|
MTWRSEHIWIDLISGSRKKSNFCWAFLLFLGSLGFVLVGTSSYLGRNLISSFPPQQITFFPQGLVMSFYGIAGLFISCYLWCTILWNVGSGYDLFDRKEGIVRIFRWGFPGKSRRIVLRFLMKDIQSDRTEVKEGVSARRVPYMEIRGQGAIPLIRTDENFTTRREIEQKAAELAYFLRVPIEVF
|
Seems to be required for the assembly of the photosystem I complex.
|
Q31910
|
Q5PQR8
|
TPRKB_RAT
|
TP53RK-binding protein
|
Rattus
|
MQLTQQLDLFPECKVTLLLFKDVKNAGDLRKKAMEGSIDGSLINANVIVDPFQILVAANKAVHLHKLGKMKTRTLSTEIIFNLSPNNNISEALKKFGISESNTSVLIVYVEDGDKQVHQEHLVSQVEGQQVPLESLPEITRLSEVRKVCSTQPEEVSR
|
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TPRKB acts as an allosteric effector that regulates the t(6)A activity of the complex. TPRKB is not required for tRNA modification.
|
Q5PQR8
|
Q5SVQ8
|
ZBT41_HUMAN
|
Zinc finger and BTB domain-containing protein 41
|
Homo
|
MKKRRKVTSNLEKIHLGYHKDSSEGNVAVECDQVTYTHSAGRPTPEALHCYQELPPSPDQRKLLSSLQYNKNLLKYLNDDRQKQPSFCDLLIIVEGKEFSAHKVVVAVGSSYFHACLSKNPSTDVVTLDHVTHSVFQHLLEFLYTSEFFVYKYEIPLVLEAAKFLDIIDAVKLLNNENVAPFHSELTEKSSPEETLNELTGRLSNNHQCKFCSRHFCYKKSLENHLAKTHRSLLLGKKHGLKMLERSFSARRSKRNRKCPVKFDDTSDDEQESGDGSDNLNQENFDKEKSDRNDSEDPGSEYNAEEDELEEEMSDEYSDIEEQSEKDHNDAEEEPEAGDSVGNVHEGLTPVVIQNSNKKILQCPKCDKTFDRIGKYESHTRVHTGEKPFECDICHQRYSTKSNLTVHRKKHSNETEFHKKEHKCPYCNKLHASKKTLAKHVKRFHPENAQEFISIKKTKSESWKCDICKKSFTRRPHLEEHMILHSQDKPFKCTYCEEHFKSRFARLKHQEKFHLGPFPCDICGRQFNDTGNLKRHIECTHGGKRKWTCFICGKSVRERTTLKEHLRIHSGEKPHLCSICGQSFRHGSSYRLHLRVHHDDKRYECDECGKTFIRHDHLTKHKKIHSGEKAHQCEECGKCFGRRDHLTVHYKSVHLGEKVWQKYKATFHQCDVCKKIFKGKSSLEMHFRTHSGEKPYKCQICNQSFRIKKTLTKHLVIHSDARPFNCQHCNATFKRKDKLKYHIDHVHEIKSPDDPLSTSEEKLVSLPVEYSSDDKIFQTETKQYMDQPKVYQSEAKTMLQNVSAEVCVPVTLVPVQMPDTPSDLVRHTTTLPPSSHEILSPQPQSTDYPRAADLAFLEKYTLTPQPANIVHPVRPEQMLDPREQSYLGTLLGLDSTTGVQNISTNEHHS
|
May be involved in transcriptional regulation.
|
Q5SVQ8
|
A6LT26
|
TIG_CLOB8
|
PPIase
|
Clostridium
|
MKAKVEKIETNVIKLEIRVEAEKFDAALTKAYNKNKGRYNIPGFRKGKVPMAMVKKFYGVEVFYDDAVNFAIDESYPEALNAENIKPVDYPQVDIVELGEGKELVYTATVTTYPEVELGEYKGLDIKKPIYEVEDTEIDKQIKEMQEKNARIEVKTEGNIAKGDIAVIDFKGYIDGVAFEGGEGSDYSLEIGSGTFIDNFEEQLIGLAVGDKKEVNVTFPEAYGKEELNGKPAMFEVEIKSIKVKELPELDDEFAKDVSAVDTFAELKENLKKTLEKNNDEKAEREFEEAVITAVIENSKMDIPEVMVNKEIDAMMQDLEGRLKYQGLSLEQYMEFTGNTTEKMRDFMKENAERKVKADLVLEAIAKTEEIKATEEELNARALELGKIYGPKDPEKMAKILVKSQRNMIEKDIILENTLKFLKENCK
|
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.
|
A6LT26
|
Q12QH9
|
TRUB_SHEDO
|
tRNA-uridine isomerase
|
Shewanella
|
MARRSKGRQIDGIVLLDKDTGMSSNYALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDADKRYLVTAKLGVRTDTSDSDGEVVQTRDINFTQAQLETALEHFRGDTMQVPSMFSALKHQGQPLYKYAREGIEVPREARPITVFELNFIKLEGDELTLDIHCSKGTYIRTITDDLGEMLGCGAHVIMLRRTQVADYPYDKMVSLADLEALVTQAQQQELAVGELLDPLLLPMDTAVANFPEINLPESMLYYVMQGQAVQASGLKIDVLVRITIGEQRKFVGIGIMNDDGLLAPKRLIVIPAEESPE
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q12QH9
|
Q6Q4D0
|
TONS_ARATH
|
Protein MGOUN 3
|
Arabidopsis
|
MGRLDVAAAKRAYRKAEEVGDRREQARWANNVGDILKNHGEYVDALKWFRIDYDISVKYLPGKDLLPTCQSLGEIYLRLENFEEALIYQKKHLQLAEEANDTVEKQRACTQLGRTYHEMFLKSEDDCEAIQSAKKYFKKAMELAQILKEKPPPGESSGFLEEYINAHNNIGMLDLDLDNPEAARTILKKGLQICDEEEVREYDAARSRLHHNLGNVFMALRSWDEAKKHIEMDINICHKINHVQGEAKGYINLAELHNKTQKYIDALLCYGKASSLAKSMQDESALVEQIEHNTKIVKKSMKVMEELREEELMLKKLSAEMTDAKGTSEERKSMLQVNACLGSLIDKSSMVFAWLKHLQYSKRKKKISDELCDKEKLSDAFMIVGESYQNLRNFRKSLKWFIRSYEGHEAIGNLEGQALAKINIGNGLDCIGEWTGALQAYEEGYRIALKANLPSIQLSALEDIHYIHMMRFGNAQKASELKETIQNLKESEHAEKAECSTQDECSETDSEGHANVSNDRPNACSSPQTPNSLRSERLADLDEANDDVPLISFLQPGKRLFKRKQVSGKQDADTDQTKKDFSVVADSQQTVAGRKRIRVILSDDESETEYELGCPKDSSHKVLRQNEEVSEESMYFDGAINYTDNRAIQDNVEEGSCSYTPLHPIKVAPNVSNCRSLSNNIAVETTGRRKKGSQCDVGDSNGTSCKTGAALVNFHAYSKTEDRKIKIEIENEHIALDSCSHDDESVKVELTCLYYLQLPDDEKSKGLLPIIHHLEYGGRVLKPLELYAILRDSSENVVIEASVDGWVHKRLMKLYMDCCQSLSEKPSMKLLKKLYISEVEDDINVSECELQDISAAPLLCALHVHNIAMLDLSHNMLGNGTMEKLKQLFASSSQMYGALTLDLHCNRFGPTALFQICECPVLFTRLEVLNVSRNRLTDACGSYLSTIVKNCRALYSLNVEHCSLTSRTIQKVANALDSKSGLSQLCIGYNNPVSGSSIQNLLAKLATLSSFAELSMNGIKLSSQVVDSLYALVKTPSLSKLLVGSSGIGTDGAIKVTESLCYQKEETVKLDLSCCGLASSFFIKLNQDVTLTSSILEFNVGGNPITEEGISALGELLRNPCSNIKVLILSKCHLKLAGLLCIIQALSDNKNLEELNLSDNAKIEDETVFGQPVKERSVMVEQEHGTCKSVTSMDKEQELCETNMECDDLEVADSEDEQIEEGTATSSSLSLPRKNHIVKELSTALSMANQLKILDLSNNGFSVEALETLYMSWSSSSSRTGIAQRHVKEETVHFYVEGKMCCGVKSCCRKD
|
Histone reader involved in homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks . Specifically recognizes and binds histone H3.1 lacking methylation at 'Lys-27' (H3K27me1) . Involved in structural and functional stabilization of chromatin; represents a link between response to DNA damage and epigenetic gene silencing . Required for cell arrangement in root and shoot apical meristems . May be involved, when interacting with TSA1, in the organization of spindle microtubules .
|
Q6Q4D0
|
Q811H0
|
ZBT42_MOUSE
|
Protein simiRP58
|
Mus
|
MEFPEHGVRLLGRLRQQRELGFLCDCTVLVGDARFPAHRAVLAACSVYFHLFYRDQPASSRDTVRLNGDIVTVPAFSRLLDFMYEGRLDLHNLPVEDVLAAASYLHMYDIVKVCKGRLRKKDPDLETRTLGTELPGQPPHPLPSWSPAFCQAAPKAKHPSLGVKATHPLPTFGPPSWQVAEQSSGALDLSLKPSPRPEQVHPPCRLQTSLCSSVQQVAQPLVKAEQDSFSEQDSSSPQSADRSPPPVCASAAQGLAVDLEPLHIEGTGSQQLGLPAEPVLDSEELGPSRHLCICPLCCKLFPSTHALQLHLSAHFRERDSVRARLSPEGSVPTCPLCSKTFSCTYTLKRHERTHSGEKPYTCVQCGKSFQYSHNLSRHAVVHTREKPHACRWCERRFTQSGDLYRHVRKFHYGLVKPLLV
|
Transcriptional repressor. Specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes.
|
Q811H0
|
Q2NIY3
|
TRUA_AYWBP
|
tRNA-uridine isomerase I
|
Candidatus Phytoplasma asteris
|
MQHFFYKLILSYDGTFYCGYQKQPQKKTVQQTFEKALKKMTHQNIPTFAASRTDKGVHSQGQTLHFQTTFSLKPKHFQKTLNYLLPPDIRVRQMHFATPNFHARYSAKSKIYQYVFSKKPLNAFNHHFQIFADKFDFVKITKALKFIEGTHNFFAFTSETQPKNFSKTIFQASLKETVHKYILVFHGNGFLKYMIRFLVGSLIEIGKNKFSLEQFQAMLLGNKTKKATLLAPAKALVLKKIFY
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q2NIY3
|
Q8UVG0
|
VM3BE_BOTER
|
ery1
|
Bothrops
|
MIQVLLVIICLEAFPYQGSSIILESGNVNDYEVVYPRKVTALSKGAVHPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSEIHYSPDGREITTYPLVEDHCYYHGRIQNDADSSASISACNGLKGHFKLQGEMYLIEPFKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKKASLLNLTPEQQAYLDAKKYVEFVVVLDHGMYKKYKDDLDKIKRRIYEIVNTMNEMFIPLNICVALTGLEIWSKGDKINVTSESWFTLILFTNWRGADLLKRKSHDNAQLLTNTDFDGSTIGRAHIGSMCHPYLSVGIIQDYSPVNLLVASTMAHEMGHNLGMHHDNDTCTCGAPSCVMAAAISKDPSKLFSNCSQEYQRKYLIKNRPQCLLNKPLRTDIISPPVCGNELLEVGEECDCGTPENCRDPCCNATTCKLTPGSQCVEGLCCDQCRFRKTGTECRAAKHDCDLPESCTGQSADCPMDDFQRNGHPCQNNNGYCYNGKCPTMENQCIDLVGPKATVAEDSCFKDNQKGNDYGYCRKENGKKIPCEPQDVKCGRLYCNDNSPGQNNPCKCIYFPRNEDRGMVLPGTKCADGKVCSNRHCVDVATAY
|
Potent activator of prothrombin (F2). Does not elicit any hemorrhagic response. Barely inhibits collagen-induced platelet aggregation. Binds neither collagen, nor the jararhagin monoclonal antibody MAJar3. Hydrolyzes the Aalpha-chain of fibrin and fibrinogen, without affecting the Bbeta- and gamma-chains. Is capable of triggering endothelial pro-inflammatory and procoagulant cell responses, but fails to trigger apoptosis. Induces von Willebrand factor release, and the expression of both ICAM1 and E-selectin (SELE) (without increase in VCAM1) in endothelial cells (HUVEC). Is also able to up-regulate the synthesis of the coagulation factor TF (F3). Enhances nitric oxide (NO) generation, prostacyclin production and interleukin-8 release.
|
Q8UVG0
|
P69823
|
ULAB_ECO57
|
Ascorbate-specific phosphotransferase enzyme IIB component
|
Escherichia
|
MTVRILAVCGNGQGSSMIMKMKVDQFLTQSNIDHTVNSCAVGEYKSELSGADIIIASTHIAGEITVTGNKYVVGVRNMLSPADFGPKLLEVIKEHFPQDVK
|
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.
|
P69823
|
Q1WTU0
|
YBEY_LIGS1
|
Endoribonuclease YbeY
|
Ligilactobacillus
|
MDLEIFDDTNSVPAEKIQLVKDVLEFSGKYLELPEDTEMSVTLMNNEQIHEINLKYRGVDKATDVISFAIEEDDPDELPIILPDDVDFEEPKNIGDMMISMDKVKEQAEYLGHSEDRELGFLTVHGFLHLNGYDHMKAEDEKVMFKLQRDILDAYGLKR
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q1WTU0
|
P86392
|
VMPA1_TITSE
|
Metalloserrulase 1
|
Tityus
|
MISYLASIFLLATVSAVPSGRVEVVFPSVETSRSGVKTVKFTALDQDVELKLRSAGEILGKRFAIQDVDVESLRRKIYRDSVNGAALLIDEDGPLTIEGIVNSKLRIQPFESGRITKDGIIAHQIVEVIDDKKSYDRVAVIPENVKRNAENVSRMARDDDCIVVEYYIVTDSAFTKRFKSNSALTNYVTVMFTGVQNLMDTLELGIGVRLLGVTTFTEKTEPSFIKDNLIPGPPAAFDPDVLISAMSKYYCNHQTGLAKDTDLIFLITARGMGDPREDGTVDINTAGIANSAGVCKPCFKSGIATDDSDYNERVDTLAHESVHLLGSPHDGEGPNLVSLEGSPGAANCPAKAGYIMGNRNDKNKYKFSPCTKKCVEYLLSKPTASCIFQQCTDF
|
Acts as a metalloprotease. Penetrates intact tissue and specifically cleaves the vesicle-associated membrane protein 2 (VAMP2) (part of the SNARE complex) involved in pancreatic secretion, thus disrupting the normal vesicular traffic.
|
P86392
|
Q47AM7
|
TATA_DECAR
|
Sec-independent protein translocase protein TatA
|
Dechloromonas
|
MGSFSIWHWLIVLVIVMLIFGTKKLRNVGQDLGGAVKGFKDGMKEANADKPAEEAQPTQQVGGHTIDVEVKEKTKS
|
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.
|
Q47AM7
|
A6UW21
|
TRPD_META3
|
Anthranilate phosphoribosyltransferase
|
Methanococcus
|
MLNKIINREDLSYEESYDLFNDLLNESEIKIGAYLSALQTKGFTANEIAGFAKAMRDNAIAIDLGKGISDTCGTGGDGYSTINISTAVSIILSCFTKVAKHGNVSITSKSGSANVLDALNIKKDCNPEEAKKMIDKTNFVFLFAPNYHPALKKIMPVRKELGIKTIFNILGPLANPANPDYQIMGVNSLDLVEKVGDALKLLGVKKALVVYGNGLDELNPNDYSTICEINENEENKIYKIHPKDIGLTPSNPIPCNSPDESAKRIIKIFSGTINEDRDFILLNAAAALYASNIAKDYKEGLKLAKEVIDNGTVLKKLKEIQKYGE
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
A6UW21
|
Q4FNF0
|
YIDD_PELUB
|
Putative membrane protein insertion efficiency factor
|
Candidatus Pelagibacter
|
MNIISNILIGLIKFYKMVISPYLTPSCRYLPTCSEYTIECLRTYGLVKAISKSTKRIFSCHPIKILGGGEGFDPVNKEFKAKK
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q4FNF0
|
A6SY03
|
TPIS_JANMA
|
Triose-phosphate isomerase
|
Janthinobacterium
|
MRRKLVAGNWKMNGSLAANTLLLTEIKSGLGNATSDVAVCVPSPYFAQCQGLLNGAAIALGAQDVSSHEAGAYTGEVSTSMLQEFDCRYVIVGHSERRAYFAETNELIAQKTVRALNAGLTPIVCVGETLDQREAGQTDSVVAEQLNVVLASIAASDLAKIVVAYEPVWAIGTGKTATPAMAQEVHAMLRKQLQAKNAEAAMQVRILYGGSMKPENAKELLAMSDIDGGLIGGAALKAADFLAIVHAA
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
A6SY03
|
Q5Z355
|
Y294_NOCFA
|
Nucleoid-associated protein NFA_2940
|
Nocardia
|
MQPGGQFDMQQLLAQAQQMQEAVMQAQAEIAATEVEGQAGGGLVKATIKATGEVQALTIDPKVVDPEDVEGLQDLVIGAINDAMARAQQLAAERLGPLAGGGSMPGLPGF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q5Z355
|
Q8RX78
|
UBN1_ARATH
|
Ubiquitously expressed nuclear protein 1
|
Arabidopsis
|
MSEVNEMSGGSIGGELLRASPKVLTAGDRKLLKVELRPGDTTYVSWKKLMRDAGKVNGLSASVPDPPPNANPNLEFRIAPGHPVEIETNEQPHSNRFNAVIEKIERLYKGNDSSDGEELDGAPDDDEYDTEDSFIDDAELDEYFEVDNSTVKHDGFYVNRGKLERMEPSTTSNQQPKKRRRKDSAKPCRDAVDVSDKHTKLSITARKKDQSTAPGSWKTQESPLPSGAQDANTSVPLDDVKHSDRANHQSRNDTSHKSRETGSSSALHQKYSNKSLHQQSTSLLGKSPPNVFAEVTVVRQKENNGMHQLANVTGSRQSSQASKKDGSNVKSKTSILEKAIRELEKVVVESRPPAITENQEADTSSQAVKRRLPRDVKLKLAKVARIAQASQGKHSTELINRLMSIVGHLIQLRSLKRNLKIMIDMGDSATREKDTRFKQINNEVLDMIKAKVSLMESQAIKPEGATSDDFQDSVEKPSLKKFVMDAALEDKLCDLYDIFIDGLDEDQGPQTKKLYVNLAELWPNRLMDYRGIKHAIFRAKERRKALYGNLAKEMDQTKMKKSMKQLVPRTDCTAQPNTELVVQRQHSGEKKLIVDPNATSTSVVTSQTMVDRSNQQQPEKLKGISSSCNPTEETRVVKRKNEAVMAEKQVVLALKKPEHPQTRVIPAPQNLNIPRTTPDLNLPS
|
May be required for replication-independent chromatin assembly.
|
Q8RX78
|
B4SUI9
|
TREA_SALNS
|
Alpha,alpha-trehalose glucohydrolase
|
Salmonella
|
MIPPEIRRSVLLQKAIKLALAGTLLTFASFSATAADPSSDTETPQPPDILLGPLFNDVQNAKLFPDQKTFADAIPNSDPLMILADYRMQRNQSGFDLRHFVDVNFTLPKAGEKYVPPAGQSLREHIDGLWPVLTRSTKNVEKWDSLLPLPESYVVPGGRFREIYYWDSYFTMLGLAESEHWDKVADMVANFGYEIDAWGHIPNGNRTYYLSRSQPPFFAFMVELLAQHEGDDALKEYLPQLQKEYAYWMEGVETLQPGQQNQRVVKLEDGSVLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLSTIRTTTIVPVDLNALLYQLEKTLARASAAAGDRAEASQYDALANARQKAIEMHLWNNKEGWYADYDLKNNKIRDQLTAAALFPLYVNAAAKDRAAKVAAAAQAHLLQPGGLATTSVKSGQQWDAPNGWAPLQWVAAEGLQNYGQDDVAMEVTWRFLTNVQHTYDREKKLVEKYDVSSTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPQEKPCDSVPSTRPASLSATPTKTPSAATQ
|
Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
|
B4SUI9
|
Q8T0W4
|
VKT2_PIMHY
|
Cysteine-rich venom protein 2
|
Pimpla
|
MNAKIVALLIVVGFVGMFNVATAADPLCSLEPAVGLCKASIPRFASVGGKCQEFIYGGCGGNANNFQTQAECEAKCG
|
Serine protease inhibitor.
|
Q8T0W4
|
Q7U330
|
TRUB_HELHP
|
tRNA-uridine isomerase
|
Helicobacter
|
MANALLVAAYKPPFLSSNACLSRLKKHFGMSKAGYLGTLDPFAKGVLVVGFGSYTRLFPHLQKVPKAYRATLWLGAKSASLDIEHIESIEIIPEYNQSDIEKILFSLKGTFDYTPPAFSAKHINGQRAYKLAREGKVFTLQQIQMSIYNITLLSYHHPFVHFEVSVSEGAYVRSIGEIIAKKLGVNGVLSSLERISEGQMSVSATEQIRILNPLEYLPYPQLENMHRFSKQMYDGKKITLKNAQKGKYIVCFEDFFSIIEIFSNGGIQYILNRIEYVDTFKKTR
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q7U330
|
Q7M715
|
TR117_MOUSE
|
Taste receptor type 2 member 117
|
Mus
|
MKHFWKILSVISQSTLSVILIVELVIGIIGNGFMVLVHCMDWVKKKKMSLVNQILTALSISRIFQLCLLFISLVINFSYTDLTTSSRMIQVMYNAWILANHFSIWIATCLTVLYFLKIANFSNSFFLYLKWRVEKVVSVTLLVSLLLLILNILLTNLETDMWTNEYQRNISCSFSSHYYAKCHRQVLRLHIIFLSVPVVLSLSTFLLLIFSLWTHHKRMQQHVQGGRDARTTAHFKALQTVIAFFLLYSIFILSVLIQIWKYELLKKNLFVVFCEVVYIAFPTFHSYILIVGDMKLRQACLPLCIIAAEIQTTLCRNFRSLKYFRLCCIF
|
Putative taste receptor which may play a role in the perception of bitterness.
|
Q7M715
|
Q31HG2
|
TPIS_HYDCU
|
Triose-phosphate isomerase
|
Hydrogenovibrio
|
MRQLFVAGNWKMHGDKASIKTLVTGLNAKADSVGDVLVAVCPPAIYLDYTKNCLMAGEIALGGQNMAIEPVQGAYTGETSASMLKDVGCQYVILGHSERRAIYGETDQDIAAKVKTALDSGLTPILCVGETLEERESGQLESVISQQLDAVISEVGIDQFADVVIAYEPVWAIGTGKTASAQQAQDVHAFIRGQLAKLNPSVAEKVIIQYGGSVKPNNASELFSQPDIDGGLIGGASLNADDFIAICQAAGEQ
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q31HG2
|
C5XNN6
|
THI41_SORBI
|
Thiazole biosynthetic enzyme 1
|
Sorghum
|
MATTAASSLLKSSFAGSRLPSATRAPSSVVVSTGGAPRTAAISASISSSNPPYDLTSFKFSPIKESIVSREMTRRYMTDMITHADTDVVIVGAGSAGLSCAYELSKDPTVRVAIVEQSVSPGGGAWLGGQLFSAMVVRKPAHLFLDELGVAYDEAADDYVVVKHAALFTSTVMSAVLARPNVKLFNAVAVEDLIVKGGRVGGVVTNWALVSMNHDTQSCMDPNVMEAKVVVSSCGHDGPFGATGVKRLQDIGMIAAVPGMKALDMNAAEDAIVRLTREVVPGMIVTGMEVAEIDGAPRMGPTFGAMMISGQKAAHLALKALGRPNAVDGTIPKVSPALREEFVIASKDDEVVDA
|
Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.
|
C5XNN6
|
P38141
|
THI2_YEAST
|
Thiamine biosynthesis regulatory protein
|
Saccharomyces
|
MVNSKRQQRSKKVASSSKVPPTKGRTFTGCWACRFKKRRCDENRPICSLCAKHGDNCSYDIRLMWLEENIYKVRKHSLISSLQARKSKSKPLCQKISKSRFKQMTHFRQLSPPTSDCEDSVHEASKETTLPNDNTFTISVRRLKIYNNAVASVFGSMTNRDYTQKRIDKKLDELLNMVENDISVVNLNCSKHGPYSVFRANPAAVTSALTDQLPSPGHSMSSAEETTTAALSSPPEDSTSLIDIIQGKIFGILWFNCYGNMILNRQEYTTWFINKMRNSLTTEFIRFLGKIIDDPDINMASCLFKECIARWSCVDWQSIAITMLVIIHGYTCPNLTKLLRVWFLQQKLLRFSMYPLVNFIINNTQDLDVLYHCNGLLGNADLFEDPYQDELTSELHVLVTERLVNSWKDTILQQLCSCQDTTLSCSQLRYWQLQLKCNQQFYKDVYAMQD
|
Positive regulator of thiamine biosynthesis.
|
P38141
|
C1AE25
|
THIM_GEMAT
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Gemmatimonas
|
MDAPSSASGPTQPRLSPADALAALRASAPLTQCITNYVAMQIAANTLLAAGAAPAMIHTVEESGAFAGLARAVTINIGTLSPAWVDGMKAAIDGATAVGTPWVLDPVAHYASAYRSAVARDLLSRRPTILRGNASEILALAGGNTAARGVDAADPVTAAGAAASALAREYGSVVAVTGAVDLVTDGTRVAMVSGGSPWMPQVTALGCSLTCLMGAFAAVTAPLEATVAALTLFAEAGARAHAHSEGPGSFAWRFLDALAAVTPDDLTGTERVSWNAP
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
C1AE25
|
Q9ABM9
|
TRMD_CAUVC
|
tRNA [GM37] methyltransferase
|
Caulobacter
|
MPFTATVLTMFPEAFPGPLGVSMIGTAWKEQDLWRLETLDIRAFSKDKRGFLDDTPAGGGAGAVLKADVIASALDSLERDGRPLLYMSARGRPLTQARVREWSKAPGIVVLCGRFEGVDQRVLDARGFEEVSVGDAVLAGGEAAAMVVIEACVRLAPGVLGNIESTLEESFEDGLLEHPQYTRPRTFEELDIPEVLLSGDHKKIDQWRKRMREETTRERRPDLWEAHLANQQAKGDPKPGKPKET
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q9ABM9
|
P31831
|
TACY_LISIV
|
Thiol-activated cytolysin
|
Listeria
|
MKKIMLLLMTLLLVSLPLAQEAQADASVYSYQGIISHMAPPASPPAKPKTPVEKKNAAQIDQYIQGLDYDKNNILVYDGEAVKNVPPKAGYKEGNQYIVVEKKKKSINQNNADIQVINSLASLTYPGALVKANSELVENQPDVLPVKRDSVTLSIDLPGMVNHDNEIVVQNATKSNINDGVNTLVDRWNNKYSEEYPNISAKIDYDQEMAYSESQLVAKFGAAFKAVNNSLNVNFGAISEGKVQEEVINFKQIYYTVNVNEPTSPSRFFGKSVTKENLQALGVNAENPPAYISSVAYGRDIFVKLSTSSHSTRVKAAFDTAFKGKSVKGDTELENIIQNASFKAVIYGGSAKDEVEIIDGDLSKLRDILKQGANFDKKNPGVPIAYTTNFLKDNQLAVVKNNSEYIETTSKAYSDGKINLDHSGAYVARFNVTWDEVSYDANGNEVVEHKKWSENDKDKLAHFTTSIYLPGNARNINIHAKECTGLAWEWWRTVVDDRNLPLVKNRNVCIWGTTLYPAYSDTVDNPIK
|
A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host 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.
|
P31831
|
Q66I85
|
YJU2B_DANRE
|
Coiled-coil domain-containing protein 130
|
Danio
|
MGERKGVNKWYPPDFDPAKHGSINGYYKTHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPATCDYVIVSGAQRKEERWDMAENEQILTTERNEKEKLETDAMYKLDHGGKDKEKLRAAIPSLNELQEHQSGWKDDFQLNSALRRKFRTEKKVIAEEEEKDNAVRLRTGLSIPLVPEREEDKKLASLLTFQSPDSYEDKKQWKRQEISSRSWFNSPSSAAGGAAGSLLQKLGQQGRGAAVAKALSSSTSTLPILVRRKSESSKSETNNTMSTILPVDTHPAAKDTDATDLPSIVNNINVSINTDINSCTTDACKASSSSEEENSIDSCATGKSLVADYSDSDSGSEV
|
May be involved in mRNA splicing.
|
Q66I85
|
P59427
|
TYSY_BUCBP
|
Thymidylate synthase
|
Buchnera
|
MKSYLVLLKKILKEGSNRKDRTGIGTLSVFGYHMEFNLKLGFPLITTKKCHFPAIVHELLWFLKGDTNIKYLNDHNISIWNPWADERGYLGPIYGEQWRSWKTKDGRVIDQIDNVIHLIKNNPNSRRIVVSSWNVGDLHKMALLPCHVLFQFHVVDHVLHCQLYQRSCDVFLGLPFNIASYSLLTHMIAQQCNLKVGNFIWTGGDVHLYKNHIKQAKKQILRRPYLLPKLVINRKPTQIFNYLLQDFNLLNYKYHPSIHAKIAI
|
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.
|
P59427
|
Q2YX99
|
TMCAL_STAAB
|
tRNA(Met) cytidine acetate ligase
|
Staphylococcus
|
MKSVGLITEYNPFHNGHQYHINQSKKLTNADVTIAIMSGNFVMRGEPAIYNKFTRAKMALSTADLVIELPATASLSSGDHFAELAVKVADYMSVDTIAFGSENNDIKTLKQLAHSINEIEQSESFSQKVKEGKSYPRIISELLEHHEALASPNNILGISYLKAIAKHAKNINAISIKRENAQHHDSLIQHHQFASGTSIRTSIISQDDHWHHVVPKDIQHLYVTPHITLNQIFPYLKYQIIAMTTESLKNIYTVNEGFENRLKSTINEATDFHHFVKSLKTKRYTYTHIQRLLMNVLLNIKPTDVTRNIRAVKVLAMNDRGRQYLKHLKTAFPERQYITNINKSNAHYFTNEIKATHIYNAISGQQQTDFNTPVIQQYR
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
|
Q2YX99
|
Q4R963
|
TCPG_MACFA
|
CCT-gamma
|
Macaca
|
MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGGGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDINDSDMMLNIINSSITTKAISRWSSLACNIALDAVKTVQFEENGRKEIDIKKYAKVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITECKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDVKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQSRQGGAPDAGQE
|
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
|
Q4R963
|
Q886N9
|
UPPS_PSESM
|
Undecaprenyl pyrophosphate synthase
|
Pseudomonas
|
MEKIKSAGPSSVPRHVAIIMDGNNRWARKRLLPGVAGHKAGVDAVRAVIEVCAEAKVEVLTLFAFSSENWQRPAEEVGALMELFFTALRRETKRLNENDISLRIIGDRSRFHPELQAAMREAEVRTSGNSRFVLQIAANYGGQWDIAQAAQRLAREVQAGHLQPEDITPQLLQTCLATGDLPLPDLCIRTGGEHRISNFLLWQLAYAELYFSDLFWPDFKHDAMRAALADFASRQRRFGKTSEQVEAGARA
|
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.
|
Q886N9
|
Q27GK7
|
TPR4_ARATH
|
WUS-interacting protein 2
|
Arabidopsis
|
MSSLSRELVFLILQFLDEEKFKDTVHRLEKESGFFFNMRYFEDSVTAGEWDDVEKYLSGFTKVDDNRYSMKIFFEIRKQKYLEALDKKDHAKAVDILVKELKVFSTFNEELFKEITMLLTLTNFRENEQLSKYGDTKSARGIMLGELKKLIEANPLFRDKLQFPSLKNSRLRTLINQSLNWQHQLCKNPRPNPDIKTLFVDHTCGHPNGAHTPSPTTNHLMGSVPKVGGFPPLGAHGPFQPTPAPLTTSLAGWMPNPSVQHPTVSAGPIGLGAPNSAVSMLKRERPRSPPTNSLSMDYQTADSESVLKRPRPFGISDGVNNLPVNVLPVTYPGQSHAHATYSTDDLPKNVSRILSQGSAIKSMDFHPVQQTMLLVGTNLGDIAIWEVGSREKLVSRSFKVWDLATCTVNLQASLASEYTAAVNRVVWSPDGGLLGVAYSKHIVHIYSYHGGEDLRNHLEIDAHAGNVNDLAFSQPNQQLCVVTCGEDKTIKVWDAVTGNKLHTFEGHEAPVYSVCPHQKENIQFIFSTAVDGKIKAWLYDNMGSRVDYDAPGRSCTSMAYCADGTRLFSCGTSKEGESFIVEWNESEGAVKRTYLGLGKRSVGVVQFDTMKNKFLVAGDEFQVKFWDMDSVDLLSSTAAEGGLPSSPCLRINKEGTLLAVSTTDNGIKILANAEGSRILHSMANRGLDSSRAPPGSVAKGPIVGTFGTPNSSTGMSLSMGERSGPVASVTGLNGDNRSLPDVKPRIADDAEKSKTWKLTEISERSQLRTLRLPDTLLPARVVKLIYTNSGGAILALAENAAHKLWKWQKSERNLLGKANSNVPPQLWQPSSGVLMTNDTREGNKEDVVPCFALSKNDSYVMSASGGKISLFNMMTFKTMTTFMAPPPAATSLAFHPQDNNIIAIGMDDSSIQIYNVRVDEVKSKLKGHQKRVTGLAFSNVLNVLVSSGADSQLCVWSMDGWEKQASKQIQIPSGHSPNPLAHTRVQFHQDQIHVLVVHASQLAIYEAPKLENMKQWIPKESSGSVTDAVYSCDSQSIYAAFDDGSVSILTATTLQLKCRIGPNSYLPSNPSSRVYPATVAAHPSEPNQFAVGLTDGGVHVIEPPGPEGKWGISAPPENGAGPSVSSAPGSDQQPR
|
Transcription corepressor of Zinc finger transcription factors GAF1/IDD2 and ENY/IDD1 in regulation of gibberellin homeostasis and signaling.
|
Q27GK7
|
Q9XFG3
|
TBG_PHYPA
|
Gamma-tubulin
|
Physcomitrium
|
MPREIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINSIQNSEYRNLYNHENVFVADHGGGAGNNWASGYHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNQMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHIPNPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLVASLIPTPRCHFLMTGYTPLTVERQANAIRKTTVLDVMRRLLQAKNIMVSSYARTKEASQAKYISILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPYVQTAHRVSGLMLASHTSIRHLFSKCISQYEKLRKKQAFLDNYRKFPMFADNDLSEFDESREIVQNLVDEYKACESADYIKWGMEDRGKQVSGEGNTSGTVDSRVGAS
|
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
|
Q9XFG3
|
Q5JDJ1
|
TRPB2_THEKO
|
Tryptophan synthase beta chain 2
|
Thermococcus
|
MKAVLPDSKIPKRWYNILPDLPEPLAPPLDPETDEPMEPEKLLRIFAEELVKQEMSTDRYIEIPKEVREIYSKIGRPTPLFRATNLERALGTPARIYFKYEGATVTGSHKINTALAQAYYAKRQGIERLVTETGAGQWGTALSLAGALLGLNVRVYMARASYQQKPYRKTIMRLYGAEIYPSPSDRTEIGRKFLAEDPNHPGGLGIAISEAIEDVLRDEKARYALGSVLNHVLMHQTVIGLEAQEQMKEFEEPDVIIGCVGGGSNFAGLAYPFVRDVLKGEAEYEFIAVEPKAAPSMTRGVYKYDYGDSGGYTPKMKMHTLGHTYYVPPIHAGGLRYHGLAPTLSVLINHGIVKPVAYHQNEVFQAAHLFAKTEGIVPAPESAHAIKGAIDRALEAKREGREEVILFNLSGHGFLDLKGYEDYLDGKLEDYEPEHFPALDNY
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
Q5JDJ1
|
E1QU22
|
TSR3_VULDI
|
20S S rRNA accumulation protein 3 homolog
|
Vulcanisaeta
|
MIPRVFIYRLPQDDPRKNTAIKLVRFGFAQLVDSIKALPSGSIILDPTVKTPLTPSDRVIAESRGLSLIDCSWKRAVDVHTKFIRGKFIRRRLPLLIAANPTHYGKPYILSTIEAVAAALYIMGFKDEAMEVLRLYKWGPNFIIINQKYLERYAAGDLSPERELLGVDDVDNGLEQLMRVLTNGD
|
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
|
E1QU22
|
Q00835
|
TRI5_FUSPO
|
Sesquiterpene cyclase
|
Fusarium
|
MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPYAAMMNYFNDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQFDERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVSDEISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMVTIECFMHGYVTWHLCDHRYRLNEISEKVKEQKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQLANVRSKDVKNVKQIEKPLLSSIELVE
|
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.
|
Q00835
|
B9M7R9
|
YIDC_GEODF
|
Membrane protein YidC
|
Geotalea
|
MEKRVVIAVILSIVVLYAFSYMFPPPVANQKEKAGPVAAVQSQPSSAKLSAIDSVPAAATPQAGLAARNIVVDTDLFIAVFSTKGGGLQSFQLKHYKDKAGAVGRDIVLKNESDGDKLSLLSEGKSFGLEPSLVFQSSAKDTKLAGTEKSSIEFTVTSQTGVILKKVYSFSGNGYGINLHQELINTGSSRVEGAISLINYNRLVAETGDGRYEVYGPVTMAGDKVITDKVSDIAKGPKQFDNNVSWSAFADKYFMDAVIAVKNSIASARVAKISDNYVQTNVTSSPLSLNPGQSASMDYRLFYGPKDLDILKAQGSRLEEAIDFGWFSALAKPLLRSIKFFYSYTHNYGLAIIIITIILKVLFFPLTHKSYKSMKEMQKLQPKMVELKEKFKNDRDAMNRAVMDLYKTHKVNPMGGCLPMLVQIPVFFALYKALMFSIELRHAPFVLWITDLSAKDPYYVTPIIMGVTMFIQQKMTPTNMDPIQAKMMLALPVVFTFMFLNFPAGLVLYWLINNILTIAQQAYINKSLPA
|
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.
|
B9M7R9
|
Q0WQK2
|
ZDHC9_ARATH
|
Zinc finger DHHC domain-containing protein At3g26935
|
Arabidopsis
|
MYVVPPPQRSDSGSNGDLRVYQTWKGSNIFFLQGRFVFGPDVRSLALTICLIAVPVTIFCIFVARKLIDDFSDSWGVSIVAVAVVFTIYDLILLLLTSGRDPGIIPRNAHPPEPETLDGNMDAGAGQTPQLRLPRIKEVQLNGITFKVKYCDTCMLYRPPRCSHCSICNNCVERFDHHCPWVGQCIGMRNYRFFFMFVFSTTLLCIYVFAFCWVYIRKIMESEHTTTWKAMLKTPASIVLIIYTFISMWFVGGLTVFHLYLISTNQTTYENFRYRYDRRSNPHNKGVVNNFKETFFSTIPPSKNDFRAMVQREPPLPPRSVAGGFMSPNMGKANDEIEMGRKAVWADMGPAMSDHGDGKHGNNERLHVKDGELGELSPDIRATVDEQSDRPSMHPRRSSWGRKSGSWDMSPEVMALAARVGEQNQNGGGSSSGSGLVTENRPT
|
Palmitoyl acyltransferase.
|
Q0WQK2
|
Q39IR6
|
UBID_BURL3
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Burkholderia cepacia complex
|
MKYKDLRDFIQRLEALGELRRVTQPVSPVLEMTELCDRVLRAGGPALLFNAPTGYDFPVLGNLFGTPRRVALGMGVDAGDDAALDSLRDLGRLLSALKEPDPPKSLKDAGKLLSLAKAVWDMAPKSVSSPPCQEIVWEGADVDLNRLPIQTCWPGDAGPLVTWGLTVTRGPNKSRQNLGIYRQQLIGRNKLIMRWLAHRGGALDFREFALQNPGKPYPVAVVLGADPATTLGAVTPVPDSLSEYQFAGLLRGSRTELAKCLTPGVDTLQVPARAEIVLEGFIYPQEGAPAPAPAGAPPRPAGNASAKYEHALEGPYGDHTGYYNEQEWFPVFTVERITMRRDAIYHSTYTGKPPDEPAVLGVALNEVFVPLLQKQFTEITDFYLPPEGCSYRMAIVQMKKSYAGHAKRVMFGVWSFLRQFMYTKFIVVVDEDVNIRDWKEVIWAITTRVDPVRDTVMVDSTPIDYLDFASPVAGLGSKMGLDATNKWPGETNREWGRPIEMDAAVKARVDRLWQEIGL
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
Q39IR6
|
Q8KGF8
|
TAL_CHLTE
|
Probable transaldolase
|
Chlorobaculum
|
MKFFIDTASLDEIKAANELGVLDGVTTNPSLIAKIVKDSTNFTYADFKAHIAKICEIVDGPVSAEVTTLKAGEMIAQGEELAAIHKNIVVKCPLTVDGLKAIKHFSSNGIKTNATLVFSPTQALLAAKAGADFVSPFVGRLDDISTSGMELVRQIVTIYDNYGYLTEVIVASVRNPLHVVESAMVGADIATIPYSVIKQLANHPLTDKGLEKFMEDAAVMKP
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q8KGF8
|
Q0A5V9
|
UBIA_ALKEH
|
4-HB polyprenyltransferase
|
Alkalilimnicola
|
MEMTADYLRDRAWQYAQLTRLNRPIGNFLLLWPMLWGLWIAAKGLPDLKVLVVFVLGVLIMRAAGCVINDYADRDFDGHVKRTTHRPMANGRVSEREALTLFVVLCLVAFGLVLLMNPLTIALSLVAVALAATYPFMKRYTHFPQVHLGAAFGWAIPMAFAAQTGAVAPVAWLLFLSAVLWATIYDTQYAMVDRDDDLKIGVKSTAVLFGQADRAIIGVLQGVMLAVLVAAGLVVGLGAFWYLGLAAAAALFAYQQWLIRERRREDCFRAFLNNNWLGGLIFLGLLLDLHLGG
|
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.
|
Q0A5V9
|
B4U3P4
|
UVRB_STREM
|
Excinuclease ABC subunit B
|
Streptococcus
|
MIDKRDFKAFKLVSKYAPSGDQPQAIEALVDNIESGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRPGQEISRDQLLNALVDIQFERNDIDFQRGRFRVRGDVVEVFPASRDEHAFRIEFFGDEIDRIREIESLTGKVLGDADHLVLFPATHFVTNDEHMEQSISKIQAELADQLKLFEAEGKLLEAQRLRQRTEYDIEMLREMGYTNGVENYSRHMDGRSAGEPPYTLLDFFPEDFLIMIDESHMTMGQIKGMYNGDKARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGDYEMEQTDTIVEQIIRPTGLLDPEVEVRPSMGQMDDLLGEINLRVERGERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNADGHVIMYADRMTDSMQRAIDETARRRAIQMAYNEEHGIIPQTIKKDIRDLISISRAVEAKATEAETNYESMTRSERQEAIKQLQKNMQEAAELLDFELAAQLRDLILELKAID
|
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.
|
B4U3P4
|
A1BEF7
|
THIG_CHLPD
|
Thiazole synthase
|
Chlorobium
|
MDFLHLGSFVFSSRLILGTGKFSNADLMIEAIKASGAQLVTVALRRFNREQIADDLFGPLSALQGITLMPNTSGASTAREAIHAAHIARELSGSPFIKVEIHPNPQHLMPDALETWEASRILAKEGFLVMPYIPADPVLAKRLEEVGCASVMPLGSAIGSGQGLANAGMIELIIRESGIPVIVDAGLRAPSEAAAAMEMGCGAVLVNSAVAVAGNPPEMANAFAEAVRAGRRAFKAELMPKSSFALSTSPLTTFLGKKS
|
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.
|
A1BEF7
|
Q03774
|
TRM82_YEAST
|
Transfer RNA methyltransferase 82
|
Saccharomyces
|
MSVIHPLQNLLTSRDGSLVFAIIKNCILSFKYQSPNHWEFAGKWSDDFDKIQESRNTTAKEQQGQSSENENENKKLKSNKGDSIKRTAAKVPSPGLGAPPIYSYIRNLRLTSDESRLIACADSDKSLLVFDVDKTSKNVLKLRKRFCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFTQEPILGHVSMLTDVHLIKDSDGHQFIITSDRDEHIKISHYPQCFIVDKWLFGHKHFVSSICCGKDYLLLSAGGDDKIFAWDWKTGKNLSTFDYNSLIKPYLNDQHLAPPRFQNENNDIIEFAVSKIIKSKNLPFVAFFVEATKCIIILEMSEKQKGDLALKQIITFPYNVISLSAHNDEFQVTLDNKESSGVQKNFAKFIEYNLNENSFVVNNEKSNEFDSAIIQSVQGDSNLVTKKEEIYPLYNVSSLRKHGEHYS
|
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
|
Q03774
|
A1RV13
|
UPP_PYRIL
|
UPRTase
|
Pyrobaculum
|
MPVKIIDHVYAQYLLTQLRNRNTKGIDFRKGLVRLGRIVGYELVRYFPTREVEVETPLGKAVGIEILGLDKVIIVQILRAAMPFVEGLLKAFPQARLGVIAARRKEEGGVVDVEVFYSKIPTVEREDIVIVADPMLATGITMTRAIEEVYRVGQPGRLIVVSVIATPVGIERVLSKYPETEIFVVAIDPTLNDKAFIVPGLGDAGDRAFST
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
A1RV13
|
P37610
|
TAUD_ECOLI
|
Sulfate starvation-induced protein 3
|
Escherichia
|
MSERLSITPLGPYIGAQISGADLTRPLSDNQFEQLYHAVLRHQVVFLRDQAITPQQQRALAQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDVTFIETPPAGAILAAKELPSTGGDTLWTSGIAAYEALSVPFRQLLSGLRAEHDFRKSFPEYKYRKTEEEHQRWREAVAKNPPLLHPVVRTHPVSGKQALFVNEGFTTRIVDVSEKESEALLSFLFAHITKPEFQVRWRWQPNDIAIWDNRVTQHYANADYLPQRRIMHRATILGDKPFYRAG
|
Catalyzes the alpha-ketoglutarate-dependent hydroxylation of taurine yielding sulfite and aminoacetaldehyde after decomposition of an unstable intermediate . Is required for the utilization of taurine (2-aminoethanesulfonate) as an alternative sulfur source for growth in the absence of sulfate . To a lesser extent, pentanesulfonate, 3-(N-morpholino)propanesulfonate and 1,3-dioxo-2-isoindolineethanesulfonate are also desulfonated by this enzyme in vitro; however, desulfonation by TauD of organosulfonates other than taurine seem to be of little or no importance for sulfur metabolism in vivo .
|
P37610
|
B2RXF5
|
ZBT42_HUMAN
|
Zinc finger and BTB domain-containing protein 42
|
Homo
|
MEFPEHGGRLLGRLRQQRELGFLCDCTVLVGDARFPAHRAVLAACSVYFHLFYRDRPAGSRDTVRLNGDIVTAPAFGRLLDFMYEGRLDLRSLPVEDVLAAASYLHMYDIVKVCKGRLQEKDRSLDPGNPAPGAEPAQPPCPWPVWTADLCPAARKAKLPPFGVKAALPPRASGPPPCQVPEESDQALDLSLKSGPRQERVHPPCVLQTPLCSQRQPGAQPLVKDERDSLSEQEESSSSRSPHSPPKPPPVPAAKGLVVGLQPLPLSGEGSRELELGAGRLASEDELGPGGPLCICPLCSKLFPSSHVLQLHLSAHFRERDSTRARLSPDGVAPTCPLCGKTFSCTYTLKRHERTHSGEKPYTCVQCGKSFQYSHNLSRHTVVHTREKPHACRWCERRFTQSGDLYRHVRKFHCGLVKSLLV
|
Transcriptional repressor. Specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes.
|
B2RXF5
|
Q084N8
|
TRPB_SHEFN
|
Tryptophan synthase beta chain
|
Shewanella
|
MTELKLNPYFGEYGGMYVPQILVPALKQLETAFVEAQQDESFIAEFTDLLKNYAGRPTALTLTRNLSPNPLVKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLGLKCKVYMGAKDIERQSPNVFRMKLMGAEVIPVTSGSSTLKDACNEAMRDWSASYDKAHYLLGTAAGPHPFPTIVREFQRMIGEETKKQILEKEGRLPDAVIACVGGGSNAIGMFADFIDEPSVELIGVEPAGKGIDTPMHGAPLKHGKTGIFFGMKSPLMQNSDGQIEESYSVSAGLDFPSVGPQHAHLNAIGRARYESATDDEALEMFQTLARCEGIIPALESAHALAYAVRMAKEATKETILVVNLSGRGDKDIFTVADILEAKQKQQESGNE
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
Q084N8
|
Q4L882
|
TRUA_STAHJ
|
tRNA-uridine isomerase I
|
Staphylococcus
|
MRILVNISYQGSQFLGFQIQQQGRTVQQQFEKILKRMHRRHVRIHPSSRTDRGVHAYEQFFHFDTDLNIEPKQWKYAMNSALPDDIYVKEVQQVDDHFHCRYDCLGKRYRYKVYQATHRNPFESGLKTFIKEDLNYSKMNEAAKHFIGTHDFTGFCSQKTEVESKVRTLYQSEIIQTDEGFDYVVTGSGFLYNMVRVLVAFLIEVGKGKRHASEVSTLLNEKNRDSVPFTAPAEGLYLEKIYLTEKDLTTDFGDNIKIHRKKSLQND
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q4L882
|
Q2VY69
|
ZN284_HUMAN
|
Zinc finger protein 284
|
Homo
|
MTMFKEAVTFKDVAVVFTEEELGLLDVSQRKLYRDVMLENFRNLLSVGHQLSHRDTFHFQREEKFWIMETATQREGNSGGKIQTELESVPETGPHEEWSCQQIWEQTASELTRPQDSISSSQFSTQGDVPSQVDAGLSIIHIGETPSEHGKCKKFFSDVSILDLHQQLHSGKISHTCNEYRKRFCYSSALCLHQKVHMGEKRYKCDVCSKAFSQNSQLQTHQRIHTGEKPFKCEQCGKSFSRRSGMYVHCKLHTGEKPHICEECGKAFIHNSQLREHQRIHTGEKPFKCYICGKSFHSRSNLNRHSMVHMQEKSFRCDTCSNSFGQRSALNSHCMDHTKEKLYKCEECGRSFTCRQDLCKHQMDHTGDKPYNCNVCGKGFRWSSCLSRHQRVHNGETTFKCDGCGKRFYMNSQGHSHQRAYREEELYKCQKCGKGYISKFNLDLHQRVHTGERPYNCKECGKSFRWASGILRHKRLHTGEKPFKCEECGKRFTENSKLRFHQRIHTGEKPYKCEECGKGFRWASTHLTHQRLHSREKLFQCEDCGKSSEHSSCLQDQQSDHSGEKTSKCEDCGKRYERRLNLDMILSLFLNDI
|
May be involved in transcriptional regulation.
|
Q2VY69
|
B4RWG2
|
Y3196_ALTMD
|
Nucleotide-binding protein MADE_1004170
|
Alteromonas
|
MKLIIISGRSGSGKSVALRALEDLGYYCVDNIPVNLLPTLTHTVVDEYDQVAVSIDVRNLPKNPDDLVEILDYLPSSWSMTIVYIDASDDVLVKRFSETRRLHPLAKLNKSLSEAIRAESALLAPIAERADLYLDTDKLTIHQLAELIRERILGKKSSRLVLVFESFGFKHGIPKDADYVFDARFLPNPHWEPDLKHLTGLDAPVEVFLGSQPVVTKFIWQIQNLITTWLPHLERNNRSYVTVAIGCTGGQHRSVYIAQTLSKTFSEIHPDVQIRHRELNQ
|
Displays ATPase and GTPase activities.
|
B4RWG2
|
B5GW45
|
TMUUS_STRCL
|
Type I terpene synthase
|
Streptomyces
|
MSLNHSDLMFYCPVDDLPHPAASGVNDRTLDWASGQGIPTADRDAGRLRAMAPGLLAARIAPDARGPVLDAFADHHTWLFAFDDEYCDRADGSGITEWASFLARLHRVVETGESALLPGNPYGLALRDIACRLSTYTTPAQLAEWLEALRSYFAALVWERSRRRDDDRLQSLDDYLLLRLRNGAMHTSITLLDTVNGYVLPRELRETPGVRALVEMTALLVSVDNDILSHHKESTSGTREANLLDVLGRTGHTTPGEAVAQAVALRNEIMRQFVRVAERVRTPAAVPELYRFTTGLARWIRANLDFSLTTTRYTGPVTERAALSPHEVPPLSGQGPAPARSDVIGWWWRIPEPLPEPGSDGADTPVRKRRAGDRPPTAGRGGAPHHQRTGPPPPVLPGGITASRSSGLQQSTWRREHR
|
Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (+)-T-muurolol via a 1,10-cyclization, which requires isomerization of FPP to nerolidyl diphosphate (NPP) and then abstraction of the pyrophosphate from intermediate NPP leading to a (E,Z)-germacradienyl (helminthogermacradienyl) cation.
|
B5GW45
|
B7LJY3
|
UVRB_ESCF3
|
Excinuclease ABC subunit B
|
Escherichia
|
MSKPFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKAMLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTVGMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQIVSTIPRFTIYPKTHYVTPRERIVQAMEEIKEELAARRKVLLENNKLLEEQRLTQRTQFDLEMMNELGYCSGIENYSRFLSGRGPGEPPPTLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEKSGGDVVDQVVRPTGLLDPIIEVRPVATQVDDLLSEIRQRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKAILYGDKITPSMAKAIGETERRREKQQKYNEEHGITPQGLNKKVVDILALGQNIAKTKAKGRGKSRPIVEPDNVPMDMSPKALQQKIHELEGLMMQHAQNLEFEEAAQIRDQLHQLRELFIAAS
|
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.
|
B7LJY3
|
Q8E7Q5
|
TRUA_STRA3
|
tRNA-uridine isomerase I
|
Streptococcus
|
MTRYKAQISYDGSAFSGFQRQPNCRTVQEEIERTLKRLNSGNDVIIHGAGRTDAGVHAYGQVIHFDLPQARDVEKLRFGLDTQCPDDIDIVKVEQVSDDFHCRYDKHIKTYEFLVDIGRPKNPMMRNYATHYPYPVIIELMQEAIKDLVGTHDFTGFTASGTSVENKVRTIFDAKIQFEASKNLLIFTFTGNGFLYKQVRNMVGTLLKIGNGRMPISQIKTILQAKNRDLAGPTAAGNGLYLKEIIYEDKECFSNFRK
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q8E7Q5
|
P77288
|
YFCV_ECOLI
|
Uncharacterized fimbrial-like protein YfcV
|
Escherichia
|
MSKFVKTAIAAAMVMGAFTSTATIAAGNNGTARFYGTIEDSVCSIVPDDHKLEVDMGDIGAEKLKNNGTTTPKNFQIRLQDCVFDTQETMTTTFTGTVSSANSGNYYTIFNTDTGAAFNNVSLAIGDSLGTSYKSGMGIDQKIVKDTATNKGKAKQTLNFKAWLVGAADAPDLGNFEANTTFQITYL
|
Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes.
|
P77288
|
Q11IP4
|
XGPT_CHESB
|
Xanthine phosphoribosyltransferase
|
unclassified Chelativorans
|
MSLPEKAFPVSWDQFHRDARALAWRLAGTNGRWQAIVCITRGGLVPAAVIARELGIRLIETVCIASYHDYSEQGELKVLKEISPSLLEEDGQNILIVDDLTDTGKTAAIVRAMMPKAHFATVYAKPKGRPLVDTFVTEVSQDTWIYFPWDLGFSYQKPIADGEIG
|
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
|
Q11IP4
|
A7FMH4
|
TYPH_YERP3
|
TdRPase
|
Yersinia
|
MFLAQEIIRKKRDGQPLSEEEIRFFINGIRDNVVSEGQIAALAMTIYFHDMSMPERVALTMAMRDSGTVLNWKSLNLNGPLVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGFDIFPDDNAFRKIIQNVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYSLSADLAQAIVGVANGAGCKTTALLTDMNQVLASSAGNGVEVREAVRFLTGEYRNPRLLEVTMALCVEMLLSGGLAHDEADARAKLQAVLDNGKAAEVFGRMVAAQKGPVDFVERYDSYLPVATLSKPVFAEQTGIITAMDTRALGMAVVALGGGRRRATDPIDYSVGLTEMARLGTRVDGQQPLAVIHANNEDDWQQAAEAVRAAITLGNNAPEETPVIYRRITE
|
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.
|
A7FMH4
|
P44560
|
TATC_HAEIN
|
Sec-independent protein translocase protein TatC
|
Haemophilus
|
MSNVDESQPLITHLVELRNRLLRCVICVVLVFVALVYFSNDIYHFVAAPLTAVMPKGATMIATNIQTPFFTPIKLTAIVAIFISVPYLLYQIWAFIAPALYQHEKRMIYPLLFSSTILFYCGVAFAYYIVFPLVFSFFTQTAPEGVTIATDISSYLDFALALFLAFGVCFEVPIAIILLCWTGITTVKALSEKRPYIIVAAFFIGMLLTPPDVFSQTLLAIPMCLLFELGLLVARFYQPKDDESAVKNNDESEKTQ
|
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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
|
P44560
|
O82827
|
UPPS_MICLU
|
Undecaprenyl pyrophosphate synthase
|
Micrococcus
|
MFPIKKRKAIKNNNINAAQIPKHIAIIMDGNGRWAKQKKMPRIKGHYEGMQTVKKITRYASDLGVKYLTLYAFSTENWSRPKDEVNYLMKLPGDFLNTFLPELIEKNVKVETIGFIDDLPDHTKKAVLEAKEKTKHNTGLTLVFALNYGGRKEIISAVQLIAERYKSGEISLDEISETHFNEYLFTANMPDPELLIRTSGEERLSNFLIWQCSYSEFVFIDEFWPDFNEESLAQCISIYQNRHRRFGGL
|
Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate. UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
|
O82827
|
P48970
|
UNIV_STRPU
|
Univin
|
Strongylocentrotus
|
MDVSKVLILTLIWLLTADSAPPDYVTLTRKMESKILRVMGLSERPRPKPNATAPQYMWDLYRQQMAATEGAAASRGGETEIGKEEEEDGRPCSETKLSSNIIRSVSHTGGDLRASNSTSLQQILLFDVASIPHAETIEAADLRLEIPALPSATDVPSLAVRIYQLESRTRLNSIVSLKDKRLRLLDVVLADLSQGYAGTIDILSTVNSWRSKKTSNHGLLLHVELMSTSGNNRRGSQVIKELGAISKKCTANLIVTSSEYRQCSKRNRRNKRQAESEAPADISSFPTASLTNLCQRHRLFVSFRDVGWENWIIAPMGYQAYYCDGECPFPLGERLNGTNHAIIQTLVNSIDNRAVPKVCCAPTKLSGISMLYFDNNENVVLRQYEDMVVEACGCR
|
Could have a critical role in early developmental decisions in the sea urchin embryo.
|
P48970
|
A4YM32
|
UREF_BRASO
|
Urease accessory protein UreF
|
unclassified Bradyrhizobium
|
MTTNDAGRIPSAAGGAELAALYRLLTWLSPAFPIGGFSYSSGLEWAVEAGDICDAAALRGWLATMLTDGSGFCDAAFLVHAHRATELDDIKRLSEVAELAAAFVPSRERQLETAAQGRAFIEIARSAWSCAGLDEAVAQCDVVVYPVAVGMVGALHGVPLEPLLHGFLHALVSNWISAGSRLVPLGQTDSQRVLAALEPVVVATADRSLHASLDDIGSATFRADLASLRHETQYTRLFRS
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
A4YM32
|
Q85FG7
|
TI214_ADICA
|
Translocon at the inner envelope membrane of chloroplasts 214
|
Adiantum
|
MNTKILLSLPWPKLMDPYMLLGFYYGLLTTLPVGPSQILCVRSFLLGGNLSGLISISGSVLAQLITASSIYCSPIYLLLLRPHLLTIVAIPYTLLFCLVIKDFPNYQILRPVTSLRDSRVARLFLISFFFQILNPIMLPNSVLTRLIYLYFFRYSTNTVFMVSTFMGWLTGQAAFNFFSRLLLSRVKGDSPILYLVAKRFIYATFSIVSISYAVAYLGRAPVSFWTKKFMNESHDREMNLWEIAEYSDLLWWFFKPWPTSFFDPSRANRSNRFVKNRRFHMNNTFYKGRTSTYFFEKCLTDGKERLSFLALPSLSIFGKEMYQSMAKSRRSFGIRLSYQNWVSKKLAKTKFFEKELTDQIKLLDTGSSFSKTMSRKTRLMGGKRRRIPRTYDPFVNNFRIRIPVSQTFLLEDDLGLSLWEWDKLATERKNRKAKKTVRINAIKDKIFTKDRRWKHGYGNPLPWEPLPSRSKRMFYFIFENRALYDYDLQNILKKIKSSPTLDVTWKEIMDLDYEDHILFLTYLEVGCCHRFGWISPLKAFLRKSSKSLSNVERRIRRLNKIGNLSMDLARYTILYFENNFDIPGGDGDFRYRKLRNVGITFAKGKPRSERLMKRYAKVSDFRRKFLKGSMRSRRRKTLLWKALQEKIRSSFFLRSAERTILFQSLIERLTTSSREEKFSELEKDTDYEFQKQLLDISLSAKRSLIGESKLTRSAIAARSDIGPIHNGRGYMLVFQSRFRKFIKLPVLIVLKNIGRILLRQNSEWNKDWTGWKKEIHINCTFDGEDFSQDELPPRWLREGIQIKIVYPFQLKPWHTDGNEKQHTLQRKHKEIGSKSRELKSKRKLKQKKHKFTYLTVLGYQTDIPFGTIQKKTSFWKPVRRKLIRICKRSLPRQIKQAYQFIHSRFEKVSKLNSTPSKKLNLISNLRQGGKLLSDYSLDEKSWMKTSSTNYVNEKTKPNCNVISNSERFIAIGGEMSPANVTRKQLVTRDQVEREFLMSIVAVDSKNLLDEKIDDPYSKITSKDLETGDTTSGDINLVNSTKFERKQLVDSEEAGLSLYLLVRELIETFVSVLINLPFTINRIFVHYFTEFLALYTKLAGILDNINEGSNLSTRSKSLQFDLPSQTCIYIDMWNIGMRGSLNLDLLVNDKRSSSNCGVKNRQSGIYVETDGVSNLYQPKMYEKQTPVHYNLIATKFLSPEIRNNHVNDLTMCFDTETGKTDEEFFDEKVARSIENWGFLNKSCKLDEINWNEWLYSLSRYNLPLTAWRNIAPRKWKVCLSELSSIETNTITELKDQVSQNKLHSYYSIYTKKSFLRNKISNFSKLRKHRNLLQNLTDSVQNGDVENLSVQRDIMEQRFHCKSCIQKSSRGGRNRISKFVHFLSSNVESKNNLNLQIDLLSWLDPDIAKTKIFLKKKKKAKQLKNPLLRNHYRYRYVLDISGRFQKVLNQLNDLTLDEREDADYIFRWKFKFETELEKFRNLISLTRMLGDDQDLITLCTNIEVNSDLLNLQFNAKTKRDMFHNLSVVSAHRLRLVFDDQDLLYKIINPLLKFKGRLRGIFRRRLYRNVYNGSYISNLSHILTERNCKQSCLYNIDDLLSPRRRREFRFLYCLLSPKIEYSQYISRIKKIDNAEKKQTLYHLPRPIRIQKIKRFLWPSHRLEEAACTGRSCVGVMTGSRFVTLRIRMYPIPLN
|
Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.
|
Q85FG7
|
B6H3B2
|
VEA_PENRW
|
Velvet complex subunit A
|
Penicillium chrysogenum species complex
|
MANRPSLMPPHNETEHSVSRITREGKQLTYKLSVMQQPERARACGAGAKSSADRRPVDPPPVVELRIFESDPANDTQKTDITFAYNANFFLYATLETARPIAHGRVGGPQSCPVLTGVPVAGVAYLDRPSQAGYFIFPDLSVRHEGRYRLSFHLYEEIKDAKDADKDSTLPLPNQIPLSATSKPGIPQAFLHFRLEVKSVPFTVYSAKKFPGLATSTSLSRIIAEQGCRVRIRRDVRMRRRGDKRDEDYEFGEERAAAYARSSDRFTTPDRYAASMDRPRSNSNGSNIESPYGFVPPDRRPSAPDYGFQCPQPYQRPMPPAPMSHSQTPSYQSHLSFGSTPSHYPAPHMPPTPPPVAPQGIYSPQHAYAQIRHPSNGSEYEGTPIAYPAPQIPVERGGYPKPPMSSYAMDPPKPNSYMDPRMPEPSLYPSTPNVPVSRPQTPNLPAMPPPKPLSNDYANHVVPSVECTSPGGSGGGGYDNVRGKRMVYQTGPTYGKRSHEDTFGLDDRSMQNGMRPDTEPYPAYRDFSGESRAALMAEMGIQLSYKRANGKIVMKAPPSST
|
Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination . The velvet complex acts as a global regulator for secondary metabolite gene expression . Controls the expression of the penicillin gene cluster . Positively controls the expression of the class V chitinase chiB1 . Positively controls the expression of the transcription factor atfA . Required for cell wall integrity and controls hyphal branching .
|
B6H3B2
|
P62017
|
VATD_SULTO
|
V-ATPase subunit D
|
Sulfurisphaera
|
MSSRKILPTKLNLINLRKQIRLTRTIKRLLENKREVLLIYLREYANEYEKLYSEVSQLLKEVYETYLMGVSAEGISTVESYANSVPPSLQVKSDLKVLFGVRIPIVKLDENSIQPQPFGDIEVSPYITKSRDAIAEAFKKILELVEMESAIRSLSTELRKTQRLINAIDSYILPYYTSSAKYIKGVLDDRTREEFVRLKMIRKVLQRRRGENVGNR
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
P62017
|
B0BSW9
|
TORD_ACTPJ
|
Chaperone protein TorD
|
Actinobacillus
|
MAHSQLLSSEERLFCYRWFHSLLAKELSEPQLQALQAGQFASFFAFLAELGFQPQVTDLQNELAKLTAYDSPRLELAADFAQCFLLEGKLSALPYASYYLDERDLSENLAVMDQWLTKFQLKINRLHNEPSDHLCIYLEVLIKLIETEQPVQVQQQFIRQQLLGWLPQWAEKTAQIHSSTAFYQIISNLLLGFLQQDIT
|
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
|
B0BSW9
|
P0DPW9
|
TX41A_SCODE
|
Toxin SSD219
|
Scolopendra
|
MKKTCVVSVFLVLLLLKFHDLSMGEEISPLKKVAPREQIFPCPGFPCPKGYFCDKGSQKCREGTD
|
Voltage-gated potassium channel inhibitor.
|
P0DPW9
|
Q8XAX1
|
YDEP_ECO57
|
Protein YdeP
|
Escherichia
|
MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNASFFAQNTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSVEFLARLGERYGFTPPHVPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQATLPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN
|
Probably involved in acid resistance.
|
Q8XAX1
|
P63315
|
TNNC1_BOVIN
|
Troponin C, slow skeletal and cardiac muscles
|
Bos
|
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLEELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
|
Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
|
P63315
|
B9VJ80
|
UBA5_BOMMO
|
Ubiquitin-like modifier-activating enzyme 5
|
Bombyx
|
MASVDELQKKIKELEAKLAAVEAKGGPMRQKIEVMSSEVVDSNPYSRLMALKRMGIVNNYEQIREKTVAVVGVGGVGSVTAEMLTRCGIGKLILFDYDKVELANMNRLFFQPHQAGLSKVDAAAATLQNINPDVTIDAYNYNITTVDNFQKFCDTISKGSLTGGAVDLVLSCVDNFEARMAINTACNELDQKWFESGVSENAVSGHIQFISPGESACFACAPPLVVATKVDERTLKREGVCAASLPTTMGIVAGFLVQNSLKYLLEFGNVTHYLGYSALTDFFPTMSLQPNPTCDDASCRARQEQRRLQPRVELAAEVTEDCGPVHQDNDWGISVLEENSPADEDCPGLKLVDGVQVAYSIPVDSSTPESSTGGAVAASELSLEDLMQQMKTM
|
E1-like enzyme which activates UFM1.
|
B9VJ80
|
Q7V2G1
|
TAL_PROMP
|
Transaldolase
|
Prochlorococcus
|
MKSILEQLSSITVVVADTGDLDAIKKFQPRDATTNPSLILAAAKNPDYIKLIDQALESSRKSLPAGFSESELIKETIDQVSVFFGKEILNLISGRVSTEVDARLSFDTEATVTKARKLINHYKSFGINKERILIKIASTWEGIKAAEILEKEGIKCNLTLLFNFCQAVACANAKITLISPFVGRILDWHKAKTGKDNFAGCEDPGVISVTKIYNYFKEKGFKTEVMGASFRNIDEIKELAGCDLLTIAPKFLDELNREEGELIKKLDEDTQSQSSIDYKFDEKDFRLSMLEDQMASEKLSEGITGFSKAIEELEELLLKRLSEINNQKLISTT
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q7V2G1
|
Q9BSH4
|
TACO1_HUMAN
|
Translational activator of mitochondrially-encoded cytochrome c oxidase I
|
Homo
|
MSAWAAASLSRAAARCLLARGPGVRAAPPRDPRPSHPEPRGCGAAPGRTLHFTAAVPAGHNKWSKVRHIKGPKDVERSRIFSKLCLNIRLAVKEGGPNPEHNSNLANILEVCRSKHMPKSTIETALKMEKSKDTYLLYEGRGPGGSSLLIEALSNSSHKCQADIRHILNKNGGVMAVGARHSFDKKGVIVVEVEDREKKAVNLERALEMAIEAGAEDVKETEDEEERNVFKFICDASSLHQVRKKLDSLGLCSVSCALEFIPNSKVQLAEPDLEQAAHLIQALSNHEDVIHVYDNIE
|
Acts as a translational activator of mitochondrially-encoded cytochrome c oxidase 1.
|
Q9BSH4
|
A4IJS3
|
UPPP_GEOTN
|
Undecaprenyl pyrophosphate phosphatase
|
Geobacillus
|
MDWMELLKAVILGMVEGLTEFAPVSSTGHMIIVDDLWLKSTEFLGKYAANTFKVVIQLGSILAAVVVFKDRFLELLGIRGRHPGGKPRLTLLHVIIGLLPAGVLGVLFEDYIDEHLFSTKTVLIGLVLGALLMIVADRFAKKAARAQTVDQITYKQAFLVGLVQCLSLWPGFSRSGSTIAGGVLVGMSHRAAADFTFIMAVPIMAGASGLSLLKNWQYVTVADIPFFIAGFLSAFVFALLAIRFFLHLINRIRLVPFAVYRIALAFIIYFLYF
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
A4IJS3
|
Q7X660
|
YSL11_ORYSJ
|
Protein YELLOW STRIPE LIKE 11
|
Oryza sativa
|
MASAAANNSSSAAYDAAETGGLLRRRNTTAAARGNAGEEEEEAEAVAPSVEQAFADKPVPSWREQLTVRAFVVGFLLSIMFNIIVMKLSLTTGVIPSLNVSASLLGFFLVRLWTAAIERVGFLKQPFTRQENTVIQTCVVSAYGVAFSGGFGSYLFGMSETIAKQATEANDPMNIKNPHLGWIIGFMFLVSFVGLFALVPMRKVMIVDYKLTYPSGTATAYLINGFHTPEGADLAKKQVRTLGKYFSISFLWAFFQWFYTAGDNCGFSSFPTFGLEAFKNRFYFDFSPTYVGVGMICPYIVNVSLLIGGIISWGIMWPLISKKKGSWYPETLPESSLLGLQAYKVFITIAVILGDGLYNFVKVFGYTIKGFIVMYKNKNSNTLPISDNGTPANATEEESFDDKRRNELFLKDQIPKTVAIGGYVVLAVITSGCLPLIIPQLKWYYILIAYIFAPIMAFCNAYGSGLTDWSLATTYGKLAIFVFGAWAGASHGGVLVGLAACGVMMNIVGTASDLMQDFKTGYMTLASPRSMFVSQVIGTAMGCVIAPCVFWLFYKSFNIGASDGAYPAPYTIMYRNMAILGVNGLSSLPKYCLTLCYIAFVAAFIINLIKDLVPERVAKYIPIPMAAAIPFYLGPYFAIDMFMGSVILYFWEWRNKDEAQSFGPAVASGLMCGDGLWALPQAVLSLVNVNPPLCMKFLSRAANAKVDTFLGN
|
May be involved in the transport of nicotianamine-chelated metals.
|
Q7X660
|
A5F7I4
|
YCIB_VIBC3
|
Inner membrane-spanning protein YciB
|
Vibrio
|
MKQLLDFIPLIIFFALYKFYDIYVATGALIAATTLQVIVTYAMYKKVEKMQLITFVMVALFGGMTLALHDDNFIKWKVTIVYVVFALGLTISQIMGKPAIKGMLGKELTLPDAVWSTINWAWVMFFSGCAALNLYVAYHLPLDVWVNFKVFGLLAATFVFTLLTGGYIYKHLPHEPKQKNQ
|
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
|
A5F7I4
|
Q1GR76
|
UPPP_SPHAL
|
Undecaprenyl pyrophosphate phosphatase
|
Sphingopyxis
|
MHDLATIILLGIIEGLTEFLPVSSTGHLILASEMLGFTGEGSAAFKIAIQLGAILAVLVAYRARFWGVGMGLLRADPAAVAFTRNILIGFLPAMLVGAVAYEGVRALLESPATVAVALLVGGIAILAIERMVKVVKVESVEAMPLRTAIAIGAVQCIAMIPGVSRSGATIMGALLMGVERRTAAEFSFFLAVPTMMGATAYSLWKDRAILTFDDMNAIAIGLFVAFLVALVVVKAFVAIVGRFGFAPFAWYRIIVGGGALLWLAWK
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q1GR76
|
Q7VRJ3
|
UBID_BLOFL
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Candidatus Blochmannia
|
MTYKDLRNFIKTLEYQGELKKIDFPVDPNLEITEIAHRTLKSQGPALLFTNPIGHSIPILCNLFGTISRIELGIGIKNILSLRDIGKLLAFLKEPQIPTGFRDFLSKIPNFRQILNMPIKHVSNAVCQENIWNNAQDIDITQMPIMKSWPGDISIAITWGITITQGFTNKRQNLGIYRHQVLSKNKIIIRWLAHRGGALDFQEWYTHSSEKKFPIAIALGADPATLIGAAIPIPNTLSEYAFSGLLRGSKTAVTKCISSNLYVPAYSEIILEGYINRDDIAVEGPFGDHTGYYNSTEKFPVCTITHITHRNNPIYHSTYTGRPPDEPSILGMAMNELFIPIIQKQFPEIIDFYLPPEGCSYRLAIVTIKKQFLGHAKKIIFGVWSCLNQFMYTKFILVCDDDINARDWKDVIWAISTRMDPARDIIIAENTPIDYLDFSSPISGLGSKMGIDATNKWPGETQRTWGKPIQMNNSIQSRINDIWDQLHIPCNEKPFKHKN
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
Q7VRJ3
|
A2BTJ3
|
THIC_PROMS
|
Thiamine biosynthesis protein ThiC
|
Prochlorococcus
|
MRSSWIKPRLGKDNVTQMNFARNGYITEEMDFVAKKENLPSSLIMEEVARGRLIIPANINHLNLEPMSIGIASRCKVNANIGASPNASDINEEVEKLKLAVKYGADTVMDLSTGGVNLDEVRQAIIQESPVPIGTVPVYQALESVHGSIDRLTEDDFLHIIEKHCQQGVDYQTIHAGLLIEHLPKVKGRITGIVSRGGGILAQWMLHHFKQNPLYTRFDDICEIFKKYDCTFSLGDSLRPGCLHDASDDAQLAELKTLGELTRRAWEHNVQVMVEGPGHVPMDQIEFNVRKQMEECSEAPFYVLGPLVTDISPGYDHISSAIGAAMAGWYGTSMLCYVTPKEHLGLPNAEDVREGLIAYKIAAHAADIARHRAGARDRDDELSHARYNFDWNKQFELSLDPERAKQYHDETLPEEIFKKAEFCSMCGPKHCPMNSKISDESLDQLKDKLEECNTSV
|
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
|
A2BTJ3
|
C5BB78
|
ZAPB_EDWI9
|
Cell division protein ZapB
|
Edwardsiella
|
MSFEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNQLNQEVQQAASNREGLLRENEQLKHEQEAWQERLRALLGKMNEVN
|
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.
|
C5BB78
|
Q2GS33
|
VPS27_CHAGB
|
Vacuolar protein sorting-associated protein 27
|
Chaetomium
|
MMGWWSSGANNALDEQIDKATSSSLEDIALNLEISDIIRSKTVQPKEAMRSLKKRINNKNPNTQLSALNLTDTCVKNGGAHFLAEIASREFMESLVSLLKAVGPGTVNAEVRAKILELIQSWATAAEGRYELGYIGEVYKTLQREGYQFPPRVTVASSMIDSNAPPEWVDSDVCMRCRTAFTFTNRKHHCRNCGNCFDQQCSTKSLPLPHLGILQAVRVDDGCYAKLTDKSSKASGAPPERSFTYSSSPAKPKGSSMQPRNARVDDGFDEDLKKALAMSLEEVKSHSRGYVSSPAANGVTSNQPKPNGHAAPKAVEEEDEDLKAAIAASLADMEEQKKQHAAALKQQASGAASSSSAAPSALPKNDYELTPLEAENINLFSTLVDRLQTQPPGTILREPQIQELYDSIGALRPKLARTYGETMSKHDTLLDLHARLSTVVRYYDRMLEERLSKAYSQHSIGGYNLPPPRQAPGPYPSLQPNAPPAAGPAENFYTGEQQQEYSHPTTHQPYPQPTLAQYGAYDKRGSVSAPSSNQYPPQQVPQHTGNWGPASSAQQYGQQPSYPPNEPPQTAQLQQTPNPAHLSAPAPAPNDSIGTTPTADPSASFYFSSQAQQQQQQQQQQQQQQQQQPQQVPSSPPDPNMSPYPNLAQPLHSYQPSLPQTPASIPAQPSQPQQAHQAPPQAQQPYWQHSAAQQTQLPPVWQPPPSAAYAGYTQESFPSAPHHAPKQPVVEESLIDL
|
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
|
Q2GS33
|
O43280
|
TREA_HUMAN
|
Alpha,alpha-trehalose glucohydrolase
|
Homo
|
MPGRTWELCLLLLLGLGLGSQEALPPPCESEIYCHGELLNQVQMAKLYQDDKQFVDMPLSIAPEQVLQTFTELSRDHNHSIPREQLQAFVHEHFQAKGQELQPWTPADWKDSPQFLQKISDAKLRAWAGQLHQLWKKLGKKMKPEVLSHPERFSLIYSEHPFIVPGGRFVEFYYWDSYWVMEGLLLSEMAETVKGMLQNFLDLVKTYGHVPNGGRVYYLQRSQPPLLTLMMDCYLTHTNDTAFLQENIETLALELDFWTKNRTVSVSLEGKNYLLNRYYVPYGGPRPESYSKDVELADTLPEGDREALWAELKAGAESGWDFSSRWLIGGPNPNSLSGIRTSKLVPVDLNAFLCQAEELMSNFYSRLGNDSQATKYRILRSQRLAALNTVLWDEQTGAWFDYDLEKKKKNREFYPSNLTPLWAGCFSDPGVADKALKYLEDNRILTYQYGIPTSLQKTGQQWDFPNAWAPLQDLVIRGLAKAPLRRAQEVAFQLAQNWIRTNFDVYSQKSAMYEKYDVSNGGQPGGGGEYEVQEGFGWTNGVVLMLLDRYGDRLTSGAKLAFLEPHCLAATLLPSLLLSLLPW
|
Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose.
|
O43280
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.