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
|
|---|---|---|---|---|---|---|
A8MDL8
|
TRPD_CALMQ
|
Anthranilate phosphoribosyltransferase
|
Caldivirga
|
MRPLLEKIARGLELSLEEAYNAALAILKMEAGEAETAALLMGLRVRGERAFEVAGFAKALRETCLRIPVNDPYVIDTAGTGGDGLRTMNVSTISALLAAYLGVKVLKHGNRSVSSSSGSADFLEALGFNISVKPETALLMLNNHRFSFAFAPMYHPAMKNVMPVRRRLGIRTIFNLVGPLANPGLVRRQVLGVAEAGIMGVMAEAAGLIGYDHLLLVHGEPGIDEVSVFGRTMIYEVKGNSIDKYVIEPPELGLRIHELRDVVVSNPMESIEKAKRGLMGVDEAALDFIAANTAMALYVAGKVKDPRDGVEAVKQIAGNSNDFWSYVNNVAAVSRRDSA
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
A8MDL8
|
Q9XFH8
|
TRXF1_ARATH
|
Thioredoxin F2
|
Arabidopsis
|
MPLSLRLSPSPTALSPTTGGFGPSRKQCRIPYSGVPTTKIGFCSLDSRKRGDSSVVRCSLETVNVSVGQVTEVDKDTFWPIVKAAGEKLVVLDMYTQWCGPCKVIAPKYKALSEKYDDVVFLKLDCNPDNRPLAKELGIRVVPTFKILKDNKVVKEVTGAKYDDLVAAIETARSAASG
|
Thiol-disulfide oxidoreductase involved in the redox regulation of enzymes of both reductive pentose phosphate pathway (Calvin-Benson cycle) and oxidative pentose phosphate pathway. Under light or reducing conditions, activates in chloroplast the glyceraldehyde-3-phosphate dehydrogenase, the phosphoribulokinase and the fructose-1,6-bisphosphate phosphatase, and inhibits the glucose-6-phosphate dehydrogenase.
|
Q9XFH8
|
Q688S6
|
YSL4_ORYSJ
|
Protein YELLOW STRIPE LIKE 4
|
Oryza sativa
|
MDASIGDPRLTSVEAAFEKNPLPGFSWLVTPRAMAVAVLLGIVFCFVGMRIQMMTGFVPALNMPVTVLSFFLLKVLARQLQKWRLTVVPFTRQENMFLITCVITCLNLAITGGFATALTGMGTIVAKTLADDLDPRDIIDYIPTGKLIIYFFLIGMAGVLSNIPLNQIMIIDYQLLFPTGSVIGHLINSFHTPEGAYIAKMQVMTIFKVFFGSFSWSIFQWFYSSGSGCGFSSFPTFGLELYKRRFYIDFSATYIGVGMMCPHIVNFGLLFGAIISWGFLYPYLETKHGEWYQTDSPSNLDGLNGYKVFISVTLIVTDGLINFLILVTSAAINFYHIRQQQQQTSGLASYISKNPSMNYDERKRIEMFLSSKIPMFVPVAAYVAWTAISMVAMPAMFDQIKYYHVGVLYLAIPVVGFCNTYATGLTDWSVSNTYAKFSPFIFAAWIARPGAIVASLLVSGITMASLHVSSQAMQDLKSAHMTLTSPRAMIAGQVFGVALSSVVSPCIFRAFEKAAKPGAPLGSKDSVYPCPYAGLYRAICIIGMGGVKGLPKYCVELCVIAVLVTIAIDALVLVSQLKGWRLHLYIPSMTVIALPFFAGSYFTLDMCLGGLLLLLWKKIDTMSAEILSAAVAAGLICGEGLFTLPSALLNMFKVLPPMCMKFLPSGQEVEVVDSFLNSSGGTVPKT
|
May be involved in the transport of nicotianamine-chelated metals.
|
Q688S6
|
Q9HMT9
|
UVRB_HALSA
|
Excinuclease ABC subunit B
|
Halobacterium
|
MSDASGPLQPDRPEADVPFRVEAPFDPAGDQPDAIAELVAGYEQGAQQQTLLGVTGSGKTNTVSWVVEELQQPTLVIAHNKTLAAQLYEEFRSLFPDNAVEYFVSYYNYYQPEAYVEQTDKYIEKDASINDEIDRLRHSATRSLLTRDDVIVVASVSAIYGLGDPRNYEEMSLRVERGQSIGRDQLLAKLVDLNYDRNDVDFTQGTFRVRGDTVEVYPMYGRYPVRVEFWGDEIDRMAKLDPLEGTVESEEPAVLFHPAEHYSVPDAEMEQAIERIRTDMHERVRHFERTGDMVAAQRIEERTTFDLEMMAEAGYCSGIENYSVYLSDREVGDAPYTLLDYFPDDFLTVIDESHRTVPQIKGQYEGDKSRKDSLVDNGFRLPTAYDNRPLTFAEFADKTDRTLYVSATPGDHERAQSANVVEQIVRPTHLVDPDISIADATGQVEDLMDRIDERVARDERVLVTTLTKRMAEDLTEYLEEAGVAVEYMHDETDTLERHELVRGLRLGEYDVLVGINLLREGLDIPEVSLVAILDADQQGFLRSETSLVQTMGRAARNVNGEVVLYADETTDAMQAAIDETQRRRRIQRAFNEDHGTTPTTIEKAVGDMNLPGAETDTADVAGDAPSDEQEAALLVEDLEARMEDAASNLEFELAADIRDRMRELREAFDLDGGDAPEDPGGVAPETEDW
|
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.
|
Q9HMT9
|
P64549
|
YFIR_ECO57
|
Protein YfiR
|
Escherichia
|
MRFSHRLFLLLILLLTGAPILAQEPSDVAKNVRMMVSGIVSYTRWPALSGPPKLCIFSSSRFSTALQENAATSLPYLPVIIHTQQEAMISGCNGFYFGNESPTFQMELTEQYPSKALLLIAEQNTECIIGSAFCLIIHNNDVRFAVNLDALSRSGVKVNPDVLMLARKKNDG
|
Repressor of the cell division arrest function of DgcN. Prevents DgcN relocation to the midcell.
|
P64549
|
Q0VEE6
|
ZN800_MOUSE
|
Zinc finger protein 800
|
Mus
|
MPLRDKYCQTDHHHHGCCEPVYILEPGDPPLLQQPVQTSKSGIQQIIECFRSGTKQLKHILLKDVDTIFECKLCRSLFRGLPNLITHKKFYCPPSLQMDDNLPDVNDKQSQAISDLLEAIYPRVDKREYIIKLEPIETNQNAVFQYISRTDNPAEVTESSSTPEQTEVQIQETSSEQLKAVPDADTEVEEAIEPPSIETVVDEAAAPTEEQPQESQADLETSDSSDLGHQLICCLCRKEFNSRRGVRRHIRKVHKKKMEELKKYIETRKTPNQSSKGRSKSVLVSLSRSCPVCCKSFATKANVRRHFDEVHRGLRRDSITPDIATKPGQPLFLDSASPKKSFKTRKQKSSKAEYNLTACKCLLCKRKYSSQIMLKRHMQIVHKITLSGANSKREKGPNNTANSSEVKVELADSVESSPPSITHSPQNELKGTNHSNEKKNTPATQKNKVKQDSESPKSASPSAAGGQQKTRKPKLSAGFDFKQLYCKLCKRQFTSKQNLTKHIELHTDGNNIYVKFYKCPLCTYETRRKRDVIRHITVVHKKSSRYLGKITASLEIRAIKKPIDFVLNKVAKRGPSREEAKHNDSKQDGTSNSPSKKYEVADVGIEVKVTKNFSLHRCNKCGKAFAKKTYLEHHKKTHKANATNSPEGNKTKGRSTRSKALV
|
May be involved in transcriptional regulation.
|
Q0VEE6
|
B7N473
|
TRPA_ECOLU
|
Tryptophan synthase alpha chain
|
Escherichia
|
MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFSKGIDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVTKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLVALKAFVQPMKAATRS
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
B7N473
|
Q87LA0
|
UVRA_VIBPA
|
Excinuclease ABC subunit A
|
Vibrio
|
MDKIEVRGARTHNLKDINLTIPRDKLTVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTITEVYDYLRLLYARVGEPRCPTHHAPLAAQTVSQMVDKVLELPEGSKMMLLAPIVKERKGEHVKTLENLAAQGFIRARIDGETCDLSDPPTLELHKKHTIEVVVDRFKVRPDLQQRLAESFETTLELSGGIAVVAPMDGDGEEIIFSANFACPQCGYSMQELEPRLFSFNNPAGACGTCDGLGVQQYFDPSRVIQDDSLSLAQGAIRGWDQKNYYYFQMLTSLADHYGFDLHAPFNSLPKKTQDVILKGSGRTEIEFKYINDRGDIRVKRHPFEGILNTLERRYRDTESNSVREELAKYISTKSCSSCGGTRLRLEARNVFIADTTLPEIVELSIADALTFFQTLKLEGQRAQIAEKVMKEINDRLQFLVNVGLNYLNLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLKTLTHLRDLGNTVLVVEHDEDAIRCADHVIDIGPGAGVHGGNVVAEGTMDEIIANPNSLTGQYLSGAKEIAVPKERTPRDPKKTVELLGATGNNLKNVDLSIPVGLFSCITGVSGSGKSTLINDTFFKIAHTQLNGATTAHPSPYKSIKGLEHFDKVIDIDQSPIGRTPRSNPATYTGIFTPIRELFAGTQESRSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGKRYNRETLEVRYKGKTIDEVLEMTVEDARTFFDPVPAIARKLQTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFHDIQQLLTVLHRLRDHGNTVVVIEHNLDVIKTADWIIDLGPEGGQGGGEIIAQGTPEDVSQIEGSHTARFLKPMLK
|
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.
|
Q87LA0
|
Q5EAW9
|
TAF3_XENLA
|
TBP-associated factor 3
|
Xenopus
|
MGVNIHELEDYIHNIEPVTFPHQIPSFPVSKNNALQFPPPGSKDAEDRKEYIPDYLPLIISSQEEEEEEQVPTDGGTSAEAMQVPLEEEEEEGEMEDDETVNDENYLSKRPLDSPETMEMPFAKRIRLMNNKGDILDGSLEPREPLSSINSQKVPSVLSPAHKIDSQDLDVSYSDQIMLSPVSKSQAPPPSESKSLIPKTKSKGGSPGQKIKSPKATPISTVIGSPIRSPKSGPKERKSPGCAKSPKSPKSPKVPLAAPPPAIKTETPNRTPLATLSEKIGRENIQIKQNQTPLDSDQLNVEIPSKKPSIADNTIEDSIDAVIARACAEQEPDPFEFSSGSESEGEVFTSPKRLNISELTTPKVSASGINPGKTSSTSVPASGGTSSSDISWTMDDSINEVIRKVSQETPTNTPANNPPCFSSPSASPPTPEPLLKVFEDKAKLPPPVELKKKTKKEQRAKKKKDKDKLKDKERSKDKNKDRSKDKEKDKEKDGTKDGKVLWKDSNKDEDSELHRFKLKDFNEIDSKSKQKENCGKKDKEKHKDKKKDKEKGKKDKDKKGKDKTKEEKMKSPSTPIMLSSKDIALPMISTPNTVRLPSLLSSMSPLLPEKLFEEKEKSKEKDKKKDKKEKKKKKDKEKVKEKEKEKKEKEKEKEKEKKEKEKVKAELSIPAPSPVIPRLTLRVGAGQDTIVISKVVSAPESKAVPPPSLPKSPPPTPSPAPAPVLVVPPQAPPAPAAASPAPTPAPSALTSNAGSSKTPVRSVVTETVSTYVIRDEWGNQIWICPGCNKPDDGSPMIGCDQCDDWYHWPCVGINAAPPEDEQWFCTKCESKKKDKKQKKRKHKAH
|
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of tbp and TBP-associated factors (TAFs).
|
Q5EAW9
|
B8ISV4
|
TAM_METNO
|
Trans-aconitate 2-methyltransferase
|
Methylobacterium
|
MADWDAAQYLKFADERTRPAADLLARVPLAAPARVVDLGCGPGNSTELLVARYPEAAILGLDTSPGMLAEARRRLPGVAFEQADVASLNPEPPPDLLFANAVLQWLPHHASLLPRLARSLAPGGCLAVQMPDNLEEPSHRLMRRVAGEPPFAARLAAAAASRTRIASFSEYDAWLTAAGCTVDIWRTTYVHALAGHRGIVEWVRGTGLRPFLDPLDAEAQAEFLARYEAALAEAYPPQADGRVLLPFPRLFLVARRTR
|
Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.
|
B8ISV4
|
Q96K58
|
ZN668_HUMAN
|
Zinc finger protein 668
|
Homo
|
MEVEAAEARSPAPGYKRSGRRYKCVSCTKTFPNAPRAARHAATHGPADCSEEVAEVKPKPETEAKAEEASGEKVSGSAAKPRPYACPLCPKAYKTAPELRSHGRSHTGEKPFPCPECGRRFMQPVCLRVHLASHAGELPFRCAHCPKAYGALSKLKIHQRGHTGERPYACADCGKSFADPSVFRKHRRTHAGLRPYSCERCGKAYAELKDLRNHERSHTGERPFLCSECGKSFSRSSSLTCHQRIHAAQKPYRCPACGKGFTQLSSYQSHERTHSGEKPFLCPRCGRMFSDPSSFRRHQRAHEGVKPYHCEKCGKDFRQPADLAMHRRVHTGDRPFKCLQCDKTFVASWDLKRHALVHSGQRPFRCEECGRAFAERASLTKHSRVHSGERPFHCNACGKSFVVSSSLRKHERTHRSSEAAGVPPAQELVVGLALPVGVAGESSAAPAAGAGLGDPPAGLLGLPPESGGVMATQWQVVGMTVEHVECQDAGVREAPGPLEGAGEAGGEEADEKPPQFVCRECKETFSTMTLLRRHERSHPELRPFPCTQCGKSFSDRAGLRKHSRTHSSVRPYTCPHCPKAFLSASDLRKHERTHPVPMGTPTPLEPLVALLGMPEEGPA
|
May be involved in transcriptional regulation.
|
Q96K58
|
Q31LZ7
|
TRHO_SYNE7
|
tRNA hydroxylation protein O
|
Synechococcus
|
MSLVLINFYRFVALGDCDRWRQWLQDLCTALGLRGTILLAPEGINAGLAGNTEAIAQFLSELQQHPPFANLSFKSATVTDWPFARLKVKVKPEIVSLGCPELNPAERTGTLVAPQDWNQLLQDPEVVLIDVRNRFEIALGSFPRAIDPQTDRFRDFPRFVQEQLLPQPPAKVAMFCTGGIRCEKASAYLLEQGIETVYQLEGGILNYLEAIAPEENHWQGDCFVFDERIAVDRQLQTPQHQLCPACGQPVVATTCSHCQDSVQASSSPK
|
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
|
Q31LZ7
|
B2V6F7
|
TATA_SULSY
|
Sec-independent protein translocase protein TatA
|
unclassified Sulfurihydrogenibium
|
MGSIGMTELLLIFGIIVLLFGAKKLPEIGRGLGEGIRSFKSAISGEEKKEDEKVVTPKEIEAEVIKKEKVKENA
|
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.
|
B2V6F7
|
A7NDM9
|
TDH_FRATF
|
L-threonine 3-dehydrogenase
|
Francisella
|
MKALAKLKKQPGIWMINDAPIPEYGYNDVLIKIKKTAICGTDLHIYNWDKWSQNTIPVPMITGHEFAGEVVAKGDGVTSVDIGDRVSGEGHLVCGQCRNCRAGKRHLCRKTIGIGVNVQGAFAEYLVMPAVNVFKIPDSISDDIASTFDPMGNAIHTALSFNLTGEDVLITGAGPIGLMAVKIARFCGARRIVITDINEYRLQMARDFGATVALNVAPFKNQDELVKQMRKVMSDIGMTEGFDVGLEMSGINSAISMMLDVMNHGGKLSLLGISAGDISVDWGAILFKGLTLKGIYGREMFETWYLMTSMLQAGMDMNPIITHRLHIDEFQKGFEIMKSGQCGKVILDWSS
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
|
A7NDM9
|
A4PCD4
|
TDT_EULMA
|
Terminal deoxynucleotidyltransferase
|
Eulemur
|
MDPLQTAHAGPRKKRPRQTGASMASTPQDVRFQDLVLFILEKKMGSTRRTFLTELARRKGFRVENEFSDSVTHIVAENNSGSDVLEWLQVQKIKASSQLEVLDVSWLIECMRTGKPVETTGKHQLVARSDCSASPNPGPQKTPPLAVQKISQYACQRRTTLNNCNHVFTDAFEILAENYEFKENEGCAVTFLRAASVLKSLPFTIITMRDTEGIPCLEDKVKCIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKIRSDKSLTFTRMQRAGFHYYEDLVSCVTRAEAEAVSVLVKEAVWAFLPDAFVTMTGGFRRGKKIGHDVDFLITSPGSTEEEEEQLLHKVMNLWEKKGLLLYCDLVESTFEKLKLPSRKVDALDHFQKCFLILKLHHQRVVDSQKSSQQDGKTWKAIRVDLVMCPYERRAFALLGWTGSRQFERDLRRYATHERRMMLDNHGLWDKTKRIFLKAESEEEIFAHLGLDYIEPSERNA
|
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.
|
A4PCD4
|
O66893
|
TOP1_AQUAE
|
Untwisting enzyme
|
Aquifex
|
MELFIVESPTKAKTIQKFLGKGFLVKATLGHVKDLPEKELGVDLRTLKAKYVYKRGKKKLVEQLKKLSRRSSIVYLGTDPDREGEAIAYFLKKDLEKVNKNIKRAVFYEITPEAIRESIRNAGDVNMNLVYAQFARRILDRLIGYLISPILWKEFKNYKLSAGRVQSPALRLIVEREREIQNFKVKKYYYVKALLRKGSEEFWAIYDYRYENPSDAKIIAKKLEKGYFSVYKVEKKKEKVSPPKPFITSDLQSEANAKFGFSSERTQKLAQELYEKGYITYPRTDSYRMNEKKAKEFMNYIEKKYGKEYVGRLRRFREKATAQGAHECIRPTSLREEIPEREELRLLYDLIFRRTIASLMKEMLLEREKVTVEAITPELKHPVYLVAKGLKIVFDGWSRVYPSEITEEKLPELYEGDLLDLVKTTLEERKTQPPPRYTEGTLIKTLEKLGIGRPSTYATIVKTLKERGYVEVKKKALVPTEIAFQVVEFLMERFPTLMDYKFTAQMEEKLDLVEEGKLNWKSVVYEFMEKIFGKELEMVR
|
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
|
O66893
|
B3QUZ7
|
THIG_CHLT3
|
Thiazole synthase
|
Chloroherpeton
|
MDELIIAGKSFKSRLILGTSRYPNPQVMMEALEASGTEMVTVAIRRMDLKSDSAENIMKFLDDKKYFLLPNTAGCYTAKEAVLTAELAREALGTNWIKLEVLGDDETLFPDIPELLKAAETLLEKDFVVLPYTNDDPITCKKLSDMGCAAVMPLGAPIGSGMGIRNPYNLQIIREQIDIPLIVDAGVGTASDVAVAFELGVDGVLLNTAVAQAKHPVQMATAIKHAALAGRMAVNAGRIPKKLYATASSPTDDMIEIDG
|
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.
|
B3QUZ7
|
Q39582
|
TBG_CHLRE
|
Gamma-tubulin
|
Chlamydomonas
|
MPREIINLQVGQCGNQVGSEFWRKLCQEHGIAKDGRLEDFATLGGDRKDVFFYQADDEQYIPRAILLDLEPRVINGIQTSDLRNLFNPENIFISKEGGGAGNNWASGYTQGEAVQETLLDMIDREAEYCDSLEGFNMCHSIAGGTGSGMGSYMLELISDRYSKKLIQTYSVFPNQSESSDVVVQPYNSLLTLKRLTLHADAVVVLDNTALDKIAVERLHLHKPDVQQINSLIATVMAASTTTLRYPGYMNNDLVGLVASLIPTPRCHFLMTGYTPLTAENAAGQVTSNIRKTTVLDVMRRLLQPKNIMVSTHTKSRDIANAKYISILNIIQGEVDPSQVHKSLQRIRERKQANFIEWGPASIQVALSKKSPYVQTAHRVSGLMLANHTSVRHLFNKVLRDYEKLMGPKQERQAFMQAYRDVPRFADAAGGGTALLEEFADAKEVVQDLANEYAACESADYIQRQMMAS
|
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.
|
Q39582
|
B2RQC2
|
UBP42_MOUSE
|
Ubiquitin-specific-processing protease 42
|
Mus
|
MTIVDKTEPSDPSTCQNQPGSCEAVSPEDMDTGSASWGAVSSISDVSSHTLPLGPVPGAVVYSNSSVPEKSKPSPPKDQVLGDGIAPPQKVLFPSEKICLKWQQSHRVGAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQTHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVTKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTISLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIIYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRAVLNQQAYVLFYIRSHDVKNGGESAHPAHSPGQSSPRPGVSQRVVNNKQVAPGFIGPQLPSHVMKNTPHLNGTTPVKDTPSSSVSSPNGNTSVNRASPATASTSVQNWSVTRPSVIPDHPKKQKITISIHNKLPARQGQAPLNNSLHGPCLEAPSKAAPSSTITNPSAIQSTSNVPTTSTSPSEACPKPMVNGKAKVGASVLVPYGAESSEESDEESKGLAKENGVDMMAGTHSDRPEAAADDGAEASSHELQEPVLLNGANSADSDSQENSLAFDSASCQVQPELHTENLFSKLNGLPGKVTPAPLQSVPEDRILETFKLTNQAKGPAGEESWTTTGGSSPKDPVSQLEPISDEPSPLEIPEAVTNGSTQTPSTTSPLEPTISCTKEDSSVVVSAEPVEGLPSVPALCNSTGTILGDTPVPELCDPGDLTANPSQPTEAVKGDTAEKAQDSAMAEVVERLSPAPSVLTGDGCEQKLLLYLSAEGSEETEDSSRSSAVSADTMPPKPDRTTTSSCEGAAEQAAGDRGDGGHVGPKAQEPSPAKEKMSSLRKVDRGHYRSRRERSSSGEHVRDSRPRPEDHHHKKRHCYSRERPKQDRHPTNSYCNGGQHLGHGDRASPERRSLSRYSHHHSRIRSGLEQDWSRYHHLENEHAWVRERFYQDKLRWDKCRYYHDRYTPLYTARDAREWRPLHGREHDRLVQSGRPYKDSYWGRKGWELQSRGKERPHFNSPREAPSLAVPLERHLQEKAALSVQDSSHSLPERFHEHKSVKSRKRRYETLENNDGRLEKKVHKSLEKDTLEEPRVKKHKKSKKKKKSKDKHRDRESRHQQESDFSGAYSDADLHRHRKKKKKKKRHSRKSEDFIKDVEMRLPKLSSYEAGGHFRRTEGSFLLADGLPVEDSGPFREKTKHLRMESRPDRCRLSEYGQGD
|
Deubiquitinating enzyme which may play an important role during spermatogenesis.
|
B2RQC2
|
V9QER4
|
TXAD_STEGR
|
Latrodectin
|
Steatoda
|
MSKLHFLILLSVIVSVFCIEPQDIGCTGISTAEFEEKDATCSKCEEDYSGNGMIDRCRSDCYSGPFFKSCVELLNKGYDEKDENVKPEW
|
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
|
V9QER4
|
B4F0U2
|
YIDD_PROMH
|
Putative membrane protein insertion efficiency factor
|
Proteus
|
MASSLSLGSKILILLIRGYQLGISPLLGPRCRFNPTCSHYGIEALRRFGMIKGSWLTVKRILKCHPLHEGGDDPVPPRKNDDNREN
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
B4F0U2
|
P08438
|
VCL_VICFA
|
Vicilin
|
Vicia
|
MAATTLKDSFPLLTLLGIAFLASVCLSSRSDQDNPFVFESNRFQTLFENENGHIRLLQKFDQHSKLLENLQNYRLLEYKSKPHTIFLPQQTDADFILVVLSGKAILTVLLPNDRNSFSLERGDTIKLPAGTIGYLVNRDDEEDLRVLDLVIPVNRPGEPQSFLLSGNQNQPSILSGFSKNILEASFNTDYKEIEKVLLEEHGKEKYHRRGLKDRRQRGQEENVIVKISRKQIEELNKNAKSSSKKSTSSESEPFNLRSREPIYSNKFGKFFEITPKRNPQLQDLNIFVNYVEINEGSLLLPHYNSRAIVIVTVNEGKGDFELVGQRNENQQGLREEYDEEKEQGEEEIRKQVQNYKAKLSPGDVLVIPAGYPVAIKASSNLNLVGFGINAENNQRYFLAGEEDNVISQIHKPVKELAFPGSAQEVDTLLENQKQSHFANAQPRERERGSQEIKDHLYSILGSF
|
Seed storage protein.
|
P08438
|
Q97VM8
|
TPIS_SACS2
|
Triose-phosphate isomerase
|
Saccharolobus
|
MKPPIIIINFKAYENSFGDKAVNLGKKIEKISKEYSVEIILSTPATMIYRMSQEVDLPIYAEHVDPVPLGAFTGAILPEMVKDAGAKGTLINHSERRLRADEIDDVLKRTKKLGLKSILCVDRYELVYPFSLLKPDAILIEPPELIGTGVSVSKAKPEVITRAVDEIRKSEGIYLIAGAGITTGEDVYKALKLGAHGIGVASAVMKAKEPEKVVEDFITSALRAISS
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q97VM8
|
Q9S3V1
|
VIOA_CHRVO
|
Flavin-dependent L-tryptophan oxidase VioA
|
Chromobacterium
|
MKHSSDICIVGAGISGLTCASHLLDSPACRGLSLRIFDMQQEAGGRIRSKMLDGKASIELGAGRYSPQLHPHFQSAMQHYSQKSEVYPFTQLKFKSHVQQKLKRAMNELSPRLKEHGKESFLQFVSRYQGHDSAVGMIRSMGYDALFLPDISAEMAYDIVGKHPEIQSVTDNDANQWFAAETGFAGLIQGIKAKVKAAGARFSLGYRLLSVRTDGDGYLLQLAGDDGWKLEHRTRHLILAIPPSAMAGLNVDFPEAWSGARYGSLPLFKGFLTYGEPWWLDYKLDDQVLIVDNPLRKIYFKGDKYLFFYTDSEMANYWRGCVAEGEDGYLEQIRTHLASALGIVRERIPQPLAHVHKYWAHGVEFCRDSDIDHPSALSHRDSGIIACSDAYTEHCGWMEGGLLSAREASRLLLQRIAA
|
The enzyme generates the imine form of indole 3-pyruvate (IPA) from L-tryptophan (L-Trp), with concomitant two-electron reduction of O(2) to H(2)O(2).
|
Q9S3V1
|
Q9VGA2
|
TI17C_DROME
|
Probable mitochondrial import inner membrane translocase subunit Tim17 3
|
Sophophora
|
MEYNRQPCPIRIVEDCGCAFMMGTIGGSLFEFLKGFRNAPTGLQRRLYGGIDLVKMRTPSIAGSFAVWGATFSTVDCALVHYRQREDAWNSILSGAATGGILAARNGIRAMANSALVGCLVLAMIEGAGAAVATINAADKGAGIVIKPQRAQWEAILETIDPKRASSTQDFALAEFERVLDKCRASREPNLLQDIPVKSHERDSKQKPFYSLLDLVKLSQMF
|
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
|
Q9VGA2
|
P44740
|
TRMO_HAEIN
|
tRNA methyltransferase O
|
Haemophilus
|
MNDLTLSPIAIIHTPYKEKFSVPRQPNLVEDGVGIVELLPPYNSPEAVRGLEQFSHLWLIFQFDQIQQGKWQPTVRPPRLGGNQRVGVFASRATHRPNPLGLSKVELRQVECINGNIFLHLGAVDLVDGTPIFDIKPYIAYADSEPNAQSSFAQEKLPVKLTVEFTEQAKSAVKKREEKRPHLSRFIRQVLEQDPRPAYQQGKPSDRIYGMSLYEFNVKWRIKAGTVNCVEVIEIEKDK
|
S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU). The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA decoding ability. Binds to tRNA.
|
P44740
|
A8AD50
|
TRMJ_CITK8
|
tRNA Cm32/Um32 methyltransferase
|
Citrobacter
|
MLQNIRIVLVETSHTGNMGSVARAMKTMGLTNLWLVNPLVKPDSQAIALAAGASDVIGNAQIVDTLDDALAGCSLVVGTSARSRTLPWPMLDPRECGLKSVAEAVNTPVALVFGRERVGLTNDELQKCHYHVAIAANPEYSSLNLAMAVQVIAYEVRMAWLATQENDETAEHEETPYPLVDDLERFYGHLEQTLLSTGFIREGHPGQVMNKLRRLFTRARPESQELNILRGILASIEQQNKGK
|
Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
|
A8AD50
|
Q8CXQ1
|
TRUA_MALP2
|
tRNA-uridine isomerase I
|
Malacoplasma
|
MTYKLKISYDGSFFRGYAKQKDENLITVQSELEKYLSLFFNTKISTFGSGRTDKYVHAIDQTVSFKCDSDYDPKSIQNFLNSKLTNIYVNSIEKVPNSFHARFSIKSKTYMYVINTGEFDVFKQRYEYQYNKSIDIKKCEDIINLFIGTKDFLSFSTSKLENTTRTIRWIRIIKKNKKIYIFINGEGFLRNMVRMIVGIILTYCENKITYQEVLDLFKNPKKGSAVIKVPGCGLYLYRTIY
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q8CXQ1
|
P48605
|
TCPG_DROME
|
Chaperonin containing TCP1 subunit 3
|
Sophophora
|
MFGGQQPILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQLSIQLDVKDKAKMADVVKACVGTKFIGKWSDLAVKIALDAVETVTLSENGRLEVDIKRYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCSLEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIARACGATIVNRTEELTEKDVGTGAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLEPRLVAGGGAVEMAASQLLTRKQVKGPYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHASHTGDGVCAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGSKKRGGNEPTNPAAMAQGQE
|
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
|
P48605
|
Q5X7R0
|
TRMB_LEGPA
|
tRNA(m7G46)-methyltransferase
|
Legionella
|
MQRKIKSYVLRAGRISNRQQQGLDLWLEDYELKFDSPTPWNFAKEFGRHDADTIVEIGFGMGTSLFAMAMNNPQCNYLGIEVHKAGVGSLVADLHEHQISNVRVVVHDAVEVLQTKIPENSLAGVQIFFPDPWHKKRHHKRRLIQSEFIQMLVKKIRPSGFIHCATDWEDYAEHILNVLSSESALFNQQKEGGYSPRPDSRPLTKFEQRGERLGHGVWDLVFIKNKEVTNDKACNSY
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
Q5X7R0
|
P31111
|
ZIP1_YEAST
|
Synaptonemal complex protein ZIP1
|
Saccharomyces
|
MSNFFRDSSMGFKPRPNIFAKLRVRDVDSDSSANTVVENSSNCLDVGSSIEGDDTFKKPHKTSTEQELITSMSLSQRNHGYSDDMEIGSPKKTTSTDQYNRILKNDVAAIENDTDEDFEITEVREVSEGVAKETKESHGDPNDSETTLKDSKMHEYTMTNGKAPLHTSINNSSTSSNDVLLEAFTNTQRICSNLKQELQKQQQDNAKLKVRLQSYASNSDKINEKVGKYKSCLETLQERIATLTSHKNNQETKLKDLRQNHQLYQRRISGFKTSIENLNKTINDLGKNKKEADAELMKKGKEIEYLKRELDDCSGQLSEEKIKNSSLIQEMGKNREEMIKSIENFFSEDKAHHLLQFNKFEERVHDLFEKKLQKHFDVAKDTLNVGLRNTTVELSSNTETMLKQQYEDIKENLEQKMSSSKDEMAKTINELSVTQKGLIMGVQEELLTSSGNIQTALVSEMNNTRQELLDDASQTAKNYASLENLVKAYKAEIVQSNEYEERIKHLESERSTLSSQKNQIISSLGTKEAQYEDLVKKLEAKNIEISQISGKEQSLTEKNENLSNELKKVQDQLEKLNNLNITTKSNYENKISSQNEIVKALVSENDTLKQRIQQLVEIKENEQKDHTTKLEAFQKNNEQLQKLNVEVVQLKAHELELEEQNRHLKNCLEKKETGVEESLSDVKTLKQQVIVLKSEKQDITAEKLELQDNLESLEEVTKNLQQKVQSQKRELEQKIKELEEIKNHKRNEPSKKGTQNFTKPSDSPKKNATTSNLFPNNSAAIHSPMKKCPKVDHISKSRINSSKETSKFNDEFDLSSSSNDDLELTNPSPIQIKPVRGKIKKGSNCMKPPISSRKKLLLVEDEDQSLKISKKRRRK
|
Required for meiotic chromosome synapsis and cell cycle progression. May act as a molecular zipper to bring homologous chromosomes in close apposition. ZIP1 may encode the transverse filaments of the synaptonemal complex.
|
P31111
|
Q8Y0Z5
|
UBIG_RALSO
|
3-demethylubiquinone 3-O-methyltransferase
|
Ralstonia
|
MTTTYANADPGELEKFSELAHRWWDPNSEFKPLHEINPLRLDWIQSTAPLAGKRVVDVGCGGGILSESMARAGANVKGIDLSRKALRVADLHSLEAGVAVDYEEIAAEALAAREPGSFDVVTCMEMLEHVPDPASVVRACATLVKPGGHVFFSTIHRNAKAYLLAVIGAEYVLNMLPRGTHDYAKFIRPSELAGFARTAGLEPAQLRGLEYNPLTGRYALTHDTSVNYLIATRRPDAP
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
Q8Y0Z5
|
A3PTG0
|
TAM_MYCSJ
|
Trans-aconitate 2-methyltransferase
|
unclassified Mycobacterium
|
MWNPEAYLSFADHRGRPFFDLLARVGADAPRRVVDLGCGPGNLTVVLRHRWPEAVVEAWDNSPEMVAAARERGVQANLGDVRGWSPQPDTDVVLSNATLQWVPEHPELLTRWAGALAAGSWLAMQVPGNFDAPSHQAVRRLADREPWAPLLHDIPFRVGKVVETPADYAALLTDAGCSVDAWETTYIHELTDAHPVLEWITGTALRPVRSRLTDEQWDRFRAELIPLLDEAYPVRADGRTFFPFRRVFVVARTG
|
Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.
|
A3PTG0
|
Q25632
|
TPM_ONCVO
|
Ov-tmy-1
|
Onchocerca
|
MDAIKKKMQAMKIEKDNALDRADAAEEKVRQMTEKLERIEEELRDTQKKMMQTENDLVKAQEDLSVANTNLEDKEKKVQEAEAEVAALNRRMTLLEEELERAEERLKIATDKLEEATHTADESERVRKVMENRSFQDEERANTVESQEKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENEIVELEEELRVVGNNLKSLEVSEEKALQREDSYQEQIRTVSVRLKEAETRAEFAERSVQKLQKKVDRLEDELVHEKERYKNISEELDQTFQELSGY
|
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
|
Q25632
|
E1C1R4
|
UBP47_CHICK
|
Ubiquitin-specific-processing protease 47
|
Gallus
|
MKEFVSMRLLPEDMFWSCRQSTLAEMKKKFAQVESAAEEPRVLCIIQDTTNSKTVNERVTLNVPASTPLKKLFEDVASKVGYVNGTFDLVWGNGDNVTDMTPIDQNSDKTILDAGFEPGKKNFLHLTDKDGEQPHIMQEESGTTEDSAQDRFIGPLPREGSVGCTNDYVSQSYSYSSVLSKSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIETTDVTRSFGWDSSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINQLYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSNQAFASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSIFIDVEDEKSPQTESCTDSGAENEGSCHSDQMSNDFSNDDGVDEGICLESNSAAERIAKVGSEKNSLLYELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSKITQEDIKKTYGGSSGSRGYYSSAFASSTNAYMLIYRLKDPARNAKFLESHEYPDHIKQLVQKERELEEQEKRQREIERNTCKIKLFCMHPTKQIMMENKLEVHKDRTLKEAVGIAYKLMDLEEAVPLDCCRLVKYDEFHDYLERSYEGEEDTPMGLLLGGVKSTYMFDLLLETRRPDQIFQCYKPGEVMVKVHVVDLKTESVAPPISVRAYLNQTVSEFKQLISKATHLPAETMRVVLERCYNDLRLLTVSSKTLKAEGFFRSNKVFIESSESLDRHVAYTDSHLWKLLDRHANTIRLYVSLPEQSPGSQFRRSIYQKPSGDLGNLDEACERVKGPAGNMKSVEAILEESTEKLKSLSLQQQQQEGDNGDSSKSTEASDFENIESPSNEIDSSASVENRELENQIQISDPENLQSEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNVDNAPIPLANGLDSHSITSSRRSKANQGKKETWDTAEEDSGTDSEYDESGKSRGETQYMYFKSEPYTADEGSGEGQKWLMVHVDKRITLSAFKQQLEPFVGVPSSHFKVFRVYASNQEFESVRLNETLSSFSDDNKITIRLGRALKKGEYRVKVYQLLVNEPEPCKFLLDAVFAKGMTVRQSKEELLPQLREQCGLDLTIDRFRLRKKTWKNPGTVFLDYHIYEEDINISSNWEVFLEILDGVEKMKSMSQLAVLSRRWRPSEMKLDSFQEVVLESSSVEELKEKLSELSGIPLENIEFAKGRGTFPCDISVLEIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDKTEELMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKIYLDGAPNKDLTQD
|
Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER).
|
E1C1R4
|
A1CW44
|
TVP38_NEOFI
|
Golgi apparatus membrane protein tvp38
|
Aspergillus subgen. Fumigati
|
MPADYTSTARALSLPMSPAESLSPAEEDTQPLWSHLASSRRNTASPSARESTGLRDQVVNQATKMLRRTKKTWRRLTFWQRIGAIGAALLAILLGLAFMIFTGQVFFWLGPVAEKWEQSWLAFFVLWLCVFFVSFPPLVGWSTFGTIAGFIFGIWKGWILYATATVLGSTCSFIVSRTILSKFVNRMMERDKRFAALALTLKYDGLKLLCMIRLCPLPYSVCNGAVSTFPTVHPLMYGLATALITPKLLVPAFIGSRIRILSEKNEEMSAGSKAVNICSIILTIGIGIFTGWYIYRRTLARAKELEAKERADIRRSLQADHAAHHPHGSFSEDPDVNTAATTLARDEEERIGFNDFDDDNVDLVIDDESGSENSPNLTKKQFQGPYRDEFTDNDSDVFGDGDGPDSQMFRLHTHVRSG
|
Golgi membrane protein involved in vesicular trafficking and spindle migration.
|
A1CW44
|
Q5E5J8
|
UBIG_ALIF1
|
3-demethylubiquinone 3-O-methyltransferase
|
Aliivibrio
|
MTQQLNVDPAEIKKFEDMASRWWDLEGEFKPLHQINPLRLNYVLENANGLFGKKVLDVGCGGGILAESMAKQGADVIGLDMGKEPLTVARLHALETGTKLEYVQSTAEQHAEENPETYDVVTCMEMLEHVPDPLSVIRSCAKMVKPGGHVFFSTLNRNIKSYLFAIVGAEQLLKLVPKGTHDHNKFIRPSELLKMLDQTALQERGITGLHYNPLTDTYSLGKNVDVNYIVHTTL
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
Q5E5J8
|
A7MQL7
|
UBIE_CROS8
|
Demethylmenaquinone methyltransferase
|
Cronobacter
|
MVEDSQDTTHFGFQTVAKEQKADMVAQVFHSVAAKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQKVLDLAGGTGDLTAKFSRLVGESGKVVLADINDSMLKMGREKLRNIGIVGNVEYVQANAEALPFPDNTFDCITISFGLRNVTDKEKALRSMFRVLKPGGRLLVLEFSKPVFEPLNKAYDAYSFHILPRVGELVAKDAGSYRYLAESIRMHPDQETLKAMMNDAGFENVNYYNMTGGIVALHRGYKF
|
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
|
A7MQL7
|
Q4UK98
|
YBEY_RICFE
|
Endoribonuclease YbeY
|
spotted fever group
|
MINVEIIKNYDKWREHKQINKSLIKKITQNVLLRFDNFSKIKQFELSILLTNTAEILTLNKQFRNIEKATNVLSFPSNELNWQDLYSKLEFLGDSDYIHLGDIAFCYEVIYNESCEQQKNFENHFIHLLIHSILHLIGFDHQNDTEANIMENLEIEILSYFGISSPY
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q4UK98
|
Q07UH0
|
TRPA_RHOP5
|
Tryptophan synthase alpha chain
|
Rhodopseudomonas
|
MTTRLDSRFADLKKQGRAAFVTFLMAGDPDLDTSLKLLQALPKAGADIIEIGMPFTDPMADGPAIQAAGLRALKAGTTLQKTLELVRAFRKADDATPLVLMGYYNPIYIYGVEPFLIDAKAAGVDGLIIVDLPPEEDAELCLPAIKAGLNFIRLATPTTDDKRLPAVLANTSGFVYYVSVTGITGAASADASAVSAAVTRIKRHTPLPVCVGFGIRTPEGARDIARHADGAVVGSALVDVLSRSLDAEGRATAATVPAVADLVASLARGVHGAAQAAE
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
Q07UH0
|
A4G912
|
Y2885_HERAR
|
Nucleotide-binding protein HEAR2885
|
Herminiimonas
|
MRIILITGISGSGKSVGLKALEDAGYFCVDNLPPTLLRALVTERLEEHGTTLAVSMDVRSASSLIGLPADLAWLRSQGHDVKVLFLTAKTDSLIARFSETRRSHPLSHRGFASDSTAERRTLTECIHEEREMLAGIEEIGHVIDTSGMRANKLRAWIKGLVESDHSPLTILFESFAFKFGVPLDADLVFDVRTLPNPHYDEALRPLTGRDAPVQDFLQTQPDATALLADIRGFVEKWLPAFKNDNRGYLTVAIGCTGGQHRSVYIVEQLAQYFRPTEHVLVRHRELD
|
Displays ATPase and GTPase activities.
|
A4G912
|
O49939
|
TLP40_SPIOL
|
40 kDa thylakoid lumen rotamase
|
Spinacia
|
MSSFINHHFYPSVCTSKHALPINPTSPFYLGIPNFRQKSRFMHLTPRCFSRQIDPLDKQKKRSFSVKECAISLALAAALISGVPSLSWERHAEALTSPVLPDLAVLISGPPIKDPEALLRYALPIDNKAIREVQKPLEDITESLRVLGLKALDSVERNLKQASRALKNGKSLIIAGLAESKKDRGVELLDKLEAGMGELQQIVENRNREGVAPKQRELLQYVGSVEEDMVDGFPYEVPEEYQTMPLLKGRAVVEMKVKVKDNPNVDNCVFRIVLDGYNAPVTAGNFLDLVERHFYDGMEIQRRDGFVVQTGDPEGPAEGFIDPSTEKPRTIPLEIMVEGEKVPVYGSTLEELGLYKAQTKLPFNAFGTMAMAREEFENNSGSSQIFWLLKESELTPSNANILDGRYAVFGYVTDNQDYLADLKVGDVIESVQAVSGVDNLVNPTYKIAG
|
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Has a regulatory effect on thylakoid protein phosphorylation.
|
O49939
|
V9QEI7
|
TXA2_LATHE
|
Latrodectin-2
|
Latrodectus
|
MLKLICIAFLVTVLTLVAGEDSLDPAEYGCADDINQEDLLKKNDVCLQCEDLHKEGVVFSLCKTNCFTTQYFTNCVKDLEEAEKEPPE
|
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
|
V9QEI7
|
B1KHE6
|
UPPP_SHEWM
|
Undecaprenyl pyrophosphate phosphatase
|
Shewanella
|
MDTFQVIILALIQGLTEFLPISSSAHLILPSQILGWEDQGLAFDVAVHIGSLLAVVLYFRKEVVSLLTSWLASIFKGQKSDDSKLAWWIILATLPAVILGFALKDMIEVYLRGPGVIAITTVLFGLLLWWADRMSRCELTEYQTGWKKALLIGFAQALALIPGTSRSGATITAALMLGLNREAAARFSFLMSIPVILGAAILMSKDLFESGHVIDYSSLALGVGVSFVAAYTCIHLFLKIISRMGMTPFVIYRLALGALLCAFIFM
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
B1KHE6
|
P37804
|
TAGL_MOUSE
|
Smooth muscle protein 22-alpha
|
Mus
|
MANKGPSYGMSREVQSKIEKKYDEELEERLVEWIVVQCGPDVGRPDRGRLGFQVWLKNGVILSKLVNSLYPEGSKPVKVPENPPSMVFKQMEQVAQFLKAAEDYGVIKTDMFQTVDLYEGKDMAAVQRTLMALGSLAVTKNDGNYRGDPNWFMKKAQEHKRDFTDSQLQEGKHVIGLQMGSNRGASQAGMTGYGRPRQIIS
|
Actin cross-linking/gelling protein.
|
P37804
|
B2HYZ7
|
TRMA_ACIBC
|
tmRNA (uracil(341)-C(5))-methyltransferase
|
Acinetobacter calcoaceticus/baumannii complex
|
MTSSYHQQLQAKIDRITTQFSEFTPPTLEVFESPEQHFRMRAEFRIWHTENDMFYAMFERNDDGKQKTVVRIDEFPIADKSINDLMPLLLAELKANSLLSQRLFEVDFLATLSGEMLVTLIYHRKLNQEWEQEAKALAEKLNIKIMGRSRGQKIVIGDDFVVEEFELLNRSFKYKQIESSFTQPNAQVCKKMLQWACDAAEGSKKHLLELYCGNGNFTLPLSLKFERVLATELAKSSVYAAQWNIEQNQIDNIQVARLSAEEFTQAYQGEREFRRLQEADIDIQSYDFDTVFVDPPRAGIDDETLKLLQSFERIIYISCNPNTLYENLKTLTQTHRVTKFALFDQFPYTHHVESGVLLEKI
|
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
|
B2HYZ7
|
Q46X09
|
ZAPD_CUPPJ
|
Z ring-associated protein D
|
Cupriavidus
|
MILYEYPFNERIRTLLRLEDLFDRLDYFLGQEHPLQHHVALTTLFEIIDVAGRADLKTDLIKELERQRQALTALRVNPQIDQEALDAIIGEIEQGIAMLNQTVGKAGQLLTDNEWLTSIRSRAIIPGGTCEFDLPAYYAWQHRPAEERRADILKWARPLVALRAGTSTVLRLLRESGQSGKVIATGGSYQQMLSGRSYQLMQVHLDDSLLAFIPEMSANKYMLWVRFTQQDGDLRPRSVDADIPFLLKLCNF
|
Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.
|
Q46X09
|
B0TLV0
|
TIG_SHEHH
|
PPIase
|
Shewanella
|
MQVSVETTQGLERRLTISVPAEQIENTVKEALKSEAKRARIPGFRPGKVPVSVINKRYGNAIRQDITGEVMQRNFIEAIIAEKLNPAGAPTFTPGSTEGENFEFVATFEIYPEVELKGLESITVEQPTAEVTEADVDSMIETLRNQHATFEVAERAAAEGDKAKINFVGSIDGEEFEGGKADDFELQLGSGRMIPGFESGVEGHKAGEEFNIEVTFPEDYHAENLKGKVATFAITLNEVQAANLPEVNDEFATLFGITEGGIDALRGEISKNMSRELEQALKANVKEQVLNGLVEQNDIELPAALIDGEVEVLRKQAMQRFGDQAANMPELPADLFTEQAARRVKVGLLLGEVIKANELKAEDERVQALIASMASAYEDPSEVVAYYNGNEELMQNMRNVALEEQAVEALLKTATLTEKAVNFEEFMNKATGRA
|
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.
|
B0TLV0
|
A8YUD6
|
Y732_LACH4
|
Nucleotide-binding protein lhv_0732
|
Lactobacillus
|
MADDKKQLLIVTGMSGAGKTVVAHDLEDMGYFVVDNLPPTLLGSFWDYNSNDFHKVAVVIDLRVKTFYTDLLDEVNSLEDNGNVQATILFLDASDDVLVARYKETRRLPPLANNGKGRLLDGIQEERRILMPIKNRSNYIINTSNLSTKDLKQKLINTFSDRKRQPFSIEVMSFGFKYGMPIDADIVMDVRFLPNPFYIPELRPFTGLDKRVFDYVMNKKETQVFYQKLLDLLETAIPGYIKEGKEKLTIAIGCTGGQHRSVSIAQQLARDLSKKYPVDITHREVSRYIRK
|
Displays ATPase and GTPase activities.
|
A8YUD6
|
O87008
|
TFTC_BURCE
|
Two component enzyme C
|
Burkholderia cepacia complex
|
MHAGEAVQQLKKAFETVASFDFRDALSKASTPVTVVATNGPFGLAGLTCSAVCSVCDRPPTVLLCINRKSYAAGIIKSNGVLSVNWLAAGQAVISQTFAGVGSVPMEERFADKGWQTIATGAPYRMDAAVSFDCTIANIVDVGSHSVIFAEVVARNHAEECTPLIYHRRQYATTRSLAE
|
Reductase component of a two-component system that degrades 2,4,5-trichlorophenol. TftC provides the FADH(2) required by TftD. TftD oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.
|
O87008
|
O82629
|
VATG2_ARATH
|
Vacuolar proton pump subunit G2
|
Arabidopsis
|
MESAGIQQLLAAEREAQQIVNAARTAKMTRLKQAKEEAETEVAEHKTSTEQGFQRKLEATSGDSGANVKRLEQETDAKIEQLKNEATRISKDVVDMLLKNVTTVNN
|
Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
|
O82629
|
Q7WFF3
|
UREF_BORBR
|
Urease accessory protein UreF
|
Bordetella
|
MHLSSPALPIGGFSYSQGLEAAIELGLVHDEASTLAWIESQLVTVMARAEAPLWCLLFEAWRAGDDAAAHGWNQWFHASRETRELRQETEQMGRSLARLAQELGWGTAATRAAVAALRPATLPAVHACACAMWALPREAGLGAYVFSWLENQVAAAIKGVPLGQMAGQRMLERLRAGLPAVLADARARAGATPPRLDTFAPQYAMVSARHETQFSRLFRS
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q7WFF3
|
P12887
|
UNG_YEAST
|
Uracil-DNA glycosylase
|
Saccharomyces
|
MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTETKAVAKEANTDKYPANSNAKDVYSKNLSSNLRTLLSLELETIDDSWFPHLMDEFKKPYFVKLKQFVTKEQADHTVFPPAKDIYSWTRLTPFNKVKVVIIGQDPYHNFNQAHGLAFSVKPPTPAPPSLKNIYKELKQEYPDFVEDNKVGDLTHWASQGVLLLNTSLTVRAHNANSHSKHGWETFTKRVVQLLIQDREADGKSLVFLLWGNNAIKLVESLLGSTSVGSGSKYPNIMVMKSVHPSPLSASRGFFGTNHFKMINDWLYNTRGEKMIDWSVVPGTSLREVQEANARLESESKDP
|
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Not involved in strand-directed mismatch repair.
|
P12887
|
P87156
|
TSR4_SCHPO
|
Probable 20S rRNA accumulation protein 4
|
Schizosaccharomyces
|
MSQKWVQTQAWLGFPDVPISQEDKPDEYSTFLGGFPVFFDGCSLNPNIIKCGNCKNLCRLLLQCYAPLEGDNLKERALYVWGCHNPSCRRVPNSIVCVRGVRLPLKSDIEAVKSPKAISHLEEKKSSPKEKKVNPFAITSESSRGLNPFSDATSANNPFSLSTDVNPSKPSSNVFSKPSFAAKAQQSITDQQKTQAKTKTKHIALTTSGMSVHPPVTETYTYPVTEAFQGMFLGLDLEYVPQNKVNSKKDDFSTFKNYTPYLNDSSEAWEKESYEKSPSVYEKTFRLFSEKISHNPTQCLRYERGGTPLLASGRDKLGQQLKSVTNFGKSPVPLCPLCKSPRLFEMQLMPHAISILNDEIAEWSTILVATCSMDCNPPINKDRVGYAVEWVGIQWD
|
Required for processing of the 20S pre-rRNA at site D to generate mature 18S rRNA.
|
P87156
|
Q2ND30
|
TATA_ERYLH
|
Sec-independent protein translocase protein TatA
|
Erythrobacter
|
MGQIGIWQILIIALVILVLFGRGKISDMMGDFGKGVSSFKKGLNEEDKPAEPAAKIEGPSHEAKPAGEAAKDPRPADKQG
|
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.
|
Q2ND30
|
Q9H9P5
|
UNKL_HUMAN
|
Zinc finger CCCH domain-containing protein 5-like
|
Homo
|
MPSVSKAAAAALSGSPPQTEKPTHYRYLKEFRTEQCPLFSQHKCAQHRPFTCFHWHFLNQRRRRPLRRRDGTFNYSPDVYCSKYNEATGVCPDGDECPYLHRTTGDTERKYHLRYYKTGTCIHETDARGHCVKNGLHCAFAHGPLDLRPPVCDVRELQAQEALQNGQLGGGEGVPDLQPGVLASQAMIEKILSEDPRWQDANFVLGSYKTEQCPKPPRLCRQGYACPHYHNSRDRRRNPRRFQYRSTPCPSVKHGDEWGEPSRCDGGDGCQYCHSRTEQQFHPESTKCNDMRQTGYCPRGPFCAFAHVEKSLGMVNEWGCHDLHLTSPSSTGSGQPGNAKRRDSPAEGGPRGSEQDSKQNHLAVFAAVHPPAPSVSSSVASSLASSAGSGSSSPTALPAPPARALPLGPASSTVEAVLGSALDLHLSNVNIASLEKDLEEQDGHDLGAAGPRSLAGSAPVAIPGSLPRAPSLHSPSSASTSPLGSLSQPLPGPVGSSAMTPPQQPPPLRSEPGTLGSAASSYSPLGLNGVPGSIWDFVSGSFSPSPSPILSAGPPSSSSASPNGAELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVIFQLRAKQCVACRERAHGAVLRPCQHHILCEPCAATAPECPYCKGQPLQW
|
May participate in a protein complex showing an E3 ligase activity regulated by RAC1. Ubiquitination is directed towards itself and possibly other substrates, such as SMARCD2/BAF60b. Intrinsic E3 ligase activity has not been proven.
|
Q9H9P5
|
Q8RKI9
|
TARI_BACSH
|
Ribitol-5-phosphate cytidylyltransferase
|
Bacillus
|
MIYAEILAGGKGSRMGNVNMPKQFLPLNKRPIIIHTVEKFLLNDRFDKILIVSPKEWINHTKDILKKFIGQDDRLVVVEGGSDRNESIMSGIRYIEKEFGIQDNDVIITHDSVRPFLTHRIIDENIDAVLQYGAVDTVISAIDTIIASEDQEFISDIPVRDNMYQGQTPQSFRISKLVELYNKLSDEQKAVLTDACKICSLAGEKVKLVRGEVFNIKVTTPYDLKVANAILQERISQ
|
Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate.
|
Q8RKI9
|
A9ILJ7
|
TRUA_BART1
|
tRNA-uridine isomerase I
|
Bartonella
|
MSRFKLTLEYDGSNYAGWQRQAKLHTIQGALEQAIFRFSGQQLTITTAGRTDAGVHATGQVAHVDFIKNWPPHTVRDALNALLRQQSEAISILNVENVPDDFDARFSAIKRHYLFKILNRRSPPALNAKRVWWIPKPLNAQAMHEAAQKLVGQHDFTTFRSAHCQAKSPIRTLERLDIQKEGEEIFIYAKARSFLHHQIRSFAGSLMEVGIGRWTAQDLEAALHAKDRKRCGVVAPPSGLYLTKVEY
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
A9ILJ7
|
Q9SRS3
|
YMG11_ARATH
|
YGGT family protein YLMG1-1
|
Arabidopsis
|
MAAITALTLRSPVYLPSSATSPRFHGFTNQPPPARLFFPLNPFPSLSIQNPKSIRISASASPITTPILQTEKSTARSSTLTGSTRSLATLAALAIAVTRVLAQKLSLAIQTSSPVIADGLRFSLSTAGPVFFASLRDRPPGYLNTPLTVVAVGIKKWLDIYSGVLMVRVLLSWFPNIPWERQPLSAIRDLCDPYLNLFRNIIPPIFDTLDVSPLLAFAVLGTLGSIVHGSTG
|
Required for the proper distribution of nucleoids in chloroplasts. The nucleoid partitioning by YLMG1-1 may be related to chloroplast division processes.
|
Q9SRS3
|
Q9A3H4
|
TOLB_CAUVC
|
Tol-Pal system protein TolB
|
Caulobacter
|
MRLRALLLMVAALLSGAAFVTPAAAQIEVDINAGAVKPLPIAIPVFSGSTRGAEIAQVITGNLERSGLFQPLNVAGVPDKLADVNVQPRFPDWQSTGAQALINGQVTVGADGGLRVDFRLWDVFSQQQLLGLQFSSTPDNWRRVAHKISDAVYERLTGEKGYFDTRVAFVAESGPKLNRIKRLAIMDQDGANPQYLTDGSYIVMTPRFSSTSQELTYMALRPTGSSIYLLNLETSRQETVGKFPGMVFAPRFSPDGSKVAFSVERNGNSDIYVMDLRSRATTRITTDPAIDTSPSFSPDGTKIVFNSDRGGQAQIYVMNTDGSGVRRISYGGGRYTTPVWSPRGDFIAFTKQTGGEFHIGVMRADGGDERLLTTSYLDEGPTWAPNGRVLMFFREGPSGNPRLWTVDITGRILRPAAYSGSASDPAWSPLLD
|
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.
|
Q9A3H4
|
E7FH11
|
ZD18A_DANRE
|
Zinc finger DHHC domain-containing protein 18-A
|
Danio
|
MKNCEYQQIDPRALRTPSSRTSSTLPCGRKGSQRLRRKWEVFPGKNRFYCDGRIMLARQCGVLPLTIGLIFITSVLFFTFDCPFLVDHLTVFIPVIGGVLFIFVVISLLQTSFTDPGILPRALPDEAADIEKQIDNSGSSTYRPPPRTKEILINDQVVKLKYCFTCKMFRPPRTSHCSLCDNCVERFDHHCPWVGNCVGKRNYRFFYAFIVSLSFLTSFIFGCVITHLTLRSQGGNGFIQAIQDSPASVVELVICFFSIWSILGLSGFHTYLVASNLTTNEDIKGSWSSKRGEESGNPYTYNNIFTNCCVVLCGPMPPSLIDRRGFVPPEDAPQTVTSDAELPAFMAKNDTNMCAQGTKELLESMANSTVIQSTCAPGKPKTAPVTQESLLNTVSITVSPPSKPPSNGCSGRQARRPIDVPCSQRGLKRAALHTHKPMLRLPSPLYSLSDSPLILSDAPDMGFIPLN
|
Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates, such as CGAS, HRAS and LCK.
|
E7FH11
|
Q02ZN8
|
Y1047_LACLS
|
Nucleotide-binding protein LACR_1047
|
Lactococcus cremoris subsp. cremoris
|
MDNKLNIVIITGMSGAGKTVAIQSFEDMGYFTVDNMPPNLIEKFVGLLNTPDNKIDKVALVVDMRSRAFFEDIQSIVTELTDNTSVNFKLLFLDANDTELVSRYKETRRSHPLAIDGRTLDGITKEREILADLKNLSEVVIDTSELTPRNLRARILQKFATSTESTFRIEVMSFGFKYGLPLDADLVFDVRFLPNPHYISELRDKNGTDQEVYDYVMEHPQSEEFYQNLMKMLVPILPAYKKEGKSVLTIAFGCTGGQHRSVAFAERVSAALREKWHLNVSHRDKDRRKETVNRS
|
Displays ATPase and GTPase activities.
|
Q02ZN8
|
Q40285
|
UFOG2_MANES
|
UDP-glucose flavonoid 3-O-glucosyltransferase 2
|
Manihot
|
FCTPMMDLADEFGIPSYIFFASGGGFLGFMLYVQKIHDEENFNPIEFKDSDTELIVPSLVNPFPTRILPSSILNKERFGQLLAIAKKFRQAKGIIVNTFLELESRAIESFKVPPLYHVGPILDVKSDGRNTHPEIMQWLDDQPEGSVVFLCFGSMGSFSEDQLKEIAYALENSGHRFLWSIRRPPPPDKIASPTDYEDPRDVLPEGFLERTVAVGKVIGWAPQVAVLAHPAIGGFVSHCGWNSVLESLWFGVPIATWPMYAEQQFNAFEMVVELGLGVEIDMGYRKESGIIVNSDKIERAIRKLMENSDEKRKKVKEMREKSKMALIDGGSSFISLGDFIKDAMEG
|
In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments.
|
Q40285
|
P28117
|
WNT5A_PLESK
|
Protein Wnt-5a
|
Plestiodon
|
SGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMKLNPRGKLVQVNSRFNAPTIHDLVYIDPSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQTERCHCKF
|
Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. Required during embryogenesis for extension of the primary anterior-posterior axis.
|
P28117
|
P18731
|
ZG62_XENLA
|
Gastrula zinc finger protein XlCGF62.1
|
Xenopus
|
IPEKPFICTECGKCFSEKRTLKHHIRTHTGEKPFICTDCGKCFSFEICLNRHYKTHTRERPFICTECGKSFSDKSRLRVHHRSHTGEKPFTCTDCGKCFSVKSILNHHRQAIHSGEKPFICTECGKGFASKHYLHGHKRTHTGEKPFVCTECGKGFASNYYLHVHKRTH
|
May be involved in transcriptional regulation.
|
P18731
|
Q8TAW3
|
ZN671_HUMAN
|
Zinc finger protein 671
|
Homo
|
MLSPVSRDASDALQGRKCLRPRSRRLPLPAAVRAHGPMAELTDSARGCVVFEDVFVYFSREEWELLDDAQRLLYHDVMLENFALLASLGIAFSRSRAVMKLERGEEPWVYDQVDMTSATEREAQRGLRPGCWHGVEDEEVSSEQSIFVAGVSEVRTLMAELESHPCDICGPILKDTLHLAKYHGGKARQKPYLCGACGKQFWFSTDFDQHQNQPNGGKLFPRKEGRDSVKSCRVHVPEKTLTCGKGRRDFSATSGLLQHQASLSSMKPHKSTKLVSGFLMGQRYHRCGECGKAFTRKDTLARHQRIHTGERPYECNECGKFFSQSYDLFKHQTVHTGERPYECSECGKFFRQISGLIEHRRVHTGERLYQCGKCGKFFSSKSNLIRHQEVHTGARPYVCSECGKEFSRKHTLVLHQRTHTGERPYECSECGKAFSQSSHLNVHWRIHSSDYECSRCGKAFSCISKLIQHQKVHSGEKPYECSKCGKAFTQRPNLIRHWKVHTGERPYVCSECGREFIRKQTLVLHQRVHAGEKL
|
May be involved in transcriptional regulation.
|
Q8TAW3
|
Q9JKT8
|
TR114_RAT
|
Taste receptor type 2 member 5
|
Rattus
|
MLGAMEGVLLSVATSEALLGIVGNTFIALVNCMDCTRNKNLYNIGFILTGLAISRICLVWILITEAYIKIFSPQLLSPINIIELISYLWIITSQLNVWFATSLSIFYFLKIANFSHHIFLWLKRRINIVFAFLIGCLLMSWLFSFPVVVKMVKDKKMLYINSSWQIHMKKSELIINYVFTNGGVFLLFIIMLIVCFLLIISLWRHSKWMQSNESGFRDLNTEVHVKTIKVLLSFIILFILHLIGITINVICLLVPENNLLFVFGLTIAFLYPCCHSLILILANSRLKRCFVRILQQLMCSEEGKEFRNT
|
Putative taste receptor which may play a role in the perception of bitterness.
|
Q9JKT8
|
Q8GZ79
|
TI201_ARATH
|
Translocon at the inner envelope membrane of chloroplasts 20-I
|
Arabidopsis
|
MITGYSTPSAHVLMSSRAFKSSSYRAAAGQTQHYLARSSLPVVKNSWGSPPSPFNELPRVSRGVPLSYLSASSSLLLNGEQGSLSGTLPVLPVRRKTLLTPRASKDVPSSFRFPPMTKKPQWWWRTLACLPYLMPLHETWMYAETAYHLHPFLEDFEFLTYPFLGAIGRLPSWFLMAYFFVAYLGIVRRKEWPHFFRFHVVMGMLLEIALQVIGTVSKWMPLGVYWGKFGMHFWTAVAFAYLFTVLESIRCALAGMYADIPFVCDAAYIQIPYD
|
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. Seems to be specific for photosynthesis-related pre-proteins. Partially redundant with TIC20-IV, but not with TIC20-II or TIC20-V.
|
Q8GZ79
|
Q5AY46
|
XPTA_EMENI
|
Xanthone prenyltransferase A
|
Aspergillus subgen. Nidulantes
|
MLKHSSAATKENDSPKLKVLDIVSKLEPSLDHSHTHWWKLTSPQLALMLEAADYSIEKQFETLLFHYHWVVPYLGPKPDADGNFKWRSLVSDVGIPLEYSWKWDTATSGPDVRLTIEPINELSGTRVDPLNQAPSLELLHRLAEILPRLDVSWASHFLSTFYDHDKLKYIKESESETGMPLRSTMLVCFEFGRNGITTKTYMSPRKLGQQGFAPLSDYHSAIAALGPSCALDAVTEFLNNSPEGPHLSPFMLAVDNIIPCSSRLKLYFATPRTSYNSIREVLTLGGRLSTVTLESKLRAIHELVKAIMPFPPDLPDDADIPFPEQVLSPTVQDLAESSDMANQRPAFVAGYQYYFDIAPGASLPDIKFYIPIRKAQMNDQAVATGLTNWMRAQGRGAFCNAYTRVLEGLAGGRDLSKCHGLHTHICVMLKGNGEFDVTSYLAPGCK
|
Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone . Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB . XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring . Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC .
|
Q5AY46
|
O49901
|
ZDS_NARPS
|
Carotene 7,8-desaturase
|
Narcissus
|
MASSTCLIHSSSFGVGGKKVKMNTMIRSKLFSIRSALDTKVSDMSVNAPKGLFPPEPEHYRGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRQFIGGKVGSFVDKRGNHIEMGLHVFFGCYNNLFRLMKKVGADENLLVKDHTHTFVNRGGEIGELDFRLPMGAPLHGIRAFLTTNQLKPYDKARNAVALALSPVVRALIDPNGAMQDIRNLDNISFSDWFLSKGGTRMSIQRMWDPVAYALGFIDCDNISARCMLTIFSLFATKTEASLLRMLKGSPDVYLSGPIRKYITDKGGRFHLRWGCREILYDELSNGDTYITGIAMSKATNKKLVKADVYVAACDVPGIKRLIPSEWREWDLFDNIYKLVGVPVVTVQLRYNGWVTEMQDLEKSRQLRAAVGLDNLLYTPDADFSCFSDLALSSPEDYYIEGQGSLIQAVLTPGDPYMPLPNDAIIERVRKQVLDLFPSSQGLEVLWSSVVKIGQSLYREGPGKDPFRPDQKTPVKNFFLAGSYTKQDYIDSMEGATLSGRQAAAYICSAGEDLAALRKKIAADHPEQLINKDSNVSDELSLV
|
Catalyzes the conversion of zeta-carotene to lycopene via the intermediary of neurosporene. It carries out two consecutive desaturations (introduction of double bonds) at positions C-7 and C-7'.
|
O49901
|
Q852F6
|
ZIP2_ORYSJ
|
ZRT/IRT-like protein 2
|
Oryza sativa
|
MAGGRGARASLHLHLAWLCAFATTAWAHGGGGGGGDSDADADGGGEGKPDLRARGLVAAKLWCLAVVFAGTLAGGVSPYFMRWNDAFLALGTQFAGGVFLGTAMMHFLADANETFADLLPGTAYPFAFMLACAGYVLTMLADCAISFVVARGGGRTEPAAAAGAGLEEGKLSSTNGNASDPPAADAAAQDHSVASMLRNASTLGDSVLLIAALCFHSVFEGIAIGVAETKADAWKALWTISLHKIFAAIAMGIALLRMLPDRPFLSCFGYAFAFAVSSPVGVGIGIVIDATTQGRVADWIFAVSMGLATGIFIYVSINHLLSKGYTPLRPVAADTPAGRLLAVVLGVAVIAVVMIWDT
|
Zinc transporter that may be involved in zinc uptake from the rhizosphere.
|
Q852F6
|
Q8K2R5
|
ZN668_MOUSE
|
Zinc finger protein 668
|
Mus
|
MEVEATEARSPGPCYKRSGRRYKCLFCTKTFPNAPRAARHAATHTPTDCTEEVREAQPKVDTEPKAEEASGDKVSASVAKPRPYACPLCPKAYKTAPELRSHGRSHTGEKPFPCPECGRRFMQPVCLRVHLASHAGELPFRCTHCPKAYGTLSKLKIHQRGHTGERPYACPDCGKSFADPSVFRKHRRTHAGLRPYSCERCGKAYAELKDLRNHERSHTGERPFLCSECGKSFSRSSSLTCHQRIHAAQKPYRCPACGKGFTQLSSYQSHERTHSGEKPFLCPRCGRMFSDPSSFRRHQRAHEGVKPYRCEKCGKDFRQPADLAMHRRVHTGDRPFKCLQCDKTFVASWDLKRHALVHSGQRPFRCEECGRAFAERASLTKHSRMHSGERPFHCNACGKSFVVLSSLRKHERTHRSNETTGAAPQQELVLGLALPVGVVGEGSAAPVAGAGVGDAPAGLLGLPPESGGVVATQWQVVGMTVEHVECQDAGVGEAPSTLGDAGEVGGEETDEKPPQFVCRECKETFSTLTLLRRHERSHPELRPFPCTQCGKSFSDRAGLRKHSRTHSSVRPYSCSQCPKAFLSASDLRKHERTHPVPIGTPIPLEPLVALLGMPEEGSA
|
May be involved in transcriptional regulation.
|
Q8K2R5
|
A1WXU9
|
TRUB_HALHL
|
tRNA-uridine isomerase
|
Halorhodospira
|
MAKRRGGRNVTGVLLFDKPAGVTSNKALQQVKRLFGARKAGHTGSLDPLATGLLPICFGDATKVSGFLLDADKRYVVTCKLGVATDTGDAEGTERDRAEVPALDEEAVERGLTGFRGPIDQLPPMYSAIKHQGQRLYDLARQGVEVEREPRRVEIYDLQLVAVRGDELELSVHCSKGTYIRTLAEDIAQALGTVGHVCALRRLGLGPYQDPAMWTEEMLAARAEQGREALDATLLPMDSALQQYTGVELADDLAYFVVQGQPVFVPKAPSEGWLRLYDRGGNFLGMGQALDDGRIGPKRLVARR
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
A1WXU9
|
P42723
|
TFXA_RHILT
|
Trifolitoxin
|
Rhizobium
|
MDNKVAKNVEVKKGSIKATFKAAVLKSKTKVDIGGSRQGCVA
|
Antibiotic whose production provides the bacterium a mechanism of host root nodule competitiveness with other invading inefficient strains.
|
P42723
|
Q3KBQ0
|
UVRC_PSEPF
|
Excinuclease ABC subunit C
|
Pseudomonas
|
MTEAFDSGAFLSTVSGRPGVYRMFDSDARLLYVGKAKSLKKRLASYFRKTGLAPKTAALVGRIAQVETTITSNETEALLLEQTLIKEWRPPYNILLRDDKSYPYVFLSDGQFPRLSIHRGAKKAKGKYFGPYPSAGAIRESLSLLQKTFFVRQCEDSYYKNRTRPCLQYQIKRCKAPCVGLVEPEVYAEDVRHSVMFLEGRSHALTNELSTAMEEAAINLEFERAAELRDQIALLRRVQDQQSMEGGTGDIDVIAAFVNPGGACVHLISVRGGRVLGSKNFFPQVGIEEEVAEVMAAFLGQYFISSPERDLPSELIVNVVHEDFPALIEAIQALRGRELSISHRVRGTRARWQQLAVTNAEQALGARLANRQHVAARFEALAEVLNLDEPPQRLECYDISHSSGEATVASCVVFGPEGAIKSDYRRYNIEGVTAGDDYAAMHQALTRRFSKLKEGEGKLPDILLVDGGKGQLSMARDVLNELAVPDLILLGVAKGATRKAGFETLYLNDAANEFTLRGDSPALHLIQQIRDEAHRFAITGHRARRGKTRRTSTLEGVAGVGPTRRRDLLKHFGGLQELSRASIEEIAKAPGISKKLAESIYANLHSE
|
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.
|
Q3KBQ0
|
Q9CJ72
|
YIDC1_LACLA
|
Membrane protein YidC 1
|
Lactococcus
|
MKKKFSLIAMAGAALLLLTACGTTAVTSSSTNLWDQIVYGFAQVIRFLSFGGLTGVGIILFTIVIRAALLPLMNIQIKSSQRMQEIQPEIKKIQAKYPSKDMESRRLMNEEIQKLYAENKVNPYMGCLPLVVQMPVLWALYQALSRVDFLKHGTFLWFEIGAKDPTFILPILAAVFTFLSSYLMMKSAPERNAMTTSMTYIMPIFILIMGVNFAAGIALYWVISNAFQVFQTMLLANPYKIIAAREAKVQVEKDKIKAREKALKKARKK
|
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.
|
Q9CJ72
|
A3PFL1
|
UBIE_CERS1
|
Demethylmenaquinone methyltransferase
|
Cereibacter
|
MSDETSNTTHFGFRTVPEGEKAGMVHGVFTRVASKYDIMNDLMSGGVHRLWKDAMMDWLAPRPGQKLLDVAGGTGDISFRFLKRAPGAEATVCDMTESMLVEGRQRADAAQMADRLDWVVGDAMALPFASNTFDVYTISFGIRNVTRVQDALNEAYRVLKPGGRLMVLEFSQLPNPMMQWAYDRYSFNVIPVMGQIVANDRDSYQYLVESIRKFPDQETFADMIRKAGFGLVKYRNLSLGIAALHSGWKI
|
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
|
A3PFL1
|
Q97FT6
|
TIG_CLOAB
|
PPIase
|
Clostridium
|
MNSKMEKLEKNVIKFEITVDESKFNEAVIKSYNKNRRRFNVPGFRKGKAPLNIIKNYYGVGVLYEDAINFCIDDTYPEVIKENDIHPVAYPEIDIVTLEEGKDFVYTAKVTVKPEVELGEYKGVEVTKVEYPVTDEDVENELKGMQEKNARIELKEDGEAVEKGDIAVIDFKGYVDDVAFEGGEGKDYSLEIGSGTFIDNFEDQLVGLKKDESKDVNVKFPEEYGKEELNGKPAKFEVTIKEIKRKELPALDDEFAKEVSEFDTLDEVKADIRSKMEKANEEKAKIEFEDKVVDAAVENAKIEIPEVMVKNETDQMLKELESRLRYQGLDLKSYYEYTNSSEEKVRDYMKETADKRVRTKLVMEKISEVEKVEATEEELKEKAKEMAQQYTNKDLDKMAELVLNSQRSMIEQDVINGKVIDLLVENAKVVE
|
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.
|
Q97FT6
|
Q8NIH0
|
TRI5_FUSAU
|
Sesquiterpene cyclase
|
Fusarium
|
MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQMLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPHPAMLNYFDDLQAGREQSHPWWALVNEHFPNVLRHFGPFCSLNLIRSTMDFFEGCWIEQYNFGGFPGSDDYPQFLRRMNGLGHCVGASLWPKDLFDERKNFLEITTAVAQMENWMVWVNDLMSFYKEFDDERDQISLVKNFVTCHEITLDEALEKLTQETLHSSKQMVAVFADKDPQVMDTIECFMHGYVTWHLCDARYRLHEIYEKVKDQDTEDAKKFCKFFEQAANVGAVAPSEWAYPQVAQLANVRAKDDMKEAHKPILSSIELVE
|
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.
|
Q8NIH0
|
P09163
|
YJAB_ECOLI
|
KAT
|
Escherichia
|
MVISIRRSRHEEGEELVAIWCRSVDATHDFLSAEYRTELEDLVRSFLPEAPLWVAVNERDQPVGFMLLSGQHMDALFIDPDVRGCGVGRVLVEHALSMAPELTTNVNEQNEQAVGFYKKVGFKVTGRSEVDDLGKPYPLLNLAYVGA
|
N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins . Binds acetyl-CoA .
|
P09163
|
B8DWC0
|
TILS_BIFA0
|
tRNA(Ile)-lysidine synthetase
|
Bifidobacterium
|
MAYSAAMKAAIGEMRDVLKAHGLGQQSKEFSAHGEHKPHDDAPFVFVACSGGRDSLALAACAQVVCAAWGIRCGAIIVDHHLQDASHKVAQQTAQTCRDLGLEPVLIVDVQVKERGQGIEAAAREARYAALVGTARRWHATAVLLAHTKDDQAESILIDLIRAAGTDAFAGMPQTQLFDDVLVLRPLLGITRAQTTRICEDEGLEYWDDPTNGDAVPLETALPASYPLRSRVRHDLMPYLSAFAGCDMVDRLARTARIARRDVEALNQEAERALAQTVEFEGNMRDLQADRLADDKLGANIDARALERWPEAIRYRVIARTLAACGLAYASRHVAAVDKLVSQWHGQGKVALPSKYSAKRKAHVIRICEDITHANRRCAKRN
|
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.
|
B8DWC0
|
Q604F8
|
TRPD_METCA
|
Anthranilate phosphoribosyltransferase
|
Methylococcus
|
MEIPEVLETLLAGKDLSPSAMRETMRKIMSGGATPAQIGAFLIALRCKGETVEEVAAAAQVLREMATKVPVSAPHLLDTCGTGGDASKTFNISTTAAFVVAAAGGRVAKHGSRSVSGRSGSADVLEAAGINIELTPDQVKTCIETLGVGFLFAQRHHGAMKYAIGPRRELGVRTLFNLLGPLTNPAGAPNQLVGVYTDPWVEGLARVLQQLGSSHVLVVHAEDGLDEISIAAPTHVAELKNGLITNYYVRPEQFGFRRAALSELAIDTVAASLKMMRGVLDNVPGPARDIVALNAGAAIYAADLTDSLEAGIRRAEAVIADGSARAKLEALAALSRQFAAS
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q604F8
|
Q13DY1
|
TSAD_RHOPS
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Rhodopseudomonas
|
MTSEQTLLVLGIETTCDETAAAVVERRADGSGRILSNIVRSQIDEHAPFGGVVPEIAARAHVDLLDGIVANAMREAGTGFAQLSGVAAAAGPGLIGGVIVGLTTAKAIALVHNTPLIAVNHLEAHALTPRLTDATEFPYCLFLASGGHTQIVAVLGVGDYVRLGTTVDDAIGEAFDKIAKMLGLPYPGGPQVERAAASGDAARFAFPRPMLGRPDANFSLSGLKTAVRNEASRLTPLEPQDINDLCAGFQAAVLDSMADRLGAGLRLFRERFGAPKALVAAGGVAANQAIRRSLREVAAKAQTTLMVPPPALCTDNGAMIAWAGAERLALGLTDTMDAAPRARWLLDANATAPGKFANTRAGF
|
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.
|
Q13DY1
|
Q037U3
|
THIT_LACP3
|
Thiamine ECF transporter S component ThiT
|
Lacticaseibacillus
|
MQQHKQLVVILETAIIAAFAMALTYIPHTTGVSAIELNYGLIPIAVLAMRRGLVPAAWAGFVWGILDLILRGIGGGSVLNPLQGILEYPIAFTLVGLMGLTFASFQKAVRGSEKVKASGYAFAGIIIGTFAKYFIHFIAGVVFWGAYAPKGTNVWVYSLIVNGGSALFSTVLTIVVVGVLLTVAPQLFVAKDGKSFSTKAA
|
Thiamine-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins and transport it into cells. Binds thiamine with a dissociation constant of 0.5 nM. Upon coexpression with its energy-coupling factor (ECF) ABC-transporter complex EcfA1A2T in Lactococcus lactis subsp. cremoris (strain NZ9000) allows thiamine uptake; uptake requires both ThiT and EcfA1A2T.
|
Q037U3
|
Q9VI58
|
TUTT_DROME
|
Terminal uridylyltransferase Tailor
|
Sophophora
|
MRIEPGDSFWTKKAMFSNAERQYFETVRPRKTSLPGSTAPNIAAPVTKATKKNKTMAEMMPNKLLYMNPLTMEAHFFLQTLNSVNQTTNPPQLDPHLANLLERIMVGIESYLDRNPTYVLPQEMAAPGEGVAFVQPQELQTIKRTFSCSSCSNRIVGTTIAKAVAHLSEQHPKPNPNNQPVQPHPTHQTKQEKKQAQVKARQHITVRLPKKARAMIVGEITNVFKDKYPIADKLKVIPEYDVIEQDLCKLLSPGFPKQPLRVYKFGSRITGIGNRSSDLDLFVDIGNTFHTFEHRASNATVAKLRAMRKFFCDSEDWRLINFIEQARVPIIKTCHLPTGIECDICLNSMGFCNTNLLKYIFESQPLTQYMCIYVKNWLERCKLTEQISTYSITLMVIYFLQLQALLPPIAMLQIEDAANQAVLVGPWVVNFAQKSFSELGLQQLKATVPVIKGFLRNFFAYFAKFDYEHFLVCPYIGQANVEIAKIERMLHARYSAYVSDNPECSIQLKKPMVVQDPIQLNHNVTKAVTKYGLQTFVDYCQQTAELLEEPSTNWRQRYAF
|
Uridylyltransferase which mediates terminal uridylation of miRNAs, leading to their degradation. Has high specificity for splicing-derived miRNAs (mirtrons) and other miRNA substrates containing a 3'-G terminal nucleotide. Appears to be a major suppressor of mirtron biogenesis.
|
Q9VI58
|
A1L2S8
|
ZFPL1_XENLA
|
Zinc finger protein-like 1
|
Xenopus
|
MGLCKCPKRKVTNLFCFEHRVNVCEHCLVANHAKCIVQSYLQWLQDSDYNPNCRLCNTLLSSKETARLVCYDLFHWSCLNDLATQQPPNTAPAGYRCPSCQGPVFPPNNLVSPVAATLREKLSTVNWARAGLGLPLIEVAEPVDDTMSHDETDYRDWSVVNSSSDNLSETPETTSQTGYTYNSVAPGAVQQSLNGNMSQDHAVTIRDTGSESVPFNAASSPRKVYDTRENARGQDAVIDFDDDKYRRRPTLNWLARILRNRSGSKSRPASSMQRFLVILIIGVLGFLTLILLMSKLGRASADNDPNLDPLLNPHIHVGKE
|
Required for cis-Golgi integrity and efficient ER to Golgi transport.
|
A1L2S8
|
B9SCB6
|
TPS2_RICCO
|
Probable terpene synthase 2
|
Ricinus
|
MSAQTLAISNLKPNTTRHLASFHPNIWGDRFLSCAAESTDIEDDMEQQVERLKEEVKKMIASADEPSQILNLIDLLQRLGVSYHFEKEIEEALQQVLNMNSDSDKDDDLHSVALRFRLLREQGLNVSCDVFNKFRDRNGHFIQTLKTDLQGMLSLYEAAHFRVHGEGILDDALAFTTTYLESIVPNLSPPLAAQISRTLRQPLRKSLARVEARHFISIYQEDTSHNEVLLTFAKLDFNLLQKLHQKELKYISLWWKDLDFVNKLPFTRDRVVEGYFWILGVYFEPQYHRARKFVTKVINVVSVIDDIYDAYGTLEELVVFTDAINRWDIDCIDQLPEYMKVCYKALLNVYEEIERALSEQGRSYRLHYAKEAMKKLVQAYLVEANWMNKNYVPTMDEYMSIALVSCAYPLLTVTSFVGMGDIATKEVFDWASNDPKIVRVASIICRLMDDIVSHEFEQKRGHIASSVECYMKQNGVSEEATRDEFNKQIVDAWKDINEEHLQPNYVPMPFRTRVVNSARIMDYLYKDDDEYTHVGELMKGSVAALLIDPA
|
Probable sesquiterpene synthase.
|
B9SCB6
|
P06561
|
TRPB_CORGL
|
Tryptophan synthase beta chain
|
Corynebacterium
|
MTEKENLGGSTLLPAYFGEFGGQFVAESLLPALDQLEKAFVDATNSPEFREELGGYLRDYLGRPTPLTECSNLPLAGEGKGFARIFLKREDLVHGGAHKTNQVIGQVLLAKRMGKTRIIAETGAGQHGTATALACALMGLECVVYMGAKDVARQQPNVYRMQLHGAKVIPVESGSGTLKDAVNEALRDWTATFHESHYLLGTAAGPHPFPTIVREFHKVISEEAKAQMLERTGKLPDVVVACVGGGSNAIGMFADFIDDEGVELVGAEPAGEGLDSGKHGATITNGQIGILHGTRSYLMRNSDGQVEESYSISAGLDYPGVGPQHAHLHATGRATYVGITDAEALQAFQYLARYEGIIPALESSHAFAYALKRAKTAEEEGQNLTILVSLSGRGDKDVDHVRRTLEENPELILKDNR
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
P06561
|
P40905
|
TBB2_ERYPI
|
Beta-2-tubulin
|
Erysiphe
|
MREIVHLQTGQCGNQIGAAFWQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVLDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYEICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAHSFRAVTVPELTQQMYDPKNMMAASDFRNGRYLTCSAIFRGKVSMKEVEDQMRNVQNKNSAYFVEWIPNNVQTALCSIPPRGLKMSSTFVGNSTSIQELFKRVGDQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVHEYQQYQDASISEGEEEYEEEQQLENEE
|
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.
|
P40905
|
P36513
|
UDB14_RABIT
|
EGT12
|
Oryctolagus
|
MSVKHVSVLLLLLQLSCCFRTGSCGKVLVWPMDFSLWMNLNVILDELVRRGHEVIVLRNSASIFIDPSKQANIKFETFPIAATKDDLEDLFVHYVSTWTNARQNSQWKYFSLLQKLFSEYSDSCENACKEVVFNKTLMTKLQESRFDILLSDAIGPCGELLAELLKIPFVYSLRFTPGYTMEKYSGGLSVPPSYVPIILSDLSGKMTFMERVNNMLCMLYFDFWFQMFNKKRWDQFYSEVLGRPVTFSELVGKADMWLIRSYWDLEFPRPTLPNIQFVGGLHCKPAKPLPKEMEEFVQSSGEEGVVVFSLGSMVSNMTEERANLIASAFAQLPQKVIWRFDGQKPETLGPNTRIYDWIPQNDLLGHPKTKAFVTHGGANGIYEAIHHGIPMVGLPLFGEQPDNIAHMTAKGAAIRLNWKTMSSEDLLNALKTVINDPSYKENVMTLSSIHHDQPMKPLDRAVFWIEYVMRHKGAKHLRVAAHDLTWFQYHSLDVVGFLVSCAAFLIFLVIKSYLFVYQKLVKIGKKQKRD
|
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
|
P36513
|
O27001
|
TFX_METTH
|
DNA-binding protein Tfx
|
Methanothermobacter
|
MSKKTFLTERQKTVLEMRERGWSQKKIARELKTTRQNVSAIERKAMENIEKSRNTLDFVKSLKSPVRILCRRGDTLDEIIKRLLEESNKEGIHVIHDSITLAFLIREKASHRIVHRVVKSDFEIGVTRDGEIIVDLNS
|
Transcriptional activator of the fmdECB operon.
|
O27001
|
A7MR03
|
XNI_CROS8
|
Flap endonuclease Xni
|
Cronobacter
|
MPVHLLIVDALNLIRRIHAVQGTPCVDTCLHALEQLIGNSQPTHAVAVFDDEARAQGWRHQLLPDYKAGRPPMPDDLHQEMPALRDAFTRRGVPCWHVEGNEADDLAATLAVKVAAAGHEATIVSTDKGYCQLLRPEIRIRDYFQKRWLDAPFIESEFGVSPGQLADFWGLAGISSSKIPGVPGIGPKSATQLINDFGTLEALYERLDDVPDKWRKKLEAHRESAFVCRAVATLKTDLQLDGNLQQLRLHG
|
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.
|
A7MR03
|
Q9P6J9
|
YHD1_SCHPO
|
Putative inorganic phosphate transporter C1683.01
|
Schizosaccharomyces
|
MKLNIFKSHGDSNTAEERPVPLEQVEAEDQQHENRFWLGLTAKEFRLMMLAGVGFFLDSYDLFIINLVTPIFEYLYWGGIEKGPNGKGHYPSGIRGLVNAASNIGNIFGQLMFGFMGDFFGRKFVYGKEMIIVIIATILLIAMPKSIHSPLSKMMWVFCWRWLLGVGIGGDYPMSAAITSERSKLNRRGTLISLIFAFQGFGTLAGAIVTIILLGCFEHPLNREGHYRKLEGVWRLQFGLALVPAIGVLIPRLMMEETQKFKNSQQLNSGDNRDPKTSLNFEDDELVKNPSVTKGHPEIHESSENYLSRSNTVENEPENIEKQFESVSAPANRSGFIQYFRQWHHFKHLLGTSVCWFLLDIAFYGVNLNQSVILKNIGFSSGTNEYRTLMKNAIGNLIIAVAGYVPGYWFNVFLVEILGRKWIQLQGFVITGLMFAILAGRWNEISTGGRFACFVIAQLFSNFGPNSTTFIYPAEVFPARVRGTAHGISAALGKCGAILASLLFNFLTSIIGYGNVMWIFCGCMWGGILFTLLLPETKGRDADEIDRVELFYGGDGKVECNSKWKSWYVNGIF
|
High-affinity transporter for external inorganic phosphate.
|
Q9P6J9
|
P37265
|
YCR41_YEAST
|
Uncharacterized protein YCR041W
|
Saccharomyces
|
MLKYVVTDIGKMCLYIWPYRVWSWRRLFIFRVLNVVSIAILFETPHRLALVPNVCLYTHMAIPLSTCLFCLCLCICIKYDITQTQANNQFLASFFVLILTINDLDVTFVI
|
May play a role in proper chromosome segregation. Suppresses the high-frequency loss of mini-chromosomes when overexpressed, and this suppression is completely dependent on silencing protein SIR4.
|
P37265
|
A9MIV9
|
YIHI_SALAR
|
Der GTPase-activating protein YihI
|
Salmonella
|
MKKPTSAPRSKAFGKQRRKTREELNQEARDRKRLKKHRGHAPGSRAAGGKPASGGGNQNQQKDPRIGSKTPIPLGVTEKVTQQHKPKSEKLMLSPQAELDLLETDERLDALLERLEAGETLNAEDQAWVDAKLDRIDELMQKLGLSYDDEEDEEEDEKQEDMMRLLRGGN
|
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
|
A9MIV9
|
P28104
|
WNT5B_ALOVU
|
Protein Wnt-5b
|
Alopias
|
SGSCSLKTCWLQLADFRKVGDLLKEKYDSAAAMKITRKGKLELVNSRFNPPTPDDLVYLDQSPDYCVKNKSTGSLGTMGRLCNKTSEGMDGCELMCCGRGYDQFKTVQVERCHCKF
|
Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.
|
P28104
|
Q2KE81
|
TRPA_RHIEC
|
Tryptophan synthase alpha chain
|
Rhizobium
|
MTARMDKRFAELKAEGRPALVTYFMGGDPDYDTSLGIMKALPEAGSDIIELGMPFSDPMADGPAIQLAGQRALKGGQTLKKTLQLAADFRKTNDLTPIVMMGYYNPIYIYGVEKFLDDALAAGIDGLIVVDLPPEMDDELCIPAIRKGINFIRLATPTTDEKRLPTVLKNTSGFVYYVSMNGITGSALPDPSLVSGAVQRIKQHTELPVCVGFGVKTAEHAKVIGGSADGVVVGTAIVNQVATSLTKDGKATPDTVQAVATLVRGLSSGARSARLVAAE
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
Q2KE81
|
Q1CVC2
|
Y033_HELPH
|
Nucleoid-associated protein HPAG1_0033
|
Helicobacter
|
MDFSQLGGLLDGMKKEFSQLEEKNKDTIHTSKSGGGMVSVSFNGVGELVDLQIDDSLLEDKEAMQIYLMSALNDGYKAVEENRKNLAFNMLGNFAKL
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q1CVC2
|
A6TE43
|
UREE_KLEP7
|
Urease accessory protein UreE
|
Klebsiella
|
MLYLTQRLEIPSAATASVTLPIDVRVKSRVKVTLNDGREAGLLLPRGLLLRGGDVLSNEEGTEFVQVIAADEGVSVVRCDDPFMLAKACYHLGNRHVPLQIMPGELRYHHDHVLDDMLRQFGLTVTFGQLPFEPEAGAYASESHGHHHAHHDHHAHSH
|
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
|
A6TE43
|
B6DCT3
|
TX401_LYCSI
|
Toxin-like structure LSTX-C7
|
Lycosa
|
MKVLVLFSVLFLTLFSYSSTEAIDEFDSDAEDDMLSLMANEQVRAKACTPRLHDCSHDRHSCCRGELFKDVCYCFYPEGEDKTEVCSCQQPKSHKYIEKVVDKAKTVVG
|
Enhances the high-affinity desensitization of human P2RX3 purinoceptors.
|
B6DCT3
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.