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2.75k
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5.51k
AlphaFoldDB
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Q9BEG8
S26A2_BOVIN
Solute carrier family 26 member 2
Bos
MSLKNEDQNDLSPKDSVKGNDQYRAPSGIHLEPEEESRNDFWQFEPSNLFRHPRIHLEPQEKSDNNFKKFVIKKLEKSCQCSSTKAKNTIFGFLPVLQWLPKYDLKKNILGDVMSGLIVGILLVPQSIAYSLLAGQEPIYGLYTSFFASLIYFILGTSRHISVGIFGILCLMIGEVVDRELYIAGYDTVHAASNESSLVNQISDKTCDRSCYAIIVGSTVTFVAGVYQVAMGFFQVGFVSVYLSDALLGGFVTGASFTILTSQVKYLLGLSLPRSAGVGSLITTWLHVFRNIRKTNICDLITSLLCLLVLLPTKELNERFKSKLKAPIPVELFVIVAATLASHFGKLNEKYGTSIAGHIPTGFMPPKAPDWNLIPRVAVDAIAIAIIGFAITVSLSEMFAKKHGYTVKANQEMYAIGFCNIIPSFFHCFTTSAALAKTLVKESTGCQTQVSGVMTALVLLLVLLVIAPLFFSLQKSVLGVITIVNLRGALCKFKDLPQMWRISRMDTVIWFVTMLSSALISTEIGLLTGVCFSMFCVILRTQKPKASLLGLVEDSEVFESMSAYKNLQAKSGIKIFRFVAPLYYVNKEYFKSVLYKKTLNPVLVKAAQRKAAKRKIKRETVTPSGIQDEVSVQLSHDPLEFHTIVIDCSAIQFLDTAGIHTLKEVRRDYEAVGIQVLLAQCNPSVRDSLARGEYCKKDEENLLFYSIYEAMTFAEDSQNQKERHIPNGPNFSSD
Sulfate transporter. May play a role in endochondral bone formation.
Q9BEG8
Q7U669
PSBA2_PARMW
Photosystem II Q(B) protein 2
Parasynechococcus marenigrum
MSTAIRSGRQSNWEAFCQWVTDTNNRIYVGWFGVLMIPCLLAATICFTIAFIAAPPVDIDGIREPVAGSLIYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVCFHFLIGISAYMGRQWELSYRLGMRPWICVAYSAPLSAAMAVFLVYPFGQGSFSDGMPLGISGTFNFMLVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTETESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVVGIWFTSMGVSTMAFNLNGFNFNQSILDGQGRVVNTWADMVNRAGLGMEVMHERNAHNFPLDLATVESTPVALQAPAIG
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Q7U669
C1EYK0
KDPB_BACC3
Potassium-translocating ATPase B chain
Bacillus cereus group
MMRPIVVKEKQIHVVEDEVRQAKTMDRDIVKHAMKQSFAKLNPKVMIKNPIMFVVEIGFIITFILSFLPSHSSSVPGWFNITVSLILLFTVLFANFAEALAEGRGKAQADSLKQSKKDVFANVVKENGDIVQVSATDLRKGDLVIVKQGEMIPSDGEVIKGLASVDESAITGESAPVIKEAGGDFCSVTGGTMVVSDEITIVITSNPGESFIDKMISLVEGAARQKTPNEIALNTVLTSLTLIFLIVVVTLPIFTNYLGFQIDTAVLVALLVCLIPTTIGGLLSAIGIAGMDRVTKFNVLAMSGKAVEAAGDINTIILDKTGTITFGNRMAHTLLPVGNETIEQVGKWAAISSVLDETPEGRSVIEYVKTKSISYNREIAEQGEFVPFKAETRMSGVDLQDGTKVRKGAVGSVIEWVRSQGGTIPKDVNQKADFISKEGGTPLVVAVDNRIYGLIYLKDTVKPGMRERFEQLRQMGIKTVMCTGDNPLTAATIAKEAGVDEFVAECKPEDKIAVIKAEQDKGKLVAMTGDGTNDAPALAQADVGLAMNSGTTAAKEAANMIDLDSNPTKIIEVVGIGKQLLMTRGALTTFSIANDIAKYFAIIPAMFTLAIPQMEALNIMKLTSPLSAILSALIFNAVIIPLLIPLAMKGIAYKPMSSNALLGRNLLIYGLGGVIVPFIGIKVIDIIVGLFI
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
C1EYK0
P0CQ91
MAK5_CRYNB
ATP-dependent RNA helicase MAK5
Cryptococcus neoformans species complex
MAKIDKKTKLKLNKKSVRAPSKPTTEKKPKKYVTADTLTWKPVKTSSFSGIDGGGGMMMLEELEDVGIEWEETDGGRKIAKFVEVESKTSKGKKNAAQEEPNQEGRGDDEKASSASETEEGKKADDKEAVEEDDEEEFPDFAGFAEEDLNAADEEEHPNLDDEPAFNDDLLPEWSSISLHPSLKRSFLASSFTAPTAIQSRAIPAGITGRDVVGVAETGSGKTLAYSLPILHYLLGQRKSKAGIKRPLSALVLCPTRELALQVMDHLNALLKHALATPDGEKPQGPPRVSVGSVVGGLSAQKQKRILERGCDVIVATPGRLWDLIKADDELATSVRTLRFLVIDEADRMIENGHFAELESIVKLTQRSTAQQGPDDDDPVFQAMATLFEESTAREDMQTFVFSATLSKDLQKNLKRRSRSWKGKGKRSSTLEDLVEKLDFRDENPEVIDLSPEGGVVSSLRESMIESTKDDKDLYLYYFLLRYPGRSIVFVNSIDSIRRLLPLLTLLQLPVFPLHSHLQQKQRLKNLDRFKSNPKGILIATDVAARGLDIPQVDHVVHFNLPRTADAYIHRSGRTARAQNEGFALQLVSPDEKSVQRALMKSLERTHELPDLPIEAGFLPSLRERLRVATEIEKAQHRATKATHDKNWLLEAAEAMDIDIDPSMLDGEDDDPDAPYYKPKKQDRGKGKASVENLKMELKALLQEKLVARGVSIRYPTSGSKVIVDDLIKSTGHGMLLGASTSKAYDQVEKTGKRKLGSGRPGAVKKKKVEGR
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
P0CQ91
P44679
YBGC_HAEIN
Acyl-CoA thioesterase YbgC
Haemophilus
MLDNGFSFPVRVYYEDTDAGGVVYHARYLHFFERARTEYLRTLNFTQQTLLEEQQLAFVVKTLAIDYCVAAKLDDLLMVETEVSEVKGATILFEQRLMRNTLMLSKATVKVACVDLGKMKPVAFPKEVKAAFHHLK
Displays acyl-CoA thioesterase activity with short chain aliphatic acyl-CoA thioesters, such as propionyl-CoA and butyryl-CoA. Enzyme activity is relatively low, suggesting that the acyl-CoA thioesters used in the assays are not the physiological substrates. Has no detectable activity with 4-hydroxybenzoyl-CoA, lauroyl-CoA (C12:0), arachidoyl-CoA (C20:0) and arachidonoyl-CoA (C20:4).
P44679
A0A3B7TLV2
BLN06_BRELC
RxLR effector protein BLN06
Bremia
MTLLHCWLLLVGHLASTAYADFITKDFKSLPPPAYDTNATQALVPYNAALEERNGPSSSTALLQYIDHKPGLMKKLLAGLSIRFAPPTMKVISTPTDMLRIDKIKNNIIKSSQWKRWARSLLEQNSMQNSHVIITKKMMDDLKPTNFFLVLLEASKDKNTKAVAKILEETQFARWCTIEHESISPMEFYDVLQLNLNEPIAYMERLPVLLRYWKYYKSVHSPMSSVATPKDIIDKQTVNRFGPYWKHTGEIAELLRLDFDSDSFFNHPARNVWLDLMKTYLDDTKTAEPLMIKTFQLLGNAAAKNLQNNVYSPIHFAERWIQANLQPIDVVTILGLDIHDSNLATNSAFSFLKVFIEKFLVNHPEADTTVVKIFSRLGSDESEKALALRKSFVSFFLRTPKFTPKTVMSIFDLTISADYVEKNPVWAIWMEYVNVYLVKNKVCPEGPLADTLEFLGSTAAADGVVRKKSIELLYSSWSGKTSQDTRIKQFLTAAARLNQLEL
Secreted effector that triggers a robust hypersensitive response (HR) in Lactuca serriola LS102. The response to BLN06 was visible as chlorosis but not as strong necrosis.
A0A3B7TLV2
B7NL82
MDTG_ECO7I
Multidrug resistance protein MdtG
Escherichia
MSPCENDPPINWKRNLIVAWLGCFLTGAAFSLVMPFLPLYVEQLGVTGHSALNMWSGIVFSITFLFSAIASPFWGGLADRKGRKLMLLRSALGMGIVMVLMGLAQNIWQFLILRALLGLLGGFVPNANALIATQVPRNKSGWALGTLSTGGVSGALLGPMAGGLLADSYGLRPVFFITASVLILCFFVTLFCIREKFQPVSKKEMLHMREVVTSLKNPKLVLSLFVTTLIIQVATGSIAPILTLYVRELAGNVSNVAFISGMIASVPGVAALLSAPRLGKLGDRIGPEKILITALIFSVLLLIPMSYVQTPLQLGILRFLLGAADGALLPAVQTLLVYNSSNQIAGRIFSYNQSFRDIGNVTGPLMGAAISANYGFRAVFLVTAGVVLFNAVYSWNSLRRRRIPQVSN
Confers resistance to fosfomycin and deoxycholate.
B7NL82
B0SFT5
NUOB_LEPBA
NDH-1 subunit B
Leptospira
MGLTETLSKPGEMFGDMFQVATLDNVVQWGQSFSLWPYPFATACCGIEYMSTACADYDIARFGAERPSFSPRQADMILVLGTITYKMAPVLRQIYDQLAEPKFVISVGACASSGGMFHTYGVLQGVDRILPVDVYVPGCPPRPEAILDALVKLQKKVQSQGLEARRQEVMRKIEEINERNKPLVVA
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B0SFT5
O97143
PLK4_DROME
Serine/threonine-protein kinase SAK
Sophophora
MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRTSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSAPGALNVFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIREEFKQVHHKLPYEQTGLFGQASTGLAEPNWPGAAKSSAFCMEAGNVPNSKQASLKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFLKFRPTYNEDRINDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYDNLPSKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPSEGLKVYDRNGMLLSDYSCSESRSLIEHGNECFTHCVNISNALEVAQTKDNSCFPVTIGRRPITDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSLSTISSTRNTSDFGTNCSRSNMLAAHQNIPIKRINVPEIGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKGDDLPFPVRDRVGQIPNIQLKLKTAPLLGSGRKTDYNNAMTPKTTTPYYNRMLL
Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers.
O97143
A0B6D7
RFCL_METTP
Clamp loader large subunit
Methanothrix
MTSWAEKYRPKNLDGILGNAKAVSELRAWAMAWEKGRPEVKCLILYGPPGVGKTSAALALASEMDWDYIELNASDQRTAEIIKSIAGPASQVSTFSGRRRLVILDEADNLHGTYDRGGAAAILRVIKNATQPVILIANEYYNIEKPLRDACRGVQFRSIRAQTIASLLREICRSEGIECEPEAVMHIAAMSGGDLRSAINDLEAAARGLKHLRLEDVATSERDVKASIFRVLDSIFKGEDSRSALEATYQLDESPEDLIHWIDENLPIVYKDRELAKGFECLSRADIFLGRVRRRQNYTLWRYAAFLMTGGVRAVSSKVRRGYTQFRPPSLWKRLGQTRKARSVRDSAARKIAAHCHVSTSYARSELLNFVGALLRSKKTGAAVAASLGLNIEEIALLTGSSPTTKKVQKLFEDAQKIIEAEQIAMIDRGLKIVDREIEKPEDKAMKYASVSKEIVQEKRQRSLFDF
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
A0B6D7
P47323
OPPB_MYCGE
Oligopeptide transport system permease protein OppB
Mycoplasma
MFKYILKRLGLAVVAMFIVMSIVFFLVNATGNVPLSATSARDIAAVQAQLQEFGFNDPIIVRYFRYWAKLFSFQADALGIYYANPNQTIGEIVFARVPNTLYVVLISFLIGSLLGIFLGMVSGLNRGKFLDAAINVLVVLFVSIPSFVVGLGLLKLAGFLNLPPRFINFDDAFFSFDRFLLASIIPILSLVFYSSAAFTYRIRNEVVEVMNQDYIKTAKSKGLGMFAVARYHIFRNSIIPSIPLFVFGISGAFSGGFIIESLFGVQGVSRILIDSVQVNETNMVMFNILFIQGIPLLASVFIEFIYVLVDPRIRIANSSNVSLLTKLKFLSSRHQWLMKWNKINSDNAQNIVFNSPLHHQLLELNAIDYKTKTVQLTTEQKTALNISATANFILLGNKCLKLKTIHG
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
P47323
Q1GPB2
RS14_SPHAL
30S ribosomal protein S14
Sphingopyxis
MAKLSSVNKNERRKKLVKKYAGRYAKLKAIAADSSLDDGERLIARLKMAEIPRNGNPTRIRNRCELTGRPRAYYRKFRLCRVQLRDLANKGLIPGVVKSSW
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.
Q1GPB2
Q7V479
RL11_PROMM
50S ribosomal protein L11
Prochlorococcus
MAKKVVSVIKLALQAGKANPAPPVGPALGQHGVNIMAFCKEYNARTQDKAGLVIPVEISVFEDRSFTFITKTPPASVLITKAAGIEKGSGESAHGKVGSLSRSQLEEIAKTKLPDLNCTSIESAMRIIEGTARNMGVSISD
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q7V479
Q7V8E7
MEND_PROMM
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
Prochlorococcus
MGLRHLVLCPGSRSGPLALAAGGMARTNRLRLSTAIDERSAAFLALGFSTATGTAAAVVTTSGTAVANLLPAAVEADRSCQPLLLLTADRPYRLKDCGANQTVNQETFLSPACRWIGQGPREGLHLFSKETLESFAEKAWQRAHHPAGAVHLNLPFEEPLHLSEEEQRMIWKGWSPKIPRSSPIKPINLAMAAEGTNGVTDQAPFALDPLRPGVVIAGAWRGLSKDLFAFQQSLREWQALSGWPVLADPLSALPSDQPGLIRSWELLLATGLLGSQEQLQVLRLGPMSASRSLEAWLKSFGDGQLLITEGDSRCLDPLGLSVQWNHGLTSWWQHHHHRWIDADAASQQATKALLRKWQISDRFAQEWLDQQLPLQGAITEPALARWLSRLLPTELPIMLAASSPVRDWLAYADKSLFSRRCFSFRGASGIDGTLSLSMGLAMALGPTLLVSGDLALLHDSNGWLLAHPQRPPLVVVLIDNGGGGIFEQLLVKTAPSEAFEQLFAMPQEVDPLALAGAHNIPHRQVACLEDLPAALEWGLFQAGPVLIRVCTHRRQDSSMRQQLREGLMMHLQSISQNGHIDL
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Q7V8E7
Q82DQ9
RL11_STRAW
50S ribosomal protein L11
Streptomyces
MPPKKKKVTGLIKLQIQAGAANPAPPVGPALGQHGVNIMEFCKAYNAATESQRGWVIPVEITVYEDRSFTFITKTPPAAKMILKAAGVEKGSGEPHKTKVAKITQAQVREIATTKLPDLNANDLDAASKIIAGTARSMGITVEG
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q82DQ9
A7STV9
SLX1_NEMVE
Structure-specific endonuclease subunit SLX1 homolog
Nematostella
MDDNIAGSGFHGVYLLYCVNPKFKGHTYIGYTVNPNRRIKQHNGGVDKGGAYKTSRKKPWNMILIVHGFPNDIIALQFEWAWQKPTVSRRLKSAATKKKPRERPVQYCFRILSELLRVGPWNRLPLHIRWLMREYEMEFDPRCLPPFHMTVVYGPLVSRKAKQKAVSSEDQRPDHKEKCIKCLDVIKIDEKLIRCPKSGCTMTAHMFCLARDFLHCGNEGGLFCLPVDGNCPQCKGSLLWGDLVKPAESIPSAEDVDEDTDDHWTQGLRL
Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
A7STV9
B9JC66
SSRP_AGRRK
Small protein B
Agrobacterium tumefaciens complex
MAPKGSQRVVKKIVAENRKARFNYEIIDTYEAGIVLMGTEVKSLREGKANIAESYASDEDGEIWLINSYLPEYLQANRFNHEPRRRRKLLLSGREIGRLRSGINREGMTLIPLKIYFNDNGRAKLELALAKGKKLHDKRQSEKERDWNRQKGRILKDNR
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
B9JC66
A5VS65
EFP_BRUO2
Elongation factor P
Brucella
MKINGNEIRPGNVIEHEGGLWVAVKTNAVKPGKGGAYNQVELKNLINGTKLNERFRAAETVERVRLEQKDFSFLYEQGEALIFMDTETYEQLELQKDFVGDRAAFLQDGMMVTVELYEEKPIGIRLPDQVTLAITEADPVVKGQTAASSYKPAVLENGIRIPVPPFITSGERVIVDTNELTYISRA
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
A5VS65
A0KYB9
PLSX_SHESA
Phosphate-acyl-ACP acyltransferase
Shewanella
MTSLTLALDAMGGDHGPHVTVPAALRALKSHSSLKIILVGDKTEIDVYLRQAEQPLLSRIEVIHTDEVVSMSDRPVHALRTRKNSSMRLSIELVRDGRAAACVSAGNTGALMAMAKVLLKTLPGVDRPALVSCLPSVTQKPVYLLDLGANISCDSETLFQFAVMGSVLCEAVDKKSRPKVALLNVGTEEIKGNDQVQQAAQILQNTDQINYTGFIEGDEIYLGNVDVIVCDGFVGNITLKTSEGIAKLLVHQLKRGLTQGFFVRFLAKLIAPRIQAVLSQMNPDHYNGASLIGLRGIVVKSHGNADETAYLQAISLAVTEAQRRLPEMIKDRLESILLDINN
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
A0KYB9
Q7MVY0
HCP_PORGI
Prismane protein
Porphyromonas
MEKKMFCYQCQETAGNKGCILKGVCGKDFSTANLMDLLVFNLKGIAIIMTSMRRAGVKADYRKADKAIMESLFATITNANFDYSSIAKRVEKTFALKAELYSLAFTQGIELPENEAVTMQGKPEEYDRLALSVGILRETDEDVRSLKELTIYGLKGLAAYAEHADRLGYVDEEINAFTERALHDVTMGLLSAEELTALVLETGSFGVKVMALLDKANTETYGNPEITEVNIGVGSRPGILISGHDLKDMEMLLEQTEGTGIDVYTHGEMLPANYYPKFKKYNHFFGNYGNAWWKQREEFETFNGPILFTTNCIVPPKANASYKDRVFTTNATGYPGFKYIESDQHGRKDFSEIIALAKTCQPPTEIESGTIIGGFAHHQVLSIADKVVEAVSSGAIRKFVVMSGCDGRQSGRNYYTEFAEALPSDTVILTSGCAKFRYNKLQLGDIGGIPRVLDAGQCNDSYSLAVIALKLKEVMGLDDINKLPIVYNIAWYEQKAVIVLLALLSLGVKNIHVGPTLPAFLSPNVAKVLIENFGIAGIGTVEEDIRTLIA
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Q7MVY0
Q4KD86
KATG_PSEF5
Peroxidase/catalase
Pseudomonas
MSNESKCPFKHTAGEGTSNRDWWPGQLNLKILHQHSRLSDPMAEGFDYAAEFKTLDLAAVKRDLQALMTDSQPWWPADFGHYGPLFIRMAWHSAGTYRIADGRGGAGGGQQRFAPLNSWPDNVSLDKARRLIWPIKQKYGRKISWADLIILTGNVALESMGFKTFGFAGGRQDVWEPEDNVYWGSETTWLDDQRYSGDRELENPLGAVQMGLIYVNPEGPNGNPDPLAAARDIRETFARMAMDDEETVALIAGGHTFGKTHGAGPATHVGPEPEAAGLEEQGLGWKSSFGTGVGGDAITSGLEVIWTTTPTRWSNDFFDHLFGYEWELTTSPAGAHQWRPKAGAGADSVPDPHDPNKRRTPSMLTTDLSLRFDPAYEAISRRFHEHPEQLAEAFSRAWFKLTHRDMGPRARYLGPEVPAEELIWQDPIPAVNHPLIDAQDIQQLKGQILNSGLSVAQLVSTAWASASTFRGSDKRGGANGARIRLAPQKDWEVNQPQQLAQVLQGLEALQSAFNSAQSTGKRVSLADLIVLGGCAAVELAAKNAGYSISVPFAPGRMDASQEQTDVESFAVLEPVADGFRNYLKPVSGITAEALLVDRAQLLTLTAPQLTVLLGGLRVLGANVGQSPHGVFTSRPGTLSNDFFVNLLDMGTQWKPQSEARDLYEGSDRATGQYKWSGTRVDLLLGSNSQLRALAEVYAAADAGEQFVKDFVAAWDKVMNLDRFDLR
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Q4KD86
Q8CEK7
FATE1_MOUSE
Fetal and adult testis-expressed transcript protein homolog
Mus
MPWVPREHSHDDVQLQEFSRNFPVGRFPYECLEADIMAKIGLEELNGLEMEVMRRQMQMTSGRLHILEDQDATWCHKEAALFTLLVSVCIANLWLWVHW
Involved in the regulation of endoplasmic reticulum (ER)-mitochondria coupling. Negatively regulates the ER-mitochondria distance and Ca(2+) transfer from ER to mitochondria possibly implicating it in the regulation of apoptosis. May collaborate with RNF183 to restrain BIK protein levels thus regulating apoptotic signaling.
Q8CEK7
P85966
AMP_TRIKH
Antimicrobial peptide 1a
Triticum
MKPHMSATVLRAPRVAAILLAVVLAAVLATAVNGAQRCGDQARGAKCPNCLCCGKYGFCGSGDAYCGAGSCQSQCRGCRDDVVGQALPAEPGSTRATAASSASARGLNLTATTGGP
Has antifungal activity against F.verticillioides (IC(50)=2.7 ug/ml). At concentrations between 45 uM and 225 uM, inhibits activity of metalloproteinase fungalysin Fv-cpm from F.verticillioides.
P85966
A5F619
PYRH_VIBC3
Uridine monophosphate kinase
Vibrio
MTTNPKPAYQRILLKLSGEALQGSEGFGIDPTVLDRMAQEVKELVELGVQVGVVIGGGNLFRGAGLAKAGMNRVVGDHMGMLATVMNGLAMRDALHRAYVNARLMSAIPLNGVCDDYSWSDAIRELRQGRVVIFAAGTGNPFFTTDSAACLRGIEIEADVVLKATKVDGVYSADPVANPDAQLYDKLAYNDVLEKELKVMDLAAFTLARDHKMPIRVFNMNKPGALRRVVMGEAEGTLISDVQ
Catalyzes the reversible phosphorylation of UMP to UDP.
A5F619
O15697
DRC4_TRYBR
T lymphocyte-triggering factor
Trypanosoma
MPPRTAAERGGRRKSVKAPPPVDPLVELTTLESVHDALAKAERLRNYFQVERDKVNDFWTITKGEVETYRNRLFNAEASIEELERSHQVEMKVYKQRVRHLIYERKKKAQACQDESDRLLREAEDRHLQRMNEIQAKLQQQDQQLRAAAADHEMNVYEKRDSHSYMVTVTKTQSHEKELARLQVSCEAKLKVLRDELELRRRAEIHEIEERKNEHINALIKQHEEKFHEMKTYYNQITTNNLEIIHSLKEEIAQMKQNDEHNETLMYDIDRENQNLVAPLEEAQREVAELQQKRKQNEQNKRGLEVTRVKLRSLREEIRRQREEHQALEERYACVHREREELKGKFESALRQAVMVVEERNEVLQQKLIESHALVEERDVQLEGVLRAMNLEPKTLELIATEVDEWLQRKNQLIKDLHFELKKGEKLYSATLLEMERRCQTANIASLPRSNFE
Cytoskeletal linker that plays a central role in the flagellum cell motility. Required for directional cell motility. Plays a role as part of a dynein regulatory system that regulates flagellar beat in response to signals from the central pair apparatus and radial spokes in procyclic cells. Also plays an essential role in the bloodstream form of the trypanosomes as its silencing is lethal for the circulating form.
O15697
A7Z4W5
RECA_BACVZ
Recombinase A
Bacillus amyloliquefaciens group
MSDRQAALDMALKQIEKQFGKGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQEKGGQAAFIDAEHALDPVYAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTRIKVVKNKVAPPFRTAEVDIMYGEGISKEGEIIDLGTELDIVQKSGSWYSYEEERLGQGRENAKQFLKENKDIMLMIQEQIREYYGLDNNGVTDKAEEVQEEMELEE
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.
A7Z4W5
A7N6I9
CYOE2_VIBC1
Heme O synthase 2
Vibrio
MSKEIALPLESGKKKIGSTYLKLTKPKVVALMLITAVVGMSLAPVVDFPWLQAAFGLVGIGLMAGSAAAFNHLIDRRIDARMARTHKRPLPSGDTNPISVAIFSTALGVIGFVLLYALVNPLTAWMTFLSLLGYAVVYTMYLKRATPQNIVIAGIAGAMPPLLGWTAVTGELHAHAWLLVMIIFIWTPPHFWAIAIHRVEDYRKVDIPMLPVTHGIEYTKTSILLYTILLTLVCILPVLVGMVGSVYLFSSLLLNAGFMYHAWKLKLSPEQNSAMETFKFSIYHLLALFVALLADHYLGLFFTP
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
A7N6I9
O35162
HSP13_RAT
Stress-70 protein chaperone microsome-associated 60 kDa protein
Rattus
MAGEMTILGSAVLTLLLAGYLAQQYLPLPTPKVIGIDLGTTYCSVGVFFPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEELEAEIGRYPFKVLHKNGMAEFSVTSNETIIVSPEYVGSRLLLKLKEMAEKYLGMPVANAVISVPAEFDLQQRNSTIQAANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKEIYQTYGFLPSRKEEIHRLRQAVEMVKLNLTLHQSAQVSVLLTVEENDSQKPQNADSKLPEDQLTPGDGHHVNRVFRPGLSDSTSGKSQVLFETEVSRKLFNTLNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAIQAGIDGGSWPLQVSALEIPNKHLQKTNFN
Has peptide-independent ATPase activity.
O35162
Q71ZG6
SYA_LISMF
Alanyl-tRNA synthetase
Listeria
MKQLSSAEVRQLFLDFFKEKGHTIEPSAPLVPNNDPTILWINSGVATMKKYFDGSVIPDNPRMANAQKSIRTNDIENVGKTARHHTFFEMLGNFSIGDYFKEGAIVFAWEFLTSPKWIGFDPDKLYVTVYPEDEEAKTLWREKIGLSDDHIVEIEDNFWDIGIGPSGPDSEIFYDRGPAFGDDASDPELYPGGENERYLEIWNLVFSQFNHNPDGTYTPLPKQNIDTGMGLERMVSIIQDAPTNFETDLFMPIIREVEQIAGVKYGHSQENDVAFKVIADHIRTVAFAIGDGALPSNEGRGYILRRLLRRAVRYAKVLTINEPFMYKLVPVVGKIMNSFYPEVENQTDFIQKVIRTEEERFHETLNEGLAILETILKTAKETNEQIIKGADIFKLYDTFGFPVELTEEYAEDHGLKVDHAGFEAEMKEQRDRARSARADVKSMQVQGELLANLTEKSAFVGYNSTEHVSEILYLIQDDTLVEEVAAGSEAQVIFKETPFYAESGGQVADKGTIESETGLAYVEDVQKAPNKQNLHRISVKEGVLKTGDTVKLAVDKVKRRETIKNHTATHLLHRALKDTLGEHVNQAGSLVSPDRLRFDFSHFGQITEEELTKLEEIVNEKIWEQINVVIEEMPIAEAKELGAMALFGEKYGDIVRVVQVGKYSIELCGGVHVRNTADIGLFKIVSETGIGAGTRRIEAVTGKEAYRFVTEQENTLKQAASLLKTTTKETPQKVEQLQADLREVKRENESLLSKLASAASADIFESPEEIGGVKVIAKQVNAKDMNQLRQFVDNWKDKKIGGILVLGAVQGDKVNLISAVSEEAIKAGYHAGKLLKEVATRCGGNGGGRPDMAQAGGKNPAELGTALDYVSTWVKEQQA
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Q71ZG6
P32335
MSS51_YEAST
Mitochondrial splicing suppressor protein 51
Saccharomyces
MTVLYAPSGATQLYFHLLRKSPHNRLVVSHQTRRHLMGFVRNALGLDPPPSPEDPTPENRFHPWDQSPSVDLRERAAKIRTLAHCPVTGKDINYTCPLSGIPTHHSREAWEMDKAYHDSKKYEILKKVNIYEHDLRSGRPFPEFDFPQQQGYDKAVNLTNWDLFFYTRSFYSMDTEFQLAAVTKMLSYPITIGSLLHKFSPYSLNPKGPITLEGLKSLAALRYTLYPLENRSLPTTTKNRAMRIFILGARAEAQLPGHVWKQLQFLFPEQSFEIHFIGPECLYKRDKQEYVKSTTPVVQRVDETLKFIYRTNFFEVFHEAQDFFPYDPYMDVFFTFHPGYASPESHGSWMGETMKALLETKCAIFTTGFNKKDLTDDINLVKSKYGKEMDVLMEPVRNVFGSTKWELNDMNPQEVYQFNMYIAGFRGKRYHTIKRQ
Has a dual role in the assembly of cytochrome oxidase subunit 1 (COX1). It has a regulative function on COX1 synthesis, acting as a translational activator specific for the COX1 mRNA, and it also binds to newly synthesized COX1 protein. Together with COX14, may act as a chaperone that binds efficiently unassembled COX1 and prevents it from unproductive aggregation. When bound to COX1, MSS51 is unable to interact with the COX1 mRNA and translation is halted. This may be a feedback control that ensures that COX1 is only produced as long as potentially harmful assembly intermediates are not accumulating.
P32335
Q9I2N4
MODC_PSEAE
Molybdenum import ATP-binding protein ModC
Pseudomonas
MDGLRLRFRRAYPGFELDIDLALPGRGVTALFGHSGSGKSTCLRCIAGLEKAAEGEVTINGETWQDSRRNLFVAPHRRALGYVFQDANLFRHLTVRRNLAFGLKRIAAAERRVELEQACALLGIEHLLERMPERLSGGEQQRVGIARALLTSPRLLLMDEPLASLDLKRKGEILPYLERLHEELDIPVLYVSHSPDEVARLADHLVLLENGKVRASGPIGETLARVDLPLALDDDAGVVIEGTVSDHDPAYGLLTLVLPGSALQMRVAHAPLAPGKRLRFKVQARDVSLNLRDDAQSSILNRLPVRVLELVDTDTAAHVLVRLDAGGNPLLARITRYSRDQLQLRPGQLLWAQIKSVAVLA
Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Q9I2N4
B8GPP4
SYP_THISH
Prolyl-tRNA synthetase
Thioalkalivibrio
MRATRFPLATLKETPADAEVISHQLMLRAGMIRRLASGLYSWTPLGLRVLRKVEGLVRDEMDRAGALELLMPAVQPAELWQESGRWEQYGPELLRLKDRHMREFCFGPTHEEVITDYVRREVKSYRQLPVNYYQIQTKFRDEIRPRFGVMRAREFLMKDAYSFHVDEDSLKETYARMHEAYTRIFTRCGLDFRAVLADTGSIGGNASHEFHVLADSGEDAIAFSDVSDYAANVELAEAVAPATERAAPGEAMRLVDTPNARTIADLVEQHGLAIEKTVKTLVVAAAEGAEAPLIALLVRGDHELNAIKAEKLPQVASPLRMATEEEIRAAIGAGPGSLGPVNLPIPCVVDRAVALMSDFGAGANIDGKHYFGINWERDLALPPVADLRNVVAGDPSPDGQGSLQIRRGIEVGHIFQLGRKYSEAMGATVLDEQGRSLVVTMGCYGIGVSRVVAAAIEQNHDAQGIIWPEALAPFTVALCPINAQKSQRLREAADALYERLLNAGFEVFYDDRGLRPGAMFADMELIGIPHRLVLGERGLDAGEIEYKGRRDTDTTQVALDGVLDFLRQRMNAAH
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
B8GPP4
Q5ZSY2
KUP3_LEGPH
Probable potassium transport system protein kup 3
Legionella
MPSTRNIETHNDSNPTLRALSLSALGIVYGDIGTSPLYTFKTVILLAGGGTPAVNTIMGSVSLIIWTLIIIASVKYIHFALRIDNDGEGGILALMSLLSLKLKQRPFIIAVGLMGAALIYGDGTITPAISVLSAVEGLEILSPSLKYYVLPIAITILITLFAIQSKGTATIGKAFGPVMAFWFLTIGILGARGVIQHPSVLAAINPIYGLSFLFSNGATGFFILCGVFLCVTGAEALYADLGHFGTAPIRCAWFGLAFPSLIFNYLGQAALVLEGASTEHNIFYMLCPGDFLLPLIILSTVATIIASQAIITGAFSMTRQAMQLGWLPRLRVTQTSSEGYGQIYIGVVNWLLMLATLGLTIGFGSSEKLAAAYGIAVSATMLCTTLLLFIALHKLWKWDIITSGLVAGLFMIVDASFFAANLTKFINGGYIPITLAIIIYSMMYIWHKGYQTIAIKQKEKNITVASFLDSIQKERVVRVPKTAVFLTSKEQDIPPILVWHVKKNHVLQDKVIILKINNLSIPRCKPGDRLQIVETGTGIWHAVANYGFMEQPHIPKLLKKLEAQGYDINIKDITYYIGHETIFVRNVRHTLSKYIKILFVFMHRNALPMSNYFHLPPESVFEIGRQIEI
Transport of potassium into the cell.
Q5ZSY2
Q9RQ80
ATPG_BUCDN
F-ATPase gamma subunit
Buchnera
MASIKEIKTQITSVVNTKKITKAMEMVAISKMRKTEERMSSGRPYSEIIRKVINHVAQGHLEYKHSYLETRKIKRIGLIIVSSDRGLCGSLNSNLFRKVLFKIQNFTQKNIPCDLILFGLKSLPVFKLCENNILSKITHLGEHPNILKVINGIDVLLKKYQIKRIDKIFIAYNEFHNKMSQYPKIIQLLPLSRIKSETISTKRWDYLYESESKLIIDSLFKRYIESQVYQSILENIASEHAARMMAMKTATENSTERIKELKLLYNKVRQATITQELTEIIAGASAVSTG
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Q9RQ80
A2QX23
ADAB_ASPNC
2-acetyl-2-decarboxamidoanthrotainin biosynthesis cluster protein B
Aspergillus subgen. Circumdati
MAFRIPFAQSFWQEYLSGQEANLPRLPEVEQVTETVMRILGGNPGRMQLQGTNTYLVGTGKFRILIDTGQGEASWIEALTKQLEANGLEISHVLLTHWHGDHTGGVPDLITYNPELSSRVYKNTPDLGQQAIHDGQKFHVEGATIRAVFTPGHAFDHMCFLLEEENALFTGDNVLGHGYSVVEDLGTYMTSLTRMADLNCALGYPAHGTRIEDLPAKMKEYIQHKESRMRQVLAALERSRARMTATGGGRRAGALTFPELINSMYGGIPDEIEQALTPFLSQVLWKLAEDRKVGFEGEPSQRRWFAVGPPAATAVRL
Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist . The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA . The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB . Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 .
A2QX23
A5EP16
GFA_BRASB
S-(hydroxymethyl)glutathione synthase
unclassified Bradyrhizobium
MTVHIHPYVDNGVKQGSGHFAGGTLVCKCHDRPVKVAVKGDVAHNHACGCTKCWKPSGATFSVIAVVPRQNVTVLENGDKLKIVDPSAVIQRYACTGCGTHMYGRIENTGHPFYGLDFIHPELFQEQGSAAPAFAAFVSSVIESGVKPEQMGEIRARLKELGLEPYDCLSPALMDAIATHVAKAKAA
Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.
A5EP16
P18405
S5A1_HUMAN
Steroid 5-alpha-reductase 1
Homo
MATATGVAEERLLAALAYLQCAVGCAVFARNRQTNSVYGRHALPSHRLRVPARAAWVVQELPSLALPLYQYASESAPRLRSAPNCILLAMFLVHYGHRCLIYPFLMRGGKPMPLLACTMAIMFCTCNGYLQSRYLSHCAVYADDWVTDPRFLIGFGLWLTGMLINIHSDHILRNLRKPGDTGYKIPRGGLFEYVTAANYFGEIMEWCGYALASWSVQGAAFAFFTFCFLSGRAKEHHEWYLRKFEEYPKFRKIIIPFLF
Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
P18405
Q04F85
RRF_OENOB
Ribosome-releasing factor
Oenococcus
MIDLKEVKERMGKVSKAFQNELINIRAGRANPNILNKIQVEYYGAPTPLNQLASVQIPEARVLLITPYDKTSLKAIEQAIFASDLGLTPQNDGSAIRLIIPQLTEDSRKELVKQVKAEAEKAKVAARNTRHDFMSDLKKDNDLSEDSRHRTEDDIQKATDLEIKDIDRIADIKEKELMEI
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Q04F85
Q6H500
RSBZ4_ORYSJ
bZIP transcription factor 15
Oryza sativa
MDIEAFIHGGSGGGDADADHPLGIFSAADLSGFGFADSSTITGGIPNHIWPQSQNLNARHPAVSTTIESQSSICAAASPTSATNLNMKESQTLGGTSGSDSESESLLDIEGGPCEQSTNPLDVKRVRRMVSNRESARRSRKRKQAHLADLESQVDQLRGENASLFKQLTDANQQFTTSVTDNRILKSDVEALRVKVKMAEDMVARGALSCGLGHLGGLSPALNPRQACRVPDVLAGLDYAGDDPFTAGLSQPEQLQMPGGEVVDAWGWDNHPNGGMSK
Probable transcription factor that binds to the DNA specific sequence 5'-TGAGTCA-3' found in seed storage protein gene promoters.
Q6H500
F1MH24
AAK1_BOVIN
Adaptor-associated kinase 1
Bos
MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINSVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKVITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPTKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKTQPPPSQPLPQSQPKQPQAPPTSQQPPSAPAQALPTQAQATPQHQQQLFLKQQQQQQTAPPAQQPAGTFYQQPQQQAQAPQFQAVHPAAQQPVIAQFPVVSQGSSQQQLIQNFYQQQQQQQQLATALHQQQLLTQQAALQQKTTAAAAPQPQAQPAAAASPAPAQEPAQIQAPVRQQPKVQTTPPPTIQGQKLGSLTPPSSPKAQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRASQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKYPEKLGGSAESLIPGFQPTQGDAFAASSFSAGTAEKRKGGQTMDSSLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLIDCSLLSNPTTDLLEEFAPIAISAPAHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL
Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Preferentially, may phosphorylate substrates on threonine residues. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity.
F1MH24
Q5VCS6
TDRD5_MOUSE
Tudor domain-containing protein 5
Mus
MSEQERIQDCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDESTKGIASLVAKQRRSHKVRNSMPKGRPSICSGRVPYRGRVPPILPAVVKSELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTLKKSVSEDKQRGWPAGKVFTQPFRMKQQGSYSTGFPVMKAHFSQPISNMEPPKQVLSMAKTPTFNSVEASRLNHTEKLNQLESTFKSVIAQIGPGGTVDPELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLLVFDADLKPLPSGGPLSSVRNSCLVQPDKKTEANPWTSSLSRNSLSTVAVKKTTWDCPLKNQKEPEQKIYKKPNLVVKPLQLQVETNKPQLSLSVANHDIPPDAVRAKKLCRLPPLDTSTLVGVFVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAEEHWTARAILHFQKLCGLKPLVGVVDEYIDGILNIFLCDTSSNEDVYFHHVLRTEGHAIVCRENAPSKGFRDFNPPALYTNASSAGDMVLTDLGHPAQQHYLNEDQEILQQAQQDINDGKCISYLKSAPKELLKDSKLSSLKTHKSCEEDPRWSILQPKDLKEENEDEVPTGMPCLESVTIGDDVWDENWLPLQAKMGKAGSPASQLFTSNLVGKKQYQTGGEMAQKDWCFSTSKDIWDDSWQPLGLANDVKGGIHTPEGPIAQEKNTSTTRIQQQPDLQYPLDSSTLPKLEEFYISLIKSQQSAERSQSEPASIQTHAGRAASKALSSTPAVGDSPENHSGSVESSPGSLKKEDVSNSRAEATAKDKSQGAIDQLSFILSPQHQISQKLYIPRSTATAVLGAAARLATSRSLLHWYPSVKGGKLEAERDGVK
Required during spermiogenesis to participate in the repression transposable elements and prevent their mobilization, which is essential for the germline integrity. Probably acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for chromatoid body (CB) assembly.
Q5VCS6
Q2S9Z8
LPXC_HAHCH
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Hahella
MIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGVVFCRTDLDPIVEIPARAENVGETLLSTTLVKSGVKIATVEHLLSALAGLGIDNCYVELSAAEVPIMDGSAGPFVFLIQSAGIAEQDAPKKFIRIKREVTVTDEDKRATFVPFDGFKVTFSIDFDHPVIKGRSQETVIDFSSTSFVKEVSRARTFGFMRDIEKLRAMNLALGGSMDNVIVVDDFKILNEDGLRYEDEFVKHKVLDAIGDLYLLGNSLIGEFKGHKSGHGLNNKLLRELLSQKDAWEVVTFEDAGEAPISYLKPVLA
Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Q2S9Z8
B9LA36
MSRA_NAUPA
Peptide-methionine (S)-S-oxide reductase
Nautilia
MPKAVFGGGCFWCLDAVFRKVDGVRDVVVGYAGGRRPNPNYEQVCTGVTGHAEVVEIDYDENTVSYDELLDIFFKIHDPTQLNRQGNDVGTQYRSIILYLDEEQKEKALKKIEELKKEGLNVVTEVKPLEIFYPAEKYHQNYFAKNPHQPYCMYVVAPKVEKYLKIKNENKKT
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
B9LA36
P59489
GREA_BUCBP
Transcript cleavage factor GreA
Buchnera
MNDQIPMTILGVEKLRKELEMLKTIKRPKIIKSIIEARQHGDLKENSEYHAAREEQGFCEGRIKEIELKLSKARIIDITKVKNNGVIIFGSTVTILNLTSNQEFTYRIVGDDESNFKRKLISINSPMSRGLVGKKVSDVATIKTPVGDVKYKILKIEYN
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.
P59489
Q6LU34
CHEB1_PHOPR
Protein-glutamate methylesterase/protein-glutamine glutaminase 1
Photobacterium
MVVDDSAVVRQVVSSVLKSDSEIEVCGAVADPLFAMTRMRMQWPDVIVLDIEMPRMDGISFLKKIMAERPTPVVICSTLTEKGADTTMQAISAGAVEIITKPKVGLKGFLHDSAKVLINAVKAASRANLKPLQRAMASNLKVTPKLSADAVLAEGNTSRLKTTEQLVAIGTSTGGTQALELVLKALPRVSPGIVIVQHMPEKFTAAFAERLDSLCEISVKEAKHKMRVLPGQALIAPGGKHMLLKRSGAQYYVEVIDGPLVSRHRPSVDVLFRSVAQSASGNALGIIMTGMGDDGVKGMLEMRRAGAVTLAQDEASCVVYGMPKEAVKCGAVERSLSLSEIPQAILDCSH
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
Q6LU34
B1KD01
AROE_SHEWM
Shikimate dehydrogenase (NADP(+))
Shewanella
MTDRYAVFGNPISHSKSPLIHGIFANETQQVLDYEAILAPKDGFESCLKLFWSQNGKGANVTAPFKEQAFNLCDELSEEAKLAGAVNTLTLLTNGKVRGDNTDGLGLVADLIRNISSLEGKRVLLLGAGGAARGSVLPLLKAGLKVYIHNRTQEKAEKLVEIFTPFGDVKALSIAELIAPFDIIINSTSSSLSGDVPAIPSCVIGVESLCYDMMYSKEMTSFNSWALELGAVKAIDGLGMLVGQAAKSFELWRGVTPEVDTTIKLLREKIKSE
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
B1KD01
P75952
COMR_ECOLI
Copper outer membrane regulator
Escherichia
MATDSTQCVKKSRGRPKVFDRDAALDKAMKLFWQHGYEATSLADLVEATGAKAPTLYAEFTNKEGLFRAVLDRYIDRFAAKHEAQLFCEEKSVESALADYFAAIANCFTSKDTPAGCFMINNCTTLSPDSGDIANTLKSRHAMQERTLQQFLCQRQARGEIPPHCDVTHLAEFLNCIIQGMSISAREGASLEKLMQIAGTTLRLWPELVK
Represses expression of BhsA/ComC by binding to its promoter region in the absence of copper.
P75952
B1KRD4
SPEA_SHEWM
Biosynthetic arginine decarboxylase
Shewanella
MSNWSINDARTGYNVNYWSQGLYGISDEGEATVSPDPTRPECSIGLNELAKDMVKSGVNLPVLVRFPQILHHRVNSLCQAFNQAIQKYQYQADYLLVYPIKVNQQQTVVEEILASQVEKEVPQLGLEAGSKPELMAVLAMAQKASSVIICNGYKDIEYIRLALIGEKLGHKVYIVLEKLSELKTVLEESKKLGVTPRLGLRVRLAFQGKGKWQASGGEKSKFGLSASQVLTVIESLKSEEMLDSLQLLHFHLGSQIANIRDIRQGVSEAGRFYCELQKLGANVKCFDVGGGLAVDYDGTRSQSSSSMNYGLTEYANNIVSVLTDICNEYEQPMPRIISESGCYLTAHHAVLITDVIGTEAYKPEDIQPPAEDAPQLLHNMWHSWNEISGRADQRALIEIYHDCQSDLTEVHSLFALGQLSLTDRAWAEQVNLRVCHELQGVMSSKYRFHRPIIDELTEKLADKFFVNFSLFQSLPDAWGIDQVFPIMPLSGLDKAPERRAVMLDITCDSDGTIDQYVDGQGIETTLPVPAWSAESPYLIGFFLVGAYQEILGDMHNLFGDTNSAVIRLDDDGRTNIESVLAGDTVADVLRYVNLDAVSFMRTYEELVNKHIQEDERANILEELQLGLKGYTYLEDFS
Catalyzes the biosynthesis of agmatine from arginine.
B1KRD4
Q2KIY6
HORM1_BOVIN
HORMA domain-containing protein 1
Bos
MATAQLQRTSMSALIFPNKISTEQQSLVLVKRLLAVSVSCITYLRGIFPECAYGTRYLDDLCVKILREDKNCPGSTQLVKWMLGCYDALHKKYLRMVVLAVYTNPEDPQTISECYQFKFKYTSNGPVMDFTSKNQSNEPNMSSADTKKASILLIRKIYILMQNLGPLPNDVCLTMKLFYYDEVTPPDYQPPGFKDGDCEGVIFEGEPMYLNVGEVPTPFHTFKVKVTTERERMENIGSGILSPKQLKTPLQKILTDKDDLEDDQEHYISDEFDTETKMEEQEKNPGCSVRREAGFICEEDEMKSKGSPDFSISHSQVEQLVSKTSELDVSESKTRSGKIFQNKMANGNQQVKSKENRKRTQLESGKTVLHPFDSSSQESVPKRRKFSEPKERI
Plays a key role in meiotic progression. Regulates 3 different functions during meiosis: ensures that sufficient numbers of processed DNA double-strand breaks (DSBs) are available for successful homology search by increasing the steady-state numbers of single-stranded DSB ends. Promotes synaptonemal-complex formation independently of its role in homology search. Plays a key role in the male mid-pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes.
Q2KIY6
B5XUP9
RPPH_KLEP3
(Di)nucleoside polyphosphate hydrolase
Klebsiella
MIDDDGYRPNVGIVICNRQGQVMWARRYGQHSWQFPQGGINPGESAEQAMYRELFEEVGLSRKDVRILASTRNWLRYKLPKRLVRWDTKPVCIGQKQKWFLLQLIGNDADINMQTSSTPEFDGWRWVSYWYPVRQVVSFKRDVYRRVMKEFASVTMSLAESAPKPQSAPAYRRKRG
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
B5XUP9
B2UU54
ACKA_HELPS
Acetokinase
Helicobacter
MEILVLNLGSSSIKFKLFDMKENKPLASGLAEKIGEEIGQLKIKSHLHHNEQELKEKLVIKDHASGLLMIRENLTKMGIIKDFNQIDAIGHRVVQGGDKFHAPILVNEKVMQEIGKLSILAPLHNPANLAGIEFVQKAHPHIPQIAVFDTAFHATMPSYAYMYALPYELYEKYQIRRYGFHGTSHHYVAKEAAKFLNTAYEEFNAISLHLGNGSSAAAIQKGKSVDTSMGLTPLEGLIMGTRCGDIDPTVVEYIAQCADKSLEEVMKILNYESGLKGICGDNDARNIEARKEKGDKQAKLAFEMCAYRIKKYIGAYMAVLKKVDAIIFTAGLGENYSALRESVCEGLEDLGIALHKPTNDNPGNGLVDLSQPDAKVKVLLIPTDEELEIALQAKEIAEKLK
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
B2UU54
Q043X8
PRMA_LACGA
Ribosomal protein L11 methyltransferase
Lactobacillus
MKLLAVKVECSHELEDGLSFFMQDELDAQGIESRKRSDFVAEGQKHDSSLVELDDIENLPKDLELTAYFNYENADKKELVKKITDKIAEMKGYGLNTGEVSISTKEVADEDWNTAWQKYYHVIDFSRHLAIVPEWEDYHPAFSDQKLIRLDPGLAFGTGGHTTTQLVLLAMERALVKPMSVLDIGTGSGILAIAASKLGASHVLGTDISDEAVTAAKENIALNDVNNINVRKANLLKDIDDKYDLIVANILADILLELIPDLDSHLNKEGKVIFSGIDYLQLPKVEKALAENNFEIKMKMQEGRWIGLLIARKPD
Methylates ribosomal protein L11.
Q043X8
Q9D9S2
TM225_MOUSE
Transmembrane protein 225
Mus
MMHIPNRSIQAANIFFSSGAILLLIVGLIMEDWVELIPKVRKDKTTHSPWLGCCPPFWPEESLEVVRRIMRMTLNISIYLNLIIGLQFSYMISQNKCVHLLVGFLSFFAGCLLFYAIIVYHHKLNKGQYVYFVNYKTKWIAFTVYLTIALFLTCGIFCFIQSTNRCECMKFCIPHTESKSQEMIPSTIEVVSLPPRCAMPRSIVHVHSVTSKDGSLNRPHTQARRVTWAL
Probably inhibits protein phosphatase 1 (PP1) in sperm via binding to catalytic subunit PPP1CC.
Q9D9S2
Q8RA55
RECA_CALS4
Recombinase A
Caldanaerobacter
MMIEKQKALEMAISQIERQFGKGAIMRLGDTAKLNVEVIPTGSLELDIALGVGGVPRGRIIEIFGPESSGKTTLALHMIAEAQKIGGTGAFIDAEHALDPVYAKNLGVNIDDLLVAQPDTGEQALEIAEALVRSGAVDIIVIDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLAGVTSKSKSIVVFINQLREKVGVMFGNPETTPGGRALKFYATIRLDVRKVDNIKQGNEIVGSRTRVKVVKNKIAPPFKQAEFDIMYGEGISREGSILDLGTALDIIEKSGSWYSYKDIKLGQGRENAKQFLKENKEIAEEIERKIRENFNLAYNKIKSAPDAIVE
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.
Q8RA55
A5UFJ9
LIPB_HAEIG
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Haemophilus
MNNSLIVRQLGLQDYQEIWHKMQDFTDTRNAETQDEIWLVQHYPVFTQGQAGKPEHLLQRSEIPVVQSDRGGQITYHAPGQQVMYVLIDIKRHKNLNVRQLVTALEQTVVKTLAEYGIESYPKPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNINMDLNPFHYINPCGYAGLEMCQLADFVNQDEADWDNVSAKLIKHFADLLGYNITTL
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
A5UFJ9
A3CSU7
CBID_METMJ
Cobalt-precorrin-6A synthase
Methanoculleus
MRDPVTDFEYPAAWVAACRSPDLLDDVRRGLAVLTASGTVLRRGFSTGTTAAAACKAAILSLACDTVREVDVTLPCGIAVRLAVDGYRGQASCRKDAGDYTADVTGGLEFVAMAAPSLSGGVQFVPGEGIGSFARDTPRHRRGTPAISAPALDCIRRSIDEAVEEADLSGTTVILTIPRGAEVAQKTLNPRVGVHGGISVLGTTGFVEPWDDHMTEGVIDRIARAPGAVVLTTGRLGLRYSRLLFPEHEAILVGNKLEEALRAVEGDAVICGLPGLILKFMNPDVLSGTGCVTVEELSATPLWEETVRRELAAFRARYPRVRVVIVDRDGRIIGEPP
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
A3CSU7
B7XIV9
HSF_ENTBH
Heat shock factor protein
Enterocytozoon
MAKRKEVTEISEMDIKKSGFVNRLYRETCDISNKYIKFDDDGDKLIIPNKIDFIKKALNKISSTKDYSSFVRQLNNYGFTKIKLDNGDSNCDIYYHQNFHRDHPDLISLITRDKSKNGDYKDNMTTFINSLQYLASCNYKQQKEINDLKDRIKTLETKYATLYEIISNAFRQGIEQYQKHNTMYFNNNSLLKNMFTYNQELDDLKDNTNVYNNAKLINQLKLDAKNSNQDDNIKKTKNAFDEFYF
DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription.
B7XIV9
A4W5D0
ACEK_ENT38
Isocitrate dehydrogenase kinase/phosphatase
Enterobacter
MSRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEHADWHAVQQAMKQRIHLYDHHVGLVVEQLRCITEGKSTDVDFLLRVKEHYTHLLPDYPRFEIAESFFNSVYCRLFDHRSLSPERLFIFSSQPARRFRAIPRPLAKDFFPEKGWEKALNNVLSDLPLRLPWQNKTRDVGYISAHLVETLGEETLRHSHLQVANELFFRNKAAWLVGKLITPDATLPFLLPIHRSDDGELFVDTCLTTSAEASIVFGFARSYFMVYAPFPAALVEWLREILPVKTTAELYMAIGCQKHAKTESYREYLYYITSTDEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDQFAPQKEMTAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPTLMALLLQEAPDKITDLGDKIAISHLYIERRMVPLNIWLEQVEGAQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRTIPAARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHDDLFRADYWRSLQTRIKEGHVEDVYAYRKRQRFCLRG
Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
A4W5D0
Q9UBL9
P2RX2_HUMAN
Purinergic receptor
Homo
MAAAQPKYPAGATARRLARGCWSALWDYETPKVIVVRNRRLGVLYRAVQLLILLYFVWYVFIVQKSYQESETGPESSIITKVKGITTSEHKVWDVEEYVKPPEGGSVFSIITRVEATHSQTQGTCPESIRVHNATCLSDADCVAGELDMLGNGLRTGRCVPYYQGPSKTCEVFGWCPVEDGASVSQFLGTMAPNFTILIKNSIHYPKFHFSKGNIADRTDGYLKRCTFHEASDLYCPIFKLGFIVEKAGESFTELAHKGGVIGVIINWDCDLDLPASECNPKYSFRRLDPKHVPASSGYNFRFAKYYKINGTTTRTLIKAYGIRIDVIVHGQAGKFSLIPTIINLATALTSVGVGSFLCDWILLTFMNKNKVYSHKKFDKVCTPSHPSGSWPVTLARVLGQAPPEPGHRSEDQHPSPPSGQEGQQGAECGPAFPPLRPCPISAPSEQMVDTPASEPAQASTPTDPKGLAQL
Ion channel gated by extracellular ATP involved in a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K(+) recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle.
Q9UBL9
Q2GZN9
NST1_CHAGB
Stress response protein NST1
Chaetomium
MKGNRNPPPPPSGPVPPSPTSKNTAKYTNKDGSKFITVPKMNTPIDSAQPSPTASSLAAKPALPPGPETEPPQTVNRKKQKRRAKAAAKAAAERAQNSPAINGLPSPSPTNDQQSADADPEDDEDEPGTGHDSGNQSLYLNGGAHGGAPGKSKKSKKKKKKNATGPAGGFPNNNPYAQDDRDHSPEPILPPPPPQQNRPGMSREKIWNTNSQEERERIKEFWLGLSEAERKSLVKVEKDAVLKKMKEQQKHTCSCTVCGRKRTAIEEELEGLYDAYYEELEQYANHPNQGEGPPMLRPRRSFGSMGGMRPRGLHSRFSNHQPSRGRIVDELEGDEEEEEVEAEAEDDGEGDEEGEDVYSEDELEDDMYSEEEQEPSEELHRSDYAADFFNFGNSLTVQGRDRLPILPSFLQNYPFSGTGNNAYGSSSLGGILTVADDLLKNDGKKFIEMMEQLAERRMAREEDARGQFERAYDHPNGERYVHSHPPPPDEEEFEDEEEEYEEDDEEEYNSPDEEDTMTEEQRMEEGRRMFQIFAARMFEQRVLTAYREKVAKERQAKLLEEIEAENQQDAQRKAKKAKDAQRRKDRAAKKKEAQAEEKARREAEKAAEEAARRAEEARKAEEQRAKAEEKRKKKEAQRKAEEEERQRKEAERLRKIQDREEAERKAREAREREKKTREEARLREKEAREQKERKDRERREQQERERREKEAKAKAEREAKEAKEAKEAKEGKDTKERRKKEERAAHKAAALAPAIPVPITLPKRSATQQPPAPPVAPVPVLPQQSTSYASPKVPVATPALPKAPTPMRARQTSQQDGSTASSGAASNSGSMASQNPSPHPITPVHASPGLMAPPSKSGVMGIGSQGSAQPPSHSASPMSFPAKLLPPQHSPFGIPPMGSAMSYPPPGLSQMPLGFANPLHREPLFPPMPGFRPASGMMPMPPGLNGPGVNRGFPLHPPPGFLGGPMESPAPSMAQAMSPGLQRDNQSPHSRQGSGSFDPSQPISRPTPIGRPASVVQGQRPSNWSPSSGPPKPEPEAHLGSRALLDDLDDGPQDFPGRLSRGGSAPGPRPAPGFPMPPFGMDPMFSHNPWAPPGVVQPNLFGPHPPPSFSPLSAHTPMGMPWGHAMPSASTFGTPGAVDRPIEPRSVAVRKMLRRACEDLANAGSAEGRDSFIPLEMIKVQVENFNHGYPIDEKDLLDICETEGNEVNGGGSFDVVNDGQGGRSIRFVSGDQRTAPQPVQLAVGYNPGSPIGGGR
May act as a negative regulator of salt tolerance.
Q2GZN9
Q07Z51
FETP_SHEFN
Probable Fe(2+)-trafficking protein
Shewanella
MARTVHCQHLNKSADGLDFQLYPGELGKRIFDNIGKEAWGLWQKKQTMLINEKKLNMMNVDDRKFLEEQMTNFLFEGKDVEIEGYVPPAEDE
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
Q07Z51
Q7CVH1
KATG_AGRFC
Peroxidase/catalase
Agrobacterium tumefaciens complex
MDATSKPAGKCPVMHGGNTASGKSVTEWWPNALNLDILHQHDTKTNPLGTSFNYREALKTLDVEALKADLRALMTDSQEWWPADWGSYVGMMARVTWHAAGSYRVTDGRGGANTGNQRFAPLNSWPDNVNTDKGRRLLWPIKKKYGNKISWADLIALAGTIAYDVAGLKTFGFAFGREDIWAPEKDTYWGDEKEWLAPSDGRYGDVSKPETLENPLAAVQMGLIYVNPEGVNGKSDPLATAAQMRETFARMGMDDEETVALTAGGHTIGKSHGNGSAANLSPDPEAAGPEYQGLGWINTKGRGIGRDTVVSGIEGAWTSEPTKWDNGFFDMLFKHEWTLTHSPAGASQWAPITIAEEDKPVDVEDASIRTIPMMTDADMALKVDPIYREISLKFKDDQDHFSDVFARAWFKLTHRDMGPKSRYVGPDVPAEDLIWQDPIPAGSTSYDVAAVKAKIAASGLSVADLVSTAWDSARTFRGSDKRGGANGARIRLAPQKDWEGNEPARLSRVLSVLEPIARETGASIADVIVLAGNYGVEQAAKAAGFDIAVPFAAGRGDASAEQTDADSFAPLEPLADGFRNWVKKDYVVSPEELLLDRAQLLGLTAPELTVLIGGLRVIGANYGGAAHGVFTDKPGALTTDFFTTLTDMAYSWVPTGNNLYEIRDRKTGAARYSATRVDLVIGSNSILRAYAEVYAQDDNREKFARDFIAAWTKVMNADRFDLI
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Q7CVH1
P46956
PHO86_YEAST
Inorganic phosphate transporter PHO86
Saccharomyces
MAVQQRKKKEGRKSDKNAPSVPQVDASLDKPLDIDAPPTIYSVNLKPEYGTAALNLSADFIRQEQALANKYLFFHPVILVVLTIGLLIYLTPRIVFPIRNTGSVAGWFYQLARINKKVVLSGLVFTAIGASFLFTLLSRVSDSYFKSKINQLVGSKGEKVFGINLNDLVARHETKDPVVNNTHIIVYRETPIALISLAPNMTLSTDENLVMSVTTVGCRRVYVKSGIIEDLIDWAMLHSKNIRSSGKYGETMKLLIDVYSFDSTLKEILKKKGFTYIQSIRVSENRLLGGLFGVKKELWGLQFHFKAEHKD
Involved in the uptake of inorganic phosphate.
P46956
P10720
PF4V_HUMAN
Platelet factor 4 variant(6-74)
Homo
MSSAARSRLTRATRQEMLFLALLLLPVVVAFARAEAEEDGDLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQALLYKKIIKEHLES
Inhibitor of angiogenesis. Inhibitor of endothelial cell chemotaxis (in vitro).
P10720
P53390
MEP3_YEAST
Ammonium transporter MEP3
Saccharomyces
MARGDGHLWTETYDSSTVAFMILGAALVFFMVPGLGFLYSGLARRKSALALIWVVIMATLVGILQWYFWGYSLAFSKTATNNKFIGNLDSFGFRNVYGKISDDSTYPELIYAIFQMMFMCVALSIIAGATAERGKLFPHMVFLFVFATLVYCPITYWIWAPGGWAYQWGVLDWAGGGNIEILSAVAGFVYSYFLGRRKENLLINFRPHNVSMVTLGTSILWFGWLLFNAASSLSPNMRSVYAFMNTCLSATTGGMTWCLLDYRSEKKWSTVGLCSGIICGLVAATPSSGCITLYGSLIQGIIAGVVCNFATKIKYYLKVDDSLDLLAEHGIAGVVGLIFNALFAADWVIGMDGTTKHKGGWLTHNWKQMYIQIAYIGASAGYCAVVTAIICFVLGKIPGVHLRVTEEAEALGLDEDQIGEFAYDYVEVRRDYYQWGVDTDALHTTCNGANSASETNPTEDSQNSSLSSATVSGQNEKSNNPKLHHAKEA
Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source. The affinity of MEP2 is about twenty times higher than that of MEP1. MEP3 has the lowest affinity.
P53390
B9MGN9
RIMP_ACIET
Ribosome maturation factor RimP
Diaphorobacter
MALQQIVEQTVAGLGYDLVEIERSAGGLLRITIDLVWVPPTDEVSAAVGVEQFITVEDCEKVTRQLQFALEVEGVDYTRLEVSSPGIDRLLRNEADFKRFEGEVIDITLKQPMGAAAGGQVHANRKKFRGTLERADSGGWQIVWSDEPPVKPGQRISKKRVPAPLQALGFTLDELREARLAPIVDFKGRGTKPGEPG
Required for maturation of 30S ribosomal subunits.
B9MGN9
Q8FEM8
HIGB_ECOL6
Toxin HigB
Escherichia
MHIISKAPFEECARKYPNDALALHSLYRVIKETDFSTPEEMRTAFPNLDNFKYRNKWYVLDVGGNNLRVIAYINFVNKRFFVKHITNHAEYDKLTRYYRENKE
Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-dependent mRNA interferase. Probably counteracted by antitoxin HigA.
Q8FEM8
P41510
PME_BRANA
Pectin methylesterase
Brassica
MAVGKIVISVASMLLVVGVAIGVVTFVNKGGGAGGDKTLNSHQKAVESLCASATDKGSCAKTLDPVKSDDPSKLIKAFMLATKDAVTKSTNFTASTEEGMGKNINATSKAVLDYCKRVLMYALEDLETIVEEMGEDLQQSGSKMDQLKQWLTGVFNYQTDCIDDIEESELRKVMGEGIAHSKILSSNAIDIFHALTTAMSQMNVKVDDMKKGNLGETPAPDRDLLEDLDQKGLPKWHSDKDRKLMAQAGRPGAPADEGIGEGGGGGGKIKPTHVVAKDGSGQFKTISEAVKACPEKNPGRCIIYIKAGVYKEQVTIPKKVNNVFMFGDGATQTIITFDRSVGLSPGTTTSLSGTVQVESEGFMAKWIGFQNTAGPLGHQAVAFRVNGDRAVIFNCRFDGYQDTLYVNNGRQFYRNIVVSGTVDFIFGKSATVIQNSLILCRKGSPGQTNHVTADGNEKGKAVKIGIVLHNCRIMADKELEADRLTVKSYLGRPWKPFATTAVIGTEIGDLIQPTGWNEWQGEKFHLTATYVEFNNRGPGANTAARVPWAKMAKSAAEVERFTVANWLTPANWIQEANVPVQLGL
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
P41510
B2HSN4
RL2_MYCMM
50S ribosomal protein L2
Mycobacterium
MAIRKYKPTTPGRRGASVSDFAEITRSTPEKSLVRPLHGHGGRNAHGRITTRHKGGGHKRAYRVIDFRRNDKDGVNAKVAHIEYDPNRTARIALLHYLDGEKRYIIAPNGLSQGDVVESGANADIKPGNNLPLRNIPAGTLVHAVELRPGGGAKLARSAGSSIQLLGKEASYASLRMPSGEIRRVDVRCRATVGEVGNAEQANINWGKAGRMRWKGKRPSVRGVVMNPVDHPHGGGEGKTSGGRHPVSPWGKPEGRTRNPNKASNKLIVRRRRTGKKHGR
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.
B2HSN4
A4STH3
NORW_AERS4
Flavorubredoxin reductase
Aeromonas
MKAATLSEAGVSREILVIGSGFAAQQLVKSLRKLDAEQPIRLITADSGDEYNKPDLSHVVSRGCTAAAMTRLSGSDFAEQQRIALVPHCPVLGIDPARRIVMTVQGEFAYGQLVLATGASAARPDLPGSEQLVTLNSQQEYAAAEGPIQQARRILVLGAGLIGCELAMDMASDGREVTLVDLADSPLSALLPAVLSQPLQQALRSQGVSLQFGLGIARIDAQPGDGWRVTLTDGRTSEQDLVIAAIGLKPNLVLAQAAGLAVERGILVDDSLQTSAPHIFALGDCAQWRGQLLPFLQPIVLGANALARTLLGTPTPLTLPPMLVKVKTPRYPLQLAGRTKGEDLAWQCRWNSHGLVAEARAEDGELCGFVVGGDQMSAAFPLLRQLPR
One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.
A4STH3
C3KWF7
FABH_CLOB6
3-oxoacyl-[acyl-carrier-protein] synthase III
Clostridium
MSNISVIGTGSYVPNNIITNDFLSTIVDTSDEWIRTRTGILERRISKEENTIYMAIESAKEAIKNANIEANDLDLIIVATLTPDNFMPSTACSVQKEIGAINALCFDISAACSGFIYGLEIACSMLKNSFRNKALIIGAENLSKIVDWKDRNTCVLFGDGAGAAILSKTKEEGILEFHSGSNGLKGEHLTCGVLKANNISNKNDRLENDNFIKMNGKEIFRFAVGAMSETICNIQEKTKWDLSEVKYIISHQANSRIIEYTAKKLNTSKDKFYMNLDKYGNTSAASIPIALDEMNKKGLLNKQDKIILVGFGGGLTFGGVAIVWSI
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
C3KWF7
Q493C0
LPXA_BLOPB
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Candidatus Blochmannia
MIHQSAIIHPSSIIEEGAIIHDNVHIGPFCFIGAQVEIGARTLLKSHIVINGITQIGEDNQIYQFASLGEVNQDLKYAKESTRIEIGHYNQIRESVTIHRGTIQGKKVTKIGNSNLFMINVHIAHDCIIGDHCVMANNVTLGGHVRVDNHTIIGGMTAIHQFCIIGTHVMIGGCSGVVQDIPPFIIAQGNHATPFGLNIEGLKRRGFSRSSVHAIRDAYKILYRSSKTVESAKEALKALAAEHPIINEFVDFLIRSQRGIIR
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q493C0
A1VYA9
SYS_CAMJJ
Seryl-tRNA(Ser/Sec) synthetase
Campylobacter
MLDLKNLQNNFDEVAKKLKNKKVDENILKKLAELFASLKKEKTALEEFQAFQNKFSKELATAEDKESLKAKLSENKSKINEQSAKVNALENELEEIAHAIPNIPDECVPVGEDEDENVELKKVLNPSSFDFTPKEHFELGESLNWLDFVRGVKISQSRFCVLKNEGALLSRALVNYMIDFNRSRGFEFVNVPFLVNGATMFGTGQLPKFKEDMYKVDDEDLYLISTSEIPVTNLYSGEILASETLPIKMTCYSACFRKEAGSAGRDTRGIIRQHQFEKVELVSITKPEQSDSVFNEMLECASDLLSSLGLAHRHLMLCTGDLGFSAAKTVDLEVWLPGQNKYREISSVSNCRDFQARRAKIRYKNEQGKNELVHTLNGSSLAVGRTLVAIMENYQDKEGKIHIPDVLKKYF
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
A1VYA9
C3MAY3
RL2_SINFN
50S ribosomal protein L2
Sinorhizobium
MALKSFNPTTPSQRQLVIVDRAGLYKGKPVKTLTEGLSSKGGRNNLGRITVRFQGGGHKRTYRLVDFKRRKFDVEGTVERLEYDPNRTAFIALVNYADGEQAYILAPQRLAAGDKVIASDKAVDVKPGNTMPLQFIPVGSIIHNVEMKPGKGGQIARSAGTYAQLVGRDQGMAILRLNSGEQRLVHGSCLASIGAVSNPDHGNINDGKAGRSRWRGKRPHVRGVVMNPVDHPHGGGEGRTSGGRHPVTPWGKPTKGKRTRSNKSTDKFIMRSRHQRKK
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.
C3MAY3
A6BM08
ATPA_GNEPA
F-ATPase subunit alpha
Gnetum
MMITIRPDEISSIIREQIEQYNNEIQVVNMGTVLQVGDGIARIHGLYEVMAGELVEFEDSTVGIALNLETQNVGVVLMGDGLTIKEGSFVKTTGKIAQIPVSDAFLGRIVNALAQPIDGRGPIPASEFRLIESPAPGIVSRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVVCVYVAIGQKASSVAQVVNMLRERSAMEYTIVVVEPADSPATLQYLAPYTGTALAEYFMYKKKHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNSQLGEGSITALPIVETQAGDVSAYIPTNVISITDGQIFLSSDLFNAGIRPAINVGLSVSRVGSAAQIKAMKQVAGKLKLELAQTAELEAFAQFASDLDKGTQDQLARGQRLRESLKQPQSTPLTVEEQIATIFTGTNGYLDRFDIREVKKFLDQLREYLKKKKPQFGEIIRTTKIFTEEAEALLREAIKEQTELFVVQQKN
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
A6BM08
P10496
GRP2_PHAVU
Glycine-rich cell wall structural protein 1.8
Phaseolus
MATIHRLPSLVFLVLLALGVCSARRALLTLDAGYGLGHGTGGGYGGAAGSYGGGGGGGSGGGGGYAGEHGVVGYGGGSGGGQGGGVGYGGDQGAGYGGGGGSGGGGGVAYGGGGERGGYGGGQGGGAGGGYGAGGEHGIGYGGGGGSGAGGGGGYNAGGAQGGGYGTGGGAGGGGGGGGDHGGGYGGGQGAGGGAGGGYGGGGEHGGGGGGGQGGGAGGGYGAGGEHGGGAGGGQGGGAGGGYGAGGEHGGGAGGGQGGGAGGGYGAGGEHGGGAGGGQGGGAGGGYGAGGEHGGGAGGGQGGGAGGGYGAGGEHGGGGGGGQGGGAGGGYAAVGEHGGGYGGGQGGGDGGGYGTGGEHGGGYGGGQGGGAGGGYGTGGEHGGGYGGGQGGGGGYGAGGDHGAAGYGGGEGGGGGSGGGYGDGGAHGGGYGGGAGGGGGYGAGGAHGGGYGGGGGIGGGHGGNVP
Responsible for plasticity of the cell wall.
P10496
A5F554
RL5_VIBC3
50S ribosomal protein L5
Vibrio
MAKLHDYYKSSVVAELTKQFSYTSVMQVPRIEKITLNMGVGEAINDKKLLENAASDMAIISGQKPLITKARKSVAGFKIREGYPIGCKVTLRGERMWDFLERLISIALPRVRDFRGVNGKSFDGRGNYSMGVREQIIFPEIDYDKVDRVRGLDITITTTAGTDEEGRALLAAFNFPFRK
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
A5F554
Q12006
PFA4_YEAST
Protein fatty acyltransferase 4
Saccharomyces
MPVKLRWPWLGIAIPTFLISFIGYGAHYFILSNFLSVPKQITFEFCLSMIWLSYYLAICTNPGRPLPNYKPPPDIWRNFCKKCQSYKPERSHHCKTCNQCVLMMDHHCPWTMNCVGFANYPHFLRFLFWIIVTTSVLFCIQAKRIYFIWQQRHLPGYFFKKSELIFLTISSPLNSFVLLTITILFLRCLFNQILNGRSQIESWDMDRLESLFNSGRLTQKLIDNTWRIYPESRSFQNKKDAEEHLTKKRPRFDELVNFPYDFDLYTNALLYLGPIHLWLWPYGVPTGDGNNFPKNGISKYEANSSLEDHILSLPWPPDGGKTNTVFNHGSSTIEMRNESGEQLIRTRLPQNGRHASREKWYNDWGESLDDFGVDVDME
Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. Palmitoylates several amino acid permeases . Palmitoylates chitin synthase CHS3, which is required for its proper export from the ER . Can palmitoylate RAS2 in vitro .
Q12006
A9HVE9
BIOF_BORPD
8-amino-7-ketopelargonate synthase
Bordetella
MQLLDNLDAALRKLDAQHLRRRRRTAESPCAPHVRVDGRDMLAFCSNDYLGLAAHPVIVAALAEGAARYGAGSGASHLISGHSHAHAQLEERLANMLAPHLEQPRALYFCTGYMANLAVLGALAGRDADIFSEALNHASLIDGARLSRARVQVYPHADLDALADMLAASRAQTRLIVSDGVFSMDGDIAPLRDLLALAERHGAWLVVDDAHGFGVLGEHGRGVLEHAGLRSPHLVLMGTLGKAAGVAGAFVAAHATVIDWLVNRARPYIFSTAAAPAQAHALMASLNLIEGSEGRQRRARLQALAQQLQARLSLRQWRHQPTPTAIQPIVLGANAHALRAAAGLESQGLWVPAIRPPTVPPGTARLRVTLSASHIPAHVDRLADALNQLDNEACHA
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
A9HVE9
A4T174
MEND_MYCGI
Menaquinone biosynthesis protein MenD
Mycolicibacterium
MNPSTAQARVVVDELVRGGVRDVVLCPGSRNAPLAFALHDADRAGRLRLHVRIDERTAGFLAIGLAVAERAPVCVAMTSGTAVANLGPAVVEANYARVPLIVLTANRPYELLGTGANQTFEQLGYFGTQVRESISLGLAGDHADMGSLNAQWRSATCRVLVAAKGSRSANAGPVQFDIPLREPLVPDADDGSAYAPEGRPGGKEWTYTPAVTFDQPLEIDLTPDTVVIAGHGAGVHPNLAHLPTVAEPTAPYAQTPLHPLALSLIRPRQVIMLGRPTLHRSVSTLLADPAVPVFALTTGPRWPDVSGNSQATGTRAVTSGAASPEWLRRCAEVNRHAVEAVRGQLAAHPLTTGLHVAAVVADAVGPGDQLVLGASNPVRDIALVGFNTADVKVRSNRGVAGIDGTVSTAIGAALAHERATGGRTVALIGDLTFVHDSSGLLVGPTEPTPRKLTIVVSNDNGGGIFELLEQGDPRFSDVSSRIFGTPHDVDVGALCRAYHVESTQIEAGELAAALAEDFDGMRVLEVKADRSSLRALHASIKAGL
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
A4T174
Q5E3F0
FABZ_ALIF1
Beta-hydroxyacyl-ACP dehydratase
Aliivibrio
MTRENKTLNITEIQELLPHRYPFLLVDRVTDFEEEKYLHAIKNVSVNEPQFTGHFPQMPIFPGVLILEAMAQATGLLAFKSFGAPAENELYYFASIDKAKFRKPVVPGDQLVLEVEFIKDRRGIALFNGVAKVDGEVVCSAELKCARREF
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Q5E3F0
Q0ACA3
LIPB_ALKEH
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Alkalilimnicola
MPPSPLTDIQVRYLGRRDYRETWSAMRRYTDERGPDTPDQLWVVSHPPVYTLGQAGRREHILDPGEIPVVETDRGGQVTYHGPGQIVLYPLLDLRRWGLGVRSLVSALEHTVISLLAGYGIASEARDDAPGVYVEGRKVASVGLRVRRGCSYHGLAVNVDVDLEPFLRINPCGYPGLEVTRLLDLGVPTPYERLEADLALHCLEAIVEYGNGGAA
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Q0ACA3
Q57JQ5
CCA_SALCH
Phosphatase
Salmonella
MKIYLVGGAVRDALLGLPVKDKDWVVVGATPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAPDVTLEADLQRRDLTINALARDDDGQIIDPYHGRRDLEARLLRHVSPAFGEDPLRVLRVARFAARYAHLSFRIADETLALMREMTAAGELEHLTPERVWKETENALTTRNPQVYFQVLRDCGALRVLFPEIDALFGVPAPAKWHPEIDTGVHTLMTLSMAAMLSPQLDVRFATLCHDLGKGLTPKNLWPRHHGHGPAGVKLVEQLCQRLRVPNDLRDLAKLVAEYHDLIHTFPILQPKTIVKLFDAIDAWRKPQRVEQIALTSEADVRGRTGFEASDYPQGRWLREAWQVAQAVPTKEVVEAGFKGIEIREELTKRRIAAVANWKEKRCPPPAS
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
Q57JQ5
A8ESZ9
UREE_ALIB4
Urease accessory protein UreE
Aliarcobacter
MTFSVIKKVIEIKKDIPFSDEVELSWFDMQKPNLTAVTKKGVNLVVKAKFTHLHENDILVCEDGIGIKVKRSEDEIFSLEFSDALTFAKTAYEIGNRHQPLQIEEFKIIVLDDISIADIIKDCYANESIKVEKTKAYFKPNGKAHHSH
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
A8ESZ9
A4FZM0
ILVD_METM5
Dihydroxy-acid dehydratase
Methanococcus
MISDNVKKGVIRSPNRALLKACGYSDEDMEKPFIGVVNSFTEVVPGHIHLKTLSDAVKHGVYANGGTPFEFNTIGICDGIAMGHEGMKYSLPSREIIADAVESMARAHGFDGLVLIPTCDKIVPGMIMGALRLNIPFIVVTGGPMLPGEFQGKKCELISLFEGVGEYQVGKITEEELKSIEECACPGAGSCAGLYTANSMACLTEALGLSLPMCATIHAVDAQKVRIAKKTGSKIVDLVKEDVKPTDILTKEAFENAILVDLALGGSTNTTLHIPAIANEIENKFITLDDFDRLSDEVPHIASIKPGGEHYMIDLHNAGGIPAVLKVLKEKIRNTKTVDGRSTLEIAESVKYVNYDVIRKVEAPVHETAGLRVLKGNLAPNGCVVKIGAVDPKMHKHEGPAKVYNSEDEAIAAILGGKIVEGDVVVIRHEGPSGGPGMREMLSPTSAICGMGLDDSVALITDGRFSGGSRGPCIGHVSPEAAAGGLIAAIENGDIIKIDMIEKEINVDLDESVIKERLSKLEEFEPKIKKGYLSRYSRLVSSADEGAVLK
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.
A4FZM0
Q3KLL2
HEMH_CHLTA
Protoheme ferro-lyase
Chlamydia
MVTYLLANFGGPRTSQEIVSFLQALLTDRDVTGGMIPSMLHRPLFSYIAKRRAPHVARQYAYLGGGSPIFQDTERLAQNLSQELQASVIPFHRYLPETHRETLQALQESQGSIVGIPLFPHYTFAVTGSIIRFFLQHLPEKPISWITQFGVHPEFVSCMQQHIRDCLAAQQIAVEDCYFLFSVHGLPQRHIRLGDPYAQQCQASFEALRGELEGKIAFQSKFGIGKWLDPSTQEVCQSLRTKKRHIVIVPFGFVSDHIETLHEIDHLYVPILLQKGYRVVRIPAINASSRWVSSLAAIVRSSPQETSLEPLLMP
Catalyzes the ferrous insertion into protoporphyrin IX.
Q3KLL2
A1AVR9
NUOH_RUTMC
NDH-1 subunit H
Candidatus Ruthia
MELWQAFVQMVYTLTPWFDGTIASILIILIKAITLVIPLMLVVAYFTYAERKVIGYMQLRIGPNRVGPKGWLQPIADALKLMTKEIIFPTKANIYLFLLAPVLAIAPAIAVWVVIPFDEDIYITNLDISLLYVLAIGSIGVYGIILAGWASNSKYPLLGALRSASLLVSYEIVIGFALATVVMIAGSVNLNTIVQAQQGGIIYWNFIPLFPMMIIFFISALIETNRAPFDVVEGESEIVGGTHVEYSGMTFAVFFLAEYANMILMAVLAVVMFFGGWHSPFEAIPYLESAFSWVPGIIWLLAKTTFFMFLYLWVRATFPRFRYDQIMRLSWKVFLPITIIWIFVVALMTQLKLEPWF
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
A1AVR9
Q4UMQ9
SECY_RICFE
Protein translocase subunit SecY
spotted fever group
MGQNFSKKSGNDLVSRIVFTILILIVCRFGSFIPIPGIDSIALSSVAEKNQSGILGMFNMLSGGSLGRMSIFALAIMPYITASIIIQLMSVAYKPLENLKKEGEVGKRKVNQLSRYLTVLLASFQAYGVAISLESIVTNTGPVVILAGFFFRVTTVITLVVGTMLLMWLGEQITQRGIGNGTSLIIFIGIISGVPSAIISMFELSRKGALSPLIALAVCIGVVVLIAIIIFFEKAQRKLLVQYPKRQVGNKIYGGEATHMPLKLNTSGVIPPIFASSILLFPATLANFSNSNSETMGMLTYYLGHGKPVYILLYVALIMFFSFFYTAIVFNSEETANNLRKYGAYIPGKRPGKNTSDYFDYILTRLTVIGGIYLSVICVIPELLMNKYVISLSLGGTSFLIVVNVVLDTMTQIQTYLFSSKYEGLMKKVKLKN
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Q4UMQ9
O74428
TCO89_SCHPO
Target of rapamycin complex 1 subunit tco89
Schizosaccharomyces
MERPSLSRRTSSSTVSTDGEGVYSRSTKERKRNFIVNSRLKRGGGHVRVNRSGRLGSVTMRPSALTRAHSQNPNSSLVNNSSAVSHLTKQRSLNDLHELNGPKHVAKNGLIPLTQRKPNCVWDDAPVDNDSTAGNLDSDSALPTPSVTTNEAADSSRASSPVTRVVAVHDNKKKIINSNISNAPPFNNTDVQASARPPAAGQDDSAADASTTKSSPVHNEVMAEPLPHSNNREVTQATNQPKWQIHSGSDIASEPPTLSRGNSLSLLANRKVPSTNVKKSQAELYDLGSSTSRTQQKLLIQRASSKFDIVEDDMDTNPSKRFSNPHTKHIMDLVRTQYRNVLRTRELIPEFLEKIRSSYSNNQNFDSQNAFNTSAAGTAGTREETISNGQNGIVASAETSKKDDGVQSASLNASMSARSHARQRSIHVPKTRKDTDYESIHQKLLQLWSQG
Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Tor2 is essential for growth. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls cell growth and ribosome biogenesis by regulating ribosomal protein gene expression. TORC1 negatively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Represses mating, meiosis and sporulation efficiency by interfering with the functions of the transcription factor ste11 and the meiosis-promoting RNA-binding protein mei2.
O74428
Q7VJ31
PROB_HELHP
Gamma-glutamyl kinase
Helicobacter
MQKPRIVLKIGSSNLCNGKIIDKTQIKALAQIISELKMRFDVILVSSGAVASGHTTLHIDRNTLQNKQALASIGQPLLMESYREALKDYAIPTAQLLLVWRDFDSRKNTTFAKDTIDTLLAHNALPIINENDTIATDEMVFGDNDRLGAYVTYYFGAKLLIILSDIDGYFDKNPHQYDDAQILPIVHSIPSQALEQTHSPHGDFATGGIVTKLIAADFLLQRKCMMFLSHGRKLDVLRDFLLHNKQSSGTLFCPADSQGIKTLI
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Q7VJ31
P20718
GRAH_HUMAN
Cytotoxic serine protease C
Homo
MQPFLLLLAFLLTPGAGTEEIIGGHEAKPHSRPYMAFVQFLQEKSRKRCGGILVRKDFVLTAAHCQGSSINVTLGAHNIKEQERTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVSMSTLATTLQEVLLTVQKDCQCERLFHGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKDVAQGILSYGNKKGTPPGVYIKVSHFLPWIKRTMKRL
Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication.
P20718
Q8U0B3
LYSK_PYRFU
Putative [LysW]-lysine/[LysW]-ornithine hydrolase
Pyrococcus
MISTEEKIEFLKRLVEIYSPTGKENGVAKFLIKSFENYGIEAYLDDVGNVIAVKKGKGPLILLAGHMDTVPGYIPVRIENGELWGRGAVDAKGPLATFFFATIESDANIIFAGLVDEEGFSKGAKNLEVPKPDYIIVGEPSGTNGVTIGYKGSLTVKFTETVEKVHGSIGVGAAEKLIEKWLTIAKYFGEGFNSLSGRIVKFVAYEREFDFFGEMIVNLRTPPGYMPPKEWDIIDFVPAYEVSRTSPLVRAFVRAIRKAGYKPKLKKKTGTADTNILGPKYGVDAIAYGPGDSKLDHTPYERIKLREYLEAIEILKNAILELSSND
Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine and the release of L-ornithine from [LysW]-L-ornithine.
Q8U0B3
Q61900
SMR3A_MOUSE
Submaxillary gland androgen-regulated protein 1
Mus
MKPLNLVLGLCILVGCFLSCECHRGPRRHDPRGPFPPPPPPHGPGIGRPHPPPFGPGIGRPPPPPFGPGIGRPPPPPPCPPVPPHPRPPSNPSPPPTPSIPPTGPPTTVQATTMPAASISITTPTARDSTDIFWRLWELINSLLQQE
May play a role in protection or detoxification.
Q61900
Q4L9R7
TRHO_STAHJ
tRNA hydroxylation protein O
Staphylococcus
MDYRVLLYYKYTTIDDPETFAAEHLEFCKSNNLKGRILVSTEGINGTLSGTKEDTDKYIEHMHSDERFADMTFKIDEAEGHAFKKMHVRPRNEIVALGLEDDVDPRVTTGKYYSPSEFKEALEDEDTVILDARNDYEFDLGHFRGAIRPDITRFRDLPDWIRENKDQLDGKNIVTYCTGGIRCEKFSGWLVKEGFENVGQLHGGIATYGKDPETKGQYWDGKMYVFDERISVDVNQVEKTVIGKEHFDGTPCERYINCSNPECNKQILVSEENEDKYLGACSYDCAKHERNRYVAKNNISDEEWNRRLENFKDVPEHAHA
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q4L9R7
A1JLB3
SYE_YERE8
Glutamyl-tRNA synthetase
Yersinia
MKIKTRFAPSPTGYLHVGGARTALYSWLFTRHFGGEFVLRIEDTDLERSTQEAIDAIMDGMNWLNLDWDEGPYFQTKRFDRYNAVIDQMLENGTAYRCYCSKERLDELREAQMTNGEKPRYDGRCRDSQCTHGADEPSVVRFRNPQAGSVIFNDKIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALGAPVPEYAHVSMILGDDGKKLSKRHGAVGVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFSVAEMTELFTLDAVSKSASAFNTEKLQWLNHHYINSLPPEQVAVHLSWQVEQLGIDTRNGPELVEIVKLLGERCKTLKEMAESCRYFYEEFDEFDADAAKKHLRPVARQPLEAVKAKLAAITEWTTENVHNAIQGTADELGVGMGKVGMPLRVAVTGAGQSPGMDVTVHAIGQARSLSRIDKALAFISEREAQQ
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).
A1JLB3
P50476
HOX3_XENLA
Homeobox protein XHOX-3
Xenopus
MEGRKEMLMYLEGGQLGTLVGKRMAHLSDAVGSPMAESQDKLVPKSPRAGPIAPTDRAEESEVEVGQATGQQRSRSPQLRISSPHPPAHSDSLSTKGQHSSSDTESDFYEEIEVSCTPDCNSAASDYQQHSAGQCSEPMGGSPVNGSDSSKGGGGSHGSFSACAGDQMRRYRTAFTREQIARLEKEFYRENYVSRPRRCELAAALNLPETTIKVWFQNRRMKDKRQRLAMTWPHPADPAFYTYMMSHAAATGNLPYPFPSHLPLPYYSHMGISAGSTAAATPFSAPLRPLDTFRVLSHPYPRPDLLCAFRHPSIYASPAHGLGSGGSPCSCLACLSTSTNGLGQRAAASDFTCSSTSRSDSFLTFTPSILSKSSSVSLDQREEVPLTR
May be required for posterior development and development of normal embryonic axial pattern.
P50476
Q32K36
RAPA_SHIDS
ATP-dependent helicase HepA
Shigella
MPFTLGQRWISDTESELGLGTVVAVDARTVTLLFPSTGENRLYARSDSPVTRVMFNPGDTITSHDGWQMQVEEVKEENGLLTYIGTRRDTEESGVALREVFLDSKLVFSKPQDRLFAGQIDRMDRFALRYRARKYSSEQFRMPYSGLRGQRTSLIPHQLNIAHDVGRRHAPRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIIVPETLQHQWLVEMLRRFNLRFALFDDERYAEAQHDAYNPFDTEQLVICSPDFVRRSKQRLEHLCEAEWDLLVVDEAHHLVWSEDAPSREYQAIEQLAEHVPGVLLLTATPEQLGMESHFARLRLLDPNRFHDFAQFVEEQKNYRPVADAVAMLLAGNKLSNDELNMLGEMIGEQDIEPLLQAANSDSEDAQSARQELVSMLMDRHGTSRVLFRNTRNGVKGFPKRELHTIKLPLPTQYQTAIKVSGIMGARKSAEDRARDMLYPERIYQEFEGDNATWWNFDPRVEWLMGYLTSHRSQKVLVICAKAATALQLEQVLREREGIRAAVFHEGMSIIERDRAAAWFAEEDTGAQVLLCSEIGSEGRNFQFASHMVMFDLPFNPDLLEQRIGRLDRIGQAHDIQIHVPYLEKTAQSVLVRWYHEGLDAFEHTCPTGRTIYDSVYNDLINYLASPDQTEGFDDLIKNCREQHEALKAQLEQGRDRLLEIHSNGGEKAQALAESIEEQDDDTNLIAFAMNLFDIIGINQDDRGDNMIVLTPSDHMLVPDFPGLSEDGITITFDREVALAREDAQFITWEHPLIRNGLDLILSGDTGSSTISLLKNKALPVGTLLVELIYVVEAQAPKQLQLNRFLPPTPVRMLLDKNGNNLAALVEFETFNRQLNAVNRHTGSKLVNAVQQDVHAILQLGEAQIEKSARALIDAARNEADEKLSAELSRLEALRAVNPNIRDDELTAIESNRQQVMESLDQAGWRLDALRLIVVTHQ
Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair.
Q32K36
Q867A9
EDN2_BOVIN
Preproendothelin-2
Bos
MPTALCSIALALLVALHEGKSQAATTPIPEQPAPLPRARGSHLRTRRCSCSSWLDKECVYFCHLDIIWVNTPGQTAPYGLGNPPRRRRRSLPRRCECYSARDPACATFCHQRPWTDAVAVPGSGSPAAAFQDGKTQATAGELLQRLRVISATKIHFARQQQKPTRETRPTHSRQRKR
Endothelins are endothelium-derived vasoconstrictor peptides.
Q867A9
A7ERA6
SEY1_SCLS1
Protein sey1
Sclerotinia
MDMATSNINGHGDRPSPAARFPTAPSVMTMNGNFASVGDAPTKEQYEHGIQVIDEQKEFNPNLNEYLQYTDTAHSGFNYHLISVFGSQSTGKSTLLNHLFGTQFGVMSERERRQTTKGIWMSKNKNQSSGASESETMADNILVMDVEGTDGRERGEDQDFERKSALFALATSEVLIVNIWEHQVGLYQGANMGLLKTVFEVNCQLFLKDKQSTPRSLLFFVIRDHLGTTPLANLKETLIQDLSAIWTSLSKPAGLENSKIEDYFDFAFAALPHKILQPDKFITEVQKLGTRFRAGRKSARAEDAGFEGGVFLPEYHRRIPADGFAVYTEGVWDQIVNNKDLDLPTQQELLAQFRCDEISREVLISFDAKIHPLEEKQGEDVRSGKPTVIADLGVTGKTARTSTIKHFETQASRYHKAVYTLKRTELEGKIDTRLKLLFHGQLLAAHKSGVASFSDAVSTAVKNGQKRAASYEFADIVEREKEVALKTFEAEMKSLYIEELSWTNFSSSYDLFEKDLNEVSGNLRKEEMRRLATHVERWVRSRLNDSIGVEFNKLGSGRGGSGAPETGEKPATEKDLWDRIWKTFTGTVKEAESKFIERAKSFDASEDEIEIGLWRLRRKSWGVLRAKIDEEVMEGNILLKLRENFEDKFRYDEAGVPRIWRPSDDIEGIYTKARESTLTLIPLLAKFKLLETSSPPELPEWIGNTPASVDPKDEEDLTPIGGVDEEEGKSLEEEMTVLSEAKRQDLVVRFKKTADGVYVEAKRSAIGGVAQVPLYFYGLLLALGWNEIVAVLRNPIYFVFLILCGVAGYVTYTLNLWGPIIRMLNAASTQGVEIGKEKLREFLKDSEVGRQALGMQGRDAGDSDAISLNTLDSRGKRVVREDEDVDEI
Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization.
A7ERA6
Q73S77
KAD_MYCPA
Adenylate monophosphate kinase
Mycobacterium avium complex (MAC)
MRVVLLGPPGAGKGTQAQKLSEKLGIPQISTGELFRSNIENGTKLGLEAKRYLDAGDLVPAELTNQLVDDRLSEPDAANGFILDGFPRSLQQAKALHEMLERRGTDIDAVLEFRVSQDELLARLKARGRADDTDEVILNRMKVYRDETAPLLDYYRDQLKTVDAVGTLDEVFARALCALGK
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Q73S77