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Full Name
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taxon
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
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10
P04173
LEU3_YEAST
Beta-IPM dehydrogenase
Saccharomyces
MSAPKKIVVLPGDHVGQEITAEAIKVLKAISDVRSNVKFDFENHLIGGAAIDATGVPLPDEALEASKKADAVLLGAVGGPKWGTGSVRPEQGLLKIRKELQLYANLRPCNFASDSLLDLSPIKPQFAKGTDFVVVRELVGGIYFGKRKEDDGDGVAWDSEQYTVPEVQRITRMAAFMALQHEPPLPIWSLDKANVLASSRLWRKTVEETIKNEFPTLKVQHQLIDSAAMILVKNPTHLNGIIITSNMFGDIISDEASVIPGSLGLLPSASLASLPDKNTAFGLYEPCHGSAPDLPKNKVNPIATILSAAMMLKLSLNLPEEGKAIEDAVKKVLDAGIRTGDLGGSNSTTEVGDAVAEEVKKILA
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.
P04173
Q164Y5
UGPC_ROSDO
sn-glycerol-3-phosphate import ATP-binding protein UgpC
Roseobacter
MAQVELKQVRKTYPNGAEAIFGVDMKIDDGELIVFVGPSGCGKSTLLRMVAGLESISSGEILIGDRVINDVSPSERDVAMVFQNYALYPHMSVRGNMSYGLKNRKMDKEEIERRITDAATMLKIDQFLDRQPNQLSGGQRQRVAMGRAIVRHPQVFLFDEPLSNLDAKLRVQMRIEIKKLQRRMNVTSIYVTHDQTEAMTLADRLAVINEGQIEQMGAPMELYSNPATLFVASFIGAPQINLIPVAFDGSAIVNGDLRIGGFSDLPMGVDLKLGVRPDVMTIDPEGQVMMNVDIVEQHGGENLIYGTIDGVFSGEGEPQEVCLKGSQTLLPNPDDKLRLRFDPDAAFIFRTDTGERLK
Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system.
Q164Y5
B2I4U0
GPMA_XYLF2
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Xylella
MTRKLVLLRHGQSQWNSMNRFTGWVDIGLTEQGHQEATMAGHLMKKEGLEFDVAHTSLLKRAIHTLQDALKALDQDWLPIYKSWRLNERHYGALQGLDKIDTAAKHGEEQVNIWRRSYDIQPPPIDLDDPSHPMRDRRYAALDRKVLPVRESLKNTLERVLPYWNDAIAPQLNDNKTVLISAHGNSLRALYKYLNKESDEKILNVNIPTGIPLLFELSDTLQVVSYRYLGDPDAAQRAAEMVANQGKAK
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
B2I4U0
Q9SLH7
PER20_ARATH
ATP28a
Arabidopsis
MEIKQKKVWLSLIVLYAITTSVLGDFGEPLLKGFYKESCPLAEEIVKHNIEVAVLKDPRMAASLLRLQFHDCFVLGCDASVLLDTHGDMLSEKQATPNLNSLRGFEVIDYIKYLLEEACPLTVSCSDILALAARDSVFLRGGPWWEVLLGRRDSLKASFAGANQFIPAPNSSLDSLIINFKQQGLNIQDLIALSGAHTIGKARCVSFKQRIVQPNMEQTFYVDEFRRHSTFRRVLGSQCKDSSRDNELSPLDIKTPAYFDNHYFINLLEGRGLLISDNVLVSEDHEGEIFQKVWEYAVNQDLFFIDFVESMLKMGNINVLTGIEGEIRENCRFVNI
May be implicated in the systemic acquired resistance response via the salicylic acid signal transduction pathway.
Q9SLH7
Q2QR07
SWT13_ORYSJ
Bidirectional sugar transporter SWEET13
Oryza sativa
MAGLSLQHPWAFAFGLLGNLISFTTYLAPIPTFYRIYKSKSTEGFQSVPYVVALFSAMLWIFYALIKSNEALLITINAAGCVIETIYIVMYLAYAPKKAKVFTTKILLLLNVGVFGVILLLTLLLSHGEQRVVSLGWVCVAFSVSVFVAPLSIIKRVIQSRSVEYMPFSLSLTLTLSAVVWFLYGLLIKDKYVALPNILGFTFGVVQMGLYVFYMNATPVAGEGKEGKGKLAAAEELPVVVNVGKLAAATPDRSTGAVHVHPVPRSCAAEAAAAEPEVLVDIPPPPPPRAVEVAAV
Confers blight susceptibility . Confers TAL effector-mediated susceptibility to Xanthomonas oryzae pv. oryzae .
Q2QR07
A8ZVP4
THIC_DESOH
Thiamine biosynthesis protein ThiC
Desulfosudis
MTQVARAKQGVVTEQMAAVAKSEGLSPEAVRDGVAAGRIVIPGNVNRRFAPVGIGSGLRTKVNANIGTSPEHHDVAEEERKLQTAVAAGAHSVMDLSTGGDLFAVRKMVLEKSPVMVGAVPIYEVAARLSAESRAFYEMTPDMLFDAIERQCAEGLDYITVHCGVTRQAAALAGADRRVTGIVSRGGSLLAAWMHDHRKENPLYEEFDRLLGIAAAYDVTLSLGDGLRPGAVADASDGAQLQELVVLGDLARRARDADVQVMIEGPGHVPIDQIGANVQMQKALCGGAPFYVLGPLTTDCAPGYDHITGAIGGAVAAAAGADFLCYVTPSEHLCLPDIDDVRVGVIAARIAAHSGDIAKKVPGALDRDMQMSACRKALDWRGMYQAAIDPCLPRQRREASHPEEESVCTMCGELCAVKTHNRMTNP
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
A8ZVP4
A7N0J0
RS14_VIBC1
30S ribosomal protein S14
Vibrio
MAKNSMKAREAKRAKLVAKFAEKRAALKAIISDVNASEEDRWNAVLTLQSLPRDSSASRQRNRCNQTGRPHGYLRKFGLSRIKVREACMKGEIPGLRKASW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
A7N0J0
A0KYA2
UPP_SHESA
UPRTase
Shewanella
MKVVEVKHPLVRHKIGLMREGDISTKRFRELAAEVGSLLTYEATADFETETVTIEGWNGPVEVDQIKGKKVTVVPILRAGLGMMDGVLEHIPSARISVVGIYRDEETLEPVPYFEKLASDMNERIALIVDPMLATGGSMIATIDLLKKRGCTSIKALVLVAAPEGIKALEAAHPDVELYTAAIDRCLNEKGYILPGLGDAGDKIFGTK
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
A0KYA2
P49100
CYB5_ORYSJ
Cytochrome b5
Oryza sativa
MSNDNKKVYTLEEVAKHNSKDDCWLIIGGKVYNVSKFLEDHPGGDDVLLSSTGKDATDDFEDVGHSTTARAMMDEYYVGDIDTSTIPARTKYVPPKQPHYNQDKTPEFIIKILQFLVPLAILGLAVAIRIYTKSESA
Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.
P49100
Q9ZMM5
APBC_HELPJ
Iron-sulfur cluster carrier protein
Helicobacter
MLTQEDVLNALKTIIYPNFEKDIVSFGFVKNITLHDNQLGLLIEIPSSSEETSAILRENISKAMQEKGVKALNLDIKTPPKPQAPKPTTKNLAKNIKHVVMISSGKGGVGKSTTSVNLSIALANLNQKVGLLDADVYGPNIPRMMGLQNADVIMDPSGKKLIPLKAFGVSVMSMGLLYDEGQSLIWRGPMLMRAIEQMLSDIIWGDLDVLVVDMPPGTGDAQLTLAQAVPLSAGITVTTPQIVSLDDAKRSLDMFKKLHIPIAGIVENMGSFVCEHCKKESEIFGSNSMSGLLEAYNTQILAKLPLEPKVRLGGDKGEPIVISHPTSVSAKIFEKMAKDLSAFLDKVEREKLADNKDIQPTQTHAYSH
Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.
Q9ZMM5
B3QQS4
RL10_CHLP8
50S ribosomal protein L10
Chlorobaculum
MMKRDKKEEIAQQIAEKFQKSQGFYFTEFQGLDVQKMGQLRLEFRKAGIEYKVVKNTLIKKALRDAAGADKLAEGLKNTTAVAFSYDDPIAPAKIIKKFSKDNEALKFKMASVDGTVFGADALPQLSEMLSKTDNIARTAGLINNMIASVPMVMNAVMRDLVSVIDQVGKLEK
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
B3QQS4
B2VEC5
NADK_ERWT9
ATP-dependent NAD kinase
Erwinia
MNKPFSCIGIVGHPRHPTALTTHEMLYRWLTAKGYQVIIEQQIARELKLEGVQTGTLAEIGRTADLAVVVGGDGNMLGAARVLARYDIKVIGINRGNLGFLTDLDPDNAQQQLADVLEGDYFVESRFLLEAQVCRQSGTPRIGTAINEVVLHPGKVAHMIEFEVYIDENFAFSQRSDGLIISTPTGSTAYSLSAGGPILTPSLDAIALVPMFPHTLSARPLVINSSSTIRLRFSHMRSDLEISCDSQIALPIQQSEDVLIRRSDYHLNLIHPKNYNYFNTLSSKLGWSKKLF
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
B2VEC5
Q2NR41
AMPA_SODGM
Leucyl aminopeptidase
Sodalis
MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISTLLRRGELEGKVGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVINKTINTLNDTGSMEAVCFLTELHVKGRNTYWKVRQAVETAKETLYTFDQLKSNKIEPRRPLRKMVFNVPTRRELTSGERAISHGLAIAAGIKAAKDLGNMPPNICNPAYLASQARQLADGYGKTTTTRVIGEQQMKELGMNAYLAVGQGSANESLMSVIEYKGSPDADARPIVLVGKGLTFDAGGISIKPADSMDEMKYDMCGAATVYGVMRMAMELNLPLNIVGVLAGCENMVDGRAFRPGDVLTTLSGQTVEVLNTDAEGRLVLCDALTYVERFEPEVVIDVATLTGACVIALGHHLTGLVSNHNPLAHELIGAAEQAGDRAWRLPLGDEFQEQLESNFADMANIGGRPGGAITAGCFLSRFARKYNWAHLDIAGTAWRSGKAKGATGRPVAMLSQFLLNRTGLNGDE
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Q2NR41
Q6AYP2
MFA3L_RAT
Microfibrillar-associated protein 3-like
Rattus
MGLLKSHLTVCLPPSVPFLILVSTLATAKSVTNSTLNGTDVVLGSVPVIIARTDHIIVKEGNSALINCSAFGIPDLEYKWYNSVGKLLKEMDDEKERGGGKWQMLDGGLLNITKVSFSDRGKYTCVASNIYGTINNTVTLRVIFTSGDMGVYYMVVCLVAFTIVMILNITRLCMMSSHLKKTEKAINEFFRTEGAEKLQKAFEIAKRIPIITSAKTLELAKVTQFKTMEFARYIEELARSVPLPPLIMNCRTIMEEIMEVVGLEEQGQNFVRHTPEGQEAPDRDEVYTIPNSLKRSESPTADSDASSLHEQPQQIAIKVSVHPQSKKDHVDDQEGENLEVKDEEETEPSEEHSPETAEPSTDITTTELTSEEASPVEAPERELPPAHLETTEPAVTCDRNTCIIYESHV
May participate in the nuclear signaling of EGFR and MAPK1/ERK2.
Q6AYP2
Q4FN05
PDXH_PELUB
Pyridoxal 5'-phosphate synthase
Candidatus Pelagibacter
MNQKNSLGLNKCFLDKIDPIDLFEVWMNEAKKTELNDPNALALATSDQNNFPSIRMVLLKDFNKDGFVFYTNLNSQKGNELKNNPKASMCFHWKSLLRQVRINGMVQKVSNKVADEYYSSRGYESRIGAWASKQSTVINNRDELLNSIEEYKKKYSNKNDVPRPEHWSGWNLIPTSIEFWLDGESRIHERLKYTKDTEGNWVKSLLSP
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Q4FN05
Q5XF78
GAMT2_ARATH
Gibberellin A(4) carboxyl methyltransferase
Arabidopsis
MESPSLPMTAKDWTTTSLHRVFAMQGGEDDLSYVNNSDSQALAITLSKPILISSLQSIKLFSDQTPIKITDLGCATGSNTFTTVDTVVETLQRRYTARCGGGGSPEFEAFFCDLPSNDFNMLFKLLAEKQKVDSPAKYFAGGVAGSFYDRLFPRGTIHVAVSLSALHWLSQIPEKVLEKESRTWNKGKTWIEGAKKEVVEAYAEQSDKDLDDFMSCRKEEMVKGGVLFVLMAGRPSGSSSQFGDQDTRAKHPFTTTMEQAWQDLIEEGLIDEETRDGFNIPAYMRSPEEVTAGIDRCGGFKIGKMDFLKIVEYSDEKQEEWKKDPVSYGRARTNLVQAAIRPMVDAYLGPDLSHELFKRYENRVSTNQEFLHITCFYGVVVFSAIRV
Methylates the carboxyl group of several gibberellins (GAs). Substrate preference is GA4 > GA34 > GA9 > GA3 > GA1 > GA51 > GA20. No activity with diterpenes abietic acid and ent-kaurenoic acid.
Q5XF78
Q0T618
EFEU_SHIF8
Ferrous iron uptake protein
Shigella
MTSRSRQAAYSGIFINETTGEFPQKEQELFEGIVAVIAVVILTWMVFWMRKVSRNVKVQLEQAVDSALQRGNHHGWALVMMVFFAVAREGLESVFFLLAAFQQDVGIWPPLGAMLGLATAVVFGFLLYWGGIRLNLGAFFKWTSLFILFVAAGLAAGAIRAFHEAGLWNHFQEIAFDMSAVLSTHSLFGTLMEGIFGYQEAPSVSEVAVWFIYLIPALVAFALPPRAGATASRSA
Uptake of Fe(2+) ions across the membrane.
Q0T618
Q8BVN7
S2541_MOUSE
Solute carrier family 25 member 41
Mus
MGVHLEVLDTGEQLMVPVDVLEEENKGTLWKFLLSGAMAGAVSRTGTAPLDRARVYMQVYSSKSNFRNLLSGLRSLVQEGGVRSLWRGNGINVLKIAPEYAIKFSVCEQSKNFFYGVHSSQLFQERVVAGSLAVAVSQTLINPMEVLKTRLTLRFTGQYKGLLDCARQILERDGTRALYRGYLPNMLGIIPYACTDLAVYELLQCLWQKLGRDMKDPSGLVSLSSVTLSTTCGQMASYPLTLVRTRMQAQDTVEGSNPTMQGVFKRILSQQGWPGLYRGMTPTLLKVLPAGGISYLVYEAMKKTLGVQVLSR
Calcium-independent ATP-Mg/Pi exchanger that catalyzes the electroneutral exchange of Mg-ATP or free ADP against an hydrogenphosphate and participates in the net transport of adenine nucleotides across the mitochondria inner membrane.
Q8BVN7
Q5HUW9
TRUA_CAMJR
tRNA-uridine isomerase I
Campylobacter
MKIKIIFSYDGTAFLGSATQPHKKGVQDALSGALSHLGIFSPLLMASRTDKGVHASYAVASVECGDYFTNLEYLQKQLNKFSHPFIHIKKIEKVKDDFEVRFDVKSREYRYIFSHSSYSPFMASYVHFYPKFDLDKANELLGFFVGKKDLKFFCKSGGDNKTTLREIFIARAYAYKDFSIFHFKANGFLRGQIRLSVASVLKVLEGKMSEKELKEQIEAKKQYNHFLAPPNGLYLSRICY
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Q5HUW9
Q9KDD7
GREA_HALH5
Transcript cleavage factor GreA
Halalkalibacterium (ex Joshi et al. 2022)
MAEEKKHYMTLEGKKKLEEELEYLKTERRKEVVERIKIARSFGDLSENSEYDSAKEEQAFVEGRISQIEKMIRNAEIIEESEGDANVVSLGKTVKFVEIPDGEEEEYTIVGSAESDPFEGKISNDSPMAQSLLGHTIDDVVIVNTPGGEMEVKILEIR
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
Q9KDD7
Q1LI69
ENGB_CUPMC
Probable GTP-binding protein EngB
Cupriavidus
MSLLHQARFFTTVNHLRDLPATAVPEVAFAGRSNAGKSTAINILCNQKRLAFSSRTPGRTQHINFFTVAPVKAPDPVGFLVDLPGYGYAEVSGSAKFHWQGLLSDYVQARTQLSGLILMMDARRPFTDLDCQMVEWFLPTGKPIHVLLTKADKLTTSDNAKALRETRKVLADYAAQMENPPALTAQLFSSLKRRGIEEAQRVVAGWLALPEAQPAVAKSDTPDTPQG
Necessary for normal cell division and for the maintenance of normal septation.
Q1LI69
Q07MP8
CTAA_RHOP5
Cytochrome aa3-controlling protein
Rhodopseudomonas
MPGSAAARPLRAVKIWLGAIAALIAAMVLVGGATRLTESGLSIVEWKPITGTLPPLTDAQWAQAFEGYKTIPQYRELNAGMSLSEFKTIFWWEWSHRLLGRVIGLAYLLPFLWFIWRGHLGGELKRRLWLIFGLGALQGAVGWWMVASGLSQRVEVAQERLAIHLTLALVIFAAIVWTLRRLDERPVGAVPLRLRITAAALLALTFVQIFFGALVAGLRAGKLYNTWPTIDGALIPSAERLWFQEPWWRNLFDNHLTVQFDHRMLAYALWALAIAHAIDAVRARAGAAARGAVWFAAALTLQAALGIFTLLYEVPIGLALAHQAVAVLVLMLGVLQLERLWPRASASAANLPKSAMAAASRN
Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Q07MP8
P20045
REPB_LACPN
Replication protein RepB
Lactiplantibacillus
MKSESKIDWTVPRPNKNPKTKQPYKRGRNWGIVVYPESLPENWKDIIRQEPIAVSPLHDKDVNPDGEKKKSHYHLVLNYKGNKSFEQIDEIARSLRAPAPQRISSLTGAVRYLTHMDNPEKYQYDNADIETFGGFDLESCLALSTGDKRQALRDMLAFISENEIMHLKDFADYCMSEEAPAGWFELLTERNTLFIKEYIKSNWQKQQYASKNINKMSD
Is essential for plasmid replication. Nicks the positive strand at the plus origin of replication.
P20045
Q6GK28
ESAA_STAAR
Type VII secretion system accessory factor EsaA
Staphylococcus
MKKKNWIYALIVTLIIIIAIVSMIFFVQTKYGDQSEKGSQSVSNKNNKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKTPSKISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSIIDNLHNAQKNVGAIMTREHGVNSKFSNYLLNPINDFPELFTDTLVNSISANKDITKWFQTYNKSLLSANSDTFRVNTDYNVSTLIEKQNSLFDEHNTAMDKMLQDYKSQKDSVELDNYINALKQMDSQIDQQSSMQDTGKEEYKQTVKENLDKLREIIQSQESPFSKGMIEDYRKQLTESLQDELANNKDLQDALNSIKMNNAQFAENLEKQLHDDIVKEPDSDTTFIYNMSKQDFIAAGLNEDEANKYEAIVKEAKRYKNEYNLKKPLAEHINLTDYDNQVAQDTSSLINDGVKVQRTETIKSNDINQLTVATDPHFNFEGDIKINGKKYDIKDQSVQLDTSNKEYKVEVNGVAKLKKDAEKDFLKDKTMHLQLLFGQANRQDEPNDKKATSVVDVTLNHNLDGRLSKDALSQQLSALSRFDAHYKMYTDTKGREDKPFDNKRLIDMMVDQVINDMESFKDDKVAVLHQIDSMEENSDKLIDDILNNKKNTTKNKEDISKLIDQLENVKKTFAEEPQEPKIDKGKNDEFNTMSSNLDKEISRISEKSTQLLSDTQESKTIADSVSGQLNQLDNNVNKLHATGRALGVRANDLNRQMAKNDKDNELFAKEFKKVLQNSKDGDRQNQALKAFMSNPVQKKNLENVLANNGNTDVISPTLFVLLMYLLSMITAYIFYSYERAKGQMNFIKDDYSSKNNLWNNAITSGVIGATGLVEGLIVGLIAMNKFHVLAGYRAKFILMVILTMMVFVLINTYLLRQVKSIGMFLMIAALGLYFVAMNNLKAAGQGVTNKISPLSYIDNMFFNYLNAEHPIGLALVILTVLVIIGFVLNMFIKHFKKERLI
Component of the type VII secretion system (Ess). Provides together with EssB and other components such as EssC and EssE a secretion platform across the cytoplasmic membrane in the host.
Q6GK28
Q3AGY2
TRPB_SYNSC
Tryptophan synthase beta chain
unclassified Synechococcus
MTSTLPNASTPDPSSLQPAVRPGAHGRFGRFGGQYVPETLMPALAELEQAAAQAWNDPAFTDELNRLLKNYVGRATPLYEAERLTAHYRRADGGPRIWLKREDLNHTGAHKINNALGQALLALRMGKKRIIAETGAGQHGVATATVCARFGLECVIYMGAEDMRRQALNVFRMRLLGATVQPVTAGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMLVRDFHAVIGEESKQQCQEAFGRLPDVLMACVGGGSNAMGLFHPFVQDMSVRLIGVEAAGDGVASGRHAATITEGRAGVLHGAMSLLLQDGDGQVMEAHSISAGLDYPGVGPEHSYLREIGRAEYAAVTDQQALDALRLVSELEGIIPALETAHAFAWLEQLCPTLADGTEVVINCSGRGDKDVNTVAEKLGDQL
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q3AGY2
Q6NXK7
DPP10_MOUSE
Dipeptidyl peptidase X
Mus
MKQEQQPTPGARATQSQPADQELGSNSPPQRNWKGIAIALLVILVVCSLITMSVILLTPDELTNSSETRLSLEELLGKGFGLHNPEPRWINDTVVVYKTNNGHVMKLNTESNASTLLLDNSTFVTFKASRHSLSPDLKYVLLAYDVKQIFHYSFTASYLIYNIHTGEVWELNPPEVEDSVLQYAAWGVQGQQLIYIFENNIYYQPDIKSSSLRLTSSGKEGIIFNGIADWLYEEELLHSHIAHWWSPDGERLAFLMINDSLVPNMIIPRFTGALYPKAKQYPYPKAGQANPSVKLYVVNLYGPTHTLELMPPDIFKSREYYITMVKWVSNTRTVVRWLNRPQNISILTLCESTTGACSRKYEMTSDTWLSKQNEEPVFSRDGSKFFMTVPVKQGGRGEFHHIAMFLVQSKSEQITVRHLTSGNWEVIRILAYDETTQKIYFLSTESSPQGRQLYSASTEGLLNRDCISCNFMKEDCTYFDASFSPMNQHFLLFCEGPKVPVVSLHITDNPSRYFLLENNSVMKETIQKKKLAKRETRILHIDDYELPLQLSFPKDFMEKNQYALLLIMDEEPGGQMVTDKFHVDWDSVLIDTDNVIVARFDGRGSGFQGLKVLQEIHRRIGSVEAKDQVAAVKYLLKQPYIDSKRLSIFGKGYGGYIASMILKSDEKFFKCGAVVAPISDMKLYASAFSERYLGMPSKEESTYQASSVLHNIHGLKEENLLIIHGTADTKVHFQHSAELIKHLIKAGVNYTLQVYPDEGYHISDKSKHHFYSTILRFFSDCLKEEVSVLPQEPEEDE
Promotes cell surface expression of the potassium channel KCND2 . Modulates the activity and gating characteristics of the potassium channel KCND2 . Has no dipeptidyl aminopeptidase activity (Probable).
Q6NXK7
Q0W8E0
PYRK_METAR
Dihydroorotate oxidase B, electron transfer subunit
Methanocella
MRPISATIKEIIDETPTIKTFRLDVDDWLHGKPGQYVMVWIRGVDEVPMTLSYDNAITVQKVGEATEALFKLKAGDSVGIRGPYGNGWEIVGDDILLISGGVGSAPLAPLGEKARRIGVNVTTLAGYRTKEEVHFEDRYRAAGELVVATDDGTYGKKGYVTDLLKSVDLKKFTQIYCCGPEKMMYRVLCALDEAGVAGLSQFSLQRYIKCGIGVCGSCCMDPDGLRVCRDGPVFDGETLLRSEMGKYARDASGRRQQI
Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Q0W8E0
Q7U9J7
GLYA_PARMW
Serine hydroxymethyltransferase
Parasynechococcus marenigrum
MSDSTASSINKGLAAADPAIAALIEKEQQRQETHLELIASENFASRAVMDAQGSVLTNKYAEGLPSKRYYGGCEHVDAIEELAIERAKELFGAAWANVQPHSGAQANFAVFLALLQPGDTIMGLDLSHGGHLTHGSPVNVSGKWFNVVQYGVDRETQRLDMEAIRQLALEHKPKLIVCGFSAYPRTIDFAAFRAIADEVGAFLLADMAHIAGLVAAGVHPSPVPHCDVVTTTTHKTLRGPRGGLILCRDADFAKKFDKAVFPGSQGGPLEHVIAAKAVAFGEALQPAFKTYSQHVVANAAALAERLIARGIDVVSGGTDNHVVLLDLRSVGMTGKVADLLVSDVHITANKNTVPFDPESPFVTSGLRLGTAALTTRGFDAGAFREVADVIADRLLNPEDDAVQQQCLRRVEALCQRFPLYAAARQPALA
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Q7U9J7
Q03VC2
CH10_LEUMM
Chaperonin-10
Leuconostoc
MLKPLGDRVIIEVTEAAEETVGGIVLASNAKDKPVTGKVVAAGTGYVLNDGTVRDLTVKVGDEVLFDKYAGQEVSFEGQDYLALHEKDIVAVVE
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.
Q03VC2
A5F2Q7
MOAC_VIBC3
Molybdenum cofactor biosynthesis protein C
Vibrio
MMSQLTHINASGEANMVDVSNKADTVREARAEAYVRMAPETLQLILSGQHHKGDVFATARIAGIQAAKRTWELIPLCHPLLLSKVEVQLEALPEQSSVRIESLCKLSGKTGVEMEALTAASVAALTIYDMCKAVQKDIVIENVRLLEKSGGKSGHFKVDA
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
A5F2Q7
A1AI75
FDHD_ECOK1
Sulfur carrier protein FdhD
Escherichia
MKKTQQKEIENVTNITGVRQIELWRRDDLQHPRLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSCNGLEVQIELSSRRFMGLKERRRALAGRTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTGCTHAAAWMLPSGELVGGHEDVGRHVALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNLTLVGFCKPGRATVYTHPQRLSN
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
A1AI75
A4F9Z0
MSHB2_SACEN
N-acetyl-1-D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase 2
Saccharopolyspora
MLVHAHPDDESTGTGATMARYANEGATVSLVTCTSGELGEVVADDLAHLRGNPDALGEHRRGEIAEALRELGDIRHHWLGGPGRFRDSGMAGEDTNDAAECFAKADRDDVTRAMVEILRAERPHVVVTYDDTGGYGHPDHIAANHALMYALGPAADPAYLPELGEPWDVPKVYWMTLPRSFVKDVQAAGIEGFEPFTVPDEDITAVLDGRDHHAKKLAALRTYRSQVSLDDGDFFATLVQDPRFAIEHYVLVRGERGPGSGPHNWENDLFAGLD
Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
A4F9Z0
P04002
ANPA_PSEAM
HPLC6
Pseudopleuronectes
MALSLFTVGQLIFLFWTMRITEASPDPAAKAAPAAAAAPAAAAPDTASDAAAAAALTAANAKAAAELTAANAAAAAAATARG
Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth.
P04002
Q9D3B1
HACD2_MOUSE
Protein-tyrosine phosphatase-like member B
Mus
MAAAAATAATKGNGGGSGRVGAGDSSGARKKKGPGPVATAYLVIYNVVMTAGWLVIAVGLVRAYLAKGSYHSLYYSIERPLKFFQTGALLEILHCAIGIVPSSVVLTSFQVMSRVFLIWAVTHSVKEVQSEDSVLLFVIAWTITEIIRYSFYTFSLLNHLPYIIKWARYTLFIVLYPMGVTGELLTIYAALPFVRQAGLYSISLPNKYNFSFDYHAFLILIMISYIPLFPQLYFHMIHQRRKVLSHTEEHKKFE
Catalyzes the third of the very long-chain fatty acids (VLCFA) elongation four-step cycle (condensation, reduction, dehydration, and reduction). This endoplasmic reticulum-elongation process is characterized by the addition of two carbons to the lipid chain through each cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of elongation. Therefore, it participates in the production of various VLCFAs involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Q9D3B1
Q3J6M9
ATPA_NITOC
F-ATPase subunit alpha
Nitrosococcus
MQLQLNAAEISELIRKRIEGFEADTEARTEGTVVSLTDGIVRIHGLADVMFGEMIEFPGNTYGLAMNLERDSVGAVILGPYQHISEGDRAKCTGRILEVPVGEALLGRVVDALGIPIDGGGPIEAQATSPIEKVAPGVITRQSVSQPVQTGLKSIDSMVPVGRGQRELIIGDRQTGKTAVAIDAIINQKGTGIKCIYVAIGQKASSVAGVVRKLEEHGALEHTIVVAASASESAALQFIAPYAGCAMGEYFRDRGEDALIIYDDLTKQAWAYRQVSLLLRRPPGREAFPGDVFYLHSRLLERSARVNAEHVEKLTEGKVKGKTGSLTALPIIETQAGDVSAFIPTNVISITDGQIFLETDLFNAGIRPAINAGLSVSRVGGAAQTKIIKKLGGGVRLDLAQYRELAAFAQFASDLDEATRKQLERGQRVTELMKQLQYSPMSVGQMAVSLFAANEGFLDDVEVDKIQDFESALQGYMRSSHGELLDKITKTGDYSDEIAAELRAAIENFKTTNTW
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Q3J6M9
Q1QSI0
RPOZ_CHRSD
Transcriptase subunit omega
Chromohalobacter
MARVTVEDCLDNVDNRFQLVMVATQRSRQLARGSRDAQLPWENDKPTVMALREIAAGLVDRSILNEAVEPPAAKPRPEREFND
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.
Q1QSI0
A0L2T2
ATPF_SHESA
F-type ATPase subunit b
Shewanella
MNFNATLIGQTVAFIIFVWFCMKFVWPPLMNAIEARQKRIADGLADADRAVKDLELAQAKATDQLKEAKATANEIIEQANKRKAQIVEEAKAEADAERAKIIAQGKAEIEAERNRVKEDLRKQVATLAIMGAEKILERSIDPAAHSDIVNKLVAEI
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
A0L2T2
A4X3B7
ENO_SALTO
2-phosphoglycerate dehydratase
Salinispora
MATIEGIVAREILDSRGNPTVEVEVGLDDGTIARAAVPSGASTGAFEAVELRDGEKDRYLGKGVTQAVSNIEDKIVDELIGYEASEQRLIDQKMLDLDGTDNKSQLGANAILGVSLAVAKAAASAAELNLFRYLGGPNAHLLPVPMMNILNGGAHADSNVDIQEFMIAPIGAPTFREALRSGAEVYHALKSVLKKKDLATGLGDEGGFAPNLPTNAAALDLISEAVEKAGYRLGTDIVFALDVAATEFFENGTYTFEGVEKTAEEMSSYYTKLADAYPIVSIEDPLAEDDWSGWRTLTASVGDRIQIVGDDLFVTNPQRIARGIAENAANSVLVKVNQIGSLTETLDAVDLAHRAGFRCMMSHRSGETEDTTIADLAVATGCGQIKTGAPARSDRVAKYNQLLRIEEELADAARYAGSGAFPRYRSA
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
A4X3B7
Q830V1
MGTE_ENTFA
Magnesium transporter MgtE
Enterococcus
MNEGQEMEEQFALLLETLKNQQMNEFRELFLALHIYEQGQFYQSLDEKDRQHLYNYLSPKELADMFDVIEEDNENMKDYLAEMRPSYAADMLAEMYTDNAVDLLNMLDKSQKAKYLSLLSSEEAGEIKELLHYEDETAGAIMTTEFVSIVANQTVRSAMYVLKNQADMAETIYYVYVVDQENHLVGVISLRDLIVNDDDTLIADILNERVISVHVGDDQEDVAQTIRDYDFLAVPVTDYDDHLLGIVTVDDIIDVIDDEAASDYSGLAGVDVEEVSENPLKAASKRLPWLITLLFLGMSTASLISNYESLVSEASILAVFISLITGTAGNAGTQSLAVAVRRLAMKDEKDSNFGRLILSEVLTGLVTGAVTGLTIMIVVGVWQHNLPLGFVIGMAMLCAITVANLAGSLIPMLMDKLGFDPAVASGPFITTLSDLTSVLIYFNIASMFMRYFV
Acts as a magnesium transporter.
Q830V1
Q3IHJ4
EX7L_PSET1
Exodeoxyribonuclease VII large subunit
Pseudoalteromonas
MFSKPLQTIYTVSRLNREIRALLEQGFASLVLTGEISNFITPASGHWYFSLKDDKAQIKAAMWRGNNRNQSYRPINGAQVTVKARVSLYEPRGDYQLIVEHMEPAGEGQFKQEFDALKMRLAAEGLFSSVYKKPLPQNINRIGVITSATGAAIKDILTVLKRRAPQLEVIIYPAMVQGKDAHLQLIKQIELANIRSEVDVLILGRGGGSLEDLWCFNHEQLARAIFNSQLPIVSAVGHEIDTTISDYVADVRAATPSAAAELVSPNTQELHNKVTQLVNRLANAFKHDMSEKRAQALQLQHRLNLCHPRNQLNQKAQRLDELSIALQQAMRNSLYQQERTLNNLTPRLMRQSPDKKLTQASHQLAQLQTRLNQAIQQQLQQANNSLALQASRLDSVSPLNVLARGYSITKTDKQKVVKSVADVKVGDTLITELVDGTLHSQVLS
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q3IHJ4
Q1R0H5
RL3_CHRSD
50S ribosomal protein L3
Chromohalobacter
MTIGLVGKKSGMTRIFTENGASVPVTVIEVEPNRVTRVKTVESDGYSAVQVTSGSRKAKHLTKAAAGQYAKSGVEAGRSLMEFRLAEGEEAPEVGGNITVSLFEAGQKVDVTGTSKGKGFQGAVKRWNFRTQDNGHGNSLAHRAPGSIGQCQTPGRVFKGKKMAGQLGNERVTVQSLEIVRVDAERNLLLVKGAVPGATDCEVIVRSAVKAR
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.
Q1R0H5
B6Q3C6
3DHQ_TALMQ
3-dehydroquinate dehydratase
Talaromyces sect. Talaromyces
MPTILILNGPNLNLLGLREPHIYGSTTLQDVENICIELGKQHNVTVDAFQSNHEGQLIDRIHEARNKVDLIVINPAAYTHTSVAIRDALLGVSIPFIEVHISNVHAREQWRHHSYFSDKAVACIVGLGTFGYEAAIQHATLKQFKDLTFRYKRGDYGEVIYYYESLPNPILVVVL
Is involved in the catabolism of quinate. Allows the utilization of quinate as carbon source via the beta-ketoadipate pathway.
B6Q3C6
Q14114
LRP8_HUMAN
Apolipoprotein E receptor 2
Homo
MGLPEPGPLRLLALLLLLLLLLLLQLQHLAAAAADPLLGGQGPAKDCEKDQFQCRNERCIPSVWRCDEDDDCLDHSDEDDCPKKTCADSDFTCDNGHCIHERWKCDGEEECPDGSDESEATCTKQVCPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCATLCAPHEFQCGNRSCLAAVFVCDGDDDCGDGSDERGCADPACGPREFRCGGDGGGACIPERWVCDRQFDCEDRSDEAAELCGRPGPGATSAPAACATASQFACRSGECVHLGWRCDGDRDCKDKSDEADCPLGTCRGDEFQCGDGTCVLAIKHCNQEQDCPDGSDEAGCLQGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECKDPDACSQICVNYKGYFKCECYPGYEMDLLTKNCKAAAGKSPSLIFTNRHEVRRIDLVKRNYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAYMDKASDPKEQEVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATVDGGRRRTLFSRNLSEPRAIAVDPLRGFMYWSDWGDQAKIEKSGLNGVDRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFSGGNRKTLISSTDFLSHPFGIAVFEDKVFWTDLENEAIFSANRLNGLEISILAENLNNPHDIVIFHELKQPRAPDACELSVQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASTMTRTVPATTRAPGTTVHRSTYQNHSTETPSLTAAVPSSVSVPRAPSISPSTLSPATSNHSQHYANEDSKMGSTVTAAVIGIIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEDEDELHIGRTAQIGHVYPAAISSFDRPLWAEPCLGETREPEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKSKRVALSLEDDGLP
(Microbial infection) Acts as a receptor for Semliki Forest virus.
Q14114
P60704
ABEC3_CRILO
DNA dC->dU-editing enzyme APOBEC3
Cricetulus
MGPFCLGCSHRKCYSPIRNLISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCDSPVSLHHGVFKNKGNIHAEVCFLYWFHDKVLKVLSPREEFKITWYMSWSPCFECAEQIVRFLATHHYLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVTMVAGDSGLGKRLLTNFRYQDSKLQEILRRMDPLSEEEFYSQFYNQRVKHLCYYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMELSQVTITCYLTWSPCPNCAWRLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPKRPFWPWKGLEIISRRTQRRLRRIKESWGLQDLVNDFGNLQLGPPMS
DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA.
P60704
Q6D1U0
TRMD_PECAS
tRNA [GM37] methyltransferase
Pectobacterium
MWIGVISLFPEMFRAITDFGVTGRAVKNGLLNVQYWSPRDFTYDRHRTVDDRPYGGGPGMLMMVQPLRDAIHAAKAAAGEGARVIYLSPQGRKLDQQGVRQLATNQKMILVCGRYEGIDERVIKTEIDEEWSIGDYVLSGGELPAMTLIDSVARFIPGVLGHQASAEEDSFADGLLDCPHFTRPEILESMDVPAVLLSGNHAEIRRWRLKQSLGRTWLRRPELLKSLALTDEQTRLLAEFQREYQSEQQEY
Specifically methylates guanosine-37 in various tRNAs.
Q6D1U0
Q4KBI1
RNH_PSEF5
Ribonuclease H
Pseudomonas
MSDSVEIFTDGACKGNPGPGGWGALLVCKGVEKELWGGEANTTNNRMELMAAIRGLEELKRQCDVQLVTDSQYVMKGINEWMANWKKRGWKTAAKEPVKNADLWQQLDEQVNRHNVTWKWVRGHTGHHGNERADQLANRGVDEVRGYKQP
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q4KBI1
Q82TF6
RECA_NITEU
Recombinase A
Nitrosomonas
MDENKNKALSAALAQIEKQYGKGSIMRLGDSDVAKDIQVVSTGSLGLDIALGVGGLPRGRIIEIYGPESSGKTTLTLQAIAEMQKLGGTAAFIDAEHALDPQYAQKIGVNVQELLISQPDNGEQALEITDMLVRSGSVDVVVVDSVAALTPRAEIEGEMGEPQMGLQARLMSQALRKLTANIKRTNTMVIFINQIRMKIGVIFGNPETTTGGNALKFYASVRLDIRRTGSIKRGEEMVGNETRVKIVKNKVAPPFKQADFDILYGEGISRESEIIELGVLHKLIEKAGAWYSYNGEKIGQGKDNVRDYLKEHKSIAHEIEQKIRAAVGLAETDSRVVPPSSGE
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.
Q82TF6
C4QXE9
CHO2_KOMPG
Phosphatidylethanolamine N-methyltransferase
Komagataella
MVKESKFSYNSKDEKKYSLGKTFRGDIFNVPETHDMVRSLFDPTVKKSVSDYLIVLSLFINGIVYYYSPVTWRIPVFIVLYSFWRLGYNLGIGILLYKQSKSHSMFHWLKQIQINGGWAKKFVELELSSKLNAQQLNSVPDEFKTWIVFRSLVNLILMNDFTTYMCLVFACSDGAFNQSLSLIFLRWVLGISFFIFNIIVKLNAHLIVKDYAWYWGDFFFRLHNNEELIFDGVFDLAPHPMYSIGYAGYYGCALMTKSYTVLIMSIFGHLLQFLFLNYVETPHIEKIYGDDNLSENTISVNKRDDSVFIGTGGKPLVMLTKNFNWLRTNDIFTVVLALYASIVPIFLPASYNNSIIILAIVVKIGTSFVLNSVLYLQSRFKSWTLSFIKNYGTINISILDNKELLERLSFQNWTLLQNNTLVLNYSMLFTISVREVMYNEKFWQTEWLPLRFILAALMILGQFLTVHQMIDSIGLFGWYYGDFFIGVLSSHKSEVTTLSRSGIYHFLNNPERVTSNLTVWALYLLFNNSNKIFLVIALLFTMNNLIVLNFIEKPHMVKLYGEQNVLKHTSGIEKSINSLFLPNHVQGTIVKLSGSIDKVIQDSSKVIDEFIRNKHNQKPKELSLKKRRNSFQQVIELIRGSTDDTLTINLQELNDQGQLQLLNLLRKDDTDFYNLGDPIKVEWNMEDHKGKDKAWIGLYNIFQTSETRTKTLVSSKGYWIPIHREKYINLSDKIRNEEDCILEDELNRGVVQFSAELLPWVPGTYELRLHANEKHEVLAISKPFDIVVKKIDVPTSDDIGDERLEDFANKLYQGFVSKLFPAVESIEDESNWFLQMHIKENARQVEKLCSTLSQSCGVHLTKKAIVDEKCLKDLSFKISKLRKMLDELML
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
C4QXE9
Q9HE02
SSN2_SCHPO
Suppressor of RNA polymerase B srb9
Schizosaccharomyces
MSYQVCFKKYVKMRQWPHVLSLRVYASYFLLYNNLPLSSAMVHDGVHLISIKTILTDQPCPNTIYYAKYQVQRKDNEDAASLLEDKEAYLRNQDCIVHAKNDLLFVYDFQAIPSIPEESSSFMLLNSGAFSRLALFQKDELALLLDLYINFLQGLKKTVLYWLCKEYNFVPIYGVLLPLKLHPSFDTQLWNIYGYPVVDLQLSVLSKGHIEFYLKPTRQTVYRLSEVDNLVKKLDTVIRLAPTGCLATLTSVHANASAQTVDALKHRYGFSLTTTSKWVGVTLESSALEFSWPLELCFLETSALRMNDDSLSSNLTDLNNLVLPSNVVNNKKELTEFANEEAEASDKRKEGFTEKEETADAVVTLVPSHSSSPVNYSINSAKSTPASIKVNEEILVADHNVSDDILMEEIDDVGITEADFDYFDLPNVEEKVEMIEPNFANTMTTLDNEEINTSISQSNTSPNLNTHENIPKQMEIQSDDRMVTEDLNPYNVEVDIPEISLNISDSKIPTSAYMPSYYSAVIFPSSISSIFQKYNYGGKYWCPSPSLSTEDLFESFSVAESVTSTDEDICSTNFIQQDFTMEYNHDFFSSSKTPTNISEQSNPDSNYDTLSLAHQVLMNESKSANFDFSFLKSLDLQPTITLGKNDLLNAILSQNLWFRSLPFWKSMTTSFMMSQDVLNFSSYMRKPIRDYLEKILLGESSAVFLSKSPENYLSSINNGHHALNDNPPSQVNFSETLVNFSQPPRVLLKYNEKKLSLDSSAPENWISLCLQPYGESKDFEVFLLSSKSPDVSSKAISFFYDVQLAYENCKLGKLNLSETSINERVMGFSTNINETDNYDDNETTQSDTATSYEQLASVCVNELSGKNVLFFYFLEDDSEKLLKACQHFICVKDSIKRLGDNKFEDKSLRICTIPNSIFDSPNSHTTNSNSFFTKVSLDIYNNDPLLMDGSLKRREPAFLLKKPLLSTLNYQLKDINPRSSALGEYALHVTYTTVEEHLLICNWNDSYGEFETERRYFLQDLEIEDALQQILEVTFTFLNSMHMDWIVIVMKIGEMSDAEYLFWDQAIIPENLQGNVSLTVGYCSAEHGPGSTSKVFSRIPYSASSTVIRNNSSHELSLVAFIREMAMPVPNDEFKKISTILARGYLALDEDESYLPLLSIHLLISRNHDPYLMLNLILKHYLSMIYLQFRTYVSFSSLPLHISTVLYQKQLLQFMASDITHPVTS
Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex.
Q9HE02
P59407
NANA_LACPL
Sialic acid lyase
Lactiplantibacillus
MSKKLLYAAQMTAFDKDGNINLDGIRALVRYNIDVNKVDGLYVCGSTGEAFMLNTDEKKQVMETVYDEANGAIDLVAQVGSLNLKEAKELAKFATDLGYPKLSAVTPFYYNFTFEQIKDYYNEILKDVDNKLLIYSIPALTGVALTTDQFAELFENPKIIGIKYTNADFYLLERVRNAFPDKLILSGFDEMLLPALALNVDGCIGSTYNLNAPRVREEMDAFEAGDIDKARQLQNISNDMITDLIANDIYPTLKLVMKHMGVDAGYVKKPMSHPTPEMEAGATAIYEKYFKN
Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate.
P59407
Q9Y933
GUAA_AERPE
Glutamine amidotransferase
Aeropyrum
MAKTLDSPGVLVVDFGGQYAHLIARRIRELGVYSEIVPATSLDALGEALPRAAGVVLSGGPGSVWGSRHDEAAAMVLQLGKPVLGICYGHQLLAKVLGGEVGRSPLPEFGPTEVEVLDYGILLNGLPSRFKVWMSHYDAVLRPPGEAKVLARTPGSPVAAMELWGRVFGVQWHPEVRHTQYGREVLDNWLSLVGAPRTWRPGDMVSELVESVKKEVGDALAVAAVSGGVDSTVAALIAKKAIGSRLYPVFIDHGLHPEGEVERVVKLLSRLGLEPVMVDAGEEFLAALEGVGDPEEKRRVVGRVYAEVLERAARDIGAEYLVQGTIYPDVIESGARPGADTIKTHHNVGGLPKDMRLKLVEPLRYFYKDEVRLLAEKLGVPRELIWKQPVPGPGLAVRVEGPITREKLRIVRRADAIVREEVEAAGLGGKLWQYFAVLTASMATGVRGDSRSYGYVVAVRAVESVDAMTAKPAELPWWLLERIARRITSEIPEVVRVVYDITSKPPSTIEWE
Catalyzes the synthesis of GMP from XMP.
Q9Y933
A4QJJ7
RR14_AETGR
30S ribosomal protein S14, chloroplastic
Aethionema
MAKKSLIYREKKRQKLEEKYHLIRRSSKKEISQIPSLSEKWKIHGKLQSPPRNSAPTRLHRRCFSTGRPRANYRDFGLSGHILREMVHACLLPGATRSSW
Binds 16S rRNA, required for the assembly of 30S particles.
A4QJJ7
A5GJ87
RECO_SYNPW
Recombination protein O
unclassified Synechococcus
MSGDRRLQGLALKVGPLGEHDRLLTLLSDDVGVVRLAVPGARRPRSSLAAAVPLTCLDLQVVGRRGLARVRQLRVLRSYSGLGQRLDTLASAQALAELAIALVSSDDPVPGLLEAVLIHLDRLERLSRTPGEEADLCLANVVQAGVHLLALGGYGLPLQACCRSGAALTPPIGQWEWRCSVLPEEGLALGALAGARLQLNPSELALLQRLPRPDLPRRSNGELLGPRPVWLKLLALLECWCRAHLPRPVRSLAMVRDCLSAAPLSDHEPT
Involved in DNA repair and RecF pathway recombination.
A5GJ87
C4K906
ATPD_HAMD5
F-type ATPase subunit delta
Candidatus Hamiltonella
MSMATIARPYAKAIFDFAVEHHSIEHWQNMLAFSAQVSAHKQVTQWLSGVMHSEKTAQIFISLCSDHLDEFSKNFIKIMAQNGRLSLLPEVLKQFMALRAMINSVIDIEVFSAIPLNEDQKKKIIFALEKRLQLKVTLNCKIDESILAGVIIRHGDRVIDGSVSNRLKRLKNFLLS
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.
C4K906
P35810
GYRA_FIBSS
DNA gyrase subunit A
Fibrobacter
MSEEMVPGSQFKSLVEQDMQDCYLRYSMSVIVARALPDARDGFKPVHRRVMYSMHKLGVVPNKGTVKSARIVGDVIGKYHPHGDVAVYDTLARMAQDFSLRYPLVFGQGNFGSIDGDSPAAMRYTEAKMNNLGALMLEDLEKETVDMGPNYDESLEEPLVLPSALPNMIVNGTSGIAVGMATNMAPHNLREVGAAIHALAENPDLTGEDLMEYVKGPDFPTGAIVCGRSGIREAYLTGHGRVRVRARTEIETDAKGKPRIIVTEIPYMVNKAELCKKIADLVRDKRIDGITDIRDESSRDIRIVIELRRDAVGEVVLNNLFKYTQLQTTFSIYNLALVNNLPKLLTLKDLLQVYIDHRLDVITRATQFDLKKAAARLHIIEGLRIATQNIDEVVKIIRQSKTTEIAKQSLQDRFSLDEIQSQAIVDMRLAQLVGLNIEKLEAEYNELIATVADLKDILEKRERRVAIMLQKLDAVVDKYGDERRTTIGEAIDDSDDEDLIAEEEQVITLSKEGYIRRLPIDTFKAQNRGGKGIIGAGLKDEDNVEQIFTASTHSYLLVFTNKGRVYWTKVYRLPEGARNGKGRPIVNFVALTEGEKVQAIVPVRKFGGYFCLVFATKKGIINKMDLTLFSRPRKAGVNAISLDEDDELVKVQLVGMSAEEYEASKNASDDDSAEAVENAAEAQAAEAAIAEESESGDAEDFANRPIPKDLLMIATKNGQAVTFPISCFRAMGRGTHGVKGITLAEGDEVISLLWLKAGNKILTITEKGYGKRSEPGSYRVTRRGSKGVRNLNVTDKIGAAVFVESVADDYDLIITSKDGQVIRIKAADIRLTGRNAQGVKAITLRDGDVVKDATALPSVEDIEQDSADAKETFDKVKGVEVDDDSVVKDDAEKQEIGPTETEE
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
P35810
P28008
PTMCB_STACA
PTS system mannitol-specific EIIB component
Staphylococcus
MDTMSNSQQNKGIGRKVQAFGSFLSSMIMPNIGAFIAWGFIAAIFIDNGWFPNKDLAQLAGPMITYLIPLLIAFSGGRLIHDLRGGIIAATATMGVIVALPDTPMLLGAMIMGPLVGWLMKKTDEFVQPRTPQGFEMLFNNFSAGILGFIMTIFGFEVLAPIMKFIMHILSVGVEALVHAHLLPLVSILVEPAKIVFLNNAINHGVFTPLGADQAAHAGQSILYTIESNPGPGIGVLIAYMIFGKGTAKATSYGAGIIQFFGGIHEIYFPYVLMRPLLFVSVILGGMTGVATYSLLDFGFKTPASPGSIIVYAINAPKGEFLHMLTGVVLAALVSFVVSALILKFTKDPKQDLAEATAQMEATKGKKSSVASKLSAKDDNKAADNKTAETTTATAASNKAEDKDSDELLDDYNTEDVDAHNYNNVDHVIFACDAGMGSSAMGASMLRNKFKNAGLENIQVTNTAINQLPKNAQLVITQKKLTDRAIKQSPDAIHISVENFLNSPRYEELINNLKEDQD
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
P28008
B8F4Q2
SUCC_GLAP5
Succinyl-CoA synthetase subunit beta
Glaesserella
MNLHEYQGKQIFAKYKLPVSQGIACKTADEAVEAIKQLKGDAWAIKCQVHAGGRGKAGGVKLVRNEAEVREFADKWLGKRLVTFQTDANGQPVNTLYVEETAGIARELYLGAVIDRSSQKVVFMASSAGGMNIEEVAAKTPELLHKVAIDPLVGGMAYQGRELAFKLGLTGDQIKQFSFIFTQLAKLFVEKDLSLLEINPLVVTTEGNLLCLDAKMVVDGNALYRQPELAAMHDPSQDDPREALAESHQLNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGFPANFLDVGGGATKERVAEAFKIILSDKAVKAVLVNIFGGIVRCDLIADGIIAAVNEVGVNVPVVVRLEGNNAELGREILAKSGLNIIAAATLTDAAVEAVKAAGGK
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP 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.
B8F4Q2
Q6Q899
DDX58_MOUSE
Retinoic acid-inducible gene I protein
Mus
MTAEQRQNLQAFRDYIKKILDPTYILSYMSSWLEDEEVQYIQAEKNNKGPMEAASLFLQYLLKLQSEGWFQAFLDALYHAGYCGLCEAIESWDFQKIEKLEEHRLLLRRLEPEFKATVDPNDILSELSECLINQECEEIRQIRDTKGRMAGAEKMAECLIRSDKENWPKVLQLALEKDNSKFSELWIVDKGFKRAESKADEDDGAEASSIQIFIQEEPECQNLSQNPGPPSEASSNNLHSPLKPRNYQLELALPAKKGKNTIICAPTGCGKTFVSLLICEHHLKKFPCGQKGKVVFFANQIPVYEQQATVFSRYFERLGYNIASISGATSDSVSVQHIIEDNDIIILTPQILVNNLNNGAIPSLSVFTLMIFDECHNTSKNHPYNQIMFRYLDHKLGESRDPLPQVVGLTASVGVGDAKTAEEAMQHICKLCAALDASVIATVRDNVAELEQVVYKPQKISRKVASRTSNTFKCIISQLMKETEKLAKDVSEELGKLFQIQNREFGTQKYEQWIVGVHKACSVFQMADKEEESRVCKALFLYTSHLRKYNDALIISEDAQMTDALNYLKAFFHDVREAAFDETERELTRRFEEKLEELEKVSRDPSNENPKLRDLYLVLQEEYHLKPETKTILFVKTRALVDALKKWIEENPALSFLKPGILTGRGRTNRATGMTLPAQKCVLEAFRASGDNNILIATSVADEGIDIAECNLVILYEYVGNVIKMIQTRGRGRARDSKCFLLTSSADVIEKEKANMIKEKIMNESILRLQTWDEMKFGKTVHRIQVNEKLLRDSQHKPQPVPDKENKKLLCGKCKNFACYTADIRVVETSHYTVLGDAFKERFVCKPHPKPKIYDNFEKKAKIFCAKQNCSHDWGIFVRYKTFEIPVIKIESFVVEDIVSGVQNRHSKWKDFHFERIQFDPAEMSV
Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines. Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments. The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms. Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons. Ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Sendai virus (SeV), Rhabdoviridae and Flaviviridae. It also detects rotavirus and orthoreovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome. Detects dsRNA produced from non-self dsDNA by RNA polymerase III. May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration.
Q6Q899
A1A1I6
HIS3_BIFAA
Phosphoribosyl-AMP cyclohydrolase
Bifidobacterium
MTNEAYDNTTTLDPRIAQRLKHDDKGLVAAVIQQFDTKEVLMVGYMNDEAIRRTLTTGRVTFWSRSRQEYWRKGDTSGHAQYVKSFALDCDGDAILVEVDQVGAACHTGKRSCFEEGGQLPVVVGHRTKEQEGQR
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
A1A1I6
P11483
ACM3_PIG
null
Sus
MTLHNNNTTSPLFPNISSSWIHGPSDAGLPPGTVTHFGSYNISQAAGNFSSPNGTTSDPLGGHTIWQVVFIAFLTGILALVTIIGNILVIVAFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLSIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFILWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAEAENFVHPTGSSRSCSSYELQQQSLKRSARRKYGRCHFWFTTKSWKPSAEQMDQDHSSSDSWNNNDAAASLENSASSDEEDIGSETRAIYSIVLKLPGHSTILNSTKLPSSDNLQVPEEELGTVDLERKASKLQAQKSMDDGGSFQKSFSKLPIQLESAVDTAKASDVNSSVGKTTATLPLSFKEATLAKRFALKTRSQITKRKRMSLIKEKKAAQTLSAILLAFIITWTPYNIMVLVNTFCDSCIPKTYWNLGYWLCYINSTVNPVCYALCNKTFRTTFKMLLLCQCDKRKRRKQQYQQRQSVIFHKRVPEQAL
The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
P11483
Q97XW1
GLPK1_SACS2
Glycerokinase 1
Saccharolobus
MNTMSHKFVLALDEGTTSARAILFDSDLNIVNIGQYEFPQYYPQPGYVEHDPEEIWEAQMLAVKKAISKIDAKQIVAIGITNQRETTVLWDAKSGKPVYNAIVWQDRRTSPITDWLKANYFKMIKDKTGLVPDPYFSASKIKWILDNVPNVREKAERGEIKFGTLDTYLIWRLTNGKAHVTDYSNASRTMLFNINKLECDREILELLKIPESILPEVKPSSEIYGYSEALGNLIPISGDAGDQQAALFGQVAFNVGEIKATYGTGSFILMNIGNNPIRSENLLTTIAWGLEKNKATYALEGSIFITGAAVQWFRDGLRAIDVSDEIEPLASNVEDNGGVYFVPAFVGLGAPYWDPYARGLIIGITRGTTKAHIARAILESMAYQTRDVIEVMQKESGISINSLKVDGGAAKDNLLMQFQADILGIKVIRPKVMETTSMGVAMLAGLGVGLWNSLEELRSIWKVDKEFIPSMSEEKRRALYSGWKEAVKRAMGWAKVVGGQV
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Q97XW1
P82807
FAXD1_NOTSC
Notecarin-D1 heavy chain
Notechis
MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRSNSLFEEIRPGNIERECIEEKCSKEEAREVFEDNEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLPNYEGKNCEKVLYQSCRVDNGNCWHFCKRVQSETQCSCAESYRLGVDGHSCVAEGDFSCGRNIKARNKREASLPDFVQSQKATLLKKSDNPSPDIRIVNGMDCKLGECPWQAVLINEKGEVFCGGTILSPIHVLTAAHCINQTKSVSVIVGEIDISRKETRRLLSVDKIYVHTKFVPPNYYYVHQNFDRVAYDYDIAIIRMKTPIQFSENVVPACLPTADFANEVLMKQDSGIVSGFGRIRFKEPTSNTLKVITVPYVDRHTCMLSSDFRITQNMFCAGYDTLPQDACQGDSGGPHITAYRDTHFITGIISWGEGCARKGKYGVYTKVSRFIPWIKKIMSLK
Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa.
P82807
A8M8Q9
LYSY_CALMQ
Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase
Caldivirga
MRRACIIGASGVIGGELLRLLLGHNNVEVVCATSRRFAGEFIYRVHPNLRGFINLKFTQPSIDAVLKSESDVVFLALPHGESVKWVPKLVESGLLAIDLSADFRLKNPDDYVKWYHWPQPHPYPDLLKAAAYGLPELHRDEIKATKVIAVPGCMATASIVSLAPLVKGHLINNDFIVVDAKIASSGAGAEGTVLDYHWHRTHVVRPYQPVGHRHTAEIEQELSLLAGSQVNVAFTPHAVDMVRGIFVTGHARLSGSISEPDLWRAYRGMYGNERFIRIVKDKAGLAHYPSVKYVVGTNMVDVGFELDQRLNRVVVFSAIDNLIRGAAGQAIQSFNINQGFPEDEGLRFITPYPV
Involved in both the arginine and lysine biosynthetic pathways.
A8M8Q9
Q9HE00
MTX1_SCHPO
Metaxin-1
Schizosaccharomyces
MGGLTKFSSYFHSIFSRFPLITFSNPYPGENEDYKTKTVMYLTMWNSDLNSEALDVNSLQWQTWAKLNDPSIVFLNVSNHASPDEKVPFIQIESRKLVLNPSLLQYFLKDESTLQQISPWMSLLINQVETAILLTMYLDNENFSEIQKKWLPNMSWPLNIIKSIGLPSQIKRKICLQLNESTLDFDAILEDASKAFSALSELLGSDKWFFNNESPSFLDVSLFAHAEIINHLPLKNDQLKVVLGTHKNLTDLTTRVRTLAGYTSAGPIALR
Involved in transport of proteins into the mitochondrion.
Q9HE00
A6LPT0
RL15_CLOB8
50S ribosomal protein L15
Clostridium
MKLHELKPAAGSKKAPKRIGRGTGSGLGRNAGKGEKGQNARSGGGVRPGFEGGQMPLYRRLPKRGFTNIFAKKIVSINLDRLNIFENGTEVTPELLLERRVVSKVLDGVKILGNGTLEKSLTVKGCKFSKSAIEKIEAAGGKVEVM
Binds to the 23S rRNA.
A6LPT0
A5UEN9
SYV_HAEIG
Valyl-tRNA synthetase
Haemophilus
MTQKFEMADRFNPSAVEQALYQHWEESGYFKPSENENAPSYCIAIPPPNVTGSLHMGHAFQQTLMDTLIRFNRMEGHNTLWQAGTDHAGIATQMVVERKIAAEEGKTRHDYGREAFINKIWDWKAYSGGTISQQMRRLGNSIDWERERFTMDDGLSNAVKEVFVRLHEEGLIYRGKRLVNWDPKLHTAISDLEVENKESKGSLWHFRYPLANDAKTADGKDYLVVATTRPETMLGDTAVAVHPEDERYQSLIGKTVILPLANREIPIIADEYVDREFGTGVVKITPAHDFNDYEVGKRHNLPMVNVLTLNANIRDEAEIIGTDGKPLAGYEATIPADYRGLERFAARKKIVADFEALGLLDEIKPHDLKVPYGDRGGVPIEPMLTDQWYVSVKPLADVAIKAVEDGEIQFVPKQYENLYFSWMRDIQDWCISRQLWWGHRIPAWYDAEGNVYVARNEEEVRSKYNLDSAVELKQDEDVLDTWFSSGLWTFSTLGWPEQTKELKMFHPTDVLITGFDIIFFWVARMIMFTMHFVKDENGKPQVPFKTVYVTGLIRDEQGQKMSKSKGNVLDPIDMIDGISLEDLLEKRTGNMMQPQLAEKIAKATRKEFAEGIAAHGTDALRFTLAALASNGRDINWDMKRLEGYRNFCNKLWNASRFVLTNEKLDLSQGEIEFSLADRWIQSEFNRTVETFRNSLSQYRFDLCANAIYEFTWNQFCDWYLELTKPVFANGNAAQIRAASQTLVHVLEKLLRLAHPLIPFITEEIWQKVKGFVDITADSIMLQPFPQVEENCFDPEAEAEIEWLKEVIVAVRNIRAESNIAPSKGLDLLFRNLSAENAKILEKQTALLKAMAKLDNVQVLAANETAPLAVAKLVGNAELLVPMAGFINKEAELARLTKEIEKYQNEVKRIENKLSNEAFVAKAPEAVIAKEREKQAEYQSGLEKIQEQYKAIEAL
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
A5UEN9
Q8W9F5
CYB_NAPIN
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Napaeozapus
MINIRKKHPLMKILNESFIDLPTPCNISSWWNFGSFLGACLAIQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWLIRYLHANGASMFFICLFLHVGRGLYYGSYTFIETWNIGILLLSAVMATAFMGYVLPWGQMSFWGATVITNLLSAILYIGSTLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAIVHLLFLHETGSNNPTGLISDADKIPFHPHYTIKDALGFLLMSLFLLSLVLFSPDLLGDPDNYSPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVIALVLSILILAIVPFLHNANQRSMIFRPLSQCLYWALVAGLITLTWIGGQPVEHPFIIIGQVASILYFLIILILMPLASFLENKLLKW
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.
Q8W9F5
Q8YAB4
ISPF_LISMO
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Listeria
MIRIGQGYDVHKLAYDRDLIIGGVKIPYEKGLLGHSDADVLLHAITDAIIGAIGAGDIGHFFPDTDMVFKDADSAELLAEIWQKVEADGFRLGNLDATIIAEKPKMAPYVEQMKLRIAELLHADSAQVNVKATTTEKLGFTGREEGIASLAVVLLEK
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Q8YAB4
Q17WZ6
MURA_HELAH
UDP-N-acetylglucosamine enolpyruvyl transferase
Helicobacter
MDFLEIVGQIPLKGGVEISGAKNSALPILAATLLSQQEVTISALPQVADIKAMASLLQNLGAELDWFNSHTLKLCAKSLRHTEATYDLVRKMRASILVLGPLLARFKECLVSLPGGCAIGARPVDLHLKAMQQLGAEITIEQGYIHAKAAKGLKGNDILFDKISVTGTENALMAASLAKGITRIINAAKEPEIAQLCTFLQSGGVEIEGVGSSELKIRGVESDALSLKDIQIIPDRIEAGTYLCVGAITNSQLKINHIIPNHLQAITDKLIEIGFPLDIQQNSIEIYPAKKRQAFEITTKEYPGFPTDMQAQFMALATQCLGTSVIEETLFENRFMHASELQRLGANISLKTNIATIHGSTELTGSDVMATDLRASSALILAALVAKGVSRVHRIYHLDRGYERLEDKINALGAKVLRLKEK
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Q17WZ6
Q8DKG1
COAE_THEVB
Dephosphocoenzyme A kinase
Thermosynechococcus
MSRLLRLGITGGIACGKSVVAGYLQRQYGVPIVDADVLARQVVAVGTPIYQAIVDRYGDGICRRDGTLDRSRLGEIVFAQPQERQWLEAQIHPAVVAEMEQAMATCDQPLMALVIPLLFEAHLEGLVDHIWVVATPPEQQLARLQQRDRLSAHAAGQRLASQLPLEEKIRRADTVLWNTGSLEELYRQVDQAFSLLGRGGKGG
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Q8DKG1
Q72B11
MNMG_DESVH
Glucose-inhibited division protein A
Desulfovibrio
MSTIRKPSPPDMYDCIVVGAGHAGCEAAMALARMGHATLLLTGNADRIGHLSCNPAIGGLAKGHMVKEIDALGGMMGLWADEAGIQFRTLNSSKGPAVRATRAQIDRDAYLRVVRRDIFAQPNLRVWQDMAESIIVEEGRAAGVRTAYGQEFRAHHVLLTTGTFLQGRIHVGLSNFPGGRLGDAPATGLSASLRAIGLELGRLKTGTTPRLLRDSIDFSMMEVQPPDDPPRPFSFRGPGVRLPQLPCHVTWTNERTHEAIRAGFDRSPMFTGVIKGTGARYCPSIEDKVARFPEKERHQVFVEPEGLESPECYPNGIPTSLPLEVQKAMIATIPGLENAQIVRPGYAIEYDYADPVQLRSTLETKALRGLWLAGQINGTSGYEEAAAQGLWAALNVSCTLRSMPPFLPGRDTAYMAVLVDDLVTKGTREPYRMFTSRAEHRLLLRENNADARLTETGRALGLVDDTHWQLFSTKRAALHSLLDELENRRITPDAAARDIFSRLGEPAPTKGVSLADILRRPSLTLPDLAPFWEGVTRFADDVREEAETIVKYSGYLARQQELVARSARMEDTVLPEDMDYTVIPGLTREIVEKLGKVRPHTLGQAARISGVTPAALTCLEIQLRKMGQR
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Q72B11
B6YTR4
DNLI_THEON
TNA1_lig
Thermococcus
MGDMKYTELSDLYRRLEKTTLKTLKTKFVADFLKKTPDELLEVVPYLILGKVFPDWDERELGVGEKLLIKAVSMATGVQEREIENSVKDTGDLGESVALALKKKKQKSFFSQPLTIKRVYQTFIKIAEASGEGSQDRKLKYLANIFMDAQPEEGKYIARTVLGMMRTGVAEGILRDAIAEAFKVKAELVERAYMLTSDFGYVAKVAKLEGNDGLGKVHIQIGKPIRPMLAQNAASVKEALLEMGAEAAFEIKYDGARVQVHKDGDRVVIYSRRLENVTRSIPEVVDAIKASIKSEKAIVEGELVAVGEGGRPRPFQYVLRRFRRKYNIEEMIEKIPLELNLFDVLYVDGEPLIDTPFRERRAKLEEIVEEGEKLKLAQQLVTKKVEEAEEFYKKALELGHEGLMAKRLDSVYEPGNRGKKWLKIKPTMEDLDLVIIGAEWGEGRRAHLLGSFLVAAYDPHSGEFVPVGKVGSGFTDEDLVEFTKMLKPLIIGGEGKFVEIEPKVVIQVTYQEIQKSPKYRSGFALRFPRYVALREDKSPEEADTIERIAQLYEFQERFKAKK
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use both ATP and NAD(+), but NAD(+) may be a preferred nucleotide cofactor.
B6YTR4
P09839
HBA_MACCA
Hemopressin
Macrotus
VLSAADKGNVKAAWDKVGGQAGEYGAEALERMFLSFPTTKTYFPHFDLAHGSAQVKGHGKKVADALTNAVGHMDDLPGALSALSDLHAYKLRVDPVNFKLLSHCLLVTLASHHPAEFTPAIHASLDKFFASVSTVLTSKYR
Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.
P09839
P21697
PLAS_SYNY3
Plastocyanin
unclassified Synechocystis
MSKKFLTILAGLLLVVSSFFLSVSPAAAANATVKMGSDSGALVFEPSTVTIKAGEEVKWVNNKLSPHNIVFAADGVDADTAAKLSHKGLAFAAGESFTSTFTEPGTYTYYCEPHRGAGMVGKVVVE
Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
P21697
Q0HJ64
OPGG_SHESM
Glucans biosynthesis protein G
Shewanella
MVSLLRCQSFKPSSSLICSLALSAAFALSSSAFAEETKPAENKPATPVVSPPKATAQPANKNQVRFTKTGTFDGDSVVKLARKLASKPYVVLKDPLPAGLAKLSYDEYRDIRFNPVSSIWRDQGLPFQMQMFHRGFYFQDLIEIAIVEANQATHLAYEPKYFTAGEVITQALPNDDIGYSGFRIHNQLNTNGVYDELMVFQGASYFRALGKGNSYGLSARGLALKTADPEGEEFPIFRAFWVERPSYDSNLIVVHALLDSPSVAGAYRFSVRPGDNTQIDVEATLFPRVELSKVGLAPSTSMFLHSLNGRHDTDDFRPEVHDSDGLLMFNGRGEHLWRPLANPRQLQVSAFSDNSPQGFGLIQRERNYASYQDLEAHYERRPSLWIEPVGNWGQGAVVLTEIPTESEIHDNIVSFWKPRQPIPAGSEYHFAYRMSWGDEPVAKTNSVVVSRTASGRADIAKATPRRLFVVDYHLNGAMPDELPLAKVESSGGVIANVVIARNAANNGYRLAFELEPEDKELIELRAELKFSTPRQVETWLYRWTL
Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Q0HJ64
A4VI15
TRMA_PSEU5
tmRNA (uracil(341)-C(5))-methyltransferase
Pseudomonas
MPLPQLDPAQYAAQLAEKAARLEELLAPFDAPAAEVFDSPREHYRLRAEFRLWREGGQRHYAMFEQGDKHKAILIDDFPIASRRINELMPQLKAAWQASEVLSFKLFQVEFLTTLSGDALITLAYHRPLDEAWQAEAEQLAADLGVSLVGRSKGKRIVIGRDYVEEQLVVAGRSFRYRQPEGAFTQPNGEVCQKMLNWAHEALGERDDDLLELYCGNGNFTLPLATRVRRVLATEISKTSVNAALANIEDNGLDNIELVRLSAEELTQALNEVRPFRRLAGIDLKSYSFGSVFVDPPRAGMDPDTCELTRRFERILYISCNPETLAQNIAQLADTHRIERCALFDQFPYTHHMEAGVLLVRR
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
A4VI15
C5CSH5
LEUC_VARPS
Isopropylmalate isomerase
Variovorax
MARTLYDKIWDEHVVHTEEDGTAILYIDRHLVHEVTSPQAFEGLREAGRKLWRISSVVATADHNTPTTGWERGYEGIADPTSKEQVTTLDKNIAEFGAAAFFPFLSKRQGIVHVIGPESGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVMATQTLLGKKAKNMLVKVEGKLPFGCTAKDIVLAIIGKIGTAGGTGYTIEFAGSAIRDLSMEGRMTVCNMAIEAGARAGLVAVDEKTIGYIKGRPLAPTGVEWDQAVAYWRTLQSDPDAAFDAVVELDATQIQPQVTWGTSPEMVVDINGRVPDPDKEKDASKRSAIERALVYMGLEPNKAMNDIFIDKVFIGSCTNSRIEDMREAAAVVKKLGQKVAKNVKLAMVVPGSGVVKEQAEREGLDVIFKAAGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVHGHFVDVRTFA
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
C5CSH5
Q9SHH7
GSTUP_ARATH
GST class-tau member 25
Arabidopsis
MADEVILLDFWPSMFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPVHKKIPVLIHNGNPVCESLIQIEYIDEVWPSKTPLLPSDPYQRAQAKFWGDFIDKKVYASARLIWGAKGEEHEAGKKEFIEILKTLESELGDKTYFGGETFGYVDIALIGFYSWFEAYEKFGSFSIEAECPKLIAWGKRCVERESVAKSLPDSEKIIKFVPELRKKLGIEIE
May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Q9SHH7
Q0AUM4
ARGB_SYNWW
NAG kinase
Syntrophomonas
MIVSAMEKAEILVEALPYIKDFYGRRVVIKYGGAAMTDCELKQKVMQDIVLMKFVGMHPIVVHGGGPEINQMLSRLGIQSEFVNGFRVTDAATMEIVEMVLGGKVNKEIVAGIHASGGKAVGISGKDGMLIQAHPADGSGKMGFVGEVQYVNPELIEKVIENGYIPVIAPIGIGEDQQSYNINADLVAAAIAVSMKADKLVLLTDVPGLMMNPADSNSLISVLKVSEVENYVQEGIIAGGMVPKVQCCVEAVTGGVGRTHIIDGRVPHSILLEIFTDEGIGTMVVNE
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Q0AUM4
O01671
SXL_MEGSC
Sex-lethal homolog
Megaselia
MYRGGRMWGMSHSLPSGMSSYAFSPQDTDFSSYPSTIGRQHSQQSQRYYQNNNCGLGSVGNMANSTNSLNSGTNNSGTNLIVNYLPQDMQDRELYSLFRTIGPINTCRIMRDYKTGYSYGYGFVDFGSEADALRAINNLNGITVRNKRIKVSFARPGGEQLRDTNLYVTNLSRSITDEQLETIFGKYGQIVQKNILRDKHTGTPRGVAFIRFNKREEAQEAISALNNVIPEGGTQPLTVRVAEEHGKSKGHVYMAPNQPPHGNMGHGNMGNMGHGNMGMAGGSGMNLNNMNAFNGMNQMVHRGRQKHSYQRKIHPYNPNFL
Unknown; apparently not involved in somatic sex determination.
O01671
Q8WHM4
MATK_LEMMN
Intron maturase
Lemna
MEDFKGYLQKGGFKQQHLLYPLLFQEYIYALAHDQGLNVNASTFNEPPEISGYDKKYSSLLVKRLINRLYQQNTFIHSVNNSKDNRFVGHNKNFYYQMISEAFAIVVEIPFSRRLVSSLKEKKEIPKYQNLRSIHSLFSFLEDKFSHLNYVSDILVPYPVHLEILVQILQCWIQDVPTLHLLRLLFQDYHNGNNRITPNKSTYGFSKDNPRLYRFLYNSYVVEYEAIFVFLRKSSSYLRSTSFGPLLERTHFYRKMKHIGVTCCNDFQKTLWLFKDALMHYVRYQGKSIMASKGNHLLMKKWKSYFVNLWQCHFHFWSQPSRIHINQFPHFSFYFLGYLSSVPINPSSAKSQMLENSFLIDTVTPKFETMISIIPMIGSLAKAKFCNLSGNPLSKPVWAELSDSDIIDRFGRIYRNLSHYYSGSSKKQTLYRIKYILRLSCARTLARKHKSTVRAFLQRLGSEFFEEFFIEEDKILSLILPTTSYSLQQLSRESVWFLDIIRINDLVNHLDL
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Q8WHM4
Q57124
Y895_HAEIN
Uncharacterized transporter HI_0895
Haemophilus
MYEEIRMKFTDIFIRRPVLAVSISLLMIILGLQAISKLAVREYPKMTTTVITVSTAYPGADANLIQAFVTSKLEESIAQADNIDYMSSTSAPSSSTITIKMKLNTDPAGALADVLAKVNAVKSALPNGIEDPSVSSSSGGSGIMYISFRSKKLDSSQVTDYINRVVKPQFFTIEGVAEVQVFGAAEYALRIWLDPQKMAAQNLSVPTVMSALSANNVQTAAGNDNGYYVSYRNKVETTTKSVEQLSNLIISSNGDDLVRLRDIATVELNKENDNSRATANGAESVVLAINPTSTANPLTVAEKIRPLYESIKTQLPDSMESDILYDRTIAINSSIHEVIKTIGEATLIVLVVILMFIGSFRAILIPILAIPISLIGVLMLLQSFNFSINLMTLLALILAIGLVVDDAIVVLENIDRHIKAGETPFRAAIIGTREIAVPVISMTIALIAVYSPMALMGGITGTLFKEFALTLAGAVFISGVVALTLSPMMSSKLLKSNAKPTWMEERVEHTLGKVNRVYEYMLDLVMLNRKSMLAFAVVIFSTLPFLFNSLSSELTPNEDKGAFIAIGNAPSSVNVDYIQNAMQPYMKNVMETPEVSFGMSIAGAPTSNSSLNIITLKDWKERSRKQSAIMNEINEKAKSIPEVSVSAFNIPEIDTGEQGPPVSIVLKTAQDYKSLANTAEKFLSAMKASGKFIYTNLDLTYDTAQMTISVDKEKAGTYGITMQQISNTLGSFLSGATVTRVDVDGRAYKVISQVKRDDRLSPESFQNYYLTASNGQSVPLSSVISMKLETQPTSLPRFSQLNSAEISAVPMPGISSGDAIAWLQQQATDNLPQGYTFDFKSEARQLVQEGNALAVTFALAVIIIFLVLAIQFESIRDPMVIMISVPLAVSGALVSLNILSFFSIAGTTLNIYSQVGLITLVGLITKHGILMCEVAKEEQLNHGKTRIEAITHAAKVRLRPILMTTAAMVAGLIPLLYATGAGAVSRFSIGIVIVAGLSIGTIFTLFVLPVVYSYVATEHKPLPVFDENKTTH
Could be a drug efflux pump.
Q57124
Q823F3
RBFA_CHLCV
Ribosome-binding factor A
Chlamydia
MTENRRIKKVNSLLREAIANVILKDVKHPKISNQWITVTRVCLSKDLHSARVYVSIMPHENTSAETLDALKASAGFIAYKASKGVVLKYFPEIHFYIEDIFSPQDHIENLLWKIREQDKN
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.
Q823F3
B1M1U6
RLMN_METRJ
tRNA m2A37 methyltransferase
Methylobacterium
MATPSLDSARAADAAIEKAPDLLPEALPGRRPSLVGLTRDALKAQLIGMGVPERESRMRAGQVWHWVNFRGASDFAEMTNVGKALKAQLAEHFTLERPEVASRQVSRDGTRKWLLRMAPTNRQEHNRGAEIECVYIPGPDRGTLCVSSQVGCTLTCSFCHTGTQRLVRNLSAAEIVQQLVTARDELGDWPGQMPSRDAGGSGEVGRLVTNIVFMGMGEPLYNLDAVVDAVGVMSDQEGLGLSRRRITVSTSGVVPQIPRLGEQANAMLAISLHAVRDDLRDELVPLNRKYPIAELLAACRAYPGLSNARRITFEYVMLKGVNDSDADARELVRLLKGIPAKINLIPFNPWPGSRYECSDWDRIERFSEIVFNAGYASPVRTPRGRDILAACGQLKSETEKLRARARLMQEEGIGVESFYAGADD
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
B1M1U6
C3XR70
ENOPH_BRAFL
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Branchiostoma
MSDSRLRRRQGTAGTDNKRRADGPHDISGLLDGVSVVLLDIEGTTTPITFVKDELFPYVCSHVRQHLEEHWKEEECQEDIAALRKQAKEDKEMDGVVLIPECTTKDDDEEARKKVLSAVVDNVLLNMDADRKVTALKQLQGHMWRAAYQTGKIKGEYVKLTFADVVPAIRGWLETGRQVYIYSSGSVEAQKLLFGFSTEGDLLELFSGHFDTTTGLKVETESYRRIAKTVGCDPANILFLTDVVREAKPSREAGMKTCLTVRPGNAPLTEEDWANYPVIKSFSELACDVSPTKMRSRGKAAT
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
C3XR70
A8EQW9
SYE1_ALIB4
Glutamyl-tRNA synthetase 1
Aliarcobacter
MAITRFAPSPTGYLHIGGLRTSLYSYLWARKTGGEFRLRIEDTDLARNSEEAMKAIIDAFDWVGLNYDGEVFYQSKRTDIYKQYIDKLLESGNAYKCYMSKEELDALRAAQEAAKQTPRYDGTWRPEPGKELPPVPAGVEPVIRIKAPTTGTIEFDDGVKGHMKFDANQVDDYVIARSNGMPTYNFVVAIDDALMGMTDVIRGDDHLSNTPKQIVVYNALGFKVPKFYHVPMINNPEGKKLSKRDGAMDVMDYKRLGYLPEALLNFLVRLGWSNGDQEIFSMKEMLELFDPSNINKSASSYNGEKLLWLNSEYIKAVSNERLIEELKFFDLDLSNYPKKNEILDLAKQRAQTLVELKKSITDIIDIPTSYEESGVKKFIKEDTKELLEKYLLLLESNKNSLDSVEKIEEFTKPFINDNGLKFPQLFQPIRIALTGGTQAPSVYDIIFILGYDEIFKRINEALKRNFQNT
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).
A8EQW9
Q4AAX4
END4_MESHJ
Endonuclease IV
Mesomycoplasma
MIKIGSHVRFRKPDYLFGAIQESLENKANTAMIFLGPPQSTFRVKPENYKLQDYQKHFFKQIPPEDIIVHAPYIINPASPIKAQFSNDFLVKEIEKINYIGAKFLVLHPGFFTSFTKEVAKKQLISSLKSILEKTKNVILLLETMSGKGSEMCANFEEIVEIVEAVESPRIGICLDTCHVWDAGYDLKNFPEFCKEIRRTRLINYLKVIHLNDSLSPLGSKKDRHANIGKGFIGLESLRKIIFDPLFANIPKILETPYVDNKPIYDQEIALLLKKV
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Q4AAX4
Q5R504
F162A_PONAB
E2-induced gene 5 protein homolog
Pongo
MGSLSGLRLAAGSCFRLCERDVFSSLRLTRSSDLKRINGFCTKPQESPRAPSRTYNRVPLHKPTEWQKKILVWSGRFKKEDEIPETVSLEMLDTAKNKMRVKISYLMIALTVVGCICMVIEGKKAAQRHESLTSLNLEKKARLREEAAMKAKTE
Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues. May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition. May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly.
Q5R504
Q8RAE4
AROQ_CALS4
Type II DHQase
Caldanaerobacter
MKRVLVIHGPNVNLTGKREKEVYGEITFEEINNMIKREAAKLDIAVKIQQSNSEGEIINLIHSAENNFDAIIINPAAYTHYSLAIMDAIASVSVPVIEVHISNIFGREEFRKVSVTASRCKGVITGFGPYSYILALYAVKFLEDSIGG
Catalyzes a trans-dehydration via an enolate intermediate.
Q8RAE4
Q0AUI3
RL2_SYNWW
50S ribosomal protein L2
Syntrophomonas
MGIKKFKPTTPSRRHMTTMSFEEITKQEPEKSLIAPLKRKAGRNVKGRITVRHRGGGHKRQYRIVDFRRVKDNVPARVAAIEYDPNRSAHIALLHYFDGHKAYIIAPHNLRVGDVIESGPNADIKTGNTLPLKDIPVGSLIHNIELRPGKGAQLVRSAGAVAQLMAKEGAYAHVRLPSGEVRLIHVNCRATIGQVGNLEHENMTLGKAGRSRWLGIRPGVRGSVMNPTDHPHGGGEGRAPIGRKYPVSPWGKIAIGGKTRRKKPSDNMIVRKRKP
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.
Q0AUI3
B4SK34
LGT_STRM5
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Stenotrophomonas maltophilia group
MIYFHDIDPIALSLGPIKVHWYGIMYLLGFTAAWLLGRKRIADGRLPGVDANGFSDLLFYAMLGVVLGGRIGYMLFYALGDFLHNPLLLFKVWDGGMSFHGGLLGVIAACWWWSRKHKLHFFDTMDFMAPLVPLGLGFGRIGNFIGAELWGKYTDGSWGVVFPSGLPAPLNQLDHATLQAQFATGALNQFARHPSQLYEALLEGLVMFVVLWAVSAKPRHRYLVGGLFALMYGLFRFAVEFVRMPDNGVYVAFDWLTRGQILSLPLIAFGLVLLVMSRRAPVLQPQLPVAAEGKA
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
B4SK34
Q5AQA3
MTND_EMENI
Acireductone dioxygenase (Ni(2+)-requiring)
Aspergillus subgen. Nidulantes
MKAYWYDNKPGDQREPHDSGRPVSEDYLASLGVIYRHFPELSDVDALAKERGYKNRDEITVSPATMGEAYEDKVKMFFAEHLHEDEEIRYIRDGEGYFDVRGKEDEWVRIRLVKDDLIILPAGIYHRFTTDNKNYIKAMRLFQEEPKWTPLNRAPELDENQHRKSYLEGLTATSIAAN
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Q5AQA3
A1UHM2
BIOD_MYCSK
Dethiobiotin synthase
unclassified Mycobacterium
MSVLVITGTDTGVGKTVATAALACAARVAGIDVAVCKPVQTGTGPVGGTGDDDLVEIGRLAGVDALHPGWRYPDPLAPVAAAERAGAALPTRDELIGMVRAADAPGRLTLVEGAGGLLVELGQDAVTLRDVATELDAPVLVVVAPGLGTLNHTALTLESLAAQHVPCAGLVIGAWPAQPGAAEIDNRDTLARLAPVRAALPAGVGSVSPVDFERISATAFDPNWLAGLL
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.
A1UHM2
Q6PUR7
SMR8B_DANRE
Smith-Magenis syndrome chromosomal region candidate gene 8 protein homolog B
Danio
MIGSPDLVAFTKETDFSEITTDSSVLPEDLSVPMYPYTGDATPWSKISSAKLKKDFILISEFSEQVGPQPLLTVPLETKACGTFDLNYFSLRIMSVDYQTSLAGSPGYGSFKLNFVEDSKVVLADSREGVFAYVHHLTLYDLEARGFVRPLCLAYVSSDENKIIQQFQRISTEFNKVSECLKTGNRKNFANELEVKLRDLEYTRVVLQKELNTVSVKCSSEREPILNGVHSFERNADEVKLNEKSSHTDEISPQEKDGCGNSRKVEVKLENENRSHFEHEQYGKQRKDKPDKTSCPMPLANKNDELASVEKLIQDYKSLLKQVTCYPTRKLRDSEYSPYEPDDLPQSFDLDLDSQFAGPMLECSVFTYTNTPSQTLQQINSTSSSRFDKRLKTLEELCDDYFYQQALQQLYSIERTFRGDACYLYTQQLCRNLLRNLKSTNFLFEDPCDLDDDVGLQIGQSTIQQPSFLPAPSFLSGPVSLESYASCVEMVPIKLELGGSSQSQVQHSTLNTPSKDNRPQVADKSPAEVEMKGEIISAPDCQGNVESVSNLMKTSISSGDSIEVLGTERSFRSQGANTLVETAMHRPPPLSSATALEGLKQGRVPTRRTCSEDSIEVLCITESISPDELRASYPCAIDEESPEQETDEKNSSQYQEDNNEKSIYVQGKISADHENACLKKLHPSVTVTPPDCPLTLEETSFQDSCQATESATMLLLDEPSRMVPDDLSDCFSYRSTTASTTSECTFPACLPKDKREGGTRRRRGRVGRAALQFMRQFPFAVHAVFSLLSGRTLVVLGSEEAAVRRLVTALSVYLPHLTKYKDSIQPWTSTPLQLTDLLNWKLIGFDRMCSFNPSSLPHCLDHYSRYLSILDVDQKTLHCPTYSGSLINLLVEPKSHFKRGNTYFTFAQSVQSKLVTKAFLLTFSHGHPSPSRPQGSSGTECFLSELHTDDKKILRYLSELIKLHFMEVTPNVLLFSYTTTSIFKL
Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy. In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation. The C9orf72-SMCR8 complex also acts as a negative regulator of autophagy initiation by interacting with the ATG1/ULK1 kinase complex and inhibiting its protein kinase activity.
Q6PUR7
O86088
PBPA_NEICI
DD-transpeptidase
Neisseria
MIKKIVTTCFGLVLGLCVFGVGLVAIAILVTYPKLPSLDSLQHYQPKMPLTIYSADGEVIGIYGEQRREFTKIGDFPEVLRNAVIAAEDKRFYQHWGVDVWGVARAVVGNIVAGGVQSGASTITQQVAKNFYLSSEKTFTRKFNEALLAYKIEQSLSKDKILELYFNQIYLGQRAYGFASAAQIYFNKDVRELTLAEVAMLAGLPKAPSAYNPIVNPERAKLRQKYILNNMLEEKMITLQQRDQALNEELHYERFVQKIDQSALYVAEMVRQELYEKYGEDAYTQGFKVYTTVRTDHQKVATEALRKALRNFDRGSSYRGAESYIDLSKGEDVEETVSQYLSGLYTVDKMVPAIVLDVTKRKNVVIQLPSGKRVTLDGRSLGFAARAVNNEKMGESRIRRGSVIRVRNNGGRWVVVQEPLLQATLVSLDAKTGAVRALVGGYDFHSKTFNRAAQAMRQPGSTFKPFIYSAALSKGMTASTMVNDAPISLPGKGANGSVWTPKNSDGRYSGYITLRQALTASKNMVSIRILMSIGVGYAHEYIQRFGFKPSELPASLSMALGTGETTPLKIAEAYSVFANGGYRVSSHVIDKIYGSDGRLRAQMQPLVAGQNAPQAIDPRNAYIMYKIMQDVVRVGTARGAAALGRSDIAGKTGTTNDNKDAWFVGFNPDVVTAVYIGFDKPKSMGRAGYGGTIAVPVWVDYMRFALKGGQGKGMKVPEGVVSSNGEYYMKERMVTDPGLVVDNSGIAAQPSRRIREDKEAGAEDVERGAADEVRQEVQETPVLPSNTGSKQPQLDSLF
Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
O86088
E3Q897
AMPP2_COLGM
Prolidase
Colletotrichum graminicola species complex
METVVDHHVIEVDEFDALFIEVKTEAAPVESVVSVAPIPARFPAKLHARKIAAELNASDGLVFLPGEPSRSYEDSDMGPAFRQRRYFYYLSGANFADCAVTYELASDRLILWVPYVEPRQVLWFGSTPGISECLKQFDVDDVRYTTQLNKFLYRHLTPGSTLYVIHADQVPLHGDFLQSAAEVRIDVTSLQPAMDQARVVKTDYEVAMIRKAAAVSALAHRRVAEKLLRLENESEIEAVYQAWCTTSGAREQAYAIIAGSGKNASTLHYDANNEPLEGREVVVFDAGCEWHCYASDITRTLPISGKFSAEAKAVYDVVAKMQDECISFIRPGTLFFDLHIHASRVAQQGLLKLGVLKGDPAEVWDAGTVAAFFPHGLGHHVGLEVHDVSGRERLLLLNNVMGAQGGRVGKREVVTPEMLGAMVQASAPGAAAAAAPPPYKGRQYLRKNMIVTVEPGIYFCREYIEGYFLSNPRHARFINKTVLERYYRVGGVRIEDDILVTDDGYENLSTGAPKGEELLRVINGKA
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
E3Q897
B2IVX7
TRHO_NOSP7
tRNA hydroxylation protein O
Nostoc
MNSENTQIVAALYKFVKLPDFAQKRDPLLSYCQAQGVKGTILLAQEGINGTIAGSRQAIDSVLWFLRSDPRLADLEYKESYTETPPFERMKVRLKSEIVTLGLPEIDPTEKVGTYVSPQEWNDLICDPEVTVIDTRNDYEVNIGTFQGAENPQTGSFREFPDYVVHNLDPTKHKKVALFCTGGIRCEKASSFMLAQGFAEVYHLKGGILKYLEEVPAQESLWQGECFVFDERVAVSHGLEEGSYELCFCCGYPISEEDKISPKYEQGISCAYCFDSLTEEKRARQQEKWRHYQTQVANSKNRDVS
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
B2IVX7
P25974
GLCB1_SOYBN
Beta-conglycinin beta subunit
Glycine subgen. Soja
MMRVRFPLLVLLGTVFLASVCVSLKVREDENNPFYLRSSNSFQTLFENQNGRIRLLQRFNKRSPQLENLRDYRIVQFQSKPNTILLPHHADADFLLFVLSGRAILTLVNNDDRDSYNLHPGDAQRIPAGTTYYLVNPHDHQNLKIIKLAIPVNKPGRYDDFFLSSTQAQQSYLQGFSHNILETSFHSEFEEINRVLFGEEEEQRQQEGVIVELSKEQIRQLSRRAKSSSRKTISSEDEPFNLRSRNPIYSNNFGKFFEITPEKNPQLRDLDIFLSSVDINEGALLLPHFNSKAIVILVINEGDANIELVGIKEQQQKQKQEEEPLEVQRYRAELSEDDVFVIPAAYPFVVNATSNLNFLAFGINAENNQRNFLAGEKDNVVRQIERQVQELAFPGSAQDVERLLKKQRESYFVDAQPQQKEEGSKGRKGPFPSILGALY
Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.
P25974
Q6FPE8
RFT1_CANGA
Oligosaccharide translocation protein RFT1
Nakaseomyces/Candida clade
MSGADILEKTTRGATFLMMGQLFSKIVTFLLNNTLVRYLSPRIFGITAFLEFIVGTVLFFSREAIRLSTQRIADGNDADNDHDHDRDDSALQVCVNFAMIPLFIGIPLSIGLIAWQYHNINGYFVTLPFFQWSVFAIWVGIILELVNEPLFVLNQHFLNYGARSRYESIAVTANCLVNFTVVYSYEKKLILTSYFDDSERFREGIAILAFALGKLAYAATLLMCYYYNYLMNFKSNKPFKLSLQKIKSKVNEKQTYYFRSDILEHFKKVYFQLCFKHLLTEGDKLIINTFCTVEEQGIYSLLSNYGSLITRLLFAPIEESLRLLLAVLLSKKDSKNLQLSMKVLVNLTKFYLYLSLLVMIFGPNNSSYLLQFLIGSKWSTNSVLHAIRVYCVYIPFLSFNGIFEAFLASVATGDQILRHSYFMMMCSFAFLINSWIFIEYLDLSVNGLIISNIINMSLRIIYSFSFIVKFYRELHTESSIFMNFTNFKATLGAAALVAILNWQMVGYVSSFNGFITSATLALILLSVILIKERATLNELIINRRAANMKSV
May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane.
Q6FPE8
A8WQT4
MICU1_CAEBR
Calcium uptake protein 1 homolog, mitochondrial
Caenorhabditis
MLRHNFRSSIFIRIVANSWSITRSVSSAPIKAESRKQQDSLKNIDSGEAYTALGNIRQKKDVFHYTDRASGTGYSHYSNSVYQHRPYIWPPLRKMYNWNYAFVIAGMVILMSDFEWIKEQIKGASTPFRPEASQKEESTDSGTEIEVKEKPKKKKLGFRERRIIEYEDRLRLYSTPDKIFRYFATLKIIDPNDESGRIFEVFMTPEDFLRSFTPGVMQPRRWGLDSFKAYNPEKHKRHKFSDPNSIFYKLGENGLINFSDYLFLMTLLSTSHADFALAFKIFDVDGNGALDKEEFTKVQQLIMSQTTVGQRHRDHVTPNSSFRVETNSALETYFFGKDGKGSLSSEKFIEFQERLQHDILKMEFERRDAMENSDGLITEESFAQLLLLHAQIAEKKQKHMLKRVKRRFKGDQSKGVSFDETKAFFEFLYHIDDVDIALHFHKMAGMSIDAKLLKRVAVKVTGIPLSDHVVDVVITLFDDNLDGKLSHEEMVAVMRRRMRRGLERPRDTGLFRLFDAVLECGKRAYHASPLPFY
Key regulator of mitochondrial calcium uniporter (MCU).
A8WQT4