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SwissProtCLAP_random_10k

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A3N1V2

MPLLSQMQEYQADTTFAQLEALRQKLREYEYHYHVLDNPLVPDAEYDRLMNELKNLEWQHPEWITVDSPTQRVGAKPLDGFAQVTHEIPMLSLDNAFSDEELDGFLRRMESYITEDPHTLAFCCEPKLDGLAVSILYVDGVLSQAATRGDGSTGEDITSNIRTIRNIPLKLNMDNPPARLEVRGEVFMPQKGFEELNERALEKGEKTFANPRNAAAGSLRQLDPKITRQRPLVLNAYGIGVYESDDELPATHFERLQWLKSIGIPVNNEIRLATGREQLLAFYANIQAKRPTLGYDIDGTVLKVNDIGLQEQLGFISRSPRWAIAYKFPSQEEMTVLNDVEFQVGRTGAITPVAKLEPVFVAGVTVSNATLHNGDEIERLGIVIGDTVIIRRAGDVIPQIVGVVMDRRPENAKKIEFPTACPVCESAVVRVEGEAVARCTGGLFCGAQRKEALKHFVSRKAMDIDGVGEKLIEQLMERELVHTPADLFKLDHTTLMRLERMGEKSAQNALNSIEKAKNTTLARFLFALGIRDVGEATAQNLANHFHNLAAIRTATFEQLQAVQDVGEVVANRIVRFWQEPHNVAVVEDLISQGVHWQDVIQVEIADNPLKGKNVVLTGTLTQLTRDQAKALLQSFGCKVSGSVSSKTDYLIAGEKAGSKLAKAQELGVKILTEQEFIALTGEN

DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide. Belongs to the NAD-dependent DNA ligase family. LigA subfamily.

Q5L0U8

MQKAVVMDEQAIRRALTRIAHEIIERNKGIDGCVLVGIKTRGIYLARRLAERIEQIEGASVPVGELDITLYRDDLTVKTDDHEPLVKGTNVPFPVTERNVILVDDVLFTGRTVRAAMDAVMDLGRPARIQLAVLVDRGHRELPIRADFVGKNVPTSRSELIVVELSEVDGIDQVSIHEK

Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil Homodimer and homohexamer; in equilibrium. Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.

P39858

MKILITGTAGFIGSHLAKKLIKQGHYVIGVDSINDYYSVSLKEDRLKSIGKENFTFNKVKLENYDDLSKVFVDEQPEVVVNLAAQAGVRYSIENPRTYIDSNIVGFMNILECSRHFNIQNLIYASSSSVYGANTSKPFSTSDNIDHPLSLYAATKKSNELMAHTYSHLYNLPTTGLRFFTVYGPWGRPDMALFKFTKAIVNDQAIDVYNHGNMMRDFTYVDDIVEAISRLVKKPASPNKEWSGADPDPGSSYAPYKVYNIGNNSPVRLMEFVEAIENKLGKEARKNYMDLQPGDVPETYANVDDLFRDIDFKPETTIQDGVNKFVDWYLEYYKK

Required for the biosynthesis of type 1 capsular polysaccharide. Capsule biogenesis; capsule polysaccharide biosynthesis. Belongs to the NAD(P)-dependent epimerase/dehydratase family.

Q82VM2

MTRLLFVLVLSVCLLPVPVKASAVKSLKTFVNKALTFQANFSQTLLDKNFQVIRKASGSMMFERPGKFRWTYDQPYQQLIVGDGKQVWFYDQDLAQVTVHRLDQALGSTPAALLAGGNTIERDFNLQEIDVQGETEWLEAIPKNQENSFELIRLGFSKTGILREMVLRDSFDQVTWLIFSEIEQNPTLTPDLFQFTPPEGVDVIRD

Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). Monomer. Belongs to the LolA family.

A4SWE1

MAKEELLEMEGLVDEILPDSRYRITLDNGHKLIAYTAGRVKKNHIRILAGDKVSLEVSPYDLSKGRITFRHIDKKQSFAGAPYRRH

One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly. Belongs to the IF-1 family.

Q9T2U5

MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (PubMed:17570365, PubMed:12923572, PubMed:17895376, PubMed:25851905). Interacts with PPIF (PubMed:19801635). Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP synthase and enhances neurons metabolic efficiency. Interacts with CLN5 and PPT1 (By similarity). Interacts with S100A1; this interaction increases F1-ATPase activity (By similarity). Interacts with MTLN (By similarity). Interacts with TTC5/STRAP; the interaction results in decreased mitochondrial ATP production (By similarity). Belongs to the ATPase alpha/beta chains family.

O18087

MKITFSPELSIPCEVCKNQSNGYHFEVLSCGACASFFRRSVVSKIKYQCKDGKKRCQIRYLDRHFCRYCRFSKCVKAGMKAEKIQKNRDLDSSPTPTDQNNCIPSDVLHDDGILIKDIRGLFKQFNPHNASEGCSKLEKLTEGLQFIRRNQERECIKIIDEMDSESLKDVQFKVIGSCATWLLFSSFFQKLEENEKVVILERLWHGWTVLEFLSRSLEIFGNKVIDEKIVFISDNTAIRLITAFENSLKTASPKKSESIKKKLELSFSVIFDELALHFINWKPTEIEISYMQWQIVWSVAEQLLSGNSLEKGEHFTEQLSKDLHEYYVRELKLENYAFRIEKMMDIVQIVQNNFY

Orphan nuclear receptor (Probable). May play a role in modulation of lifespan and immunity (PubMed:29748542). Transcription up-regulated in response to intestinal colonization by probiotic Lactobacillus fermentum strain JDFM216. Belongs to the nuclear hormone receptor family.

Q71RD2

MGAPHWWDQLQAGSSEVDWCEDNYTIVPAIAEFYNTISNVLFFILPPICMCLFRQYATCFNSGIYLIWTLLVVVGIGSVYFHATLSFLGQMLDELAVLWVLMCALAMWFPRRYLPKIFRNDRGRFKVVVSVLSAVTTCLAFVKPAINNISLMTLGVPCTALLIAELKRCDNMRVFKLGLFSGLWWTLALFCWISDRAFCELLSSFNFPYLHCMWHILICLAAYLGCVCFAYFDAASEIPEQGPVIKFWPNEKWAFIGVPYVSLLCANKKSSVKIT

Golgi ceramidase that catalyzes the hydrolysis of ceramides into sphingoid bases like sphingosine and free fatty acids at alkaline pH (PubMed:16940153, PubMed:18945876, PubMed:20207939, PubMed:20089856). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (PubMed:20207939). Has a better catalytic efficiency towards unsaturated long-chain ceramides, including C18:1-, C20:1- and C24:1-ceramides (PubMed:16940153, PubMed:18945876, PubMed:20207939, PubMed:20089856). Saturated long-chain ceramides and unsaturated very long-chain ceramides are also good substrates, whereas saturated very long-chain ceramides and short-chain ceramides are poor substrates (PubMed:20089856). Also hydrolyzes dihydroceramides to produce dihydrosphingosine (PubMed:20207939, PubMed:20628055). It is the ceramidase that controls the levels of circulating sphingosine-1-phosphate and dihydrosphingosine-1-phosphate in plasma through their production by hematopoietic cells (By similarity). Regulates cell proliferation, autophagy and apoptosis by the production of sphingosine and sphingosine-1-phosphate (PubMed:16940153, PubMed:26943039, PubMed:28294157, PubMed:29229990). As part of a p53/TP53-dependent pathway, promotes for instance autophagy and apoptosis in response to DNA damage (PubMed:26943039, PubMed:28294157, PubMed:29229990). Through the production of sphingosine, may also regulate the function of the Golgi complex and regulate the glycosylation of proteins (PubMed:18945876). H2O + N-(15Z-tetracosenoyl)-sphing-4-enine = (15Z)-tetracosenoate + sphing-4-enine H2O + N-eicosanoyl-sphing-4-enine = eicosanoate + sphing-4-enine H2O + N-octadecanoylsphing-4-enine = octadecanoate + sphing-4-enine H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-enine H2O + N-tetradecanoylsphing-4-enine = sphing-4-enine + tetradecanoate H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-enine H2O + N-tetracosanoyl-sphing-4-enine = sphing-4-enine + tetracosanoate H2O + N-(hexanoyl)sphing-4-enine = hexanoate + sphing-4-enine H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate + sphing-4-enine an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine an N-acylsphinganine + H2O = a fatty acid + sphinganine Specifically activated by lumenal, but not cytosolic Ca(2+). Inhibited by Zn(2+) or Cu(2+). Mg(2+) or Mn(2+) have no effect on ceramidase activity (PubMed:20089856). Inhibited by De-MAPP (PubMed:20207939). Optimum pH is 7.5-9.0. Lipid metabolism; sphingolipid metabolism. Highly expressed in placenta. Up-regulated upon serum deprivation (PubMed:16940153). Up-regulated by N-(4-hydroxyphenyl)retinamode/4-HPR (PubMed:20628055). Up-regulated upon DNA damage, in a p53/TP53-dependent manner, resulting in increased levels of sphingosine and sphingosine-1-phosphate (at protein level) (PubMed:26943039, PubMed:28294157, PubMed:29229990). Belongs to the alkaline ceramidase family.

Q2RCG8

MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGKWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCLETMEVVQQTRVDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMDKEEIEITTHFQRKRRVRDNMTKKMVTQRTIGKKKQRVNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLAMITYITKNQPEWFRNILSIAPIMFSNKMARLGKGYMFESKRMKLRTQIPAEMLASIDLKYFNESTRKKIEKIRPLLIDGTASLSPGMMMGMFNMLSTVLGVSILNLGQKKYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKKKSYINKTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFELKKLWEQTQSKAGLLVSDGGPNLYNIRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVMPAHGPAKSMEYDAVATTHSWIPKRNRSILNTSQRGILEDEQMYQKCCNLFEKFFPSSSYRRPVGISSMVEAMVSRARIDARIDFESGRIKKEEFSEIMKICSTIEELRRQK

RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs. a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA. Interacts (via N-terminus) with PA (via C-terminus). Interacts (via C-terminus) with PB2 (via N-terminus); this interaction is essential for transcription initiation. Phosphorylated by host PRKCA. Belongs to the influenza viruses polymerase PB1 family.

V5IN15

MAGGKGKSSGGKSSGGKTSGVEGPKKQQSHSARAGLQFPCGRVKRFLKQNTQNKMRVGAKAAVYVTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELDTLIRATIAFGGVLPHINRALLLKVEQKKKAKAQEA

Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received. Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins. Required for the RNA polymerase II and spt15/TBP recruitment to the target genes. Involved in chromosome stability (By similarity). The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. H2A or its variant H2A.Z forms a heterodimer with H2B. H2A.Z associates with the vps72/swc2 subunit of the SWR1 chromatin remodeling complex. Interacts also with rpo-9/rpb1/DNA-directed RNA polymerase II largest subunit (By similarity). Acetylated once deposited into chromatin. Belongs to the histone H2A family.

Q8XCB8

MSGFYHKHFLKLLDFTPAELNSLLQLAAKLKADKKSGKEEAKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWNGLTNEFHPTQLLADLLTMQEHLPGKPFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLVAPQACWPEAALVTECRALAQQNGGNITLTEDVAKGVEGADFIYTDVWVSMGEAKEKWAERIALLRDYQVNSKMMQLTGNPEVKFLHCLPAFHDDQTTLGKKMAEEFGLHGGMEVTDEVFESAASIVFDQAENRMHTIKAVMVATLSK

Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3. Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.

B4SWR4

MSFDIAKYPTLALVDSTQELRLLPKESLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDQLIWDVGHQAYPHKILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGIAVAAEKEGKDRRTVCVIGDGAITAGMAFEAMNHAGDIRPDMLVILNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVPPIKELLKRTEEHIKGMVVPGTLFEELGFNYIGPVDGHDVMGLISTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDPSSGCLPKSSGGLPGYSKIFGDWLCETAAKDSKLMAITPAMREGSGMVEFSRKFPDRYFDVAIAEQHAVTFAAGLAIGGYKPVVAIYSTFLQRAYDQVIHDVAIQKLPVMFAIDRAGIVGADGQTHQGAFDLSYLRCIPDMVIMTPSDENECRQMLFTGYHYNDGPTAVRYPRGNAQGVALTPLEKLPIGKGLVKRHGEKLAILNFGTLMPEAAKVAEALNATLVDMRFVKPLDDTLILEMAAQHDALVTLEENAIMGGAGSGVNEVLMAHRKPVPVLNIGLPDFFIPQGTQEEARAELGLDAAGIEAKIKAWLA

Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2 Binds 1 Mg(2+) ion per subunit. Binds 1 thiamine pyrophosphate per subunit. Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1. Homodimer. Belongs to the transketolase family. DXPS subfamily.

B5ZPM3

MAAGDFRLCDVVLDDTIGRSTPDVEHERAVAIFDLIEENSFAPIGHAGGPYRLNISLVDSKLVFAIRTEEGIDVATHILSLTPFRRIVKDYFMICESYYEAIRSATPSRIEAIDMGRRGIHNEGSQTLKDRLTGKIEVDFDTARRLFTLVCVLYWRG

Belongs to the UPF0262 family.

P58082

MTELVLNPGAVPLAEWKAIYRGASARLAESAWPVIAESAAAVQRILAKGEPVYGINTGFGKLASVRIGDADLETLQRNIVLSHAAGVGEPSPVPVIRLMMALKLASLAQGASGVRVETVRMLEEMLVEGLTPVVPCQGSVGASGDLAPLSHMAATMIGVGEIFVGGQRLPAAQALAQAGLEPLTLGPKEGLALLNGTQFSTANALAGLFEAERLFQSALVTGALSTEAAKGSDTPFDPRIHTLRRHVGQIETAAALRALMSASEIRASHLKEDERVQDPYCLRCQPQVMGAALDILRQAATTLATEANCVSDNPLIFPEADEALSGGNFHAEPVAFAADMIALAVCEIGSIAERRIAMLVDPALSGLPAFLTPKPGLNSGFMIPQVTAAALVSENKQRAYPASVDSIPTSANQEDHVSMAAHGARRLLAMVENADAVLGIELLAAAQGCDFHAPLRSSAALEAVRALTRSKVPHLSDDRHFHPDMEAANTLVRSGAVIAAVGALPGVTA

L-histidine = NH4(+) + trans-urocanate Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. Belongs to the PAL/histidase family.

A8GW95

MNLPIVKGEYRKDYNLKHLTWFKVGGNAEIFFKPVDSEDLASFLVQNKQKLPITTFGAGSNIIIRDGGIEGVTIKLGQNFSNIGFTDDGHLIVGSSCLNFSLAKFCQVNAISGFEFLVGIPGTIGGGVAMNAGAYGCEFKDILVRIEAIDFAGNFRTFTNEEIGFKYRGNNLPKDLIILKAVFKVNKGNSEDILARMNEINAARSSTQPIKERTGGSTFANPEGFKSWQLIDKAGLRGYRIGDASISELHCNFMINNGNATAKELEDLGNFVQQKVFEDSGIKLNWEIKRIGKVSSRAWLDHGIQRKIIK

Cell wall formation. NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the MurB family.

Q8C056

MFLWLFLIVSALISSTNADSDISVEICNVCSCVSVENVLYVNCEKVSVYRPNQLKPPWSNFYHLNFQNNFLNILYPNTFVNFSHAVSLHLGNNKLQNIEGGAFLGLSALKQLHLNNNELKILRADTFLGIENLEYLQADYNLIKYIERGAFNKLHKLKVLILNDNLISFLPDNIFRFASLTHLDIRGNRIQKLPYIGVLEHIGRVVELQLEDNPWNCSCDLLPLKAWLENMPYNIYIGEAICETPSDLYGRLLKETNKQELCPMGTGSDFDVRILPPSQQENGFTTPNGHTTQTTLHRLVTKPPKTTNPSKISGIVAGKALSNRNLSQIVSYQTRVPPLTPCPVPCFCKTHPSDLGLSVNCQEKNIQSMSELTPKPLNAKKLHVNGNNIKDVDISDFTEFEGLDLLHLGSNQITLIKGEVFHNLTNLRRLYLNGNQIERLYPEIFSGLHNLQYLYLEYNLIKEILAGTFDSMPNLQLLYLNNNLLKSLPVYIFSGAPLARLNLRNNKFMYLPVSGVLDQLQSLTQIDLEGNPWDCTCDLVALKLWLEKLNDGIVVKELKCETPVQFANIELKSLKNEILCPKLLNKPSATFTSPAPAITFTTPLGPIRSPPGGPVPLSILILSILVVLILTVFVAFCLLVFVLRRNKKPTVKHEGLGNSECGSMQLQLRKHDHKTNKKDGLSTEAFIPQTIEQMSKSHTCGLKESETGFMFSDPPGQKVMMRNAADKDKDLLHVDTRKRLSTIDELDELFPSRDSNVFIQNFLESKKEYNSIGVSGFEIRYPEKQQDKKNKKSLIGGNHSKIVVEQRKSEYFELKAKLQSSPDYLQVLEEQTALNKI

It is involved in synaptogenesis and promotes synapse differentiation (By similarity). Suppresses neurite outgrowth (PubMed:14550773). Interacts (via LRR 1 and 2 repeats) with PTPRD (via extracellular domain). In the adult, significant expression is detected only in the brain. Broadly expressed in embryonic brain with highest expression in subventricular zone, subplate, cortical plate, pyramidal cell layer of hippocampus, thalamus and hypothalamus. In the embryo, expressed from day 10-12 and continues through later gestational development and into adulthood. Belongs to the SLITRK family.

Q47CR9

MLELVKVLGLFAITALAEIIGCYLPWLVLTQQRPVWLLIPAAVSLGLFAWLLTLHPGAAGRIYAAYGGVYVAIALIWLWRIDGVVPTRWDLVGSAVSLAGMAIIMLQPARSV

Belongs to the UPF0060 family.

Q2IHD7

MKLPQAFYARDTRTVARALLGKVLVHLDGGVRRAARIVETEAYHGPDDRASHARAGPTPRAAIMFGPPGRAYVYLIYGTSHCMNVVTGPEGFPSAVLIRAAEPIEGCLHSTRGPGNLCRALAIRREHDNGRDLWGEELFIEDAPAPREAVVTGPRVNVGYAGPWAARPWRFALRGSAWVSRPAPAGARAARAPAPAPRPRRPRGSGP

Belongs to the DNA glycosylase MPG family.

B7MG25

MIWLTLVFASLLSVAGQLCQKQATCFAAVNKRRKHIVLWLGLALACLGLAMVLWLLVLQNVPVGIAYPMLSLNFVWVTLAAVKLWHEPVSLRHWCGVAFIIGGIVILGSTV

Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Heterodimer of ArnE and ArnF. Belongs to the ArnE family.

Q5ZS09

MKVSKLWLREWVNFSLTEQELAEQLTMAGLEVDAVNPVAGQFTHVIVAEVLDTKPHPDADKLTLCEVNINKDKPLKIVCGAANVRPGLRVALAMIGAHLPGGLQIKESKLRGELSQGMLCSATELGLAEHSEGIMELSDEAPIGMDLREYLALDDHVFDIDLTPNRADCFSILGVAREVAVLNKLPLIEQPIVTVPPAIDDGLRVNLIHSEACPRYCGRIIRNLNLEAKTPLWMAERLRRGGIRTLHPVVDVMNYVMLELGQPMHAFDLAKINGEINVRYGVSGEQLELLDGQEVVLNDNVLVIADKEKPLAMAGIMGGANSAVQEQTQHVFLESAYFNPVTIAGVARKYGLFSDSSQRFERGVDPCLQSKALERATELILSISGGEAGPVIESFDKKFLPGTVSFLFDTTKVKKLTGLSIPLNEMKNLLEGLGVVIIKETNHFFEVTIPSHRVDLQQDADLVEEIIRLYGYDKLQAQPMQTSVQAGLISAKEKIATHVSSWFSAKGYHETISYSFVDPELQEALYPQKEFMELLNPISSELSQMRAGMWPGLIASMIYNSHRQQTAVKFFEIGVVFDLDGGQLKERSCIAGLLMGEQGNLNWSESARLFDFYDLKGDLQSLFASLKLDDVEFIQSSHHALHPGQSAQIVINGKHSGWIGVLHPRLSDAFDLDQDVVLFELNLESLINPTIPLYKPISKYPQIRRDLSFLVDRQISAMQIERVIRNTVKEDWLKSFDVFDVYMGKGIPEDKKSIAVAMTLQDDTRTLVDAEINLTISAIIKKLENEFSILLRE

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe) Binds 2 magnesium ions per tetramer. Tetramer of two alpha and two beta subunits. Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.

Q47422

MNELRRRWQVMSQRERLMALACGGLVVLCLLYYLIWAPWQESVRQWQMTVERERQTVRWMQQQPPRFRRRKVRGGRXPVAISANGIGAQSAVRYGITVLRMQPQESQVSVTLARSDFNNLLHWLAELEQKNGVITQGIDVTAVPNSPGIVEVTRLSLERVL

Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in the complex assembly and recruits OutL resulting in a stable complex in the inner membrane (By similarity). Provides thus a link between the energy-providing OutE protein in the cytoplasm and the rest of the T2SS machinery (PubMed:11266368). Type II secretion system is composed of four main components: the outer membrane complex, the inner membrane complex, the cytoplasmic secretion ATPase and the periplasm-spanning pseudopilus (By similarity). Forms homodimers (By similarity). Interacts with OutL/GspL (PubMed:11266368). Interacts with OutE/GspE and OutF/GspF (By similarity). Belongs to the GSP M family.

A1US94

MTRIVDIVGREVLDSRGNPTVEVDVYLENGVFGRSAVPSGASTGAHEAVELRDGGKRYQGKGVEKAVAAINGEIFKELGGRDARNQLAIDQAMIALDGTSNKERLGANAILGVSLSVAKAAAKSFGLPLYRYIGGTQAHLLPTPMMNIINGGAHADNPIDFQEFMIIPVGAPTFKEAVRYGAEIFHTLKRYLQDAGYNTNVGDEGGFAPNLKSAEQAINLIMESITSCGYKPGEQIAIGLDCASTEFYKNSLYAYEGEGKCRDVKEQVEYLAHLVDSYPIITIEDGMAEDDWAGWKQLTQAIGNKCQLVGDDLFVTNSARLRDGIKMGAANSILIKVNQIGTLSETLDAIETAHKAGYRAIISHRSGETEDSFIADLTVATNCGQIKTGSLARSDRLAKYNQLIRIEEMLGTQARYEGNWHRR

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. Belongs to the enolase family.

P20215

MSKEVLEKELFEMLDEDVRELLSLIHEIKIDRITGNMDKQKLGKAYFQVQKIEAELYQLIKVS

This protein may be involved in virus assembly. Homodimer.

B8DE31

MPNIKSAIKRVKTAETRNSRNASQRSAMRTAIKKFDEAAANNADNAKDLYVEASKKLDSAVSKGLIHKNNAARNKSRLAAKLAK

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

Q14D09

MGATGLGFLLSWRQDNLNGTDCQGCNILYFSETTGSMCSELSLNRGLEARRKKDLKDSFLWRYGKVGCISLPLREMTAWINPPQISEIFQGYHQRVHGADALSLQTNSLRSRLSSQCLGQSFLLRTLERGRGFRALGDICGHVHEED

Expressed in testis. Detected in spermatocytes, spermatids and spermatozoa (at protein level). PRY has multiple identical or highly similar copies on chromosome Y, some of which might be non functional pseudogenes.

Q97WC7

MEWNYVIPGIPDNLFERDEEIPMTKEEIRALALSKLRIKKGDKVLDIGCGTGSITVEASLLVGNSGRVYGIDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPAILSTINEKFDRIFIGGGSEKIKEIISASWEIINKGGRIVIDAILLETVNNALSAMEKIGFVNLEITEVIIAKGMKTKVGTAMMARNPIFIISGEKP

Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7. Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10. Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.

Q7A4V3

MAVNLYDYANQLEQALRESEEYKAIKEAFANVKANEESKKLFDEFRETQINFQQKQMQGEEIAEEDLQKAQEQAQAIEKDENISALMNAEQKMSQVFQEINQIIVKPLDEIYAD

Belongs to the UPF0342 family.

Q9WVK3

MGSWKSGQSYLAAGLLQNQVAVVTGGATGIGKAISRELLHLGCNVVIASRKLDRLTAAVDELRASQPPSSSTQVTAIQCNIRKEEEVNNLVKSTLAKYGKINFLVNNAGGQFMAPAEDITAKGWQAVIETNLTGTFYMCKAVYNSWMKDHGGSIVNIIVLLNNGFPTAAHSGAARAGVYNLTKTMALTWASSGVRINCVAPGTIYSQTAVDNYGELGQTMFEMAFENIPAKRVGLPEEISPLVCFLLSPAASFITGQLINVDGGQALYTRNFTIPDHDNWPVGAGDSSFIKKVKESLKKQARL

Participates in chain elongation of fatty acids. Catalyzes the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1 to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA reductase activity. a (2E)-enoyl-CoA + H(+) + NADPH = a 2,3-saturated acyl-CoA + NADP(+) (2E)-hexenoyl-CoA + H(+) + NADPH = hexanoyl-CoA + NADP(+) (2E)-octenoyl-CoA + H(+) + NADPH = NADP(+) + octanoyl-CoA (2E)-decenoyl-CoA + H(+) + NADPH = decanoyl-CoA + NADP(+) (2E)-dodecenoyl-CoA + H(+) + NADPH = dodecanoyl-CoA + NADP(+) (2E)-tetradecenoyl-CoA + H(+) + NADPH = NADP(+) + tetradecanoyl-CoA Lipid metabolism; fatty acid biosynthesis. Interacts with PEX5, probably required to target it into peroxisomes. Highly expressed in liver and kidney. Weakly expressed in other tissues. Up-regulated by fasting. Belongs to the short-chain dehydrogenases/reductases (SDR) family.

O49232

MTMAISSALPSPLLLAASLLLLIVQAQGITRHYEFNVQMANATRLCNTKSMVTVNGQCPGPELVAREGDRVVIRVTNNVAHNISLHWHGVRQVRTGWADGPAYITQCPIQTGQSYVYNFTVAGQRGTLWWHAHISWLRATVYGALVILPKLGVPYPFPAPHKEVPVIFGEWWNADTEEVVNQAVQTGGGPNVSDAFTINGLPGPLYNCSAQDTFKLKVKPGKTYMLRLINAALNEELFFAVANHTLTVVEVDAVYVKPFTVDTLVISPGQTTNVLLTAKPYYPGANFYMSAAPYSTARPGTFGNTTVAGILEYENPAMSPSAASFVKGLPLFKPTLPQLNDTDFVTNFTDKLRSLATPEYPAAVPQSVDKRFFFTVGLGTLPCPANMTCQGPNNTQMAASMNNVSFVLPARALLQSHFTGLSSGVYAPDFPVAPLSPFNYTGTPPNNTNVKTGTKLLVLRYNTSVELVMQDTSILGIESHPLHLHGFNFFVIGQGFGNYDAVNDPAKFNLVDPVERNTVGVPAGGWVAIRFLADNPGVWFMHCHLEAHTTWGLRMAWLVLDGSHPNQKLLPPPSDLPKC

Lignin degradation and detoxification of lignin-derived products. 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O Binds 4 Cu cations per monomer. Belongs to the multicopper oxidase family.

Q8C472

MDSLYVEEVAASLVREFLSRKGLNKTFVTMDQERPRCELSINSRNDLRKVLHLEFLYKENKAKEKPLRTNLELITRYFLDNVGNTDNSESQEVPIPAIPVPKKNNKLPLRHSETTLVNIYDLSDEDTGRRTSWSEAGKARHDSLDGDILGNFVSSKKPSHKSKAAHVDLGDSLPLVPAWEKVDQLHSSEPGIDVKKTMERTRPKSGLIVRGMMAGPVASSPQDSFRKRSLRRSSALSRKLQTPEEIQQQSEPFVHTPAYLGPQEVPDSSSDSVSRSPLGQLNELSIEKPNVTSSSQGLSQRDRPRLRSVSEDSPLGYSHTEGNSRMAQDQLERAFKRQGVQPPSLRKNQLVSDRTDDKPDALQLEDVEDELIKEDIVLFPPPSMLKLQTVSKPIDLSLAKEIKTLLFGSTFCCFSEEWKLQNFSFNDIASLKYGIVQNKGGPCGVLAAVQGCVLQKLLFEGDNRTNSNLRLQPSDAQRTRCLALAIADILWRAGGKEQAVVALASGTPHFSPTGKYKADGVLETLTLYSLTSSEDLVTFIQQSVHQFEAGPYGCILLTLSAILSRSLELVRQDFDVPTSHLIGAHGYCTQELVNLLLTGRAVSNVFNDVVELDSGDGNITLLRGIEARSDIGFLSLFEHYNVCQVGCFLKTPRFPIWVVCSESHFSILFSLQPELLCDWRSERLFDLYYYDGLANQQEEIRLTVDTTKTAPADSCSDLVPPLELCIRTKWKGASVNWNGSDPIL

Probable hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins. Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Belongs to the MINDY deubiquitinase family. FAM188 subfamily.

Q9T390

MKGGRVQVITKNNSIAKHQLGEYAVHIYVLLYYLSMREILREFEEACLLQGLVSPSTRLLISCSGGQDSVTLLFLLCQLQTNWTWRLGVVYCNHMWRYGSIETPAKLARICLLFGVSCSFSVSGSRLQKEEEGRSWRLRVLCRMSSIHSWFYISTGHTASDRIETLLSNVLRGSSSSGMRSINWYTSLDTQVGHRRISIPIIRPLLGISRLELRNYANRWKLPLCYDPSNQDQRIRRNRIRHELLPYLRHWWNPQIDRLLAQTAEVTSWESSYYDLICTQICQQYEWIGDGGVRFPWRIFHSIPTSLHSRILWIFLNRALVFLNPAHGFQGNFDILQFLLETKTCHCRHGSIYISKDVDWLRMTLVK

Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2) The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding. Belongs to the tRNA(Ile)-lysidine synthase family.

Q55DX5

MSYPPNQGYPPQSNSPQPGQYGAPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQGYPPQQGYPPVGVPVGVPVGFAPGMVVGYHQGYFVGTITHDCKHDAEVLRKAMKGIGTNESDLIKVLANRNWAEREQIKREFSAKYSKDLIQDIKSETSGNFEKCLVALLTEPAHFDVEQIHSACAGAGTNENTIIEILVTRSNVQMEYIKQIFKNKHGKSLKDRLESEASGDFKKLLEKLTEPRDESPVINPMQVSKDAEDLYKAGEGKIGTDEKEFIKILTSRSLPHIAAVASEYIKHHKKHSLIKAIDSEFSGSIKTGLIAIVTYALNPYGYFAEILNKSMKGAGTNDNKLIRTVVTQMHNMPQIKTAYSTLFKNSLAHDIQADCSGDFKKLLLDIIS

Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family.

P84716

MKCLTKYSRVSETSQTCHVWQNLCFKKWQKGKKVSRGCTATCPKPKKDEVIQCCAKDKCNK

Expressed by the venom gland. Belongs to the snake three-finger toxin family. Short-chain subfamily. Orphan group III sub-subfamily.

Q0J361

MVSPDMIRNVVGIVGNVISFGLFLSPVPTFWQIIKNKNKNKKKMEVVLAAEALFMVSPDMIRNVVGIVGNVISFGLFLSPVPTFWQIIKNKNKNKKKMEVVLAAEALFMAAVALGVLLGVHTHQRRSLIVGILCVIFDTIMYSSPLTVMSQVVKTKSVEYMPLLLSVVSFLNGLYWTSYTLIRFDIFITIPNGLGVLFAAVQLILYVIYYRTTPKKQNKNLELPTVTPVAKDTSVGPISKDNDLNGSTASHVTIDITIQP

Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. Forms homooligomers and/or heterooligomers. Belongs to the SWEET sugar transporter family.

Q7M3C4

QRTNDFIKACGRELVRVWVEICGSVSWGRTA

Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. Heterodimer of a B chain and an A chain linked by two disulfide bonds. Belongs to the insulin family.

Q92ID4

MQYLISSLIFLIPSLGMLAGLSAAATVTIFLLISFLRGINRHCERLQGVWQSSNNVIPWLDHGIQKIQKDWIPLQAHGITMLFTAWCFISCLFAIHLINSLATFTQVFILLFLGFAVSNSAPFQNRLQLKKALIFGILTAILLFFIEYSSNGFLTRIFKTSFALYMLDRGCALLSITAWVAIIILLSNGKKRHTLMLYILVLYLLSISDSLASFLGFGIGGVIFILTRFMKPIFFKLIAISLITGSLLFPVIAKQIEPQDLSEKYLATQPSAAHRLFIWHFVANKIIEKPILGYGLASSKYIKAGDSEMIDYNGEKWHPLPLHPHNNILQITLELGIIGLILFLCLVYKYLKQISNLENKNFKAISYACFINYYIIGMISYNIWQIWWISSGIWVLVLMKLLVKPDIVIDN

Belongs to the O-antigen polymerase family.

Q05356

MSRRVVVTGIGVVAPGGIGAARFWDLLAGGRTATRRISLFDPARLRSQIAAECDFDPSAHGLDDETVRRCDRYVQFALVATAEAVRDAGLDTTREDPWRMGAVLGTAVGGTTRLEHDYVLVSEGGSRWDVDHRRAEPHLHRAFAPSTLASTVAETFGAQGPVQTVSTGCTSGLDAVGYAYHAIAEGRADVCLAGASDSPISPITMACFDAIKATSPSNDDPEHASRPFDARRNGFVMGEGGAVLVLEELEHARARGADVYCELAGYATFGNAHHMTGLTREGLEMARAIDTALDMARLDGTDIDYVNAHGSGTQQNDRHETAAVKRSLGEHAYRTPMSSIKSMVGHSLGAIGSIEVVACVLALAHQVVPPTANYETPDPECDLDYVPREARERELRSVLSVGSGFGGFQSAVVLTGPERRLR

Involved in developmentally regulated synthesis of a compound biosynthetically related to polyketide antibiotics which is essential for spore color in Streptomyces halstedii. Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.

Q89AH3

MRRMLINAIEIKKLRIALIDGQQLYDLNVENIDKKQRKSNIYKGKIVRIEPSLEAAFVDYGEKKNGFLPLKEISRNYFPNNCSNYRHLHIKNILKEGQECIVQIDKEERGTKGALLTTFISLAGNYLVLMPNCPHLEGISRKIEGIDRFHLKKIISMLMVPENMGIIIRTSGVGRSIETLQLDLNFRVKNWYTIKKSAEINTAPCLIHKESNIVIRTLRDYLKKDIQEIIVDNPEILELARDYMFNMNCSYFEKKIKLYTGSDPLFSYYKIESQINALLRRIVKLPSGGSIIIDYTEALTAIDINSSQSTKGVNIEETAFNTNYEAVREIARQLRLRDLGGLIVIDFIDMSVLKHQKMIELHLHQVLQKDRARVQVGSISQFGLLEMSRQCLGSPLKKINHNYLFEMQKC

Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs (By similarity). Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions. Binds 1 Mg(2+) ion per subunit. Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, RNase E assembles into a homotetramer formed by a dimer of dimers (By similarity). Belongs to the RNase E/G family. RNase E subfamily. This sequence is much shorter than orthologs.

Q10439

MSGYIRTLFIRNRFSNYRLRSQIIKYKYSNVSYLNKSALRCGQATDSTHPHILQPGELTPRISAQEYKTRRDRVASLLEDNDFMIVTSAPVRHMCGAAFYEYHQDPNFYYLTGCLEPNAVLLMFKNGASGSYDCSLYLPSKNPYIEKWEGLRTGSTLGKKLFQIENVYDSSLASSVINALGKKSNRIFYNYQTGYLSKMPAASAPEFIQDTLTKLFRTSTQRSVDELLHPLRSIKSTAELECMKEAANISSNVYREIMRKRFEKEAEMSAEFNYRFCIGGCDRSAYVPVVAGGKNGLTIHYTINNDIFRPDEMVLVDAGGEFGGYVTDISRTWPINGKFSTVQRDLYQAVLNVQKKCIKYCCTSNGWSLADIHFESVKLMHEELKQVGIHGTKREITDILYPHSIGHEIGLEIHDCSTNNGYQPLRKNQVITIEPGLYVPEEDGWPQWAQGIAIRIEDSVIVGDDKPFVLTSAAPKEIEEIEALKK

Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome. The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.

Q0VML3

MKSLLLGAIWLYQKVLSPWIGNQCRFYPTCSEYARQAVETHGSLRGSALAAKRLCKCHPWHPGGFDYVPGAVPGAEPDQEQHQCTPLCNHHSEDHSQ

Could be involved in insertion of integral membrane proteins into the membrane. Belongs to the UPF0161 family.

A4YBV6

MNPRRKKRLTLAVALIGGVAAIASLLLYALNSNLNLFYTPSEIVNGKTDTGVKPDVGQRIRVGGMVTVGSMVRDPDSLHVQFAVHDSLGGEILVTYDDLLPDLFREGQGIVAQGVLTAEGKLEATEVLAKHDENYMPPEVAEAMGQKHEKLDYSQQKAPDTK

Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. Belongs to the CcmE/CycJ family.

Q8LCM5

MFRVTGTLSAASSPAVAAASFSAALRLSITPTLAIASPPHLRWFSKFSRQFLGGRISSLRPRIPSPCPIRLSGFPALKMRASFSSGSSGSSASREILVQHLLVKNNDVELFAELQKKFLDGEEMSDLAAEYSICPSKKDGGILGWVKLGQMVPEFEEAAFKAELNQVVRCRTQFGLHLLQVLSEREPVKDIQVEELHSKMQDPVFMDEAQLIDVREPNEIEIASLPGFKVFPLRQFGTWAPDITSKLNPEKDTFVLCKVGGRSMQVANWLQSQGFKSVYNITGGIQAYSLKVDPSIPTY

Sequencing errors.

A6RLP9

MSIDLNWETLTTGPDGIALAERIRDFVHAKFQTVTLPRFIKGVKVHTFEFGSIAPEVELKDICDPLPDFYEDIDDDYVEDDEDEENSENSQTDEENEVAKTLRERRRLDRVERTANGSSHVSTPPAYIDTRYPGLRSMQASGDTGSPFLGVSTPGIPGGTSNLSYFHSQLASGLSGTQTPLAAVAGAHLPQGWPDRPSPSLHLSALRNQSHTPLSHTASERSMTPPQIADLNQQSLREKASVSTLAASSSTTRPATRDGVPEATIPEEHAGESEESTSPPRRFREPKVEDLQTVFRVRYSGNIRLSLTVDILLDYPMPSFVGIPVKLNITGLSFDGVAVLAYIRKRAHFCFLSPEDAYAAIGADEKDADASAGMKMGALLHEIKVESEIGQRENGKQVLKNVGKVEKFVLEQVRRIFEDEFVYPSFWTFLV

Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. A MMM1 homodimer associates with one molecule of MDM12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12 generate a continuous hydrophobic tunnel for phospholipid trafficking. The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers. Belongs to the MDM12 family.

Q6D5V7

MELPLGSDLARLVRVWRALVDHRLKPLELTQTHWVTLHNIYHLPPGQSQIQLAKAIGIEQPSLVRTLDQLEEKGLITRHVCAHDRRAKRIMLTESAEPIIQAVDGVISHTRSEVLFGITPEQVDELALLVARLEKNILALHENQA

Transcription regulator that can specifically activate or repress expression of target genes. Homodimer. Belongs to the SlyA family.

W0HFK8

MIPNITQLKTAALVMLFAGQALSGPVESRQASESIDAKFKAHGKKYLGNIADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKVYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGSLNALASAGTEEVAVTELDIAGASSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNPKEAYNAIAAAL

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Optimum pH is 5.0-6.0. Optimum temperature is 40 degrees Celsius. Glycan degradation; xylan degradation. Belongs to the glycosyl hydrolase 10 (cellulase F) family.

P17926

MYSSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMTKDEERAVKDELLSEKPEVKQKWASRLLAKLRKDIRPECREDFVLSITGKKPSCCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKAGQCTNPILCIQPHHISVSVKELDLYLAYFVRERDSEQSSSPRTGIASDQEDTKPNTLDSTDFQESFVTSGVFSVTELIQVSRTPVVTGTGPNFSLGELQGHLAYDLNPSSTGMRRTLPSTSSSGSKRHKSGSMEDDIDTSPGGEYYTSSNSPTSSSRNWTEDMEGGISPNVKTEMDKSPFNSPSPQDSSPRLSSFTQHHRPVIAVHSGIARSPHPSSTLHFPTTSILPQTASTYFPHTAIRYPPHLNPQDPLKDLVSLACDPSNQQPGPPTLHQARPLRTVPSWD

Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. Binds DNA as a homodimer. A number of isoforms are produced. The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Belongs to the CTF/NF-I family.

Q6XLL9

MNAKFILLLLVVATTMLLPDTQGAEVIKCRTPKDCAGPCRKQTGCPHGKCMNRTCRCNRCG

Blocker of voltage-gated potassium channels. Expressed by the venom gland. Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta). Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 06 subfamily.

A8M8F2

MLRTMLKSKIHRATVTQADLHYVGSVTVDQDLLDAADLLPGEQVAIVDINNGSRLETYVIPGKRGSGVIGINGAAAHLVHTGDLVILIAYGQMDDAEARAYQPRVVHVDSANQVIDLNADTSTAAAGTAGAPVPNPLADPA

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. H(+) + L-aspartate = beta-alanine + CO2 Binds 1 pyruvoyl group covalently per subunit. Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. Heterooctamer of four alpha and four beta subunits. Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. Belongs to the PanD family.

Q5FU33

MSASSTPRPVMLVILDGFGWREDESDNAVRLANTPTFDTLWATSPHAFLKTSGEDVGLPDGQMGNSEVGHLNIGAGRVVMQELPRISRSARDGSLAQNPALLEFIAALKASGGTCHLMGLISPGGVHAHQDHVVALTKIVSAAGVPVAVHIFSDGRDTAPRSGEDFIGKFLKELPDSVQIATLSGRYYAMDRDRRWERVALAVEAIRDAKGPHAKDALSALQASYASDKGDEFVLPTVLGDYAGMKDGDGILACNFRADRIRQLLDVLVLPDFTEYDSGRKVKFAAVCGMSRYSDHLAPYMSILFPKVPLDDLLGDVVAKAGRTQLRMAETEKYPHVTYFLNGGREVQFDGEERILVPSPKVATYDLQPEMSAPELTDKAVAAIESGKFDMIVLNFANPDMVGHTGSLSAAIKACETVDQGLGRINDAIVKAGGVLLVTADHGNCETMRDPVTGGAHTSHTLNVVPVILAHARGETIHDGRLADLAPTMLALMGVKQPDAMTGVSLLESA

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Binds 2 manganese ions per subunit. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Monomer. Belongs to the BPG-independent phosphoglycerate mutase family.

B3EFF5

MKINLDRTSSGFCIGVQGTIHVAEEKLAAKETLFSLGDVVHNEVEVKRLENLGLTTIDEAVFKELQNTSVLIRAHGEPPETYATAERNKLDITDTTCPVVSKLQRTARLLCQLGYQVIIYGKHTHPEVIGINGHCSNRAVIIKHADLSDPEELKTLDTTIKTALISQTTMDVPGFYELKTNLEKRFAESDETAGKPWTAIRDIDITAAMTGIGTMPRTVFKDTICRQVSSRNKKLHDFALANSCVIFVAGRKSSNGQVLFGICRSANPRSYFIEDIEDLEDSWFRDNEGSPVESIGICGATSTPMWLLEKVAEFIDGRFNHRDA

Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 1 [4Fe-4S] cluster per subunit. Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. Belongs to the IspH family.

Q254M8

MNKKLKVLLTNDDGIFAKGISLLVSNLLKADFADLYIVAPNTEQSGKSMSFSYTEPVSIERVDYHQPVAGAWAVSGSPVDCIKLALGDLFLDSLPDIVLSGINNGSNAGRNIFYSGTAGAAMEAVISGIPAIAFSQEEHISCFQEKKSCELIKMLVLYALSRPFPLLTGFNVNFPACENNEEWQGMKLVATGKEFAYGVPRLLCDDGKRKFYSLNDCQRLMDEDLSEECHSLLTKKITVAPLLVRNSPLGLMSEEEFQQLQQEFEDFIHSEIRS

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.

Q6KJJ9

MASTMTPYFGIVVSLIAYGIGTLLFKHSKGFFLFTPLFVAMVLGIVFLKVGNFTFEEYNTGGKMISFFLEPATIAFAIPLYKQVDKLKKYWWQILSAIVVGSICSVIVVFIVAKAIGLDTAVMNSMLPQAATTAIALPISESIGGIPAITSFAVIFNAVIVYALGALFLKTFRVKHPIAKGLALGTAGHALGVAVGIEMGEVEAAMASIAVTVVGVVTVVVIPMFMPFIG

Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses. Belongs to the CidB/LrgB family. LrgB subfamily.

Q480B3

MNLADKVLAVNNDLPIRTDSPVHSGKVRSVYWLTATDSKRLIEEKGYDVPSDTSLAIMVISDRISAFDCIWSGENDMRGVPGKGAALNAISNHWFKMFKEQGLADSHILDIPHPFVWIVQKAKPVMIEAICRQYITGSMWRSYTKGERDFCGIELPEGLAKDSKLTSLLQTPSTKGILEGIPGVPAVDDVNITRKNIEDNFEAFNFKSVDDIARYEKLLTEGFDVISTALSKIDQVFVDTKFEFGYVKDVNGDDKLIYMDEVGTPDSSRIWDGEQYRAGKVVENSKEGFRQLLLNHFPDADILLNKDRMSEREALARDNKLPLSVLMDVSKTYTDIAEKITGNKIVLSDNPKAEIIAILREQYQLID

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.

B5GS26

MSTRPVEGSAIWDVLSPHSPHAAAADGKTLVWVEAGELCGHDTAESANLARIRPGLLAAFCHPKATEDDLTLITKWMAWLFLLDDRIDESDLGRDADLLDGHLQDLQGVALGIRTASGPMSRALEEIITQASAGMGDAWQLRFRRNISDYLLACVWQAAHRQAGEFPDPEVFPHWRRAFGAIMPSFDLIERTDGGALPSCVYYSRPYQSLLTAAADLVCWTNDLMTVDKEAAHGDLHNLVLVTEHDRHQDRRTASAAVSAACEQRMRAHTSARRDLTGLTAALGLPDTVRTHADDCAASLLVWVRGHLEWGLETPRYRPGTTGTGTD

Catalyzes the conversion of (2E,6E)-farnesyl diphosphate into (-)-delta-cadinene. Cyclization mechanism involves an intermediate nerolidyl diphosphate leading to a helminthogermacradienyl cation. (2E,6E)-farnesyl diphosphate = (-)-delta-cadinene + diphosphate kcat is 0.00114 sec(-1). Belongs to the terpene synthase family.

J8G6Z1

MKMNPIVELFIKDFTKEVMEENAAIFAGAGLSMSVGYVSWAKLLEPIAQEIGLDVNKENDLVSLAQYYCNENQGNRGRINQIILDEFSRKVDLTENHKILARLPIHTYWTTNYDRLIEKALEEENKIADVKYTVKQLATTKVKRDAVVYKMHGDVEHPSEAVLIKDDYEKYSIKMDPYIKALSGDLVSKTFLFVGFSFTDPNLDYILSRVRSAYERDQRRHYCLIKKEERRPDELEADFEYRVRKQELFISDLSRFNIKTIVLNNYNEITEILQRIENNIKTKTVFLSGSAVEYNHWETEHAEQFIHQLSKELIRKDFNIVSGFGLGVGSFVINGVLEELYMNQGTIDDDRLILRPFPQGKKGEEQWDKYRRDMITRTGVSIFLYGNKIDKGQVVKAKGVQSEFNISFEQNNYVVPVGATGYIAKDLWNKVNEEFETYYPGADARMKKLFGELNNEALSIEELINTIIEFVEILSN

NAD(+) hydrolyzing component of antiviral defense system Thoeris, composed of ThsA and ThsB. Activated by a signal molecule generated by ThsB, by TIR1 and TIR2 from B.dafuensis or by BdTIR from B.distachyon. Upon activation binds and hydrolyzes NAD(+), leading to cell death and inhibition of phage replication. Not seen to bind DNA (PubMed:32499527, PubMed:34853457). Expression of ThsA and ThsB in B.subtilis (strain BEST7003) confers resistance to phages phi29, SBSphiC, SBSphiJ and SPO1 (PubMed:29371424, PubMed:34853457). At multiplicity of infection (MOI) of 0.05 Thoeris-encoding cultures grow normally when infected with SPO1, at MOI 5 cultures collapse prematurely by 90 minutes post-infection, thus the phage are not able to complete a replication cycle. NAD(+) levels fall and ADP-D-ribose levels rise 60 minutes post-infection. Thoeris cultures eventually recover, but retain the same susceptibility to SPO1 (PubMed:34853457). H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide Activated by a signal molecule generated by endogenous ThsB, by TIR1 (AC A0A5B8Z670) and TIR2 (AC A0A5B8Z260) of B.dafuensis, and by BdTIR (AC I1GTC2), a plant protein involved in defense (PubMed:34853457). Activation may alter the oligomerization state of the protein (PubMed:34853457) (Probable). kcat is 33.9 min(-1) (PubMed:32499527). Homotetramer formed by dimer of dimers; homooctamers are occasionally seen. Not seen to interact with ThsB (PubMed:32499527). In the absence of the signal generated by ThsB, 63% monomer and 20% homotetramer; in the presence of the ThsB signal product 40% of the protein is dimeric (PubMed:34853457). Has an N-terminal sirtuin-like domain (SIR2, residues 1-283) and a C-terminal SLOG (STALD)-like domain (residues 284-476) (PubMed:32499527). The SIR2 domain has NAD(+) hydrolase activity (PubMed:32499527, PubMed:34853457). The C-terminus probably drives oligomerization which activates the NADase activity of the N-terminus (PubMed:34853457) (Probable). When this gene is missing the Thoeris system does not confer phage resistance in B.subtilis. Belongs to the Thoeris B TIR-like family. Truncated N-terminus.

P97881

MSQSSGGTSTPTTTATQPTSTSTQTPGTTQLLSTTSTPTTTATQPTSTSTQTPGTTQLPSTTSTPTTTATQPTXTSTQTPGTTQLPGTTSTPTTTATQPTSTSFQTPGTTQLPSSTSTPTTTATQPTSTASQTPGTTQPPGGASSPTTTVTQPTGSSSQTPGTTQPPGGASTPTTTVTQPTGSSSQTSGTTQPPGGASSSTVTSSSSTGSNDPCNSNPCKSPASCVKLYDSYFCLCLEGYYYNNSSSCVKGTTFPGEIGMSVNETTDLEDKNSVNYQTLHSSVVKFFENTFKKTDYGQTVILKVSKDSLMSSRSVMRAATQTVYVSVVNMFGENTKEDEESVASVIKEAVKTDNNVERYFQQDRCDYYGCVKSGSNVCRNGLQCTCKPGLERLNPQVPFCVAPTCSEPCSAEKKQLCLKKDNGAMECGCMAGYRKANGKCEECPFGYSGMDCKDQFQLILTIVGTIAGAFILILLIVFIVSMRSKNKKKSGEEQNLIEDDFHNLRMRPTGFSNFGADTSIFPKVKTGVPSQTSNPYANHRSMPRPDY

Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling. Homodimer of beta subunits. Also exists as a soluble form. Cleaved into two subunits, alpha and beta, probably between the first EGF domain and the SEA domain. Beta subunit contains the cytoplasmic tail and alpha subunit the extracellular tail. The homooligomerization into dimers is dependent on intrachain disulfide bonds (By similarity). Highly glycosylated.

Q9XPJ8

MLNISKIFEEVKVMKNFTLNFGPQHPAAHGVLRLIVELESENVVRVEPHIGLLHRGTEKLIEGKTYTQALPYFDRLDYVSMNVQEHAYSLAVERLYLDSLDIELEIPQRAKVIRVLFSEITRVLNHIMATTTHAMDVGALTPFLWAFEEREKLMEFYERVSGARMHAAYIRPGGVAFDLPMNISEDIYKFVIQYRKRLEEIEDMLINNRIWKQRLVDIGIVSAEEALNYGFTGPLLRGAGIVYDIRKNYPYDDYDKYDFKIIIGEENNSYTRFIIRMKEMYQSLSIIEQALNNLRPGLIKLEGVNITAPDRAFVKKDMESCINHFKFFSEGFIIPANENYTIVEAPKGEFGIYLNANDTAKPYRCRIKAPGFLHLQGLNMMSKDHLLADVVTLIGTQDIVFGEVDR

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+) Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme. Belongs to the complex I 49 kDa subunit family.

B4E9J1

MQPPGGDAPAGCPFSGARAAQPAQAAHEAPHVPGEADAQAGWHNAQLDFSKSMSYGDYLSLNSILDAQHPLSPDHNEMLFIIQHQTSELWMKLALFELRGALDAVRTDALPPAFKMLARVSRILEQLVQAWNVLSTMTPSEYSAMRPYLGQSSGFQSYQYRQLEFLLGNKNAQMLQPHAHRPDILEQVRATLEAPSFYDEVVRLLARRGFPIAPERLERDWTQPMRHDETVEAAWLEVYRHPQQHWELYEMAEELVDLEDAFRQWRFRHVTTVERIIGFKQGTGGTSGAPYLRKMLDVVLFPELWHVRTTL

Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety. L-tryptophan + O2 = N-formyl-L-kynurenine Binds 1 heme group per subunit. Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. Homotetramer. Belongs to the tryptophan 2,3-dioxygenase family.

A0Q8G4

MRNITNFLKTFLLWELLKGLKVTGKHFFTRKVTVQYPDEKTPISNRFRGLHALRRYENGEERCIACKLCEVVCPALAITINSTEREDGTRRTSSYEIDLFKCIFCGYCEESCPVDSIVETNILEYHFEERGENIMTKAKLLAIGDKYEAQIAADRLQDKDFR

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. a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) Binds 2 [4Fe-4S] clusters per subunit. 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 23 kDa subunit family.

Q8TFF9

MDTPTWEVVAALKRNQVLNSIPKEWRKPNIRKEMISSGYVNTYEYLNLILPPEENAITNLSMLELATNIAKGNYTSYNVTKAFCHRAALAHQILNCCIEIFFDEALKKAKELDDVFQKTSKVVGPFHGIPISLKDQVDLPGKDSSIGYVSLVGKPKTEIALLAKILQDKGAIFYVKTTVPMAMMAPQTVSNLHGYTYNALNINLSSGGSSGGEGALLGSGASCCGIGTDIGGSIRIPSCFQGLYALKPSTGRISYLNVTNSYSGQELIPSVIGPMARSLKDIEFFTETVIASEAWKIDSKLLPIPWKNQSHLKSKKLIFGVLKTDGIVKPHPPIIRALNEVVAVLEKSGYEVIEISIPFQKDMLDTVVKVFSADARFEINNESQKTGEPVVSVVKRFVSDKIFKKPITVNEWWDLGNQVYKIRQMFLELWNNTAIQTLSGNSIDAIIAPIWASTSFLPESKADHLYTSLFNICDCPCVVFPFTKVDANIDLSDVSYKPLNEEDKENNDMYDPVLFDNMPVCLQVVTKKLEEEKCLAAASSIMDCLTN

a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+) Belongs to the amidase family.

C1B4A1

MSERATYAARRVLPDAPLLAAAEGRAPGRRPVWFMRQAGRSLPEYREIRSGIGMLESCFDPALVCEITMQPVRRHGVDAAILFSDIVVPLKAAGIDLDIVAGTGPVVANPVRSIADVAALPRLVPEEVGAVAQAVQLLTAELGSTPLIGFAGAPFTLASYLVEGGPSRNHERTKALMHSDPKTWHALLGTLADTTITFLQAQLRAGVDAIQLFDSWAGALSLAEYREFVLPHSERVFAEVESAKVPRIHFGVGTGELLGAMGEAGADVVGVDWRIPLDVAARRVGPGKALQGNLDPAVLFAGSAAVEKQVRRITAEADAALAAGATGHIFNLGHGVLPDTDPGALTALVELVHSL

Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. Homodimer. Belongs to the uroporphyrinogen decarboxylase family.

Q9L589

MARAVGIDLGTTNSVVAVLEGGDPVVVANSEGSRTTPSIVAFARNGEVLVGQPAKNQAVTNVDRTIRSVKRHMGTDWSIEIDGKKYTAQEISARVLMKLKRDAEAYLGEDITDAVITVPAYFNDAQRQATKEAGQIAGLNVLRIVNEPTAAALAYGLDKGEKEQTILVFDLGGGTFDVSLLEIGEGVVEVRATSGDNQLGGDDWDDRIVNWLVDKFKGTSGIDLTKDKMAMQRLREAAEKAKIELSSSQSTSINLPYITVDADKNPLFLDEQLTRAEFQRITQDLLDRTRQPFKSVIADAGISVSDIDHVVLVGGSTRMPAVTDLVKELTGGKEPNKGVNPDEVVAVGAALQAGVLKGEVKDVLLLDVTPLSLGIETKGGVMTKLIERNTTIPTKRSETFTTADDNQPSVQIQVYQGEREIAAHNKLLGSFELTGIPPAPRGVPQIEVTFDIDANGIVHVTAKDKGTGKENTIKIQEGSGLSKEEIDRMIKDAEAHAEEDRKRREEADVRNQAESLVYQTEKFVKDQREAEGGSKVPEETLSKVDAAIADAKTALGGTDITAIKSAMEKLGQESQALGQAIYEATQAESAQAGGPDGAAAGGGSGSADDVVDAEVVDDDRESK

Acts as a chaperone. By stress conditions e.g. heat shock (By similarity). Belongs to the heat shock protein 70 family.

Q2T9P5

MKRKCQDYESRLPDNTAVKQQQLPAFRLQLTASEILSGFFAIGLFCLGMGIILLLSAKSIKEVEINYTEKCATCAKLREEATNFDKECNCSISFYLPQKMEGNVYLYYKLYGFYQNLYRYILSRSNIQLVGADVKDVRNCAPFRTSDNGLPIAPCGAIANSMFNDTIVLWYNFNSSTHIRVPMVRTETAWWTDKYVKFQNPAFQNLSSAFAGTAKPPNWPKPVYELDENDPGNNGFINDDFIVWMRTAAFPNFKKLYRRLHRIGNFTEGLPAGSYSFIINYNFPVSRFQGQKAVVLSTLTWSGGSSLFLALAYLVTGAVTLLASFSMMALHLKLKERKTFFLQ

Belongs to the CDC50/LEM3 family.

P0DUD4

MGQILGKIMMSHQPQPQEERSPQRSTSGYPLQEVVDDEVLGPSAPGVDPSPPRRSLGWKRKRECLDESDDEPEKELAPEPEETWVAETLCGLKMKAKRRRVSLVLPEYYEAFNRLLEDPVIKRLLAWDKDLRVSDKYLLAMVIAYFSRAGLPSWQYQRIHFFLALYLANDMEEDDEAPKQNIFYFLYEETRSHIPLLSELWFQLCRYMNPRARKNCSQIALFRKYRFHFFCSMRCRAWVSLEELEEIQAYDPEHWVWARDRAHLS

Belongs to the Speedy/Ringo family. Could be the product of a pseudogene.

Q02353

MPALACLRRLCRHLSPQAVLFLLFVFCLFSVFVSAYYLYGWNRGLEPSADASESDCGDPPPVAPSRLLPIKPVQAVAPSRTDPLVLVFVESLYSQLGQEVVAILESSRFKYRTEIAPGKGDMPTLTDKGRGRFALIIYENILKYVNLDAWNRELLDKYCVAYGVGIIGFFKANENSLLSAQLKGFPLFLHSNLGLKDCSINPKSPLLYVTRPSEVEKGVLPGEDWTVFQSNHSTYEPVLLAKTRSSESIPHLGADAGLHAALHATVVQDLGLHDGIQRVLFGNNLNFWLHKLVFVDAVAFLTGKRLSLPLDRYILVDIDDIFVGKEGTRMKVEDVKALFDTQNELRTHIPNFTFNLGYSGKFFHTGTDAEDAGDDLLLSYVKEFWWFPHMWSHMQPHLFHNQSVLAEQMALNKKFAVEHGIPTDMGYAVAPHHSGVYPVHVQLYEAWKQVWNIRVTSTEEYPHLKPARYRRGFIHNGIMVLPRQTCGLFTHTIFYNEYPGGSSELDKIINGGELFLTVLLNPISVFMTHLSNYGNDRLGLYTFKHLVRFLHSWTNLRLQTLPPVQLAQKYFQIFSEEKDPLWQDPCEDKRHKDIWSKEKTCDRFPKLLIIGPQKTGTTALYLFLGMHPDLSSNYPSSETFEEIQFFNGHNYHKGIDWYMEFFPIPSNTTSDFYFEKSANYFDSEVAPRRAAALLPKAKVLTILINPADRAYSWYQHQRAHDDPVALKYTFHEVITAGPDASSKLRALQNRCLVPGWYATHIERWLSAFHANQILVLDGKLLRTEPAKVMDTVQKFLGVTSTVDYHKTLAFDPKKGFWCQLLEGGKTKCLGKSKGRKYPEMDLDSRAFLKDYYRDHNIELSKLLYKMGQTLPTWLREDLQNTR

Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate (PubMed:1379236, PubMed:3422231, PubMed:8483907, PubMed:9890952). Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis (PubMed:1379236, PubMed:3422231). Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response (By similarity). Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). H2O + N-acetyl-alpha-D-glucosaminyl-[heparan sulfate](n) = acetate + alpha-D-glucosaminyl-[heparan sulfate](n) 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) The deacetylase activity is specifically inhibited by N-Ethylmaleimide (PubMed:8483907). The sulfotransferase activity is specifically inhibited by 3',5'-ADP (PubMed:8483907). Glycan metabolism; heparan sulfate biosynthesis. Glycan metabolism; heparin biosynthesis. Monomer. Interacts with heparan sulfate co-polymerase subunits EXT1 and EXT2. The presence of 4 different heparan sulfate N-deacetylase/N-sulfotransferase enzymes in mammals, as well as differences in their enzyme activity suggest that some initiate heparan sulfate modification/sulfation reactions, whereas other later on fill in or extend already modified heparan sulfate sequences. Belongs to the sulfotransferase 1 family. NDST subfamily.

O28597

MDEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWNRYRPEELANPQAFAKDPEKVWKWYAWRMEKVFNAQPNKAHQAFAELERLGVLKCLITQNVDDLHERAGSRNVIHLHGSLRVVRCTSCNNSFEVESAPKIPPLPKCDKCGSLLRPGVVWFGEMLPPDVLDRAMREVERADVIIVAGTSAVVQPAASLPLIVKQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHVRKALS

NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription. H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide Binds 1 zinc ion per subunit. 2 residues (Tyr-64 and Arg-67) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity. The two SIR2 homologs in this organism, Af1 and Af2, display different substrate specificities in vitro. Af1 cannot deacetylate histones but does deacetylate BSA in a NAD-dependent manner (PubMed:11336676). Belongs to the sirtuin family. Class III subfamily.

A0JNA3

MADYLISGGTGYVPEDGLTAQQLFANADGLTYNDFLILPGFIDFTADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKIRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRNELVVAPAGVTLKEANEILQRSKKGKLPIVNDRDELVAIIARTDLKKNRDYPLASKDSHKQLLCGAAVGTREDDKYRLDLLTQAGADVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPVIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. H2O + IMP + NAD(+) = H(+) + NADH + XMP Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. Homotetramer. Belongs to the IMPDH/GMPR family. Extended N-terminus.

B2UB84

MSHAPFIAVIPARLASTRLPNKPLADIDGKPMVVRVAERAHQSSAARVVVATDAASVADACMQHHVEAVLTRADHASGTDRLAEVATVLGLPDDAIVVNVQGDEPLIAPTLIDNVAAHLRDHPDCAIATAAHPIHDPADVFNPNVVKVVLDAADRALLFSRAPLPWARDTWTPAVMAGSVAERPLPAMPVLRHIGIYAYRAGFLRRFPQLAAAPIEQTEQLEQLRAMWHGERIAVLTTDDAPAAGVDTPEDLTRVRAAWAELLAQDGP

Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Belongs to the KdsB family.

Q3SLR3

MTAPSLAPPRLIVGLGNPGRDYEETRHNAGFWFCARLAQAWGAALAHESRFHGIVGRHGTRWMLLPQTFMNRSGQAVGALARFHRIAPAEILVVHDELDIPPGQLRLKFGGGMGGHNGLKDITAHLGTQDYWRLRIGIGHPGDRSEVVNYVLKPPRREEQADIDAAIERALGLLPLIEKGEWNAATQRANSKPASPKSQETP

The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+) Monomer. Belongs to the PTH family.

A5U089

MATLADPRDIILAPVISEKSYGLLDDNVYTFLVRPDSNKTQIKIAVEKIFAVKVASVNTANRQGKRKRTRTGYGKRKSTKRAIVTLAPGSRPIDLFGAPA

One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. Part of the 50S ribosomal subunit. Contacts protein L29, and trigger factor when it is bound to the ribosome. Belongs to the universal ribosomal protein uL23 family.

B2IK67

MSKEKTPRSLGDNEAKAVARMLRVSPQKLNLVAQLIRGKKVDKALADLEFSRKRIAYDVKKTLESAIANAENNHSLDVDDLIVAEAFVGKAMVMKRFSPRARGRSGRIEKPFAHLTIVVREVTAVAAGA

This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL22 family.

A2SLD6

MSKDDVIQMQGEILENLPNATFRVKLENGHVVLGHISGKMRMHYIRILPGDKVTVELTPYDLSRARIVFRAK

One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly. Belongs to the IF-1 family.

B1IFW5

MRYLVDTHTHTIVSGHAYTTFLENVQEASNIGLKVLGTTDHGPSMPGGPNLFYFNNFKVMPRKLKGVTLLHGCEANIIDFKGMLDIPDFTQKKLDVIIASLHDVCIRPGSVEENTEALINVMENPYVDILGHIGNPSFPINEEVVVKKAKEKNVLIEINNGSFVSRKGSEETCKKVANLCKKHKVNIIVGSDSHVCFQIGRFPKADNMLKEIGMPEELIINNEENKILEYLKNKGKLKDLNLD

Binds 3 Zn(2+) ions per subunit. Belongs to the PHP family.

B6I1R2

MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKGE

Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the EPSP synthase family. MurA subfamily.

Q2U9B5

MIAIGLEGSANKLGVGIMLHPDNGNPPQVLANIRHTYVSPPGEGFLPKDTARHHRAWVVKLVKKALKEAHVSVQDVDCICFTKGPGMGAPLQSVAVAARMLSLLWGKELVGVNHCVGHIEMGRLITGSTNPVVLYVSGGNTQVIAYSSQRYRIFGETLDIAVGNCLDRFARTLHISNDPAPGYNIEQLAKKGKQLVDLPYTVKGMDCSFSGILAAVDGLATTYGLGGEGKDDETDTPIPDADGNGKPTRADLCFSLQETIFSMLVETTERAMAHVGSKEVLIVGGVGCNERLQEMMGIMARDRGGSVHATDERFCIDNGIMIAQAGLLAYSTGFRTPLKDSTCTQRFRTDDVFVKWRD

Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA Binds 1 divalent metal cation per subunit. Component of the EKC/KEOPS complex composed of at least bud32, cgi121, gon7, kae1 and pcc1; the whole complex dimerizes. Belongs to the KAE1 / TsaD family.

Q9SNK9

MGNQCQNGTLGSDYHNRFPREHAVGYVQGDSYLDLKKFDDTWPEVNNFKPTAASILRRGLDPTSINVLGRKTADLREHYIIGRKLGQGQFGTTYLCTEINTGCEYACKTIPKRKLITKEDVEDVRREIQIMHHLSGHKNVVAIKDVYEDGQAVHIVMELCAGGELFDRIQEKGHYSERKAAELIRIIVSIVAMCHSLGVMHRDLKPENFLLLDKDDDLSIKAIDFGLSVFFKPGQVFTELVGSPYYVAPEVLHKRYGPESDVWSAGVILYVLLSGVPPFWAETQQGIFDAVLKGHIDFQSDPWPKISDSAKDLIRKMLSHCPSERLKAHEVLRHPWICENGVATDQALDPSVISRLKQFSAMNKLKKLALRVIAERLSEEEIAGLREMFKAVDTKNRGVITFGELREGLRRFGAEFKDTEIGDIMEAAHNDNNVTIHYEEFIAATLPLNKIEREEHLLAAFTYFDKDGSGYITVDKLQRACGEHNMEDSLLEEIISEVDQNNDGQIDYAEFVAMMQGSNVGLGWQTMESSLNVALRDAPQVH

May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity). May be a signaling component in the response to gibberellin and cold stress (PubMed:15604699). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Activated by calcium. Autophosphorylation may play an important role in the regulation of the kinase activity. Expressed in roots (Ref.2). Expressed in leaf sheaths (Ref.2, PubMed:15604699). By gibberellin (Ref.2, PubMed:15604699). Induced by cold stress (Ref.2, PubMed:15604699, PubMed:26681628). Down-regulated by brassinosteroid, abscisic acid (ABA), and drought or cold stresses (PubMed:15604699). There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (343-373) inactivates kinase activity under calcium-free conditions. Plants over-expressing CPK7 show increased recovery rates after cold stress. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily.

Q9Y6V2

MAFTNYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDADATRIDIYAERREDLRGGFMLCFLDDGAGMDPSDAASVIQFGKSAKRTPESTQIGQYGNGLKSGSMRIGKDFILFTKKEDTMTCLFLSRTFHEEEGIDEVIVPLPTWNARTREPVTDNVEKFAIETELIYKYSPFRTEEEVMTQFMKIPGDSGTLVIIFNLKLMDNGEPELDIISNPRDIQMAETSPEGTKPERRSFRAYAAVLYIDPRMRIFIHGHKVQTKRLSCCLYKPRMYKYTSSRFKTRAEQEVKKAEHVARIAEEKAREAESKARTLEVRLGGDLTRDSRVMLRQVQNRAITLRREADVKKRIKEAKQRALKEPKELNFVFGVNIEHRDLDGMFIYNCSRLIKMYEKVGPQLEGGMACGGVVGVVDVPYLVLEPTHNKQDFADAKEYRHLLRAMGEHLAQYWKDIAIAQRGIIKFWDEFGYLSANWNQPPSSELRYKRRRAMEIPTTIQCDLCLKWRTLPFQLSSVEKDYPDTWVCSMNPDPEQDRCEASEQKQKVPLGTFRKDMKTQEEKQKQLTEKIRQQQEKLEALQKTTPIRSQADLKKLPLEVTTRPSTEEPVRRPQRPRSPPLPAVIRNAPSRPPSLPTPRPASQPRKAPVISSTPKLPALAAREEASTSRLLQPPEAPRKPANTLVKTASRPAPLVQQLSPSLLPNSKSPREVPSPKVIKTPVVKKTESPIKLSPATPSRKRSVAVSDEEEVEEEAERRKERCKRGRFVVKEEKKDSNELSDSAGEEDSADLKRAQKDKGLHVEVRVNREWYTGRVTAVEVGKHVVRWKVKFDYVPTDTTPRDRWVEKGSEDVRLMKPPSPEHQSLDTQQEGGEEEVGPVAQQAIAVAEPSTSECLRIEPDTTALSTNHETIDLLVQILRNCLRYFLPPSFPISKKQLSAMNSDELISFPLKEYFKQYEVGLQNLCNSYQSRADSRAKASEESLRTSERKLRETEEKLQKLRTNIVALLQKVQEDIDINTDDELDAYIEDLITKGD

Essential for epigenetic silencing by the HUSH (human silencing hub) complex. Recruited by HUSH to target site in heterochromatin, the ATPase activity and homodimerization are critical for HUSH-mediated silencing (PubMed:28581500, PubMed:29440755,PubMed:32693025). Represses germ cell-related genes and L1 retrotransposons in collaboration with SETDB1 and the HUSH complex, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). During DNA damage response, regulates chromatin remodeling through ATP hydrolysis. Upon DNA damage, is phosphorylated by PAK1, both colocalize to chromatin and induce H2AX expression. ATPase activity is required and dependent of phosphorylation by PAK1 and presence of DNA (PubMed:23260667). Recruits histone deacetylases, such as HDAC4, to promoter regions, causing local histone H3 deacetylation and transcriptional repression of genes such as CA9 (PubMed:20225202, PubMed:20110259). Exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY, possibly preventing its dephosphorylation (PubMed:24286864). ATP + H2O = ADP + H(+) + phosphate ATPase activity is dependent of phosphorylation by PAK1 and presence of DNA. Homodimerizes upon ATP-binding and dissociate upon ATP hydrolysis; homodimerization is required for gene silencing (PubMed:29440755). Interacts with HDAC4 (PubMed:20110259). Interacts with ACLY (PubMed:24286864). Interacts with TASOR and MPHOSPH8; the interactions associate MORC2 with the HUSH complex which recruits MORC2 to heterochromatic loci (PubMed:28581500). Mainly located in the nucleus (PubMed:20225202). Upon phosphorylation at Ser-739, recruited to damaged chromatin (PubMed:23260667). Highly expressed in smooth muscle, pancreas and testis. Phosphorylated by PAK1 at Ser-739 upon DNA damage. Phosphorylation is required for ATPase activity and recruitment to damaged chromatin. 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. Intron retention.

Q6K3K2

MPPRCRRLPLLFILLLAVRPLSAAAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPHPNHRRRHLFYKVLGGVLGGMVLLGLVVVGSAVLLGRSVRRKNQEHAVASEDMGEATLSMEVARAATKGFDSGNVIGVGGSGATVYEGVLPSGSRVAVKRFQAIGSCTKAFDSELKAMLNCPHHPNLVPLAGWCRSKDELVLVYEFMPNGNLDSALHTLGGATLPWEARFRAVYGVASALAYLHDECENRIIHRDVKSSNVMLDAEFNARLGDFGLARTVSHGGLPLTTQPAGTLGYLAPEYVHTGVATERSDVYSFGVLALEVATGRRPAERGISVVNWVWTLWGRRRLVDAADRRLQGRFVADEMRRVLLVGLCCVHPDCRKRPGMRRVVSMLDGTAPLILVPDKMPPVLLQPVPNASSMNSADTANTAFFSCR

Legume-lectin receptor-like kinase required for normal pollen development and male fertility (PubMed:31833176, PubMed:32284546). Regulates pollen exine assembly and aperture development (PubMed:31833176, PubMed:32284546). Plays a critical role in annulus formation, and may participate in the formation of the fibrillar-granular layer underneath the operculum (PubMed:32284546). May function by regulating the expression of genes involved in pollen exine development (PubMed:31833176). Kinase activity is required for its function in pollen development (PubMed:31833176). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Interacts with INP1 (PubMed:32284546). Interaction with INP1 is required for DAF1 polar localization at the future aperture sites in tetrads (PubMed:32284546). During meiosis, localizes diffusely in the cytosol and plasma membrane of microspore mother cells (MMCs). During tetrad development, localizes at the corners. At late tetrad stage, accumulates to the four corners of the tetrad, assembled into ring-like structures marking future aperture sites. When microspores are released from tetrads and preliminary aperture structures has formed, remains in a distinctly ring-shaped distribution beneath the aperture in the plasma membrane between the annulus and operculum. Expressed in roots, leaves, lemma, palea, pistil and anthers. Autophosphorylated at Thr-376; Ser-378; Thr-386; Thr-403 and Thr-657. Male sterility due to aborted pollen grains with abnormal exine an intine, and defective aperture (PubMed:32284546). Aborted pollen grains with defective apertures and intine formation, and male sterility (PubMed:32284546). In the N-terminal section; belongs to the leguminous lectin family. In the C-terminal section; belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Extended N-terminus.

Q38S00

MAYPFQLGLQDATSPIMEELTNFHDHTLMIVFLISTLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAVILILIALPSLRILYMMDEINNPVLTVKTMGHQWYWSYEYTDYEDLNFDSYMIPTSDLKPGELRLLEVDNRVVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIVLEMVPLKYFENWSASMI

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O Binds a dinuclear copper A center per subunit. Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 14 subunits. The complex is composed of a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A, COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which are encoded in the nuclear genome. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in different assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (By similarity). Found in a complex with TMEM177, COA6, COX18, COX20, SCO1 and SCO2. Interacts with TMEM177 in a COX20-dependent manner. Interacts with COX20. Interacts with COX16 (By similarity). Belongs to the cytochrome c oxidase subunit 2 family.

A9BTA7

MKIVLASNNRGKLAELQAMFAPLGVELIRQGDLFEGEAPEPHCTFVENALSKARFAAERTGLPAIADDAGMCVSHFGGLPGVDTAYYCTQFGYEKSDDNNVRALLEQMQGVADRRAAMVSTLVGVRSARDPEPLIAMGRVLGEITTERRGTQGFGFDPVMYIPELGQTFAEMDPAVKHAHSHRGRATLQMIELVRERWVR

Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. H2O + XTP = diphosphate + H(+) + XMP dITP + H2O = dIMP + diphosphate + H(+) H2O + ITP = diphosphate + H(+) + IMP Binds 1 Mg(2+) ion per subunit. Homodimer. Belongs to the HAM1 NTPase family.

Q3SH83

MPVTLSTLKALRQKGEKIAVLTCYDASFARVFDAAGVDVLLVGDSLGMVIQGHASTLPVKLAEMAYHTRCVAAGTTRAFIVADLPFGSYQPSPERAYTAAARLMAAGAHMIKLEGGAVMVDTVAFLAARGIPVCAHLGLLPQSVNQLGGYRVQGREDGDAAQLVADARALEAAGAGLIVLEMVPAALAKTVTAALSMPTIGIGAGADCAGQVLVSYDMLGLYPRAPKFSKNFLAGAGSVDAAVRAYVAAVKDGSFPAAEHAF

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate Binds 1 Mg(2+) ion per subunit. Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. Homodecamer; pentamer of dimers. Belongs to the PanB family.

A7ZCL2

MEIFKTAFLMVALMLVFIAVGGYVGGEQGMMIAFLMAAGMNIFSYFFSDKLVLKRYNAIPVDENNAHGLYEIVSRLTQKANLPMPKIYIIPEEVPNAFATGRNPSHAAVAVTEGLLKILNENEIEGVLAHELSHVRHYDILTGSVAAILAGAIAMVANFAKIGTLAGQNQNSQRNANPVIMLIIAVVMPLAATVIQMAISREREYKADKGAAYLTGHPEWLASALTKLENYSNSYVMQNASEQSAHMFIVNPFGSLTSKLSVLFRTHPSTSDRIAELQRLEQEIKRGM

Binds 1 zinc ion per subunit. Belongs to the peptidase M48B family.

Q9P7D7

MDIKDYYCVETKDSKQPGESYIYRSIHSAGKLLDTPEDGVSTVYDLLCTAAKNHGEKQAMGSRKLIKENREEREIIRKVDNEEVVEKKLWTTYELGPYEYISFNKVYEIALALGSGLVASGITSETTMLFFAATSAKWFTTAQGCSSQAIPIVTAYETLGEDGIYTSLDECKSRAIFTDPNLIPKLLGPLKQSTWVKLIVCSSTPSEDLVELVKSTAPDVEIITYDNLLSLGKEKPQPPHPPKADDICCYMYTSGSTGKPKGVVLLHRNIIAALGGINRILSQHINVKDYVLAYLPLAHIFEFIFEMCCLYWGGVLGYASPRTLTDASVVNCKGDLTEFRPTVLIGVPAVYELIKKGILAKVSSMPAHRQKVFSGSLSLKQYLIERNLPGSAALDAIVFNKVKAATGGRLRYCISGGAALAASTQAFLSSCICPVLPGYGLTETCAGSFVLSPEQWHLYANTVGFPIPSIEFKLVDIPDLGYYTDSSPPRGEVWIRGPAVCNGYLNRPEDNKAAFTEDGWFKTGDVGEIAKGNTLRLIDRKKNIVKSLNGEYIALEKIEAQFFTSPLVSNVCAYADVNHAKPVVIVNPDENGLRTYLTKNSGSSFNGNPNDTLTNLCKDSGVQHLILKELINIGKQQRLASIEIPEGVVLSDFEWTAENNFLTASRKVKRQVIVAHYSDEIQKAYSKKH

Esterification, concomitant with transport, of endogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Plays an important role in the determination of viability in the stationary phase. a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate The FACS motif is required for catalytic activity and substrate specificity. Belongs to the ATP-dependent AMP-binding enzyme family.

B8HCR6

MIIPRTGIGVDVHAFAAEGEARQLWVGGLLWPGERGLAGHSDGDPVAHAAADALFSAAGIGDLGTHFGTDRPEFAGASGVTLLAEAARIVRAAGFEIGNIAVQFVANRPKFGPRREESQQVLSDAAGAPVSVTATTSDGLGFTGRGEGISAVATALVYPRLSESIG

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.

A7ZPL2

MESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLDNVFDEESFLAFNKRVQDRLKNNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHLGRLLQFKKWGLPVSDRVTLCESAEEVLAFYHKVEEDRPTLGFDIDGVVIKVNSLEQQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTREVVFPTHCPVCGSDVERVEGEAVARCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAGKLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEESNRNVISELLAEGVHWPAPIVINAEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAEMLRLLGS

DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide. Belongs to the NAD-dependent DNA ligase family. LigA subfamily.

Q9CS21

MALQDLGENLQPWCPLGLSLEWVKTVWDLDFTEIEPLDPSIVGEILETGRDAFTKLYGSLFPFATDESGSLESIWTFFTENDISSNTLVALFCHFVQEAHKKSASAQYREYGLHAAGLYFLLLEIPGIVVNQVFHPVMFDKCIQILKRSWPQESNLTQKRKKDHSKSSKDNYRKSRKRGKPPRKEDYQVDELSREEEEEEEEIYFSGRDLCQIRDAIFNLLKNFLRLLPKFSLKEKPQSIQTCIEVFVALTSFEPIPHKFLISQARNLNEVKHISELAYYGLYLLCSPVHGEENKVIGSIFHQMLNVILMLEVGEGSRCAPLAITSQVINCRNQAVQFVSSLVDELQASVYPVLGTLLQHICAKVVDKAEYRTYAAQSLVQLLTKLPSEEYATFIAWLYKYSRSSKIPHRVFTLDVALALLTLPERELDDTVSLEHQKFLKHKFFVQEIIFDRCLDKAPTVRSKALSSFAHCLELSSSNTSESILEIFINSNLVPGIQNLSNTVLNPSPVLTSRNGYSAQSRTHNNDEQTLPGERCFMTMLRKRIKDEKINVRKSALQVLMSILKHCDILSMEQDLLILQDHCRDPAISVRKQALQSLTELVMAQPTCVPVQKAWLMGVIPVVMDCESTVQEKALECLDQLLLQNIKHHKKFHSADRSQVLAWSLLALLTIENQDLRRYLNKAFHIWSKKDKFSSTFINSVISHTDTERSAPAWMLLSKITCSSPKLDYTKIIESWERLSREQSPNSNTLGYMLCVIGHIAKHLPKGTRDKITGVIKAKLNGFQWSPELISSSVDALQKLCRASAKTVLEEQGLLKQVCGDVLATCEQHLSNILLKEDGTGNMDEGLVVKCIFTLGDIAQLCPAIVEKRVFLLIQSILASSAHSDHLPSSQGTTDALDSQPPFQPRSSAMPSVIRAHAIITLGKLCLQHEDLAKKSIPALVRELEVSEDVAVRNNVIIVICDLCIRYTVMVDNYIPNISVCLKDSDPFIRKQTLVLLTNLLQEEYVKWKGSLFFRFVSTLVDSHPDIASLGEFCLAHLLLKRNPTMFFQHFIECIFHFNSYEKHGQYNKFSQSERGKQLFLLKGKTNKEKRMRIYKFLLEHFTDEQRFNVTSKICLNILACFTDGILPMDMEASELLSDTFDILNSKEIKLLAMRAQTSKDLLEEDDVALANVVMQEAQMKIISQVQKRNFIENIIPIIISLKTVLEKNKIPALRELMNYLREVMQDYRDEINDFFAVDKQLASELEYDMKKYNEQLAQEQALTEHANATKGPEDSDRVPSAQVAPDLEAVPALAAAPMAAAAAAAPMAAAAAAAGQDNADVPPTQSRPSAPRSNFTPTLPPISENGPLKIMSSTRPMSLSTIAILNSVKKAVASKNRTRSLGALPFNVETGSPENPSSHESSLSLEKESDRTVNHVTKRAISTPENSISDVTFAAGVSYIGTPATFFTKEKHEAQEQGSDILCLSLLDKRPPQSPQWNVKSPARSHGSTRSSRRSLRKAPLKTAN

Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis. May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Specifically required for decatenation of centromeric ultrafine DNA bridges during anaphase. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size. Component of the condensin-2 complex, which contains the SMC2 and SMC4 heterodimer, and 3 non SMC subunits that probably regulate the complex: NCAPH2, NCAPD3 and NCAPG2.

Q46WL9

MAKKWLNKVKWDDNGLVPVIVQEVGTNDVLMFAFMNRDALQKTAELGEAVFWSRSRKRLWHKGEESGHVQKVHEMRLDCDEDVVLLKVTQVDNIACHTGRHSCFFQKFEGDAESGDWQTVEPVLKDPSQIYTAKP

Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide Binds 1 Mg(2+) ion per subunit. Binds 1 zinc ion per subunit. Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. Homodimer. Belongs to the PRA-CH family.

A4XHV1

MKLNVCYLEMVEYEDALHLQERLHKLRVANELEDTLLLLQHPPVITIGRRGKWENILISKEKLLQMGVKVFEVTRGGDVTYHGPGQIVGYPIFDLGTVGKDIKRFVWLLEEVFINLLKDEYGIEAYRDEKQYTGVWVGGEKIVAIGIAVKKWITMHGFAFNVNTNLEHFSWIIPCGLKDRGVTSLEKLLGHKVEFDDVVYKVAKYFGKVFGAKFRFISKEDLEEIIKIKVEDSER

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. L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein] Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes. Belongs to the LipB family.

B2IN86

MREHRPIIALDFPSFEAVKEFLALFPAEESLYLKVGMELYYAAGPEIVSYLKGLGHSVFLDLKLHDIPNTVKSAMKILSQLGVDMTNVHAAGGVEMMKAAREGLGSQAKLIAVTQLTSTSEAQMQEFQNIQTSLQESVIHYAKKTAEAGLDGVVCSAQEVQVIKQATNPDFICLTPGIRPAGVAVGDQKRVMTPADAYQIGSDYIVVGRPITQAEEPVAAYHAIKDEWTQDWN

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). H(+) + orotidine 5'-phosphate = CO2 + UMP Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. Homodimer. Belongs to the OMP decarboxylase family. Type 1 subfamily.

B7F704

MAKSSFKLDHTLERRQAEANRIREKYSDRIPVIVEKAERSDIPDIDKKKYLVPADLTVGQFVYVVRKRIKLSPEKAIFIFVKNTLPPTAALMSAIYEENKDEDGFLYMTYSGENTFGLL

Ubiquitin-like modifier involved in autophagosomes formation. May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Interacts with ATG4. The C-terminal 2 residues are removed by ATG4 to expose Gly-117 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family.

Q1MAK4

MTKLENPVLMATIGGAQGLRGEVRAKAYTADPGALGDYGHLHSMDGRSFEVLEIREMKNVVVVRFRGVNDRNAAEALNGLELYIERDNLPDEELDEDEFYYADLEGLEARDDKGVSYGTVTGVFDFGAGDLLELKGPGKRPVLIPFSEASVLEIDLEAGTLLIDPLAAGLVDDPEELSKFTPDKPKKKK

An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes. Binds ribosomal protein S19. The PRC barrel domain binds ribosomal protein S19. Belongs to the RimM family.

Q63QT6

MHERYVPADVEAAAQSDWRAADAYRSKEDANRKKFYCVSMLPYPSGKLHMGHVRNYTINDVMYRYLRMNGYNTLMPMGWDAFGMPAENAAMANGVPPAQWTYENIAYMKKQMQSMGLAIDWSREVTTCKPDYYKWNQWLFLKMLEKGVAYKKTGTVNWDPVDQTVLANEQVIDGRGWRSGALVEKREIPMYYMRITQYADELLNDLDGLGWPERVKVMQHNWIGKSFGVNFGFPYELDGEKKLLRVFTTRADTIMGVTFCAIAAEHPLAARLARDKPALQAFIDECKRGGVAEADIATMEKKGVATGFSVSHPLTGEPVEVWIGNYVLMSYGEGAVMGVPAHDERDFAFAKKYGLPIRQVIAVEGETYSTDAWQEWYGDKTRAVCVNSGKYDGLAHDAAVDAIAAELKAGGLGDKQITYRLRDWGISRQRYWGTPIPIIHCPSCGDVPVPEQDLPVVLPEDLVPDGTGNPLAKSDAFLNCTCPKCGAAAKRETDTMDTFVDSAWYFSRYAAPDAQTMVDARTDYWMPMDQYIGGIEHAILHLLYSRFWAKVMRDLGLVAFGEPAKNLLTQGMVLNETFYREDAAGKKTWYNPADVTVSFDDKGRPVGAVLKSDGQPVELGGIEKMSKSKNNGVDPQMLIDHYGADTARLFTMFAAPPEQQLEWSGAGVDGASRFLRRVWAFGFANREALAVRAPFDAAQLAEADKTLRREIHGVLKQADFDYQRLQYNTVVSAAMKMLNAIEGAKGATPAVLRETYGVLLRVLYPVVPHVTFELWKALGYADEFGPLLDAPWPKVDEAALEQAEIELVLQVNGKVRGALKVAKDASREAIEAAAVADGMFAKFAEGRPAKKIIVVPGRLVNVVV

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) Belongs to the class-I aminoacyl-tRNA synthetase family.

E2RP94

MEAGSVVRAIFDFCPSVSEELPLFVGDIIEVLAVVDEFWLLGKKEDVTGQFPSSFVEIVTIPSLKEGERLFVCISEFTSQELNSLPLHRGDLVILDDAPTASWLQGRSCWGARGFFPSSCVRELCLSSQSRRWHSQSALLQIPEYSMGQARALMGLSAQLDEELDFREGDVITIIGVPEPGWFEGELEGRRGIFPEGFVELLGPLRTVDELVSSGNHNDCIINGEEETPTGEEERGPEEDEEQPGTYGIALYRFQALEPNELDFEVGDKIRILGTLEDGWLEGSLKGRTGIFPYRFVKLFSKTRAEETMDLPKESSPTEIPDTSLDCRENPLVVEGRHKSPEYKAEKSNCVISETSASPLEHLTSECEVHKSSHQDEGTSRGPPRSPGWGHEQPLARHSPAEDPSETINGVSSQSQVPFRPRWQQNQYYSTTGRGHLSTEQYSDPLPLEAKAKDYSSRPPRGMYSPPKTFQKPVPSPHGSSCPLAPRVVRPSLLSSQLQSMVRGAKKYHTPKENASSFCSASERSEVKAGLQDRAFTADLIALGQGGGHTDLDSKLTQQLVEFEKSLSGPGAEPEAILRHFSIMNFNSEKDIVRGSSKSITPQELPERRRALRPPPPRPSTPASTSPHVLLDQNLKPEPPLAMRPSRPAPLPPSAQHRVTAVTPGLLTPGLFTHESCESPEKEGPENLDQTLDQTSQCPLVLVRIQEMEQDLDMCSPAPEEPNLTLEEKQDESLRAETPEDLEFYESNIESLNMELQQLREMTLLSSQSSSPVAPPGSMYTENPEQRMLEKRAKVIEELLQTERDYVRDLEMCIEHIMAPLQQTQIPNIDFEGLFGNMQMVIKVSKQLLADLEISDAVGPVFLDHRDELEGTYKVYCQNHDEAISLLEIYEKDEKIQKHLQDSLADLKSLYTEWGCTNYINLGSFLIKPVQRVMRYPLLLMELLNSTPESHPDKAPLTSAVLAVKEINVNINEYKRRKDLVLKYRKGDEDSLMEKISKLNIHSIIKKSNRVSSHLKHLTGFAPQIKDEAFEETEKNFRMQERLIKSFIRDLSLYLQHIRESACVKVVAAVSMWDVCMEKGHRDLEQFEKVHRYISDQLFTNFKERTERLVISPLNQLLSMFTGPHKLVQKRFDKLLDFYNCTERAEKLKDKKTLEELQSARNNYEALNAQLLDELPKFHQYAQGLFTNCIHGYAEAHCDFVRQALEQLKPLLSLLKVAGREGNLIAIFHEEHSRVLQQLQVFTFFPESLPAARKPFERKTLDRQSARKPLLGLPSYMLQSEELRASLLTRYPPEKLFQAERNFNAAQDLDVSLLEGDLVGVIKKKDPMGSQNRWLIDNGVSQGFVYSSFLKPYNTRRSHSDVSVGSHSSTESEQSSSSPRFPRQNSSGTLTFNPGSMAVSFTSGSCQKQPQDATSPKELGQEILSASSNLGCSESSPSRCPSDPDSSPQPRSWDSPEAARDISQPAPALRGYRNSRHPEIGGYSLPGRNGQGKDLTKGCARTTQALEDKNEEPESREAEGNQVYFAVYTFKARNPNELSVSANQRLKILEFKDVTGNTEWWLAEVNGKKGYVPSNYIRKAEYT

Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions in epithelial cells (By similarity). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a key role in ciliogenesis and cyst formation (PubMed:26895965). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). Binds DNM1 via its N-terminal SH3 domains. The C-terminal SH3 domain binds a complex containing actin, tubulin, Hsp70 and actin-regulatory proteins, such as ENAH, EVL, WIRE, CR16, WAVE1 and NAP1L1 (By similarity). Interacts with FASLG. Interacts (via SH3 domain 6) with WASL. Interacts (via SH3 domain 6) interacts with ENAH. Interacts (via C-terminal domain) with TJP1; required for the apical cell-cell junction localization of DNMBP (By similarity). Localizes to the apical junction, colocalizes with TJP1.

A5IU33

MVRESIPKEGENIKIQSYKHDGKIHRVWSETTILKGTDHVVIGGNDHTLVTESDGRTWITREPAIVYFHSEYWFNVICMFREDGIYYYCNLSSPFVCDEEALKYIDYDLDIKVYPNGKYHLLDEDEYEQHMNQMNYPHDIDIILRRNVDILQQWIEQKKGPFAPDFIKVWKERYKKIRQY

Belongs to the UPF0374 family.

C3MYM3

MNIILKISGKFFDEDNVNNLIVLRESIRELTDNGFRVGIVTGGGSTARRYIKLAREIGIGEAYLDLLGIWASRLNAYLVMFSLQDLAYMHVPQSLEEFIQDWSHGKVVVTGGFQPGQSTAAVAALVAEASSSKTLVVATNVDGVYEKDPRVYTDVKLIPHLTTQDLRKILEGSQSVQAGTYELLDPLAIKIVERSKIRVVVMNYRKLNRIINILKGEEVSSIIEPT

Catalyzes the reversible phosphorylation of UMP to UDP. ATP + UMP = ADP + UDP Inhibited by UTP. Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1. Homohexamer. Belongs to the UMP kinase family.

Q146X0

MSTMTPAEIVSELDKHIIGQGRAKKAVAVALRNRWRRQQVEEPLRQEITPKNILMIGPTGVGKTEIARRLAKLADAPFIKIEATKFTEVGYVGRDVDSIVRDLIEISVKQTRETEMRKVRTKAEDQAEDRILDILLPSARPVGFGASSGAADTVDEGSTTRQTFRKRLREGLLDDKEVELDVEQPQVGMDIMGPPGMEDMTEQIRSMFANIGGGKKTRRKMKVKEALKALTDEEAARMLNDEEVKTKAVQNVEQNGIVFLDEIDKIASRNEAGGGEVSRQGVQRDLLPLVEGTTINTKYGMVKTDHILFIASGAFHLAKPSDLIPELQGRFPIRVELDSLSVNDFESILVSTDASLVKQYQALLATEDVHLEFADDGIRRLAEIAYAVNEKTENIGARRLYTVIEKLLEEVSFAAGNHSGRTVQIDAAYVDRALNEVAEDEDLSRYVL

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. Belongs to the ClpX chaperone family. HslU subfamily.

Q31KV0

MGQSTLIRAKVGDRFSIGDGCPLTLFGGPCVIEGEDFSLKMAESIAKVCDRLGVQFVFKSSFDKANRTSIGSFRGYGLEEGLRILERVKTELGLPVLTDIHESQQAATVAEVVDILQIPAFLCRQTDLLLAAAATGRTVNVKKAQFLAPWDMKNVVNKLRQGGAENLLLTERGSCFGYNALVVDFRSLPLMRELGCPVVFDATHSVQIPGGAGDRSSGQREFVPVLARAAAAVGIDALFMEIHENPDQALSDGPNMIRLADLEATLRQILRVREAVAEPIGASA

D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Belongs to the KdsA family.

A0KJK9

MNLHEYQAKQLFAEYGLPVSEGYACATPQEAAEAADKIGGNTWVVKCQVHAGGRGKAGGVKLAKSKDEIRAFAQNWLGKNLVTYQTDANGQPVTKILVESCTDIAKELYLGAVVDRGSRRVVFMASTEGGVEIEKVAHETPELIHKAALDPLVGPQPYQARELAFKLGLVGEQIKQFTKIFMGLGQMFLDCDFALLEINPLVITAQGNLHCLDGKINIDANALYRQPKLRQMHDPSQDDPREAHAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVNLHGGSPANFLDVGGGATKERVTEAFKIILSDSKVQAVLVNIFGGIVRCDMIAEGIIGAVKEVGVKVPVVVRLEGNNAELGARKLADSGLNIIAATSLTDAAQQVVKAAEAK

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. Belongs to the succinate/malate CoA ligase beta subunit family.

Q05B45

MHPPPPGPLGDCLRDWEELQQDFHGIQETHRLYRLKLEELTKLQNSCTSSITRQKKRLQELALVLRKCKPSLPSEAEEAARELENQIKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILILISFTCRFLLNSRVTDAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYYQSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLARDPECKEWQVLMCGFPFLLLFLGNFFTTLRVVHQKFHNQLHGSKKE

Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis. Homooligomer and heterooligomer with TMEM120B. Belongs to the TMEM120 family.

Q57CY8

MKETFIHPTALVEPGVELGQGVSVGPFCHVQSGAIIGNDCELMSHVVITGATTLGAGTKVYPHAILGCDPQNNKHKGGPTRLNVGVNCIIREGVTMHKGSDNARGYTSIGDNCSFLAYAHVAHDCDIGDYVTFSNNVMIGGHTSIGHHAILGGGAAVHQFVRVGHHAFIGGLAAVVSDLIPYGMAIGVHAHLGGLNIIGMKRSGMERKEIHNLRHAVRMLFDRTKPIRQRAQDVLAAIPDSPTVSDMISFINVDTKRAYCTPPLDAAHGGAGHDSDED

Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP] Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. Homotrimer. Belongs to the transferase hexapeptide repeat family. LpxA subfamily.