Datasets:
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accession
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Full Name
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147
⌀
taxon
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46
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
6
10
Q47UU9
EFTU_COLP3
Elongation factor Tu
Colwellia
MAKEKFERNKPHVNVGTIGHVDHGKTTLTAAISAVLTKVHGGEVKDFAQIDNAPEERERGITINTSHIEYDTEARHYAHVDCPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHILLSRQVGVPFIIVFMNKCDVVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALQGDEAWEAKIIELADALDTYIPEPERAIDGAFIMPIEDVFSISGRGTVVTGRVERGIIKIGEEVEVVGIRDTQKSTCTGVEMFRKLLDEGRAGENCGVLLRGLKREDVERGQVLCAPGSILPHTKFESEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVELPEGVEMVMPGDNLKFVVELINPVAMDEGLRFAIREGGRTVGAGVVSKIMA
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Q47UU9
A0A0D1E6B3
PIT1_USTMA
Proteins important for tumors 1
Ustilago
MERHDGEEYIPAIFGGQPPHASQVISLMKFSQETTTWNLPIMIAQALLVSEVIRTYPAELRMLHRLFQRKHPNMAEIFFILIKYLTIFAVIFDILVTETFAARTDFDCRSWAWTSSTFYFMCSTLVFCVIGWRARIIFRTSQVASWSLSVGLMGQFAVAMWTNYRVDKADALTPAGTCAPAAQVHADASQRNAALQLHFWQSSTFWFLLYNTIFESSILMACCIKLRKTSSGPSGLTKIAKVLFSNNVHYMAGVETCNVIELVMLLGWTSSLPPVHITSIAIQIVVGLQMLIGEQEAVYSPTCSQLSYSQYSSDSGGYINKHHAATSSSNGTFSTPSRTLSYVKRPGTGTTVADIGCADASGGGQHGRKGTFSSISSVPAYVKANPIVETVSPQMPSKAQSQSIPYKREVEVTVDMSPVPPPPGPSPAPLPAPYM
Plasma membrane virulence factor required for spreading and inducing tumors in infected leaves.
A0A0D1E6B3
P62449
HIS6_BACC1
ImGP synthase subunit HisF
Bacillus cereus group
MLAKRVIPCLDVKEGRVVKGVNFIGLQDVGDPVEIAALYNDAGADEIVFLDITATHEGRKTIVDVVEKTASKVFIPLTVGGGISNVKDMYNLLRAGADKVSINSAAVRNPKLIGEGAEHFGSQCIVVAIDARKVAEDKWNVYVNGGRVDTGMDAIRWAKRVTELGAGEILLTSMDADGTKNGYDLRLTEEISKSVSVPVIASGGCGHADHIIEVFQKTAVDAALAASIFHYGEATIGDVKRKLRNANVEVRL
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
P62449
A8FPE0
TDH_SHESH
L-threonine 3-dehydrogenase
Shewanella
MKALSKLKPEEGIWMVDAPKPEMGHNDLLIKIRKTAICGTDIHIYNWDEWSQKTIPVPMVVGHEYVGEVIDMGIEVRGFDVGDRVSGEGHITCGHCRNCRGGRTHLCRNTSGVGVNRDGAFAEYLVIPAFNAFKIPDDISDDLASIFDPFGNAVHTALSFDLVGEDVLITGAGPIGIMAAAVCRHVGARHVVITDVNEYRLELANKMGATRAVNVAKESLEGVMEELGMTEGFDVGLEMSGVPSAFHSMLDTMNHGGKIAMLGIPGGEMAIDWSKVIFKGLILKGIYGREMFETWYKMASLIQSGLDISPIITHHFKIDDFQQGFDAMRSGQSGKVILNWD
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
A8FPE0
P49748
ACADV_HUMAN
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Homo
MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDALTRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRALEQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF
Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats . The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA . Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains .
P49748
Q7V8L0
MURA_PROMM
UDP-N-acetylglucosamine enolpyruvyl transferase
Prochlorococcus
MPAAVSISQEILKPHLEIQGGHTLSRELKVSGAKNSALVLMTSALLSEGPLELHNVPQLTDIQGMADILASLGVRVKRSQETVWLQADGLHHAEPPYDLVNGLRASFFCIGPLLGRLGHAKVPLPGGCRIGARPVVEHIRGLKALGAMVKVEHGVVTASVPGTSRRLKGAAIVLDCPSVGATETILMAAVLAEGTSTIENAAQEPEVQDLAKMLNAMGARVSGAGGPIITIEGVERLHGCNYSVIPDRIEAGTFLIAAAITRSIVRVSPVIPEHLNAVLQKLRDCGCTLEIDKQGITLIPGDLHGVDIITQPFPGFPTDLQAPFMALLTTAKGTSVVTEKIYENRMQHVAELQRMGASIRLQGNTAVVEGIPQLSAAPVSGNDLRAAAALVLAGLAAHGISQVDGLNHLDRGYDEIETKLNASGAHILRHQPSG
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Q7V8L0
P53700
CCHL_CANAW
Cytochrome c heme lyase
Candida
MGWFWADKPSQDTVKATSSFTTPSACPIDHSKLASSSPTCPVKLNNDNDEVLNPLNNMPMAISSERAPGQRIKLSTERTISTIPRGESEDQGLWEYPSPQQMLNAMLSKGKGDGVPEDAVESMVEVHNFLNEGAWQQILTWEDQYTQQTKVEPRLKKFTGRPHDLSPKARMYLWLGQLFPETFNTIPPFDRHDWTVLRSCGRNQGWKEVRYVIDYYGAPDDEETGMPAFMLDTRPALDNLTNARDRFTHWAYPLWKKAMGEVRD
Lyase that probably catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
P53700
A6LMR3
COAX_THEM4
Pantothenic acid kinase
Thermosipho
MKILFDVGNTHTTVALTENGKFFKIKRISTYSIQTEDELYAYLKVFFGETYDEVIVSSVVPNINHVFEFFSKKYAGKSAIFLNAQSYKGITWNVKIPSEIGADRVANIIAAERDYGKDAIVVDFGTAITIDILKEKSYEGGIIIPGFSMMINALFKGTAKLPKVELKPFNGFIGKDTESNIRIGIINTVVEGIGSVINKIKNENFRDVPVIFTGGQSKIIMDYKRDVIYDLELGLRGIYYFYESVVS
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
A6LMR3
Q0AIH5
IF1_NITEC
Translation initiation factor IF-1
Nitrosomonas
MAKEETIQMQGEVIETLPNATFRIKLENGHIVLGHISGKMRMNYIRILPGDKVTVDLTPYDLTRARITFRTK
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Q0AIH5
P0CI71
K0319_RAT
Dyslexia-associated protein KIAA0319 homolog
Rattus
MVSPPGVLSSLLLLAAMAGGSSQQCSEGRTYSDAIISPNLESIRIMRVSHTFSVGDCTAACCDLPSCDLAWWFEGSCYLVNCMRPENCEPRTTGPIRSYLTFVRRPVQRSGQLLDYGDMMLGRGSPSGAWGDSLEDLRKDLPFLGKDGGPEETAEYSDDYKELERGLLQPSNQQDPRGSAEYPDWSLLPSSDGDFNASATGDNSAASTEKLQDLTPYPLDQEQLQSLNESTWSPTPRHSEMSSMWPSSVTASPTEEGLEGEETLQLQEQPNNSSGKKVPMPSHNPSPASLESSPTTVEKSSIFTVTPWSRDPGTPTFPASTVLPGLISPSWPLSPTTSRTVKALAVSAGDNLVLTLPNGEAELKASVEPAPPADTAYTYEWSLMSHPVDFQGKIKQENKPTLHLSQLSVGLYAFRVAVSGENAFGEGYVNVTVMPAARINQPPVAIVSPQIQELSLPLTSALIDGSQSTDDAEIVSYHWEEVDGPFLGEAFLDDSPLLRLSNLDPGNYTFRLTITDSDGATNSTTAALIIRGSLDYPPVANAGPNQTITLPQNTIILNGNQSSDDHQIVLYEWFPDPGGESKEMVMQGAQTPYLHLSELQEGEYTFQLMVTDSSGQQSTALVTLTVQAENNQAPVAVAGPDKELVFPVQSAMLDGSRSSDDHGIVCYRWEHIRGPSAVEMENVDKAIATVTGLQVGTYHFRLTVRDQQGLSSTSTLTVAVKKENNSPPRAQAGGRHVLMLPNNSITLDGSRSTDDRGIVSYLWIRDGQSPAAGDIIGSSDNGAALQLTNLVEGVYTFHLLVTDSQGASDSDTAIVEVLPDPKKDGMVELILQVGVEQLTEQQKETLVRQLAVLLNVLDSDVKVLKIQAHTDVSTVIVFYVQSGSPFKVLRAADVARNLHKRLSKEKGAFLLFKVLRIDTAGCLLKCSGHGHCDPITKRCICSQLWMENLLQRYMWDGESNCEWSVFYVAALALTLTVLTGAVTWVCICCCRRRKRTKIRKKTKYTILDNMDEQERMELRPKYGIKHRSTEHNSSLMVSESEFESDQDTLFSQERMERGVLKGSLNGSARSGVSFGYYSKDR
Involved in neuronal migration during development of the cerebral neocortex. May function in a cell autonomous and a non-cell autonomous manner and play a role in appropriate adhesion between migrating neurons and radial glial fibers. May also regulate growth and differentiation of dendrites.
P0CI71
Q58CN7
CDKA2_BOVIN
DOC-1-related protein
Bos
MSYKPIAPAPSSTPGSSTPGPGTPVPTAGSVPSPSGSVPGAAGPFRPLFNDFGPPSMGYVQAMKPPGAQGSQSTYTDLLSVIEEMGKEIRPTYAGSKSAMERLKRGIIHARALVRECLAETERNART
Plays a role in regulating the self-renewal of embryonic stem cells (ESCs) and in maintaining cell survival during terminal differentiation of ESCs. Regulates microtubule organization of metaphase II oocytes. Inhibits cell cycle G1/S phase transition by repressing CDK2 expression and activation; represses CDK2 activation by inhibiting its interaction with cyclin E and A.
Q58CN7
Q81C68
SSUB_BACCR
Aliphatic sulfonates import ATP-binding protein SsuB
Bacillus cereus group
MTVSIDGVSKYFLKQTGTVQVLENINFQLEEGDFVTVIGPSGCGKSTLLKIVAGLDNDFEGEVVIDGEPILKTSKKQGFIFQEHRLFPWLTVEENIAADLSLKDKYVKDKVREWVEIVRLDGFEKSYPKEISGGMSQRVAIARALLRDPNVLLLDEPFGALDAFTRSHLQEVLLNIWEQKKTTMIFVTHDIDEAIYLSNRIIIMSAKPGKIHKVIENNLPYPRNKTSQSFQQLRTKVLQQFEYGGLIQTSI
Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Q81C68
B0BX35
SYE1_RICRO
Glutamyl-tRNA synthetase 1
spotted fever group
MTKVITRFAPSPTGMLHVGNIRAALLNWLYAKKHNGQFILRFDDTDLERSKQEYKDAIEEDLKFLNINWDQTFNQLSRLSRYDAIKNLLLDKKRLYACYETPEELELKRKFQLSKGLPPIYDRASLNLTEEQAKKYIEQGRKPHYRFLVNHEPISWHDMIKGEVKYDGKALSDPIVIRADGSMTYMLCSVIDDIDYDITHIIRGEDHVSNTAIQMQMFEALNTTPPTFGHLSLIINKDEKISKRVGGFEIATLRKEIGIEAMAIASFFSLLGSSAQILPYKSMEKLANQFEISSFSKSPTIYQPEDLERLNHKLLISLDFDTVKERLKEIDAEYIDENFWLSVSPNLQKLRDVKDWWEICHQTPNVENLNLDKEYLKQAAELLPKGEITKDSWSIWTKEITNITGRKGKELFLPLRLALTARESGPEIASVLPLIDREEIIKRLTSA
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
B0BX35
B1I461
PLSY_DESAP
Lysophosphatidic acid synthase
Candidatus Desulforudis
MSALAVILVIGLSYLVGSVPTGYLIARHVKGIDIRGHGSGNIGATNVWRTLGPGWGLASLVGDTAKGIVAVLLGRAVGVPGLELLTGAAALTGHGWSVFLRFQGGKIIATSLGVLIMLPPVALATAAAVWIAVLALTRYVSLASIIAASSVPLAFALGGVGWRHVLFGLFLALVAVYKHRANIDRLLKGKESRFSFRK
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
B1I461
P60850
ALBA_METMP
DNA/RNA-binding protein Alba
Methanococcus
MDNIVYVGNKGVMNYVLAVITQFNSENAQEVIVKARGKAISRAVDVEEMVTKRFMPEVKIKEINLGTDHIQGEDGKSINVSTIEIILFK
Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
P60850
Q9CP05
PEPT_PASMU
Tripeptide aminopeptidase
Pasteurella
MLNQQQTYKLLERFLHYTTYDTQSKSGAKISPSSAGQLKLAKHLQQELFALGLQDIDISKHSVVTAFLPSNVNPHSPTIGFIAHLDTATQCSGKNVQAEVIENYRGGDIALGVGEEFISPAHYQFLHQLIGKTLVVADGNTLLGADNKAGIAEIMTALAVLKEENLPHCNIRVAFTPDEEIGLGMQFFPVEKFPCDWAYTIDGGEVGELEYENFNAATAIVTIEGVNMHTGSAKDKMINALTLACEFQQGFPAEETPEQTEGKQGFYHLSHFTGHVEKVELQYLIRDFDRDGFEQRKIFIQQLVDRFNQQKRLKKPITLEIKDSYKNMNEVVKTVPQSVELADSAMRECGIEPIHKAIRGGTDGAWLAEQGLACPNVFTGGYNFHSKHELITLEGMQSAVNVITTIVRLATS
Cleaves the N-terminal amino acid of tripeptides.
Q9CP05
Q73YQ3
MURE_MYCPA
UDP-N-acetylmuramyl-tripeptide synthetase
Mycobacterium avium complex (MAC)
MVSVPTGLRPSAVPGVRLPALADQVGAVMAGPDRRAAVPDVTVTGVTLRAQDVLPGDLFAALPGATTHGARHAAEAIERGAVAVLTDAAGVAQLTGGRTTPTLLHPRPRSVLGQLAAAVYAHPSERLTVIGITGTSGKTTTTYLVESGLRAAGRTAGLIGTVGIRIDGADIPSALTTPEAPALQALLAAMAEQRVDTVVMEVSSHALALGRVDGTRFAVGGFTNLSRDHLDFHPTMADYFEAKALLFDPNSPLRAHRAVVCIDDEAGREMAARAGDAVTVSAEGQPAHWRAVEVAPLGTGGQQFTVIDPAGVQHRAGIRLPGHYNVANCLVALALLDAVGVSPEQAAPGLLQTRVPGRMEEIDAGQDFLALVDYAHKPGALRAVLSSLKRPDRRLAVVFGAGGERDPGKRAPMGATAAELADLVVVTDDNPRGEDPAAIRREILAGVTESGCAAEVVEIGDRRAAIRHAVAWAGPGDVVLVAGKGHETGQRTGEHTRPFDDRVELAEALREAVGPRKAQG
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Q73YQ3
B3QL20
RSGA_CHLP8
Small ribosomal subunit biogenesis GTPase RsgA
Chlorobaculum
MNETLSGVVTRVTGATYIVETGDGPKVRCRTVPSTVSENEGSNLVAVGDRVEFRPKASETEMAEGVIVRVEERRSVLERRREVRRNRSKEKEQVIAANIDQIVLITSFDDPPFNSRLVDRYLVFAESEHLPLLIVVNKIDLDEEGMVEEDLEVYRNLDCNICLVSAEDGRGIEELRELLRDRLSAFSGHSGVGKSTLINLLVGREELRTAETSGKTGKGVHTTTSSAMFQLPGGGYVIDTPGIREFNLAGITRENLRFYYTEFLRFMPECAFSSCSHTVEPGCAVIAAVESGRIDAERYESYLALLDSLDE
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
B3QL20
A8X3A7
PAT2_CAEBR
Paralyzed arrest at two-fold protein 2
Caenorhabditis
MREGSFPRRTRLLCLLAAVVLISTVTSFNIDTKNVVLHHMANNYFGYSLDFYNEQKGMPVLVVGAPEAETTNPNLSGIRRPGAVYACSVNRPTCREVHVDKMKGNLKKLNGSHLVPIEDKAYQFFGATVKSNDKHDKLLMCAPKYKYFYSKFEVIEPVGTCFYAENGFEKTEEFSSCKQEPARHGRHRLGYGQCGFSGAIPGKKNQDRVFLGAPGVWYWQGAIFSQNTKNQTDRPNTEYGSKEYDHDMMGYATATGDFDGDGIDDIVAGVPRGNDLHGKLVLYTSKLKMMINLTDEVSTQHGQYCGGALAVADVNKDGRDDIIMGCPFYTDYGSVKDAKTQERKPQYDVGKVIVFLQTAPGVFGKQLAVVGDDQWGRFGHSLAAAGDLNLDGYNDVIVGAPYAGKNKQGAVYVIHGSKDGVREKPTQKIEASQIGHGTARAFGFAVAGGVDVDGNGMPDIAVGAWKSGNAAVLLTKPVVTVTGATEPESALINVEEKNCDVDGKLGKQACRHINTCFKYEGKGDTPNDLEFDLRFNLDDHSPEPRAYFLQKDVKSDRSIKVASGSKTRDHPSSIEQRVRLEKGRQKCFRHRFFASSTMKDKLSPIHWSVNYTYVESKSGKLRGDKLEPAIDTTVPLSFQNKINIANNCGKDDLCVPDLKVTAVADREKFLLGTQDNTMLINVTVQNGGEDSYETKLYFDVPQGFEYGGIESVGADGSAPACSPTSDEPDSDGKWTFACDLGNPLPANKVVSSVVRVTASSDKPPLAPISINAHVNSSNDEEAHTIADNKVTFTIPVDFKNQLSLNGRSNPEQVDFSMTNKTRSDVFDDNEIGPVVSHLYQISNRGPSEIDAATLDIFWPSFSTEGGHLLYIITEPVVNPPNKGRCRVKQLQNVNPLNLRITNEHVPTEPPVAKTPNEYSREEDDESYEDETTTQSQTHHQTRTEHTQHHQGPVHVYERDEDKIRQNTGNWQYVEDKKKKGDYEYIPDDQEYDGDDFEDDDEDFDRAGSKRVKRAPVPKKKKKEGSRSGEPRSDKARFSDLREAVKLSKEAGGVVDYKGPLSRASVDCNGLRCTHIECDIYDLKEDEFVLVEIFSRLYTNTLVDERNPGGDISSLALARVTSTKYNWPHKPTLITAVSTNMNAIASEEGRDLPWWLYLLAILIGLAILILLILLLWRCGFFKRNRPPTEHAELRAEKQPAAHYADTQSRYAPQDQYSQGRHGQML
Required for muscle development probably through the regulation of the actin-myosin cytoskeleton. During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably through lamins such as epi-1, lam-2 and unc-52. Required for distal tip cell migration and dorsal pathfinding. Required for egg-laying. May play a role in cell motility and cell-cell interactions.
A8X3A7
A6VIV7
ILVD_METM7
Dihydroxy-acid dehydratase
Methanococcus
MISDNVKKGVIRSPNRALLKACGYSDEDMEKPFIGVVNSFTEVVPGHIHLKTLSEAVKHGVYANGGTPFEFNTIGICDGIAMGHEGMKYSLPSREIIADAVESMARAHGFDGLVLIPTCDKIVPGMIMGALRLNIPFIVVTGGPMLPGEFQGKKCELISLFEGVGEYQVGKITEEELKSIEECACPGAGSCAGLYTANSMACLTEALGLSLPMCATIHAVDAQKVRIAKKTGSKIVDLVKEDVKPTDILTKEAFENAILVDLALGGSTNTTLHIPAIANEIENKFITLDDFDRLSNEVPHIASIKPGGEHYMIDLHNAGGIPAVLNVLKGKIRDTKTVDGRSTLEIAESVKYINYDVIRKVEAPVHETAGLRVLKGNLAPNGCVVKIGAVNPKMYKHDGPAKVYNSEDEAISAILGGKIVEGDVIVIRYEGPSGGPGMREMLSPTSAICGMGLDDSVALITDGRFSGGSRGPCIGHVSPEAAAGGVIAAIENGDIIKIDMIGKEINVDLDESVIKERLSKLDEFEPKIKKGYLSRYSRLVSSADEGAVLK
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
A6VIV7
A6MMB4
RPOB_CHLSC
Plastid-encoded RNA polymerase subunit beta
Chloranthus
MLRDGNEGMSTIPGFNQIQFEGFCRFIDQGLTEELHKFPKIEDTDQEIEFQLFVETYQLVEPLIKERDAVYESLTYSSELYVPAGLIWKTSRDMQEQTVFIGNIPLMNSLGTSIVNGIYRIVINQILQSPGIYYRSELDHNGISVYTGTIISDWGGRSELEIDRKARIWARVSRKQKISILVPSSAMGSNLREILDNVCYPEIFLSFPNDKEKKKFGSKENAILEFYQQFACVGGDPIFSESLCKELQKKFFQQRCELGRIGRRNMNRRLNLDIPQNNIFLLPRDVLAAADHLIGMKFGMGTLDDMNHLKNKRIRSVADLLQDQFGLALVRLENVVRGTICGAIRHKLIPTPHNLVTSTPLTTTYESFFGLHPLSQVLDRTNPLTQIVHGRKSSYLGPGGLTGRTASFRIRDIHPSHYGRICPIDTSEGINVGLIGSLAIHARIGHWGSIESPFYEIYERSKEVQMVYLSPSRDEYYMVAAGNSLALNQGIQEEQVVPARYRQEFLTIAWEQIHLRSIFPFQYFSIGASLIPFIEHNDANRALMSSNMQRQAVPLSRSEKCIVGTGLEHQAALDSGVSVIAEHEGKIIYTETNKIVFSGNGDTISIPLVMYQRSNKNTCMHQNPQVQRGKCIKKGQILAGGASTVGGELALGKNILVAYMPWEGYNSEDAVLISERLVYGDIYTSFHIRKYEIKTHVTSQGPERITKEIPHLEANLLRNLDKNGIVMLGSWIETGDILVGKLTPQTAKESSYAPEDRLLRAILGIQVSTTRETCLKLPIGGRGRVIDVRWIQKKGGSSYNPETIRVYISQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGRPVDMVFNPLGVPSRMNVGQIFECSLGLAGDLLDRHYRIAPFDERYEQEASRKLVFPELYEASKQTANPWVFEPEYPGKSRIFDGRTGDPFEQPVIMGKSYILKLIHQVDDKIHGRSSGHYALVTQQPLRGRAKQGGQRVGEMEVWALEGFGVAHISQEMLTYKSDHIRARQEVLGTTIIGGTILNPEDAPESFRLLIRELRSLALELNHFLVSEKNFQINRKEA
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A6MMB4
P0CB78
PYRE_STRPN
Orotate phosphoribosyltransferase
Streptococcus
MTLAKDIASHLLKIQAVYLKPEEPFTWASGIKSPIYTDNRVTLAYPETRTLIENGFVEAIKEAFPEVEVIAGTATAGIPHGAIIADKMDLPFAYIRSKPKDHGAGNQIEGRVAQGQKMVVVEDLISTGGSVLEAVAAAKREGADVLGVVAIFSYQLPKADKNFADAGVKLVTLSNYSELIHLAQEEGYITPEGLDLLKRFKEDQENWQEG
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
P0CB78
Q5F8D4
LEU1_NEIG1
Alpha-isopropylmalate synthase
Neisseria
MTQANRVIIFDTTLRDGEQSPGAAMTKEEKIRVARQLEKLGADIIEAGFAAASPGDFEAVNAIAKTITKSTVCSLSRAIERDIRQAGKAVAPAPKKRIHTFIATSPIHMEYKLKMKPKQVIEAAVKAVKIAREYTDDVEFSCEDALRSQIDFLAEICGAVIEAGATTINIPDTVGYSIPYKTEEFFRELIAKTPNGGKVVWSAHCHNDLGLAVANSLAALKGGARQVECTVNGLGERAGNASVEEIVMALKVRHDLFGLETGIDTTQIVPSSKLVSTITGYPVQPNKAIVGANAFSHESGIHQDGVLKHRETYEIMSAESVGWSANRLSLGKLSGRNAFKTKLADLGIELESEEALNAAFARFKELADKKREIFDEDLHALVSDEMGNMNAESYKFISQKISTETGEEPRADIVFGIKGEEKRASATGSGPVDAIFKAIESVAQSGATLQIYSVNAVTQGTESQGETSVRLARGNRVVNGQGADTDILAATAKAYLSALSKLEFSAAKPKAQGSGTI
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Q5F8D4
B1J508
KDSB_PSEPW
CMP-2-keto-3-deoxyoctulosonic acid synthase
Pseudomonas
MSLDFTVVIPARLRSTRLPGKPLLLIAGKPMVQHVWEQARKSGAGRVVIATDDASIVEACQAFGAEVLMTRADHESGTDRLAEVAAQLGLPADAIVVNVQGDEPLIPPVIIDQVAANLAAHPEAGIATLAEPIHDPETVFNPNAVKVVSDKNGLALSFSRAPLPWARDAFAKDRNQLPQGVPYRRHIGMYAYRVGFLQDFVSWGPCWLEQTEALEQLRALWHGVRIHVADAIEAPAVGVDTAQDLERVRRLLEA
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
B1J508
A2T352
PETG_ANGEV
Cytochrome b6-f complex subunit V
Angiopteris
MVEALLSGIVLGLIPITLAGLFVTAYLQYRRGDQLDL
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
A2T352
P81045
COX17_PIG
Dopuin
Sus
PGLAAAIPAPPESQEKKPLKPCCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI
Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2).
P81045
Q492U0
RNT_BLOPB
Exoribonuclease T
Candidatus Blochmannia
MICKDDHSTLRARFRGFYPVVVDVETAGLDANINALLEIAVATFKMDEYGWLCVDGSLNFHIKSFPGAIIQPESLAFNGIDLNSPLRAAVTEQEALHEIFEMVRQGIKTQGCSRAIIVAHNAFFDHSFLMAAVERVSFMEKNPFHPFVMFDTATLSGLVFGQTVLAKACACAGVFFDKNKAHSALYDTERTAMLFCELVNKWKRLGGWPLTPCCIES
Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
Q492U0
Q8Z8H8
COBD_SALTI
L-threonine-O-3-phosphate decarboxylase
Salmonella
MALFNSAHGGNIREAATVLGISPDQLLDFSANINPLGMPVSVKRALIDNLDCIERYPDADYFHLHQALARHHQVPASWILAGNGETESIFTVASGLKPRRAIIVTPGFAEYGRALAQIGCEIRRWSLREADGWQLTDAILEALTPDLDCLFLCTPNNPTGLLPERQLLQAIADRCKSLNINLILDEAFIDFIPHETGFIPALKDNPHIWVLRSLTKFYAIPGLRLGYLVNSDDAAVARMRRQQMPWSVNALAALAGEVALQDSAWQQATWHWLREEGARFYQALCQLPLLTVYPGRANYLLLRCEREDIDLQRRLLTQRILIRSCANYPGLDSRYYRVAIRSAAQNERLLAALRNVLTGITPAD
Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
Q8Z8H8
B1YB90
PDXT_PYRNV
Pyridoxal 5'-phosphate synthase glutaminase subunit
Pyrobaculum
MKAGVLALQGDVEEHIQAFRKAAQELGRSVEVVQVKRPQDLREIAVLAIPGGESTTIGALARRTGLLDALRDAIKGGLPTLGTCAGAIFLAKEVRDSVVGETKQPILGLMDIAVVRNAFGRQRESFEVDLREEGIGALKAVFIRAPAFTKAWGSARLAAPLKHPELGQIYAAAFQGHMVATAFHPELSTTAVHRYMLNLAKT
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
B1YB90
A8FD81
CODY_BACP2
GTP-sensing transcriptional pleiotropic repressor CodY
Bacillus
MALLQKTRIINSMLQDAAGKPVNFKEMAETLRDVIDSNIFVLSRRGKLLGYSINQQIENPRMKKMLEDRQFPEEYTKSLFNIPETSSNLDINSEYTAFPIENRDLFESGLTTIVPIIGGGDRLGTLILSRLQDTFKDDDLILAEYGATVVGMEILREKAEEIEEEARSKAVVQMAISSLSYSELEAIEHIFEELDGNEGLLVASKIADRVGITRSVIVNALRKLESAGVIESRSLGMKGTYIKVLNNKFLIELENLKSH
DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor.
A8FD81
Q9Z768
MNME_CHLPN
tRNA modification GTPase MnmE
Chlamydia
MLKHDTIAAIATPPGEGSIAVVRLSGPQAIVIADRIFSGSVASFASHTIHLGQVIFEETLIDQALLLLMRSPRSFTGEDVVEFQCHGGFFACSQILDALIALGARPALPGEFSQRAFLNGKIDLVQAEAIQNLIVAENIDAFRIAQTHFQGNFSKKIQEIHTLIIEALAFLEVLADFPEEEQPDLLVPQEKIQNALHIVEDFISSFDEGQRLAQGTSLILAGKPNVGKSSLLNALLQKNRAIVTHIPGTTRDILEEQWLLQGKRIRLLDTAGQRTTDNDIEKEGIERALSAMEEADGILWVIDATQPLEDLPKILFTKPSFLLWNKADLTPPPFLDTSLPQFAISAKTGEGLTQVKQALIQWMQKQEAGKTSKVFLVSSRHHMILQEVARCLKEAQQNLYLQPPEIIALELREALHSIGMLSGKEVTESILGEIFSKFCIGK
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Q9Z768
Q8DSK2
RECX_STRMU
Regulatory protein RecX
Streptococcus
MKITKIEKKKRLYLIEIDEAEHFYITEDTIVHFMLSKNKEILPEQLEEIKTFAQFSYGKNLALYYLSFKQRTEKEVKDYLIRHDINTTVISQILTQLKEEKWLDDSKYIDNILQQNLHSGDKGAFVLKQKLLQKGIESQLIEDMLKDFDFSSICIKTAQKLLKKYQSKLPKRALKDKLKQALTTKGFSYQEAQIALEDLDIENNSENEEELIYKELDKQYRKYSKKYENYELRQRLTQSLARKGFAFDAIKNALREYL
Modulates RecA activity.
Q8DSK2
P28715
ERCC5_HUMAN
Xeroderma pigmentosum group G-complementing protein
Homo
MGVQGLWKLLECSGRQVSPEALEGKILAVDISIWLNQALKGVRDRHGNSIENPHLLTLFHRLCKLLFFRIRPIFVFDGDAPLLKKQTLVKRRQRKDLASSDSRKTTEKLLKTFLKRQAIKTAFRSKRDEALPSLTQVRRENDLYVLPPLQEEEKHSSEEEDEKEWQERMNQKQALQEEFFHNPQAIDIESEDFSSLPPEVKHEILTDMKEFTKRRRTLFEAMPEESDDFSQYQLKGLLKKNYLNQHIEHVQKEMNQQHSGHIRRQYEDEGGFLKEVESRRVVSEDTSHYILIKGIQAKTVAEVDSESLPSSSKMHGMSFDVKSSPCEKLKTEKEPDATPPSPRTLLAMQAALLGSSSEEELESENRRQARGRNAPAAVDEGSISPRTLSAIKRALDDDEDVKVCAGDDVQTGGPGAEEMRINSSTENSDEGLKVRDGKGIPFTATLASSSVNSAEEHVASTNEGREPTDSVPKEQMSLVHVGTEAFPISDESMIKDRKDRLPLESAVVRHSDAPGLPNGRELTPASPTCTNSVSKNETHAEVLEQQNELCPYESKFDSSLLSSDDETKCKPNSASEVIGPVSLQETSSIVSVPSEAVDNVENVVSFNAKEHENFLETIQEQQTTESAGQDLISIPKAVEPMEIDSEESESDGSFIEVQSVISDEELQAEFPETSKPPSEQGEEELVGTREGEAPAESESLLRDNSERDDVDGEPQEAEKDAEDSLHEWQDINLEELETLESNLLAQQNSLKAQKQQQERIAATVTGQMFLESQELLRLFGIPYIQAPMEAEAQCAILDLTDQTSGTITDDSDIWLFGARHVYRNFFNKNKFVEYYQYVDFHNQLGLDRNKLINLAYLLGSDYTEGIPTVGCVTAMEILNEFPGHGLEPLLKFSEWWHEAQKNPKIRPNPHDTKVKKKLRTLQLTPGFPNPAVAEAYLKPVVDDSKGSFLWGKPDLDKIREFCQRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKEKEAAASEIEAVSVAMEKEFELLDKAKGKTQKRGITNTLEESSSLKRKRLSDSKGKNTCGGFLGETCLSESSDGSSSEDAESSSLMNVQRRTAAKEPKTSASDSQNSVKEAPVKNGGATTSSSSDSDDDGGKEKMVLVTARSVFGKKRRKLRRARGRKRKT
Single-stranded structure-specific DNA endonuclease involved in DNA excision repair . Makes the 3'incision in DNA nucleotide excision repair (NER) . Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble . Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA . Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes . Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II . Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity . Required for DNA replication fork maintenance and preservation of genomic stability . Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site . During HRR, binds to the replication fork with high specificity and stabilizes it . Also, acts upstream of HRR, to promote the release of BRCA1 from DNA .
P28715
Q05934
VID22_YEAST
Vacuolar import and degradation protein 22
Saccharomyces
MRAMDTQVQSAERGLVLPPMNSTVSSATAATTATNTDTDTDGDRDEERESLAEDGSEWVPAYMLTRDRSRYLGHFLGVDKMLEAVKCKYCGVIIRRQGNSISMAEASQTHLWSTHKIDPNANYYSGWTGVEAGSTFMVRPPLKNHQGGSATTNSIANLLEIDEDFLKRTREKEMALPLVQSLAIIIASENLPLSFVDNTAVRLLINQNANSLSFIDHDLILNAIRSIAYNLDRIIQRTALRNNSDLSLIIDKNYLLMDPTDRSNQLSNRLKNQLFEMQKINFFSLSHSVWNNTISILSIQYYDDFHSQVKTLPLIIQNLHEYNNDPKLSIPAQLLKISQELPGLQNTVISITLPRSQIVDLLNVMDSQPFFPNTYTNAKNYYHNCIISIINSAILPLFGTPKSADITHPRQSSFSKEPLTLLDSLIDLSNIDISNSIFSRINSFLDDLQSNSWQLDKFRSLCEKFGFEFVCSKFDLSRYSTATVSLQTFLNLRPIIEEYQSSIQIEKFNEIDFQIIDYLLITLNSINRILKFFTSSKSLNFTYVLFAIMSIEKHLLSTLGSLQFQRLIAPFETFLSKIQEFKTILFSDDMNLLAMFLCPAILFEREVLEYSFHTISLSEIVDKLSTSIFSLLKRFLNLHTIGNVNNSHNTSNHSNMNIHTDNQTNNINNRSGNNSDNNDNEHDNDNDNHSNSNTPASRIDIDPTGGENSVLPEQQPQNSNNNLSFGSLSDTHHLSDSTISKEIDSIFLQIIQEDLYDYLSTVNSIVPISYRSYCEQSNFIRDSGRFKKRIITEDSIIGELEQPMNFIEELLDIHVPVCNAFWSQYLDNDAGPIIRILFKIMQCQSSSSIRGEYSFLNDFIPRVHPDLTQEIIKIKLFNDQFVASKVDYDLDTLQTASQYLP
Has a role in the negative regulation of gluconeogenesis. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. This is an indirect role and requires cyclophilin A.
Q05934
P0CJ75
HMN8_HUMAN
MT-RNR2-like protein 8
Homo
MAPRGFSCLLLSTSEIDLPVKRRA
Plays a role as a neuroprotective and antiapoptotic factor.
P0CJ75
D7BMJ2
GLGE_ARCHD
(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase
Arcanobacterium
MSTLQHKTSSARRSSRRSVAAPDFVAVSRIPIVEVSPQLLDGTAPVKSTVDESFPVQATIFREGHDKFAARAVLVDGAGHTVDSVPMCDVSPGLFRFEGWLTPRVPGPHRFFVEAWSDPYATWLHNAEIKVPAGIDVGLVFAEAEVLFKAALKGTPVRSGERAAIRDALTVISKRRALPEVKLAAARSEEVRAAFAAYPVKELVSRSREYPVFVDRVRALVGSWYELFPRSVGATRDSESGEWTSGTLRTAATDLDRVAGMGFDVVYIPPVHPIGLTNRKGRNNSLTAVPGDPGSPYAIGSDAAGGHDAIEPSLGTFEDFDVFVGRAHELGMEVALDLALQCSPDHPWVKEHPEWFTARPDGTIAYAENPPKKYQDIYPLNFDNDPEGIYKEIKRVVELWVAHGVTIFRVDNPHTKPVGFWQRLLAEFRVEHPEVIFLAEAFTNPPMMQTLGTVGFHQSYTYFTWRNERQEIEEYLMEVSHESSHRMRPAFWPTTHDILTPYIQRGGISAAAIRAILAATGSPTWGIYNGYELIENIARPGAEEHIDNEKYEFKPRNYALAEQNGMATLLTMLNSIRSKHKALQRLRNVTINPTSNDKIVSFTKVARPEETADGVMDAVIVVVNLDPYASRDATVYLDLSPFGISPRWDGGPIIEVTDEMSGETYLWNEAPYVHLDPHGQVAHVLSVKVLS
Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
D7BMJ2
Q2S5G4
CYSH_SALRD
Thioredoxin-dependent 5'-adenylylsulfate reductase
Salinibacter
MAFASDESASPWSSTRLAALNAQFEPHGPKAILNWATHTFGDDLAQGTGFGPSGIVIMHMLADLRPGTTVFYLDTDLLFPETYELCDDLDERLDVDVTRVHGGLSLDEQAEQEGEELWNRNPNRCCFLRKVKPLRNFLDDRRAWITGVRRDQSERRADTDILSWEGQYGVFKINPLANWTQKEVWKYLFEHDLPYNPKHDQGYPSLGCVPCTEPVDQADGYSREGRWSDRDKTECGLHTSPEDEDGAHAAES
Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Q2S5G4
B0C7T1
CHLN_ACAM1
Light-independent protochlorophyllide reductase subunit N
Acaryochloris
MTLADAQPQALDFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMIFAEPRYAMAELEEGDISAKLNDYEELKRLCMQIKRDRNPSVIVWIGTCTTEIIKMDLEGLAPRLESEIDIPIVVARANGLDYAFTQGEDTVLAAMAHRCPKGSAVVEESEKQERGNAITSLLNFGKKKEEVVAEESEYHDHAPLVMFGSLPDPVVTQLTLELKKQGIKVNGWLPAKRFTELPVIDEGYYVAGVNPFLSRTATTLMRRRKCKLIGAPFPIGPDGTRAWIEKICSVLDVEPKGLEEREAKIWANLEDYLEIIRGKSVFFMGDNLLEVSLARFLIRCGMTCPEIGIPYMDKRYQGAELKFLEQTCIDMGVPMPKIVEKPDNYNQVQRIYEHDVDLVITGMAHANPLEARGINTKWSVEFTFAQIHGFTNARDILELVTRPLRRNNSLKDLGWDKLVKEEAKV
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
B0C7T1
A7NBV5
RUVA_FRATF
Holliday junction ATP-dependent DNA helicase RuvA
Francisella
MISFIKGVLIEKDPTALLIDVNGIGYEVFVPMTTFYTLGDIDSQVSLYTHFVVREDAQQLYGFKSKVDKKVFQELIKVNGIGARTAIAILSGMDSKTLLHCIENKDYALLATVPGIGKKTAERLVVEIYDKLLKMANEIYAQTSGTTTTSQDSQAQQAPTSVVLANSIFNESVDALLALGYKQKDAEKMARSAMGDATTAAEVIRKALQGSIKSKG
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
A7NBV5
A0QX66
BIOD_MYCS2
Dethiobiotin synthase
Mycolicibacterium
MTVLAVTGTDTGVGKTVTTAALACAARLARRDVAVCKPVQTGTIDGDDDLGEVRRLSGVTALHGGWRYPEPLAPVAAAGRAGAPLPTRTELVGSVRAVDAAGRLTIVEGAGGLLVALGADGVTLRDLAHDLGAQVLIVVSPGLGTLNHTALTLEALAAHGLSCAGLVIGAWPAEPGVAELDNRTALEALAPVRAVLPAGAGAASPERFEALSAAAFDADWITSLS
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
A0QX66
Q9JU49
PAND_NEIMA
Aspartate 1-decarboxylase alpha chain
Neisseria
MFRTMLGGKIHRATVTEADLNYVGSITVDQDLLDAAGIYPNEKVAIVNNNNGERFETYTIAGKRGSGVICLNGAAARLVQKSDIVIIMSYVQLSEPEIAAHEPKVVLVDGNNKIRDIISYEPPHTVL
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Q9JU49
Q9BJK5
NHR97_CAEEL
Nuclear hormone receptor family member nhr-97
Caenorhabditis
MSGDAQPSSNQRATEARPPPSPPLVNEKAAIGALCVVCGDRACSHLYYGVAACHGCKCFFWRTVKSRLNYVCRYGGNCSISTAGRNACRYCRFHRCLFVGMKIEAVKMDRKLTKRKKEKTDEDDTDDGGSHESFETTTDAKRAKFDNSLLISSLQLIDKTSSAGNAKLSTLHFVQPSLQNLLDEPELLDGFRSEMSYRATRQADEQLCYDSERRLVTWAIDWCRQTAEIADVHHTNDKISLLRASCAPLVLLELGCQSSFGPSDTQIPFCNNSFLSAHCIPPSTSFLRWKTIQSLNKWAQRELKPLCLRAKEIVLLKALIALNPDANGLSSDAESSIRMLRERVHTALFQLLMENSEPITAASRLAQILLLIPQLSLMGVDVIEQVKVRNTFNKRSAFGEGLLFWQLYGDIFDDANDDSYLEHSASCSPTDSQYTTDSI
Orphan nuclear receptor.
Q9BJK5
C3P9F1
HEM1_BACAA
Glutamyl-tRNA reductase
Bacillus cereus group
MHILVVSVNYRTAPVEFREKLTFQAAELERAMTTLQNQKSVLENVIVSTCNRTEIYAVVDQLHTGRYYIKKFLADWFQLEIEEVAPYLTIFEQDGAIDHLFRVTCGLDSMVVGETQILGQIKDSFLEAQQVKATGTIFNELFKQVITLAKRAHSETTIGESAMSVSYAAVELGKKIFGELTDCHVLILGAGKMGELALQNLYGSGARKVTVMNRTLSKAEIMAEKYMGHAKPLSELQCALLEADILISSTGASDYVITKEMMTKVEKMRSGRPLFMVDIAVPRDIDPAIDELEGSFLYDIDDLQGVVEANRAERLKEAEKIQFMIEEEIVLFKTWLSTLGVVPLISALRDKALAIQSETMESLERKIPNLSDRERKVISKHTKSIINQLLKDPILVAKEIAAEEGADEKLALFAKIFDLEMEDVESRAEEVEHKRVWTPSVPSL
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
C3P9F1
C1F647
RS12_ACIC5
30S ribosomal protein S12
Acidobacterium
MPTFSQLVRKGRTAPRYKTASPALQGSPQRRGVCTRVYTQTPKKPNSALRKVARVRLTNGIEVTTYIPGIGHNLQEHSIVLIRGGRVKDLPGVRYHVVRGTLDSVGVANRKQGRSKYGAKRAKGGAAAGKK
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
C1F647
A5U9E9
PAPA2_MYCTA
Polyketide synthase-associated protein A2
Mycobacterium tuberculosis complex
MFSITTLRDWTPDPGSIICWHASPTAKAKARQAPISEVPPSYQQAQHLRRYRDHVARGLDMSRLMIFTWDLPGRCNIRAMNYAINAHLRRHDTYHSWFEFDNAEHIVRHTIADPADIEVVQAEHQNMTSAELRHHIATPQPLQWDCFLFGIIQSDDHFTFYASIAHLCVDPMIVGVLFIEIHMMYSALVGGDPPIELPPAGRYDDHCVRQYADTAALTLDSARVRRWVEFAANNDGTLPHFPLPLGDLSVPHTGKLLTETLMDEQQGERFEAACVAAGARFSGGVFACAALAERELTNCETFDVVTTTDTRRTPTELRTTGWFTGLVPITVPVASGLFDSAARVAQISFDSGKDLATVPFDRVLELARPETGLRPPRPGNFVMSFLDASIAPLSTVANSDLNFRIYDEGRVSHQVSMWVNRYQHQTTVTVLFPDNPIASESVANYIAAMKSIYIRTADGTLATLKPGT
Catalyzes the acylation of trehalose-2-sulfate by adding the palmitoyl group at the 2'-position to yield the intermediate trehalose-2-sulfate-2'-palmitate (SL659).
A5U9E9
Q5B7T4
MICA_EMENI
Nonribosomal peptide synthase micA
Aspergillus subgen. Nidulantes
MVGSVVEAHRQSVGCLRNLSQLLAWASNTSGGLIFYSREDDVLTSTRISYAELLADAGEKARLIGQITGLSSESIILLHFDTQREVIEWFWAATLAGYLPAISTPFVDDTARRKAHLLHLHAQLNQPVVLTSKRLVPEFLGLEELRLHDVESLLSSAAKDGLIQYLGVQKLAEDVAVLMLTSGSTGSAKAVPLRHGQLLTAIQGKSTHHGTLPGDVFYNWVGLDHVASLTEIHLHALILGSDQVHTAASELLRNSLQFVRLLDTHKVAYTFAPNFFLTKVLDSLRENPTFTADLSSLKALISGGESNVVVTCDKLTRELRRRGVQAEVIRPGFGMTETCAGSIYSRACPSYDIRQSLEFASLGSCIPGMHMRIMSITEPGKLAAPGESGELQVAGPVVFDHYYNDETATRNAFTPDGWFITGDLGWIDDAGNLNLAGRTKDTIIVNGVKWSSTELEAAIEEEAVSGLVRSFTVVVPTRPPGSATEEIAVVYSPAYAPEDYHARYETAQVISKTVSLLTGTKPARLIPLPQSLLEKSSLGKISHSKVRAALESGEYASIERADQLILAQYRQFKWRPAKSDSERAVQKALVEFLQVPAEGINMDDSIYDLGVSSLNLILLRSTLQRMLDPKIDIPLSIILNNPTPGAIARSIDSSRSSLAGYNAIVPLQQHRHGGTPLFCIHPGSGEVLVFVALAAHFPTRPVYALRTRGYGSNEQLFGSIEETVETYATQIRQVQPHGPYAIAGYSLGSTLAFEVAKVLEAQGEEVKFLASIDYPPHIAHYVRDLNWTDVLLHIAFFLELIDEKTMVEVTPYLHTLDRQTALTHILNIGDAERARALAIDTKHLGLISDIAENFRVNVKTYKPQGKVQHLDVFVADPPTYAARDRKDWRENKLGRWVDFCETKVEFHDCPGIHAKMLNREHIAGFAKVFKAAMRRRGV
Microperfuranone synthase is the only protein required for the biosynthesis of the secondary metabolite microperfuranone from phenylpyruvic acid (PPA) . Several steps for the microperfuranione biosynthesis have been proposed . These steps include the activation of PPA, by the micA adenylation (A) domain to AMP-phenylpyruvic acid followed by loading of the PPA unit to the thiolation and peptide carrier (T) domain and eventually transferring to the thioesterase (TE) domain . After loading another PPA unit onto the T domain, aldol condensation establishes the carbon-carbon bond between the alpha- and beta-carbon of the two PPA units . Sulfur-assisted furan ring formation, TE domain mediated hydrolysis, decarboxylation, and keto-enol tautomerization would generate microperfuranone attached to the T domain . Finally, microperfuranone is released by the TE domain .
Q5B7T4
C3PP97
RL14_RICAE
50S ribosomal protein L14
spotted fever group
MIQMQSILEVADNSGAKKVMCIKVLGGSHHMVAKLGDVIVVSVKDAIPGGKVKKGDVYKGVIVRTKTGVVRPDGSTIKFDQNALVLLNKQDEPIGTRVFGPVTRELRAKKYVRIMSLAEEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
C3PP97
Q1GXD5
RBFA_METFK
Ribosome-binding factor A
Methylobacillus
MVKEFSRSDRVAEQIQRELADLLQFEVKDPRVSSMVTVTEVEVSGDMSHAKVYYTAPQGTPELQKGLEKTAGFLRSQLARRLLLRTVPQLHFVYDASIDRGMRIAKLIDEALPPVADPDQDSEPN
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Q1GXD5
P0A434
OPD_BREDI
Phosphotriesterase
Brevundimonas
MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSPTLRAS
Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate.
P0A434
B3PC22
QUEC_CELJU
Queuosine biosynthesis protein QueC
Cellvibrio
MSRKKAVILVSGGLDSTTVIAIARSQGYDCYTISFDYGQRHRAELKAAEITAKAHGSLEHKVIRLDLGAIGGSALTDTSIDVPEEETSGIPVTYVPARNTVFLSIALGWAEVLGALDIFIGVNAVDYSGYPDCRPDYIAAYETMANLATKRGIEGERLHIRTPLINLTKAQIIQQGLALGVDYRLTVSCYQANDGGEACGKCDSCRLRKQGFEQAGVADPTRYAF
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
B3PC22
B4U4Y3
TIG_STREM
PPIase
Streptococcus
MSTSFENKATNRGVITFTISQDKIKPALDQAFNKIKKDLNAPGFRKGHMPRPVFNQRFGEEVLYEEALNIVLPAAYEGAVAELELDVVAQPKIDVVSMEKGQEWTLTAEVVTKPEVKLGDYKDLTVEVEASKEVTDEEVDAKVERERNNLAELVVKEEAAVEGDTVVIDFVGSVDGVEFDGGKGDNFSLELGSGQFIPGFEEQLVGAKAGDTVEVNVTFPENYQAEDLAGKAAKFVTTVHEVKAKEVPELDDELAKDIDEEVETLDELKAKYRKELEASKEAAYDDALEGAAIELAVENAEIVELPEEMVHDEVHRSVNEFMASMQRQGISPDMYFQLTGTSQEDLHKQHEAEADKRVKTNLVIEAIAKAEGFEASDDEIEKEINDLAAEYSMPVEQVRSLLSADMLKHDIVMKKAVEVITSSAKAK
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.
B4U4Y3
Q9H7S9
ZN703_HUMAN
Zinc finger elbow-related proline domain protein 1
Homo
MSDSPAGSNPRTPESSGSGSGGGGKRPAVPAAVSLLPPADPLRQANRLPIRVLKMLSAHTGHLLHPEYLQPLSSTPVSPIELDAKKSPLALLAQTCSQIGKPDPPPSSKLNSVAAAANGLGAEKDPGRSAPGAASAAAALKQLGDSPAEDKSSFKPYSKGSGGGDSRKDSGSSSVSSTSSSSSSSPGDKAGFRVPSAACPPFPPHGAPVSASSSSSSPGGSRGGSPHHSDCKNGGGVGGGELDKKDQEPKPSPEPAAVSRGGGGEPGAHGGAESGASGRKSEPPSALVGAGHVAPVSPYKPGHSVFPLPPSSIGYHGSIVGAYAGYPSQFVPGLDPSKSGLVGGQLSGGLGLPPGKPPSSSPLTGASPPSFLQGLCRDPYCLGGYHGASHLGGSSCSTCSAHDPAGPSLKAGGYPLVYPGHPLQPAALSSSAAQAALPGHPLYTYGFMLQNEPLPHSCNWVAASGPCDKRFATSEELLSHLRTHTALPGAEKLLAAYPGASGLGSAAAAAAAAASCHLHLPPPAAPGSPGSLSLRNPHTLGLSRYHPYGKSHLSTAGGLAVPSLPTAGPYYSPYALYGQRLASASALGYQ
Transcriptional corepressor which does not bind directly to DNA and may regulate transcription through recruitment of histone deacetylases to gene promoters. Regulates cell adhesion, migration and proliferation. May be required for segmental gene expression during hindbrain development.
Q9H7S9
P22014
TBB2_COLGR
Beta-2-tubulin
Colletotrichum graminicola species complex
MREIVHLQTGQCGNQIGAAFWQNISGEHGLDSNGVYNGTSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVLDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAHSFRAVSVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGKVAMKDVEDQMRNVLNKNSSYFVEWIPNNVQTALCSIPPRGLKMSFTFVGNSTAIQELFKRVGEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDAGVDEEEEEYEDDAPLEEEV
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.
P22014
Q87TR9
RNPA_PSESM
Protein C5
Pseudomonas
MSRDFSREKRLLTPRHFKAVFDSPTGKVPGKNLLLLARNNDLDHPRLGLVIGKKSVKLSVERNRLKRLMRESFRQHQDSLVGWDIVIVARKGLGDVENPELIQHFGKLWKRLARSRPTPEEKSEPAGVDSTDA
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Q87TR9
B0S1E4
RBFA_FINM2
Ribosome-binding factor A
Finegoldia
MNIKRVRRISSEIKKVISSSIINSLKDPRIDKLNVSVTEVKVTNDLSFATVYIAVIGDDEKKKQTLEGLNKAKGFLKKQIGENVDLRHVPQLIFKIDETSEQSMHIENLIKSIHEENHNEN
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
B0S1E4
P71007
ALBE_BACSU
Antilisterial bacteriocin subtilosin biosynthesis protein AlbE
Bacillus
MEVNLLKTHQFSTISIAASFLKPIESAAEPEEETIYFYGAAAYLKEQIIDAFGYAAGSRFMYSANLFFDQQLKTCGTRLIHPLYNGNLHVDALMKTFADLSFPSSLSFEAFEKARNELLLKIEKKFTDPFSYSAARLAEEVFGNPMYGTGMFGRRDRIKAIHPKRFLDATDFIVDLVSQQKQLNILGQVQACDVRGHAPQTSAVTSGRIPVNRHVFETETRSAAGPSVLTLGFDCGEMKDASDYIKIQLIDGLLGKYGHSALFKHFREKDLAVYHVITRYDVMNNLLLVSICTDQLHEKDIPPRVLEAVSAFHTDERELEQAKQFLRNELLLQFDSPEGLLAYMGVLRRFSCTKEALLDGISAVTCRDVLQFIATINYIGAHVVRG
Involved in the production of the bacteriocin subtilosin.
P71007
B5XQH2
SUFS_KLEP3
Selenocysteine reductase
Klebsiella
MTFSVERVRADFPVLNREVNGQPLAYLDSAASAQKPEAVIGAEAEFYRHGYAAVHRGIHTLSAEATARMEAVRQQAANFLNAGSAEEVVFVRGTTEGINLVANSWGNANVGAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLDVVPGLFDPRTRLLAITEVSNVLGTENPLAALIALAHQHGAKVLVDGAQAVMHHPVDVQALGCDFYVFSGHKLYGPTGIGVLYGRSELLQAMAPWEGGGSMIATVSLTEGTTWNRAPWRFEAGTPNTGGIIGLGAALTYVSQLGLTQIAEYEQTLMRYALEALRAVPDLILYGPAQRKGVIAFNLGQHHAYDVGSFLDNYGIAVRTGHHCAMPLMARYQVPAMCRASLAMYNTTEEVDRLVAGLQRIHKLLG
Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
B5XQH2
Q1BYX9
HEMH_BURCA
Protoheme ferro-lyase
Burkholderia cepacia complex
MRFDLEPPSSVAAAHRIGVLLINLGTPDAPTPRAVRRYLAEFLSDPRVVEIPQAVWQVLLRTLILPLRGRASAKKYAAVWMPEGSPLRVYTERQTDSVRHLLTSNGYHVMVDYAMRYGSPNISHALTQFKRAGVERVLLMPMYPQYSASTTATAFDAAFDALARMRNQPEVRTVRHYADHPAYIHALAEQVRQYWAQHGRPDFAAGDKLVLSFHGVPKRTLDLGDPYHDQCQQTGALLMAALGLSTTECHVTFQSRFGKAEWLQPYTAPTLREFGEAGVRRADVFCPGFTADCLETIEEIGMEVRDEFLAGGGKTFHRIPCLNGASAWIGALSEIVAENLQGWPVKAAQPEPVN
Catalyzes the ferrous insertion into protoporphyrin IX.
Q1BYX9
Q5HFM3
GCSPA_STAAC
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
Staphylococcus
MSHRYIPLTEKDKQEMLQTIGAKSIGELFGDVPSDILLNRDLNIAEGEAETTLLRRLNRIASKNITKETHTSFLGAGVYDHYAPSVVDAMISRSEFYTAYTPYQPEISQGELQAIFEFQTLICELTDMDVANSSMYDGMTSFAEACILAFSQTKKNKIVVSKGLHYQALQVLHTYAKTRKEFEVVEIDLDGTVTDLKKLEAAVDDETAAVAVQYPNFYGSIEDLKKIHSFIEDKKALFIVYANPLALGLLTPPGSFGADIVVGDTQPFGIPAQFGGPHCGYFATTKKLMRKVPGRLVGQTQDDEGNRGFVLTLQAREQHIRRDKATSNICSNQALNALASSIAMSALGKQGIYDIAVQNIEHANYAKQQFIKKGFEVLDGTSFNEFVVKFDKPIQQVNEELVKYNIIGGFDLGVVSDDFKNHMLIAVTELRTKDEIDTFVEKAGELND
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Q5HFM3
Q2S3R4
RL3_SALRD
50S ribosomal protein L3
Salinibacter
MSSGLIGKKVGMTSVFDDEGNNVACTVVEAGPNVVTQVKSEGRDGYSAVQLGFDNVKEKNVTQAMLGHFEKAGCPPKRMLSEFRDFGDDVDLGDVVRVQDLFQEDERIDVVGVSKGKGFQGVVKRHGFSGVGMMTHGQSDRQRHPGSIGASADPSRVFKGVRMAGQTGGERTKIQNLRVVRILADQNAILIHGSVPGPKSEYVELHKK
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.
Q2S3R4
Q48RM8
ALR_STRPM
Alanine racemase
Streptococcus
MISSFHRPTVARVNLQAIKENVASVQKHIPLGVKTYAVVKADAYGHGAVQVSKALLPQVDGYCVSNLDEALQLRQAGIDKEILILGVLLPNELELAVANAITVTIASLDWIALARLEKKECQGLKVHVKVDSGMGRIGLRSSKAVNLLIDSLKELGADVEGIFTHFATADEADDTKFNQQLQFFKKLIAGLEDKPRLVHASNSATSIWHSDTIFNAVRLGIVSYGLNPSGSDLSLPFPLQEALSLESSLVHVKMISAGDTVGYGATYTAKKSEYVGTVPIGYADGWTRNMQGFSVLVDGQFCEIIGRVSMDQLTIRLPKAYPLGTKVTLIGSNQQKNISTTDIANYRNTINYEVLCLLSDRIPRIY
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Q48RM8
Q493W6
EFP_BLOPB
Elongation factor P
Candidatus Blochmannia
MVLYNINEFRTGLKIIQNREPCVIISHESIKPGKGQAFSRVRFRQIISGKILEKTFKSGDFLESANIMEIRLVYVYHDNEFWYFMDEKNFEEIAVAAKIIGTNIKWITTQLHYIVTLWNKVPILVTPPDSIELKIIKITPIKKNSTGSSGIKLATVSTGAIVKVPFFIQLGELIKINTRSGIYISRAK
Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation.
Q493W6
Q9FJD1
OPT8_ARATH
Oligopeptide transporter 8
Arabidopsis
MKDFTDTISESECDDEISIVPQVELTVPKTDDPTSPTVTFRMWVLGITACVLLSFLNQFFWYRTNPLTISSVSAQIAVVPIGHLMAKVLPTRRFFEGTRWSFTMNPGPFSTKEHVLITVFANSGSGAVYATHILSAVKLYYKRRLDFLPALLVMITTQVLGFGWAGLYRKHLVEPGEMWWPSNLVQVSLFRALHEKENKSKWGISRNQFFVITLITSFSYYLLPGYLFTVLTTVSWLCWISPKSILVNQLGSGSAGLGIGSFGLDWSTIASYLGSPLASPFFASANIAAGFFLVMYVITPLCYYLDLYNAKTFPIYSGKLFVASGKEYKVTSIIDANFRLDRQAYAETGPVHMSTFFAVTYGLGFATLSASIFHVLIFNGKDLWTQTRGAFGKNKKMDIHTKIMKRNYKEVPLWWFLSIFAVNLAVIVFICIYYKTQIQLPWWGAFLACLIAIFFTPLVGVIMATTNQAPGLNIITEYIIGYAYPERPVANICFKTYGYISMSQSLTFLSDLKLGTYMKIPPRTMFMAQVVGTLVAVIAYAGTAWWLMAEIPNLCDTNLLPPGSQWTCPSDRVFFDASVIWGLVGPRRMFGDLGEYSNINWFFVGGAIAPALVYLASRLFPNKKWISDIHIPVLIGATAIMPPASAVNFTSWLVMAFVFGHFVFKYRREWWQRYNYVLSGGMDAGTGFMSVLLFLALQRSEIAIDWWGNSGEGCPVAKCPTAKGVVVHGCPVF
May be involved in the translocation of tetra- and pentapeptides across the cellular membrane in an energy-dependent manner.
Q9FJD1
A5FHA4
PYRG_FLAJ1
UTP--ammonia ligase
Flavobacterium
MNQTKYIFVTGGVTSSLGKGIIAASLAKLLQGRGYRTTIQKFDPYINVDPGTLNPYEHGECYVTDDGAETDLDLGHYERFLNVPTSQANNVTTGRVYLSVIEKERRGEFLGKTVQVVPHITNEIKDRMQLLGKSGDYDIVITEIGGTVGDIESLPYIESVRQLVWELGENNGIVIHLTLVPYLAAAGELKTKPTQHSVKTLMESGIKADILVCRTEHELSQELRQKLALFCNVKKEAVIQSIDASTIYEVPNLMLEEGLDVVALKKLDLPKKASPDLKNWNTFLKRLKSPKQTVNIGLVGKYVEMQDCYKSILEAFIHAGAANETKVNVISIHSEHINADNVEEKLGTLDGVLVAPGFGERGIEGKIEAVRYVRENNIPFFGICLGMQMSVIEYSRNILGYADANSTEMNEKTPHPVVNLMEEQKNITDKGGTMRLGAWKCDIKPNTLAHRIYGEKTISERHRHRYEYNNKYADELQKAGLKASGVNPDTGLVEIVELENHPFFIGVQYHPEYKSTVANPHPIFVNFVAAAVNAHKK
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
A5FHA4
A8SEF7
NU4LC_CERDE
NADH-plastoquinone oxidoreductase subunit 4L
Ceratophyllum
MMLEHELVLSAYLFSIGIYGLITSRNMVRALMCLELILNAVNMNLVTFSDLFDSRQLKGDIFSIFVIAIAAAEAAIGPAIVSSIYRNRRSTRINQSNLLNK
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.
A8SEF7
D4A7C0
GPN2_RAT
ATP-binding domain 1 family member B
Rattus
MAGAAPTTAFGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLEANLDWLRAKLEPLRGHYFLFDCPGQVELCTHHTSLRSIFSQMAQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHVELPHVNLLSKMDLIEHYGKLAFNLDYYTEVLDLSYLLDHLASDPFFSHYRQLNEKLVQLIEDYSLVSFIPLNIQDKDSIQRVLQAVDKANGYCFGVQEQRSLEALMSAAVGADFHFSSTLGIQEKYLASSDQTAEQEAMQL
Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
D4A7C0
P53469
ACT2_OXYTR
Actin, micronuclear
Sterkiella
MSDQQTCVIDNGSGVVKAGFAGEDAPRAVFPSIVGRPKNVSALIGVDSASEYLGDEAQQKRGVLKIFYPIEHGIVKDWDDMEKIWNHTFYVELRVQPDEHPILLTEAPLNPKTNREKMTQIMFETFNVPALYVVIQAVLSLYSAGSTTGIVCDAGDGVTHTVPIYEGFSIPHAVSRIQLAGRDLTTFMAKLLTERGYNFTSSAELEIVRDIKEKLCFVALEYESALKQSHDSSQFEKNYELPDGKVITIGSERFRCPEYLFKPLEMNGRELDSIQDLTYKSIQECDVDVRRDLYQNIIISGGTTMNEGIGERLLKEIENRAPKSINVKVIASADRIFAVWRGGSTRTSLSTFASMWITKEDYDENGASIVHRKCI
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
P53469
Q9P567
SUCB_NEUCR
Succinyl-CoA synthetase beta chain
Neurospora
MFKLGRNRALASAFAATSRAPLASRLPSVSQQQRRALSIHEYLSADLLRQYGIGVPKGDVARTGAEAEAIAKQIGGEDMVIKAQVLAGGRGKGTFDNGLKGGVRVIYSPTEAKMFAEQMIGHKLITKQTGAQGRLCSAVYICERKFARREFYLAVLMDRASQGPVIVSSSQGGMDIEGVAKENPEAIHTTYIDINVGVTDEMARDIATKLGFSEQCVEEAKDTIQKLYKIFCEKDATQIEINPLSETSDHKVMAMDAKFGFDDNADFRQPDIFKLRDTTQEDPDEVRAAQAGLNFIKLDGDIGCLVNGAGLAMATMDIIKLNGGQPANFLDVGGGATPAAIREAFELITSDPKVTAIFVNIFGGIVRCDAIAHGLINTVKSLDLKIPIIARLQGTNMEAARQLINDSGMKIFSIDDLQSAAEKSVQLSKVVKMARDIDVGVEFTLGI
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Q9P567
Q220R4
RUVA_ALBFT
Holliday junction ATP-dependent DNA helicase RuvA
Rhodoferax
MIGKLSGTLDDKNPPQVIVDCHGVGYEVLVPMSTFYNLPELGARVSLLTHFVVREDAQILYGFATSQERAAFRELIKISGVGPRTALSVLSGMSVAELAQAVTLQEGGRLIKVPGIGKKTAERLLLELKGKLGPDIGVAASVANDSQADILQALLALGYSDKEAAAALKALPSDVGVSEGIRLALRALGK
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
Q220R4
Q5NGP7
KDSD_FRATT
Arabinose 5-phosphate isomerase KdsD
Francisella
MEISMTSHINNAVETFRLEIETLEKLKNSIDENFEKACEIILENNRDKSRVIITGMGKSGHIGKKMAATFASTGTPAFFVHPGEAGHGDFGMITKNDVLIAISNSGTSSEIMGLLPMIKHLDIPIIAITSNPKSILARNSNVTLNLHVDKEACPLNLAPTSSTTATLVLGDALAIALLKAKNFSEKDFAFSHPNGALGRKLILKVENIMRKGNEIPIVKPTDNIRKAILEISDKGVGNTLVAENNTLLGIFTDGDLRRMFEAESFNSQRAISEVMTKNPKSISKEEMAITALEKMEKYEITSLAVVDNGHNILGIVTMHDLIKLELR
Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P).
Q5NGP7
B7VPD0
BTUD_VIBA3
Vitamin B12-transporting ATPase
Vibrio
MIQIKSLSVGARLLPLSFELKQGQVTHVIGPNGSGKSTLLEAISGVGDGYKGDIKLDGQDLSELSLQDLSLHRAYLCQSARPAFNLEVFQYLALSLPSSSHGLDIEINAALDEISQMLDISDKLHRSIQTLSGGEWQRVRLAGMCLQIWPTLNPYAKLLILDEPAAPLDIAQEALLYKLIERVAEKGIAVIMANHDLNRTLRHADQVLLLEKGVLQTSGSAEQVLVPEQLESVFNTQVKSISVDNQTYLLFG
Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system.
B7VPD0
P36383
CXG1_HUMAN
Gap junction alpha-7 protein
Homo
MSWSFLTRLLEEIHNHSTFVGKIWLTVLIVFRIVLTAVGGESIYYDEQSKFVCNTEQPGCENVCYDAFAPLSHVRFWVFQIILVATPSVMYLGYAIHKIAKMEHGEADKKAARSKPYAMRWKQHRALEETEEDNEEDPMMYPEMELESDKENKEQSQPKPKHDGRRRIREDGLMKIYVLQLLARTVFEVGFLIGQYFLYGFQVHPFYVCSRLPCPHKIDCFISRPTEKTIFLLIMYGVTGLCLLLNIWEMLHLGFGTIRDSLNSKRRELEDPGAYNYPFTWNTPSAPPGYNIAVKPDQIQYTELSNAKIAYKQNKANTAQEQQYGSHEENLPADLEALQREIRMAQERLDLAVQAYSHQNNPHGPREKKAKVGSKAGSNKSTASSKSGDGKTSVWI
One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
P36383
B6YVS9
TOP6B_THEON
Type II DNA topoisomerase VI subunit B
Thermococcus
MAEASQLFKEFKIQSVSEFFRRNAAMLGYTGKIRSLTTVVHEAVTNSLDACEEAGILPYVRVEIEELGREHYKVIVEDNGPGIPEKFITHVFGKMLAGTKAHRNIQSRGQQGIGISGAVMFAQITSGKATRVITSTGGDIIEAWVKIDVDKNEGKIVKKERHPNPKGWRGTRIELEVKNVRYVRSKQGVYWYLKLTAIANPHAHIELIEPDGKLIVFPRSSEEVPKPPVEMKPHPKGVLTDDVYRMAKKTRRNTVRRFLIGEFSRISDKKVDELIKYIAALRLIKTEKDKAVQDQLYERLMNGEVDKVLRSFKGYTKVVKQVAKLMEKPPEKLSWHEAEEIVEAFKYMKFLAPPTHGLRPIGEENIEKGLKGILKPEFVTAVTRPPKVYSGGIPFQVEVGLAYGGEISSGFDLLRYANRVPLLFDAGSCVTTLAARSIDWKRYKVDDLERAPVVLMINVISVHVPYTGTGKQSIANVDEIHNEIRLAIMDAARRLQTYLSGKHRRLYQVKRKKTFEKYVPEIAKALSILTGEPEEEVKNYFLRFIEERFAQSEVEAEEVAENA
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
B6YVS9
Q6F9D2
UVRB_ACIAD
Excinuclease ABC subunit B
Acinetobacter
MRVNDNQPFDLVTNYQPAGDQPQAIKKLVSGIEQGNRNQLLLGVTGSGKTYTMANVIAQTQRPTIVMAHNKTLAAQLYGEFKAFFPNNAVEYFVSYYDYYQPEAYVPSSDTFIEKDAAINDHIDQMRLSATRALLERRDAIIVASVSAIYGLGDPEAYMKMLLHVVEGDRINRDDLIRRLVEMQYTRNELEFLRGTYRIRGEILDVFPAESDQFAIRIELFDDEVDSIRWFDPLTGKMQRKVPRVTIYPKSHYVTPKDNLSRAIETIKDELQDQLKFFREHDKLLEAQRIEQRTRYDLEMMQQLGYTNGIENYSRHLSGRSPGAAPPTLFDYIPEDALLIIDESHVTVPQIGAMYKGDRSRKENLVNYGFRLPSALDNRPMKFEEWERIVPTTVFVSATPAKYELEKSDQIVEQVVRPTGLIDPEIEIRPVLTQVDDVLSEINIRKEMDERVLITTLTKRMAEDLTSYLKEYGVKVAYLHSDIDTVERVKIIHELRTGVYDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNIKGKAILYADRMTDSMQKAIDETERRREKQIEFNKIHGITPRSAVRQKVKEIDTGEVFNDDDIEGKISEQARALSADERHILADPKLFAKHMSKLEKEMLKASKELQFEQAARLRDEILRLKAQMLH
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.
Q6F9D2
Q2RM40
MCSB_MOOTA
Protein-arginine kinase
Moorella
MSLNLERNSKWMEGSGPQADIVISSRIRLARNLKGLPFPNLMNSDQQARVVSQVSRAIQAPMVFQAVGELKLQPLRELAPVERQILVEKHLISPDLAAGGGEKAVVLRDDEAVSIMVNEEDHLRLQCLLPAMMLHEAWRLADAADDALENELDFAFDQERGYLTACPTNVGTGLRASTMLHLPALVLTRQAGPVLSALTKVGVAVRGLYGEGTEAQGNIFQVSNQITLGRSEEEIINNLSAVTVRLADQEREARELLRRQSRWQLEDRVGRAYGVLTNARILSSQEALQLLSDVRLGAEMKIIRGLDQRLLNQLMVRIQPAFLQFSAGKEMTPMERDVHRAAMVRELLAG
Catalyzes the specific phosphorylation of arginine residues in proteins.
Q2RM40
B0C6F8
TRPA_ACAM1
Tryptophan synthase alpha chain
Acaryochloris
MTSVSDCFAQLRDRGQCALIPFLTAGDPDLATTASALRQLDASGADLIELGVPYSDPLADGPVIQAAATRALQRGTRLDQVLEMVTELSPEIRAPIILFTYYNPIYHRGVAEFLQQIAKAGVRGLVVPDLPLEESENLLQQAADLGIEVTLLVAPTSSKERIEKIALRSQGFIYLVSTTGVTGMRTKVENRVQDLIADLRQVTDKPIGVGFGISRTEHARQVMDWGADAAIVGSAFVNRLSEGSPSQGLSAISTFCRSLKSSLLLDA
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
B0C6F8
P47583
RPOB_MYCGE
Transcriptase subunit beta
Mycoplasma
MSQKSNFFQKRYSPTATRRYYGKIETNFIQPNLADIQIKSYQKFLDHDLEKLIASYFPIKSPNDRYTINFRGLHRTEPERDEAQSRAQSKTYEVGIYADLELVDNDKGTVKKARKSKKNIASNTNGVFLASMPLITHDGVFIINGIEKFVISQITRSPGIYMLTKSQLKLSNSRKRVQEGYVCEVLPANGSVMLIYISNKKKIEDAFVQILLRDAVREGAKIFPITTLLKAFGLNNREILKIFKNNEFIKRSLEAEIYNAKDFLSNVDPEIKNLLKEFRDGKTDLRRKGIASDQKLRSLVNEYVTLEKQYNALKQTSPNDSSLTALELEMENKMDSVITERAAKHIVNELSISLRDIENTEECHEVSFHALLCARFFRNKRYNLSNAGRYKVSRKLRLTERIYQKTLACDLFLKDGKLLLKKGTLLLKEEIDKIKQAAKNNEISFVNKMQLTTDGKAVDLAKESLFYETIDVYITNDNLSVSVPVIGIHNENDLNKAMTLSDFIASISYVINLPYGIGKYDDIDHLGNKRVKLINELITAKLESGFTRMERFLKEKLTIADGVNRGQQINEEGQVIEQGEKKELTIKSLINSKPIQIVIKDFFNTHQLTQFLDHQNPLSELSNKRRISAMGPGGISREDPNLDIRDVHYSQYGRICPIETPEGMNIGLIMSLASFAKIDENGFLMAPYRKIKAGVITDEVEYLTALREDEHIIAEISSLVNISNDNKILDKEIIGRYRSMQGLYDPLKIDYIDVAPHQVVSIGSSLIPFLENDDSARALMGTNMQRQAYPLIKPYAPAVGTGQEHKIASDSGLTMSSPCSGVVSYVDNSKIIITSDSSKKETVNLVKFERSNQNTCYNHKPIVEIGQRVNKDEIIVDGPAVNKSELALGQNVLVAFTTWNGYNYEDAIVISERLVKEDILTSLTINEYVAQCLSTKNGDEQITRDIPNVSDANKRYLDENGIIMVGAEVKEGDVLVGKVSPKGQVEVSPEEKLFKAIFPESVQNVRDSSLKVSHGGDGIVSAVKRFSIANGDELNDGVIEMIKVYVVQKRKIQIGDKLAGRHGNKGVISKVVPIEDMPHLEDGTPVDILLNPLGVPSRMNIGQIFETHLGYAAHKLAVRSLISSCFDQNKAKEFAIEINQPQARVERLIKGLKNQINDRNIKSEKEALEKLDNSDISLVLKEIGMSFDDLIYKIATPIFQGVNFLDLQDVMQEAGLDPQKNQGKFKLIDGRSGMPFERPISLGIMYMMKLNHMVDDKIHARAVGPYSKITQQPLGGKSQNGGQRFGEMEVWALEAYGAAYNLQELLTIKSDDVQGRNRAYAAIVKGAAFPEPGIPESFKLLTKELQGLALSVSFIYDDNTQQDSNNVSILQSDGEQDEFFNDFEFDTEGY
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
P47583
Q5M750
VQ4_ARATH
MPK3/6-targeted VQ-motif-containing protein 1
Arabidopsis
MENSPRYREATNLIPSPRCHNSNNSCGMSSSSESNKPPTTPTRHVTTRSESGNPYPTTFVQADTSSFKQVVQMLTGSAERPKHGSSLKPNPTHHQPDPRSTPSSFSIPPIKAVPNKKQSSSSASGFRLYERRNSMKNLKINPLNPVFNPVNSAFSPRKPEILSPSILDFPSLVLSPVTPLIPDPFDRSGSSNQSPNELAAEEKAMKERGFYLHPSPATTPMDPEPRLLPLFPVTSPRVSGSSSASTS
Acts as negative regulator of WRKY33 transcription factor activity in the promotion of defense gene expression. Acts as a negative regulator of pathogen-associated molecular pattern (PAMP)-induced responses to modulate resistance to pathogens.
Q5M750
Q6NQH4
TAF13_ARATH
TBP-associated factor 13
Arabidopsis
MSNTPAAAASSSSKSKAAGTSQPQEKRKTLFQKELQHMMYGFGDEQNPLPESVALVEDIVVEYVTDLTHKAQEIGSKRGRLLVDDFLYLIRKDLPKLNRCRELLAMQEELKQARKAFDVDEKELVD
TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. May be involved in polycomb repressive complex 2 (PRC2) mediated repression.
Q6NQH4
Q87SX9
CYSN_VIBPA
Sulfate adenylate transferase
Vibrio
MNSAVEAQLAELGIEGYLKQHQYKSLLRFLTCGSVDDGKSTLIGRLLHDSKQIYEDQLAAVHSDSQRVGTTGEKPDLALLVDGLQAEREQGITIDVAYRYFSTQKRKFIIADTPGHEQYTRNMATGASTCDLAVILVDARKGILDQTRRHSFISNLLGLKHFVVAINKMDLVDYSQARFEEIRDEYLKFSENLTGDIDIQIIPISALEGDNVVDKGQNLNWFEGPSLLELLETVDVDYEKGAGEFRFPVQYVNRPNLDFRGFAGTVSSGSVKVGDAIKALPSGKTSTVARIVTFDGDIEEAQAGLAVTLTLNDEIDISRGDLIVLENAQVQTTNHLLADVVWMTEQPLQPGRDYDIKIAGKKTVGHVESIRHQYDINNLSTHGAAELPLNGIGLCEWSLNESVALDNYQDCADTGGFIIIDRLTNVTVGAGMVKESLTELERGLADVSAFELELNALVRKHFPHWEAKDLSQLLKK
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Q87SX9
Q68W92
RS8_RICTY
30S ribosomal protein S8
typhus group
MSMTDNVADMLTRIRNAYKSKLINVSFPSSKIKNSILDVLQKEGYIKDYVITQKNNISYTKVALKYSINGEASICEIRRVSKPGKRVYSAIKDLKGYYNNMGIYILSTPYGVMSDREAHIKNVGGEVICKVF
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Q68W92
Q96EM0
T3HPD_HUMAN
Trans-L-3-hydroxyproline dehydratase
Homo
MESALAVPRLPPHDPGTPVLSVVDMHTGGEPLRIVLAGCPEVSGPTLLAKRRYMRQHLDHVRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGLVPAPPAGTREARVNIHCPCGLVTAFVACEDGRSHGPVRFHSVPAFVLATDLMVDVPGHGKVMVDIAYGGAFYAFVTAEKLGLDICSAKTRDLVDAASAVTEAVKAQFKINHPDSEDLAFLYGTILTDGKDAYTKEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQMRAFKSSATGSVFTGKAVREAKCGDFKAVIVEVSGQAHYTGTASFIIEDDDPLRDGFLLK
Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it.
Q96EM0
Q67S38
FLOA_SYMTH
Flotillin-like protein FloA
Symbiobacterium
MSMPGLGYLILTFVVLLLLVLFFSFVPVGLWISAAAADVRVGIFYMIGMKLRRVPPHRIVNALIKAEKAGLEISIDKLEAHYLAGGNVDRVIDALIAAQRAGIDLVFERAAAIDLAGRNVLEAVQMSVNPKVIETPVVAGVAQDGIELRAKARVTVRADINRLVGGAGEDTIIARVGEGVVSTIGSAASHKEVLENPDMISRTVLAKGLDAGTAFEIVSIDIADVDVGANIGARLRADQAEAEKVMAQAKAEERRAMAVAEEQEMRAETQRMRAKVVEAEAEVPRALAQALREGRIGVMEYLMMQNLQADTAMREALGGGQRGGQPGGQDQK
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Q67S38
Q4UP35
ACSA_XANC8
Acyl-activating enzyme
Xanthomonas
MADVYPVDPAFAADARITREQYATLYRESIEHPEQFWGKAAQRLDWFKQPTQIKDVSFALDDFHVRWFGDGELNASVNCLDRQLATRGDKTALLFEPDSPDSPSYPVTYRELYERVCKLGNALRNLGVKKGDRVTIYLPMIVDAAVAMLACARIGAVHSVVFGGFAANSIADRVIDCQSKLIITADEGLRGGKKIPLKANVDAALKIPGTNTVETVLVVRHTGGAVDMQAPRDRWFHDVVDGQPAECEPERMNAEDPLFILYTSGSTGKPKGVLHTTAGYLLFASYTHEVVFDLREDDIYWCTADVGWVTGHSYIVYGPLANGATAVMFEGVPNYPNVSRFWEVIDKHQVTIFYTAPTAIRALMREGEAPVKKTSRSSLRLLGSVGEPINPEAWRWYYEVVGDSRCPIVDTWWQTETGGILISPLAGAVDLKPGSATLPFFGVQPALVDAEGKILEGATEGNLVLLDSWPGQMRTVYGDHQRFIDTYFRTYPGSYFTGDGCRRDADGYYWITGRVDDVINVSGHRIGTAEVESALVSHPKVAEAAVVGFPHDVKGQGIYAYVTLIAGETPSEELHKELVSWVRKEIGPIASPDHLQWAPGLPKTRSGKIMRRILRKIAENAPDQLGDTSTLADPSVVDSLVNERLTR
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
Q4UP35
B0VSP5
CH60_ACIBS
Chaperonin-60
Acinetobacter calcoaceticus/baumannii complex
MSAKDVKFGDSARSKMIAGVNVLADAVKVTLGPKGRNVVIDRSFGAPHITKDGVTVAKEISLKDKFENMGAQLVREVSSKTNDIAGDGTTTATVLAQAILNEGIKSVTAGMNPMDLKRGIDIAVKTVVENIRSIAKPADDFKAIEQVGSISANSDTTVGKLIAQAMEKVGKEGVITVEEGSGFEDALDVVEGMQFDRGYISPYFANKQDTLTAELENPFILLVDKKISNIRELISVLEAVAKTGKPLLIIAEDVEGEALATLVVNNMRGIIKVCAVKAPGFGDRRKAMLQDIAILTGATVISEEVGMSLEQATLQDLGTAHKITVSKENTVIVDGAGDAAAIAERVQQIRAQIEESTSEYDREKLQERVAKLAGGVAVIKIGAATEVEMKEKKDRVDDALHATRAAVEEGVVAGGGVALVRAVNALEGLKGANEDQTAGINILRRAIEAPLRQIVANAGDEPSVVINAVKNGEGNFGYNAATGEYGDMLEMGILDPAKVTRSALEHAASVAGLMLTTECMITDIPEDKPAAPDMGGMGGMM
Together with its co-chaperonin GroES, 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.
B0VSP5
Q3BSK1
SST_XANC5
Serine O-succinyltransferase
Xanthomonas
MTEFIPAGTLYHALPSPFPMKRGGVLHQARVAYETWGTLAADRSNAILIVTGLSPNAHAAANQANPEPGWWEAMLGPGKPIDTARWFVVCVNSLGSCKGSTGPASVNPATGAPYRLSFPDLSIEDVADAAADVVRALGIAQLACLIGNSMGGMTALALLLRHPGIARSHINISGSAQALPFSIAIRSLQREAIRLDPHWNGGHYDDARYPESGMRMARKLGVITYRSALEWDGRFGRVRLDSEQAADDPFGLEFQVESYLEGHARRFVRFFDPNCYLYLSRSMDWFDLAEHVDEQPATDSAIDHAHADALPASAKPQTGVSTADTVLAGLARIRIARALAIGANTDILFPVQQQEQIADGLRAGGADAHFIGLDSPQGHDAFLVDFARFGPAVRDFLQDC
Transfers a succinyl group from succinyl-CoA to L-serine, forming succinyl-L-serine.
Q3BSK1
A8GE00
RNFC_SERP5
Rnf electron transport complex subunit C
Serratia
MLNLFAAFKKDRIWDFDGGIHPPEMKTQSSGVPLRTAPLPDKFIIPLQQHLGPEGELCVKVGDTVLKGQPLTVGRGRTVPVHAPTSGTISAITPHITAHPSGLAELCVIIQPDGEDRWCERAPVADYRQLTASELIQRIHQAGIAGLGGAGFPTASKLQGGMNGVETLILNAAECEPYITADDRLMQEHADQVIEGTQILRHLLQPKVTLIGIEDNKPEAIAALKLALRGQPGIALRVIPTKYPSGGAKQLTKILIGKEVPHGKHSSAIGVLMQNVGTAFAIKRAIVDGEPLIERVVTLTGEALSLPGNLWARIGTPVQHLLKFAGFQPQAQQMVVMGGPLMGFTLPALHVPIVKISNCILAPSVSEMAPQEQEQSCIRCGLCVDACPAGLLPQQLYWFSRGEEHEKARNHNLFDCIECGACAFVCPSNIPLVQYYRQEKAEIKAIDLEAARTAEAKARYEAKLARLEREKLAREERHKKAAVKLTDGDQDAVQAALARVRSKNAVPATGTISGDAPDNSEMNAAREARKAQARERRAQQETPVAPVTASASEDEDPRKAAVAAALARVKAKKAAPQATAVETPAESPAVVTEEDPRKAAVAAALARVKAKKAAQQATAVETPAESPAVVTEEDPRKAAVAAALARVKAKKAAQQATAVETPAESPAVVTEEDPRKAAVAAAIARAKAKRAAQSLTTADTDKE
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
A8GE00
Q4QLI0
HLDD_HAEI8
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
Haemophilus
MIIVTGGAGFIGSNIVKALNDLGRKDILVVDNLKDGTKFANLVDLDIADYCDKEDFIASIIAGDEFGDIDAVFHEGACSATTEWDGKYIMHNNYEYSKELLHYCLDREIPFFYASSAATYGDTKVFREEREFEGPLNVYGYSKFLFDQYVRNILPEAKSPVCGFRYFNVYGPRENHKGSMASVAFHLNNQILKGENPKLFAGSEGFRRDFVYVGDVAAVNIWCWQNGISGIYNLGTGNAESFRAVADAVVKFHGKGEIETIPFPEHLKSRYQEYTQADLTKLRSTGYDKPFKTVAEGVTEYMAWLNRK
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Q4QLI0
P17764
THIL_RAT
Acetoacetyl-CoA thiolase
Rattus
MAALAVLHGVVRRPLLRGLLQEVRCLGRSYASKPTLNDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQGEFGLASICNGGGGASAVLIEKL
This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms. The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA. Thereby, it plays a major role in ketone body metabolism.
P17764
A7I137
ATPL_CAMHC
Lipid-binding protein
Campylobacter
MISIYAQIASFSAIGVGIAIGVAACGGGIGMGIAANATILGMARNPSISSKLTTTMYISLAMIEAQVIYALVIVFILLYANPLLTETIAAAAK
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
A7I137
B4LYI3
EI3D1_DROVI
Eukaryotic translation initiation factor 3 subunit p66
Drosophila
MSETINTAAQFPTFEKPTVQFNEKGWGPCELPDTFKDVPYQPFSKNDRLGKICDWTSTSNNDKKYQNKYASTFGTGNQYAYYHEEDETTFHLVDTARVQKPPHQRGRFRNMRNSRSGRGRNARGGLNTHGHGMTTLSSKNVKARDPRRGMGKRFGNRGPPPKMRESSVAVRADWASIEEMDFPRLIKLSLPNIKDGEDITTCGTLEYYDKTYDRINVKNEKPLQKIDRIVHTVTTTDDPVIRRLSKTIGNVFATDAILATIMCSTRSNYSWDIVIEKVGEKIFMDKRDHTEFDLLTVNETSVEPPTDDDSSCNSPRNLAIEATFINHNFSQQVLKTGDQEAKYKFEETNPFISEDEDIQVASVGYRYKKWELGSDIVLVARCEHDGVLQTPSGEPQFLSIKALNEWDSKLANGVEWRQKLDTQRGAVLANELRNNACKLAKWTVQAVLAGSDQLKLGYVSRINPRDHSRHVILGTQQFKPHEFATQINLSMDNAWGILRCIIDLVMKQKDGKYLIMKDPNKPIIRLYDIPDNTFDSDDSDDGEGDDGEGFQQVYNYANNSNKI
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
B4LYI3
C3P8L8
PRMA_BACAA
Ribosomal protein L11 methyltransferase
Bacillus cereus group
MKWSEISIHTTEEAVEAVSHILHEAGASGVAIEDPAELTKEREQQYGEIYALNPDEYPAEGVLIKAYFPQTDSLHETIAGVKSSIDVLPSYDIEIGTGNITVNEVNEEDWATAWKKYYHPVQISDTFTIVPTWEEYTPSSPEEKIIELDPGMAFGTGTHPTTTMCIRALEKTVQPGDTIIDVGTGSGVLSIAAAKLGASSVQAYDLDPVAVESAEMNVRLNKTDDVVSVGQNSLLEGIEGPVDLIVANLLAEIILLFPEDAARVVKSGGLFITSGIIAAKEKVISEALEKAGFTIEEVLRMEDWVAIIARNA
Methylates ribosomal protein L11.
C3P8L8
Q75R63
NQRB_VIBAN
NQR-1 subunit B
Vibrio
MGLKKFLEDIEHHFEPGGKHEKWFALYEAAATLFYTPGLVTKRSSHVRDSVDLKRIMIMVWLAVFPAMFWGMYNVGHQSITALNHLYSGAELATVISGNWHYWLTEMLGGTLSTQAGWASMMLLGATYFLPIYATVFLVGGFWEVLFCMVRKHEVNEGFFVTSILFALIVPPTLPLWQAALGITFGVVVAKEIFGGTGRNFLNPALAGRAFLFFAYPAQISGDVVWTAADGFSGATALSQWAQGGNGALINKVTGEAITWMDAFVGNIPGSIGEVSTLALAIGAAFIVYMGIASWRIIAGVMVGMIAISTLFNVIGSDTNAMFNMPWHWHLVLGGFAFGMFFMATDPVSASFTNKGKWAYGILIGAMCVMIRVVNPAYPEGMMLAILFANLFAPLFDHIVIEKNIKRRLARYGK
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Q75R63
P83234
VESP_OPHHA
Ohanin
Ophiophagus
MLLFTLCFFADQENGGKALASPPGNWQKADVTFDSNTAFESLVVSPDKKTVENVGVPKGVPDSPERFSSSPCVLGSPGFRSGKHFFEVKYGTQREWAVGLAGKSVKRKGYLRLVPEERIWQKGLWWLRRLETDSDKLQKGSGKIIVFLDYDEGKVIFDLDGEVTTIQANFNGEEVVPFYYIGARVSLANL
Neurotoxin that produces dose-dependent hypolocomotion and hyperalgesia in mice. May directly act on the central nervous system, as it is 6500-fold more potent when administered intracerebroventricularly than intraperitoneal.
P83234
Q94P36
NU3M_RHIPI
NADH dehydrogenase subunit 3
Rhinolophus
MNFMLTLLTNTLLALLLVTIAFWLPQTNVYSEKSSPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWASQANNLEVMLTTALLLISLLAISLAYEWSQKGLEWTE
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Q94P36
Q7RZA5
MTAP_NEUCR
5'-methylthioadenosine phosphorylase
Neurospora
MENLPTTYDGPVHIAVIGGTGLSKLEGYVPVAALNPTTPWGSPSSPLMIFEHNGHAVAFLARHGLYHQLAPHEVPARANIAALRSIGVRTIIAFSAVGSLREEIKPMDFVIPDQIIDRTKGIRPFTFYEGGVVGHVGFADPFDAGLAQVVEKCASAMKGDGVVLHNKGTIICMEGPAFSTRAESHMYRSWGGSVINMSALPEAKLAREAELAYQMICMATDYDCWRDEAGEDVDVAMVMKYMAANGENAKHLVGAVLDELLKQDNSDLVLAKKWQGSAQGAVKFMTKPEGRDPEAMKRVEFLFPGFWEQN
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.
Q7RZA5
B5EEE7
YACG_CITBB
DNA gyrase inhibitor YacG
Citrifermentans
MNAITTIKCPQCRKETTLAGNPYRPFCSQRCKMIDLGTWADEGYRIPGEKAPESGDEEPGDE
Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.
B5EEE7
P65228
KHSE_STAAM
Homoserine kinase
Staphylococcus
MSNVLELTIPASTANLGVGFDSIGMALDKFLHLSVKETSGTKWEYIFHDDASKQLPTDETNFIYHVAQQVASKYSVDLPILCIEMRSDIPLARGLGSSASALVGAIYIANYFGDIQLSKHEVLQLATEIEGHPDNVAPTIYGGLIAGFYNDVSKETSVAHIDIPDVDVIVTIPTYELKTEASRRALPQKLTHSEAVKSSAISNTMICALAQHNYELAGKLMQQDGFHEPYRQHLIAEFDEVKTIASQHNAYATVISGAGPTILIFSRKENSGELVRSLNSQVVSCHSELVDINISGVKERIVYQ
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
P65228
A3PEH8
RL21_PROM0
50S ribosomal protein L21
Prochlorococcus
MTNSKKSSNNSSKSSELYAIAETSGQQFWFEVDRYYDIDRLNAKEKDKITLEKVLLLKDKDSISVGKPYVKDAKIELEVVSHKRDKKILVYKMRPKKKTRRKMGHRQELTRVMVKSITIGKSAPKSSSKKETVKKETKPKSEKSTN
This protein binds to 23S rRNA in the presence of protein L20.
A3PEH8
Q90ZK5
DRS8_PHYBI
Dermaseptin-gene related 2
Phyllomedusa
MAFLKKSLFLVLFLGLVSLSICEEEKRENEDEEEQEDDEQSEMKRGLWSKIKEAGKAALTAAGKAALGAVSDAVGEQ
Has antimicrobial activity.
Q90ZK5