ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q8LPF3 | MAQLTNSLNYLFSVSLLLFVSFHCLCFRFSLVAACSNSTDDQQIQHHHHRKWVGPSGHKVITVSLNGHAQFRSVQDAVDSIPKNNNKSITIKIAPGFYREKVVVPATKPYITFKGAGRDVTAIEWHDRASDLGANGQQLRTYQTASVTVYANYFTARNISFTNTAPAPLPGMQGWQAVAFRISGDKAFFSGCGFYGAQDTLCDDAGRHYFKECYIEGSIDFIFGNGRSMYKDCELHSIASRFGSIAAHGRTCPEEKTGFAFVGCRVTGTGPLYVGRAMGQYSRIVYAYTYFDALVAHGGWDDWDHKSNKSKTAFFGVYNCYGPGAAATRGVSWARALDYESAHPFIAKSFVNGRHWIAPRDA | Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 40042
Sequence Length: 362
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
O49298 | MDHKILLTPPKSLYTKCIITIIYVVSISHLNAHFITSCKQTPYPSVCDHHMSNSPLKTLDDQTDGFTFHDLVVSSTMDQAVQLHRLVSSLKQHHSLHKHATSALFDCLELYEDTIDQLNHSRRSYGQYSSPHDRQTSLSAAIANQDTCRNGFRDFKLTSSYSKYFPVQFHRNLTKSISNSLAVTKAAAEAEAVAEKYPSTGFTKFSKQRSSAGGGSHRRLLLFSDEKFPSWFPLSDRKLLEDSKTTAKADLVVAKDGSGHYTSIQQAVNAAAKLPRRNQRLVIYVKAGVYRENVVIKKSIKNVMVIGDGIDSTIVTGNRNVQDGTTTFRSATFAVSGNGFIAQGITFENTAGPEKHQAVALRSSSDFSVFYACSFKGYQDTLYLHSSRQFLRNCNIYGTVDFIFGDATAILQNCNIYARKPMSGQKNTITAQSRKEPDETTGFVIQSSTVATASETYLGRPWRSHSRTVFMKCNLGALVSPAGWLPWSGSFALSTLYYGEYGNTGAGASVSGRVKWPGYHVIKTVTEAEKFTVENFLDGNYWITATGVPVNDGL | Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 61270
Sequence Length: 554
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
|
Q9SRX4 | MESPIFILITLSFFLQSVLASSQTLSNSSTICKTTPDPKYCKSVFPHSQGNVQQYGCFSIRKSLSQSRKFIRTVDRYIKRNAHLSQPAVIRALQDCRFLAGLTMDYLLTSFETVNDTSAKTSFKPLSFPKADDIQTLLSAALTNEQTCLEGLTTAASYSATWTVRTGVALPLVNDTKLLGVSLALFTKGWVPKKKKRAGFAWAQPRSGSSTHTKPFRLFRNGALPLKMTEKTKAVYESLSRRKLADGDSNGDGDDGSMVLISDIVTVSQDGTGNFTNITAAVAAAPNNTDGSAGFFLIYVTAGIYEEYISIAKNKRYMMMIGDGINQTVVTGNRSVVDGWTTFNSATFAVTAPNFVAVNITFRNTAGPEKHQAVALRSGADFSIFYSCSFEAYQDTLYTHSLRQFYRECDVYGTVDFIFGNAAVVFQNCNLYPRKPMPNQFNAITAQGRSDPNQNTGTSIQNCTIKPADDLVSSNYTVKTYLGRPWKEYSRTVYMQSYIDGFVEPVGWREWNGDFALSTLYYAEYNNTGPGSNTTNRVTWPGYHVINSTDAANFTVTGLFIEADWIWKTGVPYTSGLIS | Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 63952
Sequence Length: 579
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
|
O23038 | MKIISLSISIGIAIIAVLASKTLFKTHPEAFGIKAISYSFKKSLCDHHHHHHHHHHHHHRHKPSDTKRKVSICDDFPKNIPPLDTDTTSYLCVDKNGCCNFTTVQSAVDAVGNFSQRRNVIWINSGMYYEKVVIPKTKPNITLQGQGFDITAIAWNDTAYSANGTFYCATVQVFGSQFVAKNISFMNVAPIPKPGDVGAQAVAIRIAGDESAFVGCGFFGAQDTLHDDRGRHYFKDCYIQGSIDFIFGNAKSLYQDCRIISMANQLSPGSKAVNGAVTANGRSSKDENSGFSFVNCTIGGTGHVWLGRAWRPYSRVVFVSTTMTDVIAPEGWNNFNDPSRDATIFYGEYNCSGPGADMSKRAPYVQKLNETQVALLINTSFIDGDQWLQFSDL | Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 43350
Sequence Length: 393
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
P0C1A9 | MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNPEDSRFFEYKSYGAGATVSKDRRQLTDAQAAEYTQSKVLGDWTPTLP | Function: Catalyzes the first step in maceration and soft-rotting of plant tissue.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 39373
Sequence Length: 366
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
Q5B7U0 | MRVQSYLSLFSLVGAALCAPREHFKRTARTSAPAGCLTVGGSGTYSTIGAAFAALGSSSSEACIYISAGTYKEQLTFQYAGPLTLYGETTDTSSYKKNTVTITHTISSPEAGSLVASATVNAAMDNFTMYNINVVNGYGKGAQAVALAASGERQGYYGCQFLGYQDTLYARVGVQYYSNCYIEGAVDYIFGDASAWFGECDIVSNGAGYITAMSRETASDPAWYCFDHCNIYGKSGLDLTGDVYLGRPWRVLARVIYQNSELSDIINAAGWTTMAEGATPLYYEIGNTGDGADTSKRLYLSEISAAVTKATVLGSDWTDWLDWSY | Function: Involved in maceration and soft-rotting of plant tissue. Active against citrus pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 34859
Sequence Length: 325
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
A1DBT4 | MHLPSLVLGLLGLGLTASASPIEERSNRSKAPDGCLTVGSSGKYSTIGAALDALGDSKSDACIFIGAGTYKEQITIDYKGKLTMYGETTDTSSYKKNQVTITHTISSPQAGTLDKSATVNVRSDGFKMYNINVINGYGKGSQAVALVANADKLGFYGCSFVGYQDTLYAKAGRQYYSNCYIEGATDYIFGNASAWFGECDIMSVGPGYITAMSRTTADQTTWYAIDNCNIYGKPGVDLTAKVYLGRPWRVLARVIYQNSQLSNIINPKGWTTMAEGATPLYYEYNNKGAGADTSKREYESSISGAVSMNTVLGSGWNSWIDTTY | Function: Involved in maceration and soft-rotting of plant tissue.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 34873
Sequence Length: 324
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
Q47474 | MSLTHYSGLAAAVSMSLILTACGGQTPNSARFQPVFPGTVSRPVLSAQEAGRFTPQHYFAHGGEYAKPVADGWTPTPIDTSRVTAAYVVGPRAGVAGATHTSIQQAVNAALRQHPGQTRVYIKLLPGTYTGTVYVPEGAPPLTLFGAGDRPEQVVVSLALDSMMSPADYRARVNPHGQYQPADPAWYMYNACATKAGATINTTCSAVMWSQSNDFQLKNLTVVNALLDTVDSGTHQAVALRTDGDRVQLENVRLLSRQDTFFVNTSDRQNSYVTDHYSRAYIKDSYIEGDVDYVFGRATAVFDRVRFHTVSSRGSKEAYVFAPDSIPSVKYGFLVINSQLTGDNGYRGAQKAKLGRAWDQGAKQTGYLPGKTANGQLVIRDSTIDSSYDLANPWGAAATTDRPFKGNISPQRDLDDIHFNRLWEYNTQVLLHE | Function: Probably involved in the degradation of methylated oligogalacturonides present in the periplasm. More active on methylated oligogalacturides than on pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Location Topology: Lipid-anchor
Sequence Mass (Da): 47190
Sequence Length: 433
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Cell outer membrane
EC: 3.1.1.11
|
Q7SDD5 | MIQPLVKASRPRLWVCSDCLLRRTLSPLLRQQRRRFTGFTAHAPKTLTGTIPVTHKNGDTKHDDSLLRSIFDSPETWKQFSGDKHGRNVGLFRNAYLTSPHGFLDFAHVSLGKARALVDKVLNAQSLDEYRAIVRHLDRLSDILCRVLDMADFVRVTHPDQQIQRTASMAWDMMYEYMNQLNTMTGLYDQLVQAMDNPQVSTTWSEEERMVAEVLKLDFAKSAVHLPKDARDKFVHLSSAISQTGTNFIQHMEPKIPYTTVEKSRMMGMDPVEVKRMASMGKVYVQTLSPQASIALRTVRDDHARHQLFMASRTASRRTVHTLEELMLLRGESAKLSGFESYGHLVLHDRMMASTPESVRQFLQALSENTRPQAQQEVADLTAAKRAHKGGDATLEPWDKDFYAESIRQAIKSRQKREDLSSYFSLGTVMQGLSRIFTRLYGIRFVPREPMPGETWHPDVRRLDVVSDVEGHVAVLYCDLFYRPLKSPNPAHFTLRCSRELSPHEIAETAHTQAENPHVLIPSFESAEFAANDGMAYSRSQDGAIKQLPTIALVCDFPQQSHNRPALLSFFQLETLFHEMGHAIHSILARTSFQNVSGTRCATDLAELPSTLMEYFAADPSVLALFARHYETDNPLPYEWVDNKIREARRFEALDTENQIILAMLDQELHSSKAVQGHIDSTEIFHSLQRQFSTAPPDPQGTAWQGFFGHLVGYGSTYYSYLFDRVLAQRVWNVVFNSGQGGAALQRENGERLKENLLKWGGSKDPWKCLAGALKDERLEGGGEKAMKLVGSWGGQRGTKSDQAV | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
Catalytic Activity: Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.
Sequence Mass (Da): 91095
Sequence Length: 805
Subcellular Location: Mitochondrion matrix
EC: 3.4.24.59
|
Q0TXL7 | MLKRLARNNSSPWICSRCLQQSQRQRRFNSTFAATATARDHAPSALYGLSASGKTDDDALRKVFDNASFWESFKRGTSNKKPSGIIGNKYLTHPDGFIDFVTVTIQRCNGVVEKVSRAETIEDFKYMVKDLDKLSDLLCRVIDLADFVRSTHPNRQFQIMAVKAYHTVFQYMNQLNTTPVLYDQLKKASDIPEVFESWTEEERIVARILMEDFARFGIGLDDATRQKLVDLSGEIAEVGSQFVEGMSPETPTLKFESKRLKGLDPNLAKALTKWGETRISTMHHEAQAVLRFVDDAEVRRETYSAVRTAGSSTIARLEKMLKLRAELAQLSGYETFSHMTLENKMAKTPEAVNTFLKALYEDSRPSVLADLHELMELKRGDAHQDNFPNRMNAWDKFYYTQKMLSTMEGAYKQRTADSLSAYFSVGTVLQGISRLFDRLYGVRLVPQETQPGEVWEDGVRRLDVISDTEGHIAVLYCDLFSRPGKTPNPAHFTLRCSREILPAELEEMQHMPHRFSSPIEAATDGMSVSYNASRNSYFQLPTIALICDFSKPSSPRPTLLNIHDVRTLFHEMGHALHSILGRTALQNVSGTRCATDIAELPSVLMEHFAFDPSVLALYARHWDTNAPLPLALLENRLAIDNRNGYSELESQILLAMLDQAYHSNLPLDPAFNSTSVYHNTYTRFASVPEPAGTRWQGFFGHLFGYGATYYSYLFDRAIASRIWKGVFNEGRDGGSLDREKGELYKNEVLRWGGGRDGWVCLAGVLRDGKVGEGGEGAMREVGKWGIDAGK | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
Catalytic Activity: Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.
Sequence Mass (Da): 89067
Sequence Length: 790
Subcellular Location: Mitochondrion matrix
EC: 3.4.24.59
|
P37932 | MIARPARDVLSSATKKQFRFRGCLAARHEPYHTSTSRAGQVAILPATTDDKTLVSVFDSPRSNAKLSAFATTGLFNHSTVTHPRALNSIAQGTLIRAHVLTNRILRAKESREELFKVVKNLDRLSDMLCSVIDLCELVRNSHPDRAWVEAANDAYEGLCQTMNELNTHVGLYDVLKIVLSDPEIVKSLSPEAYRTAMIFWNDFEKSAINLPAKEREEFVALSSEIISLGRMFLEETTAARPPAKIPPSDLAGLKDKGMGVRLQLQAQFTQRDLHVYPGSLQAQMIMRSAPAEEARRRVYIASHSSTPEQIELLERMLSTRARLARLVGRESFAAMALDDKMAKNPTNVARFLDSLMDRSRPYARRALRNLSMRKQEHLHTPPFPTIQAWDRDYYCPPEPPAPPIPLPRLTFGTVLMGLSRLFRHLYGIHLRPVKPIAGEVWHSDVHKLEVVDEERGVIGLIYADVFARRGKASGAAHYTVRCSRRTDDDDVQGDNDELTRMYPDLIKQSEEFEAVGRGPIPGLPGTYQQPLVVLLCEFARPSLGAAVLEWHEVMTLFHEMGHAMHSMIGRTEYQNVSGTRCPTDFVELPSILMEHFLNSRQVLSLFHADSTSSSSQPIGNHDEDPCHSIDTYAQIMLAALDQIYHSPAALQPGFDSTRKLARLHDEKGLIPYVPGTSFQTQFGHLFGYGATYYSYLFDRAIASRVWKDVFSSSPLSRETGERYKQEVLRYGGGKDPWEMVSALLKAPELASGDAEAMATVGRWKIEDEVGLPGRH | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
Catalytic Activity: Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.
Sequence Mass (Da): 86915
Sequence Length: 775
Subcellular Location: Mitochondrion matrix
EC: 3.4.24.59
|
Q10415 | MQVRTLLTLGKKKVIGNRQCILSLYRKYSNVQSRKAEDQLLRQIFDDQNIAVNQITKRNGIQGVGLFRNHFLSDKDTGFLRLAETASEKCKAVIEDLLLEDTEDGSIVVSKFDRISNLLCSVIDLFEFVRCAHPDKMVVMKAEEAYSYLFELMNTLNTHQGLYEKLKCSLQQTPTLKDTDPEAYTVGRVFLQDFEKSGVNLESSKRNSFVKKSSESATLGRAFFNNSMNRPQRYLTISKQRLAGSDPYFVRSLSKNDKNFIMIPTVGYEGTQALISVANPDVRKEIYMEGHKGTVEEVELLNSYLRSKAEVAKLVGKSSFADLQLIDKMANAPKHVVEFLENLSLKNSSVLKKILNNLALMKKKELNLNFLPSFDVWDREYYTARYKQSLINQKPSLNPSITNYRRFFSVGTVIQGLSRLFSSLYGLRFVPADISPGEVWHPDVNKVNVYNENDHVMGVIYFDLFARTGKTDGAAHFTIRSSRELDLTSFDDSISLGFDDATNIRVKDNKRYQIPVISLLCNFVRSSGMDPTFLDLWDVKTLFHEMGHAMHSILGHTKYQNLAGTRCATDFVELPSIIMEFFMSNPAVLPLYARYEGTEIPLPVQVLNHHNMVENSSAPLDLQSQICMAMVDQLFHSKVVLDPSFNSIDEVTNVTRKFSGFESAPPAAWYLQFSHLYGYSATYYSYIFDTVLASLIFSKLFAGNPLSREAGEKFRKAILRWGGSRSPWECVAEALEQPILATGGEEAMRRIGSEGIKATSTF | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
Catalytic Activity: Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.
Sequence Mass (Da): 86286
Sequence Length: 762
Subcellular Location: Mitochondrion matrix
EC: 3.4.24.59
|
Q9I3Y3 | MNSPALPLSRGLRIRAELKELLTLAAPIMIAQLATTAMGFVDAVMAGRASPHDLAAVALGNSIWIPMFLLMTGTLLATTAKVAQRHGAGDQPGTGPLVRQALWLALLIGPLSGAVLWWLSEPILGLMKVRPELIGPSLLYLKGIALGFPAAALYHVLRCYTNGLGRTRPSMVLGIGGLLLNIPINYALIYGHFGMPKMGGPGCGWATGSVMWFMFLGMLFWVNKASIYRASQLFSRWEWPDRATIGPLVAVGLPIGIAVFAESSIFSVIALLIGGLDENVVAGHQIALNFSALVFMIPYSLGMAVTVRVGHNLGAGLPRDARFAAGVGMAAALGYACVSASLMLLLREQIAAMYSPDPAVIAIAASLIVFSALFQFSDALQVTAAGALRGYQDTRVTMIMTLFAYWGIGLPVGYSLGLTDWFQEPTGPRGLWQGLVVGLTGAAIMLCIRLARSARRFIRQHERLQREDAEAASVLGR | Function: Multidrug efflux pump that functions as an H(+)/drug antiporter. Confers resistance to benzalkonium chloride, fluoroquinolones, ethidium bromide, acriflavine and tetraphenylphosphonium chloride.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50870
Sequence Length: 477
Subcellular Location: Cell inner membrane
|
P58120 | MNRTKTVNWKRNLFITWIGCFFVGSSFSLVMPFLPLYIQGLGVSGGNVELYSGLAFSLPALASGLVAPIWGRLADEHGRKVMMVRASIVMTLTMGGIAFAPNVWWLLGLRLLMGFFSGYIPNSTAMIASQAPKDKSGYALGTLATAMVSGTLIGPSLGGLLAEWFGMANVFLIVGALLALATLLTIFFVHENFEPIAKGEMLSSKEIINKVSNKQILFGLLVTTFIIQITSQSIEPFVTLYIKTLTTSTNNLMFISGLIVSAVGLSAMLSSSFLGRLGDKYGSHRLILIGLVFTFIIYLPMAFVQSPLQLGILRFLLGFGTGALTPSVNSLLSKITPKEGVSRIFAYAQMCSNLGMVTGPLVGSAIAGYISYRAAIVGTSLFVIVNIIWSFINFRKYLRKRSIME | Function: Efflux pump for various substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43859
Sequence Length: 405
Subcellular Location: Cell membrane
|
P0A4K4 | MTEINWKDNLRIAWFGNFLTGASISLVVPFMPIFVENLGVGSQQVAFYAGLAISVSAISAALFSPIWGILADKYGRKPMMIRAGLAMTITMGGLAFVPNIYWLIFLRLLNGVFAGFVPNATALIASQVPKEKSGSALGTLSTGVVAGTLTGPFIGGFIAELFGIRTVFLLVGSFLFLAAILTICFIKEDFQPVAKEKAIPTKELFTSVKYPYLLLNLFLTSFVIQFSAQSIGPILALYVRDLGQTENLLFVSGLIVSSMGFSSMMSAGVMGKLGDKVGNHRLLVVAQFYSVIIYLLCANASSPLQLGLYRFLFGLGTGALIPGVNALLSKMTPKAGISRVFAFNQVFFYLGGVVGPMAGSAVAGQFGYHAVFYATSLCVAFSCLFNLIQFRTLLKVKEI | Function: Efflux pump for various substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42840
Sequence Length: 399
Subcellular Location: Cell membrane
|
Q9HV31 | MSRAAVPSVRRRLLVNLLVGFVLCWLSVAALTYHLSLKQVNRLFDDDMVDFGEAALRLLDLATEDQAGEDGSITEIIERSREAIQGLPLLRRESALGYALWRDGQPLLSSLNLPPEITAQGPGFSTVEAQGTHWRVLQLNIDGFQIWISENLIYRQHTMNLLLFYSLFPLLLALPLLGGLVWFGVARGLAPLREVQAEVQQRSARHLQPIAVEAVPLEIRGLIDELNLLLERLRTALEAERRLTSDAAHEIRTPLASLRTHAQVALRSEDPKAHARGLLQVSRSVERISTLMEQILLLARLDGDALLEQFHPVNLATLAEDVLSELARQAIDKDIELSLHQETVYVMGIDLWLKAMVGNLVGNALRYTPAGGQVEIRVENRAQHAVLRVRDNGPGVALEEQQAIFTRFYRSPATSSGEGSGLGLPIVKRIVELHFGSIGLGKGLEGKGLEVQVFLPKTQPDATRPPARGPDSGRSHI | Function: Member of the two-component regulatory system PmrA/PmrB that plays a role in the regulation of resistance towards polymyxin B and cationic antimicrobial peptides in response to limiting concentrations of Mg(2+). Autoregulates also its own pmrAB operon under Mg(2+)-limiting conditions . May function as a membrane-associated protein kinase that phosphorylates PmrA in response to environmental signals leading to activation of specific gene promoters (Probable).
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52706
Sequence Length: 477
Subcellular Location: Membrane
EC: 2.7.13.3
|
G3MTW7 | MKNRVYESLTTVFSVLVVSSFLYIWFATY | Function: May bind to BasS and modulate its sensor kinase activity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3465
Sequence Length: 29
Subcellular Location: Cell inner membrane
|
Q6XQN6 | MAAEQDPEARAAARPLLTDLYQATMALGYWRAGRARDAAEFELFFRRCPFGGAFALAAGLRDCVRFLRAFRLRDADVQFLASVLPPDTDPAFFEHLRALDCSEVTVRALPEGSLAFPGVPLLQVSGPLLVVQLLETPLLCLVSYASLVATNAARLRLIAGPEKRLLEMGLRRAQGPDGGLTASTYSYLGGFDSSSNVLAGQLRGVPVAGTLAHSFVTSFSGSEVPPDPMLAPAAGEGPGVDLAAKAQVWLEQVCAHLGLGVQEPHPGERAAFVAYALAFPRAFQGLLDTYSVWRSGLPNFLAVALALGELGYRAVGVRLDSGDLLQQAQEIRKVFRAAAAQFQVPWLESVLIVVSNNIDEEALARLAQEGSEVNVIGIGTSVVTCPQQPSLGGVYKLVAVGGQPRMKLTEDPEKQTLPGSKAAFRLLGSDGSPLMDMLQLAEEPVPQAGQELRVWPPGAQEPCTVRPAQVEPLLRLCLQQGQLCEPLPSLAESRALAQLSLSRLSPEHRRLRSPAQYQVVLSERLQALVNSLCAGQSP | Cofactor: Activity is highest with Mn(2+).
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate . Helps prevent cellular oxidative stress via its role in NAD biosynthesis .
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 57578
Sequence Length: 538
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.4.21
|
Q8TMW6 | MIKSILDNDLYKFTMQMAVLELFPKAEAEYRFTNRGSHHFSEEFVEKLRRVIDEDISALMLTEDEYQWLGENCSFLKPMYLEYLKNFRFKPGEVEVCLTEEKELDIRIKGPWHSTILWEIVLMAAVSELYFTTIEKEWNGKEWDGNISATSESILTAYGEKILEIGKILEENGCLFAEFGTRRRRSFELHDQVMKTLLQIETLTGTSNVFFAKKYGLKPIGTVGHEWIMGTSALIGLRYANRFAFENWVEVYKGDLGIALTDTFGSEAFFKDMDLKLSKIYDGFRHDSGDPFTFVDRVIDHYRKMGIDPMKKVIVFSDALNAEAAIRLKKYCQDKINCSFGIGTSLTNNSEFFRESPPLNMVIKLHSVNGIPVVKLSDSPEKETGERDALRVANYIVGRKGLDE | Function: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 46457
Sequence Length: 404
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
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Q8CC86 | MEMELDSEGRMVVRPLLTDLYQATMALGYWRAGRACEAAEFELFFRHCPFGGSFALSAGLQDCMRFLRAFRLRDADVQFLASVLPPDTDPAFFEHLRALDCSGVTVRALPEGSLAFPGVPLLQVSGPLLLVQLLETPLLCLVSYASLVATNAARLRLIAGPDKKLLEMGLRRAQGPDGGFTASIYSYLGGFDSSSNTLAGQLRGVPVAGTLAHSFVTSFSGSEVPPDPMLAPASSEGPTVDLPARVNLWLKRVCLYLGLEEQEPHPGERAAFVAYALAFPRAFQGLLDSYSVRRSGLPNFLAVALALGELGYRAVGVRLDSGDLLQQAKEIRGIFRTAGAQFQMPWLESVPIAVSNNIDESELMRLAQKGSEVNVIGIGTSVVTCPKQPSMGCVYKLVSVGGQPRIKLTEDPEKQTLPGSKAAFRFLGPDGSLLLDLLQLAEEPPPKAGQELRVWPRGTQEPCTVKPAQVEPLLRLYLQQGQLCEPLPSLDESRRFAQQSLSLLRPAHKQLQSPAVYPVALSEKLRALVDSLSARGPL | Cofactor: Activity is highest with Mn(2+).
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 58265
Sequence Length: 538
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.4.21
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Q9JTM8 | MTGIIHSLLDTDLYKFTMLQVVLHQFPQTHSLYEFRCRNASTVYPLADIKEDLEVELDALCQLRFTHDELDYLRSLRFIKSDFVDYLELFQLQRRFVEVGTDDKGRLNIRIEGPMIQAMFFEIFILAIVNELYFRRLETPAVIEEGERRLQAKAARLKEIAAAQNPDEPPFLISDFGTRRRYKLAWQEHVIRTLLEAAPSIVRGTSNVFLAKKLGITPIGTMAHEFLQAFQALDVRLRNFQKAALESWVHEYRGDLGVALTDVVGMDAFLRDFDLYFAKLFDGLRHDSGDPYIWGDKAYAHYQKLKIDSRTKMLTFSDGLDIERSWALHQYFKDRFKTGFGIGTNLTNDMGHTPLNIVLKLVECNGQSVAKLSDSPGKTMTNNSTFLAYLRQVFDVPEPETP | Function: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 46340
Sequence Length: 402
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
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Q6D454 | MTLHTSPILHSLLDTDAYKLHMQQAVYHHYYDVDVAAEFRCRGDELLGVYADEIAHQVDLMRFLSLSDDEFTYLSSLPFFQQDYLNWLRNFRFNPQQVSIKNNAGKLDIRITGPWREVILWEVPLLAVISEVVHRHRSPNVTTEQAVAQLSTSLESFRQNSMNVDLSQFKLMDFGTRRRFSGDIQQTIVTALQADFPYLIGTSNYDLARRLGITPVGTQAHEWFQAHQQISPTLANSQRAALQMWLREYPTHLGIALTDCITMDAFLRDFDLPFAEAYQGLRHDSGDPVDWGEKAIAHYQRLNIDPMSKTLVFSDNLNLDKALVLYRHFCQRVNLVFGMGTRLTCDIPGVKPLNIVIKLVECNGKPVAKLSDSPGKTICQDQNFVCELRKAFDLPRVKKAS | Function: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 45867
Sequence Length: 401
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
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Q00472 | MAKKLSSPKEYKEFIDKFDVFLFDCDGVLWSGSKPIPGVTDTMKLLRSLGKQIIFVSNNSTKSRETYMNKINEHGIAAKLEEIYPSAYSSATYVKKVLKLPADKKVFVLGEAGIEDELDRVGVAHIGGTDPSLRRALASEDVEKIGPDPSVGAVLCGMDMHVTYLKYCMAFQYLQDPNCAFLLTNQDSTFPTNGKFLPGSGAISYPLIFSTGRQPKILGKPYDEMMEAIIANVNFDRKKACFVGDRLNTDIQFAKNSNLGGSLLVLTGVSKEEEILEKDAPVVPDYYVESLAKLAETA | PTM: The N-terminus is blocked.
Catalytic Activity: 4-nitrophenyl phosphate + H2O = 4-nitrophenol + H(+) + phosphate
Sequence Mass (Da): 32794
Sequence Length: 298
EC: 3.1.3.41
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P19881 | MTAQQGVPIKITNKEIAQEFLDKYDTFLFDCDGVLWLGSQALPYTLEILNLLKQLGKQLIFVTNNSTKSRLAYTKKFASFGIDVKEEQIFTSGYASAVYIRDFLKLQPGKDKVWVFGESGIGEELKLMGYESLGGADSRLDTPFDAAKSPFLVNGLDKDVSCVIAGLDTKVNYHRLAVTLQYLQKDSVHFVGTNVDSTFPQKGYTFPGAGSMIESLAFSSNRRPSYCGKPNQNMLNSIISAFNLDRSKCCMVGDRLNTDMKFGVEGGLGGTLLVLSGIETEERALKISHDYPRPKFYIDKLGDIYTLTNNEL | Function: PHO13 is dispensable for vegetative growth and sporulation.
Catalytic Activity: 4-nitrophenyl phosphate + H2O = 4-nitrophenol + H(+) + phosphate
Sequence Mass (Da): 34625
Sequence Length: 312
EC: 3.1.3.41
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Q8TCS8 | MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISSGKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLSDIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFTDYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCDGRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKDKNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESNGSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYNGDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEARDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHPTALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSSNSQ | Function: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules . Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 85951
Sequence Length: 783
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q8K1R3 | MAACRLCCLCPCLRPLGCGPLGRPGRNRALSYLQMRALWSSTGSRAVTVDLGHRKLEISSGKLARFADGCAVIQSGDTAVMVTAVSKTKASPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGSSDREVLTSRVIDRSIRPLFPAGYFYDTQVLCNLLAVDGINEPDILAVNGASVALSLSDIPWNGPVGAVRIGMIDGECVVNPTRREMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKEIGVAKRTPQKIFTPSAEIVKYTKIIAMEKLYAVFTDYEHDKVSRDEAVNKIRLDTEEHLKEKFPEVDQFEIIESFNIVAKEVFRSIILNEYKRCDGRDLTSLRNISCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESSIKSDQIITAINGVKDKNFMLHYEFPPYATNETGKVTGVNRRELGHGALAEKALCPVIPKDFPFTIRVTSEVLESNGSSSMASACGGSLALMDAGVPISSAVAGVAVGLVTKTNPEKGEIEDYRLLTDILGIEDYNGDMDFKIAGTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVKVPLSKRAKFVGPGGYHLKKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNSQLDQRKIKHPTALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTALKTLNDRSSIVMGEPVSQSSNSNP | Function: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules (By similarity). Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 85683
Sequence Length: 783
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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A3DCH7 | MYKTFSMELAGRTLTIETGKLAQLANGSVLVRYGDTVVLSTATASATPREGVDFFPLSVDYEERLYAVGKIPGGFIKREGKPSEKAILTARVIDRPLRPLFPKDLRNDVAIVNTVLSVDQDNSPELAALLGSSIAVSISDIPFNGPVGAVILGLIDGEVIINPTEKQKEISQMYVTLAGTRNKIVMIEAGANEVPDEVMLDAIKKGHEEIKKIVDFIDGIVKEVGKPKFEYESAEVPEEIFNAVREYAYDKMREAVLAVDKQVRDKNIDDLTKEITEHFAEVFPEMEPAIKEAIYKLEKKVVREYILEEGRRVDGRRLDEIRPLSAEVGLLPRVHGSGLFTRGQTQVLSSVTLGAMGDVQILDGIDTEETKRYMHHYNFPGFSVGEAKSSRGPGRREIGHGALAERALEPVIPSEEEFPYTIRVVSEVLMSNGSTSQGSVCGSTLALMDAGVPIKKPVAGISAGLVVDENNPDRFVTFMDIQGIEDFFGDMDFKVAGTKDGITAIQVDIKIDGLTEEIIKQAFELTRKGRLYIIDNVLLKAIPEPRKQMSKYAPKIISTTINPDKIREVIGPGGKMINKIIDETGVKIDINDDGRVYIFSSDIQAGKRARSMIEAIAKDIEPGQVFLGRVIRVTSFGAFVEFLPGKEGLVHISKLDKKRVERVEDIVRVGDQILVKVIEIDKQGRVNLSRKDAMEDEWDK | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 77318
Sequence Length: 700
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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A5EXU0 | MKHSVSFTYGQHQVTLETGEIARQADGAVIVNMDDTIVLVTVVANKTVAEGQDFFPLTVDYQEKNYAAGKIPGGFFKREGRPSEEETLISRLIDRPIRPLFADGFLNEVQIIATVLSYNPEVSPDIPSIIGASAALKLSGLPFNGPIAAARVGYVNDAYVLNPSPKALKNSRLDLVVAGTESAVLMVESEADQLSEAVMLEAVMFGHRQQQVVIKSINELAAQAAKPAWAWQSPARDEQLDTEVKNHFEERLVAAYQIAHKQTRQETVAQIHADAVALLGIQNNAHGWEETLVNEYVHHLAYRIVRDRILKKQPRIDGRDTKTVRPITIHTSVLPRAHGSALFTRGETQALVVATLGTGRDAQLLDTLDGEVRDNFMLHYNFLPFSVGEIGRIGSPKRREIGHGRLARRGLSAVLPLEEDFPYTIRVVSEITESNGSSSMASVCGSSLALMDAGVPVQTPVAGIAMGLIKEGDEFAILTDILGDEDHLGDMDFKVAGSATGVTALQMDIKINGITEEIMRQALSQAHEGRLHILEVMNQAIAAPRAELSDYAPRFSSMRIDTEKIKDVIGKGGATIRSITEQTGTTIEIEDDGSVKIAATDKAAAANARRLIEEIVAEPEIGRIYDAKVTKITDFGAFLQFLPGKEGLVHISQIADYRVNDVRDELTEGQEVKVKLLEIDRQGRVRLSIKEAK | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 75726
Sequence Length: 693
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B8E2S5 | MRQTYSFKKDFAGKTLKIDIGKVAWQATGAALVQYGETTVLVTVVASEEKKEDVDFFPLTVEYVERLYAAGKIPGGFFKREGKPTEPEILFARLIDRPLRPLFSKDFRNEVQVIVTVLSYDHENSTDIPSIIGASCAIMLAGLPFKGPIGAVRVGWDGKEWYINPSVALSNSLLLDLVVAGTKDAVLMIEGDGKEVPEEIFLEGIIRAHEQIGEVINFQEEILSMVNPVPFNYEPFVVNENLKKDVLEYVTVDQIRDAIFTPSKSERQKALEDLKKRVIEHFKPIYGEITAQIDEIINQEAKAILTKVILEEKRRVDGRRLNELRPVSCEVGVLSRVHGSALFQRGETQVLSVVTLGAGEEQIIESVIESEPKRYIHHYNFPPFSVGEAKPLRGPKRREIGHGALAERALLPLIPKEEEFPYTIRVVSEVLSSNGSTSMASVCGSSLSLMDAGVPIKTHVAGVAMGLIKEGEKFEVLTDIQGLEDALGGMDFKIAGTKNGITAVQLDIKVDGLSYEIIEKTLKQAKEARYQILDIMEKTISQPRPEISPYAPRIMVLEINPNKIGDLIGPSGKNIKKIIEETHTTINIKPEGLVYISAPDQESAEKAAQMVQEYTRDIKEGDIFLGKVIRVTDYGAFVEILPGKIGLLHISKYKTTGTGKNQTREEINLGDEILIKVDSIDPSGRISLSRKDL | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76821
Sequence Length: 693
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B4RC48 | MFDIKRKTIEWGGKTLTLETGRMARQADGAVLATYGETMVLATAVFAKSPKPGQDFFPLTVNYQEKFYAAGKIPGSFPRREGAPSQKETLTSRLIDRPIRPLFVKGFKNEVQVICTVLAHDLENDPDIVAMVAASAALVLSGVPFMGPIAAARVGYVNGEYVLNPTLDEMKESAMDLVVAGTAEAVMMVESEIKELTEEQVLGGVTFAHKGMQPVIDAIIELAEHSAKEPFDFQPDDTDEIAAKVKDLIGGDLRAAYQITGKSERHAAIGAAKEKAMTAFAKSEANPEGYDANKLGGVFKEIEADIVRRSILETGKRIDGRTVDQVRPILGEVGVLPRAHGSALFTRGETQALCVTTLGTGDDEQLIDALEGKYFEKFMLHYNFPPFSVGETGRMGSPGRREVGHGKLAWRALRPMLPSYEEFPYTIRIVSEIFESNGSSSMATVCGSSLALMDAGVPLKKPVSGIAMGLILEKDGFAVLSDILGDEDHLGDMDFKVAGTADGITSLQMDIKIAGITEEIMKKALEQAKGGRDHILAEMNKAMTAPRAELGEFAPKIETIKIPVDKIREVIGSGGKVIREIVEKTGAKIDIGEDGTIKIAAAEQTKIDAAKEWIKSIASEPEVGQIYTGKVVKIVDFGAFVNFFGAKDGLVHVSQISNERVAKVSDVLTEGQQVKVKLLGFDDRGKTRLSMKVVDQETGEDLSKSNEKAEEPADA | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 77215
Sequence Length: 715
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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P41121 | MLNPIVRKFQYGQHTVTIETGMMARQATAAVMVNMDDTAVFVTVVGQKKVKAGQDFFPLTVNYQERTYAAGRIPGSFFRREGRPGEGETLVARLIDRPLRPLFPEGFLNEVRIVATVVSVNPQINPDIVAMIGASAALALSGIPFNGPIGAARVGYINDQYVLNPTSDELKNSRLDLVVSGTAGAVLMVESEADLLTEEQMLGAVVFGHDQQQVVIDNINALAAEAGKEKWDWVPEPVNQALHDRVAELAESRLGDAYRITEKQERYAQVDAIKDEVTAALLEQDETLEEAEIHEILGSLEKNVVRSRVLSGEPRIDGREKDMVRALDVRTGVLPRTHGSALFTRGETQALVTATLGTERDAQIIDELMGERTDRFLLHYNFPPYSVGETGMMGSPKRREIGHGRLAKRGVLAVMPKANEFPYTVRVVSEITESNGSSSMASVCGASLALMDAGVPIKAAVAGIAMGLVKEGDNFVVLSDILGDEDHLGDMDFKVAGSCEGISALQMDIKIEGITREIMQVALNQAKGARLHILSVMEQAITTPRDDISQFAPRIHTIKINPDKIKDVIGKGGSVIRALTEETGTTIEIEDDGTVKIAATDGEKAKHAISRIEEITAEIEVGRIYAGKVTRIVDFGAFVAIGGGKEGLVHISQIADKRVEKVADYLQVGQETSVKVLEIDRQGRVRLSIKEATAGTAVEEAPPAPQSAE | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76745
Sequence Length: 709
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B3QZG1 | MDLNTKNNNKKVFEIIFENNVLRIEIGEISRQANGSVMLFYKDTVILSVAVCGDKKNSLNFLPLTVNYQEKLYAAGKIPGGFLRREGKPSDQEILCSRLIDRTIRPLFSKNFKNEVQLINMVLSSDPDGNNENIALLGSSLALLISDIPFFEPVSSVCVGKIGDNLIINPTLSQRENSSFFLILAGTKDSLNMVEMSSKEISENNFLESIKFGHEIIKKLCLFQTEIANQIGKTKIKIPLHNVNNLLEVEIKDKYFSEIEMILKNKCNVNNVKKSDILKKLKENVLENYKEKFLNNKKDNFNLLDLENQKLYLNEVEIIFDFLVRTIIRETILKENIRPDGRNSSEIRSITSRIDILPRTHGSALFTRGGTQSLAIVTLGTLRESKIIDDLSDEVDKRFMLHYNFPAFAVGSVGRYLAPSRREIGHGMLAEKALECVLPSENDFPYSIRVVSEILDSNGSSSQATICASSMALMSAGVPLKSLVAGVAMGLIVDDIDKINHYTILSDIEGLEDYQGDIDFKIAGTKVGITALQLDIKIKGITLEIFEKVLEQAKKDRIKILNEMEKVINKSRNEVSKYAPKVKMILIKPEKIRDIIGSGGKIINQIIEKHDNVKIDIMQDGKIYIMHQNMEIVDLTVTYIQNFLKKIKVENVYEVKILRFVKDKMDKTFGAIAEIFPGIEGFIHISKLENYKVDKVEDVLKIGQIILVKCIKINERGQIDLSKKDVFK | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 82279
Sequence Length: 728
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B2RIW6 | MLNVVSKTIDLGDGRSIKIETGKLAKQADGAVTVTMGNTVLLATVCAAKDANPGCDFMPLQVEYKEKYSAIGRFPGGFTRREGKASDYEILTCRLVDRALRPLFPDNYHAEVFVNVILFSADGEDMPDALAGLAASAALAVSDIPFNGPISEVRVARVDGRYIVNPTFEQLERADIDLMVGATMDNIMMVEGEMDEVQESEMLEGIRVAHEAIKVQCKAQLELSEAVGKLQKREYSHEVNDEDLRKKVHDECYARAYEVATSGTGKHERGEAFEKIVEEFKAQYTEEELAEKAEMIARYYHDVEKEAMRRAILDEGKRLDGRKATEIRPIWIETDCLPGPHGSAIFTRGETQSLTTVTLGTKSDEKLVDDVLNYTKERFLLHYNFPPFSTGEARPQRGVGRREIGHGNLAHRALKRMIPTDYPYVVRVISDILESNGSSSMATVCAGTLALRDAGVQIRKPVSGIAMGLISENQGKNYAILSDILGDEDHLGDMDFKVTGTKDGITATQMDIKVDGLSYEILENALEQAKQGRLHILGKIMEAQPETRDDLKPHAPRIEKMHIGKEFIGAVIGPGGKIIQGIQEKSGATVNIEEVDGMGVIEISGTNKPCIDAAIGMIKGIVAMPEVGETYPGKITSVMPYGCFVEFLPGKEGLLHISEVDWKRFETIEDTNLKEGESINVKLLDIDPKTGKFKLSRKVLLEKPEGYVEPQPRERRERREGGREGGRNFERRGGDRDHREPRG | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 82228
Sequence Length: 743
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B4S5G5 | MSMFIRKEIDLGSGKTLSIETGKMAKQADGSAIVRLNDTMVLATVVSSKTPPSPNQSFFPLQVEYREKYSAAGKFPGGFFKREGRPSEKEILSARLIDRALRPLFPDGYYQDTQIIISVISSDQINDADVLGGVAASAAIMVSDIPFQNSMSEVRVGRVNGEYIVNPNINELRDSDIDISIGGTENTICMLEGEMDEISEAEMLEAIRFGHEAIKKICALQNEIAAEVGKTARTFSAAKAPDNLRQSIAEICSNELKELAYMPLCKEERAEKTAEIYKNAKAQTLQRYQQEITPEVIAAEPEKALYLNEQIIGDAIHSIEKQVMREMILDDAKRLDGRRLDEVRPISIELGLIPRAHGSALFTRGETQALVTLTLGTKKDAQMIDTLTDDADKRFMLHYNFPPFSVGETGRVGGTSRREIGHGNLAERAIRKVAPAESAFPYTIRIVSDILESNGSSSMASVCGGALAAMDGGVPLRKPVSGIAMGLIKEGDRYAVLSDILGNEDHLGDMDFKVAGTADGITACQMDIKIDGLDYHILEQALEQALHGRLHILDKMNEAIQEPRTEIGKYAPKLTTIQIPVDAIGMVIGKGGETIRSITEETGAEINIEDDGTVTIASASGEGASAALETIKLLISKPEVGTVYSGKVRDIREDLGAFVEFLPKTDGLVHISEISNERVAKVSDHLKPGDKVKVKLVDVRKDPRTGKTRFALSIKALAEKSADNGASDKAEANR | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 79779
Sequence Length: 734
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q49X62 | MSQEKKVFKTEWANRSLTIETGQLAKQANGAVLVRYGDTVVLSTAVASKEPRDGDFFPLMVNYEEKMYAAGKIPGGFKKREGRPSDEATLTARLIDRPIRPLFPKGYKYDVQIMNTVLSADPDCSPEMAAMIGSSMALSVSDIPFQGPIAGVKVGYIDGEYVINPTVAQKEVSRLDLEVAGHKDAVNMVEAGASEITESEMLEAIFFGHSEIQRLVNFQQEIVDHIQPKKKAFVPVEKDEVLVEKVKQLTQENGLKDAVLTFDKQQRDINLDALKEKVAAEFIDEEDADNEVLIKEVNSILNDLVKEEVRRLIAEEKIRPDGRKTDEIRPLESEVGVLPRAHGSGLFTRGQTQALSVLTLGSMSEYQILDGLGEEEQKRFMHHYNFPNYSVGETGPVRSPGRREIGHGALGERALSHIIPDLKDFPYTVRIVSEVLESNGSSSQASICGSTLALMDAGVPIKAPVAGIAMGLVTRDDSYTILTDIQGMEDALGDMDFKVAGTAEGITAIQMDIKIDGLTKEIIKEALDQAREGRLAILDHMLQTIDTSRSELSAFAPKVVTMTIKPEKIRDVIGPGGKKINEIIDETGVKLDIEQDGTIFIGAVDKDAIARARSIIEDITREAEVGQVYEGKVKRIEKYGAFVELFPGKDALVHISQIANERIDKVEDVLKVGDIFKIKVTEIDKQGRVNASHKALL | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76672
Sequence Length: 697
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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D2ZZC1 | MQYGMDSFGLRGIPHQVFIKKKEGKIMSLAWWKRELFGGWTHFEAVWLLMFLGIQAVVFVFNPDSWLASVAAVTGILCVVFVGKGKISNYLFGLISVSLYAYVSYTFKLYGEMMLNLLVYVPVQFVGFAMWRKHMALGETAETEEVKAKALTVRQWLLVVAASVVGTSVYIEWLHHLGSALPTLDGVTVVVSIVAQVLMILRYREQWALWIVVNILTISLWAVAWFKNGETSLPLLLMYVMYLCNSVYGYINWTKLVKRHSGQ | Function: Required for nicotinamide riboside transport across the inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29908
Sequence Length: 263
Subcellular Location: Cell inner membrane
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P40797 | MNSPRSNAVNGGSGGAISALPSTLAQLALRDKQQAASASASSATNGSSGSESLVGVGGRPPNQPPSVPVAASGKLDTSGGGASNGDSNKLTHDLQEKEHQQAQKPQKPPLPVRQKPMEIAGYVGFANLPNQVYRKAVKRGFEFTLMVVGASGLGKSTLINSMFLSDIYNAEQYPGPSLRKKKTVAVEATKVMLKENGVNLTLTVVDTPGFGDAVDNSNCWVPILEYVDSKYEEYLTAESRVYRKTISDSRVHCCLYFIAPSGHGLLPLDIACMQSLSDKVNLVPVIAKADTMTPDEVHLFKKQILNEIAQHKIKIYDFPATLEDAAEEAKTTQNLRSRVPFAVVGANTIIEQDGKKVRGRRYPWGLVEVENLTHCDFIALRNMVIRTHLQDLKDVTNNVHYENYRCRKLSELGLVDGKARLSNKNPLTQMEEEKREHEQKMKKMEAEMEQVFDMKVKEKMQKLRDSELELARRHEERKKALELQIRELEEKRREFEREKKEWEDVNHVTLEELKRRSLGANSSTDNVDGKKEKKKKGLF | Function: Involved in cytokinesis and possibly cellularization . Also acts as an enhancer of the sina gene, thus having a role in photoreceptor development . May be involved in p53-dependent apoptosis .
PTM: Ubiquitinated by park, leading to its degradation by the proteasome.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60143
Sequence Length: 539
Subcellular Location: Apical cell membrane
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Q01860 | MAGHLASDFAFSPPPGGGGDGPGGPEPGWVDPRTWLSFQGPPGGPGIGPGVGPGSEVWGIPPCPPPYEFCGGMAYCGPQVGVGLVPQGGLETSQPEGEAGVGVESNSDGASPEPCTVTPGAVKLEKEKLEQNPEESQDIKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSFKNMCKLRPLLQKWVEEADNNENLQEICKAETLVQARKRKRTSIENRVRGNLENLFLQCPKPTLQQISHIAQQLGLEKDVVRVWFCNRRQKGKRSSSDYAQREDFEAAGSPFSGGPVSFPLAPGPHFGTPGYGSPHFTALYSSVPFPEGEAFPPVSVTTLGSPMHSN | Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 or SOX15 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency.
PTM: Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression.
Sequence Mass (Da): 38571
Sequence Length: 360
Domain: The POU-specific domain mediates interaction with PKM.
Subcellular Location: Cytoplasm
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P20263 | MAGHLASDFAFSPPPGGGDGSAGLEPGWVDPRTWLSFQGPPGGPGIGPGSEVLGISPCPPAYEFCGGMAYCGPQVGLGLVPQVGVETLQPEGQAGARVESNSEGTSSEPCADRPNAVKLEKVEPTPEESQDMKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSLKNMCKLRPLLEKWVEEADNNENLQEICKSETLVQARKRKRTSIENRVRWSLETMFLKCPKPSLQQITHIANQLGLEKDVVRVWFCNRRQKGKRSSIEYSQREEYEATGTPFPGGAVSFPLPPGPHFGTPGYGSPHFTTLYSVPFPEGEAFPSVPVTALGSPMHSN | Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') . Forms a trimeric complex with SOX2 or SOX15 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 . Critical for early embryogenesis and for embryonic stem cell pluripotency .
PTM: Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression.
Sequence Mass (Da): 38216
Sequence Length: 352
Domain: The POU-specific domain mediates interaction with PKM.
Subcellular Location: Cytoplasm
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Q9TSV5 | MAGHLASDFAFSPPPGGGGDGPGGPEPGWVDPRTWLSFQGPPGGSGIGPGVGPGAEVWGLPACPPPYDFCGGMAYCAPQVGVGLVPQGGLETPQPEGEAGAGVESNSEGASPEPCAAPAGAAKLDKEKLEPNPEESQDIKALQKDLEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSFKNMCKLRPLLQKWVEEADNNENLQEICKAETLVQARKRKRTSIENRVRGNLESMFLQCPKPTLQQISHIAQQLGLEKDVVRVWFCNRRQKGKRSSSDYSQREDFEAAGSPFPGGPVSFPLAPGPHFGTPGYGGPHFTTLYSSVPFPEGEAFPSVSVTPLGSPMHSN | Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 or SOX15 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency.
PTM: Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression (By similarity).
Sequence Mass (Da): 38342
Sequence Length: 360
Domain: The POU-specific domain mediates interaction with PKM.
Subcellular Location: Cytoplasm
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P56223 | MPGISSPILTNAQGQVIGALPWVVNSASVATPAPAQSLQVQAVTPQLLLNAQGQVIATLASSPLPQPVAVRKPSTPESPAKSEVQPIQPTQAVPPPAVILTSPAPALKPSASAPIPITCSETPTVSQLVSKPHTPSLDEDGINLEEIREFAKNFKIRRLSLGLTQTQVGQALTATEGPAYSQSAICRFEKLDITPKSAQKLKPVLEKWLNEAELRNQEGQQNLMEFVGGEPSKKRKRRTSFTPQAIEALNAYFEKNPLPTGQEITEIAKELNYDREVVRVWFCNRRQTLKNTSKLNVFQIP | Function: Transcription factor that binds preferentially to a variant of the octamer motif (5'-ATGATAAT-3').
Sequence Mass (Da): 32702
Sequence Length: 301
Domain: Contains two direct repeats of 7 amino acids in the N-terminus.
Subcellular Location: Nucleus
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P20177 | IKKEGLWIPKLEPERVVSILEWDRAAEPEHRLEAICASMIEAWGYDDLLNHIRRFYLWVLDQAPYKQLSAEGKAPYISEVALKSLYTGKPATSCELEVYNKIHQEQHDEFDDSQMKFVFQSDKEKLNVGEQQKSKDKESRQRDQEGENSNRQIIPDRDINAGTTGTFSVPKLKKISGKLSLPKIKGKGLLNLDHLLVYVPNQDDISNNIATQEQLEAWHEGVKNAYEVDDQQMEIICNGLMVWCIENGTSGDLQGEWTMMDGEKQVTFPLKPILDFAKPTLRQIMAHFSQAAESYIEFRNSTEKYMPRYGLQRNLTDYGLARYAFDFYRLTSKTPARAREAHMQMKAAAIRGKSNHMFGLDGNVGTDEENTERHTANDVNRNMHHIAGARF | Function: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.
PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 44876
Sequence Length: 391
Subcellular Location: Virion
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P27913 | MNNQRKKTGRPSFNMLKRARNRVSTGSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWSSFKKNGAIKVLRGFKKEISSMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPTLIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCEDTMTYKCPRITERQPDDVDCWCNATDTWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETWALRHPGFTVIGLFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKNKPTLDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDANFVCRRTFVDRGWGNGCGLFGKGSFLTCAKFKCVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTIATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNRVVLLTMKKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFAGHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVIDKEKPVNIEAEPPFGESYIVVGSGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIFGTAYGILFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGKELKCG | Function: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, wereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86845
Sequence Length: 791
Domain: The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.
Subcellular Location: Virion
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P19724 | LVRKSCERLYEGRMGVWNGSLKAELRPAEKVLAKKTRSFTAAPLDTLLGAKVCVDDFNNWFYSKNMECPWTVGMTKFYKGWDEFLRKFPDGWVYCDADGSQFDSSLTPYLLNAVLSIRLWAMEDWDIGEQMLKNLYGEITYTPILTPDGTIVKKFKGNNSGQPSTVVDNTLMVLITMYYALRKAGYDTKTQEDMCVFYINGDDLCIAIHPDHEHVLDSFSRSFAELGLKYDFTQRHRNKQNLWFMSHRGILIDDIYIPKLEPERIVAILEWDKSKLPEHRLEAITAAMIESWGYGDLTHQIRRFYQWVLEQAPFNELAKQGRAPYVSEVGLRRLYTSERGSMDELEAYIDKYFERERGDSPELLVYHESRSTDDYQLVCSNNTHVFHQSKNEAVDTGLNEKFKEKEKQKEKEKEKQKEKEKDDASDGNDVSTSTKTGERDRDVNVGTSGTFTVPRIKSFTDKMILPRIKGKSVLNLNHLLQYNPQQIDISNTRATQSQFEKWYEGVRNDYGLNDNEMQVMLNGLMVWCIENGTSPDISGVWVMMDGETQVDYPIKPLIEHATPSFRQIMAHFSNAAEAYIAKRNATERYMPRYGIKRNLTDISLARYAFDFYEVNSKTPDRAREAHMQMKAAALRNTSRRMFGMDGSVSNKEENTERHTVEDVNRDMHSLLGMRN | Function: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.
PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 78151
Sequence Length: 675
Subcellular Location: Virion
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P21294 | QQQPFATIAQEGKAPYIASMALRKLYMDRAVDEEELRAFTEMMVALDDEFEFDSYEVHHQANDTIDAVGDNKKDAKPEQGSIQSNPNKGKEKDVNAGTSGTHTVPRIKAITPKMRMPKSKGATVLNLEHLLEYAPQQIDISNTRATQSQFDTWYEAVRMAYDIGETEMPTVMNGLMVWCIENGTSPNVNGVWVMMDGNEQVGYPLKPIVENAKPTLRQIMAHFSDVAEAYIEMRNKKEPYMPRYGLIRNLRDVGLARYAFDFYEVTSRTPVRAREAHIQMKAAALKSAQPRLFGLDGGISTQEENTERHTTEDVSPSMHTLLGVKNM | Function: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.
PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 36868
Sequence Length: 327
Subcellular Location: Virion
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P32574 | KDEIIDAGIDGKKGGGKKDTQDAGESNKGKEKDKDINAGSKGSGVPRLQKITKKMNLPMVKGSMVLDLDHLIEYKPDQTKLFNTRATDAQFATWYEGVKAEYELSDDQMGVIMNPFMVWCIENGTSPDINGVWVMMDGDEQVEYPLKPMVENAKPTLRQIMHHFSDAAEAYIEMRCASGPYMPRYGLLRNLRDKNLARYAFDFYEVNAKTSDRAREAVSGEKAAALSNVTNKLFGLDGNVATISEDTERHTARDVNQNMHTLLGMGAPQ | Function: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
Sequence Mass (Da): 29934
Sequence Length: 269
Subcellular Location: Virion
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P94544 | MHKKDIIRLLETIAVYMELKGDNPFKVSAFRKAAAALEQDDRSLSEMDDMMSLSGIGKGTYSVIKEYIDEGKSSTLESLQKEVPEGLVPLLKLPGLGGKKIAKLYKELGVHDAESLKEACEQQKVQGLAGFGKKSEEKILQALGEAGKQPERFPIGYALRIAREIEEHLSQFTHIIKFSRAGSLRRARETVKDLDYIIATDHPAEVREQLLELPNIKSVIASGDTKVSVILSFEYETSVDFRLVTEEQFPTTLHHFTGSKDHNIKMRQIAKERGERISEYGVETVETGEIKTFPSEREFYAHFGLPLIPPEIRESGQEVETYSDSIELIELGQIKGDLHMHSTWSDGAFSIREMAEACIKKGYQYMAITDHSQYLKVANGLTAERLKQQAKEIDALNAEFENFRILKGVEMDILPDGTLDYDDDVLAEMDIVIASIHSSFNQPEHVIMKRLETALTNKHVDIIAHPTGRLIGRRAGYEIDIDQLIELARKTNTALELNANPARLDLRTEHLMKANEQGVTLVINTDAHNIEMLDDMKTGVTAARKGWTETKNVLNARSLKDVEAFLKRND | Cofactor: Probably binds 2 divalent metal cations per N-terminal polymerase domain. Mn(2+) is more effective than Mg(2+) for DNA polymerase activity.
Function: Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely involved in resecting unannealed 3'-termini during DNA repair. The same PolX molecule could perform the subsequent gap-filling step. Does not display 5'-deoxyribose 5'-phosphate (dRP) lyase activity, as predicted by the lack of the lysine and tyrosine residues responsible for the dRP lyase activity in some other PolX members.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 64120
Sequence Length: 570
Domain: The 3'-5' exonuclease activity resides in the C-terminal PHP domain.
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Q4V5R4 | MEPKSQDQAPNRDDPDLQTEPLTIAQSITSFYMYNPYEKRSVEVPLTNCDAFISLLKCVIGTGILAMPLAFRCSGFVMGTVMSILLMILLTYSIHLLIADMTECCRRRRVPQVSMPEAVRIAYEEGPKWINCFGRAAGFMTTCVLVFGQFLLCTVYLVFVSKNFKEIGDHYIERYNERYYVLVACLLLLPLFMIRRLKYLVPLNLISNFLLYAGFALIMYYLFNGLPNINDREMVTPPVEWIEFIAIAAFSLTAVGSMLVVEAHMAHPQSYLGLFGVLNLAVLFILLSNMFFGIIGYWRFGDNVHASITLNIPQDEILSQFIKVFIASGIFLSYPLNGFVVITVMFSDYENSEPRGRYRTLIEYVVRLLFLFLTGAVAIGVPNLAALTELEGAFSLSNLNLLCPALIDVFLNYNVGYGRLMWKLIRDILLILIGLIFGIVGCTVALMQLIRDFQLTLNSM | Function: Probable glutamate transporter which transports extracellular glutamate into the cells. Regulates the production of intracellular reactive oxygen species (ROS) probably by controlling the synthesis of antioxidant glutathione. By regulating ROS production in blood cells, required for maintaining bacteria phagocytosis following infection with S.aureus and possibly E.coli.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52035
Sequence Length: 460
Subcellular Location: Cell membrane
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Q9BGN0 | MAKLLLLTLLGASLAFVGERLLAFRNSFGAVQELEPVEPQNCVLIEGLENGSEDIDILPSGLAFISSGLKYPGMPNFAPDEPGKIFLIDMNEKNPRAQELEISNGFEKESFNPHGISTFIDKDHTVYLYVVNHPHMKSTVEIFKFEEQQRSLVHLKTIKHELLKSVNNIVVLGPEQFYATRDHYFTNYVLALLEMFLDLHWTSVLFYSPKEVKVVAKGFSSANGITVSLDKKYVYVADATAKNVHVMEKHDNWDLTELKVIHLDTLVDNLSVDPATGDILAGCHPNGMKLLNYNPEDPPGSEVLRIQNVLSEKPRVSTVYTNDGSVLQGSTVASVYQGKILIGTIFHKTLYCVL | Cofactor: Binds 2 calcium ions per subunit.
Function: Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters (By similarity). Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents.
PTM: Glycosylated.
Catalytic Activity: a phenyl acetate + H2O = a phenol + acetate + H(+)
Sequence Mass (Da): 39507
Sequence Length: 354
Subcellular Location: Secreted
EC: 3.1.1.2
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P54660 | MLVLRNLLALVTLALLFTLSSAQYTLSVSNSASGSKCTTAVSAKLNACNTGCLNSFNIVESSNGKGLVFKTFINAACSGEYESLSQFTCAANQKIPTTSYIVSCNSTPSSNSTTDSDSSSGSTVMIGLASSLLFAFATLLALF | Function: Binds F-actin and nucleates actin assembly. Major high affinity link between the plasma membrane and the cortical actin network.
PTM: Disulfide bond(s) stabilize the native, actin-binding conformation of ponticulin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14770
Sequence Length: 143
Subcellular Location: Cell membrane
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Q54M25 | MLFIKSLLLLLSLIFAVSNATGYVGFKVDGPGCNATKIITLENGACQTVCTNLYGKVTPTNDPSKFNLNPFIDVDCKTPLMAEQQVTCLPDNKPFKVSTLTVTCIPDTTSSSTSPSSTSPSSTSPASTLIGSIAFVTLAALFALI | Function: Binds F-actin and nucleates actin assembly.
PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 15188
Sequence Length: 145
Subcellular Location: Cell membrane
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Q54LB9 | MKLNNSLLLLIVAIIASSNAAETFSNFQVTNSEASSPCVTTPVELKVNTCQSACDSILNVLPVTGSTSKFTFNQFGAQDTKCAATPTSSNEFTCVDGKSKVAIGTTTYSVVCVPDKTNSSESDSSDSTRIGASFALFALALLSMLAL | PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 15294
Sequence Length: 147
Subcellular Location: Cell membrane
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Q54SJ8 | MLLNKSLLLLVAFVFAIVSATTYSEFKITGTNPLTQETCDPSIVYTSQNGACQGVCGMFGKLVATSNSTQFNVEMYGSAGCVGPLGTTGLTCLPNEQVIKVTETISVVCFADKDEPSGDDSSGDDSSAAATMIASFSAILIALLFALL | PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 15356
Sequence Length: 148
Subcellular Location: Cell membrane
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Q54BG3 | MQTFKKLILILLLLALFVFSNGQYTFNVLNKAPGSKCENGTMAELNTCSKDCLTSFLILKSIDKKSLTFTTFNNNQCNGDYNTQTTFDCKPTPQNISQTQYFISCEEQTSKPTSSPIHSNSTIKSTSTTTTSTPLPHKDTPHHSASSSSIVVRLTPIFFIAFASLIFLFGF | PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18932
Sequence Length: 171
Subcellular Location: Cell membrane
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Q54LH6 | MKFIPALIIFVFTIFALTNSETTYSGFKITSADPKNPCSISVPQTDVGTKCIDVCGQGNINIAAVSGETNKYDINGYQATDQCKNSAGQQTLTCGTPVTVGVFSIDCAPDAGATTAAVTTAATTAAVTTAATTAAVTTASTTAAFTTTGTSSTIVIPFALILSLLLSVITL | PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 17322
Sequence Length: 171
Subcellular Location: Cell membrane
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Q54LM2 | MKLLNSLVLLAALCAITANGKIVEDTPDPSTVYNLFQLSSSDGGCDPAGTHSPDANVNVSVDKCRNVCNKNIKISKGTSTNQFTFQTYNDNSCSQATSDQALSFTCSDNVKKQLGTSIYSVICSTGSDSTNPTSTPSTTPSATPTVTPSTTPTVTPTVTPSTTPTVAPTVPPTTPPSTTTGSGSTVVASFGLIVSILLASLAL | Function: Binds F-actin and nucleates actin assembly.
PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20730
Sequence Length: 203
Subcellular Location: Cell membrane
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Q54GU3 | MRLLNNLILMVVLFVAVSNATTKFTFNTFSVRNTEDQTCFTKTAKTTDDSTKVDINKCTVGCGGSMKIRKGTKSQQYQFELFSSTDCTGETTSKVLFVCPNPSIDAISIKSTSNTIKCGTLPPDSEIKEDDTATAVVNDENNNETKNEPKTKTKSTPKSPSTPKTNNSNEDSDLTTSSSDSSSSTKSSPKSKSSTEVNENKPKSDNETAEGNNASSNIATFSLVIISLLVASLF | Function: Binds F-actin and nucleates actin assembly.
PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25152
Sequence Length: 234
Subcellular Location: Cell membrane
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Q1ZXQ9 | MKNLILLFLLISIINLIQSLPLDSVINFYVNSTVGSCKGKQLEVSLDVCNNGCSNSFKITSSKDNVNNYNFTSYIETDDKQCLTNNYTINLFNCSIDNAALVGPYSVKCIFKETPSPSNSSNPSPSPNTTSSSSLSSSSLNSNEPNQTTKPPKTNEPQKNNSTSNIPNFFAIFGFLVLIIFILGDKI | Function: Binds F-actin and nucleates actin assembly.
PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20414
Sequence Length: 187
Subcellular Location: Cell membrane
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Q54IM7 | MKLTLLLIISFILFSNVVFSQKFNLFNFEQNHCLTTPELFLDECQLLNSTLPMCKGYMRVTYVSSNTYEFSIFNTSTPLCGQVNRKAGSNFTCDQSTNGVKQNYTGFSVTCISTSNESSLSSKTQQSIVFTVLLLSLALIASIF | Function: Binds F-actin and nucleates actin assembly.
PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16081
Sequence Length: 144
Subcellular Location: Cell membrane
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Q54T57 | MKFLSTLILLLSVLALVRGEQYNKFTVDLNGVCTNSGSLDTCTNQCGNAGGSFQISQSGGEYQYEQYATKDCDLMASLTSKFACLADEAPVTLGLGNIKITCQDPSNSASSPLTTAVLFVVAFAAAIALLL | Function: Binds F-actin and nucleates actin assembly.
PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13745
Sequence Length: 131
Subcellular Location: Cell membrane
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P13653 | MALQLLPSTLSVPKKGSSMGAVAVKDTAAFLGVSSKAKKASLAVRTQVATAPSPVTTSPGSTASSPSGKKTLRQGVVVITGASSGLGLAAAKALAETGKWHVVMACRDFLKASKAAKAAGMADGSYTVMHLDLASLDSVRQFVDAFRRAEMPLDVLVCNAAIYRPTARTPTFTADGHEMSVGVNHLGHFLLARLLMEDLQKSDYPSRRMVIVGSITGNSNTLAGNVPPKASLGDLRGLAGGLSGASGSAMIDGDESFDGAKAYKDSKVCNMLTMQEFHRRYHEETGITFSSLYPGCIATTGLFREHIPLFRTLFPPFQKFVTKGFVSEAESGKRLAQVVAEPVLTKSGVYWSWNKDSASFENQLSQEASDPEKARKVWELSEKLVGLA | Function: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Catalytic Activity: chlorophyllide a + NADP(+) = H(+) + NADPH + protochlorophyllide a
Sequence Mass (Da): 41181
Sequence Length: 388
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
Subcellular Location: Plastid
EC: 1.3.1.33
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B5CY96 | MSYKYIFLLSAFTLGVPPGIYCQGRNEVVVDYNTRRFLSGVSELDRSKYFNIHSTSDDDKDVGKFLADYQVGLGRKFWGPYSYAYNKTHEVGKYPQMKPYSGNISVKRYIATEHPYVQHIQGGIDVQAAGAWSAEYYSNSELVPEFFEPLNEPFVHANDAGFTVQGQAMRELMVDFYASIGKHIHNNPRLNGKMKVIGYAAAYPAWEDGNFNYWNTRMKMFIDRAGAYMDGFSVHLYDGINVTGTDTKRSGSNSEAVLDMVEAYSYIKFGHVKPLAISEFGGIDNSKPDDSYDDISSVRSVSSFNHFLFNLMERQDNLFISIPFVSDKAEWHITAANNYTSYSAALFIPDNPQNLKNTTWRLNDKKYFFELWKNVKGERVDITSSNPDIQVQAFKDGGRLYIALDNLDDNPQTVYLNNKNSWKDVSNVTKRSLYVNYNAGIEYTEQNVPSMPESISIVPNQTIVLVADVSSSAFTNSIIRNKYYSSEYLKPISAGSSLSFPFTGIESGSGRASLRMSIGRPVSASKKPVVKINGTAVSVPDNWKGYGQSNRNIFFGMIEVPFDIQLLKNGDNNVDITFSDGGGHVSSMILQVEKYTVSTLQNGTFSEGLSAWQPLGNYGTVCVQTDNAGNNVACISGHAGLMQRVDMESGRTYRFSADVKTEGACKLKVMLQDMSTGTVYTEEFSSPGNYKAVSFDFNSTVKKVVCAIVCERQNDAAWIDNIVLLPQN | Function: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone.
Catalytic Activity: Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran.
Sequence Mass (Da): 81281
Sequence Length: 728
EC: 3.2.1.178
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D7GXG0 | MKKVLLFLIFLVSANLSAQLPSPTNGKKWEKVEQLSDEFNGNSIDTNKWYDYHPFWEGRAPSNFKKGNAFVSDGFLNLRSTLRKEPSSVQDPFKDIWVDAAAAVSKTKAQPGYYYEARFKASSLSMTSSFWFRVGQFSEIDVIEHIGNPSKENRQDDLPYQYHVNTHYYGKHAGLQPLGTEYKMPGRGRDNFYTYGFWWKSPNELLFYFNGKQVMRIVPRVPLDEELRMIFDTEVFPFATAGVANIGLPKPENLRDNSKNTMKVDWVRVYKLVDGTAAEDSSDAPIGSYISLKKTQGDGKFVTGEKDGSQLVARGSTVQSWEKFKVEKHPKGGITLKANSNGKYVQVQGSDINKPVRAAGDFQGDWEQFEWKSKGNGLVALKNVLTGKWLQAPWTENNAIIRPKGPVDNGWETFAWKKETSPTASTALSAQLETKTVDGIRVYPSPASETLTIEGVEGENGLRVFDSTGNPVLKKEGILGRKERLNVSGLIKGNYLLRTGSGEQTWFQKN | Function: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone. Displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites.
Catalytic Activity: Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran.
Sequence Mass (Da): 57311
Sequence Length: 510
Subcellular Location: Periplasm
EC: 3.2.1.178
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P80522 | MSKTAPKTYITSGHSGCAGCCDAFAAKFTLMGAGPNTIVINPTGCLEVMSTPFPYSSWQVPWIHSLFENAGAVASGVEAALKALGKKDDVKVVSIGGDGSTMDIGLGALSGAFERGHDFTYVCMDNEAYMNTGVQRSSGTPFDASTTTTPAGKVSFGNPRPKKNMPAIMAAHGSPYVATTSIGFPRDMIRKVKKATEIVGPTYIHAQAPCPTGWGFDTSKTLEIAKLAVETCLWPMYEMENGEITQVRKVKNPRPVEEYLRAQKRFKHLFTMEGGEEEIKKIQAIADWNIKHFELQ | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Catalytic Activity: CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 32056
Sequence Length: 296
EC: 1.2.7.1
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Q57714 | MIVMQFPREEYFAPGHRGCAGCGAAIVARLLLKVAGKDTIITNATGCLEVMTTPYPETSWRVPWIHTAFENAAATASGIEAAVKALKRKRGKFADKKINVIAIGGDGGTADIGFQALSGAMERGHDILYIMYDNEAYMNTGIQRSSSTPFMAATTTSPAGSKIRGEDRPKKDMTMIMAAHGIPYVATACISYPEDFMRKVKKALSIEGPKFIQVLQPCTTGWGYPPEKTIEIGRLAVETGIFPLYEIENGEFRITYKPAKRKPVREYLKMQKRYRHLTDEDIERIQKYIDEKCKLLGL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Catalytic Activity: CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 33098
Sequence Length: 298
EC: 1.2.7.1
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P80901 | MKIPEEEFLAPGHRGCAGCGATVGVRLALKVLGKNTVAVSSTGCLEVITTPYPETAWEIPWIHVAFENAAAVASGVERALRARGRGEVNVVAFAGDGGTADIGLQSLSGAMERGHNIIYICYDNEAYMNTGIQRSASTPYGASTTTSPHGKESFGEDRPKKNMPLIMAAHGVPYVATASISYPEDFMEKVRKARDIEGPAYIHLHQPCTTGWGFDPSKTVELGRLAVETGSWILYEIEDGDFRVTYRPVQRKPVEEYLNAQKRFRHLTEEQKAKIQEYVDSVCQELRI | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Catalytic Activity: CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 31623
Sequence Length: 288
EC: 1.2.7.1
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B5CY92 | MRKTVLYLSAASLFLSSYTLKNDKEYSLAEEHIKNLPEAPEGYKWVVNEDYTDEFNGKRLNAAKWHAKSPYWTNGRPPATFKAENVSVKKGCLRIINTVLSPTEGLDGKPGDKYRLAGGAVASVKNQAHYGYYETRMKASLTTMSSTFWLSNRPVMKEIMKGGKKIKTWSSQELDIIETMGIIRSVNPDNPWNKTWNMQMNSNTHYWYQEQGGKRTDNTAKRSDVVSYMTDPSAEDFHTYGCWWVDANTVKFYYDGKYMYTIKPTTKYTDTPFDRPMFIHIVTETYDWEKQVPTAEDLKDKDKSTTYYDWVRAYKLVPIEE | Function: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone.
Catalytic Activity: Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran.
Sequence Mass (Da): 37253
Sequence Length: 321
EC: 3.2.1.178
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Q51485 | MYKNKKTRPAARTVGCLFALGALGLGSAAHAAEAFSPNSKWMLGDWGGKRTELLEKGYDFKLEYVGEAAANLDGGYDDDKTGRYTDQFALGVHMDLEKILGWKATEFQFTVTERNGKNLSNDRIGDPRAGHISSVQEVWGRGQTWRLTQLWLKQQYFDGALDVKFGRFGEGEDFNSFPCDFQNLAFCGSQVGNWAGSIWYNWPVSQWALRVKYNFAPDWYVQVGAYEQNPSNLETGNGFKMSGSGTKGALLPVELIWQPKVGAEQLPGEYRLGYYYSTAKADDVYDDVDGQPQGLTGNDFKSRGSKHGWWVVAQQQVTSHNGDASRGLSLFANLTVHDKATNVVDNYQQLGVVYKGPFDARPKDDIGLGIARIHVNDDVKKRQRLVNQVNGIDDYDNPLYQPLQDTEYNAELYYGVHVTDWLTVRPNLQYIKQPGGVDEVDNALVAGIKIQTVF | Function: Substrate-selective channel for a variety of different sugars. Could potentially facilitate the diffusion of diverse compounds, dependent on the presence of a hydroxyl group, but is presumably restricted to carbohydrates. Involved in the transport of glucose, mannitol, fructose and glycerol (sugars able to support the growth of P.aeruginosa). Facilitates glucose diffusion across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50754
Sequence Length: 454
Subcellular Location: Cell outer membrane
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Q51805 | MAVRKPPITTREYWAPGHAACAGCGCATALRLATKALSEAMEEKYGDPNAFAIAHATGCMEVVSAVFPYTAWKAPWIHVAFENAAAVASGIEAAWKKLGRKGKILAIGGDGGTADIGLQALSGMLERWHNVLYLMYDNEAYMNTGIQRSSSTPYGAWTTTSPPGKYSVGEDKPKKWVALIAAAHQIPYVATASIGNPLDFVRKIKKAGKIDGPAFVQVLCTCPTGWRSPLEKGVEIARLAIETGIWPLFEIENGDIWNIKIQPPGGGAKVYKEGNRVVRIEFKKPIEEYLKLQGRFKHLFKRPEAIEELRNQVKAMWKVLGVEAILPRPEE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Catalytic Activity: CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36261
Sequence Length: 331
EC: 1.2.7.1
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Q56317 | MPVNIKQLAQEFDKKEIGITQGHRLCPGCGAPITVKFVMMIARHLGYEPVVGLATGCLEVSTSIYPYTAWSVPYIHNAFENVAATMSGVETAYKALKNKGKIPEDKKYAFIAFGGDGGTYDIGLQSLSGMLERGHKVLYVLYDNEGYMNTGNQRSGSTPPGSDTTTAPVGKKLPGKVQLKKNIVEIVAAHENVYAATASLSEPMDFFAKVEKALNFDGPSFLAVFSPCVRFWRVNDDKTVEISKLAVETKYWPLYEVERGVYRVTRKPRQFKPVEEFLKAQGRFRKLLSRPDAKEIVDELQEYVDRRWERLLTLEEVTKDKPIR | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Catalytic Activity: CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36385
Sequence Length: 324
EC: 1.2.7.1
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D7GXF9 | MKLSNQFLITITLLITSITFAQEAPHFKPGEDPRQPHQEWKLIENMSDEFEGKKIDEKKWQISGQGWIGRAPGLFLAENISLNNGSLQITTTMLPEPIVKNNKTYTHGGGYVGSRNGMTYGYYECEMKANKTFMSSTFWLINEGKDRLGCDKRTTELDIQESVGQITNDADWMKYFDQTMNSNTHSRNIPEGCEYEKGSSKGKAELGGKAYEDFHVYGVWWKSKDEIIFFLDGKMQSKVTPPADFDIEMYLRMVVETYDWNPVPKDGGMTGSKEDRTTTYNWVRSWQLVDSKN | Function: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone. In contrast to PorA, tolerates the presence of 3-6-anhydro-L-galactose in subsite -2.
Catalytic Activity: Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran.
Sequence Mass (Da): 33622
Sequence Length: 293
Subcellular Location: Periplasm
EC: 3.2.1.178
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Q7Q3N5 | MDYYYDDYYDEYYDHPDQAAARLFHRDLSIEETIKNCVHPSLRFATQYITNFIAINLLFSVLVLIVRKLFPTAQRSLHLLSCVCGAALVYRVIDHGFYHFLQLAVSLYAVQWTLHRWLTGTGRYIKTPFIVIAYGIGNLLVSELLEPSPETWNRIRGTQMILLMKALSLAFDTDDNHSLRSQLTVLSYSGYILCPANIVLGPWISFNDYLTIWKPPAGIEPKQCRSSSGRRMLIHVFRIVTSALMAVGFLLTSNCMIDYLLAPINSWKWVRAYGRALSFRTSHYFIGYLSQCSMMAAAADWHRAEDERSIMLPVSSLYRITSPMAVEFPRSLVQVVTAWNIPMHLWLKRYIFRTTKRPFGTGTAIALTYIISSLLHGLHYRLWITLLTIGSWTFVEHEVRKKLATIYSACVLVGKCPSSCTVHQHKSNSVFCTVINMLFFALNIFNLIYLGCIFESSEGPPDEVQQDKSMFGPWTELNYASHWLLVFAYLFYFVI | Function: Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors.
Catalytic Activity: (9Z)-hexadecenoyl-CoA + [Wnt protein]-L-serine = [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56957
Sequence Length: 495
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.250
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Q22329 | MDNGHGYEEFELLEDGSLGECSTQVANATFLTISKLICLVVAFKFIKHIPISTTVRVYVHVFASTFTVMWFSRNHLQSAIIYNMFSLISLALAIKQFSGYIILAGNISLLIALQNFCRHYRSEDYFLSIRGILMIHIMRLTTVAFNLEKANSNKFRFVQFSSYVEYIYFPPFIIFGPYLSFEQFFKMRDKKWTGSENELGFIIQSLLAIFNAITLAIISSCHFEFFEPSSQFMEDALTAMSFRFSHYFVCLSTQAFVLMLGSDVVVANPLNIEFSRSTLQTVSEWNKPFHTFLHENIFKRRLFNSTACNVFFTFAVSSLLHGLDFQMTITLLALGFIAYSETVFRKRLSARYSMCVAAKACPVRSNSLSCKHRHSNKTGRALIINLFFLMLSMYHLVFTGMTFTDDYSAIGYPFDHAWKIWGSHYYSSFMISFLFLALSKII | Function: Key regulator of the Wnt signaling pathway that mediates lipid modification of Wnt proteins . Acts as a protein-serine O-palmitoleoyltransferase that catalyzes the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins (By similarity). Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors (By similarity). Has a role in cell specification, specifically in blastomere signaling . Involved in cytosketetal polarity . Required for the orientation of mitotic spindle axis .
Catalytic Activity: (9Z)-hexadecenoyl-CoA + [Wnt protein]-L-serine = [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50874
Sequence Length: 442
Subcellular Location: Membrane
EC: 2.3.1.250
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Q9VWV9 | MDYQYFEEESDYIDLDEEEEDDDVVTAGSLDHRFGQPNGEEDYYFGGDDVEEELVVDGHGVLELAGRLLESLQSCVQPSVLQVMQYVAPMLLLCLLCRLLCLLYSQRRRLTSLAPLHLFHFACGLIILQITVGYRLLLLLLLAAVGYLLLQLLRLGRRGAQVLAVLTVGSQFLYELLIWRRRSDWPQLRGIQMVVNMKLISLGFDLTASGQLQARIPGPFAYLGYIYSPATCALGPWVSFGCYMDCLVPRNSWLVSLRRLLPNVVICVLAVTVSNCVAPALSDFFGDSSHFLVMYWDALSVRSSHYFVGMMAQALLVASDQRLDGATKESDMLGPLISQPWRIEWPRSISSLVRSWNIPMHEWLKRYIYAPCKPTASTSRGRILVVVLSTYLVSSLLHGMDLRIYLVLISLAFLAEGESLLRRQLASLLNACITANLCPGKERCRYSHCPSKRRLNSLSYWLARLTNLAFTALAIFHLAYLGVVLLGDDLEVGEDGDSFLWHWQQAGYLSHYIGLGTFVLYLFIS | Function: Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins. Serine palmitoleoylation of Wnt proteins is required for efficient binding to frizzled receptors (By similarity). Also facilitates the glycosylation of Wnt family members, including wg and Wnt5. The cotranslational disulfide bond formation of wg competes with the N-glycosylation. Porc stimulates the post-translational N-glycosylation by anchoring wg at the ER membrane, probably through acylation .
Catalytic Activity: (9Z)-hexadecenoyl-CoA + [Wnt protein]-L-serine = [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59195
Sequence Length: 525
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.250
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Q9JJJ7 | MATFSRQEFFQQLLQGCLLPTVQQGLDQIWLLLTICFACRLLWRLGLPSYLKHASTVAGGFFSLYHFFQLHMVWVVLLSLLCYLVLFLCRHSSHRGVFLSVTILIYLLMGEMHMVDTVTWHKMRGAQMIVAMKAVSLGFDLDRGEVGAVPSPVEFMGYLYFVGTIVFGPWISFHSYLQAVQGRPLSRRWLKKVARSLALALLCLVLSTCVGPYLFPYFIPLDGDRLLRNKKRKARGTMVRWLRAYESAVSFHFSNYFVGFLSEATATLAGAGFTEEKDHLEWDLTVSRPLNVELPRSMVEVVTSWNLPMSYWLNNYVFKNALRLGTFSAVLVTYAASALLHGFSFHLAAVLLSLAFITYVEHVLRKRLAQILSACILSKRCLPDCSHRHRLGLGVRALNLLFGALAIFHLSYLGSLFDVDVDDTTEEQGYGMAYTVHKWSELSWASHWVTFGCWIFYRLIG | Function: Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors.
Catalytic Activity: (9Z)-hexadecenoyl-CoA + [Wnt protein]-L-serine = [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52508
Sequence Length: 461
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.250
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O48741 | MALQAAYSLLPSTISIQKEGKFNASLKETTFTGSSFSNHLRAEKISTLLTIKEQRRQKPRFSTGIRAQTVTATPPANEASPEQKKTERKGTAVITGASSGLGLATAKALADTGKWHVIMACRNFLKAEKAARSVGMSKEDYTVMHLDLASLESVKQFVENFRRTEQPLDVLVCNAAVYQPTAKEPSFTAEGFEISVGTNHLGHFLLSRLLLDDLKKSDYPSKRMIIVGSITGNTNTLAGNVPPKANLGDLRGLASGLNGQNSSMIDGGEFDGAKAYKDSKVCNMLTMQELHRRYHEETGVTFASLYPGCIATTGLFREHIPLFRLLFPPFQKYITKGYVSEEEAGKRLAQVVSDPSLGKSGVYWSWNNNSSSFENQLSKEASDAEKAKKLWEVSEKLVGLA | Function: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Catalytic Activity: chlorophyllide a + NADP(+) = H(+) + NADPH + protochlorophyllide a
Sequence Mass (Da): 43883
Sequence Length: 401
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
Subcellular Location: Plastid
EC: 1.3.1.33
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O66148 | MAQDQKPTVVITGASSGVGLYAAKALVKRGWHVVMACRNLEKADSAAKSLGMSPDSYTLMHIDLGSLDSVRKFVTQFRESGKSLDALVCNAAVYMPLLKEPMRSPEGYELSVATNHFGHFLLCNLLLEDLKHSTHNDPRLIILGTVTANSKELGGKIPIPAPADLGDLSGLEAGFKAPIAMIDGKPFKAGKAYKDSKLCNMITSRELHRRYHDSTGIVFNTLYPGCVADTPLFRNSLPVFQKVFPWFQKNITGGYVSQELAGERTAQVVADPEFKQSGVHWSWGNRQKEGRESFVQELSEKVTDDAKAKRMWELSEKLVGLA | Function: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Catalytic Activity: chlorophyllide a + NADP(+) = H(+) + NADPH + protochlorophyllide a
Sequence Mass (Da): 35400
Sequence Length: 322
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
EC: 1.3.1.33
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O80333 | MPKRSNGSLVVRCAVSVVRFSKENVSCDLASENFTFSRDSFPVVSTVLRVSEAVYRMAAVASLGSALSVSSAALSQNVSVSNNATKESAFLGLRMGEVAKFGGALLSVSTVAANLKSKPGVLSVNAVTAPAETMNKPSSKKTATKSTCIITGASSGLGLATAKALADTGEWHVIMACRDFLKAERAARSVGIPKDSYTVIHCDLASFDSVRAFVDNFRRTERQLDVLVCNAAVYFPTDKEPKFSAEGFELSVGTNHMGHFLLARLLMEDLQKAKDSLKRMIIVGSITGNSNTVAGNVPPKANLGHLRGLAGGLNGVNSSSMIDGGEFDGAKAYKDSKVCNMFTMQEFHRRYHAETGITFSSLYPGCIAETGLFRNHVTLFRTLFPPFQKYITKGYVSEEEAGKRMAQVVSDPKLSKSGVYWSWNKDSGSFENELSEEASNPEKAKRLWELSERLSGLV | Function: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Catalytic Activity: chlorophyllide a + NADP(+) = H(+) + NADPH + protochlorophyllide a
Sequence Mass (Da): 49387
Sequence Length: 458
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
Subcellular Location: Plastid
EC: 1.3.1.33
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Q59987 | MEQPMKPTVIITGASSGVGLYGAKALIDKGWHVIMACRNLDKTQKVADELGFPKDSYTIIKLDLGYLDSVRRFVAQFRELGRPLKALVCNAAVYFPLLDEPLWSADDYELSVATNHLGHFLLCNLLLEDLKACPDADKRLIILGTVTANSKELGGKIPIPAPPDLGNFEGFEAGFKKPIAMINNKKFKSGKAYKDSKLCNMLTTRELHRRFHQETGIVFNSLYPGCVADTPLFRNHYSLFRTIFPWFQKNVTKGYVSQELAGERVAMVVADDKFKDSGVHWSWGNRQQAGREAFVQELSEQGSDAQKAQRMWDLSEKLVGLV | Function: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Catalytic Activity: chlorophyllide a + NADP(+) = H(+) + NADPH + protochlorophyllide a
Sequence Mass (Da): 36062
Sequence Length: 322
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
EC: 1.3.1.33
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Q9UT98 | MIRAANGFRISVRNTAVCLAPNFRQLKGFSIINLGSLQYFRYNSVYSKSIRLVNTLENRIVPVYKECASPQSIGGKSNLKQLQWPKPPKNILILKKRMDERVDHCFETLVQHLQQTYPDICIITETDVAKKFSYLNLYTWTEISDLEQKVDAIITVGGDGTILHAASLFARSGMPPILSFSLGTLGFLLPFDFGSFQTAFADFYNSRSFVLMRMRLRVAMKTKLYNESIYAMNEMHIHRGLSPHMAVLKVFVNDKFLTEAVADGLIISTPTGSTAYSLSSGGPIVHPSINALLLTPICPNSLSFRPVLFPDTFKISIETSNKSRVRPQLSIDGRPLGLTDIGQRIDITSVKDNAIPCIIRSHKEDDWVSDIVSLLRWNHPFHRKGW | Function: Phosphorylates both NADH and NAD(+), with a preference for NADH. Anti-oxidant factor and key source of the cellular reductant NADPH (By similarity).
Catalytic Activity: ATP + NADH = ADP + H(+) + NADPH
Sequence Mass (Da): 43500
Sequence Length: 386
Subcellular Location: Mitochondrion
EC: 2.7.1.86
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Q06892 | MFVRVKLNKPVKWYRFYSTLDSHSLKLQSGSKFVKIKPVNNLRSSSSADFVSPPNSKLQSLIWQNPLQNVYITKKPWTPSTREAMVEFITHLHESYPEVNVIVQPDVAEEISQDFKSPLENDPNRPHILYTGPEQDIVNRTDLLVTLGGDGTILHGVSMFGNTQVPPVLAFALGTLGFLSPFDFKEHKKVFQEVISSRAKCLHRTRLECHLKKKDSNSSIVTHAMNDIFLHRGNSPHLTNLDIFIDGEFLTRTTADGVALATPTGSTAYSLSAGGSIVSPLVPAILMTPICPRSLSFRPLILPHSSHIRIKIGSKLNQKPVNSVVKLSVDGIPQQDLDVGDEIYVINEVGTIYIDGTQLPTTRKTENDFNNSKKPKRSGIYCVAKTENDWIRGINELLGFNSSFRLTKRQTDND | Function: Phosphorylates both NADH and NAD(+), with a twofold preference for NADH. Anti-oxidant factor and key source of the cellular reductant NADPH.
Catalytic Activity: ATP + NADH = ADP + H(+) + NADPH
Sequence Mass (Da): 46247
Sequence Length: 414
Subcellular Location: Mitochondrion matrix
EC: 2.7.1.86
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Q15063 | MIPFLPMFSLLLLLIVNPINANNHYDKILAHSRIRGRDQGPNVCALQQILGTKKKYFSTCKNWYKKSICGQKTTVLYECCPGYMRMEGMKGCPAVLPIDHVYGTLGIVGATTTQRYSDASKLREEIEGKGSFTYFAPSNEAWDNLDSDIRRGLESNVNVELLNALHSHMINKRMLTKDLKNGMIIPSMYNNLGLFINHYPNGVVTVNCARIIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDDLSSFRAAAITSDILEALGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSESIMGGAVFETLEGNTIEIGCDGDSITVNGIKMVNKKDIVTNNGVIHLIDQVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASALRPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLNELYNGQILETIGGKQLRVFVYRTAVCIENSCMEKGSKQGRNGAIHIFREIIKPAEKSLHEKLKQDKRFSTFLSLLEAADLKELLTQPGDWTLFVPTNDAFKGMTSEEKEILIRDKNALQNIILYHLTPGVFIGKGFEPGVTNILKTTQGSKIFLKEVNDTLLVNELKSKESDIMTTNGVIHVVDKLLYPADTPVGNDQLLEILNKLIKYIQIKFVRGSTFKEIPVTVYTTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETITEVIHGEPIIKKYTKIIDGVPVEITEKETREERIITGPEIKYTRISTGGGETEETLKKLLQEEVTKVTKFIEGGDGHLFEDEEIKRLLQGDTPVRKLQANKKVQGSRRRLREGRSQ | Function: Induces cell attachment and spreading and plays a role in cell adhesion . Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity).
PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated; gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation; this may be required for calcium binding . According to a more recent report, does not contain vitamin K-dependent gamma-carboxyglutamate residues .
Sequence Mass (Da): 93314
Sequence Length: 836
Subcellular Location: Golgi apparatus
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Q9SA05 | MAGRVESSIGGGEIDEEGDERGSMWDLDQSLDQPMDEEAGRLRNMYREKKFSAFLLLQLSFQSLGVVYGDLGTSPLYVFYNTFPRGIKDPEDIIGALSLIIYSLTLIPLLKYVFVVCKANDNGQGGTFALYSLLCRHAKVSTIPNQHRTDEELTTYSRTTFHERSFAAKTKRWLENGTSRKNALLILVLVGTCMVIGDGILTPAISVLSAAGGLRVNLPHINNGIVVVVAVVILVSLFSVQHYGTDRVGWLFAPIVFLWFLFIASIGMFNIWKHDPSVLKAFSPVYIFRYFKRGGQDRWTSLGGIMLSITGIEALFADLSHFPVSAVQFAFTVIVFPCLLLAYSGQAAYLRKYPHHVEDAFYQSIPKRVYWPMFIIATAAAIVASQATISATFSLIKQALAHGCFPRVKVVHTSRKFLGQIYVPDINWILMILCIAVTAGFKNQNQIGNAYGTAVVIVMLVTTLLMMLIMILVWRCHWVLVLLFTLLSLVVECTYFSAVLFKVNQGGWVPLVIAAAFLVIMYVWHYGTLKRYEFEMHSKVSMAWILGLGPSLGLVRVPGIGLVYTELASGVPHIFSHFITNLPATHSVVIFVCVKNLPVYTVPQEERFLVKRIGPKNFHMFRCVARYGYRDLHKKDDDFEKRLFESLFLFLRLESMMEGCSDSEDYSVCGSQQRQSRDGVNGNGNEIRNVSTFDTFDSIESVIAPTTTKRTSHTVTGSSQMSGGGDEVEFINGCRDAGVVHIMGNTVVRARREARFYKRIAIDYVYAFLRKICRENSAIFNVPQESLLNVGQIFYV | Function: Putative potassium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89220
Sequence Length: 796
Subcellular Location: Cell membrane
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O64769 | MAARVEAATMGGEIDEEESDERGSMWDLDQKLDQSMDEEAGRLRNMYREKKFSALLLLQLSFQSLGVVYGDLGTSPLYVFYNTFPHGIKDPEDIIGALSLIIYSLTLIPLLKYVFVVCKANDNGQGGTFALYSLLCRHAKVKTIQNQHRTDEELTTYSRTTFHEHSFAAKTKRWLEKRTSRKTALLILVLVGTCMVIGDGILTPAISVLSAAGGLRVNLPHISNGVVVFVAVVILVSLFSVQHYGTDRVGWLFAPIVFLWFLSIASIGMYNIWKHDTSVLKAFSPVYIYRYFKRGGRDRWTSLGGIMLSITGIEALFADLSHFPVSAVQIAFTVIVFPCLLLAYSGQAAYIRRYPDHVADAFYRSIPGSVYWPMFIIATAAAIVASQATISATFSLVKQALAHGCFPRVKVVHTSRKFLGQIYVPDINWILMILCIAVTAGFKNQSQIGNAYGTAVVIVMLVTTLLMTLIMILVWRCHWVLVLIFTVLSLVVECTYFSAMLFKIDQGGWVPLVIAAAFLLIMWVWHYGTLKRYEFEMHCRVSMAWILGLGPSLGLVRVPGVGLVYTELASGVPHIFSHFITNLPAIHSVVVFVCVKNLPVYTVPEEERFLVKRIGPKNFHMFRCVARYGYRDLHKKDDDFEKRLFESLFLYVRLESMMEGGCSDSDDYSICGSQQQLKDTLGNGNENENLATFDTFDSIESITPVKRVSNTVTASSQMSGVDELEFINGCRDAGVVHIMGNTVVRARREARFYKKIAIDYVYAFLRKICREHSVIYNVPQESLLNVGQIFYV | Function: Probable potassium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88966
Sequence Length: 792
Subcellular Location: Cell membrane
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O80739 | MEEIEEGSSNNSIRRVGTGSSDRRWVDGSEVDSETPLFSEIRDRDYSFGNLRRRLMKKPKRADSLDVEAMEIAGSHGHNLKDLSLLTTLGIAFQTLGVVYGDMGTSPLYVFSDVFSKVPIRSEVDVLGALSLVIYTIAVIPLAKYVFVVLKANDNGEGGTFALYSLICRYAKVNKLPNQQPADEQISSFRLKLPTPELERALGIKEALETKGYLKTLLLLLVLMGTSMIIGDGILTPAMSVMSAMSGLQGEVKGFGTNALVMSSIVILVALFSIQRFGTGKVGFLFAPVLALWFFSLGAIGIYNLLKYDFTVIRALNPFYIVLFFNKNSKQAWSALGGCVLCITGAEAMFADLGHFSVRSIQMAFTCVVFPCLLLAYMGQAAYLTKHPEASARIFYDSVPKSLFWPVFVIATLAAMIASQAMISATFSCVKQAMALGCFPRLKIIHTSKKRIGQIYIPVINWFLMIMCILVVSIFRSTTHIANAYGIAEVGVMMVSTVLVTLVMLLIWQTNIFLALCFPLIFGSVETIYLLAVLTKILEGGWVPLVFATFFLTVMYIWNYGSVLKYQSEVRERISMDFMRELGSTLGTIRIPGIGLLYNELVQGIPSIFGQFLLTLPAIHSTIIFVCIKYVPVPVVPQEERFLFRRVCPKDYHMFRCIARYGYKDVRKEDSRVFEQLLIESLEKFLRCEALEDALESTLNDFDPDRVSVASDTYTDDLMAPLIHRAKRSEPEQELDSEVLPSSSVGSSMEEDPALEYELAALREATDSGLTYLLAHGDVRAKKNSIFVKKLVINYFYAFLRRNCRAGAANLTVPHMNILQAGMTYMV | Function: Putative potassium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92088
Sequence Length: 827
Subcellular Location: Cell membrane
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O18734 | MAAQRLGKRVLSKLQSPSRARGPGGSPGGLQKRHARVTVKYDRRELQRRLDVEKWIDGRLEELYRGREADMPDEVNIDELLELESEEERSRKIQGLLKSCTNPTENFVQELLVKLRGLHKQPGLRQPSPSGDGSLSPRQDRARTAPP | Function: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.
PTM: Phosphorylation of Thr-38 induces a conformation change.
Sequence Mass (Da): 16672
Sequence Length: 147
Subcellular Location: Cytoplasm
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Q96C90 | MADSGTAGGAALAAPAPGPGSGGPGPRVYFQSPPGAAGEGPGGADDEGPVRRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPELEIDVDELLDMESDDARAARVKELLVDCYKPTEAFISGLLDKIRGMQKLSTPQKK | Function: Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated (By similarity).
PTM: Phosphorylated primarily on Thr-57 by PKC (in vitro). An unknown Ser is also phosphorylated by PKC (in vitro) (By similarity).
Sequence Mass (Da): 15911
Sequence Length: 147
Subcellular Location: Cytoplasm
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Q62084 | MADSGPAGGAALAAPAPGPGSGSTGPRVYFQSPPGAAGEGPGGADDDGPVRRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPELEIDVDELLDMESDDTRAARVKELLVDCYKPTEAFISGLLDKIRGMQKLSTPQKK | Function: Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated.
PTM: Phosphorylated primarily on Thr-57 by PKC (in vitro). An unknown Ser is also phosphorylated by PKC (in vitro).
Sequence Mass (Da): 15957
Sequence Length: 147
Subcellular Location: Cytoplasm
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Q8MIK9 | MADSGPAGGAALAAPAPGPGSGGAGPRVYFQSPPGAAGEGPGGADDEGPVRRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPELEIDVDELLDMESDDTRAARVKELLVDCYKPTEAFISGLLDKIRGMQKLSTPQKK | Function: Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated (By similarity).
PTM: Phosphorylated primarily on Thr-57 by PKC (in vitro). An unknown Ser is also phosphorylated by PKC (in vitro) (By similarity).
Sequence Mass (Da): 15911
Sequence Length: 147
Subcellular Location: Cytoplasm
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Q8TAE6 | MSVATGSSETAGGASGGGARVFFQSPRGGAGGSPGSSSGSGSSREDSAPVATAAAAGQVQQQQQRRHQQGKVTVKYDRKELRKRLVLEEWIVEQLGQLYGCEEEEMPEVEIDIDDLLDADSDEERASKLQEALVDCYKPTEEFIKELLSRIRGMRKLSPPQKKSV | Function: Inhibitor of the PP1 regulatory subunit PPP1CA.
PTM: Has over 600-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction (By similarity). The main inhibitory site appears to be Thr-73.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17843
Sequence Length: 165
Subcellular Location: Cytoplasm
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Q8R4R9 | MSVVTGGGEAAGGTSGGGARVFFQSPRGGTGGSRESSSHSGSSREDSAPVATVAAAGQVQQQQRRHQQGKVTVKYDRKELRKRLVLEEWIVEQLGQLYGCEEEEMPDVEIDIDDLLDADSEEERASKLQEALVDCYKPTEEFIRELLSRIRGMRKLSPPQKKSV | Function: Inhibitor of the PP1 regulatory subunit PPP1CA.
PTM: Has over 600-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. The main inhibitory site appears to be Thr-72 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17980
Sequence Length: 164
Subcellular Location: Endomembrane system
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Q9NXH3 | MLSSSPASCTSPSPDGENPCKKVHWASGRRRTSSTDSESKSHPDSSKIPRSRRPSRLTVKYDRGQLQRWLEMEQWVDAQVQELFQDQATPSEPEIDLEALMDLSTEEQKTQLEAILGNCPRPTEAFISELLSQLKKLRRLSRPQK | Function: Inhibitor of PPP1CA. Has inhibitory activity only when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.
PTM: Phosphorylated on several residues.
Sequence Mass (Da): 16508
Sequence Length: 145
Subcellular Location: Cytoplasm
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Q7TT52 | MLSSSPASCTSPSPGTDNPDKKVHWASEKRRRASSTDSESKTHLDISKLPRSRRPSRLTVKYDRGHLQRWLEMEQWVDAQVQELFQGQEESSEPEIDLEALMDLSTEDQRTQLEAILQDCPGNREPFISELLSQLKRLRRLSRPSK | Function: Inhibitor of PPP1CA. Has inhibitory activity only when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction (By similarity).
PTM: Phosphorylated on several residues.
Sequence Mass (Da): 16817
Sequence Length: 146
Subcellular Location: Cytoplasm
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P06726 | MSQASSSPGEGPSSEAAAISEAEAASGSFGRLHCQVLRLITNVEGGSLEAGRLRLLDLRTNIEVSRPSVLCCFQENKSPHDTVDLTDLNIKGRCVVGEQDRLLVDLNNFGPRRLTPGSENNTVSVLAFALPLDRVPVSGLHLFQSQRRGGEENRPRMEARAIIRRTAHHWAVRLTVTPNWRRRTDSSLEAGQIFVSQFAFRAGAIPLTLVDALEQLACSDPNTYIHKTETDERGQWIMLFLHHDSPHPPTSVFLHFSVYTHRAEVVARHNPYPHLRRLPDNGFQLLIPKSFTLTRIHPEYIVQIQNAFETNQTHDTIFFPENIPGVSIEAGPLPDRVRITLRVTLTGDQAVHLEHRQPLGRIHFFRRGFWTLTPGKPDKIKRPQVQLRAGLFPRSNVMRGAVSEFLPQSPGLPPTEEEEEEEEEDDEDDLSSTPTPTPLSEAMFAGFEEASGDEDSDTQAGLSPALILTGQRRRSGNNGALTLVIPSWHVFASLDDLVPLTVSVQHAALRPTSYLRSDMDGDVRTAADISSTLRSVPAPRPSPISTASTSSTPRSRPRI | Function: Stimulates viral immediate-early (IE) transcription. Plays a role in the inhibition of the host innate repsonse by targeting STING1 and thus the cGAS-STING pathway . Counteracts also host DAXX-mediated repression of viral transcription. Displaces a DAXX-binding protein, ATRX, from nuclear domain 10 sites (ND10) shortly after infection . Increases the basal level of SUMOylated DAXX in infected cells . Stimulates quiescent cells to re-enter the cell cycle, proceed through G1 and enter the S phase . Interacts with hypophosphorylated forms of RB1 and induces their degradation by the proteasome without involving ubiquitin conjugation .
PTM: S-nitrosylation limits ability to undermine the cGAS/STING antiviral pathway.
Sequence Mass (Da): 61949
Sequence Length: 559
Subcellular Location: Virion tegument
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O48840 | MVVKYTMSMSFFVIFASTVTIIVHGFPSTLDGPLNPVTAPLDPNLNPIAFDLPESDPSFVKPISEFLLPEQISVSLSYSFDSVWISWVTGEYQIGEKDSAPLDPNCVQSIVQYREFDVRRTRKQNATGHSIVYNQQYSSENGFMNYTSGIIHHVQLTGLKPNTLYRYQCGDPSLSAMSKEYYFRTMPKSTSENYPHRIVVAGDLGLTYNTSTVLGHILSNHPDLVVLLGGFSYADTYLANKTKLDCSSCHCDQNGTSSDCGSCYSSGETYQPRWDYWGRFMEPLTANVPTMMVAGEHEIEPQTENNLTFAAYSSRFAFPSNESGSFSPLYYSFNAGGAHFIVLNSYTLYDNSSDQYIWLESDLIKINRSETPWVVATWSLPWYSTFKGHYREAESMRIHLEDLLYNYRVDIVFNSHVDAYERSNRVYNYTLDQCGPVYITTGAGGAGKLETQHVDDPGNIPDPSQNYSCRSSGLNSTLEPVKDETCPVKQPEYSAYRESSFGFGILEVKNETHALWSWNRNQDLYYLAADVIHIVRQPEMCSVCN | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 61543
Sequence Length: 545
Subcellular Location: Secreted
EC: 3.1.3.2
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P35482 | MFKRSLIAASLSVAALVSAQAMAVTGGGASLPAELYKGSADSILPANFSYAVTGSGTGKNAFLTNNSSLFGTTGTVHYAGSDSVLSGSELTTYNSNYNGTYGPLIQIPSVATSVTVPYRKDGNTTLNLTSAQLCDAFSGAKTTWGQLLGTTDSTPIRIVYRTGSSGTTELFTRHLNSICPTRFATNSTFTNARLPAGGTLPSNWVGVAATSTVVSTVKATNGSLGYVSPDAVNINSNAEVSRVNGNLPTQANVSTALGSVAPPANAADRADPSKWVPVFTNPSAGYSIVGYTNFVFGQCYKDASVSTDVRAFINKHYGGTTTNAAVAAHGFIPLTPAWKSAIVSAFYTGTSENLAIGNTNVCNTKGRP | Function: Has both a phosphomonoesterase and phosphodiesterase activity.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 37885
Sequence Length: 368
Subcellular Location: Secreted
EC: 3.1.3.1
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K4LAH1 | MYKRSLIAASLSVAALVSAQAMAEINGGGATLPQQLYQEPGVLTAGFAAYIGAGSGNGKAAFLNNDYTKFVAGTTNKNVHWAGSDSKLSKTNETNPYLSAHGSAWGPLIQVPSVATSVALPFNKSGSNAVNFADVNTLCGVFSGRLTDWSQIPGSGRSGAITVAYRSESSGTTELFTRFLNASCSSALEGGTFAITTSFGNSFSGGLPAGAVSAQGSQAVMNTLNAAEGRITYMSPDFAAPTLAGLDDATKVAQVRGVSPAPANVSAAIGAVTPPTTAQRSDPNNWVPVFAATASATDPSVRPYPTTGYPILGFTNLIFSQCYADATQTQQVRDFFTRHYGASVNNDTAITNHRFVPLPASWKLAVRQSFLTSTNNLYIGHSNVCNGIGRPL | Function: Has both a phosphomonoesterase and phosphodiesterase activity.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 40663
Sequence Length: 392
Subcellular Location: Secreted
EC: 3.1.3.1
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Q92058 | MKAFLLTLLAQLCSASLVPEREKDPEYWRQQAQETLRDALRLQHLNQNVAKNLILFLGDGMGVSTVTAARILKGQLQHRKGEESLLEMDKFPYVALAKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAGVTRDRCNTTKGQEVTSILRWAKDEGKAVGIVTTTRVTHATPSAAYAHSANRDWYSDGEMPLDALEGGCKDIARQLVDNIPDIEVILGGGRKYMFPKNTSDVEYPQEERHRGTRLDGKDLVQAWHDTKPAGKVAKYVWHRRELLALNVSRVDFLLGLFEPGDMVYELDRNNETDPSLSEMVAVAIRMLQKNPRGFFLLVEGGRIDHGHHEGKAKQALHEAVELDRAVGLAGRLTSPRDTLSVVTADHSHVFTFGGYTPRGNPIFGLAPMQSDVDRKPFTSILYGNGPGYKIVGGERENVSAVDFAHANYQAQAAVPLRQETHGGEDVAVFARGPMAHLLHGVDEQNYIPHAMAYAACIGPNRAHCSSAARPAATATLLPVLLLLLLLC | Cofactor: Binds 1 Mg(2+) ion.
Function: Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis (By similarity). Has broad substrate specificity and can hydrolyze a considerable variety of compounds: however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi) and pyridoxal 5'-phosphate (PLP) are natural substrates (By similarity). Plays an essential role in skeletal and dental mineralization via its ability to hydrolyze extracellular diphosphate, a potent mineralization inhibitor, to phosphate: it thereby promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration (By similarity). Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, in order to provide a sufficient amount of PLP in the brain, an essential cofactor for enzymes catalyzing the synthesis of diverse neurotransmitters (By similarity). Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (By similarity). Involved in the establishment and growth of feather germs .
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 56760
Sequence Length: 519
Domain: Calcium-binding is structural and does not influence the alkaline phosphatase activity. At very high concentrations, calcium can however substitute for zinc at zinc-binding sites, leading to strongly reduced enzyme activity.
Subcellular Location: Cell membrane
EC: 3.1.3.1
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P05186 | MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF | Cofactor: Binds 1 Mg(2+) ion.
Function: Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis . Has broad substrate specificity and can hydrolyze a considerable variety of compounds: however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi), pyridoxal 5'-phosphate (PLP) and N-phosphocreatine are natural substrates . Plays an essential role in skeletal and dental mineralization via its ability to hydrolyze extracellular diphosphate, a potent mineralization inhibitor, to phosphate: it thereby promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration . Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix (By similarity). Also promotes dephosphorylation of osteopontin (SSP1), an inhibitor of hydroxyapatite crystallization in its phosphorylated state; it is however unclear whether ALPL/TNAP mediates SSP1 dephosphorylation via a direct or indirect manner (By similarity). Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, in order to provide a sufficient amount of PLP in the brain, an essential cofactor for enzymes catalyzing the synthesis of diverse neurotransmitters . Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (By similarity). Also capable of dephosphorylating microbial products, such as lipopolysaccharides (LPS) as well as other phosphorylated small-molecules, such as poly-inosine:cytosine (poly I:C) . Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating hydrolysis of N-phosphocreatine to initiate a futile cycle of creatine dephosphorylation and phosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity).
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 57305
Sequence Length: 524
Domain: Calcium-binding is structural and does not influence the alkaline phosphatase activity . At very high concentrations, calcium can however substitute for zinc at zinc-binding sites, leading to strongly reduced enzyme activity .
Subcellular Location: Cell membrane
EC: 3.1.3.1
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P29523 | MSTWWLVVVAAAAAAGLVRAEDRYHPERLAAGEASAATRSAAESEASFWVREAQEAIERREREGAGAKQAAGHAKNVVMFLGDGMSVPTLAAARTLLGQRRGQTGEEASLHFEQFPTLGLAKTYCVNAQVPDSSCTATAYLCGVKANQGTLGVTAAVPRHDCEASTDVTKRVQSIAEWALADGRDVGIVTTTRITHASPAGTFAKVANRNWENDNDVKQEGHDVNRCPDIAHQLIKMAPGNKFKVIFGGGRREFLPTTQVDEEGTRGLRTDGRNLIEEWQNDKESQKVSYKYLWNRQELLKLGSSPPDYLLGLFEGSHLQYHLEGDESTEPTLAELTDVAIRVLSRNERGFFLFVEGGRIDHAHHDNYAHLALDETIEMDRAVKVATDALKEDESLVVVTADHTHVMSFNGYSPRGTDVLGTVRSLDSNRMPFMVLSYTNGPGARIQQNGVRPDVTTDANFGALRWRTHTDVPLDSETHGGDDVTVFAWGVHHWMFSGLYEQTHVPHRMAWAACMGPGRHVCVSAATVPTAALLSLLLAAFITLRHQCFL | Cofactor: Binds 1 Mg(2+) ion.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 60281
Sequence Length: 550
Subcellular Location: Cell membrane
EC: 3.1.3.1
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