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W4VSB6

MNTAGRLLLLCLALGLVFESLGIPVADDVEAVRDTDPDEKDPSVHNSLKAVYGDCGGERCRFGCCKTDDGEEKCQHFGCP

Probable toxin with unknown function (Probable). Expressed by the venom duct. The cysteine framework is VI/VII (C-C-CC-C-C). Displays a mini-granulin fold, a structure composed of two short, stacked beta-hairpins connected by two parallel disulfide bonds. This newly described fold is derived from the same cysteine connectivity as knottins (ICK fold). The name 'mini-granulin fold' comes from the structural homology with the N-terminal region of the human granulin. Belongs to the conotoxin H superfamily.

Q9I6Z1

MSEEPTVSPPSPEQPAAQPAKPARPAARRAPRKPATRRPRVASPAQKAREEIQAISQKPVALQVASAPHGSSEDSTSASLPANYPYHTRMRRNEYEKAKHDLQIELLKVQSWVKETGQRVVVLFEGRDAAGKGGTIKRFMEHLNPRGARIVALEKPSSQEQGQWYFQRYIQHLPTAGEMVFFDRSWYNRAGVERVMGFCSPLQYLEFMRQAPELERMLTNSGILLFKYWFSVSREEQLRRFISRRDDPLKHWKLSPIDIKSLDKWDDYTAAKQAMFFHTDTADAPWTVIKSDDKKRARLNCIRHFLHSLDYPDKDRRIAHEPDPLLVGPASRVIEEDEKVYAEAAAAPGHANLDIPA

Uses inorganic polyphosphate (polyP) as a donor to convert GDP to GTP and ADP to ATP. Shows a preference for GDP. Can also catalyze the synthesis of polyP from GTP or ATP, but the rate of polyP utilization is 75-fold greater than the rate of polyP synthesis. [phosphate](n) + GTP = [phosphate](n+1) + GDP [phosphate](n) + ATP = [phosphate](n+1) + ADP Mg(2+) is preferred for polyP utilization and Mn(2+) is preferred for polyP synthesis. Homotetramer. Also forms octamers. Belongs to the polyphosphate kinase 2 (PPK2) family. Class I subfamily. Truncated N-terminus.

P22998

MARKTVAAALALVAGAAVAVTGNAPAQAVPPGEKDVTAVMFEWNFASVARECTDRLGPAGYGYVQVSPPQEHLQGGQWWTSYQPVSYKIAGRLGDRTAFKNMIDTCHAAGVKVVADSVINHMANGSGTGTGGTSFSKYDYPGLYSGSDMDDCRATISNYQDRANVQNCELVQLPDLDTGEDHVRGKIAGYLNDLASLGVDGFRIDAAKHMPAADLANIKSRLTNPNVFWKLEAIHGAGEAVSPSEYLGSGDVQEFRYARDLKRVLQGEKLSYLKNFGEAWGHMPSGQSGVFVDNHDTERGGDTLSYKDGANYTLASVFMLAWPYGSPDVHSGYEWTDKDAGPPNNGQVNACYTDGWKCQHAWREISSMVAFRNTARGQAVTNWWDNGNNAIAFGRGSKAYVAINHETSALTRTFQTSLPAGSYCDVQSNTPVTVNSSGQFTATLAANTAVALHVNATGCGSTPTTPPTTPPATSGASFNVTATTVVGQNIYVTGNRAELGNWAPASALKLDPATYPVWKLTVGLPAGTSFEYKYIRKDAAGNVTWESGANRTATVPASGQLVLNDTFRS

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 1 Ca(2+) ion per subunit. Monomer. By maltose, and repression by glucose. Belongs to the glycosyl hydrolase 13 family.

Q8VE54

MGDRRFIDFQFQDLNSSLRPRLGNATANNTCIVDDSFKYNLNGAVYSVVFILGLITNSASLFVFCFRMKMRSETAIFITNLALSDLLFVCTLPFKIFYNFNRHWPFGDTLCKISGTAFLTNIYGSMLFLTCISVDRFLAIVYPFRSRTIRTRRNSAIVCAGVWILVLSGGISASLFSTTNVNNATTTCFEGFSKRVWKTYLSKITIFIEVVGFIIPLILNVSCSSVVLRTLRKPATLSQIGTNKKKVLKMITVHMAVFVVCFVPYNSVLFLYALVRSQAITNCLLERFAKIMYPITLCLATLNCCFDPFIYYFTLESFQKSFYINTHIRMESLFKTETPLTPKPSLPAIQEEVSDQTTNNGGELMLESTF

Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Transduces a signal by increasing the intracellular calcium ions and by stimulating adenylyl cyclase activity. The rank order of potency for agonists of this receptor is 1-oleoyl- > 1-stearoyl- > 1-palmitoyl- > 1-myristoyl- > 1-alkyl- > 1-alkenyl-LPA (By similarity). Belongs to the G-protein coupled receptor 1 family.

Q74ZK6

MQLSWKDIPTVPTSNDMLDIVLNRTQRKTPTVIRAGFKITRIRAFYMRKVKFTCEGFIEKFDDILKGFPNINDVHPFHRDLMDTLYEKNHYKVSLASVSRAKTLVEQVARDYVRLLKFGQSLFQCKQLKRAALGRMATIMKKLKDPLVYLEQVRQHLGRLPSIDPNTRTLLICGYPNVGKSSFLRCITKADVEVQPYAFTTKSLYVGHFDYKYLRFQAIDTPGILDRPTEEMNNIEMQSIYAIAHLRSTVLYFMDLSEQCGFTIEAQVKLFHSIKPLFANKSVMVVINKTDIIRPEDLDEERQEMLKSIMDFPGVEIMTTSCINEENVMAVRNKACEKLLASRIENKLKSQTRITNVLNKIHVAHPQKRDDGVERTPYIPEAFKNVKKYDPEDPERRPLARDIEAENGGAGVFNINLKDSYLLENDEWKNDVMPEILNGRNVYDFLDPDIAAKLQALEEEEERLEAEGFYESDDDAIEGMDDEDVEDIREKAAWIRDKQKKMINAARSRKALKNRGTMPRSKMAKSFEDMEKHMSSLGHNMSALQSKQSAAAAKNRYTESGADIVYGNNESAKTAGKLRQSDRLMDGVADASMRSKADRMAKLHRRERNRQARQGEADRHATASLPKHLFSGKRGIGSNDRR

Involved in the biogenesis of the 60S ribosomal subunit. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.

B7N2S2

MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQEPSAARQAFRKKLREGQLDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQALTTSDFERILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNESTENIGARRLHTVLERLMEEISYDASDLSGQTITIDADYVSKHLDALVADEDLSRFIL

ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP. By heat shock. Belongs to the ClpX chaperone family. HslU subfamily.

Q2MCF0

MPIIQSVERALQILDLFNEQATELKITDISKLMGLSKSTLHSLLKTLQLHGYIDQNPENGKYRLGMKLVERGHFVVGSIDIRQKAKGWLTELSRRTGQTTHLGILDGREGVYIEKIEGKLAAIAYSRIGRRLPVHATAIGKVLIAWLGEAELNALLEGYQYTTFTPATLASREALMSALAQTREQGYALDSEENEQGVRCVAVPVWNHESRVIAALSLSTLTSRVDDAELANFREQLQQAGLALSRALGYPA

Involved in regulation of xylonate catabolism. Represses the expression of both yagA and yagEF operons. Binds mainly at a single site within the spacer of the bidirectional transcription units yagA and yagEF. Activity may be controlled by xylonate. Expressed in the exponentially growing phase. Level decreases down to an undetectable level during stationary phase.

P80886

MNIHEYQGKEVLRKYGVSVPEGKVAFTAEEAVESAKSLSSSVYVVKAQIHAGGRGKAGGVKIAKSLDEVKAYAEELLGKTLVTHQTGPDGQVIKRLLIEEGCDIKKEYYIGLVLDRATSRIVLMASEEGGTEIEEVAEKTPEKIKKAVIDPAVGLQGYQAREIAFAINIPKELVGKAAKFMLGLYKAFVEKDCSIAEINPLVVTGDGNVMALDAKLNFDSNALYRQKDIMEYRDLDEEDPKEIEASKYDLSYISLDGNIGCMVNGAGLAMSTMDIIKHYGGEPANFLDVGGGATAEKVTEAFKIILSDQNVKGIFVNIFGGIMKCDVIAEGVVEATRQVGLTLPLVVRLEGTNVDLGKKILSESGLNITSAESMADGAQKIVSLV

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. ATP + CoA + succinate = ADP + phosphate + succinyl-CoA Binds 1 Mg(2+) ion per subunit. Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. Heterotetramer of two alpha and two beta subunits (By similarity). Interacts with BrxC (PubMed:33722570). Belongs to the succinate/malate CoA ligase beta subunit family.

A0LTH9

MTADTPSWPEVLSALLARRDLTEAEAAWAMHQIMSGEATDAQIAAFAVALRAKGESAEEVSGLSSVMLALAAPVPPIGEALDIVGSGGDRAHTVNISTMAAIVAAATGVVVAKHGNRAASSACGSADLLEALGVAIDLDGAGVARCIERAGIGFCFAPVFHPSLRYAAVARREIGIPTVFNFLGPLTNPARPTASAVGVADPRMAPVVAGVLARRGMRALVFRGDDGLDELTVTTTSTVWVVRDGSVQEVAFDPRAVGIEPADTAALRGADARHNAAVARAVLSGERGPIRDAVLLNAAAGLTAFDTPRPDQLVDQISAAMTRCAAAIDTGKAAQLLDAWVEASQAARGVDADRS

Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate Binds 2 magnesium ions per monomer. Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. Homodimer. Belongs to the anthranilate phosphoribosyltransferase family.

Q99W73

MITLYNTLTRQKEVFKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQELNQSVPEIAEKYIAAFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESGGDVYFRTRKFEGYGKLSHQSIDDLKVGARIDAGEHKEDALDFTLWKKAKPGEISWNSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDLQFPHHENEIAQSEAHNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINYNLELVESARSGLERIRNSYQLIEERAQIATNIENQQTYIDQIDAILNRFETVMNDDFNTANAITAWYDLAKLANKYVLENTTSTEVIDKFKAVYQIFSDVLGVPLKSKNADELLDEDVEKLIEERNEARKNKDFARADEIRDMLKSQNIILEDTPQGVRFKRG

ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys) Binds 1 zinc ion per subunit. Monomer. Belongs to the class-I aminoacyl-tRNA synthetase family.

Q60CR0

MTSPRKILVTSALPYANGPIHLGHLVEYIQTDIWVRFQKMRGHDCRYVCADDTHGTPIMLRAEKEGISPEELIARVHGEHLRDFTGFHIEFDNYYSTHSEETRAHAADIYGRLKDRGLIESRAIEQYFDPVKEMFLPDRFIKGECPKCHAKDQYGDSCEVCGTTYSPTDLINPYSVVSGAAPVRRESVHYFFKLGECAEFLKDWTRSGALQTEAANKLNEWFEAGLSDWDISRDAPYFGFEIPDAPGKYFYVWLDAPIGYMGSFQNLCDRLGLDFAEYWKKDSEAELYHFIGKDILYFHALFWPAMLEHSGFRTPTRIFAHGFLTVNGEKMSKSRGTFITAQSYLEQGLNPEWLRYYYACKLNGTMEDIDLSLEDFVARVNSDLVGKYINIASRTAGFVTKFFDGRLDVPMQLADGEALDFLIDRLRDSAEEISGYYDSRDYNKAIRKIMELADEVNIFVNEKKPWEIAKRDDSYSRGYLRVVCAITLNLFRLLTIYLKPILPRLAEAVEGFLKIPSLTWQDAQTLLPQGHTINDYQHLMTRIDPKQVDALVEANRQSLQATAGQPEPHSQVRHAEHQQRQVQPIAETISIDDFAKVDLRIARIANAEHVEGADKLLKLTLDLGGETRTVFAGIKSAYAPETLIGRLTVMVANLAPRKMKFGLSEGMVLAAGPGGGDIFLLSPDEGAQPGMKVK

Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met) Binds 1 zinc ion per subunit. Homodimer. Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.

A8A683

MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLDIADYMDKEDFLIQIMAGEEFGDVEAIFHEGACSSTTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATYGGRTSDFIESREYEKPLNVYGYSKFLFDEYVRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNKGESPKLFEGSENFKRDFVYVGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADATLAYHKKGQIEYIPFPDKLKGRYQAFTQADLTNLRAAGYDKPFKTVAEGVMEYMAWLNRDA

Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose Binds 1 NADP(+) per subunit. Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. Homopentamer. Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain. Belongs to the NAD(P)-dependent epimerase/dehydratase family. HldD subfamily.

A5V230

MRKSVDELSARLGVTFSDQRLLEQALTHSSFLNEHVEERMHLDSNERLEFLGDAIINFLAARLVFERFPDAGEGELTAWRTALIRTETLAGFAQRYNLGAYVLLARGEESSGARQRQALLADTFEAVIAALFLDQGLNAVRTFLLPLFEAELASLPDRTLPVDYKSRLQARIQAERRVTPRYHEIDRSGPEHRPEFTVEVRAGEERLGTGKGPSKQAAEQAAARAALDALEGGTDGR

Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. Endonucleolytic cleavage to 5'-phosphomonoester. Homodimer. Belongs to the ribonuclease III family.

Q0I5H9

MIRIGHGFDVHAFGGEGPIIIGGVAIPYEKGLVAHSDGDVALHALTDALLGAMALGDIGKLFPDTDIQYKGADSRRLLRTAYQAILDKGYQVGNVDITIIAQAPKMRPYIDAMRTVIAQDLHCDIEQVNVKATTTEKLGFTGRSEGIACEAVALLIKQTGTK

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). 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP Binds 1 divalent metal cation per subunit. Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. Homotrimer. Belongs to the IspF family.

V5IKJ1

MAATALDHLSLGGKIQWLAQLNTEFQPAREFRRTSIICTIGPKTNSVEAINKLRDAGLNVVRMNFSHGSYEYHQSVIDNARQAEKVHPGRPIAIALDTKGPEIRTGNTKNDEDIPISAGTILNITTDEKYKDECTIEHMYVDYVNITKVIAPGRIIYVDDGVLAFEVLEIVDDKTIKVKARNNGYISSRKGVNLPNTDVDLPALSEKDKADLRFGVKNKVDMVFASFIRRGQDIKDIREVLGEDGKQIQIIAKIENRQGLNNFAEILAETDGVMVARGDLGIEIPAAEVFAAQKKIIAMCNIAGKPVICATQMLESMIKNPRPTRAEISDVGNAVTDGADCVMLSGETAKGAYPTEAVREMSEAVLKAENTIPYVSHFEELCSLAKRPVSIVESCAMASVRASLDLNAAAILVLSTSGESARLISKYRPVCPIIMITRNDSASRYAHLYRGVYPFLFPESKPDFSKVNWQEDVDRRIKWGLSHGIGLKVLNEGETVVVVQGWKGGMGNTNTFRIVKADVNHLGLGQP

ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. Homotetramer. Belongs to the pyruvate kinase family.

Q7LWA9

MAGLKSFLASSWLLPVACGASQSIVPSTSATAAYSQFTIPASADVGANLVANIDDPQAVNAQSVCPGYKASDVKHSSQGFTASLELAGDPCNVYGTDVDSLTLTVEYQAKDRLNIQIVPTYFDASNASWYILSEELVPRPKASQNASVPQSDFVVSWSNEPSFNFKVIRKATGDVLFNTKGSTLVYENQFIEFVTLLPEEYNLYGLGERMNQLRLLENANLTLYAADIADPIDDNIYGHHAFYLDTRYYKVGGQNKSHTIVKSSEAEPSQEYVSYSHGVFLRNAHGQEILLRDQKLIWRTLGGSVDLTFYSGPTQAEVTKQYQLSTVGLPAMQQYNTLGFHQCRWGYNNWSEFEDVLANFERFEIPLEYLWADIDYMHGYRNFDNDQHRFSYEEGEKFLNKLHAGGRRWVPIVDGALYIPNPENASDAYETYDRGAKDDVFIKNPDGSLYIGAVWPGYTVYPDWHHPKASDFWANELVTWWNKLHYDGVWYDMAEVSSFCVGSCGTGNLSMNPAHPPFALPGEPGNVVYDYPEGFNITNATEAASASAGAASQSAAASSTTTSAPYLRTTPTPGVRNVDHPPYVINHVQPGHDLSVHAISPNSTHSDGVQEYDVHSLYGHQGINATYHGLLKVWENKRPFIIARSTFSGSGKWAGHWGGDNFSKWGSMFFSISQALQFSLFGIPMFGVDTCGFNGNTDEELCNRWMQLSAFFPFYRNHNVLSAIPQEPYRWASVIDATKAAMNIRYAILPYFYTLFHLAHTTGSTVMRALAWEFPNDPSLAAVGTQFLVGPSVMVIPVLEPQVDTVQGVFPGVGHGEVWYDWYSQTAVDAKPGVNTTISAPLGHIPVFVRGGSILPMQEVALTTRDARKTPWSLLASLSSNGTASGQLYLDDGESVYPEDTLSVDFLASRSTLRASARGTWKEANPLANVTVLGVTEKPSSVTLNGETLSSDSVKYNATSHVLHVGGLQKHTADGAWAKDWVLKW

Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch. Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose. By maltose. Belongs to the glycosyl hydrolase 31 family.

Q6AY97

MDDDDFGGFEAAETFDGEQGGNQAVSPAVPWATFPAVSGVRLSPASPELILDHDRSSPSSGHLRSDAVISSPDDTRADSSLVNQTISKVQLQQSAHTHLNIPLFPLGLTDESNHGALALEDEPEGPGVHVSNSQLRQKISSLETKLKASEEEKQRIKKDVESLMEKHSVLEKDFLKEKEQDAVSFQARYRELQEKHKQELEDMRKAGHEALSIIVDEYKALLQSSVKQQLDAIEKQYVSAIEKQAHRCEELLHAQHQRLLEVLDTEKELLKEKIQEALTQQSQEQKETLGKCLQEEMQKNKETLESAVKLEKEAMKDVITKAVEEERENLEKVHAEEREMWKTEHARDQERVAEAIQAAVQEQQRMSQEAVKAAIAEEQRRSEKAMEEAVKRTRDELVEYVREQRRLDQVTRQRSLSSLELFLSCAQKQLSALIATEPVDIE

Involved in the regulation of membrane traffic through the trans-Golgi network (TGN). Functions in close cooperation with the GGAs in the sorting of hydrolases to lysosomes. Homodimer. Interacts with GGA1, GGA2 and AP1G1. Colocalizes with GGA1, GGA2 and GGA3.

G8ZFU7

MLIDRFGRPVTNLRISLTKECNLNCFYCHREGQLDGERTMKPEEIERIVRIASRLGIKKVKLTGGEPTIRKDIVEIIRRIRPYVVDLSLTTNGTTLYTLAEELKEAGLDRVNISLDTLDRKKYKMITGFDVLDQVIKGIEKATKLFYPVKLNMVVMRGINDDEIWDLIRFAGKVNAILQLIEIEVPREMENSQFFKDFFYPLKPLEEEFEKIAVEIRERRMHRRRKYFLPVDGKVVEVEVVRSMHNTVFCMNCTRLRLTADGYLKTCLLRRDDLIDILGPLRNGASDAELVDIFKRAVLMRRPYWT

Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate. AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate. Cofactor biosynthesis; molybdopterin biosynthesis. Belongs to the radical SAM superfamily. MoaA family.

P52829

MTKGKRTFQPNNRRRARVHGFRLRMRTRAGRSIVSSRRRKGRRTLSA

Belongs to the bacterial ribosomal protein bL34 family.

P0C5B4

MVLIRVQANLLILQLSYAQKSSELIIGGDECNINEHRFLVALYTSRSRRFYCGGTLINQEWVLTAAHCDRKNIRIKLGMHSEKVPNEDAETRVPKEKFFCLSSKTYTKWDKDIMLMRLKRPVNNSTHIAPVSLPSNPPSVDSVCRVMGWGTITSPQETYPDVPHCANINILDYEVCQAAHGGLPATSRTLCAGILKGGKDSCKGDSGGPLICNGQFQGIASWGAHPCGQSLKPGVYTKVFDYTEWIQSIIAGNTDATCPP

Thrombin-like snake venom serine protease. The recombinant form clots fibrinogen by cleaving fibrinogen Aalpha chain (FGA), and slowly Bbeta chain (FGB). Has amidolytic activities. Completely inhibited by PMSF, and N-tosyl-Lphenylalanine chloromethyl ketone (TPCK) and poorly inhibited by benzamidine and derivates. Not inhibited by EDTA, heparin and hirudin. Optimum pH is 7.5-8.0. Optimum temperature is 40-50 degrees Celsius. Monomer. Expressed by the venom gland. Has no activity on gamma chain. Belongs to the peptidase S1 family. Snake venom subfamily.

A1CJC1

MSNPPHGGVLKDLLARDAPRHDQLETEAEQLPAIVLTERQLCDLELIMNGGFSPLEGFMNQKDYDNVCENVRLADGNLFSMPITLDVSKAVIDESQLKAGSRVTLRDFRDDRNLAILTIDDIYRPDKAREAKLVFGGDKEHPAIKFLNNTVQEFYIGGKVEAINKLNHYDYVALRYTPAELRVHFDKLGWSRVVAFQTRNPMHRAHRELTVRAARARQANVLIHPVVGLTKPGDIDHFTRVRAYQALLPRYPNGMAVLGLLGLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNSKGEEFYGPYDAQHAVEKYREELGIEVVEFQQVTYLPDTDEYKPKDEVPAGVKTLDISGTELRNRLRTGAPIPEWFSYPEVVKILRESSRPRSTQGFTIFLTGYMNSGKDAIARALQVTLNQQGGRSVSLLLGDTVRHELSSELGFSREDRHTNVQRIAFVAGELTRAGAAVIAAPIAPYEESRNAARDAVTQGGGNFFLVHVATPLEYCEKTDKRGIYAKARRGEIKGFTGVDDPYETPSNAHLTVDVSKQTVRSIVHEIILMLETEGFFDRA

Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids. ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. Homohexamer. Dimer of trimers. The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme. In the N-terminal section; belongs to the sulfate adenylyltransferase family. In the C-terminal section; belongs to the APS kinase family.

Q8GH95

MLAESVLGNLKEGGSSKELDFIDLEWFDAQKRMGRFTSQKGAELVLKLKNPPKMGLCDGDILFEDATSLIAINIIPTPTLHVYADSTAQVARLCYEVGNRHASLYYGDSPLSFKTPFERPLQVLFDKLALRYEVLKSKLDASQRISVSAPHADPLQEGSAPLKFKSALDLQIVIKK

Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family.

Q2IRA3

MAIFAEAETWVAIAFVILMGIFAYLGVHRTVLKALDNRRDRIKAELDEARKLKDEAAKLLADYRARRAQAEREAEAIVASAKADAERIAAESKAKLEDFVVRRTKTAESKIALAEAQALADVRAAAAEAAVSAAAIVLSQSVKGQVADDLLGKGIQEVRSKLN

F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family.

A6VDJ1

MGIFDWKHWIVILIVVVLVFGTKRLKNLGSDVGEAIKGFRKAVNTEEDDKKEQPAAQPAQPLNQPHTIDAQAQKVEEPARKD

Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. The Tat system comprises two distinct complexes: a TatABC complex, containing multiple copies of TatA, TatB and TatC subunits, and a separate TatA complex, containing only TatA subunits. Substrates initially bind to the TatABC complex, which probably triggers association of the separate TatA complex to form the active translocon. Belongs to the TatA/E family.

Q96JA2

METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM

Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:22431096, PubMed:10814726, PubMed:11799477, PubMed:18551513). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence. Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Interacts with SREBF1, SREBF2, SUN2 and TMEM43. Interacts with TMEM201 (By similarity). Proteolytically processed isoform A interacts with NARF. Interacts with SUN1. Prelamin-A/C interacts with EMD. Interacts with MLIP. Interacts with DMPK; may regulate nuclear envelope stability. Interacts with SUV39H1; the interaction increases stability of SUV39H1. Interacts with SYNE2. Interacts with ITSN1 isoform 2 (PubMed:29599122). Interacts with IFFO1; enables the formation of an interior nucleoskeleton that is recruited to DNA double-strand breaks (PubMed:31548606). Interacts (via C-terminus) with LEMD2 (via N-terminus) (in vitro). Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C. In the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle cells (VSMCs) from aged individuals and in atherosclerotic lesions, where it often colocalizes with senescent and degenerate VSMCs. Prelamin-A/C expression increases with age and disease. In normal aging, the accumulation of prelamin-A/C is caused in part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative stress. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations. Phosphorylation status of S-22 determines its localization between double-strand break (DSB) sites and the nuclear matrix (PubMed:31548606). Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C. The prelamin-A/C maturation pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated cleavage of the last three amino acids, methylation of the C-terminal cysteine and endoproteolytic removal of the last 15 C-terminal amino acids. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage. Sumoylation is necessary for the localization to the nuclear envelope. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. HGPS is caused by the toxic accumulation of a truncated form of lamin-A/C. This mutant protein, called progerin (isoform 6), acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. The mutant form is mainly generated by a silent or missense mutation at codon 608 of prelamin A that causes activation of a cryptic splice donor site, resulting in production of isoform 6 with a deletion of 50 amino acids near the C terminus. Progerin lacks the conserved ZMPSTE24/FACE1 cleavage site and therefore remains permanently farnesylated. Thus, although it can enter the nucleus and associate with the nuclear envelope, it cannot incorporate normally into the nuclear lamina (PubMed:12714972). The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Defects in LMNA may cause a late-onset cardiocutaneous progeria syndrome characterized by cutaneous manifestations of aging appearing in the third decade of life, cardiac valve calcification and dysfunction, prominent atherosclerosis, and cardiomyopathy, leading to death on average in the fourth decade. There are three types of lamins in human cells: A, B, and C. The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively. Disease-associated isoform. Polymorphism at codon 608 results in activation of a cryptic splice donor site within exon 11, resulting in a truncated protein product that lacks the site for endoproteolytic cleavage. Belongs to the intermediate filament family.

B5XNL5

MHNQAPIQRRKSKRIYVGNVPIGDGAPIAVQSMTNTRTTDVAATVSQIKALERVGADIVRVSVPTMDAAEAFKLIKQQVNVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGNEERIRTVVDCARDKNIPIRIGVNAGSLEKDLQEKYGEPTPQALLESAMRHVDHLDRLNFDQFKVSVKASDVFLAVESYRLLAKQIDQPLHLGITEAGGARSGAVKSAIGLGLLLSEGIGDTLRVSLAADPVEEIKVGFDILKSLRIRARGINFIACPTCSRQEFDVIGTVNALEQRLEDIITPMDVSIIGCVVNGPGEALVSTLGVTGGNKKSGLYEDGVRKDRLDNDDMIDQLEARIRAKASMLDEARRIDVQQLEAK

Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin] Binds 1 [4Fe-4S] cluster. Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6. Belongs to the IspG family.

Q797F9

MAKKTMGIHHITAIVGHPQENTDFYAGVLGLRLVKQTVNFDDPGTYHLYFGNEGGKPGTIITFFPWAGARQGVIGDGQVGVTSYVVPKGAMAFWEKRLEKFNVPYTKIERFGEQYVEFDDPHGLHLEIVEREEGEANTWTFGEVTPDVAIKGFGGATLLSEQPDKTADLLENIMGLERVGKEGDFVRYRSAGDIGNVIDLKLTPIGRGQMGAGTVHHIAWRANDDEDQLDWQRYIASHGYGVTPVRDRNYFNAIYFREHGEILFEIATDPPGFAHDETQETMGEKLMLPVQYEPHRTQIEQGLLPFEVRELD

Putative ring-cleavage dioxygenase that may contribute to the degradation of aromatic compounds. Binds 1 Fe(2+) ion. Repressed by MhqR. Strongly induced by stress due to exposure to 2-methylhydroquinone (2-MHQ) and less strongly induced after diamide or catechol stress. Not induced by oxidative stress due to hydrogen peroxide or methylglyoxal. Belongs to the extradiol ring-cleavage dioxygenase family.

Q9UTG7

MSCPIDSKKLEEICLEAAQPVLKASEYDGDKTAEMNQSVIYAVLNALNKETQSYKWIVSSTLVQKLPEDHPSRGVHAAHAACWNCEKDGMTTIKESGEAIDVVLSIMWISI

Acts as a non-catalytic accessory component of a dynein complex. Belongs to the dynein light chain Tctex-type family.

A4T3S4

MSDHGRMHSTGSEVAAPVAPDPDTEGVHPHFNRRVTSFRARRSTISDGQQATWDRLWPQLGRQARDGDEPPGPLDTDAWFGRHAPVVLEIGCGTGTSTLAMAQAEPGIDVVAVEVYRRGLAQLLSAIDRTAATEHPVSNIRLIRGDGVDVLTHMFGSASLTGVRVFFPDPWPKARHHKRRLLQPDTMALIADRLRPGGVLHAATDHQGYAAHIAEVGDAEPRLRRVAMDSADLPMSVTRPVTKYERKALAGPVVTELLWERTP

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine tRNA modification; N(7)-methylguanine-tRNA biosynthesis. Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Q86VM4

MRHCINCCIQLLPDGAHKQQVNCQGGPHHGHQACPTCKGENKILFRVDSKQMNLLAVLEVRTEGNENWGGFLRFKKGKRCSLVFGLIIMTLVMASYILSGAHQELLISSPFHYGGFPSNPSLMDSENPSDTKEHHHQSSVNNISYMKDYPSIKLIINSITTRIEFTTRQLPDLEDLKKQELHMFSVIPNKFLPNSKSPCWYEEFSGQNTTDPYLTNSYVLYSKRFRSTFDALRKAFWGHLAHAHGKHFRLRCLPHFYIIGQPKCGTTDLYDRLRLHPEVKFSAIKEPHWWTRKRFGIVRLRDGLRDRYPVEDYLDLFDLAAHQIHQGLQASSAKEQSKMNTIIIGEASASTMWDNNAWTFFYDNSTDGEPPFLTQDFIHAFQPNARLIVMLRDPVERLYSDYLYFASSNKSADDFHEKVTEALQLFENCMLDYSLRACVYNNTLNNAMPVRLQVGLYAVYLLDWLSVFDKQQFLILRLEDHASNVKYTMHKVFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPITQKILRDFYRPFNARLAQVLADEAFAWKTT

Sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo. n 3'-phosphoadenylyl sulfate + dermatan 4'-sulfate = n adenosine 3',5'-bisphosphate + dermatan 4',6'-bissulfate + n H(+) n 3'-phosphoadenylyl sulfate + chondroitin 4'-sulfate = n adenosine 3',5'-bisphosphate + chondroitin 4',6'-bissulfate + n H(+) Inhibited by phenyl beta-GalNAc(4,6-SO(4)). Homodimer; disulfide-linked (Potential). The relevance of homodimerization is however unsure. May interact with phosphorylated proteins in resting B-cells, including HCK. A small fraction may also be present at the cell surface, where it acts as a B-cell receptor. Expressed in B-cell-enriched tissues but not in fetal or adult thymus. Expressed in fetal and adult spleen, lymph node, tonsil, bone marrow and peripheral leukocytes. Not expressed in T-cells. In pro-B, pre-B, and mature B-cell lines, it colocalizes with RAG1. Glycosylated. Belongs to the sulfotransferase 1 family.

Q8CE78

MAALSKSIPHNCYEIGHTWHPSCRVSFLQITWGALEESLRIYAPLYLIAAVLRKRKLEYYLYKLLPEILQSASFLTANGALYITFFCILRKILGKFYSWTPGFGAALPASYVAILIERKSRRGLLTIYMANLATETLFRMGVARGTITTLRNGEVLLFCITAAMYMFFFRCKDGLKGFTFSALRFIVGKEEIPTHSYSPETAYAKVEQKREKHKGTPRAMSIIALVRTLVDSVCKHGPRHRCCKHYEDNCISYCIKGFIRMFSVGYLIQCCLRIPSAFRHLFTEPSRLLSLFYNKENFQLGAFLGSFVSIYKGTSCFLRWIRNLDDELHAIVAGFLAGVSMMFYKSTTISMYLASKLVETMYFKGIEAGKVPYFPQADTIIYSISTAICFHAAVMEVQNLRPSYWKFLLRLTKGRFALMNRKALDVFGTGASREFHNFIPRLDPRYTVVTPELPIDFS

Involved in mitochondrial metabolism by regulating the balance between mitochondrial fusion and fission (PubMed:27863209). May act as a regulator of mitochondrial fission that promotes DNM1L-dependent fission through activation of DNM1L (PubMed:27863209). May be involved in peroxisome organization (By similarity). Up-regulated following cold exposure and upon fasting. Age-dependent pathologies, characterized by accelerated aging in the retina similar to macular degeneration of the retina (PubMed:27863209). Retina show higher sensitivity to oxidative stress (PubMed:27863209). Defects are caused by impaired balance between mitochondrial fusion and fission (PubMed:27863209). Belongs to the TMEM135 family.

A6SXY6

MTLVSDHENDDMNPFRVRSRREVIALLRSIGERNQLVRMVINHGADTIVTSILNIDETNDTVLLDCAPTAIMNQRVLDSNKLSFETVLENIRILFNSPSAESCMYENLPAFVIPLPTSVVRLQRREFYRVPTPLTAPVSCTVPYTTEGVTIEVATTLHNISGGGVSLVDEKKLLSTTIGLTYQNCKIVLPGSGLITVALQVRNVLELTLTNGKSINRIGCEFINPSNGTLATVQKYITKIEREQNAKATGLG

Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Binds 1 c-di-GMP dimer per subunit. Increasing levels of c-di-GMP lead to decreased motility. Monomer. Interacts with the flagellar basal bodies. Belongs to the YcgR family.

Q9EQR5

MRPPVPSAPLALWVLGCFSLLLWLWALCTACHRKRAQRQQTGLQDSLVPVEMPLLRQTHLCSLSKSDTRLHELHRGPRSSIAPRPASMDLLHPRWLEMSRGSTRSQVPNSAFPPRQLPRAPPAAPATAPSTSSEATYSNVGLAAIPRASLAASPVVWAGTQLTISCARLGPGAEYACIQKHKGTEQGCQELQQKAKVIPATQMDVLYSRVCKPKRRDPRPVTDQLNLQDGRTSLPLGSDVEYEAINLRGQDMKQGPLENVYESIKEMGL

Involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and TCR (T-cell antigen receptor)-mediated T-cell signaling in T-cells. In absence of TCR signaling, may be involved in CD4-mediated inhibition of T-cell activation. Couples activation of these receptors and their associated kinases with distal intracellular events such as calcium mobilization or MAPK activation through the recruitment of PLCG2, GRB2, GRAP2, and other signaling molecules. When phosphorylated in response to TCR stimulation and/or CD4 costimulation, interacts with LCK, CSK, FYN, PTPN11/SHP2, GRB2, PIK3R1 and GRAP2 (By similarity). When phosphorylated in response to BCR activation, interacts with LYN, PIK3R1, PLCG2 and GRB2. Present in lipid rafts. Recruited to the immunological synapse upon conjugation of T-cell with antigen-presenting cell. Expressed in spleen and lung. Present in primary B-cells and peripheral T-cells (at protein level). Up-regulated in T-cells following TCR engagement. Palmitoylation of Cys-28 and Cys-31 is required for raft targeting. Phosphorylated on tyrosines upon TCR activation and/or CD4 coreceptor stimulation, or upon BCR stimulation; which leads to the recruitment of SH2-containing proteins.

Q9C0A2

MEPAVGGPGPLIVNNKQPQPPPPPPPAAAQPPPGAPRAAAGLLPGGKAREFNRNQRKDSEGYSESPDLEFEYADTDKWAAELSELYSYTEGPEFLMNRKCFEEDFRIHVTDKKWTELDTNQHRTHAMRLLDGLEVTAREKRLKVARAILYVAQGTFGECSSEAEVQSWMRYNIFLLLEVGTFNALVELLNMEIDNSAACSSAVRKPAISLADSTDLRVLLNIMYLIVETVHQECEGDKAEWRTMRQTFRAELGSPLYNNEPFAIMLFGMVTKFCSGHAPHFPMKKVLLLLWKTVLCTLGGFEELQSMKAEKRSILGLPPLPEDSIKVIRNMRAASPPASASDLIEQQQKRGRREHKALIKQDNLDAFNERDPYKADDSREEEEENDDDNSLEGETFPLERDEVMPPPLQHPQTDRLTCPKGLPWAPKVREKDIEMFLESSRSKFIGYTLGSDTNTVVGLPRPIHESIKTLKQHKYTSIAEVQAQMEEEYLRSPLSGGEEEVEQVPAETLYQGLLPSLPQYMIALLKILLAAAPTSKAKTDSINILADVLPEEMPTTVLQSMKLGVDVNRHKEVIVKAISAVLLLLLKHFKLNHVYQFEYMAQHLVFANCIPLILKFFNQNIMSYITAKNSISVLDYPHCVVHELPELTAESLEAGDSNQFCWRNLFSCINLLRILNKLTKWKHSRTMMLVVFKSAPILKRALKVKQAMMQLYVLKLLKVQTKYLGRQWRKSNMKTMSAIYQKVRHRLNDDWAYGNDLDARPWDFQAEECALRANIERFNARRYDRAHSNPDFLPVDNCLQSVLGQRVDLPEDFQMNYDLWLEREVFSKPISWEELLQ

Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. Component of striatin-interacting phosphatase and kinase (STRIPAK) complex (By similarity). Interacts with CDC42BPB (PubMed:25743393). Interacts with CTTNBP2NL (PubMed:18782753). Enriched on the plasma membrane. Belongs to the STRIP family. Extended N-terminus.

Q8Z098

MNKIAYLQCPTGISGDMCLGTLVSLGVPVAYLTEKLNNLGIAEEYKLRAEKVQRNGQEATKVHVDLLDHHHHDHEHHHHGRHLPEIEQMILQAGLPPRAEAWSLAVFRQLAVAEGSVHGIAPEKVHFHEVGAVDAIVDIVGTCLGLDWLGIASDNAGFPLLYCSAFPTGGGTVRAAHGQMAVPVPAVLKLWEMRGCPVYSNGIDRELVTPTGAAIATTLVKEFGAPPPMTIKQVGLGAGTINLPIPNILRLWLGESANLQANITDSAANSPTLETISVLETQIDDLNPQAIGYVFEQLFAVGALDVFTQPIGMKKSRPGILLTVICHPETLNDCEAVLFCETTTLGIRRTTQQRAVLQREFKPIQTKYGTVRIKIAWHGQSPEKVITNVQPEYEDCAELARKHKIPWREIQQLALQGWYESIQNSK

Belongs to the LarC family.

B1Y8J4

MNRDSRTALVLFSGGQDSTTCLAWALTRFAHVETLAFDYGQRHRIELDCRLTVLAQLREQFPDWAERLGADHLLDLSLLAQISDTALTTEREIELQANGLPNTFVPGRNLLFLGMAATLAYRRSASVLVGGMCETDYSGYPDCRDNTLKALQVALSLGLAAPMTIETPLMFLTKAQTWTLAEDLGGAPLVELITEHTHTCYLGERGQRHAWGHGCGHCPACELRHAGHAAWLGGR

Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate Binds 1 zinc ion per subunit. Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. Belongs to the QueC family.

P58059

MAKHLKFIARTVMVQEGNVEGAYRTLNRILTTDGLTEVISRRRYYEKPCRRRQRESYETCRRIYNMEMARKINFLMRKNRADPWLGC

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. Belongs to the bacterial ribosomal protein bS21 family.

Q90220

MIQVLLITICLAVFPFQGSSIVLDSGNLNEFEVVYPEKVTALPRAAVKNKYEDAMQYEFKVNGEPLLLHLERNKGLFSDDYSEIHYSPDAREISAYPSVEDHCFYHGRVENDADSTASLSACDGLKAHFKIQGEMYLIEPLEVSDTDAHAVFKYENVEKEDEPPKMCGVTQNWESYESTKKASQLNVSPDQQRFPQRFIKLAIYVDHGMYTKYAGNSERITKRVHQMINNINMMCRALNIVTSLSVLRIWSEKDLITVNASAPSSLTLFGAWRETVLLNRTSHDHAQLMTATIFNGNVIGRAPVGGMCDPKRSVAIVRDHNAILFIVAVTMTHEMGHNLGMHHDEDKCNCNTCIMSKVLSRQPSYEFSDCNENEYQTYVTDHSPQCILNDPLRPDTVSTPVSGNELLEAGEECDCGSPGNPCCDAATCKLRQGAQCAEGLCCDQCRFMKKGTVCRIARGDDMDDYCNGISAGCPRNPFHA

Impairs hemostasis in the envenomed animal. Inhibits platelet aggregation and bone resorption. Binds 1 zinc ion per subunit. Monomer. Expressed by the venom gland. The disintegrin belongs to the medium disintegrin subfamily. Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily. The disintegrin is also encoded by another precursor (AC Q1PBD1).

A4JCG7

MTNADPHELQKFSDLAHRWWDPNAEFKPLHDLNPVRLGWIDSHAHLAGKRALDIGCGGGILSESMAGLGAQVKGIDLSNEALGVADLHSLESGITVDYEAIAAEAIAEREPGSYDVVTCMEMLEHVPSPAGVVSACAKLVKPGGWVFFSTLNRNLKSYLFAVIGAEYIAQMLPKGTHDYARFIRPSELAGFVRATDLHIVELKGITYHPIGKRFALSNDTDINYLVACRRGA

O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-adenosyl-L-homocysteine Cofactor biosynthesis; ubiquinone biosynthesis. Belongs to the methyltransferase superfamily. UbiG/COQ3 family.

Q9UHE7

MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKEALLAGHLLCSPEQAVELSALLAQTKFGDYNQNTAKYNYEELCAKELSSATLNSIVAKHKELEGTSQASAEYQVLQIVSAMENYGIEWHSVRDSEGQKLLIGVGPEGISICKDDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSKEVYDHARRALYNAGVVDLVSRNNQSPSHSPLKSSESSMNCSSCEGLSCQQTRVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESCAAQLQSCPVCRSRVEHVQHVYLPTHTSLLNLTVI

E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR. S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Can bind 1 iron ion per dimer. Iron binding seems to decrease LDLR degradation activity. Protein modification; protein ubiquitination. Homodimer. Interacts with the E2 ubiquitin-conjugating enzyme, UBE2D1 (via RING-type zinc finger). Interacts with myosin regulatory light chain (MRLC) and TMEM4. Ubiquitously expressed. Expressed in fetal tissues and higher levels were detected in placenta and fetal lung. Expression is directly activated by NR1H2 and NR1H3. Expression is not dependent of the sterol-response element-binding proteins (SREBPs). Expression is indirectly induced by LDL. The RING domain mediates ubiquitination and the neurite outgrowth inhibitory activity. The FERM domain binds phospholipids and mediates lipoprotein receptors recognition at the plasma membrane through their cytoplasmic tails. The RING-type zinc finger mediates the interaction with UBE2D E2 enzymes. Autoubiquitinated.

Q8YE61

MALDIKICGLKTPEAVAAALDGGATHIGFIFFPKSPRHITPDAAARLRAAATGRAVAVAVTVDADDEALDEIVKTVRPDMLQLHGGETPERVRFLKERYNLPVMKAFSIREAGDLEAIAPYRGIADRFLFDAKPPKGSELPGGNGISFDWNLLAALDADIDYMLSGGLNADNIAEALLKTGAPGIDISSGVECAPGEKDVRLIENFFQAVADANAQPFARRA

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. Belongs to the TrpF family.

Q16965

MRPWCQLALLACLSLKWLTSHVTAESFLCDDSELCENGYLRFGRSMSVEEPHFRLERRSYPPVVYHKRFLRFGRSQEPDIEDYARAIALIESEEPLYRKRRSADADGQSEKVLHRARREAESEHKSLEEVSPDTKQDVEKRDADDVLDAEKRFMRFGKRFMRFGRGSSDDDESGDDDVQDLTDIGDGLGGEGEVNKRFMRFGKRFMRFGKREDGEPDKRFMRFGKSMADNDLDKRFMRFGKRFMRFGKSLPDSEVDKRFMRFGKSVDGDVDKRFMRFGKSVDGDVDKRFMRFGKSVDGDVDKRFMRFGKSVDGDVDKRFMRFGKSVDGDVDKRFMRFGKSVDDDVDKRFMRFGKSVDGDVDKRFMRFGKSVDDAVDKRFMRFGKSVDSDLDKRFMRFGKSVGSDEVDKRFMRFGKSVGSDEVDKRFMRFGKSLGTDDVNKRFMRFGKSLGTDDVNKRFMRFGKSLGTEDVDKRFMRFGKSLGTDDVDKRFMRFGKSLGTDDVDKRFMRFGKSLGTEDVDKRFMRFGKSLGTDDVDKRFMRFGKSLGTEDVDKRFMRFGKRFMRFGRSVGDSKYRSASSESVMTTDSKQTTEQATNKS

FMRFamide induces contractions in visceral and somatic musculature as well as in the heart. FLRF-amide. FMRF-amide. Belongs to the FARP (FMRFamide related peptide) family.

Q833W8

MLTLTAGKKAAMDRLSTQEGIISALAIDQRGALKKMIKALDVEPTDAQIETFKELVSKELTPYASAILLDPEYGLPAAKARDTEAGLLLAYEKTGYDATTPGRLPDLLADWSVLRLKEEGADAIKFLLYYDVDEDPEINHQKHVFIERLGSECAEEDLPFYLELVSYDAQIADATSLEYAKVKPHKVNEMMKEFSKPQYKVDVLKVEVPVNMNFVEGFAPAETAYTKEEAANYFLEQSQATDLPFIFLSAGVSTELFQETLRFAKEAGSTFNGVLCGRATWKNGVKPFVEAGETAACDWLKTEGRENIESLNEVIAATASSWHAKVQVNEG

D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 2/2. Belongs to the aldolase LacD family.

B5RL05

MSRLFQKEDDIVALATPFFSSALCVIRSSGVSAIEKFSKMFSDPSKLLEASGHTIHYGYILDNETKEKLDEVVVCLYRAPKSFTGQDSIEVMAHGSLIGIRRIIDFFLKVGFRMAEPGEFTLRSFLAGKLDLTKAEAINELISAKTRQVHALAVNKLSGSLFDKIDLIKKDILNFLSAISVYLDYETDDNEVVIPVDIILKSKSELERLIDSYDTARKLENGVTLVLAGSVNVGKSSLFNLLLKEDRAIVSSYAGTTRDYIQASFEFDGILFNVFDTAGLRETSDFVEQLGIVRSNSLIKEASLIFYVVDLSGKLTDDDLKFIDAYKEDSRVLFVLNKVDLEQNNQTVEFFNSNNVVSLNTVKISTKTLFGINSLYDRIRSLIAVDYMKTSDYDVVISSTRQAELLKRAYALIIELLSKIEQNISYDMLAFDVYEVVNVLGEITGEVTSDDVLDNMFKNFCLGK

Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. Binds 1 potassium ion per subunit. Homodimer. Heterotetramer of two MnmE and two MnmG subunits. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.

G3ECR4

MKINFSLLDEPMEVNLGTVLVIEDVSVFAQLVKEFYQYDEQSNLTIFDSKIRSIRSSELLLITDILGYDINTSQVLKLLHTDIVSQLNDKPEVRSEIDSLVSLITDIIMAECIENELDIEYDEITLLELIKALGVRIETKSCTVFEKIFEILQIFKYLVKKRILVFVNSLSYFSKDEIYQILEYTKLSQADVLFLEPRQIEGIQQFILDKDYILMPYNN

CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (Probable). Binds dsDNA (By similarity). When the CRISPR3/cas system consisting of cas9-cas1-cas2-csn2-CRISPR3 or just cas9-CRISPR3 is expressed in E.coli it prevents plasmids homologous to spacers 1 or 2 from transforming. Homotetramer. Plasmid transformation is still inhibited. Belongs to the CRISPR-associated Csn2 protein family.

Q72HP8

MRIGYGEDSHRLEEGRPLYLCGLLIPSPVGALAHSDGDAALHALTDALLSAYGLGDIGLLFPDTDPRWRGERSEVFLREALRLVEARGARLLQASLVLTLDRPKLGPHRKALVDSLARLLRLPQDRIGLTFKTSEGLAPSHVQARAVVLLDG

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). 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP Binds 1 divalent metal cation per subunit. Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. Homotrimer. Belongs to the IspF family.

B2UCW3

MNVKTVKCPSCGKPVPWVPESRYRPFCSERCKQIDLGAWAAEQYTIPVVEEDDLPDAPGNDTSGKLN

Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase. Binds 1 zinc ion. Interacts with GyrB. Belongs to the DNA gyrase inhibitor YacG family.

Q6CR06

MNIKQFFVPAGKPLSGLAVGLSIFLTALFLVNNLVYPINEHLLLKPDSLFKFDLNRISLYPLAHLSFFHLFFNVISTFSMIVMFEESHGTLYTGVILNLLAVFTAIPYCLIGSLLFPNVEIGGASGWFFSFLGYFAVKESRVRNSVMITSTFSFPTLYFPVALLFVTALLAPGSSLPGHAIGLLLGYFMGLKENWVAKITPPSFVLKKIETWVDPLINLIPFGIKYYREVEVDRSLEYTSVYLGSESRLPLHNTDTPAEPTFQGNGRVLGN

Probable serine protease. Belongs to the peptidase S54 family.

A5VIX0

MGKIHELDNILANQIAAGEVIERPASIVKELVENSLDAHSHRVDIIVENSGLDSVRVIDDGDGIAAEDISLAFHRHATSKINSRHDLFKVQTMGFRGEALPSIASVADVTLTTAQAGQEEGTMIHLRGGKELVVKPAGARQGTDIKVTDLFFNTPARLKYLKSPQTELTRITDIINRLALANPAVAFSFTHNGRELFRSAGNNNLQQVVAAIYGVQAGRKMLEISGADDDFKVSGFVSLPELTRASRQYITITINHRYIRNFELTKAIIQGYESKLMVGRYPIAVINIDLDPVLVDVNVHPAKREVRLSKEQQLIKLIAETIRQRIAVENLIPDVDADQFIPNDDEVADLDRRLKEASPVYHAAPISAVPATEKAATEIPTPEADNPAHADALDSEIPAPIVIHHLEDLNTPAMQKFDERYQNEGEVTPFSAPVPTMTKKPVKPANIELDVHDKQDQQQNRFPDLQYIGQLQGTFLLAQAGDGLYIVDQHAAQERINYEYYRQKIGEVSADQQNFLVPLVLNYSTVDAMTINQHLDTLAAVGLELESFGQNSFILRSHPTWFKEGQEEDTAEEMIDWLIKNGKLTVKEFRMKTAIMMSCKRAIKANHHLDEREAKALLKRLPQCENPFNCPHGRPVTVHFNDQDLEKMFKRIQDSHTPYADDFDDHEF

This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex. Belongs to the DNA mismatch repair MutL/HexB family.

Q07LA7

MSFTFAIIGRPNVGKSTLFNRLVGQKLALVDDTPGVTRDRREGEGRLGDLEFTLIDTAGLDEGAKGSLTERMQQQTETAIELADALMFVFDARAGLTPNDRAFADFARRANKPVILVANKSEGKAGEIGAMESYALGLGDPVQISAEHGEGLSELYDAFRALMPEPDEEAEEDDDVEGLTEEEFSKRPIRVAIVGRPNAGKSTMINHLLGEERLLTSPEAGTTRDSIAVSVDYKGRQFRIFDTAGLRRRSRIEEKLEKLSVADALRAVRFAEVVVLMLDAQTKFEEQDLRIADLIEREGRALVIAVNKWDLVERHPGQIGALRTEADHWLPQVKGVPIVAVSGLMGEGIDRLMSAIEDSYATWNRRVPTAALNRWFEQAIQTNPPPAVSGRRLKLNYVTQAKARPPSFIVFCSRADAVPESYLRYLVNSLRNYFELPGTPVRIMLREKANPFAHKRKRPS

GTPase that plays an essential role in the late steps of ribosome biogenesis. Associates with the 50S ribosomal subunit. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.

Q1C5B1

MNASDLIRIMQFGDSVLPVGAFTFSNGVESAIQTGIVHDVATLKGFVLTALKQAASCDGMGVVVAHRAVVADDRDGIIRADWAVNNRKLNEESRLMATRMGKKLAEMSIHVVEHPLISWWLEQIKNGNTAGTYPVTQAVVMAAQGIGQREVVVMHQYGVAMTILSAAMRLMRVTHFDTQHILFELNHDIEKFCDIAEIGDINQMSSYVPIVDVLAAVHVKAHVRLFSN

Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel. Belongs to the UreF family.

P55312

MDPSKYRPSSAYDTPFLTTNAGGPVYNNVSSLTVGPRGPVLLEDYYLIEKLATFDREKIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGAQTPVICRFSTVVHERGSPESIRDIRGFAVKFYTREGNFDLVGNNVPVFFNRDAKSFPDTIRALKPNPKSHIQENWRILDFFSFLPESLHTFAFFYDDVCLPTDYRHMEGFGVHAYQLINKEGKAHYVKFHWKPTCGVKSMSEEEAIRVGGTNHSHATKDLYDSIAAGNYPEWKLFIQTMDPEDVDKFDFDPLDVTKTWPEDLLPLIPVGRLVLNRNIDNFFAENEQLAFNPGHIVPGIYYSEDKLLQTRIFAYADTQRHRIGPNYMQLPVNAPKCGHHNNHRDGAMNMTHRDEEVDYLPSRFDPCRPAEQYPIPACVLNGRRTNCVIPKENNFKQAGERYRSWESDRQDRYITKWVESLSDPRVTHEIRSIWISYLSQADKSCGQKVASRLTVKPTM

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. 2 H2O2 = 2 H2O + O2 Homotetramer. Belongs to the catalase family.

Q12JN5

MSLADSVLAVNNDLPIRTDKPVHSGKVRSVYWLTESDSRRLINDKGYKVPLDTPLAIMVISDRISAFDCIFHGEGGLQGIPGKGAALNAISNHWFKLFAEQGLADSHILDIPHPFVWIVQKARPIKVEAICRQYITGSMWRAYAKGEREFCGIRLPEGLKKDQKLPELIITPSTKGILTGIPGVPAQDDVNISRQDIEANYQAFGFESLSDIDLYETLLKDGFKVISDALAQLDQVFVDTKFEFGYVTDKNGQSKLIYMDEVGTPDSSRIWDGAAYRDSKIVENSKEGFRQFLLNHVADADVLLNKDRMPEREALARDNALPLDAMMNVSRTYTGVAEKVTGKTITLAANPKADIIAILKKNYGLID

5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. Belongs to the SAICAR synthetase family.

Q62Q38

MTNGTIHNKDGFLNRIAERLGRNRRSAGVTVPDYIHQPQHRVYQGYTQDELVGVLKDHCRKIHTELIETDVIGLHDALYEQAARFGGGPVMIPKDDRFKEYGLSGLLTDKWPNEGTKVWEWDAAAGDENIQRAEQANIGVTFSEITLAESGTVVLFSSKDKGRSVSLLPTTYIAIVPKSTIVPRMTQASAIIKQKIADGDVIPSCINYVTGPSNSADIEMDLVVGVHGPVKAAYIVVEDR

Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Belongs to the LutC/YkgG family.

V5N6J4

MEKKIIFLCFFVSLLTLPEFISSQVLVEDDVPFPEKKFADRGECIRACAAKFTDGDLSKIKDVLPRYYKCVCWYYPTS

Expressed by the venom gland. Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta). Since the toxin contains only 2 disulfide bonds, it is called 2ds-CSalpha/beta. Belongs to the SLPTX(15) family.

Q7M8G1

MLKRILITNDDGFDSPGLLALKEALCDVAHLTVVAPANEKSACGHGLTLTSPLRFIKLDDDVYKLRDGTPTDCIYLALNALYEEHSKPDLIISGINLGSNMGEDITYSGTASGAMEGVIHGIPSVAFSQLLHDKNTFGFDFALAKKVVRELTLKILSGGFPLGDRKFLNVNIPYVGIEEFKGYKVTEMGYRLYGNDAHLHRNPRGEEHYWLGLHPLAWNERNNARESDFKVATEGYVSITPIKLDLTSYEDIKELEAWI

Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate Binds 1 divalent metal cation per subunit. Belongs to the SurE nucleotidase family.

Q6GER9

MSELFSNDNIFLNVNVNSQNEAIEKAGKALVDSGAVTDAYIQAMKDREQVVSTFMGNGLAIPHGTDEAKTNVIHSGLTLLQIPEGVDWDGEVVKVVVGIAGKDGEHLDLLSKIAITFSEEGNVDRIVQAKSAEEIKQVFEEADA

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. Homodimer or homotrimer. Seems to be a monomer when not phosphorylated. The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.

B9E332

MLVISRKKGESLLIGEDIEITVTKIEEGAVKLSISAPRSVTILRKELYREIEEENKNSAASDISVLKKLKGKK

A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW. Homodimer; the beta-strands of each monomer intercalate to form a hydrophobic core, while the alpha-helices form wings that extend away from the core. Belongs to the CsrA/RsmA family.

B5RMX2

MATSKSGGSSKNGRDSISKRLGVKRSGGQFVRAGEIIIRQRGTKFHKGKNSGLGRDHTIFALKDGIVEFKTSKGRKYINII

Belongs to the bacterial ribosomal protein bL27 family.

B1XD36

MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDVDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVHNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGNPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate [protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-tyrosine + H(+) + UMP Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity. Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing. Belongs to the GlnD family.

A8WFG5

MKIKNSLKALKARHRDNRLVRRKGRVYIINKQNPRFKARQG

Belongs to the bacterial ribosomal protein bL36 family.

Q90XB6

MKTSWFALFLAVLSTELLTSHSSTLKSLRFRGRVQQERKNIRPNIILVLTDDQDVELGSLQVMNKTRRIMENGGASFINAFVTTPMCCPSRSSMLTGKYVHNHNIYTNNENCSSPSWQATHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWVGLVKNSRFYNYTISRNGNKEKHGFDYAKDYFTDLITNESINYFRMSKRIYPHRPIMMVISHAAPHGPEDSAPQFSELYPNASQHITPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNVLQRKRLQTLMSVDDSMERLYQMLAEMGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSVVPQIVLNIDLAPTILDIAGLDTPPDMDGKSVLKLLDLERPGNRFRTNKKTKIWRDTFLVERGKFLRKKEEANKNTQQSNQLPKYERVKELCQQARYQTACEQPGQKWQCTEDASGKLRIHKCKVSSDILAIRKRTRSIHSRGYSGKDKDCNCGDTDFRNSRTQRKNQRQFLRNPSAQKYKPRFVHTRQTRSLSVEFEGEIYDINLEEEELQVLKTRSITKRHNAENDKKAEETDGAPGDTMVADGTDVIGQPSSVRVTHKCFILPNDTIRCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPDECDCTKQSYYNKEKGVKTQEKIKSHLHPFKEAAQEVDSKLQLFKENRRRKKERKGKKRQKKGDECSLPGLTCFTHDNNHWQTAPFWNLGSFCACTSSNNNTYWCLRTVNDTHNFLFCEFATGFLEFFDMNTDPYQLTNTVHTVERGILNQLHVQLMELRSCQGYKQCNPRPKGLETGNKDGGSYDPHRGQLWDGWEG

Regulates Wnt signaling through desulfation of cell surface heparan sulfate proteoglycans. Binds 1 Ca(2+) ion per subunit. Also localized on the cell surface. Expressed in the ventral spinal cord and paraxial mesoderm as well as in the floor plate. The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. Belongs to the sulfatase family.

B7V9S6

MTHDLAASGLRFGIEEEFFLLDASDLDIVRSAPAGFVAACRDTLGEHFAEEMFECQVEVASPVFSTLAEAARFHGQARQRLAHLAMDFGLRSLCVGTHPFADWRRARSNPAAHFARLFEDQGRVARRSLVCGLHVHVEIPPSHDRMAVLQRVLPWLPLLLALSASSPFRGGRRSGLASYRRALCGEWPRMNIPPALPDEDAYRRHLALLRETGCIREDGQVWWMIRPSSHVPTLELRICDACPRLADALSLAGLFRALVGEALDADPRALPVARDACLEENYWQALRYGCAGRYLVEGRCVGAGDWLEMAWRQCRPQARRGNEWAYQHACGLLEETSAARQLRRYRRLREAGQERHPALRRLVEELLEENLQPALAG

ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily.

A1KRT0

MIMQEWFQNLFAATLGLGDLGITVGLVVSVIVKIVIILIPLILTVAYLTYFERKVIGFMQLRVGPNVTGPWGLIQPFADVFKLLFKEVTRPKLSNKALFYIGPIMSLAPSFAAWAVIPFNEEWVLTNINIGLLYILMITSLSVYGVIIAGWASNSKYSFLGAMRASAQSISYEIAMSAALVCVVMVSGSMNFSDIVAAQAKGIAGGSVFSWNWLPLFPIFIVYLISAVAETNRAPFDVAEGESEIVAGHHVEYSGFAFALFFLAEYIFMILIAALTSLMFLGGWLSPFPQSWGFIGTPSAFWMFVKMAAVLYWYLWIRATFPRYRYDQIMRLGWKVLIPIGFAYIVILGVWMISPLNLWK

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. a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex. Belongs to the complex I subunit 1 family.

Q5GXT9

MNELLLNLVDPLHQWFLGLGDGGVVLWSVLKILLIAVPVIVSVAFYVVWERKLIGWMHVRHGPMYVGMGIFQAFADVFKLLFKEILQPSSSHKAMFIIAPLLTLAPAFAAWSVVPFDAKLVLSNANVGLLYLLAMTSLGVYGIILAGWASNSKYAFLGAMRSAAQVVSYEIAMGFALVGVMIASGSVNLSQIVFAQAGNSGFFDWFLIPLFPLFIVYWVSGVAETNRAPFDVVEGESEIVAGHMVEYSGGAFALFFLAEYANMILVSFLISIFFLGGWLSPIQGWVNADISPWIDWLWKGGWPWLLMKVFFFASAYIWFRASFPRYRYDQIMRLGWKVFIPLTIVWIAVTALMVFYGVIQKGV

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. a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex. Belongs to the complex I subunit 1 family.

Q0BK41

MNWEMVIGLEVHIQLSTKSKLFSTSATKYGQHQNTQAAFLDLGLPGTLPVVNKEAIRKAVIFGLAVDAKISKDSFFARKNYFYPDLSKGYQISQSTNPIVQEGRLEIETSKGLKTIRIERAHLEEDAGKSVHGYIAGETGLDYNRAGTPLLEIVTYPDFRSAEEVVAYLKKLHQLVKHLGICDGNMQEGSFRCDVNLSIRPQGQAKFGTRAELKNINSFRFIDKAIEYEYARQVSVLESGGEVVQETRLYDADANETRSMRAKEDAFDYRYFPDPDLLPLVITDEYIESIKKQMPLKSEEREAVYREHLAEQEVEFLLSNLEIADYYDKVAVVIGYKPAYNWITVDLISTLNRAEKEFSSDVVPAEILLEIIANVQKDIISQANAKKVIAEYIDAPSAIEAIIEKLGLKQVSDEGMIRELVQGIIAANPQQAADFKAGKTKLMSFFVGQAMKASKGKANPKQVNQIVQEELNK

Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate Heterotrimer of A, B and C subunits. Belongs to the GatB/GatE family. GatB subfamily.

Q15X57

MDKKSARLRRATRARKKISELAAHRLVINRTPRHIYAQLIAPCGSQVLAAASTVEADLRTTVKSTGNAEAAVAVGKAIAERAIEKGIKTVAFDRSGFKYHGRVKALADAAREAGLQF

This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs. Belongs to the universal ribosomal protein uL18 family.

D4ATC3

MKFSSLAAATALVAGSVVAADLDPIVIKVGVRSALIPGWPKGGSKFFYKSNGTEFFMKGIAYQQEFSTNGTSSDKNNYQDPLADVESCRRDIPLMQQLQTNTIRVYAIDPKKDHKQCMKLLQDAGIYVVADLSEPSTSIIRDDPKWDDVLYTRYTSVVDELAQYSNVIGFFAGNEVSNNSTNTDASAFVKAAVRDMKAYIKQKNYRSMGVGYATNDDAEIRKDMTAYFNCNKQEESIDFWGYNIYSWCGDSSYTESGYDKVVEEFKTFNVPVFFAEYGCNEVQPRKFTEVQALYGDKMTPVVSGGIVYMYFQEENDYGLVKIEGGKPKKLPDFNSLQKQISKIKPSGVQMDSYKPTNTALSTCPKSSTWKASVKLPPTPNKDLCSCMVKSLSCVAKPSVTGKELGKLFGTVCGSDKDACKGITADATSGTYGAYSMCSPSEKLSFAFNQYYQHQSAKGNGANACDFGGAATAQKSEKPSGSCANLVDQAGQDGTGSVTSAPGSGGNKPDQGAASTISAPSVNLGIVKLGAYIFCAVLAGAGMILI

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis (By similarity). Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. Belongs to the glycosyl hydrolase 72 family.

Q24JX3

MSDHWRTISEEHRPHAPSRWSQGRKRCSDGKLRRHDDTDSTVFDTKPSEEPQARPDSFTTPESHKPVARCKDWGSAVEEDEQLREKVDQDIARYRRKLLINEFGRRERRSSSGSSDSKDSSTHGEMETDPAVITRRQKQINYGKNTIAYDRYIKAVPRHLREPNVHPRTPNKFKKYSRRSWDQQIRLWRIALHQWDPPAAEGSDLQPFMEEDMVCTETSSQENLFTGTPTKVRKVEADDAFDLEPCFIEEELLS

Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3' end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP) (PubMed:8957003, PubMed:9858606). Could play an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery. Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression (By similarity). Interacts with mif4gd. Nuclear (coiled bodies). Widely expressed. Very low levels in stage I oocytes, gradually increasing throughout oogenesis. Further increase is achieved during early embryogenesis. Phosphorylated on Thr-60 during mitosis. Belongs to the SLBP family.

Q9JPX9

MLMPKRVKFRREHRGKMRGRAKGGTEVHFGEYGLQALEASWITNRQIEAARIAMTRYMKRGGKVWIKIFPSKPYTAKPLEVRMGSGKGAPEGWVAVVKPGKVMFEISGVSEEVAREALRLASHKLPVKCKFVKREEVGGDANEN

Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL16 family.

Q820M6

MTIDYKKTLNLLDTSFPMRGDLARREPAMLKAWQERNLYRKIRAISQGRPKFILHDGPPYANGDIHIGHAVNKILKDIIIKSKTLSGFDAPYVPGWDCHGLPIEHQIEKKYGKHLPADQVRKLCRAFAQEQIDRQKADFMRLGVLGDWEHPYLTMNYAIEAGIIRALGKIFRNGHLYQGQKPVNWCIDCGSALAEAEVEYENKRSPAIDVGFEIIGRKDVCHPLAGVMAAEIPAGTRIFAVIWTTTPWTLPANQAVCVHPEFDYSLVSTSRGWLLLASELTNACLARYQLEGRVVATCKGLALEGLSLQHPFADRIVKVICGRHVTLEAGTGLVHTAPAHGLDDYFIGQQYGLPSDSPVKGDGKFSEQISLVGGMFVWKANDVVIDTLRSSGHLLHAEEIEHSYPHCWRHKTPIIFRATPQWFIGMQRQTAESQSFGESLRDLALRAVELTRFYPAWGRARLEAMIGNRPDWCISRQRNWGVPMTFFIHKEAHTLHPRTPELLEKVAGLVEQQGIEAWFSLDATELLGEEAQHYQKLTDTLDVWFDSGTTHETVLKQNIQLRHPADLYLEGSDQHRGWFQSSLLTGCAIDGCAPYTALLTHGFVVDGQGYKMSKSKGNVIAPQKIADTLGADILRLWVASTDYSGELSISDEILKRTVETYRRIRNTLRFLLANLADFNLAADALPPAEWVEIDRYMLAYTAALQNDLLGFYERYEFHQAVARLHHFCSEDLGGFYLDILKDRLYTSMANGIPRRSAQNALYHIVHSLVRLFAPVLSFTAEEVWQELGESAEDSVFLHTWHCFPDQSEILSDAQILIPRWQRLRELRARVLKQLEDARIQGEIGSSLAAIVEIHAAGEDFALLDSLGDDLRFVLITSEVHLQRVDDAAGEVIRVTASPHMKCERCWHYRQDVGSVPEHSSLCSRCVSNLAGSGEYRRFA

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile) Binds 1 zinc ion per subunit. Monomer. IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

O42665

MKFSSIPIASTLLSLLVASSVTASPLRRRDDPLNGRQFGLLALHSGNEYVHLHGFYVGDSGSVYLDPADGTDDAATFTMSNGQLSVGNRYASVSANGEIVFKSDTNSTSSGFSVGEAISSGYSLKYNGTESAVACPSLVNNQVYQVFFGVGNGNPSCVGIAVLAVLPQPISSSSTYNSTTSSYHNSTSTPPPTITSTKASTVTSTEATTVTTTTAVTVTATETYTVTATNGGSTITSTGASTVTSTQPSTVTSTQRKNTATTTKTTTYVGPSPSASSVVAYTTKCIVVPVITTAASQSEAATPSPSAAVYPLFPHGIRLIDSTKPEANSGNVYSPVVFQKQNNHTNTIFTFDVPQVSGSCELNFHLDTSGFPITVEGVNGTGRFILFNLSSVANDSTVYSNRPNRIAEIGRFNCSSSGCDYATNVTCPDSYTAVSYEMMALTDDSYLSFFEEADPLEGLTLRV

Belongs to the but2 family.

A5CW51

MSNDYYLIIPAGGIGTRMHSEKDNINRKIKIAKQYLKLDNGLTILDQTLKILLNIDQIKGCIIALANKDYLFTKSKFNNHSKLITTVIGGKKRMNSVFNGLKALTNLAKDDDWILVHDSVRPCVKASEIINLMNQLKHHETGGLLATKVVDTIKQASNNIVNTTIDRSNLWQAQTPQMYRFGVLLKALNTVINDGMNITDEASAIEYLRLKSVLVKSSKSNIKITNSEDLELANFYLTQYKE

Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.

Q8TEM2

MRSSLAPGVWFFRAFSRDSWFRGLILLLTFLIYACYHMSRKPISIVKSRLHQNCSEQIKPINDTHSLNDTMWCSWAPFDKDNYKELLGGVDNAFLIAYAIGMFISGVFGERLPLRYYLSAGMLLSGLFTSLFGLGYFWNIHELWYFVVIQVCNGLVQTTGWPSVVTCVGNWFGKGKRGFIMGIWNSHTSVGNILGSLIAGIWVNGQWGLSFIVPGIITAVMGVITFLFLIEHPEDVDCAPPQHHGEPAENQDNPEDPGNSPCSIRESGLETVAKCSKGPCEEPAAISFFGALRIPGVVEFSLCLLFAKLVSYTFLYWLPLYIANVAHFSAKEAGDLSTLFDVGGIIGGIVAGLVSDYTNGRATTCCVMLILAAPMMFLYNYIGQDGIASSIVMLIICGGLVNGPYALITTAVSADLGTHKSLKGNAKALSTVTAIIDGTGSIGAALGPLLAGLISPTGWNNVFYMLISADVLACLLLCRLVYKEILAWKVSLSRGSGYKEI

Inorganic phosphate and glucose-6-phosphate antiporter. May transport cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocate inorganic phosphate into the opposite direction. Independent of a lumenal glucose-6-phosphatase. May not play a role in homeostatic regulation of blood glucose levels. Inhibited by vanadate but not by chlorogenic acid. Detected in intestine and pancreas. Lower expression is also detected in liver and kidney. Belongs to the major facilitator superfamily. Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family. Extended N-terminus.

Q45715

MNSNRKNENEIINALSIPAVSNHSAQMDLSPDARIEDSLCVAEGNNIDPFVSASTVQTGISIAGRILGVLGVPFAGQLASFYSFLVGELWPSGRDPWEIFMEHVEQIVRQQQITDSVRDTAIARLEGLGRGYRSYQQALETWLDNRNDARSRSIIRERYIALELDITTAIPLFSIRNEEVPLLMVYAQAANLHLLLLRDASLFGSEWGMSSADVNQYYQEQIRYTEEYSNHCVQWYNTGLNRLRGTTAETWVRYNQFRRDLTLGVLDLVALFPSYDTRTYPIPTTAQLTREVYTDPNGVVAGPNNSWFRNGASFSAIENAIIRQPHLYDFLTNLTIYTRRSQVGTTIMNLWAGHRITFNRIQGGSTSEMVYGAITNPVSVSDIPFVNRDVYRTVSLAGGLGSLSGIRYGLTRVDFDMIFRNHPDIVTGLFYHPGHAGIATQVKDSDTELPPETTEQPNYRAFSHLLSHISMGPTTQDVPPVYSWTHQSADRTNTINSDRITQIPLVKAHTLQSGTTVVKGPGFTGGDILRRTSGGPFAFSNVNLDFNLSQRYRARIRYASTTNLRIYVTVAGERIFAGQFDKTMDAGAPLTFQSFSYATINTAFTFPERSSSLTIGADTFSSGNEVYVDRFELIQVTATFEAESDLERARKAVNALFTSTNPRGLKTDVTDYHIDQVSNLVECLSDEFCLDKKRELLEEVKYAKRLSDERNLLQDPTFTSISGQTDRGWIGSTGISIQGGDDIFKENYVRLPGTVDECYPTYLYQKIDESQLKSYTRYQLRGYIEDSQDLEIYLIRYNAKHETLSVPGTESPWPSSGVYPSGRCGEPNRCAPRIEWNPDLDCSCRYGEKCVHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHAKLGNLEFIEEKPLLGKALSRVKRAEKKWRDKYEKLQLETKRVYTEAKESVDALFVDSQYDKLQANTNIGIIHGADKQVHRIREPYLSELPVIPSINAAIFEELEGHIFKAYSLYDARNVIKNGDFNNGLSCWNVKGHVDVQQNHHRSVLVLSEWEAEVSQKVRVCPDRGYILRVTAYKEGYGEGCVTIHEFEDNTDVLKFRNFVEEEVYPNNTVTCNDYTTNQSAEGSTDACNSYNRGYEDGYENRYEPNPSAPVNYTPTYEEGMYTDTQGYNHCVSDRGYRNHTPLPAGYVTLELEYFPETEQVWIEIGETEGTFIVGSVELLLMEE

Promotes colloidosmotic lysis by binding to the midgut epithelial cells of insects. Selectively toxic to Artogeia rapae but not active on Plutella xylostella. The crystal protein is produced during sporulation and is accumulated both as an inclusion and as part of the spore coat. Toxic segment of the protein is located in the N-terminus. Belongs to the delta endotoxin family.

C6DFS2

MRHRKSGRQLNRNSSHRQAMFRNMASSLVRHEIIKTTLPKAKELRRVVEPLITLAKTDSVANRRLAFARTRDNEIVAKLFNELGPRFASRAGGYTRILKCGFRAGDNAPMAYIELVDRSVSQTEEVATAE

Part of the 50S ribosomal subunit. Contacts protein L32. Belongs to the bacterial ribosomal protein bL17 family.

A5DSN1

MSNSLLILGSTGLVGGQVVKFAQTSKDFSKIFTVTRRKPEFANTASTTESPRIDTIVETDSSKWPQAISNLEPAPLAYISAFGTTRANAGSAEKFKEIDYGINYESAKAAKEAGAKVCVLVSSYGANAKSPFLYMKTKGELENAIIDLKFPYTIILQPGVLLGERNESKGFGNDWAVKFGKLCKGTWFAPLLQPIEASDLGRIAVEFAERGLKGEFRENVLKVSGSELTELVDDFKIV

Belongs to the FMP52 family.

P35945

MAEEQAYHVNKGLECIKALRARPLDPLVVEEALAAWVETSEGQTLDRMSSDEAEADHQDISKPCFPAAGPGKSSMSRCHDQGLGGSNSCDEELGAFIGDSSMHSTEVQHYHVYDHSGEKVEGVEDADSILVQSGADDGVEVWGGDEESENSDVDSGEPDPEGSAPADWGSSPISPATRASDVETVEGDEIQKLLEDQSRIRKMTKAGKTLVVPPIPSQERPTASEKPIKKGTDVKSTSSGTMAESSSTGGATRPALKSQWGPSGPNASAENALASASNVSPTQGSKTESGTTTSRISQSNIEPEDDYDDELFSDIQDIKTALAKLHDDQQIIITRLESLVSLKGEIDSIKKQISKQNISISTIEGHLSSVMIAIPGFGKDPNDPTADVDINPDLRPIIGRDSGRALAEVLKKPASERQSKDTGKLGIESKGLLKKEFQLKPIEKKSSSAIRFVPDGSVASRSVIRSIIKSSHLGEDRKDYLMSLLNDIQGSKDLAQFHQMLVKILKN

Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis. Partially edited. RNA editing at this position consists of an insertion of one guanine nucleotide. The sequence displayed here is the P protein, derived from the unedited RNA. The edited RNA version gives rise to the V protein (AC P60169). Belongs to the morbillivirus P protein family.

A0A1D8PCL1

MSSKIERIFSGPALKINTYLDKLPKIYNVFFIASISTIAGMMFGFDISSMSAFIGAEHYMRYFNSPGSDIQGFITSSMALGSFFGSIASSFVSEPFGRRLSLLTCAFFWMVGAAIQSSVQNRAQLIIGRIISGIGVGFGSAVAPVYGAELAPRKIRGLIGGMFQFFVTLGIMIMFYLSFGLGHINGVASFRIAWGLQIVPGLCLFLGCFFIPESPRWLAKQGQWEAAEEIVAKIQAHGDRENPDVLIEISEIKDQLLLEESSKQIGYATLFTKKYIQRTFTAIFAQIWQQLTGMNVMMYYIVYIFQMAGYSGNSNLVASSIQYVINTCVTVPALYFIDKVGRRPLLIGGATMMMAFQFGLAGILGQYSIPWPDSGNDSVNIRIPEDNKSASKGAIACCYLFVASFAFTWGVGIWVYCAEIWGDNRVAQRGNAISTSANWILNFAIAMYTPTGFKNISWKTYIIYGVFCFAMATHVYFGFPETKGKRLEEIGQMWEERVPAWRSRSWQPTVPIASDAELARKMEVEHEEDKLMNEDSNSESRENQA

High-affinity glucose transporter (PubMed:10612724, PubMed:12187386). Acts as a multifunctional complement-evasion molecule that causes down-regulation of complement activation by acquisition of human complement factors FH and C4BP (PubMed:21844307). Functions also as a human immunodeficiency virus (HIV) receptor via binding the viral gp160 protein (PubMed:21844307). Modulates hyphae formation (PubMed:21844307). Interacts with the human complement factors FH and C4BP (PubMed:21844307). Binds also human immunodeficiency virus (HIV) protein gp160 (PubMed:21844307). Expressed in presence of 2 percent glucose (PubMed:12187386). Expression is induced by progesterone and drugs such as cycloheximide, benomyl and chloramphenicol (PubMed:10612724). Reduces the binding of human FH and C4Bp as well as of human immunodeficiency virus (HIV) gp160 protein onto C.albicans cell surface (PubMed:21844307). Reduces ability to form hyphae (PubMed:21844307). Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.

Q2UGK1

MSEGSNSTSAAASTQRQVRVQLTSKQEDIALPENTGPILVPTGLRRYALSTLVNNLLGNDKPIPFEFLINGSFLRTSIDEYLTANGISAETTLEIEYVRALIPPLHIASFEHDDWVSSVDVLSTTSPAASLASATIAAGQERILSGSYDGLLRVWNMSSQIVATSPSAADGGHTASIKAAKFISPNSIVSAGLDRTVRVWKYSEDGDGFSGKIAPQLELYGHKGPINSLSVHAPSNRILSASSDHSIGFWSTKKSDAPAAPEDLLPSAALRSSKRRKLNSSVTIPQRGPLALLSSHSAPVSAAIFDSNDSTVGYSASWDHSLRTWDLVTATLVDTRTTSHSLLSLEHLPEHHLLAAGTSARHITLIDPRVSATTIAAMTLRGHTNAVVSLARDPKSSYGLISGSHDGTCRIWDIRATKTDKDGVVGESVYSISRKSLEEQGKSEAKRIGGEGVKVFGVAWDGTVGIVSAGEDKRIQINRGEGVLSSA

Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. Component of the NOP7 complex, composed of erb1, nop7 and ytm1. The complex is held together by erb1, which interacts with nop7 via its N-terminal domain and with ytm1 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex associates with the 66S pre-ribosome. Interacts (via UBL domain) with mdn1 (via VWFA/MIDAS domain). Belongs to the WD repeat WDR12/YTM1 family.

C4K346

MEFKVNSECSEKQSSDCIVIGIFESGEFSPSAEKVNKISHGYLKGLPQNADLQGKAEQALLLHHVPHVAAERVLLIGCGKEEELDERRYKKLIKKMVNTLKETGAKNVFCYLPELKVKGKDIDWKIRSAIEVIQDALYCFDHYKSTKTLHALNQITFIVTATQTKAAQTAIQEGIALAVGINEAKNLANTPPNICNPAYLNASARKWAEKFKNVRVSVVNEDEMKKLGMNAYLAVGQGSKNESLMSIIEYKSGKIPAGTKPIVLVGKGMTFDSGGISIKPSQNMDEMKYDMCGAATVFGVMNVVAELNLPLYVIGVLAGAENMPGGNAYRPGDILTTLSGQTVEVLNTDAEGRLVLCDALTYVERFDPELVIDIATLTGACVVALGHHMSGLMSNHAPLAEDLLHASEQSGDLAWRLPLGEEYQEQLDSNFADMANIGGRTAGAITAGCFLSRFTHQYHWAHLDIAGTAWRTGKEKGATGRPVALLSQFLLNKALAQKQGA

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.

P60020

MEEPGAQCAPPPPAGSETWVPQANLSSAPSQNCSAKDYIYQDSISLPWKVLLVMLLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDFWLSSDITCCTASILHLCVIALDRYWAITDAVEYSAKRTPKRAAVMIALVWVFSISISLPPFFWRQAKAEEEVSECVVNTDHILYTVYSTVGAFYFPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSINSRVPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCTS

G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries (By similarity). Homodimer. Heterodimer with HTR1D (By similarity). Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. Phosphorylated. Palmitoylated. A residue in the 7th transmembrane region ('Thr-355' in human, 'Asn-351' in mouse and rat) is important for species-specific sensitivity to various agonists. Belongs to the G-protein coupled receptor 1 family.

Q9L639

MKKNHLVKYLLISPSLPVGGFCYSEGLESYLKIKNLEEPDHIRNLITNELKIGQIRIEAKCLIEFFDIFVELKIANNINKNRRRLLSLDKWLLSFRDTVEIRDQQTQMAKSLFELTKEFGFEYLYEKNKNISWSLAWSWACFSFQINKLEMIENFIYAWTANQLSAAIRLIPMGSIKAQTIQLELLDLISEVSQEIVDSNINDLYVGNISLSMAQQNHNDLYTKLFRN

Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel. Belongs to the UreF family.

Q21HN6

MIEQDRIIDANAKSREEQIDRAVRPKSLKEYIGQPVVREQMEIFIGAAQARGDSLDHTLVFGPPGLGKTTLANIIAAEMGADLKSTSGPVLEKAGDLAALMTNLEPGDVLFIDEIHRLSPVVEEILYPAMEDFQLDIMIGEGPAARSIKLELPPFTLVGATTRAGLLTSPLRDRFGIVQRLEFYNIEDLTHIVERSASLMGVAMDTPGAREVAKRSRGTPRIANRLLRRVRDYAEVKSDGTVTAQIADLALNMLNVDEHGFDHMDRRLLLTLIEKFGGGPVGVDSLAAAISEERDTIEDVLEPYLIQQGFIMRTPRGRMATQLAYQHFGLNVPAALKQDSLPGI

The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. ATP + H2O = ADP + H(+) + phosphate Forms a complex with RuvA. Belongs to the RuvB family.

Q47AM7

MGSFSIWHWLIVLVIVMLIFGTKKLRNVGQDLGGAVKGFKDGMKEANADKPAEEAQPTQQVGGHTIDVEVKEKTKS

Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. The Tat system comprises two distinct complexes: a TatABC complex, containing multiple copies of TatA, TatB and TatC subunits, and a separate TatA complex, containing only TatA subunits. Substrates initially bind to the TatABC complex, which probably triggers association of the separate TatA complex to form the active translocon. Belongs to the TatA/E family.

B7J6R6

MKISAFDIRPGNILEYEKGLWRVLKTDFVKPGKGGAFVQVEMKNIETGTKSNTRFRSGEAMEKAVVEPRTMQYLYADATGYVFMDNENFEQLILSEDLLEGQTGYLLPNTEIQVNLHNERPIGVELPPVVILEVREAEPSIKGQTATGSYKSAQMETGITVMVPQFVNAGEKIRVNTVDGSYIDRA

Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-33 is required for alleviation. Protein biosynthesis; polypeptide chain elongation. May be beta-lysylated on the epsilon-amino group of Lys-33 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC (if this protein is present). Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety may extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. Hydroxylation of the C5 position on Lys-33 may allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA. Belongs to the elongation factor P family.

A7H643

MAKKSMIAKAARKPKFKVRAYTRCQICGRPHSVYRDFGICRVCLRKMGNEGLIPGLKKASW

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. Binds 1 zinc ion per subunit. Part of the 30S ribosomal subunit. Contacts proteins S3 and S10. Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.

B8D9F8

MLNPIVRKFQYGQHTITLETGVIARQANAAVMASMDETAVFVTVVGQKKIHTGQKFFPLTVNYQERTYAAGRIPGGFFRREGRPSENEILTARLIDRPLRPLFPKKFLNEIQIIATVVSVNPQINPDIISIIGASAALSLSGIPFYGPVGAARVGYINNQYILNPISDDMKNSSLDLVVSGTQNAILMVEAESKILSEEKILGAIIFGHQQQQVVINNIRSLSNEASKLPWVISYPETNKTLELKIINSFEKNISDAYVIFNKQDRIEKLNSIKENIIKLFLDENSNIDTLEIEDIFQKIEKKVVRKRILSNQTRIDGREKDMIRALDVRTGILPRTHGSALFTRGETQSLVSVTLGTSRDAQNLDELLGDRIDNFLFHYNFPPYSVGEIGMVGSPKRREIGHGRLAKRSLLAVMPTLENFPYTIRVVSEITESNGSSSMASVCGASLALMDAGVPIKSAVAGISMGLVKEGNQHVLLSDILGDEDHLGDMDFKVAGTEEGITALQMDMKIEGITNEIIHSALNEARLARLHILNVMNQALNESRSEISEFAPRIHIIKINPEKIKDVIGKGGSVIRMLTEETGTIIEIEDDGTVKISSTVKEKAKNAIRRIKEITAEIEVGRIYSGKVTRIVDFGAFVSIGLGKEGLVHISQISDKRVDKVSNHLKIDQIISVKVLEIDRQGRLRLSIKEIDSSILSNKSINNSII

Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n) Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Belongs to the polyribonucleotide nucleotidyltransferase family.

Q8AVI4

MSSSAGKDKEPKVSSGTKEREKEAKAVGPVKESKDKDLKSKVKDAKEGKRDPVGAQAGVAFSLDNTIKRANPASGMRKKASNAEVIKELSKCREENSTRLDLAKKSIHMLPVSIKDLTQITELYLYGNKLQSLPAEVGNLVNLVKLALSENSLTSLPDSLDNLKKLCMLDLRHNKLREIPPVVYRLSSLTTLFLRFNRITAVEKDLKMLPKLTMLSIRENKIKHLPAEIGELCNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAVPRSLSKCSELDELNLENNNISTLPEGLLSSLVKVNSLTLARNCFQSYPVGGPSQFSSIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSIEVLILSNNLLKKLPHGIGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV

Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of raf1 kinase and stimulate raf1 activity at specialized signaling complexes (By similarity). Belongs to the SHOC2 family.

Q5F682

MARVCKVTGKRPMSGNNVSHANNKTKRRFLPNLQSRRFWVESENRWVRLRVSNAALRTIDKVGIDVVLADLRARGEA

Belongs to the bacterial ribosomal protein bL28 family.

Q31HD4

MQILQVKKQLVLTSRLKDLGHLPLKALSSETGEIFVAMDPVGTKDGDWVFTIANSAARDAAGDKRLLTDLTVGGIIDDWQPKQK

Probably forms vertices in the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. Has been modeled to induce curvature upon insertion into an otherwise flat hexagonal layer of major carboxysome subunits. Homopentamer. This bacterium makes alpha-type carboxysomes. The tight homopentamer forms a pore with an opening of about 3.5 Angstroms in diameter which is positively charged. Belongs to the CcmL/EutN family. CsoS4 subfamily.

C0RG67

MANTPSAKKAVRKIAARTEINKSRRSRVRTFVRKLEDALLSGDKQAAEVAFKAVEPELMRAASKGVVHKNTAARKVSRLAKRVKALNA

Binds directly to 16S ribosomal RNA. Belongs to the bacterial ribosomal protein bS20 family.

Q9S3P4

MKKNTLSAILMTLFLFISCNNSGKGGDSASTNPADESAKGPNLTEISKKITDSNAFVLAVKEVETLVLSIDELAKKAIGQKIDNNNGLAALNNQNGSLLAGAYAISTLITEKLSKLKNLEELKTEIAKAKKCSEEFTNKLKSGHADLGKQDATDDHAKAAILKTHATTDKGAKEFKDLFESVEGLLKAAQVALTNSVKELTSPVVAESPKKP

Not known; major immunodominant protein. In at least some strains (20004, B31, IPA2, not represented here) this gene is encoded on a 26 kb circular plasmid, so it is possible this is also encoded on a plasmid in the strains given here.

A9MUB9

MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp) Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.

B5F8E4

MIIYLHGFDSNSPGNHEKVLQLQFIDPDVRLVSYSTRHPKHDMQHLLKEVDKMLQLNVDERPLICGVGLGGYWAERIGFLCDIRQVVFNPNLFPYENMEGKIDRPEEYADIATKCVTNFREKNRDRCLVILSRHDEALDSQRSAQALHPFYEIVWDEEQTHKFKNISPHLQRIKAFKTLG

Belongs to the UPF0227 family.

Q7VDK9

MANSSPVYDWFQERLEIQDIADDVTSKYVPPHVNIFYCLGGITLVCFLIQFATGFAMTFYYKPTVTEAYNSVSYLMTDVSFGWLIRSVHRWSASMMVLMLILHVFRVYLTGGFKRPRELTWVTGVVMAVITVAFGVTGYSLPWDQVGYWAVKIVSGVPAAIPVVGDFMVELLRGGESVGQTTLTRFYSLHTFVLPWTLAIFMLMHFLMIRKQGISGPL

Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently. The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer. Heme 1 (or BH or b566) is high-potential and absorbs at about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs at about 562 nm. Belongs to the cytochrome b family. PetB subfamily.

A6QLD5

MDEMPEPPAMTVHLLANAGQGLLLQQTLDQLLDCICPDIRLFLVSERASPVKYYDKCHSKRSRFPGMSVLLFLKENLGEERLFHVLDSLQHWPWQCYPTQNAQGRPCPYILANQEFYSLDSQMPIWGVRQVHCGTEILRVTLYCSFDNYEDAIRLYAMILQREATLQKSNFCFFVLYSTETFALQLSLKQLPLGTSVDPKEASVLQFKVQEIGQLVPLLPHPCVPISRTRWQTQDYDGNKILLQVQLNPGLGVRNGEPPFLNGTLGADTLPHGSRLTPVSAIRTLELRSRRIRGRRFKVSSVELPEPGGRPVSDGSSNTWWKSAGGSAQPSSPATESQPQLSSLHLEPGARMKVLGRENSFEKLEAETNVDTGFTMVSSEPRPSFASRFPRNLQTHQPPSCLSTSFSGSAASKNNRIFKERVHPLPLAGQRDLGAKKILSKCPLPLPVQGEAKEAEEEFFI

Interacts with CHD7 and CHD8. Belongs to the FAM124 family.

Q6L1Y6

MEDYDLVIIGAGPTGLFATFLAGLRDIKSITLEALDYVGGQIPELYPEKPVYDVQGIPKINAIKLRDQMYEQAKTFNNRIELNSKVTDIIKENDIFKIEVNGVYKYNARAVLLCTGIGDFTPRKIGCEGEDRFFNKGLTYTVKDTEKFRDLTVAVVGGGDSALDYATELANTARHVYIIHHSENFKAAEKTIDLARKNEKITFIVNSSVISIDGGSKLESIKIKNELTNDISELGLDALVVAIGHVGRANIYKSLPLQLSPNKRGVLVNSKLETNIPGIYAAGDVASVEGEPANPLIAIGGAQAYQAINYIKKYINPQASFFGGHSSNLKI

H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin] Binds 1 FAD per subunit. Homodimer. Belongs to the ferredoxin--NADP reductase type 2 family.

P06945

MEEFVIPVFSERDIPYSLLNHYPLAIQIDVKVDDEGGKHNLIKIPESDMIDVPRLSIIEALNYRPKRNDGVVVPRLLDITLRAYDNRKSAKNAKGVEFMTDTKWMKWAIDDKMDIQPLKVTLDNHCSVNHQLFNCIVKARSANADTIYYDYYPLENGAKRCNHTNLDLLRSLTTTEMFHILQGAAYALKTTYELVAHSERENMSESYQVGTQRWIQLRKGTKIGYRGQPYERFISSLVQVIIKGKIPDEIRTEIAELNRIKDEWKNAAYDRTEIRALELCKILSAIGRKMLDVQEEPKDEMALSTRFQFKLDEKFIRTDQEHVNIFKVGGSATDDGRFYALIAIAGTDTQQGRVWRTNPYPCLRGALIAAECELGDVYFTLRQTYKWSLRPEYGQRERPLEDNKYVFARLNLFDTNLAVGDEIIHWRYEVYQPKETTHDDGYICVSQKGDDELLCEVDEDRYKEMFDRMIQGGWDQERFKLHNILTEPNLLTIDFEKDAYLGARSELVFPPYYDKWINSPMFNARLKIARGEIATWKADDPWSNRAVHGYIKTSAESLEYALGPYYDLRLQLFGDTLSLGQRQSAVFEHMAQQDDFSTLTDYTKGRTVCPHSGGTFYTFRKVALIILSNYERLDPSLHEGREHETYMHPAVNDVFRRHVLEMKDFSQLICFVFDYIFEKHVQLRNAKEARRIIYLIQNTSGAYRLDVLREAFPNFLKHVMNLRDVKRICDLNVINFFPLLFLVQDNISYWHRQWSIPMILFDQVIRLIPVEVGAYANRFGLKSFFNFIRFHPGDSKKRQDADDTHKEFGSICFEYYTTTKISQGEIDVPVVTSKLDTLKLHVASLCAGLADSLVYTLPVAHPKKSIVLIIVGDDKLEPQIRSEQIVNKYYYSRRHISGVVSICVNQGGQLKVHSMGITRHRICDKSILKYKCKVVLVRMPGHVFGNDELMTKLLNV

The VP2 protein is one of the two proteins (with VP5) which constitute the virus particle outer capsid. It is the major target of the host immunogenic response. Responsible for viral attachment to target host cell, probably by binding to sialic acid. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity). Belongs to the orbivirus VP2 family.

P21031

MNTRTDVTNDNIDKNPTKRGDRNIPGRNERFNDQNRFNNDRPRPKPRLQPNQPPKQDNKCREENGDFINIRLCAYEKEYCNDGYLSPAYYMLKQVDDEEMSCWSELSSLVRSRKAVGFPLLKAAKRISHGSMLYFEQLKNSKVVKLTPQVKCLNDTVIFQTVVILYSMYKRGIYSNEFCFDLVSIPRTNIVFSVNQLMFNICTDILVVLSICGNRLYRTNLPQSCYLNFIHGHETIARRGYEHSNYFFEWLIKNHISLLTKQTMDILKVKKKYATGAPVNRLLEPGTLVYVPKEDYYFIGISLTDVSISDNVRVLFSTDGIVLEIEDFNIKHLFMAGEMFVRSQSSTIIV

Might be required for transcription of early genes. Localizes in cytoplasmic virus factories and present in the virion core. Belongs to the poxviridae L3 family.