Datasets:
Synthyra
/
TremblNLP

Dataset card Data Studio Files Community
1
ids
stringlengths
6
10
seqs
stringlengths
16
1.02k
texts
stringlengths
117
4.4k
A0A6B1ABZ6
MAQRTPSQHARSTRGAGLGTEPSSAVWDVVARVDTGELATAAALLHNLHPADQADALAALDGRERRRLLDRIDSHTLAELLPFLTPEELEHVAPDVALPQLTAALDETPAQLGADVLHAIPLTDAELVLDRLPKAGLVEPLLQHDDDSAGGIMAPELMVLGPHLAAEQALTVLRAAAPAPTVRDTVYIVDTEGVLLGSIGLHSLVFAPPMTALRDLMEPIGPTVTTDMDQEDALKILQRFGLHALPVLDDDGRLVGVTTSDDLLDIAQQEATEDMYRLVGLVDDQALTTPVTTALRRRLPWLLLNLATAFAAAAVVAAFESTLARVAALAIFLPIIAGQGGNAGMQVTTLAVRAMALGEFDRHFTRLVLPRETIIGIVSGIAFGLLVGVVGWVWQDNPWLGVAVGAAMLGTMVVAGLFGLLIPIILRGLGADPALAASIFVTTATDMLGFLFFLGLAALLIQRIA
Function: Acts as a magnesium transporter. Subcellular Location: Cell membrane Sequence Length: 465 Sequence Mass (Da): 49057 Location Topology: Multi-pass membrane protein
Q7PSX4
MTPLGKMSSVWLTSVSVFLLLLLQQPPVDGELFTALADMEELLETEAVLITNLDNYVQAQEEKLMQLRQKMHEYRREHAEAARDVSAYLSNPVNAFLLTKRLTTDWRYVENLMTYEVGKEFLENVTAYRSVLKFPSDEDLNGAAVALMRLQDTYNLDTASLARGMLNGVQYSTELSAGDCFELGRQSYLNGDYYHTVLWMREAMDRLTGEVNRTATKEDVLEYLAFSTFKQGNIQTALSMTEELLELVPDHERAVSNKAYYVKELQKEAQQKILRGDDGSEEVPVDTTTKEATPHVYDTNERKLYEQLCRGEQQPPIELRSQLVCRYTTNSSPFLRIGPLKLEEAYLRPYIVIYHDVMSDREIERIKHYARPRFRRATVQNYKTGELEFANYRISKSAWLKDAEDEMIRTISQRVEDMTGLTMETAEELQVVNYGIGGHYEPHFDFARREERNAFKSLGTGNRIATVLFYMSDVTQGGATVFPSLNLALWPRKGTAAFWFNLHASGRGDYATRHAACPVLTGTKWVSNKWIHERGQEFRRPCGLQLDHSAEEF
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. EC: 1.14.11.2 Subcellular Location: Endoplasmic reticulum lumen Sequence Length: 553 Sequence Mass (Da): 63567
A0A134BKY5
MGKKNVLAMILAGGEGKRLMPLTLDRAKPAVPFGGTYRLIDFALSNVVNSGYLRSVVLTQYKSHSLDRHLATTWRMSDLLSNYVAPVPAQQRRGKHWYLGSADAVYQSLNIVRDENPDYILIIGADNIYRMDFSQMVDDHIKSGLPCTVAGIRQPIELSSAFGVIDQTNGTINRFIEKPDTCEGLPDDPTKFLASMGNYVFTTKDLVAALEEDAKNEESKHDMGGDLVPYFVKHGGVNCYDFIENEVPGATDRDRDYWRDVGTIDAFYEAHLDLLSVSPVFNLYNFDWPTYTKLDAWLPPAKSTFNDETRRGMALDSIVSPGVIISGARAERSMLSPMVHLHSFASVDGSVLMNGVDVERSAVIHNAILDKNVRVAEGVQIGVDHDKDRERGFTVSEGGITVVPKGTIVDH
Pathway: Glycan biosynthesis; glycogen biosynthesis. Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc. EC: 2.7.7.27 Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate Sequence Length: 411 Sequence Mass (Da): 45473
A0A034VMP3
MAFAGLKKQINKANQYVTEKMGGAEGTKLDMDFMEMERKTDVTVELVEELQLKTKEFLQPNPTARAKMAAVKGISKLSGQAKSNTYPQPEGLLADCMLMYGKKLGEDNSVFAQALVEFGEALKQMADVKYSLDDNIKQNVLEPLHHLQTKELKEVMHHRKKLQGRRLDFDCKRRRQAKDEEIRGAEEKFAESLHLAQMGMFNLLENDTEHVSQLVTFAEALYEFHSQCAEILRGLQETLHEKREEAESRPKAEFVPKTLLDLNLDGTGTNDTDSVSTPAHRASAASPLPSPLRSPAKSLVPGATTPQRQQQPCCQALYDFEPENPGELGFKENDTITLLSRVDDNWYEGSLNGRTGYFPQSYVQVVVPLPNGN
Function: Required presynaptically at the neuromuscular junction. Implicated in synaptic vesicle endocytosis. Subcellular Location: Membrane Sequence Length: 373 Sequence Mass (Da): 41845 Location Topology: Peripheral membrane protein
A0A6S7FLT7
MARNRVNQQFRRERTFSSSSTVSTDDGHHDLSEQIVVDVTLEYFYKPRTLTALGFLLLYLAYFAFTHDPHLELSKNIFKGLIAISVVFLFVCMLVAPNGPFTRPHPLLWRIVFGISVIYLLALTFLLFLNYRQIKDILIFIDDDLKYAGPDMKEYATDCRLSWAKLYESMDLFILSHFIGWAGKSLLMRHAVLCWSASITWEITEVFFAHLLPNFKECWWDAILLDIVICNGLGIYVGMYLCKKLEMRTYHWESIKDIQSTTGKLRRAILQFTPASWTRVNWTDSNSTYKRLFAVYILGVVWQLVELNTFFLKHIFHIPNPHYLNISRLLLISIISAPTIRQYYIFVTDTRTKRLGTQCWVFITITTVELLICIKFGTELFAKTEKINIVMWLLFQLVFSFLIVCVMVIRRNRSAGSETKGEILANLPSDENSKTYNYVNSNGKHVVEHEGLGPRPSSINIQRV
Pathway: Lipid metabolism. Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine. Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine EC: 2.7.8.29 Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 464 Sequence Mass (Da): 53898 Location Topology: Multi-pass membrane protein
A0A376MW51
MRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ
Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Subcellular Location: Cell inner membrane Sequence Length: 70 Sequence Mass (Da): 7974 Location Topology: Single-pass membrane protein
A0A2E7UZP5
MGGILLLEDGRMFTGEAFGARTTRVGEVVFNTAMTGYQEVLTDPSYREQIVTMTTPHIGNYGVNEQDMESTQIHVSGFIVRKLSRRPSNFRSQGGLEPWLRAAGIPGLQGIDSRALVRHIRDKGAMRAVISTDGTSVEALRERLNDWPGMAGRALAYEVSRSSPEVTTEGKSGSLRVNLVDGGAKRNIGRLLAQAGCTVREVPLSAKAAQWMDDCDLLFFSNGPGDPAALGDVVQEIRKVVGKRPMAGICLGHQLLALALGAETYKLPYGHRGANHPVRDEVSGRVEITSQNHGFCVSREALEKIGATVTHTHLNDGTVAGFAHAAHRIAAVQFHPEASPGPRDSEHLVLGRFLALAQASEPSP
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. EC: 6.3.5.5 Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate Sequence Length: 364 Sequence Mass (Da): 39158
A0A6N9N4F8
MDTIRITKCFTFDMAHALKGYDGLCRNIHGHTYMLRVTLAGKIKHEDSNPKNGFVLDFGDV
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. EC: 4.1.2.50 Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate Sequence Length: 61 Sequence Mass (Da): 6914
A0A164BUF5
MKIAVAGAGAVGGYFGALLKKAGHDVVFLARGKHLEAMKKSGLVVKTNDQLLTIDGVFTDKIEDFADCELILFCVKSTDTESTAEQIASLQNDRAVVLTLQNGVDNEEKLAQILGGKRLLSAATYLSSHVEEPGVIKHSGRAKLVIGALDESLISFRDKVADLFRQAEIFVKTTDDIMLDKWKKLLWNATFNPLAALSKATVGEIMEHKELRKTAENACREVMRVANKIGIPLDEEMFHRTFANSGAALKHKPSMLQDRLKGKRMEIESLCGFIVKKGRQIGVETPVLQTLYSNLLFLETHR
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2. Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. EC: 1.1.1.169 Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH Sequence Length: 302 Sequence Mass (Da): 33338
A0A3C0K3H4
MKEVTTADRKDDHIRINLEENVQFNSISNGLDKLYFVHNSVPETNMSQIDTSIDIFGKELRMPLLISCMTGGTDKSGNINRILAEVAQQMGIGLGLGSMRVVLEDHEKIDSFCLRELAPDILLLANIGAVQLNYGVTVDDCRQLVDLSESDALVLHFNPLQEAVQDEGQTNFSGLLNKIEHLCNEFSRDSIPVIAKEVGWGFSEQVCKKLSEVGISAIDVAGAGGTSWSQVEMYRSDDESNKKVASVFENWGISTVEAILNAGKGAPDIPCIASGGLRNGLEMAKCLSLGASLAGMAHPFLVAAMNSPERLMSTIYEIEQQLRVAMFCTGSSDIENLKKQILIDKK
Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate EC: 5.3.3.2 Subcellular Location: Cytoplasm Sequence Length: 346 Sequence Mass (Da): 37728
A0A6S7KN11
VEKFKHNQQPHNSLHSMFNIHTGNTLPLNENWPHLQIDAVSLYLLVLAQMIASGLTIIYTLDEVSFIQNLIYYIERAYRTPDYGIWERGCRSNNGHRELHSSSIGMAKAALESLNGFNLFGSQGTSSSVIYVDPDAFNRNCTILKTLLPRESSSKETDAALLCIIGYPAFVVDDEKLKETTGERVVENLM
Pathway: Glycan biosynthesis; glycogen metabolism. Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. Subcellular Location: Cell membrane Sequence Length: 190 Sequence Mass (Da): 21379 Location Topology: Lipid-anchor
A0A0N5CVL4
MNSSNILIFQVEVSKVEAPPLFDKALITHLERLSLVRFSDEQAIYNLKQAVSYANQLKLVDTTGIEPLETLLENIPCPLRDDIVDEDVMTKNEVLMNAAKTVEDYFVTPPGNIPLEESDKQYLEKIEQ
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate EC: 6.3.5.- Subcellular Location: Mitochondrion Sequence Length: 128 Sequence Mass (Da): 14538
A0A0A9Y7X6
MSWDSPRRDGDILCCCEFLDSGGERNHILACCCNCQELDLCCERLVTCQKVPKTIIWKIFSTATNRMRVPWRGGAVQISLDSVAPVLLIPVILLIAAHGPMMSVITFSFLPLFLLYTHFLFMKIKPHNSFFLSWTITSTVLLFLLLWSFSEMLEIRNDEFFVFLLITAAALYSINKVKQKEILSFVTEDQLLDGGEKCSECSILLPPRAYHCTSCNACILKRDQHCSWLHCCIGQYNHFWYMMFLIATLSQFVLYSNLILTTACHPFRVIGSIMLPDDCSDVYFDLVYAICFVSSIYCIEGAAFVFSVLALECWLITLGITGHEYRNRSKRSYCCGLVMSRPYSKGFLRNWILFWKGADISYQMYKI
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 367 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 42155 Location Topology: Multi-pass membrane protein
A0A2E2WDA1
MPVTWTMLVAVGTGGALGAVARFAVSRQVSLWLGAALPWGTLAVNVLGSFLLGFLAAWFRSRTELPPEWQALWTVGFLGAFTTFSTFSNEVVGLLQADASLRALATIAANVLLCLCCCWGGVWLARSFGAALNAAA
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Subcellular Location: Cell membrane Sequence Length: 136 Sequence Mass (Da): 14280 Location Topology: Multi-pass membrane protein
A0A5K1JEJ1
MEKTLILLAGPPATGKTDLADRIKARHTSESFLSVSLDDVKEEYWDTYGFNNAEEKAQVDASALQEWFRRLDVAMADGPQIMCDYPFSAKQHDRLAELADKNGYRVLTIRLVADPVMISKRYRARDLKPTRHLAHIVTHYHKGDVLEDRSKGDDLVDLDILVDRIKNRGYDTFELGHTIELDVTNVDTVDYPGFLAKVDEYLDDPSSVATIAAKAGAELTDENLCSRIDYTLLKPTATWDQIDAICAEAFEYGCASACIPPSYIARAHKVYPDLALTTVVAFPLGYMTSSAKAAEAADAYANGASEIDMVIDQGMVKARDYQAIEDDIRAVREAVPNATLKVIVETCYLAQETKRPICHAVEAAGADFIKTSTGFGTAGAQVEDVYLFAQELGGRVKVKASGGVRTKEDLALMSGAGADRIGASASPRKLFGTR
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate EC: 4.1.2.4 Subcellular Location: Cytoplasm Sequence Length: 434 Sequence Mass (Da): 47477
Q5TNL1
MDTKTALPWVIIVAAGLFLRAAISLHSYSGQNQPPKYGDYEAQRHWQEVTVNLPVSDWYRNTTDNDPLYWGLDYPPLSAYHSYLVGLWARRWHNESYVALYESRGISTDQHKQFMRNTVLLLDVLLYLPAILYATYTVRKRLANDRSEVAEWASLTLAVLFPGQILIDNGHFQYNNASLGLCALAVVALLERKTLAGAVLFCLALNYKQMELYHALPFFFYLLRDCFTGSDKSSTVLERLTAGVSRLAVLGVTVLATFLVLWLPWLSSLEAAGQLVHRIFPVARGVFEDKVSNVWCMVNVLVKLRNFPNTTMALVCLLCTLLAVLPSGLHLLLQKASTIRSFLYSLAVTALGFFLFSFHVHEKSILLVALPVTLLLPLEPLAACWFLQIATFSMFPLLHKDGLTVPFVGLSLISLALLRTARGAQSGNKARDSSYDLLHLRGLLPESVANNVTGSVLVTLFYLSLLGQVLLLVAFLCLPAPAHLPFLHSLAISAYSCGHFVLFYMYFNYRQFCGGEGTVANKQSTKISHKKKAK
Pathway: Protein modification; protein glycosylation. EC: 2.4.1.- Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 534 Sequence Mass (Da): 59631 Location Topology: Multi-pass membrane protein
A0A399YSF9
MSDALDATPEHLQPDDYRSGVVAVVGRPNVGKSTLINAILGQKIAAVSPKPQTTRKTQFGIYTTDAVQILFVDTPGIHLPRHKLGEYMVQVATQALKDADVILWVIDTTEAPGKGEQAIAEMIASVQTPVMLALNKVDTLAPDADLSAHLALTPHVEAHRISALTGEGVAALVESLAARMPPGPQYYPEDQVTEVNLRAIASEVVREKVMSNTEEEIPHATAVEVTEYRERPDGTHYISATIYVERLSQKGIIIGQKGQMIKKIGTEARQDLIAIVDGPVYLDLHVSVLKNWRSDPRAMQRFGYRVQRDKE
Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism. Subcellular Location: Cytoplasm Sequence Length: 311 Sequence Mass (Da): 34083 Location Topology: Peripheral membrane protein
A0A2N5VZA2
MSIPPFFNRGTGTTSTLTGKGRLSSRDPDRAVRETDLDAAAARVSAISKNYLHDRFAGLLTRPSHAGEGSTLRPPWVNIGTHHRTYVIDSLTERFMVGGQGAKKKQVLSLGAGSDSRFWRLRERYCTTGEAWPVGRWVETDLQMTVGQKIRSVLANDSLRALCGPQLAVSPGPELPVGAPAPYIDLPSDPTDLYADNYCLLSADLRRPAELIDKLQSVPPTGSSKDPLLDPAAPTLIIAELLFLYLSPSHTAACLAALTAFFKGPLMIITYEALDLGDSFSRMMVQNLAGRGLSLAGFECNRSVASQIARLEEHGFTEIVSTDMKSLRVGVATAEEGRGEEWKTRWEGELERIRRLEFLDEVEELELILQHYAVSWATRNPHSPARSTVGFYLPTF
Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. EC: 2.1.1.233 Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine Sequence Length: 396 Sequence Mass (Da): 43545
A0A358QMU1
MPSPTKSSGKVGIHVNDLFGGVCRAPAPDLTGGVGPLDPEGRSGAGGILAADLTRRSVCVLQVVLIAAQVVLAILVILGILLQTPKATGLGGVIGGGGDSGGGYRRRRGLEAGLLRASAVFIALFVIVAAINVWINNTA
Function: Involved in protein export. Participates in an early event of protein translocation. Subcellular Location: Cell membrane Sequence Length: 139 Sequence Mass (Da): 13905 Location Topology: Multi-pass membrane protein
A0A510DWG4
MEPEFFNSIAEKWQKIWEEKGVFRADPSNDRSNKKFITVPFPYTNSPMHIGHGRTYISADVYARYLRMKGYNVLFPFAFQFTGTPILSVADAIRKGDTELIESFSTIYNIPKEKIQEMKDPFKLAEYFKSEMEKTAKKLGLSIDWRRTFDTTDENFQRFIQWQFEKLRKGGYLVSGSDVVGFCPVDNFPVGMHDTKGDVEPEIEDMDVIFFDGESFLFPVATSRPETVFGAVGIAIADEEYVVVEETENSKHKSYVVSRKVFGKLSYQKSLKEVRSISPEELVKLKARNPLTGRDVKIVKGRMVNPSFGTGLVMLVPAHDPSHMLMAREGGIDEAIPVISTPDLPEIPGMGIDTEDPAELRDYIDSIYRAEYYKGTMRDNIIQMVPEFMRQKVKDYIAGRRVIDARKDVRDLLRVMDRYDRIYEISNGPIYCRCGAEIVVKKIEDQWFLAYDDPKWKNQTLHSLNLIKFVPPEVRKDFEKAIFNMKRRAVGRSRGIGVKLPWNGSQIIDSLSDSTIYTAFYTFSHIAKGKKLTDEALDYILLGMGSPEEIEKTNEIDVKDVIKMRNEFEYWYPVDSRHSGRDLVQNHLPFFIYNHLAIFGEEMLPKQIVLNGFIRVGGKKMSKSLRNIYPLEKAIREFGVDPIRVALSSSALIIQDTDFDPRNVEATGEQLKKVFGLINRILELQGNDIDKNEENSLADKWLSTLMRRRIAEANKKYSQMEFKDVFDLVIYKLYEDLKDYTELGESLNPRLLRKVASAWIRMICPAVPHMAEELWSKSFDGLASVQPFPTEDEFKEYEEAEFEVSYLNELIENIRNLESVISKEAEKIIIYVNDDKSLKDAVREAIDSIEQGKGLKDFLFEVKGDEKELEMLFRRIEQYDKKLRGLLAKYANASEMEILTKNVNYLMRKLNVSEISIFDSNDPMSPDIKGKKRSALPFSPAIVII
Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) EC: 6.1.1.4 Subcellular Location: Cytoplasm Sequence Length: 945 Sequence Mass (Da): 108925
Q7QBF1
MALIIRSIYSGYSYLVDKTDERVVELPLLRSVWTVPLITGAYLYFVLDLGPKLMANRKPFEMRRFLCAYNLAQVAANVWTFAMGVRYLRTYNFSFVCQPLRLDRSDQSMDEMHLAYAYFLLKILDLADTVFFVLRKKQSHVTFLHVYHHTIMALSASLFLRYLSGGHCFMLGMLNTFVHAVMYFYFFLTIYRPEAVRGASWKRYVTLLQMAQFAYNVLHFFRPIVLGVDCGYPRAVMWFVGMQNIFMLLMFSDFYRRAYLRTPKAAAHAN
Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA EC: 2.3.1.199 Subcellular Location: Membrane Sequence Length: 270 Sequence Mass (Da): 31707 Location Topology: Multi-pass membrane protein
A0A520XX50
MPTFRPDLVDIPVYRPGRTPGEVRREYGLESIVKLASNECPYEPFPPVTEAIGRAASAINRYPDNGTREVRSAVAAFLEVSPDQLWFGGGSNELIYVTALAVGGPGTSAVYAAPSFGLYRIATRLAMAEGVEVPLDEDDRHDLDAILAAIRPDTTVVYVCNPNNPTGTHVSAAQVEAFVEAVPERVLVVVDEAYFEFPTAPDFASALPLVADRDNVVVARTFSKAYGLAGLRAGFFIGPAPTLEELRRIQLPFSVSTLAQVAAIEAVKHQDLVQERTSANRRGLEAITAGLATRGIDFADSQTNFVYVRPPMDATGCFEALQRRGIIVRDLGGAIRISVGTEEENRRLLEALDEVLG
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. EC: 2.6.1.9 Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate Sequence Length: 357 Sequence Mass (Da): 38574
A0A0A9XLA5
MATDELISESDKPIVMRALLLRHRHVQESESRGFRFNVRRNTSSYSSLQNLNEEARKRSLIPAASAVDTTKTNLLSPPNLFNHTAVDIKEETYLSSTEDLARKVHKESILKRIPIGAEATTVLVGAVEFLEQPTIAFVRLAEGIHIPSITEVPIPVRFMFICLGPSSADLDYHEIGRSISTLMSNPEFHGIAYRAEGRKELLSAINEFLDSSIVLPPGNWDRNSLLPFEDLKAKSDAIRRRQSRVALPKITADQKALLPEVIDEIIHVPVLGPVVRLKRHGDGDGWKKKDDPLRRTKIPFGGLYNDIKRRFPHYLSDFRDGIDGQCLAAAIFMYFAALSGAITFGGLMADKTNNLVGISETLIATSLSGIAFALLSGQPLVIVGATGPLLLFDESLYTFCLTADIDYLTMRVFIGIWLLIIALMVSFFEGSVLVKLFTRFTEEIFASLISLLYIVESVMKICKIYYKHPMMSLMSYAHEYCLAVNDTMPCSFTTVLSLVENSTVSPLLNTTARNFTTGLETALLEKANQNSNSSGHSNSTGMSTYFEPPVQNEPNTALFCTILALGTFFIAYYLRQFRNSKFLGRSARRALGDFGVPIAIVLMVGLDYFVPGVYTEKLKVPEGLSPSAPDVRGWIIPPTGLERSFPVWVGFASVVPALLVYILLFMETHISELI
Catalytic Activity: chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out) Subcellular Location: Cell membrane Sequence Length: 674 Sequence Mass (Da): 74826 Location Topology: Multi-pass membrane protein
A0A7D9DX79
MAENFQGSAQNELILSRSFPCQLIKWKASVDQKVSKGSILAVYKKISGEVSNKSEIVVLPKLKSHVGGSVKRLLVAEGEHVKPGQAVILLDVCEHKTVMKEMCAECGADLRQEPGIPGQLKEPVSASVALVHNIPELRVSQKEAEILATKDKVTLLRNGKLVLLVDLDQTLIHTTTENVHPDMKDVYHFQLPGQNCWYHTKFRPGWRKFLEDMSKCFELHIFTMGSRMYAHTIARMLDPSGVLFADRIRSRDESFDMFSKYRDLRALFPCDDSMVCIIDDREDIWDCAPNLVTVKPYRFFTGTGDIHAPPGSEQAFTHPPAIPLHEDASEVEVKDSTDGDNDEDEKASKDGGAPTIKNSPDGSQKNASESEKFGTNGSSGKDKEVHEINHNEKGTRCDDTCEGKHDNEATGKEEEEKTDSNEIQDVEGQDSEKENQEASSKVYKKANDEDAVDGNYIEDHDDYLLYLEEILRRIHGSFYQVVAWNKQSEEKGSDPTTRVAPDLRCIVPELRRNVLKGTNIVFTGVIPTNTRHEDSQAWKIAQQFGASVSKDLLTQKNNADRSRRTTHVVAARPGTEKVCHALRFPSVRLVNPNWLWTCAERWEWVDERLFPIEDYHEHKIRTNDTPTLSRQGTPKGQHGKDDNSKKGNLSDEDSAEHITDDNMRIVLNPFLSFSSGEMDAMDKEVEDLMKSSDEEDDKDDSNEQILGSVSSSSNSTENGDSLPKIDHATGEDIPDGIDVPDGIDAPKGKAINFSTIKQNRREDEGSPSKRRKLDFKVGDDDGSEGEFSSDGGSSGSNSGDDDGNDMAALLEAELAEFN
Function: This promotes the activity of RNA polymerase II. Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate EC: 3.1.3.16 Subcellular Location: Nucleus Sequence Length: 818 Sequence Mass (Da): 91156
A0A0A8J7R6
MNVNNCAKIVPVIIAGGVGSRLWPMSREEHPKQFLPLLHDSLSLLQQTLSRVNNKHFDAPLVICNEEHRFLVAQQLKELNLLNNNIILEPCSRNTAPAITLAALSLKNKDCIMLVLAADHFIGDGDYFLNFIKKASTAIDDQSLITFGITPSHPETGYGYIKKGKSISDDVFMVDKFVEKPNKEKAEEYIAEKLYLWNSGMFMFKPMAYLRELKKYHPNIYDVCSSSIDSIVSDMDFRRIDKTIFESCANESVDYAVMENSSHVKVLQFDSQWSDVGAWGALWEISDKDTHGNCISGDVFLNDSKNCYIKSDGVFTSAIGLNNIVVVASKDSVLVSHRDSVQNVKNVVNYLKENNRYEYKRHNVRYLPWGTTLSLVDSSKYKINFVTIEPGKSISLQKHYHRNEQWTILSGTAVVYIDGIKKIITENQTVHIPIGCTHSIHNPGIIPVEFLETQIGECIDPSDVFRLEK
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1. EC: 2.7.7.13 Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose Sequence Length: 469 Sequence Mass (Da): 53048
A0A090IEM6
MASLHFKFAAMNSGKSTQLIQAHFNYIERGMYPLAMTPECDSRYGKGVIGARVGLKLEVDVFEKETNLFTTISTRLENQKIDVFIIDEGQFLSREQVYQLANVVDQLNIPVIVYGLKTDFKLEMFEGSYHLMCLADKVEELKTVCWCGNKAHMNARVSDSGVVLREGEQVEIGGNERYVSLCRKHFMNGNASR
Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+) EC: 2.7.1.21 Subcellular Location: Cytoplasm Sequence Length: 193 Sequence Mass (Da): 21872
Q7Q862
MSNYVERMSVQYHNFSQGADPLIDSWPLMQTPTPILTISGLYLLFVLWIGPRWMEHRKPIELRRTLIVYNAAQVIISTAFCLTPFFTGLFGQYMSMSCGEPMTGISKELQLSVWNGAWMYLLLKIIELLDTVFFVLRKKQNQVSFLHVYHHTIMVLFTWFYLKYIPGTQAAFIGVLNSFVHIFMYTYYLLAALGPQSPKEKKLWDQKYLFWKRHLTTLQLLQFGIMLCYFVLINSMQCQVPRALTYFFVSNITIFLFLFINFYRQAYRKRPATVKAD
Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA EC: 2.3.1.199 Subcellular Location: Membrane Sequence Length: 277 Sequence Mass (Da): 32687 Location Topology: Multi-pass membrane protein
F6ZX71
MTVTLDFEESLTDSPRTRAAMEEVECEVSDLESRLEKLVKLSSHMNDGGRQYCSSSRHFVEALRDLSHHSQKDSMLSECLERFSDGLSKIIDSHVELLENIQFSFKQRLLHLLKEDLRSFRDSRKDMERCREGLESALHHNAETARRKAQEAQDAASAVQGSRKAFRDRALEYALQINVIQGKKKFDILQFMLQLMDAQASSLAQSHHAMQALDQYRNELAAQVHRSVLEAAREQRDMEQKVTLIKAKDPSDEDSVLQGDGAQVVIEGYLFKRASNTFKTWSRRWFSIQNNQLVYQKKVDVLTVVIVDLRLCAVKLCPEAERRFCFEVVSPAKSCMLQAESDRVLQLWVSAVQRSITTAYSDNKRESGSLRLPRSPAEAPAQEKGVQGAQDAVLRVPGNASCCDCRTAEPEWASINLGVTLCIECSGIHRSLGVHFSKVRSLTLDSWEPELIKLMCELGNSTINGIYEARIEDMNIRKPTAASSRSEKEVWIRAKYVEKKFITKLPQSSLRSPRHSQPDPPSHSPKARTLGQRPNSGPDLKALSRPFAQTELQRPISSPGAQRQNTEETEIEPENGRQVRLRKATRPLLRPKPGLATARAEGADGKDVRSLHPGALLYRAVEHRCLPTMADALAHGADVNWVRSEERGYTPLIRAVLSNSLVASEFLLQNGASVNQTDKDGRGPLHHATLQGYTGLACLFLKRGADINAVDNSGKDVLSIAIENANADIVTLLRLVKMREADIALGQSGDETYLDIFRDFSLMASDAPEKLSRRSFDLHLSTL
Function: GTPase-activating protein for the ADP ribosylation factor family. Subcellular Location: Endosome membrane Sequence Length: 783 Domain: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate protein binding to PIP2 or PIP3 containing membranes. Sequence Mass (Da): 87643 Location Topology: Peripheral membrane protein
A0A3B9VER6
MYESGMVVVDGLFISNSYLLTGKDFQNLLLWKPRVGEAYTVCNAERKFFRARVTKLKSDKAEIFVFEGPCESVESDLTITLLQAIPEKERMELIIQKVTELGVSSIIPFKSKCSISIEERDAKQKKSHKWGEIALKAAKQCRRASIPQVHPYCNFADAVHATAQCDLKILFWENEKDTDLKKTILNVKDLGLNNIAVMIGPEGGFEDAEITGAREAGFITVGIGQRILRTETAAIVTVGLIQYELGNLG
Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine EC: 2.1.1.193 Subcellular Location: Cytoplasm Sequence Length: 249 Sequence Mass (Da): 27716
A0A6L7M9X6
MGLPTEDRKVHSIVAANQNQYWFNPQMRGFAEECGVFGVYGPGHDVARRTYFGLYTLQHRGQESSGIVVSDGKRLKLHKRMGLVSQVYDNQSLSELRGDLAIGHNRYSTTGSNRIENAQPIVTETEFGPLAIVHNGNLTNTDELRQQLLAQNKTILGTSDTEVILAVVASAPGSDPVQKIVNGISQLQGSFALIFLTADRLIAVRDKLGNRPLCLGRSDDTILIASESCAFAALEANFERDILAGEVVVIDAEGVSTISRDHMAPPALCLFEYIYFARPDSDIEGVNLYRARLAMGRALARQAPVDADLVIGIPDSATAAAIGYAEAAGIPYGEGLAKSRYIGRTFIEPDDETRKLGIKLKLNALPAITAGKRLVVVDDSIVRGNTTREIVKHLKEAGHAAEVHMRISSPPVRWPCFYGVDIQQPSQLIAHAFSVDQICSSIGADSLAYLTLDSLKKAVDSPRAQLCTGCFTRDYPAPVRPGVGKHAFEPAVEPALTP
Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. EC: 2.4.2.14 Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine Sequence Length: 498 Sequence Mass (Da): 53930
A0A376YED8
MPAIGELRQPVWPAEVYGSISHCGTTALAVVSRQPIGIDIEEIFSVQTARELTDNIITPAEHERLADCGLAFSLALTLAFSAKESAFKASEIQTDAGFLDYQIISWNKQQVIIHRENEMFAVHWQIKEKIVITLCQHD
Pathway: Siderophore biosynthesis; enterobactin biosynthesis. Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively. Catalytic Activity: apo-[aryl-carrier protein] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[aryl-carrier protein] Subcellular Location: Membrane Sequence Length: 138 Sequence Mass (Da): 15423
A0A1W6S4L2
MYVPLLRPSLFMCCSFRYARILIGFCRFLTAIAIYSSIWVAPSDSQQGENYRIIYVHVPAAWMSSLIHIAMAISSVLFSLTKHPLFQLFSETGAKIGASFTLFTLVTGGFWGKPMWGTFRVWDARPTPASILFFIHLGALRFQEFPADVASISTCIGLINIPIIKFSVNWWNTLHQPSSISQFGTPIHISMPIPIFSIFASFLFSTGILFISETRQIILSFHFQRKSQ
Function: May be involved in the export of heme to the mitochondrion for the biogenesis of c-type cytochromes. Subcellular Location: Membrane Sequence Length: 228 Sequence Mass (Da): 25787 Location Topology: Multi-pass membrane protein
Q7PK15
MECFSKVIVLYQILALQWFSPKRYRTFDCESLFFITLNFCIITGLFCWIYQHQSLVIYSDNALGYVVDFLKFLLMVFTYYSLFLESGYQRGVLYKVWDELERLHNIFPSAKWALQPQAHLRTVALFVVYMSWWELTYAYWITKSARSSNFTILFWVLFLLLHLRQLQILLYTNVLGFCLKAINSELAWTIELSNGASRYGGRRSDGQICGYLRKLMEGFARVERLLELLNQAFGYSLAIIKLINNIYILTDTYWIVHGFMSGKVFDSVYLECCLSSKFICLMINLHSNERILSEFHRTRVLLHCIHLRWQLRCDQGWQMVQHFLLKLESTQPFTMTALSMYRLDYGTLMQIAFNVTTSISLFIQASQ
Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Subcellular Location: Cell membrane Sequence Length: 367 Sequence Mass (Da): 43337 Location Topology: Multi-pass membrane protein
A0A162SWJ6
MKPLQSRLLISFLAITLSMTVMNAIVIRIVATNHFRSFLNGQTRHTEIITMLVRHLTIALSQTLISMAIVIVILTFAISWWLSKRLTYPLRTLIEQAEALAKGHFFHNSNPSNSHNEITYLSSTLNHMSQQLAQQANLRERLIQDVSHELRTPLTALKASLAAIIDGVWMPTPERFALLMAEVTRFEKMVLDLERSMIQTQPTMRAKVPVNISNCLHLAIEHVKAIIEEKKIIFHVGILPVDQYVLTDADQLLQVFVNLLDNAYKYTLPHHSIEVKVEVTSRDIKTTIRDTGIGIPMKDLPYICERFYRVESSRDRKTGGTGLGLAIAKEIIIDSNGSLQIESQLGIGTIATVILPKVLSTFVSFS
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. EC: 2.7.13.3 Subcellular Location: Membrane Sequence Length: 366 Sequence Mass (Da): 41201 Location Topology: Multi-pass membrane protein
A0A6S7GN33
MMCIIRIFVALLAVINGLDGKAVDTAVNHQKKGLYFGLMISCETGRSSIDYLDYGCFCGLGGAGTPVDDLDKCCSRHDQCYSDLLTNNICQLSLSTYSITYKYHECSKCAQPDEYSWWDSLGYETVACRKALCECDAVAARCFKKAKFNDLFKHYDQAKC
Cofactor: Binds 1 Ca(2+) ion per subunit. Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) EC: 3.1.1.4 Subcellular Location: Secreted Sequence Length: 160 Sequence Mass (Da): 17890
A0A7D9I203
MKLPRFLFYLFLFVIILVLLNVLLMFYLTHSRIYALNDYEKFDFDYKVNEDSFLSIHDLPEDTSGEYYVHKNFIRSQSTDSSRDIVLASHCTGDHLHHLVSLTQVWQGPLSIAVFIPGYNLENTLSTLYILYGCFIKVRRQVTIHLVHPISVVLNDSDLMFLIRKSEEVHTKCSKALKEIKNTNKNVGINYDRKIEYPNNLLRNTAKQGVASQYSLVVDIDMKPNQNLYTDFMNFARKNNLFDGGNSFYNDKSVFVLPAFEINSKKTDDMPKDKSQLISLLDNGAVRPFYYDICWKCQRPTDYEKWRSLAGEDMDVGYEIKWQDPWEPFFISPRSAPDYDERFKQYGFNRISHACELHVASYRYFILDQGFLVHQGFKDGTSFHKTKNDENDKNRILFRTFKTELKDKYPDSVNRC
Pathway: Protein modification; protein glycosylation. Catalytic Activity: 3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP Subcellular Location: Golgi apparatus membrane Sequence Length: 416 Sequence Mass (Da): 48871 Location Topology: Single-pass type II membrane protein
A0A523JCR2
MGRAGELVLLVLAAGKGTRMRSRQPKMLHPVCGRPMLLHVTALGRGLGAKRCIVVLGSGQEELRGALAHEPVEIVVQSEQLGTGHALLQAREALQGHRGPVLIVHGDQPLYRTSTLETLLDVFRSRSADLALLVGELPDPTGYGRILRGPDGRIDRIVEETEASPEVRALREVNLGIYVAEAAFLFKTLSRVADRNEKREYFLTDIVELALEAGHRVETASLEDLSEGLGVNDRADLARAEAVLRRRIAEHWMTQGVTLVDPERTYLDADIEIGPDSVLEPGCRLRAGTRIGAGCRIEPNVVIDASSIGDNVLIKPHCFIEQARVGDGCIIGPSAHLRPNTQLEDGVRIGNFVEVKNSRLGRGTKADHLAYIGDADIGEHVTIGCGAITVNYDGQKKSRTVIGDGSFVGCNANLIAPVKLEANAYVAAGSTITQDVPGGALAVGRARQRNVEGWRQRRFGKRDAD
Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine Subcellular Location: Cytoplasm Sequence Length: 465 Sequence Mass (Da): 50205
A0A6N9GWK3
MQEPTTLPSDGSPPSNLDAEVSIIGSLLIDGDAILRIEPFLRPEHFYGEQNAEIYTACRELFMESVGIDQETVRDRLIAKDILEDVGGDAYLSAAVAATPHSVHIVDYAHLVHNAYVIRQLGQAGIQINEIGSNYSNTRDVDRAVKAAEEIIFRIGQTYESADFLPIRDARSIIEFFDPPTVDDTDESNQPIATGFESLDRVLGGFHRSDMIVLAARPGFGKSTLALNVGLNAAKNGKTVGIFSLEMGIDQVAHRMAAAHARINIQNVRNDHLTAAERDRLSDAYGYLSDMRIYVDDAALQTASALSAKARRLKLQAGLDFLIVDYMQLISGSSSGGREANRVQEVSEISRYLKAIARDLNIPVLACSQLNRAVEQRKSHEPRLADLRESGSIEQDADVVMFIHRDDKNMSEEEWNRRNPTQVYPRGLTEIMIAKHRHGPTANIEMSVRDEWGLFSSVSEPGMD
Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. EC: 3.6.4.12 Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Sequence Length: 464 Sequence Mass (Da): 51363
A0A7D9DKM5
MTSGRNLKCCSNLFCAVLFLKTCVVITTVYVLFNFHFNREKRHFSVQPLARSLTNWTRGYLDRYFERSTSKNSTGIPSKSHKKVLVLVGFNATKKRRVRKRNKRKDGKKRAIIFVGIISAPQLIFRRNALRRSWLKQCKRKGIPCLFFTDSQDMYGNKLPDHINVPLQQEQLLHGDLIQTQSPGGINFARRYLWILNWANARYKFEYFLRVDDDYFVCMDRLLLELPHRSREKLYWGHVHCSPAGGIRVDEGFVIVSNDLAQTFLREQNKTLMCHAYGDQAMAMWINNIPGVTYFGDRRVHHAVAARDHILQYYDDICGNFLALHGSYPVEVEKFWLHSLSKRKKKKYSIPGITYPCGTMDKTFNYTSFRGTYNAKPKPCRNNPIWNIAGFYRGRNGQ
EC: 2.4.1.- Subcellular Location: Golgi apparatus membrane Sequence Length: 398 Sequence Mass (Da): 46476 Location Topology: Single-pass type II membrane protein
A0A6S7FBY1
MGKKNRSNKDAKAKRSKPEEDAIVSSLLEKTSSLLATNAKEQWNEHVAIRELLDKIQKIQVQTEKDEKQKRSDFLPKFSEWLKENGADSENVEVYSSSDYDCGVRAVTTFQAGEKIFNIPRKLILTSEHSSSTFLGSIIETDKLLRVMPNVVLALKLLNESHEEDSFWKPYIDILPRKFSTPLFFTQEELSALQGSQVLNNVLNLYRSIARQYAYLHQIFKKIPTNNKLNFMKSFTYSQYRWAVSIVMTRQNQIPCSSGNGLHLALIPFLDMCNHCEGHFTTDYDLSTDSCVCFALYSYKPGDQVFIFYGPRSNSDFFVHSGFYYEENKHDLLHIKLGISSSDSLYTLKTQLLSQIPVNVKNLAVTNAEFPLTKDLLAFLRIFCITEDKGKQLAEETVENLQSLLCDHSVQVSKQNEKKVWSFLETRCSLLLRQYPTTKEQDDEALESCDLSENTQLAMKLRRNEKLLLIKAMSFCKDTKEHLLEDHLVIYPGPNSFLACVIL
Catalytic Activity: L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine EC: 2.1.1.85 Subcellular Location: Cytoplasm Sequence Length: 503 Sequence Mass (Da): 57722
A0A6N6L5T5
MQEDNKLSRRQFLKILAVAGGAGVVAKLGFDAISRLEKVSETRLLMGTIVNLTVIAPSQTQAQTALDGTFAEMQRLIATFDHRQVDSPVAVLNSTGKLIDASAEMLAVTAEALHVAEMTQGAFDITVKPLLDAYQAGRAPTQKEMDRVDYRGVLIKGKTIEVAQPGMEITFDGIAKGYIVDQGVAVLAEHGFHDVIVEAGGDLRVAGAGENGDAWRIGINDPRPTQEQMLETIAMAPGAVATSGDYIHVFTTDKSLHHIIDPHLGASPPELASVSVIACSAMLADALSTALMVMGPEAGIELVETLPTVEAMTVSKEKHTTRSSGFPTSA
Cofactor: Magnesium. Can also use manganese. EC: 2.7.1.180 Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+) Sequence Length: 330 Sequence Mass (Da): 34928
A0A6S7FXW2
MQLFYRFLHFLVTLIFSLLISFRYYFKLTRRKIRGVFYRTSECDIKNGVATLRSLPRHLTFIVMEKDVDLCILARLVVWSITAGISYISIQTSEGDLDKRKTEFYGEVYQIRQEMSTCDYELHFTDKDSAEQNGVNGAAHKSLRKVHVNILSYHEGKEDVTKAAQTFCTKVKNKEAQSKIMNIEHLSNLLEVNKDFPDPELAITFGPVDSICAYPPWQIRLTEFISIPSLQVMDHTLFLQTLQQYNKCEQRLGR
Pathway: Protein modification; protein glycosylation. EC: 2.5.1.87 Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate Sequence Length: 254 Sequence Mass (Da): 29564
A0A803J315
MPLQLNSTSWILLCLLLQCLADNPGVKIQITQNGLYYGAEYLISQISSVSLSDITGSVTIASQSMDYSLTQVKMVSFQYSNSSANFIPEKGFQISIYGGNSTVNGTWQLDSSIMQDSGLSILTLKGISATVTLGMRQSNKNMVSIFLISCQSEINGIDFRVEGGVDYVYDAVKGPMENIIRSKVNEMLCSALRLQISDWDQSLSAFLSNMSLSSGLDLSLTKDPIFSKQYAEMDVKGGSDTNISMAGGHPSAPMTFSKLPDSMVQVCISEFSLNVAIRASFAANVFTNLFSGFTSFRNIRTSDLSDFLPEISQHFPEPSPVQIRIYQSTAPTLYVKPSNVTVAFVGVLQTYAMPSNTTRRLLFTATTAFSISSNISVSNKSQANGMNITGSIILSSFQLQINRNESSINIPEDVSNEKGIQDIIKVTFTTFLNEKIGKAGIYIPLDFLRNLSIYMKDRFILLAGDLQMSSDFLSS
Function: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Subcellular Location: Secreted Sequence Length: 475 Domain: The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues. Sequence Mass (Da): 51966
A0A6I8R6U1
MARTSLQVCALLLAISGMTCILVSTVSTRWRVSSTAGTIITATSIFEGLWMNCIATSSGSVQCKRFSSMFSLAIHIQVCRALMIISLVLGLMSCIVSIFGLKCTKFGTSNEQTKGKIALSGGLIFILAGLLTLTAVSWYAAMITAQFFDPLYLGTKYELGSALYIGWAASLLSILGGSFLCCSFKKKKPATKAGAYKYNYQDPDSDFKQFKERKETSVASKAYV
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Subcellular Location: Cell junction Sequence Length: 224 Sequence Mass (Da): 24217 Location Topology: Multi-pass membrane protein
A0A6L7JH07
MYPWLSARPRIRSRGPRGRNGDGTPRAPDSCHDGPREERVGPIDSLQLKSPAKINLGLEVLRKRTDSFHDLSSIMLAIDLCDEVRVRPVDDPENSEQHDEFSHSGLTEQALNAYCSSVRVKTKPNASVKKTIPIAAGLGGGSSNAAVVLSAANHLSGRALSDSELADVASHVGSDVPFFLSGGCALVAGRGDIRKRDLPIPKVWIVLANPGVELSTPDVFRELDSSEFTSGARTRVLAASLATEKPRWDHLHNGLQAAAERLCPQIRETLAALRAHTPWTLLSGSGATCFGIFEGEESSLAAEKDLTLAGYWTWAGRPMGRWTIADLRI
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. EC: 2.7.1.148 Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+) Sequence Length: 329 Sequence Mass (Da): 35513
A7DT64
MQSASKLIYRGKLLGSLPTVGEIHKEIAVSEETVTWISLQRDIIANILLGKDPRLLVIVGPCSIHDVQAAVDYAKRLFVLQNKYLSKMYIVMRTYFEKPRTRKGWKGIMHDPDLNGSYDVEKGIRYARQCLSSITTMRVATATEFLDPFLTPYIADLICWGAIGARTTESQTHRQLASGLHCPVGFKNSTDGNINLAIDAIIAAREQHIVYMTSLTNSISTLLTDGNPHGHLILRGGREPNYGLSDITKAVKLMHDEGINHRLIIDCSHGNSGKVAKRQISVARQVIDNRKKIPGYVAGIMVESFLQDGKQSDSFPLEYGQSVTDECISWQQTEQLLSTLAAQL
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). EC: 2.5.1.54 Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate Sequence Length: 344 Sequence Mass (Da): 38225
A0A853T408
MQRIGFSGTLDPITNGHMWVIGEARSLADEVIVFLSQNPAKRPQFPAEDRKRIIEQSARECGWDNVQVVIVKGDYTARAAKKHGCDYLIRGIRTTADFDYENLIQQTNVDVLQGAKTIFVMPPRDLGSVSSSFVKALEGPVGWNWTMKKFVPGPAYQAWILDCLRKEWEALWHYATASQADIALADHWFAHLTGPQAYGGADRHYHNLDHLVHGLSEIRVWADNTYTPKRDSALVKKAFWFHDAVYSHDDDALYSSEEASAQLWLASGLDAGDNQDVAQLIRATDHFQGPGISHALKDAMLSADLAILGQDEEVYQAYTQAIGREYAHVDPARFNEQRGLALQHLCAKAQAGQLFGDAYFADQYNERAIDNMQKEIAALAGG
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate EC: 2.7.7.3 Subcellular Location: Cytoplasm Sequence Length: 382 Sequence Mass (Da): 42622
A0A2E7URL2
MPTIADILQKTEDWFRTRGVPSARRQAQATVGFAIGVEPLQLVLQHDKPLSDAELEQIRAIVKRRGAREPWAYIEGSAGFHAFDFVVRAGVLCPRPDTETLVDAALALIPESADPVYVADVGSGTGCVGLSIAGSRSGVRLYATDVSDIALDVTRENVAALDLSQRVAVLSGPLLEPIPPSRPIDIVVSNPPYIPSAHIDTLMPEVRDYEPRLALDGGADGLDVYRALIPTAARRARKAVLVEIGHDQAEAVTALFRDAGLHHVQVHKDLGGRDRVISGHVHPVDQPAPDTAASADGDHQPARVFY
Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif. EC: 2.1.1.297 Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine Sequence Length: 306 Sequence Mass (Da): 32846
A0A534YIR0
MPGPTVRHDFPILSRTVHGQRPLVYLDNAATSQKPKPVLEAMASYYERSNANVHRGIHLLAEEATEELESARTVAALFIGARSEHGIVFTKGTTEAINLVAEGWAAHKLKPGDEIVVTALEHHANLLPWQRAAARSGATLRAIPATPSGELDPDFVFGPRTRLLAFSHVSNAVGTLLPVARLVKAAKEHGAVVVLDAAQSVPHLKLDVHALGCDFVAFSAHKALGPTGIGVLWGTPDRLAETEPLILGGGMVREATLGSATFLDPPRRFEGGTPPIAEAVGLRVALEYLTRIGMDRVQAHDRALVRTALDRLRQIPDLTIYGPDVPEDRVGIVSFNLRGVHPHDLAAFLDQRGIAVRAGNHCAQPLMTALRTPGIVRASFALYNTLDEVDVLARALHEARELCP
Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. EC: 2.8.1.7 Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine Sequence Length: 404 Sequence Mass (Da): 43507
Q5TR92
MDLRASAESGHNNELTMTEERKITSTPVMEFYRDKCVLITGGTGFIGRLLIEKLLRINVRQIILLSRPKKGKTTQQRCDDLFSSIVFMNLKKDCPTFIERVKLVDADLQHPSLGLSDESIEYIVNNAQIVLHAASDVRFDQALKKAIEVNVRGTRDLLRIAEKIVNLELFVYISTAYSNCPQGLIKEQFYTPPSEPEKMIQLVEAMDERFEEHMNKTVNDFIHPWPNTYVYTKALTEDVVRQYGELLPIAVVRPSIVIATNEEPIGGWTDNIYGLNGVIAGVALGIIRIMHVDDNNKADIIPADIVVNTVLAAGWQTYVERFIYHHLRKGDRPLPEAKTNGELKGVAKPRTKIYNCVTGNDNPISYQKIYKYSIEVGKHCPPKKSLWIVCHNTTTNKYLYEFYKVIYHLLPALLIDTYLRVIRRTPRVMDLYRKVHKFATVIEYFANGRWTFENDNLKSLREKLSPDDQIMFQCNIQKIEWADYFWTYIHGLRKHIANEPLENLDEAIKRHKQMRIVHYFILAAYYSIWALLIFYLCKAVGMLVF
Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. EC: 1.2.1.84 Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+) Sequence Length: 545 Sequence Mass (Da): 63059
A0A162SUZ5
MARAWERPVGTRDFFGDAMRQRNQIIHAIRNTAKTFDYDEIETPMLEYSQTFQFGLLRDDEERLFRTFDPAGHTLALRPEMTTPVARVAATLLAREPLPLRLMYAAKTYQTPTLRAKQTIEVTQAGFECIGDEGLEADAEVIALAVRSLQALGIQTFRIAIGHTGYVQTWFEKIPETLARGLRQAMLEKDWVQYETELKPYQSATWYDAVRSLPRVRGTRTALLQARSAATDPAGRACCDELLTLFDLLDLYGVLEYVHVDLGLVLDHDYYTGPVFEGYAEHLGQPICVGGRYDNLLGCFDRPLPATGCALFVERLMRVVAEPQEEEERIVVRYVEKGRMSALSFAEWLRRKGSIVRTERMPSDAMGAEGETAGGCSGGIMRVLEVSGARVHGDVRLQDDYRAFLREGGITC
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. Subcellular Location: Cytoplasm Sequence Length: 412 Sequence Mass (Da): 46348
Q7PYM6
MRKFQRFLASVVALAVLYGVYRYSFRKDSEGNYLFLLPGEGGRSASDSEQQSSAVSSEREWSSVDPSRLANLTGFEYVIANDICKENGSFSELLGVILVTSYVGHDEIRAAHRQAISQQKLLSMGLLRIFSLASIPPTERFITQAAIEAEQRLHGDLIQGNFVEAYRNLTYKHLMSLQWATQHCRGAKYLLKMDDDIVYDPFYIQNYLSDLHQSDEARTHRHQHLLAGYVFRSKKVIRLQANKWYVSRDEFPGDIYPPYLSGWLYITNQRTARALAAESQKAGSNFFWIDDTFITGILAQRLQIQPIALNRWYSSNSEFLDCCIRDMKRYSYQCDYYVGPNGGNGKLIMEFIQELERCYDNACYQRPPGKSLTATCVAEYKQQIQPDHGTAMISQMKLRK
EC: 2.4.1.- Subcellular Location: Golgi apparatus membrane Sequence Length: 400 Sequence Mass (Da): 45953 Location Topology: Single-pass type II membrane protein
A0A6L7YFK2
MRVLGLTGGIASGKSTAAAQLKELGVVVLDADRYGHRAYEPDSPGFHAVVNEFGHDIVGEDGEIDRRILGGKVFGDPEKMERLTDIVWPEIRRLAAEEIAELREREPETVIVLEAAVMIEAGWQDLCDEVWVIATEPATAIKRLRDRNSLNAEQAQARLDSQLTNRERRRHAKIYIDNSGTQKQFRDQIDHEWMRLHRRIKQAEGRARAQARREAEARAAARAKGG
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+) EC: 2.7.1.24 Subcellular Location: Cytoplasm Sequence Length: 226 Sequence Mass (Da): 25465
A0A1U8CCL1
MCCQFLRQLLAKESQHSTPVGRFLLPVLMGFRLLLLISSGPGVFGDDEKEFTCHLGEPGCKTVCYDVFRPLSPLRFWAFQVILMAVPSAVYVGFTLYHVIGYREEPGKENKGQESRMGHGEDVSGAASFRLLWAYVAHLGARLALEGAALGAQYHLYGFKMPGTFLCREDPCIGSITCFQSHPSEKTVLLNAMFGISVACLLFTSLELVLLGLGRFWRAYELKLPFLKNLPTAKSSVRRKDPADDLSVVETKEPL
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Subcellular Location: Cell junction Sequence Length: 255 Sequence Mass (Da): 28313 Location Topology: Multi-pass membrane protein
A0A2X1KBA9
MLKEQGLTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKVDANIAEQVIIQYGGSVNASNAAELFAQPDIDGALVGGASLKADAFAVIVKAAEAAKQA
Pathway: Carbohydrate biosynthesis; gluconeogenesis. Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate EC: 5.3.1.1 Subcellular Location: Cytoplasm Sequence Length: 141 Sequence Mass (Da): 14504
A0A496ZHX0
MKLEEIRSRIDKIDRELLVILQERMGLALRSSKFKETVSDPEREKSMLARIERMNLDLIKGSFSKQLLQTIITESKRLQKENRPLVAFQGEHGAYGEVAARRLVPEGAYIPCMEFVDVFRGVEEGALDLGVVPVENSLEGAVTQVNELLTTTRLKVIGEAKVPVNHCLLATEDTDYREIRMVYSHPQALAQCRGFLTRNKLEPRPFYDTAGAAKMLARENLKAAAAIASALSAELYNLEIIKEKIEDGPSNSTRFLLLSREANVGGGNKTSIIFATPHTAGSLYSVLRLFAETDINLTRIASMPLRSEPSNYSFFLDFEGSESNEKIADVLDKMEKLTISMKNLGTYPADDGKQPVACLKQVSDRKKD
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O EC: 4.2.1.51 Subcellular Location: Cytoplasm Sequence Length: 368 Sequence Mass (Da): 41059
A0A935ZQ66
MIGWLSGTVFAREPIAGEVILDVGGVGYQIAVSLQTLAAVPECGRPCALWIHTHVREDALALFGFADPIERRAFRLLLGVPQVGPKLAIGVLGGFPLAELLAAIEGEQRTLLERIPGVGKRTAERILLDLKDKVGVLRDQLGSGRAPSQPVTPDGSSFADDARAVLVNLGWKVKDVDAALTKVDDGEQPSLDALVRRALAQLMSRP
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. Subcellular Location: Cytoplasm Sequence Length: 206 Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB. Sequence Mass (Da): 21956
A0A536M6X1
MVRLFRRKKDEEPIGAEEDAAGVTAVTEGPVPPPEATAPEDEAAPVDQAVERTRRTWFSRIGGMFRRGLNEELWEELEETLVAADTGVTTTIKVIDDLRERVKQESIRDPEQALGVLKEDLIATLEVDTGRGQIWHSNGHRQTLPRPAIILVVGVNGTGKTTSIGKLAHAYRSQGKKLVLAAADTFRAAAIEQLKEWGQRTGVDVVAHKQGADPGAVVFDALSAAESRGADVLIIDTAGRLHTKAHLMEELMKVNRVIQRKYPEAPHEVLLVLDATTGQNAMHQAKYFTEAVGVTGVVLAKLDGTAKGGVIFSICDQLRVPVRFVGTGERPQDLAPFEPREFVEALFAS
Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Subcellular Location: Cell membrane Sequence Length: 349 Sequence Mass (Da): 38016 Location Topology: Peripheral membrane protein
A0A3L7WEV0
METERLHAETLAAAAASIDRAAAIIRRGGLVAFPTETVYGLGGDATNPLAVARIFEAKGRPTFDPLIVHVADRADLVRVFTTEALRDPRLTALADALWPGPLTIVAASLAEIPGLVRAGLPNVGVRIPRHETARALIRAAGVPIAAPSANRFGLLSPTRADHVLNQLDGRIDALLLGEATEVGVESSVVALAPDTPAVLLRPGGVPLEQLRELLAPYGGVEHADRRAPAPSGAALPAPGMTTAHYAPRTPLYVVVPGEVALLRTKLPHLQRVAVVGPDDAATKALAEAARAAGLTVAQSVALSPTLDHARAASRLFDLLHSIDGALGGERSAGILVAPYPSDGLGLAIADRLHRAAAAQHQRDA
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate EC: 2.7.7.87 Subcellular Location: Cytoplasm Sequence Length: 364 Sequence Mass (Da): 37695
A0A0A9YDE2
MSEILSPRESGVFISKNAKHVSIHEEAIPKMVHDLYLALEKGGLRKYSITEHETFPSKHLSQKEALNYVLFLDALNFCFWSPPGKPHWTVKFQDVSYTGYFALCAAVARAYDEGIHIFDPTVYSKFTLSELEEMLKGENGVPAPMVEERLKCLQEVGTVLLAKFGGSFENVVLQAKNSAQALLKLVVENFPCFDDSCDYLGKRVSFHKRAQILVGDVWGLYYGQGISEFRDVDTITMFADYRVPQVLVAYGILQYSDELMGVLRKNEILQSGCEFEIEIRGCSIRAVDLVVQAMREYMRKDDRVYYSECNDISVDNYLWSYRREHVARMDATPFHKVISIYY
Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly. EC: 3.2.2.- Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-phosphate + queuine Sequence Length: 342 Sequence Mass (Da): 39197
Q8VQ48
MSDKSFIAVVMAGGTGSRLWPLSRELYPKQFLKIGGELSLLQSTLNRLSKLSFDAPLVITNDNHRFIVAEQLRQMNQLSGNIILEPCGKNTAPAIALAAFSALKRDKNKDPILLVLAADHIIKNEEAFCEAIKSAMFMAEEDKIVTFGIIPTYAETGYGYINIGARVESNIEVDNAHFYVAKKFVEKPERELAEKYFSSKKYLWNSGMFMFKASVFLSELKKYRPDIFEVCEEAISASSKDLDFIRLPERMFEKCPSESIDFAVMENTKRCVVCPVDIGWSDVGSWQSLWELSDKSPSGDVCKGDTLTYNTKNNYIYSDSALVAAVGVENIVIVQTKDAVLVANKSEVQDVKKIVDLLKKNNRTEHVTHREVFRPWGKFDSIDQGDRYTVKKIVVKPGEGLSLRMHHHRSEHWIVLSGTAKVILEGTEKLITVNESIYIPLGASYSLENPGVIPLILIEVSSGDYLGEDDIVRQKERYKKKINHE
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1. EC: 2.7.7.13 Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose Sequence Length: 485 Sequence Mass (Da): 54622
A0A8T7EAF1
MNKFFGFLIILFLLAMTVCGVGSSLDGLFLIHGGSMEPTFPQDTILGIDNEAYSTSLPQRGDIILFDPPHNPNDDVLLLKRVIGLPGETVEVWAEGVFVNGTLLNEPYNYAK
Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. EC: 3.4.21.89 Subcellular Location: Membrane Sequence Length: 112 Sequence Mass (Da): 12271 Location Topology: Single-pass type II membrane protein
A0A350IUE7
MRRRQAGRLGVVFALIGVVVVLVAAAAATLLFGRVELEAAGSGSPVVITVRSGESLSQLADALESQGVIKSAFWFSAYARLRGVHLHAGNYQVDSAMEASEVIDVLEGAPYCPPVSFVIPEGFTVAQIASRVAATKGLDVTRQEYLDAVAQDSYDAPFLSIRPAGDTSLEGFLFPATYSVPDCATAHQVVQEQLDGFRSNVVPDLPSSGSQAYADLITASIVQAEGVSSSFANISSVVHNRLAIGMNLQIDAIVMYGLHQSGLAMSAADEATDTPYNSYLHPGLPPTPIDNPGLATVQAAVHPASTPYLFYVSACGQTYYSITDAVHEQQVQEYEGKPCS
Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. EC: 4.2.2.- Subcellular Location: Cell membrane Sequence Length: 340 Sequence Mass (Da): 35917 Location Topology: Single-pass membrane protein
A0A6I8R1Y3
MHGFQAGMNITIVQAISSLKKYPLPLNSGKEAKILQNFGDSICKMLDDRLEKHYAECGPNIPIHTVPSSSSTLRKAQRQPKAPSPLSIPHALEPPEQESQDLSPSKKKKTGGKKQREYVPQRRSGGYAVLLTLYRDTKSPSSRGYMTKAELQKEAQPLCDKSFTLTDPNSKYTAWTSVSTLIQKELVIKTHSPARYSLTEKGLELAQRLEEAEDQGRADGFPRQVQASSNEEEEQEEAESETNPYIHADPVQCPDQQLNLAYSHNAKNTSSDPPSVQYNHVPEFTLHPGDFNILLCVDFIETTGGAAHRKQELVTELRRNGVNFDVRKLHIGDFLWIAQEKVQPVPGQLRIPQARELVLDYVVERKRMDDLCGSIIDGRFREQKFRLKRCGLRRPIYLVEDHGSAQHLSIPETTLQQAIVNTQVVDGFFIKRTKDVRESAAYLTIMTRYLQGIYSRKSLLSCTKEEEWKCDRSLRPDASSCILVEFKDFNEGAMKNKAQTVKEVFARQLMQISGVSGEKAAAILEKYSTPASLMSAYESCSSAEEKEKLLSSVKCGKLQRNLGPVLSKTISQLYCTKEPLS
Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). EC: 3.1.22.- Subcellular Location: Nucleus Sequence Length: 581 Sequence Mass (Da): 65341
A0A661WGM3
MTEFILASKSPRRKILLRNLIDPFIVVNSEVEEQEIPGEKPPELVKRLAKEKALQGAANLSPNSLNNALVIGADTIVVDGEEVLGKPLDQADAARILEQLKGKTHQVLSGIALYDLSSGEIRTSLVCTEVEMREYTEDEIQEYIASGDPLDKAGAYGIQNRDFNPAPQFYGCFANVMGLPLCHLAVLMKEMGIDTDHRVAERCQESIEYQCPVYNDILAGVKRNNPESN
Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP EC: 3.6.1.9 Subcellular Location: Cytoplasm Sequence Length: 229 Sequence Mass (Da): 25300
A0A3B9MCE9
MSTPAQRMVAEQLLPNGVSDPRVIEVMSEIPREEFLSSRVRRHAYENRALAIDCGQTISQPLVVALMTQALAPKAEDHALEVGTGSGYQAAVLSRLVRHVITLELEPSLAEHASATLSRLGYSNVEVAVADGTFGWPAYAPYDIILVAAASPDVPPALVDQLAPDGRLVIPLGRSSDEHQDLRVYQRRGEVMAWRSLFPVRFVPLR
Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine EC: 2.1.1.77 Subcellular Location: Cytoplasm Sequence Length: 206 Sequence Mass (Da): 22545
A0A6B1A640
MSTQTSVSDNETIVARDRVELLRAEILRHNHLYHALNEPEISDADYDALFAELKSLEARYPELASADSPTQTVGAPPGRTFAVVEHRLRMLSLGNAFNAEELLAWRQRAADLLDREEWTYVSEPKIDGLAIALVYEHGRLVQAATRGDGRAGEDVTANLRAIDAVPNELSGNPPPRFEVRGEIYMPKSGFDAMNAEIAEQNERRRDEGRASLTLYANPRNAAAGSVRQKDPSVTGTRPLSIGVYQLGWCDDAVTPDTHWETLGWLSEFGFPTTPDAAHHSGIEDALAACERWTQRRDSQAFEMDGVVVKVDDLGLQADLGIVGREPRWAIAWKFPPQEASTVVEQILVNVGRTGSINPYARLRPVRVGGVQVTNATLHNLDDIRRKDIREGDTVVIRRAGEVIPQVVRPVLERRADDSVPWTMPDDCPACGAGIVRSDDDAMHYCSDRSCSAIQQRSLEHFASRGAMDIRGLGEKMIGLLLAEGLICDAAEIYTIPDRLEELARVPGLGQVKKRKNEETYEVGDRLRNLAAAIERSKSRGLSYLLVGLGIRHVGGENANLLADEFRSLDNILLAPAESLAAVEGVGPIIAESIVEWALDGDNWSLVHRLQAAGVEDEVQRSDDEPVETPLDGLRFVLTGRFGAMTRPQAEAQLKALGAAVGSSVSKNTTALFAGEAAGSKRTKAESLGLPIWDEDRLIAALEEPSALLNWLTEEEPADAN
Function: 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. EC: 6.5.1.2 Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide. Sequence Length: 720 Sequence Mass (Da): 78791
A0A6B1DZR4
MTHIPVLLDETIVALMPDGVAPARLVDGTVGAGGHSQALLEAGAGRLLGCDLDAQALRIARQVLGGHSERTNLFHGSYLQMADYARELGWPAVDAILLDLGLSSLQLDDPVRGFSFRYAARLDMRFDTTSDSSAQDLVNTLPAGELARLLFHYGEERHARRIARAIVAARPVCTTRELADLIAAALPAASRRASRIHPATRSFQALRIAVNAELVAIERVIPIAVDLLRAGGRLAIISFHSLEDRIVKKAFRELAENRIAPPGMASLGERRARIRLVNRKPIIPSQAEIQRNPRSRSAKLRIAEKL
Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine EC: 2.1.1.199 Subcellular Location: Cytoplasm Sequence Length: 306 Sequence Mass (Da): 33379
Q7QA55
MSEKINSKKSPRISKMTNRSFLWGVMAAFLTWSISIYLYWNLSNTPTNGAGGSEQRLAKAPTSATAAEDTRQLILRNQNSLIDASDERLHKKSSKWAEKGKSLFKEKYARFMHEKEKRRISHRLIDELQPMLIQPNGTDEFGMVQNSEEQFIRDIGYRKHAFNVLVSNKLGPFRPIPDTRHKLCQAQVYDKVLPVASVVMCFYNEHLETLVRSIHTVLKRTPAYLLKELILVDDCSDFEDLTVGGQLEKELAQLGTNKVRLLRNTDREGLIRSRVYGARNATGQVLIFLDSHIEVNVDWIEPLLARIKHDRTILAMPVIDIINSDTFVYTASPLVRGGFNWGLHFKWDNLPKGSLERDTDFVGPFNSPTMAGGLFAIDRAYFKELGEYDMGMDVWGGENLEISFRAWQCGGSIELLPCSRIGHVFRKRRPYGSPDGQDTMIRNSLRLAHVWMDDYIRYFYEQQPQAHHVPYGNVSERQRLRERLGCKPFRWYLDNIYPQLRVPGEKTSSDARDATQPKFEPWHSRKRNYVASFQIRLSNSSLCLSTELDSEKSLWKKGSGLVLQPCLRVKHQTWYETEKSELVLGQLLCLDAPSSATKGRPKLNKCHEMGGDQAWKHRKTSGTPIYNIASGSCLTVKDIRKGSPVGLDLCVSSPRSTWDLVIS
Pathway: Protein modification; protein glycosylation. EC: 2.4.1.- Subcellular Location: Golgi apparatus membrane Sequence Length: 663 Sequence Mass (Da): 75780 Location Topology: Single-pass type II membrane protein
A0A936PWX1
MFPDLLTLQTPFGVQALHTYGLLLILGFFAATLVTGARMRQVGMNSDRLVPLMLIAIPSSILGARLLHFLGSTDRADFLAAPWILFDLTQGGMAFLGGAIGGVISGSLYAKRAGLNVWKMADVGAPSIMLGLSIGRLGCFAAGCCHGTACPAPVEGMITGDLFPGGQLVNVEGFPWVAMVFNKGVGVGSIIGAPVYPTQLWESLGALTLFGVLSLMWRYARRFDGQILAATMILYPPMRYTIETFRGDELRGTNLLGMFSTSQLTGLIVLTISFGLIAWRWPKGLAPETPLTTSDLDPDLDPELLKR
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer). Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate EC: 2.5.1.145 Subcellular Location: Cell membrane Sequence Length: 307 Sequence Mass (Da): 32884 Location Topology: Multi-pass membrane protein
A0A6B0W9T6
MTQPIDEAMLNAARAARRERIYRLVRPLEEFGSTEAASGIVIVIAVVLAMIAANTALSSYYDDFIHYHIAVDLGFFHLDTGLQHWVNDGLMVIFFFVVGMEIKREVVAGELAGGRKVWAPIAAAAGGMVVPVLIFFAIVDDPTARQGWAIPMATDIAIAVGVITIVGARVPAGLKVLLLALAIVDDIGAIAVIAVFYTEDINLTALGITVGLLVLVYLMNRNGIEPILLYVVVGLFAWTTAHESGIHPTILGVALGIMTPLQPLYRSTVMPDLIEALMRRIRVIEQEEDVERRHHDRVGALLTLSELSDRAISPLDRIEHRLLPWSAFLVVPLFAFANAGVDLRGGALEESMSSPLALGIGLGLLVGKPVGVTLATWIAVRLGAELPAGVTWLGIFAIGLVAGIGFTVALFVTELSFEAELLLTQAKVGIFIASVLAGVIGLGMLYAASARISQR
Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out) Subcellular Location: Cell inner membrane Sequence Length: 455 Sequence Mass (Da): 48663 Location Topology: Multi-pass membrane protein
A0A938RB42
MVTGQRPVLPRIFELLKMTMNPKRVVIIGGGPGGYVAAIRAAQLGAKATLIEKDKIGGTCLNHGCIPTKALLHDARMLHSLRRSSVFKILSIDPSGLLEPMMDRKKKVVEELVKGVEILLESHRVVVKKGQADLISPNQVVLFDGEDGKEILEADAIILAPGSKSKALPGLTPDGDKIITSDEALEIKKIPRELVIIGGGYIGIEFATLFNLLGSRVTVVEILENILPGLEGELVRNLRRFLERDGVKILTQSSVEGVQKNEDGLRLMVKTPQRTQEINAEKLLMAVGREPSLDLNFSKAGIETSPKGIKVNRHMETTSPNVYAIGDAVEGIMLAHVAMEHGMVAAENVMGLNREWDSPLIPLCIFSHPEVASIGLTEKEAKAKGEIKIGRFSFRSSPKAVISGETDGLIKVIASRENDTVLGVHIIGPEASVLLSIASTMIESKLKEFTRFIQAHPTIPEALKEACLDADGLAIHLPKPLRSLSPSPHGGRGRPAYR
Cofactor: Binds 1 FAD per subunit. EC: 1.8.1.4 Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH Sequence Length: 498 Sequence Mass (Da): 53929
A0A179HLJ9
MTKIPYNRVHVRGDVLFTARGGNIHSFSLLDGSHISAWQHPDVAKVAEAMKAIADAQKAGEAEETQGQIQGTEESEPPAKRQKREGDEGAGADDAPAQKEDVVVPGDAPKEHSKKKGKGGKGNASAKKQVARVPDRPVITLLTSTTDGQHVLAVSGHDKVIWVFEHDGQGGLSLLNQRTMPKRPCAIAIAPDAQIICADKFGDVYALPLIMTERSPSSGAGRVSTSTPAKKSSEPAANTFTVHSQRNLEALENQRKQLELQRQKAAEKEEGPDFDLTLLLGHVSMLTSLVLAESDGRRYIVTSDRDEHIRVSRYIPQAHVIEGFCLGHKEFVSEVAIPASRGDILISGGGDEELFVWDWKAGKLLSKASILSLAREIAPDTSKVAVTGICSLTYPSESGDLTYVLVICEQIKAIFTWQLTPDNILNHPGVIQLPANPLQLAVANAEPNSNTLPKIIVAADPGQASEAKSLQIFALAMSEGRLSVAKELPVHDDKLESSAAEASDKEIHNLLYTVENLRKQTGGTDGEAGEDEPEADVEGDIPAKEA
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. Subcellular Location: Nucleus Sequence Length: 546 Sequence Mass (Da): 58632
A0A4Q0DLR6
MIRMILAINNQCFIGKNNTLMYRLKDDMLNFKKMTQNNIVVMGRKTFESLNNRGLPNRLNVVVTSKAETFEDIQTITTHDMKRSETFTKEGHVVYITPDSFINQFLPFHRDSEDEIWVIGGAQVYEAATPFASEIICTFVDDDEVGDVALKPKLFGGFTHLATLKSVDVDEDNDKPYEITQLVRHEDLEHKLRELQAQQHEMEKEQTQNNLSTPLENGGLRQGEAFVIAATTSAALSQIDTESREDSSDSDSSSSDSSSSSSD
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. EC: 1.5.1.3 Sequence Length: 263 Sequence Mass (Da): 29595
Q4H2Q1
MLDNGLPRMQCRCIGECPDHKYNSTCDLKPNAKCFKKLYINEYGEEELRAGCLGSQDDYLNQCHNKAKTEFEDPTAVACCNNGTMCNDYLDLGLPEYYDEPSDTPVSEANSDVITVIAVTVPVFCFLFGLIIMFYYIRLCRRESLRRRQIENENKKALCPVLYGDRGDLEGHNEMMENWSSLAGTSSGSGMPLLVQRTISRQIEILHEIGKGRYGTVMLGKWREEKVALKIFNSSDEESWFRETEIYQTVLLRHDNILGFIAADISGAGSWTQLFLITEYHKHGSLYYYLQNRAINIAEALKLAYTACCGLAHLHTEIAGTQGKPAIAHRDVKSQNILVKLDGQCCIADMGLAVCFSRLHETIDVGKHDRSRRQGTKRYMSPEVLAQSFHPDSFEAYKASDVYSFALVLWEIINRTEVNGFANDYHLPYHDVVGNDPDFDEMRKIVVLENLRPEIYKQWQAHKIMSTYTTTLQECWSPRPESRLSMLRLRKTLYFLLNGGRGPVEAGSSESDRKPSASSSSSVKEEEHSSC
EC: 2.7.11.30 Subcellular Location: Membrane Sequence Length: 531 Sequence Mass (Da): 60307 Location Topology: Single-pass type I membrane protein
Q7Q823
MKSFTLLICYGLFVLHAARGDEWNYPTPGTNGVMSEPERWGGQCDNGRRQSPIDLTIAAAVRGQFAPLFFSNYMLPLKQPRVTNTGHSIQINNRDSAITMQGGGLGGRFVLDQMHFHWGSEHTLDDTRYGLELHLVHHDTRYASLEDAVQARNGVAVLGVLFHVGSQPNMHIDTILDTATEIQNEVGKEALLRGKLSPYNLLPSNRTSFYRYEGSLTTPACAESVIWTVFTESISVSLEQVERFKAIHDQTGRELVNNFRSVQPLNTRALVYATEWDQQGNNFATKMTSNVVFLGAIVLLVITSRLSYH
Function: Reversible hydration of carbon dioxide. EC: 4.2.1.1 Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O Sequence Length: 309 Sequence Mass (Da): 34543
A0A1B2I4J7
MAPKIGIIMGSASDIPVVEKGTPVLEELGIEFEVAIASAHRTPADVENYAKGARKRGIKALVAVAGLSAALPGVVAAATTLPVIGVPVKGGAMDGLDALLSIAQMPPGVPAASVGLNGAKNACLLAARIVAATDDELTAKLEAYAEKEASKVRESRKKLENLPAAPADAY
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2. Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). EC: 5.4.99.18 Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate Sequence Length: 170 Sequence Mass (Da): 17175
A0A8H8LYY2
MLAARTARRFIPPRTLLTRSFASSSEDYDIVVIGGGPAGLALAAGLGSNKFTSQFKTALVEASNLNNIRTWSESPGHYSNRVSSLTNESLAFIQGSWDHVESGRTCPVEAMQVWDGVSDARIHFLPSDLTRLPTTGEVPSSMATMTENLNLQRGILKRLDELPAVELLDSVKVENIEHGPDEGSNWPIVKTSNGRSLRCRLLIGADGFNSPVRKFAGIASSGYNYDTHSVVATLFHSERPNHASLAHMTQFNSTTAFQRFLPTGPIACLPLSPIASSLVWSTTPSIAGALKATSPETLAVFINAAFRLPEPALHELYASLLSSHQKSTPLLAEEAKAIVERAESSHSIQPHDARSSSVQTHTGVPPEGAHSFPPFVIGIQPKSIAGFPLKYSHAESYIGTGKGARTVLVGDAAHTVHPLAGQGLNMGLADAAALVNCLEHAVATGADIGSYTALQPYMRARYMPNQSLLLATDGLHKLYGTTSSPIVWARSTGLEVINELGPLKGALMGVAGASPETKTAVWNTLATGVENLVSAGDVLRALGGGLKDTISKIGTNVLQNGANAVRKATR
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis. Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6. Catalytic Activity: 4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] EC: 1.14.13.- Subcellular Location: Mitochondrion inner membrane Sequence Length: 570 Sequence Mass (Da): 60400 Location Topology: Peripheral membrane protein
Q7Q0V1
MNNYIKFMEVLGNVKHLKRTGWVLRKVKDCETVSGHMYRMAMMSFFLEDSHGLDRIRVMEMSLVHDLAEGIVGDITPYCGVSREEKLLKEFSAMTEIASLLGPNKDKMLALFNEYEEGKTPEAKFVKDLDRLDMVMQAYEYEKRDSCPQKLQEFFDSTENKFFHPLVVDIVNAIKEQRAKAASTVVDNPNC
Function: Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP). EC: 3.1.3.89 Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Sequence Length: 191 Sequence Mass (Da): 22030
A0A034WL87
MDSVFEAYLGPDGVLAGAVAGAVGEPDDIPKTNTTVWVLGKRYNAIQELDLIRRDIQSRLWCTYRRGFVPLGAPQLTTDKGWGCTLRCGQMILAQALIDLHLGREWFWTPEIRDATYLKIVNRFEDSRKSYFSIHQIALMGDSEDKKVGQWFGPNTVAQVLKKLVRYDDWCSIVIHVAMDNTIVTDDIYSLCLENPSNDETWKPLLLIIPLRLGLSDINPIYVPALKICFELPGSCGMIGGRPNQALYFVGYVDDEVLYLDPHTTQRSGSVGQKTTQDEIDFDATFHQRYAGRIGFQQMDPSMAMCFLCKSRLSFEVLLDNLRTKVLAACTQPLLEITKSRSAEWVSTPSAGIESNFTTINTVGLVNCNTSTISATAASSDATNSNTPRTTIAKSLGTSARATCAAAEAAAALENYKNRCYRTLSSCDSEDFENVNHIHATSLTRNGRDVDPDGDSDEDFEIIS
Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine EC: 3.4.22.- Subcellular Location: Cytoplasm Sequence Length: 464 Sequence Mass (Da): 51379
A0A814XNU3
MPPPTSTVSRKRTRSTNVSEDNNDHEQATSTSTIVSSQPISTAPPKRQRNNPPSTTSSVVSHTNYSLRNRSITSDTQHSSTRISSIENSQRYNLRPRHLQSQIQLPQISTSHSIGVSRRPTSTTHRQIPSTTTTTQQEQPTSSIVQPRQYRLVYISDDDDQPTTTTQSSAAIVNTTFNLVTDDEDDDLTRPQVPPRRTARSTSNTGHNTRSRTSTDPTNTTTIDNQDFSNGGVAHVRLNRAIEIVIDSIQSLEGAVNNFDQLVFRLIYGRLGTRNEFENIEGMIRLSRILNLNFPSRLTQDEIDALPKIKFIHKSESTSSILLVEKCPICLTEFNDQEIINKLHCTHLFHLECISTWLSENDSCPTCRRKRTTNLTSGVTVGVVVGRRKSEQTTNEQRAFDILAQNPLIDGHNDWAMIIRAILQNNISGHDFYNMTQYDRKNGTPSQTDIIRLRKGQVGGQFWSIYTSCEHQGKDAIMSFMEQIDVMNRLIEKYSDVFQFVRTANEIRQAFQAKRIASLFGVEGGQAIESSFSILRLFYQMGVRYMTLTHNCNTPWADQNQVDRINSTLIKNNGLTEFGEKIITEMNRLGMLIDLSHVSKKTMLDVLNITRSPVIFSHSSAWTLCNHTRNVQDDVLQLIKSNRGIVMVAFTPGFIICNRQRRVTIPDVAAHINHIRNVAGIDSVGIGADYDGIDDTPEGLEDVSTYPKIIEYLISQGNWTNDDIIKLIGGNIIRVIEENEKISRDLQKIIQPFEDLIPLNDLIKYNLTQCRYLDMYTDTSYL
Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid EC: 3.4.13.19 Subcellular Location: Membrane Sequence Length: 782 Sequence Mass (Da): 88530 Location Topology: Lipid-anchor
Q7QKD2
MGALIWRILVLCFIASCSQLPVTVAQYLSSCKTPGGDGEPGTCVLVRECPFARALLMKQKHSNNDIRYLEAIRCGMLETKALVCCNAPNITADSSSSSASIDGLVDGETIDGLVENRFSTPEEKRGLLPEVCGVDTYRGPIRGELAQLFHFPWNVLIQHRTKDGEHRCHCGGSLISDRYVLTAARCIMGIKKTWTIVSVRVGELNLQTDPDCDDSTAGVTECASPVEDIPIEKITVPSNYTGTGSPAVKQDIALLRLARRVEFSESVAPICLPLNTSNWVGYSTEQDGSFYESGWGKTPDAAAGGDNKWNYVSVGVAREVCRDRYPHASIDGEQICAMPRSEQNTCRGDTGGPLMYQSGTDGAWYLMGVGSFRKQCAIVGEPAVYTNVATFTDWIVENLEP
EC: 3.4.21.- Subcellular Location: Secreted Sequence Length: 401 Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure. Sequence Mass (Da): 43595
A0A1B8SYQ7
MYKLNEQQQHELLELLCALIRHKSENPPGEEQQVAEFIYHYFKQENIDVEMQEVAPGRPNVIAHLKGSGKGKHLLFNGHIDVVPCGCGWSTEPFDPVIKDGKVFGRGAADMKSGVAAMMYAATLLKRNQDAFSGNLTLVFNVDEERINLGMLHYIKDGISADYAIIGEPTSLGVCIAHKGVSRYNLSTKGTAGHAAKTRYPDSAISKMAKILPAIEQHRTSVEEISHPLLGNASMIITTINGGTAPNIVPQHCDIEIDRRLVPGEEKQEIEARLHQAIAQYNKGEEIDYHLDNYLFIPASDIPADHELTKVALDTVSRFTEKTAQPEIFEATCEAPFFSVTSEIPTLIMGPGGLAQAHVKDEFVEIKELYLAAEIYYDMANILLNK
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3. EC: 3.5.1.18 Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate Sequence Length: 386 Sequence Mass (Da): 42711
A0A5B0MVW2
MFNSNQTTTTTTTTPVRRNNRNSTIGLNSQQQQQQHSLPQLPSTTTTNQQQQQQQPYYNHHHQHQHSESLDYSSAEHLPNLKSSTHSSEHHHQQQQQLTNRHAISSPKLPKSEPLQLRSYSGVLEIRMPNEPQQQQQQLPRNSLNNKSVLHQSSNLSLDKHHRSGNPLISSTGSTLKPRRRPPRVYETHPGNLVFCCRGRLISSKPSHSIPLTRRRRPKNRRRIEEEGSRVEDRAGEEVEEAEGEGESEGRRLYLPLQTLASVALLLAIPILFLYSTAPTLIHRSGFGIFLLALFCYLWMLTLSSMAKTVSSDPGILPRGLDPNPEMVWKPAPIDPPASNDLPNSNLQSLSQQQHPGGGGGEKAFEYDQVGEWELLPRWIKVESKQLNPSSSNKPIPLDFLPDEDVGWIQSKWCSTCESYRPPRSSHCRMCDCCIDGIDHHCSYLNNCIGSRNYRSFFTFLMTSVMSLMMIIGCSIWKLFFELDRQQQDPNGGEGSNNSQAILDNLQRNPISIAILLLSFLLLLPISALLGYHMFLTFNGLTTVEYIKTQTTKRVLKENKKLISQIYEGEVVEGQREHPSRAEDEGGRGKRVWATLLRRLFLINPELQTHPSSADPQHNHPHPQTTTHSSHAPNHQPPPQIRRSNNFTIGRLCRPDTDPYIDWAGTI
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 667 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 75697 Location Topology: Multi-pass membrane protein
A0A1I8PBU2
MANLSRESAILFVLAYIFLQVVYTNSYSHFRLPTSIQPEHYHLKVITHMDNTATFRYEGQISMRFRVLEATNNITMHALNLNIDNTSLVLSKVKDREFHMCLEDIDILPEFDYFIMILCQTLIKDEIYRVQMKFSSFLNTKSNGYYRSSYKDAATNETRWLSVTKFEPAFARAAFPCLDEPQYKARFTIWLGHHRSRTALSNMPREKQKPLEDVHDYVWSIFEESVPMSTYLVAYSVNDFVYKASSIEMYKLVLRTWSRQDSINKSGYVVEMAPRILKYYEDVLGIPYPLPKMDQIALPDFNKGGMENWGLVTYAEKVLYYDPNTRSPLDKLHTVRLMAHEFAHQWFGNLVTMKWWSDLWLNEGFATYIASLCVEYIHPEFQAYITDSFFSLVSSFDKDVALNSRPLSQEVFRTSEIRNRFDTISYRKGSAVLRMVHMILGNDAFFEGVYDYLEKHKYSNANQDDLWYAFSKTANKCNNPLDMKTVMDSWSLQSGFPLVKVNRNYQTGTIEITQHRFVQHNIFIPDDEIRKCWWIPLTYTTAGEKNFRTTKPRYWLQCNETQVGVPVIFDNVAKSNEWIIFNIQASAVYKVMYDIHNWRLLSEALKREPLENFPILNRGQIVNDAISLAWNGYHGYDIAFDILEYLFKEREYLPWALAMRGLANVCNFLKAFPIQYESFKSFIRHIIAPVFKHLNGFSTLNLANLLPFQYRLKSIVIQWACRVDLKDCIKASKNYFQRWALSQGLEYDEIFLKDLRDTVYCTAIRHGTINDWNSLWQRYLETRDSLFLEALACSRNETLIEDFISLIFSPEKQISNRETIHAFNAIVNSEVGLPLAWKYFFANFPRLCKDFEISHLAAELTLSINSLNDLGDLMAFANPGEECCEFPLKITNSSMENIHFRIDWIKRNLDIIEAYLRNRLSTSRA
Cofactor: Binds 1 zinc ion per subunit. EC: 3.4.11.- Subcellular Location: Cell membrane Sequence Length: 925 Sequence Mass (Da): 108510 Location Topology: Lipid-anchor
A0A7D9L162
LSERTYSLWGYMWQNVNDFVNPLFNELKTHFLRPRTSPQYIRCWRAMYNRHENVMHSRETVTDAITSLVDQNDSIQDHISLLSKRIELMKIILDKETDNDLKIVNGPEEGVDKVGDERSEGEITTTTDNENPSCEVERELRRQGITLSELVSDNPRLSLDWQPFRGVTQCSCASPIDSLTRKYHCWNCGQVFCRRCIDYQTSLPGHYSENKVPVCKSCFKKIEKKPRTAT
EC: 3.1.3.48 Subcellular Location: Cytoplasm Sequence Length: 230 Sequence Mass (Da): 26767 Location Topology: Peripheral membrane protein
A0A084A2M1
MSSQTVAAKRWFSKEWLLEQKSLIALLVLIAVVSSMSPNFFTVNNLFNILQQTSVNAIMAVGMTLVILTSGIDLSVGSLLALTGAIAASMVGLEINAVAAVAAALALGALVGAGTGFIVAKGKVQAFIATLVMMLLLRGVTMVYTNGSPINTGFTDVADAFGWFGIGRPLGVPTPIWIMAIVFIAAWYMLHHTRLGRYIYALGGNEAATRLSGINIDRVKIIVYSLCGLLAALAGVIEVARLSSAQPTAGTGYELDAIAAVVLGGTSLAGGKGRIVGTLIGALILGFLSNGLNLLGVSSYYQMIVKAVVILLAVLVDDKSSK
Function: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Probably responsible for the translocation of the substrate across the membrane. Subcellular Location: Cell inner membrane Sequence Length: 322 Sequence Mass (Da): 33419 Location Topology: Multi-pass membrane protein
A0A944NEL1
MSRIAKSTLIIAFFFGIDKILGFYRALKINQHFGLSYELDVFNVANNIPDLLSALISGGALGVALIPVLSEYIKQKGKPSAWELFSRILNFAFITTGLIAILISIFAPWLVDKIIAPGFPYEQKLLTVELLRFDLLAILIFSISGLVMAGLQANQHFLFPAMAPGFYNLGQIFGILVLAPSEGLKIGSITFPAYGLGIRGLVYGVILGAFLHLTIQVPGLIIHKFKWTPKVDLKNPGVKKVLALLGPRVITMLFIQMFFIVRDNLASGLGEGSVSALNLGWFIMQVPETLLGTAVAIAFLPTISEIFIQGDKNEFMEMVNKAIRALIGITIPVAFLMAVGLKPLIIAAFPSFTQEGVALVLIASRIYLLGLTSHALLEITSRSFYAQQDAKTPLIAAAINAFLYFGLAVFLSRSLEIAGIAWANTIAFTTETLLLLYLLNRRYPGLARVKNTFLKIVLSSGLGALIFDLILQLDQLSTYSPLVQAAISTGLMGLVFILLIPVIWPELRPLVKSAQK
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. Subcellular Location: Cell membrane Sequence Length: 516 Sequence Mass (Da): 56284 Location Topology: Multi-pass membrane protein
A0A6N8YRI6
MEQQAQNAEREPSFEEALAQLRETVQTLEEGNVSLEEATRLLAQGAELARTCNDLLAKAELQVSRIRRNFQGQADKADEPDSLMASPQQDFGMFDDAPR
Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates. EC: 3.1.11.6 Subcellular Location: Cytoplasm Sequence Length: 99 Sequence Mass (Da): 11066
A0A936U592
MSMREAIRQVRDAAQTLNARGPKPFPVVVQGLEAVIVGGVLGVERKDWIVPGLRERVGAVLRGCPVERLADASVGARPYRVAPVSQDPANRLLHAVGLSLAERDRATLCFVGQGSASCGAFHEALNLAALHRVNLIIVAHTWNLDEPGAPLARQLAGTLASKALAFGVHATTVDGGLVTAVLSAVAEARAHGGPHLIEARLHRGDDPLRRAEEELTEHEPSAVAQTG
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). EC: 1.2.4.4 Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2 Sequence Length: 227 Sequence Mass (Da): 23922
A0A803JZ88
MDLRVLYLIQLGSCLLGVGAGSNTEEEEEERPEDAHPPGHKSHHWNYQDIHQWDSDYPHCGGPEQSPINVVTSATTFDSNLRPILLSGYNVPPSRTLSLENNGHTVVLDLPDSLLIIGGLPQTYRATQLHFHWGSQDDPGSEHTVNGQRFPGEMHVVHYSAEYSSATEASTHPGGLAVLGVFIQEGEEENPAFQNLLPYLQNITEEGESIEIPGFDIRGLLPQRLDRYYHYDGSLTTPPCYQTVNWTLFNQTILLSPEQMDLLEDTIHADHDHILQNNFRAPQSLNGRLVLSSFSPKVSGRRLPGAAPNPAGTSPAPDNSSPNHSSQGTGESVEASLSTGDMLAIIFGVLFSVTSVAFCLYVRRNRSRNKRLGNENKSNVIYKAATAEDNVA
Function: Reversible hydration of carbon dioxide. EC: 4.2.1.1 Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O Sequence Length: 392 Sequence Mass (Da): 43116
A0A2E7UV41
MLEPPTSPRPLRVEWLGRRPYLEVQEEMKALLLRRIAGDAPDTLLLVEHQPTFTVGRRRGAMASVKNPGEVPVVEVARGGDVTFHGPGQLTAYPICALPPHRHDLHAWMHGLEGVVDGVLARWDIKGERDERNTGVWVDGKKIAAVGIACKRWVTWHGVALNIKVNLDYYGRIDPCGMDSSLVTRMADHVSRCPTVRDTARAFSTEFRRWWMDWSKPPP
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. Function: 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. Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein] EC: 2.3.1.181 Subcellular Location: Cytoplasm Sequence Length: 219 Sequence Mass (Da): 24699
Q4H396
MATSSFLAWFWNERFWLPHNTTWADLRNTEDATYAQATDLWVMIPYSIVLYIIRFIIERLIARPLGRKLNISDIPNRPPSSNAVLDKVFSSITRYPKDERLKGLCKQLDWSERQVQRWFRKKREIHRPSKLIKFSETVWRLLFYTGVLTFGIFAMHFTSPKCPWETRMCWVGYPDKQQLTLSSYWYYQTELAFYASCTITQFFDIKRKDFWVMCIHHFATILLICFSYSINMLNIGMLIMQLHDFSDVFLEASKIAKYLKHDVLATTGLVCFSLTFMLARIVYFPFWVLNSIYFDAWEVVGPFPSWYIFCVWLSLLQFLHIYWCSFIVKGVVKMVKQGGAATDERSESEATDSDEGNEENRKKSGLGDAPSNGVTLRKPVAK
Pathway: Lipid metabolism; sphingolipid metabolism. Catalytic Activity: octadecanoyl-CoA + sphinganine = CoA + H(+) + N-(octadecanoyl)-sphinganine Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 382 Sequence Mass (Da): 44872 Location Topology: Multi-pass membrane protein
A0A2G6NL04
MAGLRLRKASLLRKGWQYDAVFGRGRRLRGEGYTLVVIENGQAESRLGISVHRKIRGAVRRNRIKRIVRESFRIGRSSYPQGCDIVCVIYPDFACTDPDAVTTSVKRLLACRGT
Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. EC: 3.1.26.5 Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. Sequence Length: 114 Sequence Mass (Da): 12867
Q5TSB4
MFRIADFTVRWRKMMNKFTCETASISLLHVSSVKSHLLSTMKGSNVASTLDESYENAISSLNSLQSNSSVLQDSILRKHSEDNKHINDTLKYLLRIGVSMDHLNQLPVIHVSGTKGKGSTCAMIESILRSNGYRTGFFSSPHLVSVKERVRLNGMPLSSDKFRLYFWKIYKQLLAYREHSRDMPSYFCFLTILALDVFLRESVDVCVIEVGIGGRYDCTNVLPKTGTVGITSLGLEHTKLLGNTLEEIAWQKAGIIKRGSDVFSVVQPSECMEIIREECRKLKANLFVVPSELKAYQWAKKPELVNESCDILDILELNTSLAIQIATNWMNKNISEISQENITSIVTKQTVEGIDRCFWPGRLQRILYDTKKTLYLDGAHTLESIHLCARWYNMKSHSQYKRLLIFNTTGDRDSAKLLSTLSSMIKFDAAFFTPSVPRDTVTCVDAMNHNFPFELQLQRCRQNYEYWSQTIQHKEGFLHESIESVFKQIDEDFVFKGETCDILITGSIHLIGAAFVALNLERFMCTSTTQ
Cofactor: A monovalent cation. Pathway: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. Function: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. EC: 6.3.2.17 Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate Sequence Length: 530 Sequence Mass (Da): 60369
A0A6B1BYA7
MSGAIQPYPWGSREVLPQIMGVPPTGEPQAELWLGAHPRAPSVLRRSGTNRPLNQVIANDPIGELGEDAAQTFGGELPFLLKILAVDQPLSLQTHPTLSQAQAGFDSEDEQGIPLDAEHRSYRDRNHKPELICALEPFTALCGLRPPDSAAALLDSLEVDALDPAISFLQAGEIAPALRWLLEQTPESGTEIAQQVAAACSKPGPFPDERLWGVRIGEQHPGDIGVAIALMLNLVRLEPGQALFLGAGNLHVYLRGAVVEIMANSDNVLRGGLTVKHVDVPALLDAVNCRPHDVLVQAPTGPCFTFEAPVPDFSLTRVELDGSQRFAPSGPEIVLCASGSVKVAGHKITGGGAVWVPAGAGALEMAGNALVFRAATGD
Cofactor: Binds 1 zinc ion per subunit. EC: 5.3.1.8 Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate Sequence Length: 378 Sequence Mass (Da): 39883
A0A2E5IVE0
MTETVATAEKLEGSRVRLSVEVPVADLQAEYGRAVQRVSRRVKIPGFRPGKAPRQMVENAAGMATVMQEMLETLVPRAYTSALEETGVTPVDQPELDISDPPSLDMPFVFSAEVAVAPTVVLGDIGDVSIDVPDVSVTPEEIDQELEQLRMSQSAWDATDRVAISGDMVQTRIQISAAGLDPDEPQPYNVIVGENGFPEGFDDAVIGQSGGDKVSYEADIPADDPNETLRGKKVAFEIEIDGVSERRLPELDDEFARSVGPFDDLEALRARVSESISERKTHEAQHQIEDGAVEALVGRTTFDIAEVLVDREREQVDKDRTQALVNQGVAVDTYLAMRGETRESWDDEAKTEALRRIRRSLALEQYAEAEGIAADAEELEAEIERVVAYYPEARRNLVRSNLARDESRAQVENTVRSRKALGKLVEKVTGGAELPHDHHHHDHDEPPPELAAVAEADESEGETLPDVDNAGAPETTEPERPE
Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) EC: 5.2.1.8 Subcellular Location: Cytoplasm Sequence Length: 482 Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own. Sequence Mass (Da): 52898
A0A7D9HU31
MFNQRVLVFLIVVTAVICLAYRVHLFYYSPRPVGPTTSYEVLVLPDKQRILYENKTTRLLRDLLQSSYLKIQPFKINGDDIMVFLHIQKTGGTYFGKNLVTNLHLERKCDKVVSMRSRFMCKRPNSDEFWLYARYSTGWVCGLHADWTTWNSCLPKLLKSRLSKKHFNETKLLYITILRDPVDRFLSEFKHVQRGATWLSSKFVCNNKKYKLPICYKGANWSNVSLSGFLNCPYNLAFNRQTRMLANLTEVECYIYDNKIEEFNYSQQYGKLMLESAKRNLRSMAYFGLVEYQRESQYLFEKTFGLKFKKKLTQVPGNETISGETSSTLTTRLLLRIRKATRLDRQLYNYAKALFFRRLKYFEKVDEMGKF
Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+) EC: 2.8.2.- Subcellular Location: Membrane Sequence Length: 371 Sequence Mass (Da): 43906 Location Topology: Single-pass type II membrane protein
A0A6S7FWV2
MKQQGILLLFIVLLYNISLAFFAPLESNDNSVSVEYGGVTAEQLLAYSKHDAKYNVISNEIDSFSWPSFLKGLECDACKFITGFMQGLFRLNKTDEFIASAAIFWCEKLKIEDTRVCSGIIPEFKNEALSVFDEVGLAPKEICGLILGPSCSVVRDLYPDWNISLPNVPKPPVHPIPSPKPGSPTYTILQLSDVHIDHQYAENTSTKCGEPLCCRKYNGEGKAGYWGSYECDIPMRTFEASLKHIKDIHQHIDFVYWTGDVPPHNVWNQSRTDQLVAMESAVKLFIKYFPNTPVYPAMGNHESAPVNSFPPPYVKGHSSNKWLLDAFADFWSFWLPSDTMPTIRRGGYYTVLHTKGFRIISLNDNYCNNENWWLLINNTDPAGELQWLIKVLQAAEDSKEKVHIIGHMPVGRSTCLKHWSWNYYKIIDRYESIILGQFFGHTHQDHFELYYDLENKTRATNIAYIGPSLTTYQNLNPGYRMYTVDGNYDKSTYAVLDHSTYYLDLVSTTRDKMVWKFEYSAKEAYRMSSLQPAEWDDFVTRLGNNYTMFQMYYKYKWKCSPFGAKCTTRACIVGEMCDLRSGRSHDDDFFCRNVTRPEYNMC
Cofactor: Binds 2 Zn(2+) ions per subunit. Function: Converts sphingomyelin to ceramide. Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine Subcellular Location: Secreted Sequence Length: 602 Sequence Mass (Da): 69293
A0A520Y320
MKRISPSGPVAGTVRLPGSKSITNRALLVAALASGESRLVGALRSDDTEAMIDSLSRLGVAVSWDGYDLIVAGSDGSLGAGDTEIDVRGSGTTARFLTAACTVRDGTVVVDGNRRMRQRPIGDLVRALGELGAAVEVLGEEDRPPVRVHGPALTGGAAILDASRSSQFASAVLMVAPCADGDTVLELREPIVSRPYIDQTLEVMRAFGAEAAWDGPTTLTVAAGGYAARDFIIEGDASAAAYPLVAAAVCGGSVRVGPLPEGSLQADLGLIPILERMGAEVRREGDDVILNGHPQTLAAVSENMNDAPDAVVALAVAALFAGGETRLTDIANLRIKESNRMEDLAMELRKLGGIAATGPDFLVVEGGELRAATIDPHDDHRMAMSFAVAGLRIPGVEIEDPECVAKTWPGFFAALESITTPLIIAVDGPGGVGKSTVSQAVAGRFGLGHLETGGMYRAGALAVLEAGIDIGDEAAVAALIDTLTVDVVDGRVIMNGTDVTDVLRTEAVSTASSRVSAVPRVREALVALQRRWVRPDGGGAVVEGRDIGTVVFPDSPAKVYLTARPDVRAIRRVRDLGLSEDDIPRIAADLAARDERDSTRAVSPLRPADDALILDTSDMPIEQVIDTVARFVIDRGRHPTT
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate Subcellular Location: Cytoplasm Sequence Length: 641 Sequence Mass (Da): 66804