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
|
|---|---|---|---|---|---|---|
B0K8Q5
|
MOAC_THEP3
|
Molybdenum cofactor biosynthesis protein C
|
Thermoanaerobacter
|
MNLTHINEEGRARMVDVSEKAETKREAVAIGSIYMKNETLRRIHEGTIKKGDVLAVAQVAGIMAAKNTSHMIPMCHPIMITGCDISFNLDFENSKIDIKAVVKTVGQTGVEMEALTAVTVAALTIYDMCKAIDRDMVISEIMLVKKSGGKSGLYEREV
|
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
|
B0K8Q5
|
Q71E95
|
CYB_ICHAL
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Ichneumia
|
MTNIRKSHPLIKIVNESFIDLPAPSNISAWWNFGSLLGVCLILQILTGLFLAMHYTSDTATAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGVYYGSYTFMETWNIGILLLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIISALAAVHLLFLHETGSNNPSGISSDSDKIPFHPYYTIKDILGLLVMLMLLMTLVLFSPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSIMVLAIVPLLHTSNQRGMMFRPLGQCLFWLLVADLLTLTWIGGQPVGHPFITIGQLASILYFSIILILMPIFGTIENQLLKW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q71E95
|
A1W2R0
|
RL2_ACISJ
|
50S ribosomal protein L2
|
unclassified Acidovorax
|
MAVIKIKPTSPGQRGAVKISRDHLYKGEAFAGLLEPQFQKAGRNNNGHITTRHKGGGHKHHYRVVDFRRNKDAIPAKVERIEYDPNRTAHIALVCYADGERRYIIAPRNLEVGATIVSGSEAPIRVGNTLPIRNIPVGSTIHCIELKPGAGAQIARSAGTSATLLAREGVYAQVRMRSGEVRKIHIECRATIGEVANEEHSLRQLGKAGVKRWMGIRPTVRGVAMNPIDHPHGGGEGRTGEGRHAVDPWGNLTKGYRTRNNKRTQVMIVSRRKK
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
|
A1W2R0
|
B4T4I0
|
LPLA_SALNS
|
Lipoate--protein ligase
|
Salmonella
|
MTTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTHIVLAALNSLGVMADASGRNDLVVKTPDGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLAIYLNPDKKKLAAKGITSVRSRVANLTELLPGITHKQVCQAVTEAFFVHYGERVDAEVISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGVITRAQVFTDSLNPAPLEALAERLQGCLYRADKLQETCEALLVDFPEQEKELRELSAWIAEAVR
|
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
|
B4T4I0
|
Q0HWD3
|
ZIPA_SHESR
|
Cell division protein ZipA
|
Shewanella
|
MEDLQLVLFVLGAIAIVAVLVHGFWSIRRQQPKSLKDSPMGNFYKKQAERGEGAPKRVDADGFDADGIGAVRVRKANEAHTPEAPAFNPYLKQEAKTQPQPVEPVQVEPKPLFEQEPSMAQPDFSLQSPTAKEQHRGPKASRQEPVLQGHSANLAQAHVGQSHAAMVAQKVAEEQRAQVQMPTQTALFDDEEPYEEEQSQAVEQADDDLGEPRDVLVLHVVAKEGQQLNGAELLPCFLTLNFKYGDMNIFHRHVDNAGNGKVLFSIANMVKPGIFDPDNMEQFSTQGVVFFMTLPCYGDALMNFSIMLNSARQLADDIDAVVLDGQRQPWGEFTKQDYLHRIRANA
|
Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
|
Q0HWD3
|
A1U380
|
LIPA_MARN8
|
Sulfur insertion protein LipA
|
Marinobacter
|
MSESAKPRITSGSKFRNEHGFSAIKDGVKRSSSNTEGKSLERKPKWLRARMPGGERYDAVRRNVTEHRLSTVCQESHCPNIGECWTNGTATIMVMGSVCTRACKFCAVDTGNPKGWLDPEEPENTAKSVELMGLRYIVLTSVDRDDLPDGGAAHYAACVSAIKQRTPEVAVEALTPDFDAVMSDVEKVVDSGLDVFAQNVETVKRLTSRVRDPRAGYEKTLSVLAHAKKHRPDVLTKTSLMLGLGETEEEILETMDDLRAIGVDILTLGQYLRPTPNHLPVERYVTPEEFNRYRDIGLEKGFMEVPSGPMVRSSYRADRVFDKNNLGLSVPEVPVPDKAMQIPVKAVD
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
|
A1U380
|
Q8TKU7
|
CYAS_METAC
|
Cysteate synthase
|
Methanosarcina
|
MGRFILKCLKCGREYSQEYRLTCENDDSFLRAEYLEKKLELRKQPGIGRFHSWLPVQEELTTEAGPITYKSEALARELGLSNLYIGFSGYWPEKGAFIKTCSFKELEAHPTMQLLKESGGKAIVLASAGNTGRAFAHVSALTGTDVYIVVPDSGIPKLWLPEEPTDSIHLISMTPGNDYTDAINLAGRIAKLPGMVPEGGARNVARREGMGTVMLDAAVTIGKMPDHYFQAVGSGTGGISAWEASLRLREDGRFGSKLPKLQLTQNLPFVPMYNAWQEGRRDIIPEIDMKDAKKRIEETYATVLTNRAPPYSVTGGLYDALVDTDGIMYAVSKEEALDAKALFESLEGIDILPPSAVAAASLLKAVEAGNVGKDDTILLNIAGGGFKRLKEDFTLFQIEPEITVSNPDVPLEELKL
|
Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate. Does not display threonine synthase activity like the paralog protein ThrC.
|
Q8TKU7
|
Q34376
|
CYB_DASRO
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Dasykaluta
|
MISLRKSHPLLKIINHAFIDLPAPSNISAWWNFGSLLGICLIIQILTGLFLAMHYTSDTLTAFSSVAHICRDVNYGWLLRNLHANGASMFFMCLFLHVGRGIYYGSYLYKETWNIGVILLLTVMATAFVGYVLPWGQMSFWGATVIMNLLSAIPYIGTTLAEWIWGGFAVDKATLTRFFAFHFILPFIIVAFAAVHLLFLHETGSNNPTGINPDSDKIPFHPYYTIKDALGLIFLILSLLLLGLFSPDLLGDPDNFSPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLASILILLIIPLLHTANQRSMMFRPIFQTLFWILTADLITLTWIGGQPVEQPFIIIGQLALMLYFLLILALMPLAGMFENYMLEPKW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q34376
|
A0B5R2
|
CETZ_METTP
|
Cell-structure-related euryarchaeota tubulin/FtsZ homolog
|
Methanothrix
|
MLNVLMLGVGQCGNRILDAVNRQAFGGSRLAKYYSKQRFPSRVETIAINTAINDLKELKFTAAKDRLHVPNLHGVGANRSKGKQGFWENQEMILEEIEKRGDFDLIFVMTSVSGGTGSSFSPLMIHELKKRYKNATIVPIAVLPFREEGTIYLQNAAFCLREMIEVEADGMILVDNQYLKRFSGDIASAYDRINTMVAQRLLFLIEALDSEMLSVTDLGDFKTVMNGGLRMGTLGYYQADKKSPSIRAAIKNSLREVGLLYPANVDAGEAGRAMIVIQGSREYLNVDEITKEIESLTETIGHVFKGIVIKKGEPRVLSVLSLERAPGLVELYEKAKWAIQEERERKDRARSELYEAFEQINDLEEIY
|
Involved in cell shape control.
|
A0B5R2
|
Q8H1Q7
|
GMPP3_ARATH
|
Probable mannose-1-phosphate guanylyltransferase 3
|
Arabidopsis
|
MPKPLVDFGNKPMILHQIEALKGAGVTEVVLAINHQQPEVMLNFVKEYEKKLEIKITFSQETEPLGTAGPLALARDKLVDESGQPFFVLNSDVICEYPLLEMIEFHKTNRAEASIMVTEVDDPSKYGVVVTEEGTARVESFVEKPKHFVGNKINAGIYLLSPSVLDRIELRRTSIEKEIFPKIASEKKLYAMVLPGFWMDIGQPKDYITGQRMYLNSLREKTPQELATGDNIIGNVLVHESAVIGEGCLIGPDVVIGPGCVIDSGVRLFGCTVMRGVWIKEHACISNSIVGWDSTVGRWARVFNITVLGKDVNVADAEVYNSGVVIEEQGL
|
Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants.
|
Q8H1Q7
|
P0C523
|
CYB_ORYSI
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Oryza sativa
|
MTIRNQRFSLLKQPIYSTLNQHLIDYPLPSILSYWWGFGSLAGICLVIQIVTGVFLAMNYTPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFFIVVYLHIFRGLYYASYSSPREFVWCLGVVIFLLMIVTAFIGYVLPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNATLNRFFSLHYLLPFILVGASLLHLAALHQYGSNNPLGVHSEMDKIAFYPYFYVKDLVGWVAFAIFFSIWIFFAPNVLGHPDNYIPANPMSTPPHIVPEWYFLPIYAILRSIPDKAGGVAAIALVFISLLALPFFKEMYVRSSSFRPIYQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQISSFFFFLFFAITPILGRVGRGIPKYYTDETHRTGSFS
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
P0C523
|
H2L006
|
TSP14_CAEEL
|
Tetraspanin-14
|
Caenorhabditis
|
MPHRAPRRFMKTAPGACDWEQCLLMGSGEPTRARAVVSSSHKQRKPRQEISACLKWLVFLLNSIVFLVGVGILALGVYLFIKDFREVKLVDIILNPAILISIFGFSICVVSFFGFMGALRDNIFLLKCFAACVFLSYILVVAVTLVFFTLFYTDTTEGLSANWLLLYAVKNYHTNRNLAEIMDALQENLECCGVSSIAQGYRDWNMSYQFNCTNSNPQPEKCGVPFSCCRKSVISEAAGSSNPLLPAMRSLECWQNALTKRPGDLEHDIYTRGCLQPLRTLFESHAVHVGAFVALLIVPVCISVCLTNILAKQVDHQRYLLEREARRNDRRRKRDHNRRDQLNSLDLLEEGKFNNASANATRPRPPDIPPPLPPIEHVPRKKSRNASSSPTRKPKSAGVENAAARRKRTATTTRTPPAAAGPAPTPQATTTNRTHQWVLQQTDLVPQKSKS
|
Together with tsp-12, regulates cell fate specification in the postembryonic mesodermal M lineage, body size and male development, probably by positively modulating BMP-like Sma/Mab signaling . Together with tsp-12, probably acts by modulating the activation of glp-1, Notch-like receptor, to regulate germline maturation .
|
H2L006
|
A4XZ78
|
RL5_PSEMY
|
50S ribosomal protein L5
|
Pseudomonas
|
MARLKEIYRKEIAPKLKEELKLANVMEVPRITKITLNMGLGEAIGDKKVIENAVADLEKITGQKVVVTHARKSIAGFKVREGWPIGVKVTLRRERMYEFLDRLLSISLPRVRDFRGLNAKSFDGRGNYSMGVKEQIIFPEIDYDKIDALRGLDITLTTTARNDDEGRALLRAFNFPFRN
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
A4XZ78
|
Q5BJZ6
|
CARME_RAT
|
Anserine-producing methyltransferase
|
Rattus
|
MQRRRRAPPASQPAQDSGHSEEVEVQFSAGRLGSAAPAGPPVRGTAEDEERLEREHFWKVINAFRYYGTSMHERVNRTERQFRSLPDNQQKLLPQFPLHLDKIRKCVDHNQEILLTIVNDCIHMFENKEYGEDANGKIMPASTFDMDKLKSTLKQFVRDWSGTGKAERDACYKPIIKEIIKNFPKERWDPSKVNILVPGAGLGRLAWEIAMLGYACQGNEWSFFMLFSSNFVLNRCSEVDKYKLYPWIHQFSNNRRSADQIRPIFFPDVDPHSLPPGSNFSMTAGDFQEIYSECNTWDCIATCFFIDTAHNVIDYIDTIWRILKPGGIWINLGPLLYHFENLANELSIELSYEDIKNVVLQYGFQLEVEKESVLSTYTVNDLSMMKYYYECVLFVVRKPQ
|
N-methyltransferase that catalyzes the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
|
Q5BJZ6
|
Q55GG6
|
ERCC1_DICDI
|
DNA excision repair protein ERCC-1
|
Dictyostelium
|
MSSQQTDNNPIPTTTTNNNTNNDNDIASTNNNTNNDDDSTTTNTSTNKPRKRFVIPSASQALKKSDLSMVEINSKLKQAEENAKQAEDLQKSNAIILTPKSTTTMTTTTTPVQQRMPIPSILAKRNVNTTTTTSTSPLSTSPPISSPLQTPYYSPSFVKNPTSPAPINKPIGPSLPMRPSLPKKPAAYSTTLSTYSSSSSSYSSSTTTQNYQHIDKIYANSKQRGSLMMNSFSKNIIIEYSELQYPDFILNSNTLVFYLPSLKTHRDNPNLIQDRIKGLSTLMTNSDSFTLRILLVFADLSDSDNCEQFINELNLIAIKLQFTLIVCWSQIEAAKYLEAYKTFNNRAPDPIKARAQPIELGGKSKNEQVLTSIKSVNKTDATTLLKNFQTMQQIFTCQKTTLSKLPGFGPVKVQKFYNTINQPFKTKPSTKTTTTTTTTTTTTTSANISSNNNNNNINTNDGNNNNNTINNINFNNDENEVDQDPLNFSFDFGGNGNGDGDSDGDGESENQINT
|
Structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair.
|
Q55GG6
|
P95519
|
IHFB_MANHA
|
Integration host factor subunit beta
|
Mannheimia
|
MTKSELIESLASKNPSLPIKMVEHCVKELLEQLTATLEEGERIEVRGFGSFSLHYRQPRLGRNPKTGESVLLGAKYVPHFKAGKDLKERVDLL
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
P95519
|
Q24009
|
BICC_DROME
|
Protein bicaudal C
|
Sophophora
|
MLSCASFNKLMYPSAADVAKPPMVGLEVEAGSIGSLSSLHALPSTTSVGSGAPSETQSEISSVDSDWSDIRAIAMKLGVQNPDDLHTERFKVDRQKLEQLIKAESSIEGMNGAEYFFHDIMNTTDTYVSWPCRLKIGAKSKKDPHVRIVGKVDQVQRAKERILSSLDSRGTRVIMKMDVSYTDHSYIIGRGGNNIKRIMDDTHTHIHFPDSNRSNPTEKSNQVSLCGSLEGVERARALVRLSTPLLISFEMPVMGPNKPQPDHETPYIKMIETKFNVQVIFSTRPKLHTSLVLVKGSEKESAQVRDATQLLINFACESIASQILVNVQMEISPQHHEIVKGKNNVNLLSIMERTQTKIIFPDLSDMNVKPLKKSQVTISGRIDDVYLARQQLLGNLPVALIFDFPDNHNDASEIMSLNTKYGVYITLRQKQRQSTLAIVVKGVEKFIDKIYEARQEILRLATPFVKPEIPDYYFMPKDKDLNLAYRTQLTALLAGYVDSPKTPSLLPPSLAGQLTPYANNNHLLLNANGLATPTGVCAPTQKYMQLHNSFQQAQNRSMVAGGQSNNGNYLQVPGAVAPPLKPPTVSPRNSCSQNTSGYQSFSSSTTSLEQSYPPYAQLPGTVSSTSSSTAGSQNRAHYSPDSTYGSEGGGVGGGGGGGARLGRRLSDGVLLGLSNSNGGGGNSGGAHLLPGSAESYRSLHYDLGGNKHSGHRAFDFDMKRALGYKAMERTPVAGELRTPTTAWMGMGLSSTSPAPAPLENGENGAAGGGASSGWRLPPGLGSPYGLSATTGLLDATPVNRRMQLAKHKDIQTLLTSLGLEHYIKIFVLNEIDLEVFTTLTEENLMELGIAAFGARKKLLTAIHTLLANEAACSTMPSSSSSQNSSSPRFSGSAAPGAERRPSNQW
|
RNA-binding protein that is involved in oogenesis. Required for correct targeting of the migrating anterior follicle cells and the establishment of anterior-posterior polarity in the oocyte. May act as translational repressor of oskar during oogenesis. Function seems to be sensitive to small changes in expression.
|
Q24009
|
Q07YC7
|
GCST_SHEFN
|
Glycine cleavage system T protein
|
Shewanella
|
MASKTVLFNKHLESKAKMVDFHGWEMPINYGSQIEEHHAVRQDAGMFDVSHMTVVDVTGSDACAFLRKLLANDVAKLTVPGKALYGGMLDENAGIIDDLITYYLTDTHYRVVVNSATRDKDLAWINKQAAAFDVVVTERPELAMIAVQGPNAKAKAATVFSAEQNAAVEGMKPFFGVQSASLFIATTGYTGEAGYEIIVPETEAEALWQALLDAGVKPCGLGARDTLRLEAGMNLYGQDMDESINPLAANMGWTVAWEPSERDFIGRDALTAIKAAGTDKLVGLVMEEKGVLRHDMAVFFTDADGVEHQGVITSGSFSPTLGYSIAMARVPSGIGAIAEVEMRKKRVNVKVIAPSFVRNGKQAF
|
The glycine cleavage system catalyzes the degradation of glycine.
|
Q07YC7
|
Q9UY53
|
PCKG_PYRAB
|
Phosphoenolpyruvate carboxykinase [GTP]
|
Pyrococcus
|
MEKLKRFLPEDQYEKLAAINNPYLHEFLAEWIEWLKPSKVFVCTDSPEDEEYVRWKALYYGEEKMLEMPRHTVHYDNYYDQARDKANTKLLVPKGVTLPFLNTMDREEGLKEIREIMKGIMKGKELFICFFVLGPRNSIFTIPAVQLTDSAYVAHSEFLLYRKGYEEFKRLGPTKNFLKFVHSAGELDERKTSKNLDKRRIYIDLVDETVYSANTQYGGNTIGLKKLAFRLTIQRAVREGWLSEHMFLMRVNGPNGRKTYFTGAYPSMCGKTSTAMIPWENIVGDDLVFIKNVDGTARAVNVEIGVFGIIEGINEKDDPIIWQVLHSPVEIIFSNVLVKDGKPYWNGMGIEIPDEGENHSGKWWRGKRDKEGNEIPPSHKNARFTVRLEAFPNLDKEALENPCGVEVGGMIFGGRDPDTWPPVREAFDWEHGVITMGASLESETTAATLGKEGVRAFNPMSILDFLSVHLGDYIRNYLEFGRKLKKKPKIFAVNYFLRENGKWLNEKLDKAVWLKWMELRVHGDVEAIETPIGYIPKYEDLRELFKQVLNKEYKKEDYEKQFKIRVPELLAKIDRIWNIYEPIGNIPEELFKQLEEERERLLKAREKYGDYISPFSLL
|
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
|
Q9UY53
|
Q6D1S8
|
RECA_PECAS
|
Recombinase A
|
Pectobacterium
|
MAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHALDPIYAKKLGVDIDNLLCSQPDTGEQALEICDALTRSGAVDVIIVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQANTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRTGAIKEGEEVVGSETRVKVVKNKVAAPFKQAEFQILYGEGINIHGELVDLGVKHKLIEKAGAWYSYNGDKIGQGKANACNFLKENPTISAELDKKLREMLLHKGNELKPAAAGNSHDEDELAGEGKEEF
|
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
|
Q6D1S8
|
C6EHJ8
|
RUTD_ECOBD
|
Aminohydrolase
|
Escherichia
|
MKLSLSPPPYADAPVVVLISGLGGSGSYWLPQLAVLEQEYQVVCYDQRGTGNNPDTLAEDYSIAQMAAELHQALVAAGIEHYAVVGHALGALVGMQLALDYPASVTVLISVNGWLRINAHTRRCFQVRERLLYSGGAQAWVEAQPLFLYPADWMAARAPRLEAEDALALAHFQGKNNLLRRLNALKRADFSHHADRIRCPVQIICASDDLLVPTACSSELHAALPDSQKMVMPYGGHACNVTDPETFNALLLNGLASLLHHREAAL
|
Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
|
C6EHJ8
|
Q5MJP4
|
SCX2_ANUPH
|
Phaiodotoxin-2
|
Anuroctonus
|
KFIRHKDESFYECGQLIGYQQYCVNACQAHGSKEKGYCKGMAPFGLPGGCYCPKLPSNRVKMCFGALESKCA
|
Sodium channel (Nav) specific neurotoxin.
|
Q5MJP4
|
Q6YRK2
|
RL9_ONYPE
|
50S ribosomal protein L9
|
Candidatus Phytoplasma asteris
|
MFSKNKHNTKFIVIACVIVVLILILFCLDFQNIQEIIETINQLTNNQNPSQNTASEMSGMRRKIIFFIFNFFGKIILASFVISFLLHIKKNAQIKRLKNKLSLWSKLSFHVSQIGEEVLNELPIGIVLIDISSQEIQWLNPYASFILKNPEINSPLAQINENMAQLISTSDAIPKTIITLENKKFECFYKKDLNVFYLFDATEKEQIKHLFLQKTLALAMITFDNLAESLIRYDLSEQSQIQGEYLSALSDYIEPYEGYLKQLIDDRFLLLLNRQNLDKMLENKFIILDTIRNISYKYQLKVTLSMGIACWNLSYEKLATYSQNAIELAQKRGGDQVVVNIENEKIKYFGAKIASLSKQSKVHARINAQNLVDILKKHPHCFIMGHTHTDLDALGSVIAFYKIATTIHPESNNYIILDEEKLDKSLIPVYNQLIKTEAKTSLNIITTQQASKMIKDNSLIAVLDTQTKDMVNSPELLSLTSNVVVVDHHRATEEIIPSIFSYVESSASSTVELLVEVMGFLEKEVHITAFEASIMYAGILIDTNAFIYRTSSRTFEVASKLKDLGADAIEVKSWLRKDFDKVLEINKLISEMEIFMDRFAIIQSSEIYENRSFLAQVAEGVLNIRNVDAAFMIAQIADNKIAISARSYNEINVQTIMEQMEGGGHLNSAATQLEGTNIKTVTDTLKHFLKLEYEKGEKNMEIILLTDIPNKGKKHEIIKVNNGYGNFLIQNKKALLADKTNLAAIKQSQMLEQEQKRNHELLMHKLKQEIDDKKITLDIQLGPKGKIYGKITLKQIAEEFLKVHNITLDRKKISLEGEIIAIGIYPVDVFLTDQIKATFFLNVTERKSK
|
Binds to the 23S rRNA.
|
Q6YRK2
|
Q6D4U2
|
TRPD_PECAS
|
Anthranilate phosphoribosyltransferase
|
Pectobacterium
|
MQLSSTQPSSKTQEPSTAQDVITMQHILEKLYGANSISRQESQALFGAIIRGELEASQLAAALISMKVRGEHPDEIAGAATALLADAQPFPRPDYLFADIVGTGGDGTNSINISTASAFVAASCGLKIAKHGNRSVSSRSGSSDLLSAFGIKLDMSAQDSRQALDDLGVCFLFAPQYHLGFRHAMPVRQQLKTRTVFNVLGPLVNPARPPLALIGVYSPELVRPIAETLKVLGYQRAAVVHGGGMDEVAIHAPTQVAELNHGEIETYELTHRDFGLDTHPLSALQGGTPEENRDILASLLQGKGERAHAAAVAANVALLLRLFGQEDLRQNAQQALEVIHSGQAYQRVIALSARG
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q6D4U2
|
C3TS06
|
STX74_ANEVI
|
Neurotoxin 7
|
Anemonia
|
MMNRLLVFLMLGAFMLVVSANDAYGDEPAFKDLNQGDESLGKRKSCCPCWLRGNCFWGQNCYPEGCSGPKV
|
Voltage-gated sodium channel (Nav) inhibitor. 1 uM completely inhibits insect voltage-gated sodium channel inactivation (DmNav1 from D.melanogaster).
|
C3TS06
|
P20487
|
FLIJ_BACSU
|
Chemotaxis CheF protein
|
Bacillus
|
MAYQFRFQKLLELKENEKDQSLSEYQQSVSEFENVAEKLYENMSKKELLEQNKEKKLKSGMSVQEMRHYQQFVSNLDNTIYHYQKLVIMKRNQMNQKQEILTEKNIEVKKFEKMREKQFKMFALEDKAAEMKEMDDISIKQFMIQGH
|
Flagellar protein that affects chemotactic events.
|
P20487
|
Q332S2
|
NU1C_LACSA
|
NADH-plastoquinone oxidoreductase subunit 1
|
Lactuca
|
MIIDTTEVQAINSFSILESLKEVYGIIWMLIPIFTLVLGITIGVLVIVWLEREISAGIQQRIGPEYAGPLGILQALADGTKLLFKENLLPSRGDTRLFSIGPSIAVISILLSYLVIPFSYHLVLADLSIGVFLWIAISSIAPVGLLMSGYGSNNKYSFLGGLRAAAQSISYEIPLTLCVLSISLLSNSSSTVDIVEAQSKYGFWGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKFGLFYVASYLNLLVSSLFVTVLYLGGWNLSIPYIFVPEVFEITKRGRVFGTIIGIFITLAKTYLFLFIPIATRWTLPRLRMDQLLNLGWKFLLPISLGNLLLTTCSQLISL
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
Q332S2
|
A0L4Y9
|
RL19_MAGMM
|
50S ribosomal protein L19
|
Magnetococcus
|
MNQVQAFEQSMIPETAVPKFGAGDTLKVHVKVVEGTRERIQVFEGVCIGRMNAGLRSTFTVRKISFGEGVERTFPVYSPRVDKIEVIRHGDVRRAKLYYLRGRTGKASRIKEKRDW
|
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
|
A0L4Y9
|
Q9MUU5
|
RK5_MESVI
|
50S ribosomal protein L5, chloroplastic
|
Mesostigma
|
MVQRLKTLYLESAVLKLQETFGYKNPHQIPRIKKIVINCGLSEASQNSKSLESAMKELSIIAGQKGVITRAKKAIAGFKIREGLPIGICITLRGDSMYAFLDRLINLALPRIRDFQGVSSKSFDGHGNYNLGLKEQLMFPEIDYDQIDKIRGMDICIVTNAKTDSEGFYLLEVLGMPFKEKFAN
|
Binds 5S rRNA, forms part of the central protuberance of the 50S subunit.
|
Q9MUU5
|
A0A193PS46
|
STBB_STABI
|
Nonribosomal peptide synthase-like protein stbB
|
Stachybotrys
|
MGSLGSSQLKPFNKAPIDFVSTKRQPGAVCSLPELVDYNAQHNASHNFCIQGKPGGEFDTFTHADFKVAAANCAKWLKANLPLGASQAPNAITKNAPVALFMESDFGLVVHEFALLSLGIPPLVLSVRLPPNAIMHLLKSTGATSFIVSQKLSGPAKPALAALAANGIATAVGNPYTSFLEPGVDVASKGTFEVPENPDDITLLLHSSGTTGLPKPIPISHRMLMFAVSTAKFDTEDEAQGLNVSSLPLFHGFGLVAPGISMTVGKTTVYPASDGIPNIVSIIDLIKRTNARSLMTVPFLLDDVINNEEGLRVLAGLDFVGTGGAALGPGVGDKLAAAGIKLLNFYGTTESGPLSLVFVPKDNYNWKFFRLRTDMNFEIANLEPKDGVKRYRLTIRAFGEGEDQEIADQLIRNDEYPETDFAAVGRDDDVIVLATGEKASPQILENMLTEAPMVKAAIAFGENQFNLGVIVEPKEPLAEGGEAAFKELIWPIIVAAGQKMDAHSVIPSQEAVIVVPNGVRVPRTDKGSIARKEVYALFADAMKDVYEKLARAVGGADLKPLDLETLEEDIKALIIEHSGLKVPAEGLSAEESLFDFGLDSLQALKLRRVLAAAANKSEAMKDVNVDKVIPPEFVYLNPSVAQMAAAIKNPSAGSAAPTVDANAYKGVEKFAEQYALPGASAEEKAPSVRERAIVVVTGSSGSLGSHVVATLARDPKVMRVVVMVRQGSKPFDREPWTSRGINLKEDEFAKIVPLPVDPTAENLGVDPMMYGMLQNNLTHIVHAAWPMNYLTTLPSFQYQFEYLSGLLKLATSGNTANKRRFIFVSSIAAVARLSLSNSGAMISETPVEPVDAACGIGYADGKLVCEKILEKAAVSHAGQLEIAYVRCGQMTGSRATGAWNADEQIPMIFRTAKNLGVLPRIPGTLSWIPVDDAAQYIMDLSFFEGALPIASHLENPVRQSWADLMDGAGKFLGIQKSVSWPEWLELAGAAEDGPQDKYPVKKLFAFFKFSFGPMASGAVILGTDVARAHSATIKNMGALDASTIMKYFLHWQKINYL
|
Nonribosomal peptide synthase-like protein; part of the cluster that mediates the biosynthesis of LL-Z1272-beta, also known as ilicicolin B, a prenylated aryl-aldehyde produced by several fungi and that serves as a key pathway intermediate for many fungal meroterpenoids . The first step in the pathway is performed by the non-reducing polyketide synthase stbA that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units . The prenyltransferase stbC then prenylates orsenilic acid into grifolic acid . Finally, grifolic acid is reduced to ilicicolin B by the NRPS-like protein stbB .
|
A0A193PS46
|
Q6HLF2
|
LEU3_BACHK
|
Beta-IPM dehydrogenase
|
Bacillus cereus group
|
MEKRIVCLAGDGVGPEVMESAKGVLHMVERLYGHHFHLQDEHFGGVAIDLTGQPLPQRTLAACLASDAVLLGAVGGPRWDGAKERPEKGLLALRKGLGVFANVRPVTVESATAHLSPLKKADEIDFVVVRELTGGIYFSYPKKRTDEVATDTLTYHRHEIERIVSYAFQLASKRKKKVTSIDKANVLESSKLWRTVTEEVALRYPDVELEHILVDAAAMELIRNPGRFDVIVTENLFGDILSDEASVLAGSLGMLPSASHAEKGPSLYEPIHGSAPDIAGKNKANPIAMMRSVAMMLGQSFGLTREGCAIEEAISAVLKSGKCTADIGGAETTTSFTKAVMQEMEEQALVGRGR
|
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
|
Q6HLF2
|
A9KLM3
|
RIMM_LACP7
|
Ribosome maturation factor RimM
|
Lachnospiraceae
|
MEDLLRVGVISSTHGIKGEVKVFPTTDDMNRFKKLKMVTLDTGKEQKELEIENVKFFKQFVILKFKGIDNINDIEKYKGKDLLISRENAVDLAEGEFFIFDLIGLQAEEEDGNSLGELTEVLQTGANDVFVIKTKQGKEILIPYIDDCVKKIDLNEKKLVVHLIPGLVE
|
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
|
A9KLM3
|
Q2YIU9
|
ALR_BRUA2
|
Alanine racemase
|
Brucella
|
MSLPFSQDERDLAAGGILTIDLAALRHNYSAIATRIAPTRTAAVVKADAYGLGASRVAPAFYEAGCRDFFVAHLGEAVALKPFLKPDATLYVLNGLQPGTEAACAREGILPVLNSLEQVENWAALATRLGKKLPALLQFDTGMSRLGLSAKEFDRLLENVTLLSRIDIKFAISHLANGDEPGNAVNARQLAKMTALLARLPKLPAALANSGGTFLGKTYYFDLARPGIALYGIDPERQHDFSDKVAHENKKPKHSILPVLTLSARVIQVRDVDKGATVGYGGTYVANGPMRIATIAVGYADGLFRSLSNKGAAFFGDTRLPIIGRVSMDSITLDVTSLPEGTLKLGSLVELIGPHQRLEDVARDCDTIPYEILTALGNRYARVYVYVNGGGTSTTA
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
Q2YIU9
|
B4PIW8
|
UBP36_DROYA
|
Ubiquitin-specific-processing protease 36
|
Sophophora
|
MPVSMAVCETANVVNAALRESLGGNSSAAGSSIDQAKSGEDSNGSLQNHIVANAKRILMAKIEYEEVPNYHESVLENLKSKYIVIKPGNPGAINGFGGKNNTGKVVGANGHDNNGARKQAEHPNNQSHHNNHNNHPHPTSNPNELPKPKRVLYPRENIRIGWKQSERKWQVGTGMINVGNTCYLNSTLQALLHIPALANWLVSEQAHLENCNVAESGGGCIVCAMAKTLLATQSNQSAVRPFLIYSKLKQICKHMVVGRQEDAHEFLRFLVEAMERAYLMRFRNYKELDQLVKETTPLGQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKADSLEDAFEGHFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMIGNKLTKQISLKPRIDLSKYAARSPAAQAQPLTYRLVSMVTHLGVSQHCGHYTAIGSTDTGSYYNFDDSYVRPIAMQSVCNTNAYIMFYELDLSQAASPAANRPNGVRLTNGHSTTPVPAATVSSPSPTRFIGPQLPPGGVNGYSNGNAQKTAIQFKQHHQQSQQNGFQLGTGKFQDTAKPPLVGAHAKGDANPVPTANGNKSSSTSSNSSSNHKSINQQQYLPISSEDEDSEDEMTPRPTTAQLPSMPKMTDDHTEKPKSPVKIQVKTPVKTPLKSLVPYESASEEEEAPQPNPRKRRSEEDSSESDQESGQTNGHSKTNGSLTNGSASSSVHVNNSKQKTDAIDEIFKSLKKSADSDDDDDEEESSIQLTNGWHPQKQSQSQSKAPPSPKTPPSPAVIKSKTGIWKVTRNDEVDDIDDDDDEEDEAPAKIQTPSKTHRNPFSSTKPSTESPATPGAKRQKLLNGSAVKSHQQPRVGNGYQSEATSNGSTINELLKQSHRGYGSSVLSWNGKPAELEKEPFELVCAKRIAGHGSVDGSDIVESSVAVNASSGSDSNDVVVIALLVDAREQRQRDLDDDEENEMDRGRQRKVKSSGSAKANNASNSTPGYNPFQEYEGQKRWNKNGGGGGGFPRFYNQNFRQNFQQRNKFKFNRFGGPGSAKFQQQRALQRHLAAGGGFSRRQPSAQQQQQQS
|
Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4). Controls selective autophagy activation by ubiquitinated proteins.
|
B4PIW8
|
A3N1E6
|
RECX_ACTP2
|
Regulatory protein RecX
|
Actinobacillus
|
MTNYTAINYLLYLLSKRDYSEQDLRRKLVQKEYSQEEIEQAIERAQANNWQSDERYCAGFIRYRSQQGIGPRRLKQELKLKGIKDWLINQELENAEIDWFILAEQVFEKKRPQVWDIKAKQKMWRFMLSRGFYNDHFSHLMDIDYNDTEYE
|
Modulates RecA activity.
|
A3N1E6
|
Q91554
|
ARGN2_XENLA
|
Arginase, non-hepatic 2
|
Xenopus
|
MSIRSNFVRLLKKQVSIIKLQKKCSHSVAVIGAPFSKGQKRRGVEHGPAAIRSAGLIERLSNLGCNVCDFGDLHFSKVPNDELYNSIVKHPRTVGLACKVLAEEVSKAVGAGHTCVTLGGDHSLAFGSITGHAQQCPDLCVIWVDAHADINTPLTTPSGNLHGQPVSFLLRELQDKVPPIPGFSWAKPCLSKSDIVYIGLRDLDPAEQFILKNYNISYYSMRHIDCMGIKKVMEKTFDQLLGRRDRPIHLSFDIDAFDPALAPATGTPVIGGLTYREGVYITEEIHNTGMLSAVDLVEVNPVLAATSEEVKATANLAVDVIASCFGQTREGAHTRADTIIDVLPTPSTSYESDNEEQVRI
|
As well as its role in the urea cycle, may be involved in tissue remodeling.
|
Q91554
|
C0HK45
|
LTX2A_ECTBR
|
Ponericin-Q42
|
Ectatomma
|
FWGAVWKILSKVLPHIPGTVKWLQEKV
|
Antimicrobial peptide forming an alpha-helix in watery and membraneous environments, enabling it to perforate membranes. Active against Gram-negative bacteria E.coli DH5alpha (MIC=5 uM), E.coli MH1 (MIC=0.6 uM) and P.aeruginosa PAO1 (MIC=10 uM) and against Gram-positive bacteria B.subtilis VKM B-501 (MIC=0.6 uM) and A.globiformis VKM Ac-1112 (MIC=0.2 uM). Has cytolytic and hemolytic activity.
|
C0HK45
|
Q16AH6
|
PCKA_ROSDO
|
Phosphoenolpyruvate carboxykinase (ATP)
|
Roseobacter
|
MTHGRVNPDFRLEDQGITGLGTVYYNLIEPDLIQYALARGEGSLGKGGSFLVTTGKFTGRSPKDKHVVKTDSVADTIWWENNREMSPEGFDQLYTDMLAHMEGRDYFVEDLTGGSDPKHAINVRMVTELAWHGLFIRHMLRRPDREDLDDFIADFTVINCPSFQADPAKHNCRSETVIAMNFDKKLILIGGTEYAGENKKSVFTLLNYLLPEKGVMPMHCSANHAVGNPVDTAVFFGLSGTGKTTLSADPARTLIGDDEHGWSDTGTFNFEGGCYAKTISLNPEAEPEIYATTEKFGTVIENMVYDAETKDLDFEDDSLTANMRCAYPLHYISNASQAARGGHPKNIIMLTCDAFGVLPPISRLTPAQAMYHFLSGFTSKVAGTERGVTEPEPTFSTCFGAPFMPRRPEVYGNLLREKIATHGATCWLVNTGWTGGAYGTGSRMPIKATRGLLTAALDGSLADAEFRKDPNFGFQVPVDVTGVPGILLDPRRTWDDAEAYDRQAAKLVKMFSDNFEQYLPFIDEDVRAAAIS
|
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
|
Q16AH6
|
Q05638
|
CHIX_STROI
|
Exochitinase 1
|
Streptomyces
|
MDRFRPLAVLIAAALTLSGTTALSSAARAADADLARNGGFEAGLDGWTCTAGTTVNSPVRSGSSALKATPAGSDNARCAQTVTVQPNSQYTLSGHVQGSYVYLGASGTGTTDVSTWTQSAPDWRQLTTTFRTGPSTTRVTLYTHGWYGTGAYHADDISLVGPGGGTEQPPAPPTGLRTGSVTATSVALSWSPVTGATGYAVYRDGVKVATASGTSATVTGLTPDTAYAFQVAAVNGAGESAKSATVTATTAPGTGGGSADLPPHALVGYLHASFANGSGYTRLADVPDSWDVIDLAFGEPTSVTSGDIRFDRCPATECPNVESDAEFKAAIKAKQAAGKKVLISIGGQNGQVQLTTTAARDTFVSSVSKIIDEYGLDGLDIDFEGHSLSLNADDTDFKNPKTPVIVNLIQALKTLKAKYGDDFVLTMAPETFFVQLGYQYYGTGKWGGQDPRAGAYLPVIHALRDDLTLLHVQDYNSGPIMGLDNQYHSMGGADFHIAMTDMLLTGFPVAGDAANVFPPLRADQVAIGMPATTNAGNGHVAPAEAVKTLDCLTRKTNCGSYATHGTWPALRALMTWSINWDRFGGWEFQRTFDGYFG
|
Exochitinase that generates exclusively chitobiose from chitotetraose, chitohexaose, and colloidal high-molecular mass chitin.
|
Q05638
|
Q0TUE3
|
ACPS_CLOP1
|
4'-phosphopantetheinyl transferase AcpS
|
Clostridium
|
MIIGIGVDIIEIERVRQAIQNNKNFLSKLFTEREIDYFISRNMNSEVIAGNFAAKEAVSKALGTGIRGFSFKDIEILRNELGKPEVILHNGANLIGNKLVENNNSLRVHLSISHNNSSAIAYSVLEGEYYGNM
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
Q0TUE3
|
Q3II82
|
RL9_PSET1
|
50S ribosomal protein L9
|
Pseudoalteromonas
|
MQVILLDKIANLGGLGDQVVVKSGFARNFLFPQGKAVPATKANIETFDARRAELEAKIADQLVAAQARADKLEALAEVTLVSKAGDEGKLFGSIGTRDIADAISAVGVEVAKSEVRLPLGTIRETGEFDVSIAVHSEVTATIKVIVIAEA
|
Binds to the 23S rRNA.
|
Q3II82
|
Q28133
|
ALL2_BOVIN
|
Dermal allergen BDA20
|
Bos
|
MKAVFLTLLFGLVCTAQETPAEIDPSKIPGEWRIIYAAADNKDKIVEGGPLRNYYRRIECINDCESLSITFYLKDQGTCLLLTEVAKRQEGYVYVLEFYGTNTLEVIHVSENMLVTYVENYDGERITKMTEGLAKGTSFTPEELEKYQQLNSERGVPNENIENLIKTDNCPP
|
Probable pheromone carrier.
|
Q28133
|
Q7XJ39
|
NLT2A_ORYSJ
|
Non-specific lipid-transfer protein 2A
|
Oryza sativa
|
MARAQLVLVALVAAALLLAGPHTTMAAISCGQVNSAVSPCLSYARGGSGPSAACCSGVRSLNSAASTTADRRTACNCLKNVAGSISGLNAGNAASIPSKCGVSIPYTISPSIDCSSVN
|
Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
|
Q7XJ39
|
A6R989
|
URM1_AJECN
|
Ubiquitin-related modifier 1
|
unclassified Histoplasma
|
MGSIASPSLSSSSQLLTITVEFTGGLESIFNNTRKHTLSIPATYPSPSTGEPEPTSVASLVHYLIENVMEDTRQELFVVDGAVRPGILVLINDADWELEGEEKYQIQQGDNILFVSTLHGG
|
Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
|
A6R989
|
Q2GHF4
|
RS6_EHRCR
|
30S ribosomal protein S6
|
Ehrlichia
|
MPLYEFTFIAQQGLTQYELEGLVKGLSSLLTKNGAELLKYEYWGLLDFAYTIDKMNKGHYCMIYIKATPSSMDEFKRKVRLNEDILRFLCLKKDKLPKGDSLMIQASQV
|
Binds together with S18 to 16S ribosomal RNA.
|
Q2GHF4
|
Q5YTA2
|
DXS_NOCFA
|
1-deoxyxylulose-5-phosphate synthase
|
Nocardia
|
MGVLSRVDTPEDVRRLNVAELRELAEEIREFLVRKVAATGGHLGPNLGVVELTIALHRVFDSPADPLIFDTGHQAYVHKILTGRKDRFDDLRKQGGLSGYPSRAESPHDWVESSHASAALSYADGLAKAFALGGQDRHVVAVVGDGALTGGMCWEALNNIAAAPDRPVVVVVNDNGRSYAPTIGGLADRLTALRTQPAYEHALDAGKRLLKSIPRVGESAYSMVHAVKAGIKDAVSPQELFSDLGLKYVGPVDGHDVVAMESALRRAKDFGGPVVVHAVTQKGRGYEHAENHVADQMHACDPIDPLTGRPLGGAKARGWTSVFSEELIEHARRRSDIVAITAAMPGPTGLSAFGERFPDRMFDVGIAEQHAMASAAGLALGGMHPVVAIYSTFLNRAFDQLLMDVALLKQPVTVVLDRAGITGPDGASHNGMWDLSLLGIIPGIRVAAPRDAATLREELGEALAVTDGPTVLRFPKGSVAEDLTAVERIDGVDVLRAADPESAVRTQRGDVLIVAVGPFARIGLAAAELLAPEGVSVTVVDPRWVLPVSDTVVKLAENYRLVVTLEDSGLHGGIGSTVSARLRSVGLDVPTRDLGVPQQFLDHASRDQVLEQLGLTPTDVARRIAGWLDAR
|
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
|
Q5YTA2
|
Q58522
|
VAPB3_METJA
|
Putative antitoxin VapB3
|
Methanocaldococcus
|
MINMATITIDDDVYKELLKLKGRKSVSEFIKELLEERKRKNLDVFMIAFGSRSEEDVEKLKKELKEAEKWMQSLIQV
|
Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is VapC3 (Potential).
|
Q58522
|
Q93ZX1
|
RFC4_ARATH
|
Protein EMBRYO DEFECTIVE 1968
|
Arabidopsis
|
MAPVLQSSQPWVEKYRPKQVKDVAHQEEVVRVLTNTLQTADCPHMLFYGPPGTGKTTTALAIAHQLFGPELYKSRVLELNASDDRGINVVRTKIKDFAAVAVGSNHRQSGYPCPSFKIIILDEADSMTEDAQNALRRTMETYSKVTRFFFICNYISRIIEPLASRCAKFRFKPLSEEVMSNRILHICNEEGLSLDGEALSTLSSISQGDLRRAITYLQSATRLFGSTITSTDLLNVSGVVPLEVVNKLFTACKSGDFDIANKEVDNIVAEGYPASQIINQLFDIVAEADSDITDMQKAKICKCLAETDKRLVDGADEYLQLLDVASSTICALSEMAQDF
|
May be involved in DNA replication and thus regulate cell proliferation.
|
Q93ZX1
|
Q7NZ33
|
HSCA_CHRVO
|
Chaperone protein HscA homolog
|
Chromobacterium
|
MALLQIAEPGLSAAPHQHRLAVGIDLGTTNSLVATVRSGSAAVLPDETGRSLLPSVVRYGDQGVLAVGYDAQKEQNRDPHNTIVSVKRFMGRGVSDIKDAGSLPYRFVDAPGMVQLVTRAGVKSPVEVSSDILRALKERAEASLGGELTGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDNGSEGTYVVYDLGGGTLDVSILKLTRGVFEVLATSGDSALGGDDFDHRVFCWLLEQAGVTAPSAHDMRLLHTRAREAKEALTDHASTRVTAILSDGQSLDLELDQATLHAITKTLVDKTLTPVRKALRDAKIAPEDIQGVVMVGGATRMPHVQKAVADYFGRAPLTNLDPDKVVALGAAIQANVLAGNKQDDEWLLLDVLPLSLGIETMGGLTEKIIPRNSTIPVARAQDFTTFKDGQTAMSIHVLQGERELVSDCRSLAKFTLTGIPPMVAGAARIRITFQVDADGLLSVTAREQTSGVESSIEVKPSYGLSDDEISRMLSESLANVQEDIEARKLREAIVDAESLRDATLNALAQDGDLLDQAERAEVEAAVAAVASAIAEGVTRRVNEASAALNHATETFASRRMDRNIQRALKGHKITDL
|
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
|
Q7NZ33
|
Q55BD5
|
CSN7_DICDI
|
COP9 signalosome complex subunit 7
|
Dictyostelium
|
MTTQQETLTDGNALKQFVVLAKSSKGRAIVSIIEKALNHPSVFVFGELLDMPNVQQLKETEFKNYYDLLLIFAYGSFIDYKNKKDSLPQLTPQMITKLKQLTIVFLSSTSNVIPYSVLQEQIEITNVRELEDLIIDSIYQNIIKGKLDQKNKHLEIDFSIGRDVQPEQLDSMINCLNNWSSTSQKLLDDISGLITHSDKVHLQYRKEKEEFESKFEIAKLNTKNDSPAEQLYYDSMEYSDEVRMKKGPKIKGKDYNKRP
|
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity.
|
Q55BD5
|
P16312
|
PEPT1_DERMI
|
Major mite fecal allergen Der m 1
|
Dermatophagoides
|
TQACRINSGNVPSELDLRSLRTVTPIRMQG
|
Thiol protease that hydrolyzes proteins, with a preference for Phe or basic residues.
|
P16312
|
A6LPQ0
|
RL11_CLOB8
|
50S ribosomal protein L11
|
Clostridium
|
MAKKVTGMIKLQLQAGKATPAPPVGPALGQHGVNIMGFCKEFNAKTANQAGYIIPVVITVYQDRSFSFILKTPPAAVLIKKEIGLESGSGVPNKTKVGKLTQDQLKKIAETKMPDLNAASLESAMRMIAGTARSMGVTIEE
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
A6LPQ0
|
Q0SNH3
|
RL13_BORAP
|
50S ribosomal protein L13
|
Borreliella
|
MNKITNNVTIWIKPKTVEKKWYVIDAADRVLGKVAVDVVRILRGKHKAYYTPHQDLGDNVIVINASKVRLTGKKYQQKLYYRHSRYPGGLYSDTFRTLSERKPCAPLEIAIKGMLPKGPLGRGLFRNLKVFSGSEHTLKAQNPVKLEANLER
|
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
|
Q0SNH3
|
B1IKX1
|
LDH_CLOBK
|
L-lactate dehydrogenase
|
Clostridium
|
MIKKRNTTKISVIGAGSVGATTAYALMLSGVATEIVLVDVNKAKTEGEAMDLSHGADFVKPVNILSGDYKDTEGSDIVVITAGAAQKVGETRLQLINKNINIFKSIIPEVVKYNKDAILLVVSNPVDVLSYVTYKLSGFPKERVIGSGTVLDTSRLKHEIGKRYKIDPRNVNTYIMGEHGDSEIATWSVTNIQNIKIDEYANKENLEYNDNFRKEVYENVKNAAYEVINRKGATFYAIALAVTRIVKAILGDEKTILPVSTLVENYYGIKDVYLGMPCIVGGSGIEKALSIDLNKTEASKLVKSAETLKNTLNNASGL
|
Catalyzes the conversion of lactate to pyruvate.
|
B1IKX1
|
Q6BIH5
|
FYV4_DEBHA
|
Protein FYV4, mitochondrial
|
Debaryomyces
|
MSFRLFARPLIQMPKLAAPRCINITPIRPISASAISLKTNTSTSTKENVHDLETFFKLIGRDCIEHLDAFESDLQKFLKTSSKDMKNMGIDVSTRRYMLRWIHKFQNDLEPLREHKRGKKKNGGERNAKTVLAKRTALKRLEEKERFESQELEAERKGEREF
|
Involved in telomere length regulation.
|
Q6BIH5
|
P72761
|
CCMK2_SYNY3
|
Carbon dioxide-concentrating mechanism protein CcmK2
|
unclassified Synechocystis
|
MSIAVGMIETRGFPAVVEAADSMVKAARVTLVGYEKIGSGRVTVIVRGDVSEVQASVSAGIEAANRVNGGEVLSTHIIARPHENLEYVLPIRYTEEVEQFRTY
|
One of the shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. The central pore probably regulates metabolite flux . Hexamers make sheets that form the facets of the polyhedral carboxysome (Probable) .
|
P72761
|
P82536
|
TLP20_SPIOL
|
Thylakoid lumenal 18 kDa protein
|
Spinacia
|
SAEETPLQSKVTNKVYFDISIGNPVGKVVIGLFGDDVPQTAENFR
|
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
|
P82536
|
Q5HRS7
|
RECR_STAEQ
|
Recombination protein RecR
|
Staphylococcus
|
MHYPEPISKLIDSFMKLPGIGPKTAQRLAFHTLDMKEDDVVKFAKALVDVKRELTYCSVCGHITENDPCYICEDKQRDRSVICVVEDDKDVIAMEKMREYKGLYHVLHGSISPMDGIGPEDINIPALVERLKNDEVKELILAMNPNLEGESTAMYISRLVKPIGIKVTRLAQGLSVGGDLEYADEVTLSKAIAGRTEM
|
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
|
Q5HRS7
|
Q67NB6
|
DXS_SYMTH
|
1-deoxyxylulose-5-phosphate synthase
|
Symbiobacterium
|
MHLRDLTGPEQLKRLAPAELAQLAAEIRRVILETVATNGGHLAPNLGVVELTLALHIVFDSPRDKILWDVSHQSYVHKLLTGRLHQFHTLRQFGGIAGFTDPRESVHDHFHWGHASTSISAAVGMAKARDLAGDDYEVVAVIGDGALTGGMAYEALDHAGHDKTKVIVVLNDNSMSIAPNVGGISNYLARIRTGPSYQRVKHDVAEALRQIPLIGPQALELADRLKEGVKHLLVHNMFFEDLGFTYLGPVDGHNVSALVDVLRQARAYPGPTVVHVVTTKGKGVPYAEQLPDKFHGGGPFDVATGRTGPGSLTYSEVFGNVMCKLAAEDPRVCAITAAMPSGTGLSRFARQFPDRYFDVGIAEQHAVTFAAGLAKGGMRPVFAVYSTFLQRAYDQVIHDVALQNLPVTLAIDRGGLVEDGATHQGVFDVAYLRAIPNMVVMAPKDENELQHMLYTALCHDGPAALRYPRGKAQGVPLDETLQPLPIGRGEVMQEGADVALIGLGTMARVCQEAARLLAEKSISAMVINPRFVKPLDAELLLRAGREVGAVVTVEEACLAGGFGSAVLELYAAHGVNARVERMGIPDEFVDHGQPARYLERYGLTPEGVAQRAEALLLRMRSDLAAQPARRSRSVRRLSGAKAAGNGET
|
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
|
Q67NB6
|
Q81IS8
|
TSAD_BACCR
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Bacillus cereus group
|
MGEYIMEKNTIILGIETSCDETAVAVVKNGTEIIANVVASQIESHKRFGGVVPEIASRHHVEEITVVLEEALKEANITFDDIDAIAVTEGPGLVGALLIGVNAAKAVAFAHDIPLVGVHHIAGHIYANRLVKEVQFPLLSLVVSGGHTELVYMKEHGSFEVIGETRDDAAGEAYDKVARTLSMPYPGGPHIDRLAHEGEPTIDLPRAWLEPDSYDFSFSGLKSAVINTVHNAKQRGIEIAPEDLAASFQESVIDVLVTKAARAAEAYNVKQLLLAGGVAANKGLRARLEEEFAQKENIELIIPPLSLCTDNAAMIAAAGTIAYEQGKRATLALNANPGLDIEA
|
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.
|
Q81IS8
|
B5BCP4
|
ARNT_SALPK
|
Undecaprenyl phosphate-alpha-L-Ara4N transferase
|
Salmonella
|
MMKSIRYYLAFTAFIALYYVIPVNSRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWINSLGQWLFGATNFGVRAGAILTTLLAAALVAWLTFRLWRDKRTALLASVIFLSLFAVYSIGTYAVLDPMIALWLTAGMCCFWQGMQATTRTGKIGMFLLLGATCGLGVLTKGFLALAVPVVSVLPWVIVQKRWKDFLLYGWLAVLSCFVVVLPWAIAIARREADFWHYFFWVEHIQRFAMSDAQHKAPFWYYLPVLLAGSLPWLGLLPGALKLGWRERNGAFYLLGWTIMPLLFFSIAKGKLPTYVLSCFAPIAILMARFVLHNVKEGVAALRVNGGINLVFGIIGIVAAFVVSSWGPLKSPVWTHIETYKVFCVWGVFTVWAFVGWYSLCHSPKYLLPAFCPLGLALLFGFSVPDRVMESKQPQFFVEMTQAPLASSRYILADSVGVAAGLAWSLKRDDIMLYGHAGELRYGLSYPDVQNKFVKADDFNAWLNQHRQEGIITLVLSIDKDEDISALSLPPADNVDYQGRLVLIQYRPK
|
Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
|
B5BCP4
|
A0A2A5K485
|
AZG2_PAELB
|
Nucleobase transporter PlAzg2
|
Paenibacillus
|
MYVSSLLFLYASESYESFIFHFQMCYNKAHNGFMPSIFQQLKGLGEGLQWKVGISLDHQEKQTSSHEKEMTSPNSATRLIPSDWRRELLAGTVSFFAAVYIIIVNSSILADAGIPQEAGIIATILASAIGCFIMGLWGNAPLVIVPGMGINAMFTYTLVQGMGLTWQQALAAVMMSGICFFAISMTSLVEKLRTAIPASLQEAISVGIGLMLVLIGLHKGGVIASDRSSVIAVQSFADPGVLVTLATLALTCILYIRKVPGNLLLAIIGGSALAYLFKAVPSKAATGVGGSSWSSYGDLFGQLSVKGASITTLVIAVFSLTLVIVFENVGLINAQLKMSGRTERFKRVTQATSLTVILSGIFGTSPTVSTVEAAAGISAGGRTGWASIATGTLFLLSFIAMPVITLVPDQAVAPILIFIGGLMMPAVRHISFERMEEGLPAFFIIAFIPLMHSIVDGIAIGFISYALFHIAVGKWREVKPLFYIISLLFVMHFVLQTM
|
Transports adenine, guanine, hypoxanthine, xanthine, cytosine and uracil. Transport is probably proton-dependent.
|
A0A2A5K485
|
A5ILC9
|
RPOZ_THEP1
|
Transcriptase subunit omega
|
Thermotoga
|
MEKMVKFNLRYDELLKKIPYKYAIPVVVAKRAEAIREYAKPFVITDDENPVSIAFMELSLNYIRIKNEEILKALIPKVK
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
|
A5ILC9
|
A5E2R6
|
CIAO1_LODEL
|
Probable cytosolic iron-sulfur protein assembly protein 1
|
Lodderomyces
|
MKLLHSIKAHDDKVWSLSSHPTLPLLATASTDKCSNIYRLSCSNASSSSSSSSPPSPPSPPSSSSPRRNFPQIAHLEDTHRRSVRSVSFKPPMGGIDHQDSNILDLPALASGSFDSTISIWGIDEPDDDNTYEIEEIIANQKEFLASPGNEWNLMAVIEGHENEIKAVDWNFSGRYLASCSRDKTVWIWETDPETLEEFECVAVLTDHTQDVKHVTWHPTRNLLASSSYDDTIRVYKQEFDDDEWSCVGMIDGHEGTVWCSKFESPKSPKAKDGTTRLVSVSDDLSARVWASKDNTGFNGGSEQLQSQSQTHLPSSIRHNAEEMVWEQESTLPQIHTHAIYSVAWSSSSGKIATAGSDGRIVVYKETNAGWEVENIQESAHGVYEINCVIWAKLDLDQEVLISGGDDGNVNIWEV
|
Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
|
A5E2R6
|
O82616
|
SCRK5_ARATH
|
Probable fructokinase-5
|
Arabidopsis
|
MANTPLIVSFGEMLIDFVPDTSGVSLAESTGFLKAPGGAPANVACAITKLGGKSAFIGKFGDDEFGHMLVNILKKNGVNSEGVCFDTNARTALAFVTLKKDGEREFMFYRNPSADMLLKESELNKDLIKKAKIFHYGSISLISEPCRTAHMAAMKTAKDAGVLLSYDPNVRLPLWPSTEAAIEGIKSIWNEADIIKVSDDEVTFLTRGDAEKDDVVLSLMHDKLKLLIVTDGEKGCRYYTKKFKGRVPGYAVKAVDTTGAGDSFVGAFLVSLGKDGSILDDEGKLKEALAFANACGAVCTTQKGAIPALPTPADAQKLMKSKSK
|
May play an important role in maintaining the flux of carbon towards starch formation.
|
O82616
|
A8MJJ8
|
CH10_ALKOO
|
Chaperonin-10
|
Alkaliphilus
|
MNIKPLGDRVVIKRVEAEETTKSGIVLPGSAKEQPQLAEVMAVGPGGVIEGKEVVMEVKVGDKVIFSKYAGTEVKFDGVEYTILKQSDILAVVE
|
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
|
A8MJJ8
|
Q9D513
|
MEIOB_MOUSE
|
Protein expressed in male leptotene and zygotene spermatocytes 675
|
Mus
|
MAKFFALKNFTALSDLHPNMANLKIIGIVIGKTDVKGFPDRKNIGSERYTFSFTIRDSPCHFVNVSSWGSEDYIRSLSESFRVAECVIIENPLIQRKDTEREEKFSPATPSNYKLLLSENHSMVKVCSPYEVDTKLLSLIHLPVKESRDYYSLADIVANGHSLDGRIINVLAAVRSVGEPKYFTTSDRRKGQRCEVKLFDETEPSFTMTCWDNESILLAQSWMARETVIFASDVRINFNKFQNCMAATVISKTIITVNPDTPEANILLNYIRENKETNVADEIDSYLKESVNLNTIVDVYTVEQLKVKALKSEGKADPFYGILYAYISTLNIDDETTKVVRNRCSSCGYIVNEASNTCTICNQDSSRLKSFFLSFDVLVDLTDHTGTLHSCSLSGSIAEETLGCTINEFLTMTSEQKTKLKWQLLLERSKIYLKLILSHRARGGLKVTILSCKLADPTEASRNLARQGHT
|
Single-stranded DNA-binding protein required for homologous recombination in meiosis I. Required for double strand breaks (DSBs) repair and crossover formation and promotion of faithful and complete synapsis. Not required for the initial loading of recombinases but required to maintain a proper number of RAD51 and DMC1 foci after the zygotene stage. May act by ensuring the stabilization of recombinases, which is required for successful homology search and meiotic recombination. Displays Single-stranded DNA 3'-5' exonuclease activity in vitro.
|
Q9D513
|
Q03PV7
|
RL3_LEVBA
|
50S ribosomal protein L3
|
Levilactobacillus
|
MTTKGILGKKVGMTQVFTDAGELIPVTVVEATPNVVLQVKTMENDGYNAIQLGYQDKREVLSNKPEQGHVAKANTTPKRFIREFTDVELGDYKVADEVKVDTFQAGDIVDVTGVTKGHGYQGNIHKDGQSRGPMAHGSRYHRRPGSLGAIINRVFPGMKLPGRMGNKQVTIQNLVIVKADVENNVLLIKGNVPGANKSLVTVKSAVRPPRPKQSEK
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
Q03PV7
|
Q6GUG4
|
P2Y13_RAT
|
P2Y purinoceptor 13
|
Rattus
|
MLGTVNTTGMQGFNKSERCPRDTRMTQLLFPVLYTVVFFTGVLLNTLALWVFIHIPSNSTFIIYLKNTLVADLIMTLMLPFKILSDSRLAPWQLRGFVCTFSSVVFYETMYVGIMMLGLIAFDRFLKIVVPFRKTFVKKTAFAKIVSISIWLLMFLISLPNMILNKEATASTVKKCASLKSPLGLLWHQVVSHTCQFIFWTVFILMLLFYTVIAKKVYDSYRKFKSRDSKHKRLEAKVFIVMAVFFVCFAPFHFVRVPYTHSQTTNKTDCRLENQLFLAKESTLFLATTNICMDPLIYIILCKKFTRKVPCMRWRTKTAASSDEHHSSQTDNITLS
|
Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system.
|
Q6GUG4
|
A3QCH0
|
GUAA_SHELP
|
Glutamine amidotransferase
|
Shewanella
|
MSNIHDHKILILDFGSQYTQLIARRIREIGVYCELWAWDVSEEQIKAFAPNGIILAGGPESVTADNSPRAPEYVFNAGVPVLGICYGMQTMSEQLGGKVIQGVGEGEFGYAQVEVQAASELFKSIEDAVSDSGKALLDVWMSHGDKVSEIPEGFVTVAKTDTCPYAAMANEEKRFYGVQFHPEVTHTRQGKRMLEHFALDICQCEANWKPSSIIEDAVARIKEQVGDDEVILGLSGGVDSSVVAMLLHRAIGSKLTCVFVDNGLLRLNEADQVLEMFGDHFGLNIVHVDAESRFLDALAGEAEPEAKRKIIGKVFVDIFDEESRKCVNAKWLAQGTIYPDVIESAGSATGKAHVIKSHHNVGGLPDDMELGLVEPLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELHKADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGRVSNRIINEIDGISRVVYDISGKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
A3QCH0
|
A1BBM5
|
4HYPE_PARDP
|
4-hydroxyproline 2-epimerase
|
Paracoccus
|
MTQYIFPCIDGHTCGNPVRLVAGGAPRLEGATMLEKRAHFLREFDWIRTGLMFEPRGHDMMSGAILYPPTRGDCDVAVLYIETSGCLPMCGHGTIGTITMGIENGLIVPRTPGRLSIETPAGKVDIEYRQEGRHVEEVRLTNVPGFLYAEGLTAEVEGLGEIVVDVAYGGNFYAIVEPQKNFRDMADHTAGELIGWSLTLRAALNQKYEFTHPEHPQINGLSHIQWTGAPTVPGAHARNAVFYGDKAIDRSPCGTGTSARMAQLAARGRLGVGDEFWHESIIGSIFKGRIEAAATVAGRDAIIPSIAGWARQTGLNTIFIDAERDPFAHGFVVK
|
Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate, which would allow P.denitrificans to grow on t4LHyp as a sole carbon source . Also seems to be involved in an alternative catabolic pathway that degrades trans-4-hydroxy-L-proline betaine (tHyp-B) to alpha-ketoglutarate; this pathway would permit the utilization of tHyp-B as a sole carbon and nitrogen source .
|
A1BBM5
|
A0A172M490
|
RLR63_PLAVT
|
Secreted RxLR effector protein 63
|
Plasmopara
|
MQRFPYSLLLLLLSATNRSRRHHITRPGRSIHWCLVRPTRPNRMLRAIRTCGARYWRNWPLNWPRKAGLTRRSSARIGLSDALRPCPTLFGCFKRRYARQAMSCYCRTEWRVNWLKKKRRGSSRWRRESSVWRCWK
|
Effector that partially suppresses the tobacco programmed cell death induced by cell death-inducing proteins.
|
A0A172M490
|
Q8CXR2
|
MTAP_LEPIN
|
5'-methylthioadenosine phosphorylase
|
Leptospira
|
MSYNVRAAIIGGTGLYSLEGMELIEEIFPDTPWGKPSDKIKIGKYKGKLIAFLPRHGIGHFLSPPEVPNHANICALKQLGVEEIVAFSSVGSLREEIKPLDFVLPSQIIDRTRFRNSTYFGNGVVAHAPFAEPFSPNLSKRIAQTAKKIGLEIHLDKTLVCMEGPLFSTKAESHLYRSWGADIINMTVLPEAKLAREAEIAYQMICMSTDYDCWREGEESVTVEMVIANLTKNAETAKKLLSELIHVLGNGDDLSLKNSTRYSIITAPEKRNSETVKKLRVLFPEYF
|
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
|
Q8CXR2
|
A9MF27
|
FTSB_SALAR
|
Cell division protein FtsB
|
Salmonella
|
MGKLTLLLLALLVWLQYSLWFGKNGIHDYSRVNDDVVAQQATNAKLKARNDQLFAEIDDLNGGQEAIEERARNELSMTKPGETFYRLVPDASKRAQTAGQNNR
|
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
|
A9MF27
|
Q4JUI9
|
RF1_CORJK
|
Peptide chain release factor 1
|
Corynebacterium
|
MSQSPSVIDDILAEYQGLEMQLSDPELHNDPAAARKVGKRFSELQPIIQTHQKLEQAREDQEAASEMASEDKEFAEEAKRLEEEISELEEQLTDLLAPRDPHDGDDIVMEIKSGAGGEEAALFAGELARMYQRYAERHGFSTEILGLNETDLGGVKDMTLSIRSKQPSRDGAWSEFKFEGGVHRVQRIPVTESQGRIQTSAAGVLVYPEPDEVEDVHIDDKDIRVDVYRSSGKGGQGVNTTDSAVRITHLPTNIVVTCQKERSQIQNRARAMQVLAARLQQLKEEEAEAEAAEGRAAQIRTMDRSERIRTYNFPESRVSDHRIGYKANNLDSVLDGDLEALLAALKEADRARRLEAED
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
Q4JUI9
|
A0L2B4
|
MEND_SHESA
|
Menaquinone biosynthesis protein MenD
|
Shewanella
|
MRTENTATLNLMWGALILEELARLGVQHVCMAPGSRSTPLTLAAAQQTKLKRHLHFDERGLGFMALGLAKASCAPVAIITTSGTAVANLYPAIVEAWLTHVPLIVLSGDRPPELLGCGANQAIVQPAIFANYAQQVNLPTPDAHIAPQMLLTTLDEAVANQTRPVHINCMYREPLYPSEMSGTILDSESPYLRPLQTWLQHAKPYTQYGKSEQLSSPSDDAIMRFVHGKGVIIAGTLTPEQDPQQLIALSQKIGWPLLTDAQSQLRQHPAAIGNIDQLLQHPKARNLLQEADRVLVFGGRLLSKRLIAYLAEQNWHSYWQVLPQQDRLDPSHNAKHIWHANAAQFAQLNWYRSSSANWANTLVTYNDELHSLFVRNIDQGEFGEAQVIRAIANTRPLEQQLFIGNSLPVRLYDMYAPVSCCTATTYTNRGASGIDGLLATACGIAAHQGKPTSLIIGDLSQLHDLNSFAIARSLTSPLVIIILNNDGGNIFNLLPVPNEELRSDYYRLSHGLEFGYAAAMFNLPYNQVDNLADFQSCYHEALDYQGASVIEVSVSQHQASEQIAALNLWVKQS
|
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
|
A0L2B4
|
P56936
|
REPA1_BUCAI
|
Probable replication-associated protein repA1
|
Buchnera
|
MIIRKCYINNPNPFFTPPKNNKRRPSFICYAMKRASEIDVARCELNYILQIKNIKIGFPVKRFRRLNEHRACAMRAMVLAMLYHFNISSDLVQASVEQLSDECGLSTLSKAGNKSITRASRLITNFMEPMGFVTCKKTWDKILGNYMPKMITLTPLFFMLFGVSEKKLMDAKKQQLGWINKNLISKGFKPITMIDAKRRSKDTQIKNIFQYRISKHAFYKKKRNAQRLISLDEKEARQTILRALVAKYSITELTKLGPNGLKKQVNISYYYLRKIATNTYPDN
|
This protein is essential for plasmid replication; it is involved in copy control functions.
|
P56936
|
Q10MI9
|
NAS2_ORYSJ
|
S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 2
|
Oryza sativa
|
MEAQNQEVAALVEKIAGLHAAISKLPSLSPSAEVDALFTDLVTACVPASPVDVAKLGPEAQAMREELIRLCSAAEGHLEAHYADMLAAFDNPLDHLARFPYYGNYVNLSKLEYDLLVRYVPGIAPTRVAFVGSGPLPFSSLVLAAHHLPDAVFDNYDRCGAANERARRLFRGADEGLGARMAFHTADVATLTGELGAYDVVFLAALVGMAAEEKAGVIAHLGAHMADGAALVVRSAHGARGFLYPIVDLEDIRRGGFDVLAVYHPDDEVINSVIVARKADPRRGGGLAGARGAVPVVSPPCKCCKMEAAAGAFQKAEEFAAKRLSV
|
Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serve as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
|
Q10MI9
|
Q0AUG8
|
RL1_SYNWW
|
50S ribosomal protein L1
|
Syntrophomonas
|
MKRGKNYQQAGEKFDRLTLYEPKEALELVKEIAKAKFDETVEVHIKLGVDPRHADQQVRGTVSLPNGTGKTRKVLVFAKGEKIKEAELAGADYVGGEDLAEKIQGGWFDFDVAVATPDMMAVVGKMGKILGPRGLMPNPKAGTVTFDIERTIKELKAGRIEYRVDKSAIVHAPIGRISFEVDKLQENLNAFAEALLKARPAAAKGQYMRSVTVCSTMSPGVKINPLVLMAANK
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
Q0AUG8
|
Q12D54
|
PPNP_POLSJ
|
Xanthosine phosphorylase
|
unclassified Polaromonas
|
MITEKIDNISVTTKANVYFDGKCVSHGITFTDGTKKSVGVILPATLTFNTGAPEIMECVAGACEYRLAGSDSWVKSAAGEKFSVPGNAKFDIRVAEGFEAYHYICHFG
|
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
|
Q12D54
|
P01418
|
3S11_DENVI
|
Neurotoxin 4.11.3
|
Dendroaspis
|
RICYNHQSTTPATTKSCGENSCYKKTWSDHRGTIIERGCGCPKVKRGVHLHCCQSDKCNN
|
Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
|
P01418
|
C3KCS7
|
MRAY_PSEFS
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Pseudomonas
|
MLLLLAEYLQQFHKGFAVFQYLTLRGILGVLTALCLSLFLGPWMIRTLQNLQIGQSVRNDGPQSHLSKSGTPTMGGALILSSIGISTLLWADLHNRYVWVVLLVTLLFGAIGWVDDYRKVIEKNSKGLPSRWKYFWQSVFGVGAAIFLYTTAPSAVETTLIIPMLKDASIPLGIGFVVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGALGIFCYLSGNVKFAEYLLIPYVPGAGELIVFCGALIGAGLGFLWFNTYPAQVFMGDVGALALGAALGTIAVIVRQEIVLFIMGGVFVMETLSVVIQVASFKLTGRRVFRMAPIHHHFELKGWPEPRVIVRFWIITVILVLVGLATLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
C3KCS7
|
B4U769
|
RS13_HYDS0
|
30S ribosomal protein S13
|
unclassified Hydrogenobaculum
|
MARIAGVDLPDHKKLEVALTYIYGIGWSKAREVCEQTGIPSIKKLGELTPEELNQLRRYIEQNIKVEGDLRREVQLNIKRLVDIGTYRGLRHVRGLPVRGQQTKTNARTRKGRRKGTVANKKKVSK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
B4U769
|
P34477
|
UBC7_CAEEL
|
Ubiquitin-protein ligase 7
|
Caenorhabditis
|
MEQSSLLLKKQLADMRRVPVDGFSAGLVDDNDIYKWEVLVIGPPDTLYEGGFFKAILDFPRDYPQKPPKMKFISEIWHPNIDKEGNVCISILHDPGDDKWGYERPEERWLPVHTVETILLSVISMLTDPNFESPANVDAAKMQRENYAEFKKKVAQCVRRSQEE
|
Catalyzes the covalent attachment of ubiquitin to other proteins.
|
P34477
|
B4R8N3
|
RL18_PHEZH
|
50S ribosomal protein L18
|
Phenylobacterium
|
MALSPRDTTKRRAQRVRTRLRKVANGRPRLSVFRSAKNIYAQVIDDERGVTLAAASSLEGEKKDKGSDKDAAARVGALVAQRAIEKGVKDVVFDRGGYLYHGRVKALADAAREAGLNF
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This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
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B4R8N3
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Q54GQ1
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MTMR_DICDI
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Myotubularin-related protein DDB_G0290005
|
Dictyostelium
|
MFSNKNTDNVENDNNNALGSVIARINSQNIITKNKAPVISEDFETQDFDYPSFDDETPNYDRPQPTMVENFTLLPGEFVLMITKNVVNLSLTTTTHRIGTLYQTNYQMFFIDDSTRQLVSTIANGQLLQIKKLKGHVTVKYHDNTTPNNNNNNNNNNNNNNNNTNNNNNNNINKSNNSSTDQLNSFSLEKQPSQNENLNNNNNNNNNNNNGNNNINNNNLMNSLTQPSTSSRSRLLKSNSTPINLNESSTSTNSPTLSSTTTTTTTTSSTNGNCSTNTWYSNGVSEKALILEIRCKDFMITRYCLPFNEKGNEAFELMNKLICNNYQDSNQLFSMSYSPFKGVISPIDGWLFYDPIEEYTRQGLIGNSNGSDEWRLTKMNSKYELCSTYPQHFIIPFSISDYLLNKSSSHRNKNRFPVVTWRHKQTHATLSRSSQQTGKSRCEEDELLIQAIRKSKTILPNNNNQQQQPQQQQQTLYIIDIKSTSSSPTSSSSSHCEDISHYSQCQIESECLSNIHELRESQLKLFKVIRNWNEKKGWSEIQSTGWLDQLSKLLMVTKKILTHLHLEGFSCLIHCIDGWDRTCQLSSLVQLCADPYYRTIKGFIVLISKEWLSFGHKFMTRNGQSISSTSTTTTNSSSNGQLTSSSSNTSISSNATTTTTTTTSSKQTSPVFLQFIDVVWQLTKQFPTSFEFSDSFLSVILHHLNSNLFGTFLYDSEKERQQNNLPTETQSLWTLLLSAQKNSSLLNPLFNQQLSNETSSTTNLTATTSIPLTNSTTLDQQLQFKNNNDDGVLFPNPKGVQLWSDYFLKWRNPPKASRKSNTLIAHSLGVSYVNGDLIAFQKKKRSRRSKDGASGSSSGSSGSSSKHHHHHHHHHHHHHHRKSTDEKDSKEKSSKSSRSRTSSSSKRKSLSTSSNSITQPDIKINETITTTTTTPTNTTTLTNTSTTPRNTTTLTNASTTPTTTTTTTTTTTPTKDETINESVQVNNDKLKSPSGDDIKQEQDEMNQFTSQHPNNQMESSSEINQQNEQSQLEQQQEQQQQQEQQLQHEQQQIEQQQLQKQQQQQEQQEQQELEQQEQPNETITYSMESDSQSSISQNQNQLQQQQQQQTLLDPIDESSLLATTTTTTSSTAITSASKLEKELRKQEKEKRKLEKEKKQKERAERKLEKEKKRDQKEREQKEKELLEQQKPKADITVVLQSPSKKKAMSLTMPVRGTKSRISIFSSPLVPTLHPNLSDQNSQTNSSGDNSGNVNNSPNLTSTPISNLSNNNNNNNNSNENSNNNNNNNNNNNDNTSFSKRIFKTLRGTKTFNREPTPTVGTALN
|
Phosphatase that acts on lipids with a phosphoinositol headgroup.
|
Q54GQ1
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Q6P632
|
NAA20_XENTR
|
NatB catalytic subunit
|
Silurana
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MTSLRPFTCDDLFRFNNINLDPLTETYGIPFYLQYLAHWPEYFIVAEAPGGELMGYIMGKAEGSVAREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNGEPDEDAYDMRKALSRDTEKKSIVPLPHPVRPEDIE
|
Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration.
|
Q6P632
|
Q975J3
|
RL5_SULTO
|
50S ribosomal protein L5
|
Sulfurisphaera
|
MAETQTVNPMRKLRLEKVTVNIGVGEAGERLQKAYQLLQELTGVKPVYTIAKRTIREFGVRKGAPIGVKVTLRGKKAEEFLNKVLAAVGHRIKASSFDEYGNVSFGIAEHVLIPGTRYDPEIGIFGMDVAITLVRPGFRVARRRRKKAHIPKRHRTVSKEEAMEFLKQNFNVTIVEG
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
Q975J3
|
A0JWY7
|
PSA_ARTS2
|
Proteasome core protein PrcA
|
Arthrobacter
|
MTQQFYVSPEQLMKDRADFARKGIARGRSVVVISCEEGIALVAENPSPSLHKIGEIYDKIAFAAVGKYNEFESLRQAGVRYADVRGYSYDREDVTARGLASVYAQSLGAVFTAEQKPFEVELAVAEVGGNQSDDHLYRLTFDGSIADEKRFIVMGGQADKVAETVEGGWQQELNFAGAIRLAMKGLVTDKEAGELPASALEVAVLDRASESTRGSRRAFRRLGDDEIAALLSKEN
|
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
|
A0JWY7
|
Q8X823
|
BIOF_ECO57
|
8-amino-7-ketopelargonate synthase
|
Escherichia
|
MSWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWKQGAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIVADRLSHASLLEAASLSPSQLRRFVHNDVTHLARLLASPCPGQQLVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGTCWLQKVKPELLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQGCWVTAIRPPTVPSGTARLRLTLTAAHEMQDIDRLLEVLHGNG
|
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
|
Q8X823
|
B6IVF3
|
RIMP_RHOCS
|
Ribosome maturation factor RimP
|
Rhodospirillum
|
MEAVERIGRIIEPSVEAMGYELVRVQLSGGQRPTLQIMAERSDGAAMTVEDCADISRAVSALLDVEDPLPGAYTLEVSSPGIDRPLTRLKDFERFAGFEARLETKAPVDGRKRFRGFLAGIEDDAVRLALPVEKKARKGAKAAPTRDAADAGEAGDAEATLVVIPFGLVLKAKLELTDELLTAAAAEQGAAPGTEGGAMEVEEDARPARRPHQPKPKKAKKKGPGRFSKAGAGEDVDGADGGPAAGPGAQDE
|
Required for maturation of 30S ribosomal subunits.
|
B6IVF3
|
Q32HR2
|
CBPA_SHIDS
|
Curved DNA-binding protein
|
Shigella
|
MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEAHFKEVAEAWEVLSDEQRRAEYDQMWQHRNDPQFNRQFHHSDGQSFNAEDFDDIFSSIFGQHARQSRQRPAARGHDIEIEVAVFLEETLTEHKRTISYNLPVYNAFGMIEQEIPKTLNVKIPAGVGNGQRIRLKGQGTPGENGGPNGDLWLVIHIAPHPLFDIVGQDLEIVVPVSPWEAALGAKVTVPTLKESILLTIPPGSQAGQRLRVKGKGLVSKKQTGDLYAVLKIVMPPKPDENTAALWQQLADAQSSFDPRKDWGKA
|
DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.
|
Q32HR2
|
B2FHZ1
|
ATPD_STRMK
|
F-type ATPase subunit delta
|
Stenotrophomonas maltophilia group
|
MSQALTLARPYARAAFATARDEGAFAPWSDALAFSAHVAVDPRVAALLANPELGRDDAVALLAPVSHGETYSRFLAILAESHRLPLLPEISGMFDALRAEAEHVVKATVTSAAELSAGELDAIKVALRKRFNREVDVTTAVDASLIGGAVIDAGDVVIDGSLKGKLARLQTALAN
|
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
|
B2FHZ1
|
Q8U3D6
|
ACDA2_PYRFU
|
ADP-forming acetyl coenzyme A synthetase II subunit alpha
|
Pyrococcus
|
MLDYFFNPRGIAVIGASNDPKKLGYEVFKNLKEYQGGKVYPVNVREEEVQGVKAYKSVKEIPGEVDLAIIVVPKKFVKQTLIECGEKGVKGVVIITAGFGETGEEGKREEKELVEIAHKYGMRIIGPNCVGIMNTHANLNATFITVAKKGNVAFISQSGALGAGIVYKTIKEDIGFSKFISVGNMADLDFADLMEYLADTQEDKAIALYIEGIKDGRRFIEVAKKVTKKKPVIALKAGKSESGSRAAASHTGSLAGSWKIYEAAFKQSGVLVANTIDEMLSMARAFTQPLPKGNRVAIMTNAGGPGVLTADEIDKRGLKLANLEEKTIEELRSFLPPMAAVKNPVDMIASARGEDYYRTAKLLLQDPNVDILIAICVVPTFAGMTPTEHAEGIIRAVKEVNNGKPVLALFMAGYVSEKAKELLEKNGIPTYERPEDVAAAAYALVQQAKNVGGGVNG
|
Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as phenylacetyl-CoA, indoleacetyl-CoA and isobutyryl-CoA, but not succinyl-CoA. Seems to be involved primarily in the degradation of aryl-CoA esters to the corresponding acids. Participates in the conversion of acetyl-CoA to acetate and in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.
|
Q8U3D6
|
B7J4C0
|
ISPD_ACIF2
|
MEP cytidylyltransferase
|
Acidithiobacillus
|
MERVWVVIPAGGRGQRFGAAQAKQYVLLRDRPVIAHTLAAFLGEPRIAGIQLVLPGEDIATGAWRELLGPMPAPLLPPVVGGGLRADSVRLGLEALLRQGAVPSDWVLVHDAARPCLRREDLLRLLESLANAPQGALLAVPVADTLKRGEDGCSSGTVDREGLWRALTPQAFPLGALLAALEAARAGNRQITDEASAMEAQGWRPRLIPGHGDNIKVTLSDDLMLAAAILAARSEEG
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
B7J4C0
|
Q7VJV1
|
FLGI_HELHP
|
Basal body P-ring protein
|
Helicobacter
|
MRRKNNNKIWIWVATLILSISALYGQKINQIAQIVGIRDNSLVGYGLVIGLNGTGDKSGSKFTMQSIANMLESVNVKLSANDIKSKNVAAVMVTASLPPFARQGDKLDILVSSIGDAKSINGGTLVMTPLTGVDGNIYALAQGNITFGESGSTLSGTIIGGASVEREIAYNLYNQENATLSLKSSDLQNAIKIQQALNDVFRDAIAVAVDARTIKLKKPENLSMVEFLALVEEVEIDYSRKERIVIDEKSGTIVAGVGITIDPVVVTHGDITIKISDEMPDDPEAIKLEDGTMMSRAQGTISSTNGTKPTVSSVVKALQRMGATPRNVISILESMKKSGALNADIEVM
|
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
|
Q7VJV1
|
Q82S12
|
FPG_NITEU
|
DNA-(apurinic or apyrimidinic site) lyase MutM
|
Nitrosomonas
|
MPELPEVEITRRGIDTHLAGRVITQISIRNPVLRWPISAGLIALLPGQRINAIARRAKYLLFACSRGTLIMHLGMSGNLRVLPESTPPQLHDHFDLQVDNGMMLRFRDPRRFGAILWWDGDIRQHPLLQKLGPEPLSDDFDGQFLYTKTRGRNASIKEVLMNQHIVVGIGNIYANEALFQAGISPLAAAGSLNTMQCERLVDAVKATLLRAIKAGGSSLRDFTDCEGSPGYFQQQYWVYGRAGQSCRQCGELVSKTRQGQRSTFFCARCQH
|
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
|
Q82S12
|
Q9KU20
|
RLUD_VIBCH
|
rRNA-uridine isomerase D
|
Vibrio
|
MAHQIELTQTVKDSQLGQRLDQAVAELFTDFSRSRLKEWLLEGKIAVNGDVITKPRTKVMGGEVITVQAELEDEQRWEAQDLPLNIVYEDDDIIVINKPRDFVVHPGAGQADKTVLNALLFHYSPIAEVPRAGIVHRLDKDTTGLMVVAKTVPAQTRLVRALQKRDVTREYEAIVIGTMTAGGMIDKPIGRHSTKRTLMSVSPMGKHAVTHYRVAEHFREHTRLRLRLETGRTHQIRVHMAYLQHPLLGDTAYGGRARIPKGATEELTEMIRDFDRQALHAVMLKFEHPVTGEELEFHAPVPDDMVEMTLALREDAKLNRTEEY
|
Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA.
|
Q9KU20
|
C5CUX0
|
RF2_VARPS
|
Peptide chain release factor 2
|
Variovorax
|
MDAEQINQIGATLADLSARTADLRRYLDYDAKAERLRTVNASLEDPNVWNDPKKAQELGREKKSLDDVVVTLDRLTSGLSDNTELYEMSKEDGDMDGLQSIADDAAALETDIKQLEFRRMFNNPADPLNAFVDIQAGAGGTEACDWASMLLRQYLKYAERKGFKTQIEDETPGDTAGIKGATIKVEGDYAFGLLRTETGVHRLVRKSPFDSSGGRHTSFASIFVYPEIDDSIEIEINPADVRTDTFRASGAGGQHINKTDSAVRLTHIPTGIVVQCQDGRSQHSNRDVAWKRLRSRLYDHEMRKRQEEQQKLEDSKTDVGWGHQIRSYVLDNSRIKDLRTNVEVSATQKVLDGDLDVFIEASLKQGV
|
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
|
C5CUX0
|
Q92A57
|
SCPA_LISIN
|
Segregation and condensation protein A
|
Listeria
|
MVEMNFKVEAFEGPLDLLLHLIGQLEVDIYDIPMAEITDQYMEFVHTMQEMELDVASEYLVMAATLLAIKSKMLLPKQELEIDYDTLEEEEDPRDALVEKLMEYKRFKEAAKELKEKEAERSFYFSKPPMDLAEYDEGTKVAELDVSLNDMLSAFNKMLRRKKLNKPLHTRITTQEISIDDRMNSVLGKLHQQTNHRLRFDELFEEQTKEQLVVTFLALLELMKRKLVEVEQSASFADLYVQGKGEELS
|
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.
|
Q92A57
|
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