ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8LPF3 | MAQLTNSLNYLFSVSLLLFVSFHCLCFRFSLVAACSNSTDDQQIQHHHHRKWVGPSGHKVITVSLNGHAQFRSVQDAVDSIPKNNNKSITIKIAPGFYREKVVVPATKPYITFKGAGRDVTAIEWHDRASDLGANGQQLRTYQTASVTVYANYFTARNISFTNTAPAPLPGMQGWQAVAFRISGDKAFFSGCGFYGAQDTLCDDAGRHYFKECYIEGSIDFIFGNGRSMYKDCELHSIASRFGSIAAHGRTCPEEKTGFAFVGCRVTGTGPLYVGRAMGQYSRIVYAYTYFDALVAHGGWDDWDHKSNKSKTAFFGVYNC... | 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 degrad... |
O49298 | MDHKILLTPPKSLYTKCIITIIYVVSISHLNAHFITSCKQTPYPSVCDHHMSNSPLKTLDDQTDGFTFHDLVVSSTMDQAVQLHRLVSSLKQHHSLHKHATSALFDCLELYEDTIDQLNHSRRSYGQYSSPHDRQTSLSAAIANQDTCRNGFRDFKLTSSYSKYFPVQFHRNLTKSISNSLAVTKAAAEAEAVAEKYPSTGFTKFSKQRSSAGGGSHRRLLLFSDEKFPSWFPLSDRKLLEDSKTTAKADLVVAKDGSGHYTSIQQAVNAAAKLPRRNQRLVIYVKAGVYRENVVIKKSIKNVMVIGDGIDSTIVTGNRN... | 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 degrad... |
Q9SRX4 | MESPIFILITLSFFLQSVLASSQTLSNSSTICKTTPDPKYCKSVFPHSQGNVQQYGCFSIRKSLSQSRKFIRTVDRYIKRNAHLSQPAVIRALQDCRFLAGLTMDYLLTSFETVNDTSAKTSFKPLSFPKADDIQTLLSAALTNEQTCLEGLTTAASYSATWTVRTGVALPLVNDTKLLGVSLALFTKGWVPKKKKRAGFAWAQPRSGSSTHTKPFRLFRNGALPLKMTEKTKAVYESLSRRKLADGDSNGDGDDGSMVLISDIVTVSQDGTGNFTNITAAVAAAPNNTDGSAGFFLIYVTAGIYEEYISIAKNKRYMMM... | 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 degrad... |
O23038 | MKIISLSISIGIAIIAVLASKTLFKTHPEAFGIKAISYSFKKSLCDHHHHHHHHHHHHHRHKPSDTKRKVSICDDFPKNIPPLDTDTTSYLCVDKNGCCNFTTVQSAVDAVGNFSQRRNVIWINSGMYYEKVVIPKTKPNITLQGQGFDITAIAWNDTAYSANGTFYCATVQVFGSQFVAKNISFMNVAPIPKPGDVGAQAVAIRIAGDESAFVGCGFFGAQDTLHDDRGRHYFKDCYIQGSIDFIFGNAKSLYQDCRIISMANQLSPGSKAVNGAVTANGRSSKDENSGFSFVNCTIGGTGHVWLGRAWRPYSRVVFVS... | 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 degrad... |
P0C1A9 | MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNP... | 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-dehyd... |
Q5B7U0 | MRVQSYLSLFSLVGAALCAPREHFKRTARTSAPAGCLTVGGSGTYSTIGAAFAALGSSSSEACIYISAGTYKEQLTFQYAGPLTLYGETTDTSSYKKNTVTITHTISSPEAGSLVASATVNAAMDNFTMYNINVVNGYGKGAQAVALAASGERQGYYGCQFLGYQDTLYARVGVQYYSNCYIEGAVDYIFGDASAWFGECDIVSNGAGYITAMSRETASDPAWYCFDHCNIYGKSGLDLTGDVYLGRPWRVLARVIYQNSELSDIINAAGWTTMAEGATPLYYEIGNTGDGADTSKRLYLSEISAAVTKATVLGSDWTDW... | 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 degrad... |
A1DBT4 | MHLPSLVLGLLGLGLTASASPIEERSNRSKAPDGCLTVGSSGKYSTIGAALDALGDSKSDACIFIGAGTYKEQITIDYKGKLTMYGETTDTSSYKKNQVTITHTISSPQAGTLDKSATVNVRSDGFKMYNINVINGYGKGSQAVALVANADKLGFYGCSFVGYQDTLYAKAGRQYYSNCYIEGATDYIFGNASAWFGECDIMSVGPGYITAMSRTTADQTTWYAIDNCNIYGKPGVDLTAKVYLGRPWRVLARVIYQNSQLSNIINPKGWTTMAEGATPLYYEYNNKGAGADTSKREYESSISGAVSMNTVLGSGWNSWI... | 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-glu... |
Q47474 | MSLTHYSGLAAAVSMSLILTACGGQTPNSARFQPVFPGTVSRPVLSAQEAGRFTPQHYFAHGGEYAKPVADGWTPTPIDTSRVTAAYVVGPRAGVAGATHTSIQQAVNAALRQHPGQTRVYIKLLPGTYTGTVYVPEGAPPLTLFGAGDRPEQVVVSLALDSMMSPADYRARVNPHGQYQPADPAWYMYNACATKAGATINTTCSAVMWSQSNDFQLKNLTVVNALLDTVDSGTHQAVALRTDGDRVQLENVRLLSRQDTFFVNTSDRQNSYVTDHYSRAYIKDSYIEGDVDYVFGRATAVFDRVRFHTVSSRGSKEAYV... | 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:... |
Q7SDD5 | MIQPLVKASRPRLWVCSDCLLRRTLSPLLRQQRRRFTGFTAHAPKTLTGTIPVTHKNGDTKHDDSLLRSIFDSPETWKQFSGDKHGRNVGLFRNAYLTSPHGFLDFAHVSLGKARALVDKVLNAQSLDEYRAIVRHLDRLSDILCRVLDMADFVRVTHPDQQIQRTASMAWDMMYEYMNQLNTMTGLYDQLVQAMDNPQVSTTWSEEERMVAEVLKLDFAKSAVHLPKDARDKFVHLSSAISQTGTNFIQHMEPKIPYTTVEKSRMMGMDPVEVKRMASMGKVYVQTLSPQASIALRTVRDDHARHQLFMASRTASRRTV... | 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 b... |
Q0TXL7 | MLKRLARNNSSPWICSRCLQQSQRQRRFNSTFAATATARDHAPSALYGLSASGKTDDDALRKVFDNASFWESFKRGTSNKKPSGIIGNKYLTHPDGFIDFVTVTIQRCNGVVEKVSRAETIEDFKYMVKDLDKLSDLLCRVIDLADFVRSTHPNRQFQIMAVKAYHTVFQYMNQLNTTPVLYDQLKKASDIPEVFESWTEEERIVARILMEDFARFGIGLDDATRQKLVDLSGEIAEVGSQFVEGMSPETPTLKFESKRLKGLDPNLAKALTKWGETRISTMHHEAQAVLRFVDDAEVRRETYSAVRTAGSSTIARLEKM... | 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 b... |
P37932 | MIARPARDVLSSATKKQFRFRGCLAARHEPYHTSTSRAGQVAILPATTDDKTLVSVFDSPRSNAKLSAFATTGLFNHSTVTHPRALNSIAQGTLIRAHVLTNRILRAKESREELFKVVKNLDRLSDMLCSVIDLCELVRNSHPDRAWVEAANDAYEGLCQTMNELNTHVGLYDVLKIVLSDPEIVKSLSPEAYRTAMIFWNDFEKSAINLPAKEREEFVALSSEIISLGRMFLEETTAARPPAKIPPSDLAGLKDKGMGVRLQLQAQFTQRDLHVYPGSLQAQMIMRSAPAEEARRRVYIASHSSTPEQIELLERMLSTR... | 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 b... |
Q10415 | MQVRTLLTLGKKKVIGNRQCILSLYRKYSNVQSRKAEDQLLRQIFDDQNIAVNQITKRNGIQGVGLFRNHFLSDKDTGFLRLAETASEKCKAVIEDLLLEDTEDGSIVVSKFDRISNLLCSVIDLFEFVRCAHPDKMVVMKAEEAYSYLFELMNTLNTHQGLYEKLKCSLQQTPTLKDTDPEAYTVGRVFLQDFEKSGVNLESSKRNSFVKKSSESATLGRAFFNNSMNRPQRYLTISKQRLAGSDPYFVRSLSKNDKNFIMIPTVGYEGTQALISVANPDVRKEIYMEGHKGTVEEVELLNSYLRSKAEVAKLVGKSSF... | 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 b... |
Q9I3Y3 | MNSPALPLSRGLRIRAELKELLTLAAPIMIAQLATTAMGFVDAVMAGRASPHDLAAVALGNSIWIPMFLLMTGTLLATTAKVAQRHGAGDQPGTGPLVRQALWLALLIGPLSGAVLWWLSEPILGLMKVRPELIGPSLLYLKGIALGFPAAALYHVLRCYTNGLGRTRPSMVLGIGGLLLNIPINYALIYGHFGMPKMGGPGCGWATGSVMWFMFLGMLFWVNKASIYRASQLFSRWEWPDRATIGPLVAVGLPIGIAVFAESSIFSVIALLIGGLDENVVAGHQIALNFSALVFMIPYSLGMAVTVRVGHNLGAGLPRD... | 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:... |
P58120 | MNRTKTVNWKRNLFITWIGCFFVGSSFSLVMPFLPLYIQGLGVSGGNVELYSGLAFSLPALASGLVAPIWGRLADEHGRKVMMVRASIVMTLTMGGIAFAPNVWWLLGLRLLMGFFSGYIPNSTAMIASQAPKDKSGYALGTLATAMVSGTLIGPSLGGLLAEWFGMANVFLIVGALLALATLLTIFFVHENFEPIAKGEMLSSKEIINKVSNKQILFGLLVTTFIIQITSQSIEPFVTLYIKTLTTSTNNLMFISGLIVSAVGLSAMLSSSFLGRLGDKYGSHRLILIGLVFTFIIYLPMAFVQSPLQLGILRFLLGFG... | Function: Efflux pump for various substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43859
Sequence Length: 405
Subcellular Location: Cell membrane
|
P0A4K4 | MTEINWKDNLRIAWFGNFLTGASISLVVPFMPIFVENLGVGSQQVAFYAGLAISVSAISAALFSPIWGILADKYGRKPMMIRAGLAMTITMGGLAFVPNIYWLIFLRLLNGVFAGFVPNATALIASQVPKEKSGSALGTLSTGVVAGTLTGPFIGGFIAELFGIRTVFLLVGSFLFLAAILTICFIKEDFQPVAKEKAIPTKELFTSVKYPYLLLNLFLTSFVIQFSAQSIGPILALYVRDLGQTENLLFVSGLIVSSMGFSSMMSAGVMGKLGDKVGNHRLLVVAQFYSVIIYLLCANASSPLQLGLYRFLFGLGTGAL... | Function: Efflux pump for various substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42840
Sequence Length: 399
Subcellular Location: Cell membrane
|
Q9HV31 | MSRAAVPSVRRRLLVNLLVGFVLCWLSVAALTYHLSLKQVNRLFDDDMVDFGEAALRLLDLATEDQAGEDGSITEIIERSREAIQGLPLLRRESALGYALWRDGQPLLSSLNLPPEITAQGPGFSTVEAQGTHWRVLQLNIDGFQIWISENLIYRQHTMNLLLFYSLFPLLLALPLLGGLVWFGVARGLAPLREVQAEVQQRSARHLQPIAVEAVPLEIRGLIDELNLLLERLRTALEAERRLTSDAAHEIRTPLASLRTHAQVALRSEDPKAHARGLLQVSRSVERISTLMEQILLLARLDGDALLEQFHPVNLATLAE... | 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 membr... |
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 | MAAEQDPEARAAARPLLTDLYQATMALGYWRAGRARDAAEFELFFRRCPFGGAFALAAGLRDCVRFLRAFRLRDADVQFLASVLPPDTDPAFFEHLRALDCSEVTVRALPEGSLAFPGVPLLQVSGPLLVVQLLETPLLCLVSYASLVATNAARLRLIAGPEKRLLEMGLRRAQGPDGGLTASTYSYLGGFDSSSNVLAGQLRGVPVAGTLAHSFVTSFSGSEVPPDPMLAPAAGEGPGVDLAAKAQVWLEQVCAHLGLGVQEPHPGERAAFVAYALAFPRAFQGLLDTYSVWRSGLPNFLAVALALGELGYRAVGVRLD... | 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 .
PT... |
Q8TMW6 | MIKSILDNDLYKFTMQMAVLELFPKAEAEYRFTNRGSHHFSEEFVEKLRRVIDEDISALMLTEDEYQWLGENCSFLKPMYLEYLKNFRFKPGEVEVCLTEEKELDIRIKGPWHSTILWEIVLMAAVSELYFTTIEKEWNGKEWDGNISATSESILTAYGEKILEIGKILEENGCLFAEFGTRRRRSFELHDQVMKTLLQIETLTGTSNVFFAKKYGLKPIGTVGHEWIMGTSALIGLRYANRFAFENWVEVYKGDLGIALTDTFGSEAFFKDMDLKLSKIYDGFRHDSGDPFTFVDRVIDHYRKMGIDPMKKVIVFSDAL... | 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 ... |
Q8CC86 | MEMELDSEGRMVVRPLLTDLYQATMALGYWRAGRACEAAEFELFFRHCPFGGSFALSAGLQDCMRFLRAFRLRDADVQFLASVLPPDTDPAFFEHLRALDCSGVTVRALPEGSLAFPGVPLLQVSGPLLLVQLLETPLLCLVSYASLVATNAARLRLIAGPDKKLLEMGLRRAQGPDGGFTASIYSYLGGFDSSSNTLAGQLRGVPVAGTLAHSFVTSFSGSEVPPDPMLAPASSEGPTVDLPARVNLWLKRVCLYLGLEEQEPHPGERAAFVAYALAFPRAFQGLLDSYSVRRSGLPNFLAVALALGELGYRAVGVRLD... | 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:... |
Q9JTM8 | MTGIIHSLLDTDLYKFTMLQVVLHQFPQTHSLYEFRCRNASTVYPLADIKEDLEVELDALCQLRFTHDELDYLRSLRFIKSDFVDYLELFQLQRRFVEVGTDDKGRLNIRIEGPMIQAMFFEIFILAIVNELYFRRLETPAVIEEGERRLQAKAARLKEIAAAQNPDEPPFLISDFGTRRRYKLAWQEHVIRTLLEAAPSIVRGTSNVFLAKKLGITPIGTMAHEFLQAFQALDVRLRNFQKAALESWVHEYRGDLGVALTDVVGMDAFLRDFDLYFAKLFDGLRHDSGDPYIWGDKAYAHYQKLKIDSRTKMLTFSDGL... | 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 ... |
Q6D454 | MTLHTSPILHSLLDTDAYKLHMQQAVYHHYYDVDVAAEFRCRGDELLGVYADEIAHQVDLMRFLSLSDDEFTYLSSLPFFQQDYLNWLRNFRFNPQQVSIKNNAGKLDIRITGPWREVILWEVPLLAVISEVVHRHRSPNVTTEQAVAQLSTSLESFRQNSMNVDLSQFKLMDFGTRRRFSGDIQQTIVTALQADFPYLIGTSNYDLARRLGITPVGTQAHEWFQAHQQISPTLANSQRAALQMWLREYPTHLGIALTDCITMDAFLRDFDLPFAEAYQGLRHDSGDPVDWGEKAIAHYQRLNIDPMSKTLVFSDNLNLD... | 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 ... |
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
|
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
|
Q8TCS8 | MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISSGKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLSDIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFTDYEHDKVSRDEAVNKIRLDT... | 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) com... |
Q8K1R3 | MAACRLCCLCPCLRPLGCGPLGRPGRNRALSYLQMRALWSSTGSRAVTVDLGHRKLEISSGKLARFADGCAVIQSGDTAVMVTAVSKTKASPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGSSDREVLTSRVIDRSIRPLFPAGYFYDTQVLCNLLAVDGINEPDILAVNGASVALSLSDIPWNGPVGAVRIGMIDGECVVNPTRREMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKEIGVAKRTPQKIFTPSAEIVKYTKIIAMEKLYAVFTDYEHDKVSRDEAVNKIRLDT... | 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) com... |
A3DCH7 | MYKTFSMELAGRTLTIETGKLAQLANGSVLVRYGDTVVLSTATASATPREGVDFFPLSVDYEERLYAVGKIPGGFIKREGKPSEKAILTARVIDRPLRPLFPKDLRNDVAIVNTVLSVDQDNSPELAALLGSSIAVSISDIPFNGPVGAVILGLIDGEVIINPTEKQKEISQMYVTLAGTRNKIVMIEAGANEVPDEVMLDAIKKGHEEIKKIVDFIDGIVKEVGKPKFEYESAEVPEEIFNAVREYAYDKMREAVLAVDKQVRDKNIDDLTKEITEHFAEVFPEMEPAIKEAIYKLEKKVVREYILEEGRRVDGRRLDE... | 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.... |
A5EXU0 | MKHSVSFTYGQHQVTLETGEIARQADGAVIVNMDDTIVLVTVVANKTVAEGQDFFPLTVDYQEKNYAAGKIPGGFFKREGRPSEEETLISRLIDRPIRPLFADGFLNEVQIIATVLSYNPEVSPDIPSIIGASAALKLSGLPFNGPIAAARVGYVNDAYVLNPSPKALKNSRLDLVVAGTESAVLMVESEADQLSEAVMLEAVMFGHRQQQVVIKSINELAAQAAKPAWAWQSPARDEQLDTEVKNHFEERLVAAYQIAHKQTRQETVAQIHADAVALLGIQNNAHGWEETLVNEYVHHLAYRIVRDRILKKQPRIDGRD... | 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.... |
B8E2S5 | MRQTYSFKKDFAGKTLKIDIGKVAWQATGAALVQYGETTVLVTVVASEEKKEDVDFFPLTVEYVERLYAAGKIPGGFFKREGKPTEPEILFARLIDRPLRPLFSKDFRNEVQVIVTVLSYDHENSTDIPSIIGASCAIMLAGLPFKGPIGAVRVGWDGKEWYINPSVALSNSLLLDLVVAGTKDAVLMIEGDGKEVPEEIFLEGIIRAHEQIGEVINFQEEILSMVNPVPFNYEPFVVNENLKKDVLEYVTVDQIRDAIFTPSKSERQKALEDLKKRVIEHFKPIYGEITAQIDEIINQEAKAILTKVILEEKRRVDGRR... | 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.... |
B4RC48 | MFDIKRKTIEWGGKTLTLETGRMARQADGAVLATYGETMVLATAVFAKSPKPGQDFFPLTVNYQEKFYAAGKIPGSFPRREGAPSQKETLTSRLIDRPIRPLFVKGFKNEVQVICTVLAHDLENDPDIVAMVAASAALVLSGVPFMGPIAAARVGYVNGEYVLNPTLDEMKESAMDLVVAGTAEAVMMVESEIKELTEEQVLGGVTFAHKGMQPVIDAIIELAEHSAKEPFDFQPDDTDEIAAKVKDLIGGDLRAAYQITGKSERHAAIGAAKEKAMTAFAKSEANPEGYDANKLGGVFKEIEADIVRRSILETGKRIDG... | 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.... |
P41121 | MLNPIVRKFQYGQHTVTIETGMMARQATAAVMVNMDDTAVFVTVVGQKKVKAGQDFFPLTVNYQERTYAAGRIPGSFFRREGRPGEGETLVARLIDRPLRPLFPEGFLNEVRIVATVVSVNPQINPDIVAMIGASAALALSGIPFNGPIGAARVGYINDQYVLNPTSDELKNSRLDLVVSGTAGAVLMVESEADLLTEEQMLGAVVFGHDQQQVVIDNINALAAEAGKEKWDWVPEPVNQALHDRVAELAESRLGDAYRITEKQERYAQVDAIKDEVTAALLEQDETLEEAEIHEILGSLEKNVVRSRVLSGEPRIDGRE... | 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.... |
B3QZG1 | MDLNTKNNNKKVFEIIFENNVLRIEIGEISRQANGSVMLFYKDTVILSVAVCGDKKNSLNFLPLTVNYQEKLYAAGKIPGGFLRREGKPSDQEILCSRLIDRTIRPLFSKNFKNEVQLINMVLSSDPDGNNENIALLGSSLALLISDIPFFEPVSSVCVGKIGDNLIINPTLSQRENSSFFLILAGTKDSLNMVEMSSKEISENNFLESIKFGHEIIKKLCLFQTEIANQIGKTKIKIPLHNVNNLLEVEIKDKYFSEIEMILKNKCNVNNVKKSDILKKLKENVLENYKEKFLNNKKDNFNLLDLENQKLYLNEVEIIF... | 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.... |
B2RIW6 | MLNVVSKTIDLGDGRSIKIETGKLAKQADGAVTVTMGNTVLLATVCAAKDANPGCDFMPLQVEYKEKYSAIGRFPGGFTRREGKASDYEILTCRLVDRALRPLFPDNYHAEVFVNVILFSADGEDMPDALAGLAASAALAVSDIPFNGPISEVRVARVDGRYIVNPTFEQLERADIDLMVGATMDNIMMVEGEMDEVQESEMLEGIRVAHEAIKVQCKAQLELSEAVGKLQKREYSHEVNDEDLRKKVHDECYARAYEVATSGTGKHERGEAFEKIVEEFKAQYTEEELAEKAEMIARYYHDVEKEAMRRAILDEGKRLD... | 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.... |
B4S5G5 | MSMFIRKEIDLGSGKTLSIETGKMAKQADGSAIVRLNDTMVLATVVSSKTPPSPNQSFFPLQVEYREKYSAAGKFPGGFFKREGRPSEKEILSARLIDRALRPLFPDGYYQDTQIIISVISSDQINDADVLGGVAASAAIMVSDIPFQNSMSEVRVGRVNGEYIVNPNINELRDSDIDISIGGTENTICMLEGEMDEISEAEMLEAIRFGHEAIKKICALQNEIAAEVGKTARTFSAAKAPDNLRQSIAEICSNELKELAYMPLCKEERAEKTAEIYKNAKAQTLQRYQQEITPEVIAAEPEKALYLNEQIIGDAIHSIE... | 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.... |
Q49X62 | MSQEKKVFKTEWANRSLTIETGQLAKQANGAVLVRYGDTVVLSTAVASKEPRDGDFFPLMVNYEEKMYAAGKIPGGFKKREGRPSDEATLTARLIDRPIRPLFPKGYKYDVQIMNTVLSADPDCSPEMAAMIGSSMALSVSDIPFQGPIAGVKVGYIDGEYVINPTVAQKEVSRLDLEVAGHKDAVNMVEAGASEITESEMLEAIFFGHSEIQRLVNFQQEIVDHIQPKKKAFVPVEKDEVLVEKVKQLTQENGLKDAVLTFDKQQRDINLDALKEKVAAEFIDEEDADNEVLIKEVNSILNDLVKEEVRRLIAEEKIRP... | 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.... |
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 | MNSPRSNAVNGGSGGAISALPSTLAQLALRDKQQAASASASSATNGSSGSESLVGVGGRPPNQPPSVPVAASGKLDTSGGGASNGDSNKLTHDLQEKEHQQAQKPQKPPLPVRQKPMEIAGYVGFANLPNQVYRKAVKRGFEFTLMVVGASGLGKSTLINSMFLSDIYNAEQYPGPSLRKKKTVAVEATKVMLKENGVNLTLTVVDTPGFGDAVDNSNCWVPILEYVDSKYEEYLTAESRVYRKTISDSRVHCCLYFIAPSGHGLLPLDIACMQSLSDKVNLVPVIAKADTMTPDEVHLFKKQILNEIAQHKIKIYDFPA... | 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 prot... |
Q01860 | MAGHLASDFAFSPPPGGGGDGPGGPEPGWVDPRTWLSFQGPPGGPGIGPGVGPGSEVWGIPPCPPPYEFCGGMAYCGPQVGVGLVPQGGLETSQPEGEAGVGVESNSDGASPEPCTVTPGAVKLEKEKLEQNPEESQDIKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSFKNMCKLRPLLQKWVEEADNNENLQEICKAETLVQARKRKRTSIENRVRGNLENLFLQCPKPTLQQISHIAQQLGLEKDVVRVWFCNRRQKGKRSSSDYAQREDFEAAGSPFSGGPVSFPLAPGPHF... | 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 pluripo... |
P20263 | MAGHLASDFAFSPPPGGGDGSAGLEPGWVDPRTWLSFQGPPGGPGIGPGSEVLGISPCPPAYEFCGGMAYCGPQVGLGLVPQVGVETLQPEGQAGARVESNSEGTSSEPCADRPNAVKLEKVEPTPEESQDMKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSLKNMCKLRPLLEKWVEEADNNENLQEICKSETLVQARKRKRTSIENRVRWSLETMFLKCPKPSLQQITHIANQLGLEKDVVRVWFCNRRQKGKRSSIEYSQREEYEATGTPFPGGAVSFPLPPGPHFGTPGYGS... | 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 pluri... |
Q9TSV5 | MAGHLASDFAFSPPPGGGGDGPGGPEPGWVDPRTWLSFQGPPGGSGIGPGVGPGAEVWGLPACPPPYDFCGGMAYCAPQVGVGLVPQGGLETPQPEGEAGAGVESNSEGASPEPCAAPAGAAKLDKEKLEPNPEESQDIKALQKDLEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSFKNMCKLRPLLQKWVEEADNNENLQEICKAETLVQARKRKRTSIENRVRGNLESMFLQCPKPTLQQISHIAQQLGLEKDVVRVWFCNRRQKGKRSSSDYSQREDFEAAGSPFPGGPVSFPLAPGPHF... | 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 pluripo... |
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 | IKKEGLWIPKLEPERVVSILEWDRAAEPEHRLEAICASMIEAWGYDDLLNHIRRFYLWVLDQAPYKQLSAEGKAPYISEVALKSLYTGKPATSCELEVYNKIHQEQHDEFDDSQMKFVFQSDKEKLNVGEQQKSKDKESRQRDQEGENSNRQIIPDRDINAGTTGTFSVPKLKKISGKLSLPKIKGKGLLNLDHLLVYVPNQDDISNNIATQEQLEAWHEGVKNAYEVDDQQMEIICNGLMVWCIENGTSGDLQGEWTMMDGEKQVTFPLKPILDFAKPTLRQIMAHFSQAAESYIEFRNSTEKYMPRYGLQRNLTDYGL... | 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 cle... |
P27913 | MNNQRKKTGRPSFNMLKRARNRVSTGSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWSSFKKNGAIKVLRGFKKEISSMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPTLIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCEDTMTYKCPRITERQPDDVDCWCNATDTWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETWALRHPGFTVIGLFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKNKPT... | 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 nucl... |
P19724 | LVRKSCERLYEGRMGVWNGSLKAELRPAEKVLAKKTRSFTAAPLDTLLGAKVCVDDFNNWFYSKNMECPWTVGMTKFYKGWDEFLRKFPDGWVYCDADGSQFDSSLTPYLLNAVLSIRLWAMEDWDIGEQMLKNLYGEITYTPILTPDGTIVKKFKGNNSGQPSTVVDNTLMVLITMYYALRKAGYDTKTQEDMCVFYINGDDLCIAIHPDHEHVLDSFSRSFAELGLKYDFTQRHRNKQNLWFMSHRGILIDDIYIPKLEPERIVAILEWDKSKLPEHRLEAITAAMIESWGYGDLTHQIRRFYQWVLEQAPFNELAKQ... | 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 cle... |
P21294 | QQQPFATIAQEGKAPYIASMALRKLYMDRAVDEEELRAFTEMMVALDDEFEFDSYEVHHQANDTIDAVGDNKKDAKPEQGSIQSNPNKGKEKDVNAGTSGTHTVPRIKAITPKMRMPKSKGATVLNLEHLLEYAPQQIDISNTRATQSQFDTWYEAVRMAYDIGETEMPTVMNGLMVWCIENGTSPNVNGVWVMMDGNEQVGYPLKPIVENAKPTLRQIMAHFSDVAEAYIEMRNKKEPYMPRYGLIRNLRDVGLARYAFDFYEVTSRTPVRAREAHIQMKAAALKSAQPRLFGLDGGISTQEENTERHTTEDVSPSMHT... | 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 cle... |
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... |
P94544 | MHKKDIIRLLETIAVYMELKGDNPFKVSAFRKAAAALEQDDRSLSEMDDMMSLSGIGKGTYSVIKEYIDEGKSSTLESLQKEVPEGLVPLLKLPGLGGKKIAKLYKELGVHDAESLKEACEQQKVQGLAGFGKKSEEKILQALGEAGKQPERFPIGYALRIAREIEEHLSQFTHIIKFSRAGSLRRARETVKDLDYIIATDHPAEVREQLLELPNIKSVIASGDTKVSVILSFEYETSVDFRLVTEEQFPTTLHHFTGSKDHNIKMRQIAKERGERISEYGVETVETGEIKTFPSEREFYAHFGLPLIPPEIRESGQEVE... | 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 gro... |
Q4V5R4 | MEPKSQDQAPNRDDPDLQTEPLTIAQSITSFYMYNPYEKRSVEVPLTNCDAFISLLKCVIGTGILAMPLAFRCSGFVMGTVMSILLMILLTYSIHLLIADMTECCRRRRVPQVSMPEAVRIAYEEGPKWINCFGRAAGFMTTCVLVFGQFLLCTVYLVFVSKNFKEIGDHYIERYNERYYVLVACLLLLPLFMIRRLKYLVPLNLISNFLLYAGFALIMYYLFNGLPNINDREMVTPPVEWIEFIAIAAFSLTAVGSMLVVEAHMAHPQSYLGLFGVLNLAVLFILLSNMFFGIIGYWRFGDNVHASITLNIPQDEILSQ... | 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 phago... |
Q9BGN0 | MAKLLLLTLLGASLAFVGERLLAFRNSFGAVQELEPVEPQNCVLIEGLENGSEDIDILPSGLAFISSGLKYPGMPNFAPDEPGKIFLIDMNEKNPRAQELEISNGFEKESFNPHGISTFIDKDHTVYLYVVNHPHMKSTVEIFKFEEQQRSLVHLKTIKHELLKSVNNIVVLGPEQFYATRDHYFTNYVLALLEMFLDLHWTSVLFYSPKEVKVVAKGFSSANGITVSLDKKYVYVADATAKNVHVMEKHDNWDLTELKVIHLDTLVDNLSVDPATGDILAGCHPNGMKLLNYNPEDPPGSEVLRIQNVLSEKPRVSTVY... | 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... |
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
... |
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 | MALQLLPSTLSVPKKGSSMGAVAVKDTAAFLGVSSKAKKASLAVRTQVATAPSPVTTSPGSTASSPSGKKTLRQGVVVITGASSGLGLAAAKALAETGKWHVVMACRDFLKASKAAKAAGMADGSYTVMHLDLASLDSVRQFVDAFRRAEMPLDVLVCNAAIYRPTARTPTFTADGHEMSVGVNHLGHFLLARLLMEDLQKSDYPSRRMVIVGSITGNSNTLAGNVPPKASLGDLRGLAGGLSGASGSAMIDGDESFDGAKAYKDSKVCNMLTMQEFHRRYHEETGITFSSLYPGCIATTGLFREHIPLFRTLFPPFQKF... | 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 Locatio... |
B5CY96 | MSYKYIFLLSAFTLGVPPGIYCQGRNEVVVDYNTRRFLSGVSELDRSKYFNIHSTSDDDKDVGKFLADYQVGLGRKFWGPYSYAYNKTHEVGKYPQMKPYSGNISVKRYIATEHPYVQHIQGGIDVQAAGAWSAEYYSNSELVPEFFEPLNEPFVHANDAGFTVQGQAMRELMVDFYASIGKHIHNNPRLNGKMKVIGYAAAYPAWEDGNFNYWNTRMKMFIDRAGAYMDGFSVHLYDGINVTGTDTKRSGSNSEAVLDMVEAYSYIKFGHVKPLAISEFGGIDNSKPDDSYDDISSVRSVSSFNHFLFNLMERQDNLFI... | 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. Inact... |
D7GXG0 | MKKVLLFLIFLVSANLSAQLPSPTNGKKWEKVEQLSDEFNGNSIDTNKWYDYHPFWEGRAPSNFKKGNAFVSDGFLNLRSTLRKEPSSVQDPFKDIWVDAAAAVSKTKAQPGYYYEARFKASSLSMTSSFWFRVGQFSEIDVIEHIGNPSKENRQDDLPYQYHVNTHYYGKHAGLQPLGTEYKMPGRGRDNFYTYGFWWKSPNELLFYFNGKQVMRIVPRVPLDEELRMIFDTEVFPFATAGVANIGLPKPENLRDNSKNTMKVDWVRVYKLVDGTAAEDSSDAPIGSYISLKKTQGDGKFVTGEKDGSQLVARGSTVQS... | 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. Inact... |
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
|
B5CY92 | MRKTVLYLSAASLFLSSYTLKNDKEYSLAEEHIKNLPEAPEGYKWVVNEDYTDEFNGKRLNAAKWHAKSPYWTNGRPPATFKAENVSVKKGCLRIINTVLSPTEGLDGKPGDKYRLAGGAVASVKNQAHYGYYETRMKASLTTMSSTFWLSNRPVMKEIMKGGKKIKTWSSQELDIIETMGIIRSVNPDNPWNKTWNMQMNSNTHYWYQEQGGKRTDNTAKRSDVVSYMTDPSAEDFHTYGCWWVDANTVKFYYDGKYMYTIKPTTKYTDTPFDRPMFIHIVTETYDWEKQVPTAEDLKDKDKSTTYYDWVRAYKLVPIE... | 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. Inact... |
Q51485 | MYKNKKTRPAARTVGCLFALGALGLGSAAHAAEAFSPNSKWMLGDWGGKRTELLEKGYDFKLEYVGEAAANLDGGYDDDKTGRYTDQFALGVHMDLEKILGWKATEFQFTVTERNGKNLSNDRIGDPRAGHISSVQEVWGRGQTWRLTQLWLKQQYFDGALDVKFGRFGEGEDFNSFPCDFQNLAFCGSQVGNWAGSIWYNWPVSQWALRVKYNFAPDWYVQVGAYEQNPSNLETGNGFKMSGSGTKGALLPVELIWQPKVGAEQLPGEYRLGYYYSTAKADDVYDDVDGQPQGLTGNDFKSRGSKHGWWVVAQQQVTSH... | 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 su... |
Q51805 | MAVRKPPITTREYWAPGHAACAGCGCATALRLATKALSEAMEEKYGDPNAFAIAHATGCMEVVSAVFPYTAWKAPWIHVAFENAAAVASGIEAAWKKLGRKGKILAIGGDGGTADIGLQALSGMLERWHNVLYLMYDNEAYMNTGIQRSSSTPYGAWTTTSPPGKYSVGEDKPKKWVALIAAAHQIPYVATASIGNPLDFVRKIKKAGKIDGPAFVQVLCTCPTGWRSPLEKGVEIARLAIETGIWPLFEIENGDIWNIKIQPPGGGAKVYKEGNRVVRIEFKKPIEEYLKLQGRFKHLFKRPEAIEELRNQVKAMWKVL... | 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 | MPVNIKQLAQEFDKKEIGITQGHRLCPGCGAPITVKFVMMIARHLGYEPVVGLATGCLEVSTSIYPYTAWSVPYIHNAFENVAATMSGVETAYKALKNKGKIPEDKKYAFIAFGGDGGTYDIGLQSLSGMLERGHKVLYVLYDNEGYMNTGNQRSGSTPPGSDTTTAPVGKKLPGKVQLKKNIVEIVAAHENVYAATASLSEPMDFFAKVEKALNFDGPSFLAVFSPCVRFWRVNDDKTVEISKLAVETKYWPLYEVERGVYRVTRKPRQFKPVEEFLKAQGRFRKLLSRPDAKEIVDELQEYVDRRWERLLTLEEVTKD... | 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. Inact... |
Q7Q3N5 | MDYYYDDYYDEYYDHPDQAAARLFHRDLSIEETIKNCVHPSLRFATQYITNFIAINLLFSVLVLIVRKLFPTAQRSLHLLSCVCGAALVYRVIDHGFYHFLQLAVSLYAVQWTLHRWLTGTGRYIKTPFIVIAYGIGNLLVSELLEPSPETWNRIRGTQMILLMKALSLAFDTDDNHSLRSQLTVLSYSGYILCPANIVLGPWISFNDYLTIWKPPAGIEPKQCRSSSGRRMLIHVFRIVTSALMAVGFLLTSNCMIDYLLAPINSWKWVRAYGRALSFRTSHYFIGYLSQCSMMAAAADWHRAEDERSIMLPVSSLYRI... | 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.... |
Q22329 | MDNGHGYEEFELLEDGSLGECSTQVANATFLTISKLICLVVAFKFIKHIPISTTVRVYVHVFASTFTVMWFSRNHLQSAIIYNMFSLISLALAIKQFSGYIILAGNISLLIALQNFCRHYRSEDYFLSIRGILMIHIMRLTTVAFNLEKANSNKFRFVQFSSYVEYIYFPPFIIFGPYLSFEQFFKMRDKKWTGSENELGFIIQSLLAIFNAITLAIISSCHFEFFEPSSQFMEDALTAMSFRFSHYFVCLSTQAFVLMLGSDVVVANPLNIEFSRSTLQTVSEWNKPFHTFLHENIFKRRLFNSTACNVFFTFAVSSLL... | 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 p... |
Q9VWV9 | MDYQYFEEESDYIDLDEEEEDDDVVTAGSLDHRFGQPNGEEDYYFGGDDVEEELVVDGHGVLELAGRLLESLQSCVQPSVLQVMQYVAPMLLLCLLCRLLCLLYSQRRRLTSLAPLHLFHFACGLIILQITVGYRLLLLLLLAAVGYLLLQLLRLGRRGAQVLAVLTVGSQFLYELLIWRRRSDWPQLRGIQMVVNMKLISLGFDLTASGQLQARIPGPFAYLGYIYSPATCALGPWVSFGCYMDCLVPRNSWLVSLRRLLPNVVICVLAVTVSNCVAPALSDFFGDSSHFLVMYWDALSVRSSHYFVGMMAQALLVASD... | 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 ... |
Q9JJJ7 | MATFSRQEFFQQLLQGCLLPTVQQGLDQIWLLLTICFACRLLWRLGLPSYLKHASTVAGGFFSLYHFFQLHMVWVVLLSLLCYLVLFLCRHSSHRGVFLSVTILIYLLMGEMHMVDTVTWHKMRGAQMIVAMKAVSLGFDLDRGEVGAVPSPVEFMGYLYFVGTIVFGPWISFHSYLQAVQGRPLSRRWLKKVARSLALALLCLVLSTCVGPYLFPYFIPLDGDRLLRNKKRKARGTMVRWLRAYESAVSFHFSNYFVGFLSEATATLAGAGFTEEKDHLEWDLTVSRPLNVELPRSMVEVVTSWNLPMSYWLNNYVFKN... | 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.... |
O48741 | MALQAAYSLLPSTISIQKEGKFNASLKETTFTGSSFSNHLRAEKISTLLTIKEQRRQKPRFSTGIRAQTVTATPPANEASPEQKKTERKGTAVITGASSGLGLATAKALADTGKWHVIMACRNFLKAEKAARSVGMSKEDYTVMHLDLASLESVKQFVENFRRTEQPLDVLVCNAAVYQPTAKEPSFTAEGFEISVGTNHLGHFLLSRLLLDDLKKSDYPSKRMIIVGSITGNTNTLAGNVPPKANLGDLRGLASGLNGQNSSMIDGGEFDGAKAYKDSKVCNMLTMQELHRRYHEETGVTFASLYPGCIATTGLFREHI... | 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 Locatio... |
O66148 | MAQDQKPTVVITGASSGVGLYAAKALVKRGWHVVMACRNLEKADSAAKSLGMSPDSYTLMHIDLGSLDSVRKFVTQFRESGKSLDALVCNAAVYMPLLKEPMRSPEGYELSVATNHFGHFLLCNLLLEDLKHSTHNDPRLIILGTVTANSKELGGKIPIPAPADLGDLSGLEAGFKAPIAMIDGKPFKAGKAYKDSKLCNMITSRELHRRYHDSTGIVFNTLYPGCVADTPLFRNSLPVFQKVFPWFQKNITGGYVSQELAGERTAQVVADPEFKQSGVHWSWGNRQKEGRESFVQELSEKVTDDAKAKRMWELSEKLVG... | 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 | MPKRSNGSLVVRCAVSVVRFSKENVSCDLASENFTFSRDSFPVVSTVLRVSEAVYRMAAVASLGSALSVSSAALSQNVSVSNNATKESAFLGLRMGEVAKFGGALLSVSTVAANLKSKPGVLSVNAVTAPAETMNKPSSKKTATKSTCIITGASSGLGLATAKALADTGEWHVIMACRDFLKAERAARSVGIPKDSYTVIHCDLASFDSVRAFVDNFRRTERQLDVLVCNAAVYFPTDKEPKFSAEGFELSVGTNHMGHFLLARLLMEDLQKAKDSLKRMIIVGSITGNSNTVAGNVPPKANLGHLRGLAGGLNGVNSSS... | 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 Locatio... |
Q59987 | MEQPMKPTVIITGASSGVGLYGAKALIDKGWHVIMACRNLDKTQKVADELGFPKDSYTIIKLDLGYLDSVRRFVAQFRELGRPLKALVCNAAVYFPLLDEPLWSADDYELSVATNHLGHFLLCNLLLEDLKACPDADKRLIILGTVTANSKELGGKIPIPAPPDLGNFEGFEAGFKKPIAMINNKKFKSGKAYKDSKLCNMLTTRELHRRFHQETGIVFNSLYPGCVADTPLFRNHYSLFRTIFPWFQKNVTKGYVSQELAGERVAMVVADDKFKDSGVHWSWGNRQQAGREAFVQELSEQGSDAQKAQRMWDLSEKLVG... | 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 | MIRAANGFRISVRNTAVCLAPNFRQLKGFSIINLGSLQYFRYNSVYSKSIRLVNTLENRIVPVYKECASPQSIGGKSNLKQLQWPKPPKNILILKKRMDERVDHCFETLVQHLQQTYPDICIITETDVAKKFSYLNLYTWTEISDLEQKVDAIITVGGDGTILHAASLFARSGMPPILSFSLGTLGFLLPFDFGSFQTAFADFYNSRSFVLMRMRLRVAMKTKLYNESIYAMNEMHIHRGLSPHMAVLKVFVNDKFLTEAVADGLIISTPTGSTAYSLSSGGPIVHPSINALLLTPICPNSLSFRPVLFPDTFKISIETS... | 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 | MFVRVKLNKPVKWYRFYSTLDSHSLKLQSGSKFVKIKPVNNLRSSSSADFVSPPNSKLQSLIWQNPLQNVYITKKPWTPSTREAMVEFITHLHESYPEVNVIVQPDVAEEISQDFKSPLENDPNRPHILYTGPEQDIVNRTDLLVTLGGDGTILHGVSMFGNTQVPPVLAFALGTLGFLSPFDFKEHKKVFQEVISSRAKCLHRTRLECHLKKKDSNSSIVTHAMNDIFLHRGNSPHLTNLDIFIDGEFLTRTTADGVALATPTGSTAYSLSAGGSIVSPLVPAILMTPICPRSLSFRPLILPHSSHIRIKIGSKLNQKP... | 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 | MIPFLPMFSLLLLLIVNPINANNHYDKILAHSRIRGRDQGPNVCALQQILGTKKKYFSTCKNWYKKSICGQKTTVLYECCPGYMRMEGMKGCPAVLPIDHVYGTLGIVGATTTQRYSDASKLREEIEGKGSFTYFAPSNEAWDNLDSDIRRGLESNVNVELLNALHSHMINKRMLTKDLKNGMIIPSMYNNLGLFINHYPNGVVTVNCARIIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDDLSSFRAAAITSDILEALGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSESIMGGAV... | 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-carbox... |
Q9SA05 | MAGRVESSIGGGEIDEEGDERGSMWDLDQSLDQPMDEEAGRLRNMYREKKFSAFLLLQLSFQSLGVVYGDLGTSPLYVFYNTFPRGIKDPEDIIGALSLIIYSLTLIPLLKYVFVVCKANDNGQGGTFALYSLLCRHAKVSTIPNQHRTDEELTTYSRTTFHERSFAAKTKRWLENGTSRKNALLILVLVGTCMVIGDGILTPAISVLSAAGGLRVNLPHINNGIVVVVAVVILVSLFSVQHYGTDRVGWLFAPIVFLWFLFIASIGMFNIWKHDPSVLKAFSPVYIFRYFKRGGQDRWTSLGGIMLSITGIEALFADLS... | 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 | MAARVEAATMGGEIDEEESDERGSMWDLDQKLDQSMDEEAGRLRNMYREKKFSALLLLQLSFQSLGVVYGDLGTSPLYVFYNTFPHGIKDPEDIIGALSLIIYSLTLIPLLKYVFVVCKANDNGQGGTFALYSLLCRHAKVKTIQNQHRTDEELTTYSRTTFHEHSFAAKTKRWLEKRTSRKTALLILVLVGTCMVIGDGILTPAISVLSAAGGLRVNLPHISNGVVVFVAVVILVSLFSVQHYGTDRVGWLFAPIVFLWFLSIASIGMYNIWKHDTSVLKAFSPVYIYRYFKRGGRDRWTSLGGIMLSITGIEALFADL... | 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 | MEEIEEGSSNNSIRRVGTGSSDRRWVDGSEVDSETPLFSEIRDRDYSFGNLRRRLMKKPKRADSLDVEAMEIAGSHGHNLKDLSLLTTLGIAFQTLGVVYGDMGTSPLYVFSDVFSKVPIRSEVDVLGALSLVIYTIAVIPLAKYVFVVLKANDNGEGGTFALYSLICRYAKVNKLPNQQPADEQISSFRLKLPTPELERALGIKEALETKGYLKTLLLLLVLMGTSMIIGDGILTPAMSVMSAMSGLQGEVKGFGTNALVMSSIVILVALFSIQRFGTGKVGFLFAPVLALWFFSLGAIGIYNLLKYDFTVIRALNPFY... | 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 Len... |
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: Cytopla... |
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: Cytopla... |
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.
Locati... |
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).
Locati... |
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: Cytopla... |
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 L... |
P06726 | MSQASSSPGEGPSSEAAAISEAEAASGSFGRLHCQVLRLITNVEGGSLEAGRLRLLDLRTNIEVSRPSVLCCFQENKSPHDTVDLTDLNIKGRCVVGEQDRLLVDLNNFGPRRLTPGSENNTVSVLAFALPLDRVPVSGLHLFQSQRRGGEENRPRMEARAIIRRTAHHWAVRLTVTPNWRRRTDSSLEAGQIFVSQFAFRAGAIPLTLVDALEQLACSDPNTYIHKTETDERGQWIMLFLHHDSPHPPTSVFLHFSVYTHRAEVVARHNPYPHLRRLPDNGFQLLIPKSFTLTRIHPEYIVQIQNAFETNQTHDTIFFP... | 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 (ND1... |
O48840 | MVVKYTMSMSFFVIFASTVTIIVHGFPSTLDGPLNPVTAPLDPNLNPIAFDLPESDPSFVKPISEFLLPEQISVSLSYSFDSVWISWVTGEYQIGEKDSAPLDPNCVQSIVQYREFDVRRTRKQNATGHSIVYNQQYSSENGFMNYTSGIIHHVQLTGLKPNTLYRYQCGDPSLSAMSKEYYFRTMPKSTSENYPHRIVVAGDLGLTYNTSTVLGHILSNHPDLVVLLGGFSYADTYLANKTKLDCSSCHCDQNGTSSDCGSCYSSGETYQPRWDYWGRFMEPLTANVPTMMVAGEHEIEPQTENNLTFAAYSSRFAFPS... | 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 | MFKRSLIAASLSVAALVSAQAMAVTGGGASLPAELYKGSADSILPANFSYAVTGSGTGKNAFLTNNSSLFGTTGTVHYAGSDSVLSGSELTTYNSNYNGTYGPLIQIPSVATSVTVPYRKDGNTTLNLTSAQLCDAFSGAKTTWGQLLGTTDSTPIRIVYRTGSSGTTELFTRHLNSICPTRFATNSTFTNARLPAGGTLPSNWVGVAATSTVVSTVKATNGSLGYVSPDAVNINSNAEVSRVNGNLPTQANVSTALGSVAPPANAADRADPSKWVPVFTNPSAGYSIVGYTNFVFGQCYKDASVSTDVRAFINKHYGGT... | 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 | MYKRSLIAASLSVAALVSAQAMAEINGGGATLPQQLYQEPGVLTAGFAAYIGAGSGNGKAAFLNNDYTKFVAGTTNKNVHWAGSDSKLSKTNETNPYLSAHGSAWGPLIQVPSVATSVALPFNKSGSNAVNFADVNTLCGVFSGRLTDWSQIPGSGRSGAITVAYRSESSGTTELFTRFLNASCSSALEGGTFAITTSFGNSFSGGLPAGAVSAQGSQAVMNTLNAAEGRITYMSPDFAAPTLAGLDDATKVAQVRGVSPAPANVSAAIGAVTPPTTAQRSDPNNWVPVFAATASATDPSVRPYPTTGYPILGFTNLIFS... | 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 | MKAFLLTLLAQLCSASLVPEREKDPEYWRQQAQETLRDALRLQHLNQNVAKNLILFLGDGMGVSTVTAARILKGQLQHRKGEESLLEMDKFPYVALAKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAGVTRDRCNTTKGQEVTSILRWAKDEGKAVGIVTTTRVTHATPSAAYAHSANRDWYSDGEMPLDALEGGCKDIARQLVDNIPDIEVILGGGRKYMFPKNTSDVEYPQEERHRGTRLDGKDLVQAWHDTKPAGKVAKYVWHRRELLALNVSRVDFLLGLFEPGDMVYELDRNNETDPSLSEMVAVAIRMLQ... | 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, suc... |
P05186 | MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQIL... | 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 diphosphat... |
P29523 | MSTWWLVVVAAAAAAGLVRAEDRYHPERLAAGEASAATRSAAESEASFWVREAQEAIERREREGAGAKQAAGHAKNVVMFLGDGMSVPTLAAARTLLGQRRGQTGEEASLHFEQFPTLGLAKTYCVNAQVPDSSCTATAYLCGVKANQGTLGVTAAVPRHDCEASTDVTKRVQSIAEWALADGRDVGIVTTTRITHASPAGTFAKVANRNWENDNDVKQEGHDVNRCPDIAHQLIKMAPGNKFKVIFGGGRREFLPTTQVDEEGTRGLRTDGRNLIEEWQNDKESQKVSYKYLWNRQELLKLGSSPPDYLLGLFEGSHLQ... | 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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