ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O14344 | MSAFKPYTEALEVLKKYEKKDGLSIDDLIRHNFQGGLTFNDFLILPGYIDFVPNNVSLETRISRNIVLKTPFMSSPMDTVTEDQMAIYMALLGGIGVIHHNCTPEEQAAMVRKVKKYENGFILDPVVFSPQHTVGDVLKIKETKGFSGIPITENGKLRGKLVGIVTSRDVQFHKDTNTPVTEVMTPREELITTAEGISLERANEMLRKSKKGKLPVVDKDDNLVALLSLTDLMKNLHFPLASKTSDTKQLMVAAAIGTRDDDRTRLALLAEAGLDAVVIDSSQGNSCFQIEMIKWIKKTYPKIDVIAGNVVTREQTASLI... | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XM... |
Q4L385 | MWENKFAKESLTFDDVLLIPAASDVLPNDADLSVELSERIKLNIPVISAGMDTVTESKMAIAMARQGGLGVIHKNMGIEEQAEEVQKVKRSENGVITNPFYLTPDESVYEAEALMGKYRISGVPIVSDKESRELVGILTNRDLRFIEDFSIKISDVMTKENLITAPVGTTLDEAETILQEHKIEKLPLVENGRLEGLITIKDIEKVLEFPHAAKDAHGRLLAAAAIGTSKDTEIRAQKLVEAGVDALIIDTAHGHSSGVIQEVKKMKEKYPEITIVAGNVATAEATRALFEAGADVVKVGIGPGSICTTRVVAGVGVPQI... | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XM... |
P05701 | MMNEHSIDTDNRKANNALYLFIIIGLIPLLCIFVVYYKTPDALLLRKIATSTENLPSITSSYNPLMTKVMDIYCKTAPFLALILYILTFKIRKLINNTDRNTVLRSCLLSPLVYAAIVYLFCFRNFELTTAGRPVRLMATNDATLLLFYIGLYSIIFFTTYITLFTPVTAFKLLKKRQ | Function: This protein is able to protect a cell, which harbors the plasmid ColA encoding colicin A, against colicin A.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20464
Sequence Length: 178
Subcellular Location: Cell inner membrane
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P22426 | MTSNKDKNKKANEILYAFSIIGIIPLMAILILRINDPYSQVLYYLYNKVAFLPSITSLHDPVMTTLMSNYNKTAPVMGILVFLCTYKTREIIKPVTRKLVVQSCFWGPVFYAILIYITLFYNLELTTAGGFFKLLSHNVITLFILYCSIYFTVLTMTYAILLMPLLVIKYFKGRQ | Function: This protein is able to protect a cell, which harbors the plasmid ColB encoding colicin B, against colicin B.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20186
Sequence Length: 175
Subcellular Location: Cell inner membrane
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P08701 | MNRKYYFNNMWWGWVTGGYMLYMSWDYEFKYRLLFWCISLCGMVLYPVAKWYIEDTALKFTRPDFWNSGFFADTPGKMGLLAVYTGTVFILSLPLSMIYILSVIIKRLSVR | Function: This protein is able to protect a cell, which harbors the plasmid ColIa-CA53 encoding colicin Ia, against colicin Ia.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13283
Sequence Length: 111
Subcellular Location: Cell membrane
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P08702 | MKLDISVKYLLKSLIPILIILTVFYLGWKDNQENARMFYAFIGCIISAITFPFSMRIIQKMVIRFTGKEFWQKDFFTNPVGGSLTAIFELFCFVISVPVVAIYLIFILCKALSGK | Function: This protein is able to protect a cell, which harbors the plasmid IncI1 ColIb-P9 encoding colicin Ib, against colicin Ib.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13219
Sequence Length: 115
Subcellular Location: Cell membrane
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P29681 | MKPVALILVFLAISQARVLNLPKEAIDIPVAIVEDKEPPVALSLVKEEVKAEEVKPEEVKPIAQEEKAKDLKEEVKPEIKPEIKEQPKPDIKDEIKEDLKADIKEELKEKIEEQINELPNAKPLELKEKSLEAEEKPQEIKEEVQQPEIKKEATEIKEEPAQNILKSLPAEETVVVPAEELSPNPVEQEQSENQDAAHPQVRQATQATPTQQSTTQGNFVQQLIQNSPIGQFLNQFQPQPAAAAAPAAAQVQADDAAAAAPATPAPTVPGFLNPQAAITSAQQAVQNAAQSAVNATTQAFQGIQQFASNLGNQFQNTLSS... | Function: Probably has an essential role in embryogenesis, induces morphogenesis of imaginal disks, and may participate in multimolecular aggregates.
Sequence Mass (Da): 49809
Sequence Length: 466
Domain: The regions 203-253, 256-333 and 335-377 are thought to contain either alpha helical or beta pleated sheet motifs.
... |
Q8JIR8 | MHLKTGLIFLAICLALQVQGSREIPSKTNHGEAKQLADASGSDKTERTTKRSRVSTIRRIFDMAKHRTKRSPFFSTGVKICPQESVKQILASHQAYYRLRVCQEAVWEAFRIFLDRIPDTSEYQNWVTACQRETFCIFDIGKNFSNSQEHLEIIQRRVKHRTFQERKDEISTDKTGGKKLEDIPSVSTGPPSASLSTYTLVPNGTLLNEIVNETKTPVKELGTNTVPELPAEQMVEFSVTLTDQEYTAELSDPNSPQYRQLAAKFQLQMQKIFEKLPGFKEIHVLGFKQKKEKDGSSSTIARYMVNFERDGSEIKSTADD... | Function: Chondroitin sulfate-, heparin- and hyaluronan-binding protein . May serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix (By similarity).
PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic acid).
Sequence Mass (Da): 102684
Sequence Length: 928
Subcel... |
Q17R60 | MYLETRRAIFVFWIFLQVQGTKDISINIYHSETKDIDNPPRNETTESTEKMYKMSTMRRIFDLAKHRTKRSAFFPTGVKVCPQESMKQILDSLQAYYRLRVCQEAVWEAYRIFLDRIPDTGEYQDWVSICQQETFCLFDIGKNFSNSQEHLDLLQQRIKQRSFPDRKDEISAEKTLGEPGETIVISTDVANVSLGPFPLTPDDTLLNEILDNTLNDTKMPTTERETEFAVLEEQRVELSVSLVNQKFKAELADSQSPYYQELAGKSQLQMQKIFKKLPGFKKIHVLGFRPKKEKDGSSSTEMQLTAIFKRHSAEAKSPAS... | Function: Chondroitin sulfate-, heparin- and hyaluronan-binding protein (By similarity). May serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix .
PTM: The N-terminus is blocked.
Sequence Mass (Da): 89387
Sequence Length: 797
Subcellular Location: Cell projection
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Q94F00 | MGRSLIFSGNMSLRISHLPRSSLPLQNPISGRTVNRTFRYRCTRILSNSFKSTTRLQTKAVLSEVSDQTRYPRIGAKTTGTISPAHLLEVVELAAKTGAEVVMEAVNKPRNITYKGLSDLVTDTDKASEAAILEVVKKNFSDHLILGEEGGIIGDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLYRGNPAAASVVEFVGGPMCWNTRTFSATAGGGALCNGQKIHVSKTDAVERALLITGFGYEHDDAWSTNMELFKEFTDVSRGVRRLGAAAVDMCHVALGIAESYWEYRLKPWDMAAGVLIVEEAGGAVTRMDGG... | Function: Phosphatase acting preferentially on D-myoinositol 1-phosphate (D-Ins 1-P).
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Mass (Da): 40445
Sequence Length: 371
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
Sub... |
P83891 | XVGDLKTPAILRVTNAYLFN | Function: Binds DNA.
PTM: Phosphorylated.
Sequence Mass (Da): 2217
Sequence Length: 20
Subcellular Location: Cytoplasm
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P9WJ98 | MVPAGLCAYRDLRRKRARKWGDTVTQPDDPRRVGVIVELIDHTIAIAKLNERGDLVQRLTRARQRITDPQVRVVIAGLLKQGKSQLLNSLLNLPAARVGDDEATVVITVVSYSAQPSARLVLAAGPDGTTAAVDIPVDDISTDVRRAPHAGGREVLRVEVGAPSPLLRGGLAFIDTPGVGGLGQPHLSATLGLLPEADAVLVVSDTSQEFTEPEMWFVRQAHQICPVGAVVATKTDLYPRWREIVNANAAHLQRARVPMPIIAVSSLLRSHAVTLNDKELNEESNFPAIVKFLSEQVLSRATERVRAGVLGEIRSATEQL... | Function: Participates in the development of tolerance to both isoniazid and ethambutol. May function through a MDR-pump like mechanism, although it does not appear to directly transport isoniazid from the cell (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70083
Sequence Length: 6... |
F1QR98 | MLCLQESGDCLRDQMRYMMRSLQDLKHLRRSCVAPPVGPPVRLRACKQLIAQRERRARLRISDASEASSYDSACCLSSSLEEEESASDPSAVSSPSSERSLEFDSGYSEASWQDEGVVLRRTKNIRVSSTACLRTNQLSNTRARPKSTSDACLESWTSFETASDPEDWTTSLLTRGRNRQPLVLGDNSFADLIHNWMDLPECPEQTELKHSSGRSFAKDFLVNIKRRIAGFSRSADGRRKSSDVTKLSKSIVPTKRLSCQIDVQHKMPFFYKSHTGLNELDTDYYQFSALMKSGSRTPIVCNDIIGYI | Function: Inhibitor of the serine/threonine-protein kinase pak4/pak5 (By similarity). Acts by binding pak4/pak5 in a substrate-like manner, inhibiting the protein kinase activity (By similarity). Required for the proper migration of neural crest cells during embryonic development, probably by inhibiting pak4/pak5 .
Seq... |
F1QPR4 | MLCVRNSGECFRDHMRHMMRSLQDLKQIREPDDQSKCSYVTRARQKRIKQREQLSRLRISDVSDTSTYDSACCLASPLEEEEDQENHAERLAQGSPSSIKSLDFDSGYSEASWQDEGVVLRRTRNVRVSSSACVRTNRIRPKSTSDACLERWTSFEASDPTDWTTSLLTRGRNRQPLVLGDNSFADLIKNWMDLPECPDSAELKPSRKTAFLVNMRRKIAGISKGLEERRSAEAKRMSCPVGFQPPKPFFHQSHTSLHPMGTDFYQFSSVMKSGSRQPIICNDVIGYI | Function: Inhibitor of the serine/threonine-protein kinase pak4/pak5. Acts by binding pak4/pak5 in a substrate-like manner, inhibiting the protein kinase activity.
Sequence Mass (Da): 32880
Sequence Length: 288
Domain: The Inka box (also named iBox or inca box) binds and inhibits PAK4 by binding a substrate-like manner... |
Q96EL1 | MDMHSARLDSFLSQLRWELLCGRDTGSPSMPGPLQPTSQTGPDVQPSHQLRASGALEEDSVCCVEEEEEEEEEAVVTEDRDAALGGPREHALDWDSGFSEVSGSTWREEELPVSQRPAPSAQPLRRQCLSVSGLPMPSRAPVASVPPVHHPRPKSTPDACLEHWQGLEAEDWTAALLNRGRSRQPLVLGDNCFADLVHNWMELPETGSEGGDGGGHRARARPPQFLLGLSEQLRRRLARARRTAMAGKRLSCPPRPEPELPADVSRFAALMSCRSRQPIICNDVSYL | Function: Inhibitor of the serine/threonine-protein kinase PAK4 . Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity .
Sequence Mass (Da): 31574
Sequence Length: 287
Domain: Contains 2 Inka boxes (also named iBox or inca box) . The Inka boxes bind and inhibit PAK4 by binding a subst... |
Q9CX62 | MHSARLDSFLSQLRWELLCARDTGSPPMSGPLQPKPRTDQNVQPKRQFRASDVLEEDSVCCVEEEEEEGLVAEDKGLPLGCPREHALDWDSGFSEVSGSTWREEEPSVPQRQAPRERPPHSQRFSVSDIPMRSRAAVTNIPPAHRPRPKSTPDACLEHWQGLEAEDWTAALLNRGRSRQPLVLGDNCFADLVHNWMELPEATSEGSDGDVPRARARPPQFLLGLSEQLRRRLARARRTAMASKRLSCPPRSEPDLPADISRFAALMNCRSRQPIIYNDVSYL | Function: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Sequence Mass (Da): 31804
Sequence Length: 282
Domain: Contains 2 Inka boxes (also named iBox or inca box). The Inka boxes bind and inhibit PAK4 by binding a substrat... |
Q9NTI7 | MTMESREMDCYLRRLKQELMSMKEVGDGLQDQMNCMMGALQELKLLQVQTALEQLEISGGGPVPGSPEGPRTQCEHPCWEGGRGPARPTVCSPSSQPSLGSSTKFPSHRSVCGRDLAPLPRTQPHQSCAQQGPERVEPDDWTSTLMSRGRNRQPLVLGDNVFADLVGNWLDLPELEKGGEKGETGGAREPKGEKGQPQELGRRFALTANIFKKFLRSVRPDRDRLLKEKPGWVTPMVPESRTGRSQKVKKRSLSKGSGHFPFPGTGEHRRGENPPTSCPKALEHSPSGFDINTAVWV | Function: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Sequence Mass (Da): 32759
Sequence Length: 297
Domain: The Inka box (also named iBox or inca box) binds and inhibits PAK4 by binding a substrate-like manner.
Subcellu... |
Q80VY2 | MTKESKDMDCYLRRLKQELMSMKEVGDGLQDQMNCMMGALQELKLLQVQTALEQLEISGGTPTFSCPESSQEQPECPRWQGSGGPAGPAAWTSSSQPSFDSSPKLPCRRSVCGKELAVLPKTQLPEEHQSCTQQGTEWVEPDDWTSTLMSRGRNRQPLVLGDNVFADLVGNWLDLPELEKGGEKGETGGSIEPKGEKGQSRELGRKFALTANIFRKFLRSVRPDRDRLLKEKPGWMTPMVSESRAGRSKKVKKRSLSKGSGRFPFSSTGEPRHIETPATSSPKALEPSCRGFDINTAVWV | Function: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Sequence Mass (Da): 33233
Sequence Length: 300
Domain: The Inka box (also named iBox or inca box) binds and inhibits PAK4 by binding a substrate-like manner.
Subcellu... |
P0DJM0 | MRKKRYVWLKSILVAILVFGSGVWINTSNGTNAQAATITQDTPINQIFTDTALAEKMKTVLGKTNVTDTVSQTDLDQVTTLQADRLGIKSIDGVEYLNNLTQINFSNNQLTDITPLKNLTKLVDILMNNNQIADITPLANLTNLTGLTLFNNQITDIDPLKNLTNLNRLELSSNTISDISALSGLTSLQQLSFGNQVTDLKPLANLTTLERLDISSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTNLTDLDLANNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALT... | Function: Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells . Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin-2 function as receptors... |
P0DQD3 | MKEKHNPRRKYCLISGLAIIFSLWIIIGNGAKVQAETITVSTPIKQIFPDDAFAETIKDNLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVTKLFLNGNKLTDIKPLTNLKNLGWLFLDENKIKDLSSLKDLKKLKSLSLEHNGISDINGLVHLPQLESLYLGNNKITDITVLSRLTKLDTLSLEDNQISDIVPLAGLTKLQNLYLSKNHISDLRALAGLKNLDVLELFSQECLNKPINHQSNLVVPNTVKNTDGSLVTPEIISDDGDYEKPNVKWHLPEFTNEVSFIFYQPVTIGKAKARFHGRVTQPLK... | Cofactor: Binds 2 Ca(2+) ions; binding site 1 has a 10-fold higher affinity binding site 2 . Loss of Ca(2+)-binding has no measurable effect on host receptor activation or invasion by Listeria, suggesting ion-binding is fortuitous .
Function: Mediates the entry of L.monocytogenes into normally non-phagocytic mammalian ... |
P71451 | MLKKNNWLQNAVIAMLVLIVGLCINMGSGTKVQAESIQRPTPINQVFPDPGLANAVKQNLGKQSVTDLVSQKELSGVQNFNGDNSNIQSLAGMQFFTNLKELHLSHNQISDLSPLKDLTKLEELSVNRNRLKNLNGIPSACLSRLFLDNNELRDTDSLIHLKNLEILSIRNNKLKSIVMLGFLSKLEVLDLHGNEITNTGGLTRLKKVNWIDLTGQKCVNEPVKYQPELYITNTVKDPDGRWISPYYISNGGSYVDGCVLWELPVYTDEVSYKFSEYINVGETEAIFDGTVTQPIKN | Function: A virulence enhancer that has at least 2 dissociable functions in infection; it impairs translocation of host transcription factor NF-kappa-B to the nucleus and antagonizes the function of the Tuba dynamin-binding protein, promoting bacterial spreading . Perturbs the morphology of host cell junctions by impai... |
Q5B7I9 | MEKTQTPSLTPDELSARSSTPFEEREEEEEVHYVGHLKFSFIFVGLCLSVFQVALSLQDIGWYGSAYLFTDCAFQLVFGRLYSMLPVKIVYLGALLLFEIGSIICATAPNSIALILGRTIAGIGAGGILSGALTILSQSVPRAKVAVFNGILGAVNGIAFICGPLLAGGIINGTTWRWIFYINPIISAPTFFITVFLLKLDPPKTNVKTWRGRIAMLDLPAFTLFLGSILCLILALLWGGKEYSWKNARIIVLFILFGVIMLAFMLVQKRKGDDALVPMRILCQRSIAFGMFFSFCTSGTGFILEYYLPIWLQVIKDLSV... | Function: MFS efflux transporter; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor . In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 d... |
Q5B7I7 | MAKETRFYPYTSNGGATLGVSGPDFAILAGDTRSTAGYNINTRYEPKVFTIQDARDRSIVISVIGFAADGRALKERLDAIVAMYKYQHGKNIGLRACAQRVSTMLYEKRFFPYQLQTMVAGIDADGQGAIYYYDPAGCIEKRSHCAAGEASSLMLPFLDSQAPRLQPLSLQTAQQLVRDAYTGATERHIEVGDHLQMLVVTREGVSEQLVDLKKD | Function: Proteasome subunit beta type-6; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor . In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto ... |
Q5B7I6 | MRILFFHGHTQTGPVFERKTVRLREHIQRAYPGSTFFFPTGPIAYKVSDRLDYLSEIQRERSDNFKDPDLIETHAWFRLFEDDPPRGLLESLDIAAEILRVEGPFDGVICFSQGSVVGSMMASLLEGPRRRQRFDEYAASFPGAVRYPKSYKNINHPPLKFGITYGAYMGTSPVFNAFYSEPLIETPFLHFMGEFDPVVPSEMVAAVDKAQIGGSRRRKVMHPGAHAIPVGDRYHEAVVDFIRSACETSPTYFDLPSDEVPLLSYNDTPEQTPFQTPLLTPSLSSAVSTTSIPSSEATILATRRLDQWEKSRSPRSNIRP... | Function: Esterase; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor . In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB ... |
P21327 | MSDILQELLRVSEKAANIARACRQQETLFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKENMENKFPGLGKKIFGEESNEFTNDLGEKIIMRLGPTEEETVALLSKVLNGNKLASEALAKVVHQDVFFSDPALDSVEINIPQDILGIWVDPIDSTYQYIKGSADITPNQGIFPSGLQCVTVLIGVYDIQTGVPLMGVINQPFVSQDLHTRRWKGQCYWGLSYLGTNIHSLLPPVSTRSNSEAQSQGTQNPSSEGSCRFSVVISTSEKETIKGALSHVCGERIFRAAGAGYKSLCVILGLADIYIFSEDTTFKWDSCA... | Function: Mg(2+)-dependent phosphatase that catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate and participates in inositol phosphate metabolism.
Catalytic Activity: 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
Sequenc... |
C4M633 | MQTSLFEFANVLITAVKEASYSISKFKEEVEIKYKSDGSEVTQVDTQSQQIIFSIIKNKYPTINIIGEEDVENGIPDNQLPTITQLSFGSLENKIININDIIIYVDPLDGTDCYTHKQYDSVCVLVGVTYKGKPMIGIVSKPFYNNEITFAIENYISSISLQPLNDKIIFVCSKKNDIQHLIKSFPDPYEVKYKGGSGAKMMAIIHQEADIYYHPLIQSCTWDTLAAQVILEAQGGIVCDIYGNPLCYPSSKKESMRHKKGVLCLSPRAKKYLPYMLSISKTILL | Cofactor: Binds 3 Mg(2+) per subunit.
Function: Catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate . Is also able to convert 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP but with less efficiency .
Catalytic Activity: 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosph... |
P49441 | MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEALARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQCVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRRNGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAA... | Function: Mg(2+)-dependent phosphatase that catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate and participates in inositol phosphate metabolism.
Catalytic Activity: 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
Sequenc... |
Q8A7J9 | MKRPSFLPVLIGTGFGSGFSPFAPGTAGALLASIIWIALYFLLPFTALLWTTAALVVLFTFAGIWAANKLESCWGEDPSRVVVDEMVGVWIPLLAVPDNDRWYWYVIAAFALFRIFDIVKPLGVRKMENFKGGVGVMMDDVLAGVYSFILIAVARWVIG | Function: May be responsible for the conversion of phosphatidylinositol phosphate diacylglycerol (PIP-DAG) to phosphatidylinositol diacylglycerol (PI-DAG), making it a key enzyme in the inositol glycerophospholipid biosynthesis pathway.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)... |
C8AW47 | MSKHAVVQFGVVYALLFPGVFGFVPSPTNVSVVCHNFVNVLYWNYSNPTEQTKFAIKVEPYESPSQTVDTSQTYLDISSYSTDVEDDYLVLLTAHDGQEKSEDVSIRFTYSKDYFDENKHKYKCSLDFPAVNTSVHKDVIEVSFQHPFKLYKQEIMKEEFTYKITHDEQMVKYSCFEDEDLCNAEVHFNQSVAGQCVELKLEGVIAGIPSYTYSNVCVPQPTPETDKTGIIAALIGGATVVLFIIMGFVWLLWRKWSNIPQMPQGLWCIISKQSHTMLLSQPEPTDICPVTSQGPLNYLTEEDQSVSARDDTGADPPVVS... | Function: Receptor which shows binding specificity for the cytokine ifng1 (interferon gamma 1).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38670
Sequence Length: 344
Subcellular Location: Cell membrane
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Q9VBB3 | MAANIAAAAAAAQEVDPVLKKAIKLLHSSNPTSAAELRLLLDEALKARFGPEKSLTNNMTPRMLEDEANFSGRAATPPQQPINADEIINLTNSPDKEPSDSVDTIADSDDGLSAVGIVNTGDTGDFGDLNCCVCGEMVFTATNRLIECSKCGAMYHQECHKPPITKEEAADDQEQNWQCDTCCNKPTSSGRTTSSAAAVTPTVFIADEPMPLTSKAKSSVASSRSSNSSNSSSPFYRPEPSSSTNASSSSSSKHGHKSSSSSSSKSHKEERSSKSTAASSLSAIGGMEKHNSSGTSSRRSGSSTKSSSKSSSSKHHESGS... | Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing . Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 . Required for the normal expression of the Integrator comple... |
Q9VEX5 | MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSADGGATGAAGNATGSGGSQFSKSLWTCACESSIEYCRVVWDLFPGKKHVRFIVSDTAAHIVNTWRPSTQNMAHVMNAMLIVGVPSRNVPTSSDYSVIHGLRAAIEALAEPTDEQLAAMADFGTDELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNTLAAPPSKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISPLLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGAT... | Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing . Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1 and U5 . Plays a role as a regulator of spermatogenesis . Crucial regulator ... |
Q39041 | MASSDALLPISAREEEPLCPYTRLPMADPNQETHGPRRRRPFKGLLAVSFGLLFIAFYVALIATHDGSRSNDEGIDETETITSRARLAGVSEKRNDGLWKLSGDRNTPAFEWNNSMLSWQRTAFHFQPEQNWMNDPNGPLFYKGWYHFFYQYNPNAAVWGDIVWGHAVSRDLIHWVHLPIAMVADQWYDSNGVWTGSATFLPDGSIVMLYTGSTDKAVQVQNLAYPEDPNDPLLLKWVKFPGNPVLVPPPGILPKDFRDPTTAWKTSEGKWRITIGSKLNKTGISLVYDTIDFKTYEKLDTLLHRVPNTGMWECVDFYPV... | Function: Possible role in the continued mobilization of sucrose to sink organs . Regulates root elongation .
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 73844
Sequence L... |
Q9FXA8 | MSAIYLLRKISTKTPSRFHRSLFFSTFSKDSPPDLSRTTSIRHLSSSQRFVSSSIYCFPQSKILPNRFSEKTTGISVRQFSTSVETNLSDKSFERIHVQSDAILERIHKNEEEVETVSIGSEKVVREESEAEKEAWRILENAVVRYCGSPVGTVAANDPGDKMPLNYDQVFIRDFVPSALAFLLKGEGDIVRNFLLHTLQLQSWEKTVDCYSPGQGLMPASFKVRTVALDENTTEEVLDPDFGESAIGRVAPVDSGLWWIILLRAYGKITGDFSLQERIDVQTGIKLIMNLCLADGFDMFPTLLVTDGSCMIDRRMGIHG... | Function: Mitochondrial invertase that cleaves sucrose into glucose and fructose and is involved in the regulation of multiple tissue development and floral transition. May generate glucose as a substrate for mitochondria-associated hexokinase, contributing to mitochondrial reactive oxygen species homeostasis.
Catalyti... |
P29000 | MATQCYDPENSASRYTLLPDQPDSGHRKSLKIISGIFLSVFLLLSVAFFPILNNQSPDLQIDSRSPAPPSRGVSQGVSDKTFRDVAGASHVSYAWSNAMLSWQRTAYHFQPQKNWMNDPNGPLYHKGWYHLFYQYNPDSAIWGNITWGHAVSKDLIHWLYLPFAMVPDQWYDINGVWTGSATILPDGQIMMLYTGDTDDYVQVQNLAYPANLSDPLLLDWVKFKGNPVLVPPPGIGVKDFRDPTTAWTGPQNGQWLLTIGSKIGKTGVALVYETSNFTSFKLLDGVLHAVPGTGMWECVDFYPVSTKKTNGLDTSYNGPG... | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 70097
Sequence Length: 636
Pathway: Glycan biosynthesis; sucrose metabolism.
Subcellular Location: Membrane
EC: 3.2.1.26
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P80065 | MDTYHFLPSRDLEHASSYTPRPDSPETRHEPDPDRSKTNRRPIKIVSSVLLSTLILSFVIFLLVNPNVQQVVRKKVSKNSNGEDRNKASKSPEMLGPPSRGVSQGVSEKSFRQATAEPSYPWTNDMLSWQRTSFHFQPQENWMNDPNGPLFHMGWYHLFYQYNPDSAIWGNITWGHAISRDLINWLHLPFAMQPDQWYDINGVWTGSATVLPDGKIVMLYTGDTDDLVQVQNLAYPANLSDPLLLDWIKYPDNPVMFPPPGIGSTDFRDPTTAWIGRDGKWRITIGSKVNKTGISLMYKTTDFITYELLDNLLHAVPGTG... | Function: May participate in the regulation of the hexose level in mature tissues and in the utilization of sucrose stored in vacuoles.
PTM: N-glycosylated; high-mannose and high-xylose complex glycans.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of terminal non-reducing beta-... |
F8DT27 | MFNFNASRWTRAQAMKVNKFDLTTSMPEIGTDFPIMRDDLWLWDTWPLRDINGNPVSFKGWNVIFSLVADRNIPWNDRHSHARIGYFYSKDGKSWVYGGHLLQESANTRTAEWSGGTIMAPGSRNQVETFFTSTLFDKNGVREAVAAVTKGRIYADSEGVWFKGFDQSTDLFQADGLFYQNYAENNLWNFRDPHVFINPEDGETYALFEANVATVRGEDDIGEDEIGPVPANTVVPKDANLCSASIGIARCLSPDRTEWELLPPLLTAFGVNDQMERPHVIFQNGLTYLFTISHDSTYADGLTGSDGLYGFVSENGIFGP... | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 46100
Sequence Length: 413
Subcellular Location: Secreted
EC: 3.2.1.26
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P42412 | MAEIRKLKNYINGEWVESKTDQYEDVVNPATKEVLCQVPISTKEDIDYAAQTAAEAFKTWSKVAVPRRARILFNFQQLLSQHKEELAHLITIENGKNTKEALGEVGRGIENVEFAAGAPSLMMGDSLASIATDVEAANYRYPIGVVGGIAPFNFPMMVPCWMFPMAIALGNTFILKPSERTPLLTEKLVELFEKAGLPKGVFNVVYGAHDVVNGILEHPEIKAISFVGSKPVGEYVYKKGSENLKRVQSLTGAKNHTIVLNDANLEDTVTNIVGAAFGSAGERCMACAVVTVEEGIADEFMAKLQEKVADIKIGNGLDDG... | Function: Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively.
Catalytic Activity: 3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH
Sequence Mass (Da): 53453
Sequence Length: 487
Pathway: Polyol metabolism; myo-inositol de... |
P42413 | MSYLLRKPQSHEVSNGVKLVHEVTTSNSDLTYVEFKVLDLASGSSYTEELKKQEICIVAVTGKITVTDHESTFENIGTRESVFERKPTDSVYISNDRAFEITAVSDARVALCYSPSEKQLPTKLIKAEDNGIEHRGQFSNKRTVHNILPDSDPSANSLLVVEVYTDSGNWSSYPPHKHDQDNLPEESFLEETYYHELDPGQGFVFQRVYTDDRSIDETMTVGNENVVIVPAGYHPVGVPDGYTSYYLNVMAGPTRKWKFYNDPAHEWILER | Function: Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate).
Catalytic Activity: 5-deoxy-D-glucuronate = 5-dehydro-2-deoxy-D-gluconate
Sequence Mass (Da): 30706
Sequence Length: 271
Pathway: Polyol metabolism; myo-inositol degradation into ac... |
Q5KYR2 | MSRLIIPSHSPNEEGNVVRVTPESVGWEYVGFEVYVLAKGQTLRKETKDQEACLVLLKGKANISTKLERWEQIGLRMDVFEKVPPYSVYVPANDVYEVEAMTDVEVAVCLAPGKGTYPARLIPPSEVGVEIRGAGNIERRVHNILPESQPADSLLVVEVFTPEGNWSSYPPHKHDQDNLPHESYLEETYYHKINPGHGFMVQRVYTDDRSIDETMVVKNGDVVLVPKGYHPVSAPPGYEGYYLNVMAGPVRTWKFHNDPDHDWVMESKLAAKQKEK | Function: Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate).
Catalytic Activity: 5-deoxy-D-glucuronate = 5-dehydro-2-deoxy-D-gluconate
Sequence Mass (Da): 31186
Sequence Length: 276
Pathway: Polyol metabolism; myo-inositol degradation into ac... |
Q9X7U5 | MSELLGVAVLGAGHMGADHIRRVDQVVSGARVAAVADPDAERAKEAVGGIGGTGRITVHTDVEAALDAPGVEAVLIASPGEAHEEALLAAFARGLPVLCEKPMAPNSAGALRVVEAEARLGRRLAQIGFMRRYDAEYRQLKSLLDGGRLGRPLMLHCVHRNVSSPPHFTSAMLINSSVSHEIDAARWLLGQELSAVTVLRPRPSAGAPEGLLDPQLVLFETEGGAVVDVEVFVNCGFGYEVRCEAVCEAGSARIGAAHTMMVTAAGGAREEVPQDYLVRFADAYDREVQSWVDATRRGLVTGPGTWDGYAAAAVAEAGVR... | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 36020
Sequence Length: 342
EC: 1.1.1.18
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Q9WYP5 | MRIGVIGLGRIGTIHAENLKMIDDAILYAISDVREDRLREMKEKLGVEKAYKDPHELIEDPNVDAVLVCSSTNTHSELVIACAKAKKHVFCEKPLSLNLADVDRMIEETKKADVILFTGFNRRFDRNFKKLKEAVENGTIGKPHVLRITSRDPAPPPLDYIRVSGGIFLDMTIHDFDMARYIMGEEVEEVFADGSVLVDEEIGKAGDVDTAVVVLRFKSGALGVIDNSRRAVYGYDQRIEVFGSKGRIFADNVRETTVVLTDEQGDRGSRYLYFFLERYRDSYLEELKTFIKNVKSGEPPAVSGEDGKMALLLGYAAKKS... | Function: Catalyzes the NAD(+)-dependent oxidation of myo-inositol (MI) to 2-keto-myo-inositol (scyllo-inosose), and thus probably functions in a myo-inositol degradation pathway together with IolM, IolN and IolO. Has no activity with scyllo-inositol and much reduced activity (78-fold lower catalytic efficiency) with 1... |
P42419 | MKLCFNEATTLENSNLKLDLELCEKHGYDYIEIRTMDKLPEYLKDHSLDDLAEYFQTHHIKPLALNALVFFNNRDEKGHNEIITEFKGMMETCKTLGVKYVVAVPLVTEQKIVKEEIKKSSVDVLTELSDIAEPYGVKIALEFVGHPQCTVNTFEQAYEIVNTVNRDNVGLVLDSFHFHAMGSNIESLKQADGKKIFIYHIDDTEDFPIGFLTDEDRVWPGQGAIDLDAHLSALKEIGFSDVVSVELFRPEYYKLTAEEAIQTAKKTTVDVVSKYFSM | Cofactor: Binds 1 divalent metal cation per subunit. Can use Mn(2+), Fe(2+) or Co(2+).
Function: Involved in the reversible interconverion of 2-keto-myo-inositol (2KMI, inosose or 2,4,6/3,5-pentahydroxycyclohexanone) to 1-keto-D-chiro-inositol (1KDCI or 2,3,5/4,6-pentahydroxycyclohexanone).
Catalytic Activity: scyllo-i... |
Q5WKY5 | MGFVPMAPLLADAKKDSYAIGQFNINGLQWAKAILAGAESQQSPVIAAASDRLIDYLGGFQTVVAMMGALTDELGITVPVVLHLDHGLSIERCKKAVDAGFSSVMFDGSHYPINENIDMTKEVVAYAHAHNVSVEGEVGTVGGMEDGLMAEIKYADVEECQRFVCETNVDALAAALGSVHGKYKGEPKLGFNEMAAISASTNVPLVLHGASGIPDEQLQRAIKLGHAKININTECMIAWSDACRTTFAEQETAFEPRLLLQEGLAMVQATVEKKIKQFGAANKAAGSASLQRR | Function: Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP).
Catalytic Activity: 6-phospho-5-dehydro-2-deoxy-D-gluconate = 3-oxopropanoate + dihydroxyacetone phosphate
Sequence Mass (Da): 31239
Sequence... |
P42420 | MAFVSMKELLEDAKREQYAIGQFNINGLQWTKAILQAAQKEQSPVIAAASDRLVDYLGGFKTIAAMVGALIEDMAITVPVVLHLDHGSSAERCRQAIDAGFSSVMIDGSHQPIDENIAMTKEVTDYAAKHGVSVEAEVGTVGGMEDGLVGGVRYADITECERIVKETNIDALAAALGSVHGKYQGEPNLGFKEMEAISRMTDIPLVLHGASGIPQDQIKKAITLGHAKININTECMVAWTDETRRMFQENSDLYEPRGYLTPGIEAVEETVRSKMREFGSAGKAAKQQVG | Function: Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP).
Catalytic Activity: 6-phospho-5-dehydro-2-deoxy-D-gluconate = 3-oxopropanoate + dihydroxyacetone phosphate
Sequence Mass (Da): 31372
Sequence... |
Q9WYP3 | MRAVRLHAKWDPRPEFKLGPKDIEGKLTWLGSKVWRYPEVRVEEVPEPRIEKPTEIIIKVKACGICGSDVHMAQTDEEGYILYPGLTGFPVTLGHEFSGVVVEAGPEAINRRTNKRFEIGEPVCAEEMLWCGHCRPCAEGFPNHCENLNELGFNVDGAFAEYVKVDAKYAWSLRELEGVYEGDRLFLAGSLVEPTSVAYNAVIVRGGGIRPGDNVVILGGGPIGLAAVAILKHAGASKVILSEPSEVRRNLAKELGADHVIDPTKENFVEAVLDYTNGLGAKLFLEATGVPQLVWPQIEEVIWRARGINATVAIVARADA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent oxidation of scyllo-inosose (2-keto-myo-inositol) to 3-dehydro-scyllo-inosose (diketo-inositol), and thus probably functions in a myo-inositol degradation pathway together with IolG, IolN and IolO. Has no activity on myo-inositol, D-chi... |
Q9WYP4 | MERPTGVYFQTMTMKQIRERLKQCDLIIIPVGSTENHGPNAPTGEDTFLVTRMAEQVALKTGCTVAEPIWYGYHPYHHIGMPGTVPVKDEAFIDYLVSVIAGFWNTGFRKQILLNGHGQEFVIPIAIHKFAKIFQVPAIIINLNWYHAIQDKFKTKEEGGPYETPFIHADEVETSWSLALFPEFMHQEWAVDTEPKGFLPEGHIDKAGNLLHRPIAWYGHVGGGPIEVVAYPEGVVGKATLASAEKAKEGVEALLDYLEKLVRDIMERFPAGKLPPAEMLSQRPKEELEALTKEPLTEGWRNLYTAGNLWG | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the ring-opening hydrolysis of 3-dehydro-scyllo-inosose (diketo-inositol) to 5-dehydro-L-gluconate, and thus probably functions in a myo-inositol degradation pathway together with IolG, IolM and IolO.
Catalytic Activity: 3-dehydro-scyllo-inosose + H2O = 5-d... |
Q9WYP7 | MKLSLVISTSDAAFDALAFKGDLRKGMELAKRVGYQAVEIAVRDPSIVDWNEVKILSEELNLPICAIGTGQAYLADGLSLTHPNDEIRKKAIERVVKHTEVAGMFGALVIIGLVRGRREGRSYEETEELFIESMKRLLELTEHAKFVIEPLNRYETDFINTIDDALRILRKINSNRVGILADTFHMNIEEVNIPESLKRAGEKLYHFHVADSNRWAPGCGHFDFRSVFNTLKEIGYNRYVSVECLPLPGGMEEAAEIAFKTLKELIIKLT | Cofactor: Binds 1 divalent metal cation per subunit. Mn(2+) is the most efficient metal cofactor, but can also use other divalent metal cations such as Ni(2+), Mg(2+), and, to a lesser extent, Co(2+) and Zn(2+), but not Ca(2+), Cu(2+), and Fe(2+).
Function: Catalyzes the reversible epimerization between 5-keto-L-glucon... |
O34718 | MNKQGNQMSFLRTIILVSTFGGLLFGYDTGVLNGALPYMGEPDQLNLNAFTEGLVTSSLLFGAALGAVFGGRMSDFNGRRKNILFLAVIFFISTIGCTFAPNVTVMIISRFVLGIAVGGASVTVPAYLAEMSPVESRGRMVTQNELMIVSGQLLAFVFNAILGTTMGDNSHVWRFMLVIASLPALFLFFGMIRMPESPRWLVSKGRKEDALRVLKKIRDEKRAAAELQEIEFAFKKEDQLEKATFKDLSVPWVRRIVFIGLGIAIVQQITGVNSIMYYGTEILRNSGFQTEAALIGNIANGVISVLATFVGIWLLGRVGR... | Function: Major myo-inositol uptake transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51633
Sequence Length: 473
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA.
Subcellular Location: Cell membrane
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Q9UHH9 | MSPAFRAMDVEPRAKGVLLEPFVHQVGGHSCVLRFNETTLCKPLVPREHQFYETLPAEMRKFTPQYKGVVSVRFEEDEDRNLCLIAYPLKGDHGIVDIVDNSDCEPKSKLLRWTTNKKHHVLETEKTPKDWVRQHRKEEKMKSHKLEEEFEWLKKSEVLYYTVEKKGNISSQLKHYNPWSMKCHQQQLQRMKENAKHRNQYKFILLENLTSRYEVPCVLDLKMGTRQHGDDASEEKAANQIRKCQQSTSAVIGVRVCGMQVYQAGSGQLMFMNKYHGRKLSVQGFKEALFQFFHNGRYLRRELLGPVLKKLTELKAVLER... | Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5).
Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP
Sequence Mass (Da): 49186
Sequence Length: 426
Pathway: Phospholipid metabolism; phosph... |
Q9R0U1 | MSPAFRTMDVEPRTKGILLEPFVHQVGGHSCVLRFNETTLCKPLVPREHQFYETLPAEMRRFTPQYKGVVSVRFEEDEDRNLCLIAYPLKGDHGPVDIVDNSDCEPKSKLLRWTNKKHHVLETEKSPKDWVRQHRKEEKMKSHKLEEEFEWLKKSEVLYYSVEKKGTVSSQLKHYNPWSMKCHQQQLQRMKENAKHRNQYKFILLENLTCRYEVPCVLDLKMGTRQHGDDASEEKAANQIRKCQQSTSAVIGVRVCGMQVYQAGTGQLMFMNKYHGRKLSVQGFKEALFQFFHNGRYLRRELLGPVLKKLTELKAVLERQ... | Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5).
Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP
Sequence Mass (Da): 49164
Sequence Length: 425
Pathway: Phospholipid metabolism; phosph... |
Q96PC2 | MVVQNSADAGDMRAGVQLEPFLHQVGGHMSVMKYDEHTVCKPLVSREQRFYESLPLAMKRFTPQYKGTVTVHLWKDSTGHLSLVANPVKESQEPFKVSTESAAVAIWQTLQQTTGSNGSDCTLAQWPHAQLARSPKESPAKALLRSEPHLNTPAFSLVEDTNGNQVERKSFNPWGLQCHQAHLTRLCSEYPENKRHRFLLLENVVSQYTHPCVLDLKMGTRQHGDDASEEKKARHMRKCAQSTSACLGVRICGMQVYQTDKKYFLCKDKYYGRKLSVEGFRQALYQFLHNGSHLRRELLEPILHQLRALLSVIRSQSSYR... | Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4.
Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP
Sequence Mass (Da): 46417
Seq... |
Q8BWD2 | MVVRHSSDKGKIGVGVPLEPFLHQVGGHLSVLQYDAYTVCKPLVSQEQKFYESLPLAMKCFTPKYKGTITVRLRRDSRGHLGLVANPLKENLEPFQVSPESRAVALWQTLQQTTGSESSPCPLTQLARSLKESAAKVLLRSDCHLSTQASPLVESEDGSQVERKGFNPWGLHCHQAHLTRLCSQYPEDKRHRFLLLENVVSQYKQPCILDLKMGTRQHGDDASEEKKARHMKKCAQSTSACLGVRICGMQVYQTDQKSFLCKDKYYGRKLSVEGFRQALSQFLHDGTRLRAELLEPILRRLQALLTVIRSQSSYRFYSSS... | Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4 (By similarity).
Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP
Sequence Mass... |
Q83RJ4 | MSIMLPINNNFSLSQNSFYNTISGTYADYFSAWDKWEKQALPGENRNEAVSLLKECLINQFSELQLNRLNLSSLPDNLPPQITVLEITQNALISLPELPASLEYLDACDNRLSTLPELPASLKHLDVDNNQLTMLPELPALLEYINADNNQLTMLPELPTSLEVLSVRNNQLTFLPELPESLEALDVSTNLLESLPAVPVRNHHSEETEIFFRCRENRITHIPENILSLDPTCTIILEDNPLSSRIRESLSQQTAQPDYHGPRIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLS... | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Synthesizes a 'Lys-48'-linked ubiquitin chain, which requires non-covalent binding between ubiquitin and the host ... |
Q8VSC3 | MLPINNNFSLPQNSFYNTISGTYADYFSAWDKWEKQALPGEERDEAVSRLKECLINNSDELRLDRLNLSSLPDNLPAQITLLNVSYNQLTNLPELPVTLKKLYSASNKLSELPVLPPALESLQVQHNELENLPALPDSLLTMNISYNEIVSLPSLPQALKNLRATRNFLTELPAFSEGNNPVVREYFFDRNQISHIPESILNLRNECSIHISDNPLSSHALPALQRLTSSPDYHGPRIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASA... | Function: Effector E3 ubiquitin ligase that interferes with host's ubiquitination pathway and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell . Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), a ubiquitin-binding adapter protein, which results in TNIP1-dependent ... |
A7MB64 | MALGLFRVCLVVVTAIINHPLLFPRENTTVPENEEEIIRQMQAHQEKLQLEQLRLEEEMARLAADKEAEKEALERVAEEGQQQNESRTAWDLWSTLCMILFLVIEVWRQDHQDAPSPECLGSDEDELPDLEGAPLRGLTLPNRATLDHFYERCIRGATADAARTREFVEGFVDDLLEALRSLCSRDSDMEVEDFIGVDSMYENWQVNKPLLCDLFVPFMPPEPYHFHPELWCSSRSVPLDRQGYGQIKVVRADEDTLGCICGKTKLGEDMLCLLHGRNNVVHHGSKAADPLCAPNSPYLDTMRVMKWFQTALTRAWHRIE... | Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63432
Sequence Length: 556
Subcellular Location: Cell membrane
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Q567X9 | MQGAIARVCMVVVAAILNHPLLFPNENTTVPEQDEDLLARMKEHQEKLEAEQKRLEQEISQNETSVIGDQDGYGWYFWSALCLVIFFTIEVCRQDLISAEIPDPAEDEDGDCSTGYHSAKSIALDRGTLNNFCKTRFFPYTNESGRVREFIEGFADDLLEALRSICDLKADLEVEDFAGIGSMFESWRVSKPPTCDLIVPFSPPQPLRFQFELWCDPSTEIPLDLQGCGRIQLIKPGGNGTDCLCGSIDLGDDMLCLLHNRNECEVLEDDALPELLCARDTTYLSKGQIMRWFQISVSKAWGKISHKYDFELAFRNLDFP... | Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 61362
Sequence Length: 539
Subcellular Location: Cell membrane
|
Q8IWB1 | MAMGLFRVCLVVVTAIINHPLLFPRENATVPENEEEIIRKMQAHQEKLQLEQLRLEEEVARLAAEKEALEQVAEEGRQQNETRVAWDLWSTLCMILFLMIEVWRQDHQEGPSPECLGGEEDELPGLGGAPLQGLTLPNKATLGHFYERCIRGATADAARTREFLEGFVDDLLEALRSLCNRDTDMEVEDFIGVDSMYENWQVDRPLLCHLFVPFTPPEPYRFHPELWCSGRSVPLDRQGYGQIKVVRADGDTLSCICGKTKLGEDMLCLLHGRNSMAPPCGDMENLLCATDSLYLDTMQVMKWFQTALTRAWKGIAHKYE... | Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 62060
Sequence Length: 547
Subcellular Location: Cell membrane
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Q3TNL8 | MAMELFRVCLVVVTAIINHPLLFPRENATIPENEEEIIRKMQEHQEKLRLEQLRLEEEVSRLEAEKEALRQVEEEQQQLEAHTAWDLWTTLCMVLFLIIEVLRQNHQEGTFPECLGGDEDELSGLGGTLLQGLPLPNRATLDHFYEHCIRSTTGDATRTQEFVEGFVDDLLEALRSTYNGKTDMELEDFIGVGSMYENWQVERPLRCHLFIPFIPPEPYSFHPEFWCSSLSTPLERQGYGQIKVTLADGNPLGCVCGKAKLEEDMLCLLYGKNRGAWPSSAGCGEMEGLLCSRESSYLDVMQVMKWFQMALTRAWHRIAH... | Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63238
Sequence Length: 555
Subcellular Location: Cell membrane
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P05154 | MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPS... | Function: Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a pr... |
P70458 | MRFFPILCLVLFISHGVASRRHSHSKKKKAKESSVGAVGPPSSKDFAFRLYRALVSESPGQNVFFSPLSVSMSLGMLSLGAGLKTKTQILDGLGLSLQQGQEDKLHKGFQQLLQRFRQPSDGLQLSLGSALFKDPAVHIRDDFLSAMKTLYMSDTFSTNFGNPEIAKKQINNYVAKQTKGKIVDFIKDLDSTHVMIVVNYIFFKAKWQTAFSETNTHKMDFHVTPKRTTQVPMMNREDGYSYYLDQNISCTVVGIPYQGNAIALFILPSEGKMKQVEDGLDERTLRNWLKMFTKRRLDLYLPKFSIEATYKLENVLPKLG... | Function: Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a pr... |
Q94ID3 | MTELNFHLLPIISDRFTTTTTTSPSFSSHSSSSSSLLSFTKRRRKHQPLVSSIRMEQSRSRNRKDKVVVILGATGAGKSRLSVDLATRFPSEIINSDKIQVYEGLEITTNQITLQDRRGVPHHLLGVINPEHGELTAGEFRSAASNVVKEITSRQKVPIIAGGSNSFVHALLAQRFDPKFDPFSSGSCLISSDLRYECCFIWVDVSETVLYEYLLRRVDEMMDSGMFEELSRFYDPVKSGLETRFGIRKAIGVPEFDGYFKEYPPEKKMIKWDALRKAAYDKAVDDIKRNTWTLAKRQVKKIEMLKDAGWEIERVDATAS... | Function: Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP, ADP and AMP. Adenine, adenosine, isopentenylpyrophosphate and 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBDP) are not used as substrates.
Catalytic Activity: AMP + dimethyla... |
Q15306 | MNLEGGGRGGEFGMSAVSCGNGKLRQWLIDQIDSGKYPGLVWENEEKSIFRIPWKHAGKQDYNREEDAALFKAWALFKGKFREGIDKPDPPTWKTRLRCALNKSNDFEELVERSQLDISDPYKVYRIVPEGAKKGAKQLTLEDPQMSMSHPYTMTTPYPSLPAQQVHNYMMPPLDRSWRDYVPDQPHPEIPYQCPMTFGPRGHHWQGPACENGCQVTGTFYACAPPESQAPGVPTEPSIRSAEALAFSDCRLHICLYYREILVKELTTSSPEGCRISHGHTYDASNLDQVLFPYPEDNGQRKNIEKLLSHLERGVVLWMA... | Function: Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dend... |
Q64287 | MNLETGSRGSEFGMSAVSCGNGKLRQWLIDQIDSGKYPGLVWENEEKSVFRIPWKHAGKQDYNREEDAALFKAWALFKGKFREGIDKPDPPTWKTRLRCALNKSNDFEELVERSQLDISDPYKVYRIVPEGAKKGAKQLTLDDTQMAMGHPYPMTAPYGSLPAQQVHNYMMPPHDRSWRDYAPDQSHPEIPYQCPVTFGPRGHHWQGPSCENGCQVTGTFYACAPPESQAPGIPIEPSIRSAEALALSDCRLHICLYYRDILVKELTTTSPEGCRISHGHTYDVSNLDQVLFPYPDDNGQRKNIEKLLSHLERGLVLWMA... | Function: Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dend... |
Q13568 | MNQSIPVAPTPPRRVRLKPWLVAQVNSCQYPGLQWVNGEKKLFCIPWRHATRHGPSQDGDNTIFKAWAKETGKYTEGVDEADPAKWKANLRCALNKSRDFRLIYDGPRDMPPQPYKIYEVCSNGPAPTDSQPPEDYSFGAGEEEEEEEELQRMLPSLSLTEDVKWPPTLQPPTLRPPTLQPPTLQPPVVLGPPAPDPSPLAPPPGNPAGFRELLSEVLEPGPLPASLPPAGEQLLPDLLISPHMLPLTDLEIKFQYRGRPPRALTISNPHGCRLFYSQLEATQEQVELFGPISLEQVRFPSPEDIPSDKQRFYTNQLLDV... | Function: Transcription factor that plays a critical role in innate immunity by activating expression of type I interferon (IFN) IFNA and INFB and inflammatory cytokines downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9 . Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN... |
Q08DD6 | MALHPRRVRLKPWLVAQVDSGLYPGLIWLHRDSKRFQIPWKHATRHSPQQEEENTIFKAWAVETGKYQEGVDDPDPAKWKAQLRCALNKSREFNLMYDGTKEVPMNPVKIYQVCDIPQPQGSIINPGSTGSAPWDEKDNDVDEEDEEDELDQSQHHVPIQDTFPFLNINGSPIAPASVGNCSVGNCSPEAVWPKTEPLEMEVPQAPIQPFYSSPELWISSLPMTDLDIKFQYRGKEYGQTMTVSNPQGCRLFYGDLGPMPDQEELFGPVSLEQVKFPGPEHITNEKQKLFTSKLLDVMDRGLILEVSGHAIYAIRLCQCK... | Function: Probable DNA-binding transcriptional activator. It is a key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development. Plays a role in regulating mammary epithelial cell proliferation (By similarity). May regulate WDR65 transcription (By similarity).
PT... |
O14896 | MALHPRRVRLKPWLVAQVDSGLYPGLIWLHRDSKRFQIPWKHATRHSPQQEEENTIFKAWAVETGKYQEGVDDPDPAKWKAQLRCALNKSREFNLMYDGTKEVPMNPVKIYQVCDIPQPQGSIINPGSTGSAPWDEKDNDVDEEDEEDELDQSQHHVPIQDTFPFLNINGSPMAPASVGNCSVGNCSPEAVWPKTEPLEMEVPQAPIQPFYSSPELWISSLPMTDLDIKFQYRGKEYGQTMTVSNPQGCRLFYGDLGPMPDQEELFGPVSLEQVKFPGPEHITNEKQKLFTSKLLDVMDRGLILEVSGHAIYAIRLCQCK... | Function: Probable DNA-binding transcriptional activator. Key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development (By similarity). Plays a role in regulating mammary epithelial cell proliferation (By similarity). May regulate WDR65 transcription (By similar... |
Q92985 | MALAPERAAPRVLFGEWLLGEISSGCYEGLQWLDEARTCFRVPWKHFARKDLSEADARIFKAWAVARGRWPPSSRGGGPPPEAETAERAGWKTNFRCALRSTRRFVMLRDNSGDPADPHKVYALSRELCWREGPGTDQTEAEAPAAVPPPQGGPPGPFLAHTHAGLQAPGPLPAPAGDKGDLLLQAVQQSCLADHLLTASWGADPVPTKAPGEGQEGLPLTGACAGGPGLPAGELYGWAVETTPSPGPQPAALTTGEAAAPESPHQAEPYLSPSPSACTAVQEPSPGALDVTIMYKGRTVLQKVVGHPSCTFLYGPPDPA... | Function: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses . Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulat... |
P70434 | MAEVRGVQRVLFGDWLLGEVSSGQYEGLQWLNEARTVFRVPWKHFGRRDLDEEDAQIFKAWAVARGRWPPSGVNLPPPEAEAAERRERRGWKTNFRCALHSTGRFILRQDNSGDPVDPHKVYELSRELGSTVGPATENREEVSLSNALPTQGVSPGSFLARENAGLQTPSPLLSSDAGDLLLQVLQYSHILESESGADPVPPQAPGQEQDRVYEEPYAAWQVEAVPSPRPQQPALTERSLGFLDVTIMYKGRTVLQAVVGHPRCVFLYSPMAPAVRTSEPQPVIFPSPAELPDQKQLHYTETLLQHVSPGLQLELRGPSL... | Function: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses . Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulat... |
Q02556 | MCDRNGGRRLRQWLIEQIDSSMYPGLIWENEEKSMFRIPWKHAGKQDYNQEVDASIFKAWAVFKGKFKEGDKAEPATWKTRLRCALNKSPDFEEVTDRSQLDISEPYKVYRIVPEEEQKCKLGVATAGCVNEVTEMECGRSEIDELIKEPSVDDYMGMIKRSPSPPEACRSQLLPDWWAQQPSTGVPLVTGYTTYDAHHSAFSQMVISFYYGGKLVGQATTTCPEGCRLSLSQPGLPGTKLYGPEGLELVRFPPADAIPSERQRQVTRKLFGHLERGVLLHSSRQGVFVKRLCQGRVFCSGNAVVCKGRPNKLERDEVVQ... | Function: Transcription factor that specifically binds to the upstream regulatory region of type I interferon (IFN) and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) . Can both act as a transcriptional activator or repressor (By similarity). Plays a negative regulatory role in cells of the i... |
P23611 | MCDRNGGRRLRQWLIEQIDSSMYPGLIWENDEKTMFRIPWKHAGKQDYNQEVDASIFKAWAVFKGKFKEGDKAEPATWKTRLRCALNKSPDFEEVTDRSQLDISEPYKVYRIVPEEEQKCKLGVAPAGCMSEVPEMECGRSEIEELIKEPSVDEYMGMTKRSPSPPEACRSQILPDWWVQQPSAGLPLVTGYAAYDTHHSAFSQMVISFYYGGKLVGQATTTCLEGCRLSLSQPGLPKLYGPDGLEPVCFPTADTIPSERQRQVTRKLFGHLERGVLLHSNRKGVFVKRLCQGRVFCSGNAVVCKGRPNKLERDEVVQVF... | Function: Transcription factor that specifically binds to the upstream regulatory region of type I interferon (IFN) and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) . Can both act as a transcriptional activator or repressor . Plays a negative regulatory role in cells of the immune system . ... |
Q00978 | MASGRARCTRKLRNWVVEQVESGQFPGVCWDDTAKTMFRIPWKHAGKQDFREDQDAAFFKAWAIFKGKYKEGDTGGPAVWKTRLRCALNKSSEFKEVPERGRMDVAEPYKVYQLLPPGIVSGQPGTQKVPSKRQHSSVSSERKEEEDAMQNCTLSPSVLQDSLNNEEEGASGGAVHSDIGSSSSSSSPEPQEVTDTTEAPFQGDQRSLEFLLPPEPDYSLLLTFIYNGRVVGEAQVQSLDCRLVAEPSGSESSMEQVLFPKPGPLEPTQRLLSQLERGILVASNPRGLFVQRLCPIPISWNAPQAPPGPGPHLLPSNECV... | Function: Transcription factor that plays an essential role in anti-viral immunity. It mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associ... |
A6NK06 | MMLKSITESFATAIHGLKVGHLTDRVIQRSKRMILDTLGAGFLGTTTEVFHIASQYSKIYSSNISSTVWGQPDIRLPPTYAAFVNGVAIHSMDFDDTWHPATHPSGAVLPVLTALAEALPRSPKFSGLDLLLAFNVGIEVQGRLLHFAKEANDMPKRFHPPSVVGTLGSAAAASKFLGLSSTKCREALAIAVSHAGAPMANAATQTKPLHIGNAAKHGIEAAFLAMLGLQGNKQVLDLEAGFGAFYANYSPKVLPSIASYSWLLDQQDVAFKRFPAHLSTHWVADAAASVRKHLVAERALLPTDYIKRIVLRIPNVQYVN... | Function: Cis-aconitate decarboxylase that catalyzes production of itaconate and is involved in the inhibition of the inflammatory response . Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expres... |
P54987 | MMLKSVTESFAGMIHGLKVNHLTDGIIRRSKRMILDSLGVGFLGTGTEVFHKVTQYSKIYSSNTSSTVWGRPDFRLPPTYAAFVNGVAVHSMDFDDTWHPATHPSGAVLPVLTALSEALPQIPKFSGLDLLLAFNVGIEVQGRLMHFSKEAKDIPKRFHPPSVVGTLGSAAAASKFLGLSLTKCREALAIAVSHAGAPIANAATQTKPLHIGNAAKHGMEATFLAMLGLQGNKQILDLGSGFGAFYANYSPEDLPSLDSHIWLLDQQDVAFKSFPAHLATHWVADAAAAVRKHLVTPERALFPADHIERIVLRIPDVQYV... | Function: Cis-aconitate decarboxylase that catalyzes production of itaconate and is involved in the inhibition of the inflammatory response . Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expres... |
A5F9G0 | MSRFNPSPVSLSVTLGLMFSASAFAQDATKTDETMVVTAAGYAQVIQNAPASISVISREDLESRYYRDVTDALKSVPGVTVTGGGDTTDISIRGMGSNYTLILVDGKRQTSRQTRPNSDGPGIEQGWLPPLQAIERIEVIRGPMSTLYGSDAIGGVINIITRKDQQQWSGNVQLSTVVQENRASGDEQSANFFVTGPLSDALSLQVYGQTTQRDEDEIEHGYGDKSLRSLTSKLNYQLNPDHQLQLEAGVSAQDRENNVGKSAQSSGCRGTCSNTDNQYRRNHVAVSHQGDWQGVGQSDTYLQYEENTNKSREMSIDNTV... | Function: Involved in the initial step of iron uptake by binding ferric vibriobactin, an iron chelatin siderophore that allows V.cholerae to extract iron from the environment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71641
Sequence Length: 652
Subcellular Location: Cell outer membrane
|
Q3IFI3 | MKLPIYLDYAATTPVDERVAKEMMQCLTMDGNFGNPASRSHRFGWQAEEVVDQARTDVADLINADPREIVFTSGATESNNLAIKGAAQFYKKKGKHIITAKTEHKAVIDTCRELERQGFEVTYMDVEENGLLDLQKLADTMRDDTVLVSIMHVNNELGVIQDIATIGEMCRERKIMFHVDAAQSAGKVLIDVQQLKVDFMSFSGHKVYGPKGVGALYVRRKPRARLEAQMHGGGHERGMRSGTLATHQLVGMGTAFRVAKQDFEKDHAHISALRKRLIDGIMSDMEEVYFNGTQDQSVPGIVNISFNFVEGESLLMAVKD... | Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaff... |
Q1RHY6 | MNTQLNNLILPIYMDYQATTPLDPRVMEAMLPYFTTKFGNPHSHSHSFGWEAENAVEEARGDIAKLIGAEAKEIIFTSGATESNNLAIKGIAKFYGNKKNHIITVVSEHKCVLDACRHLEQEGVKVTYLPIKPNGIIDLEVLKNAITDQTMLVSVMAVNNEIGVIQPLKEIGKICREKGVFFHSDSAQGFGKVPIDVNECNIDLASISGHKIYGPKGIGALYVRKKPRVRITPLINGGGQERGMRSGTLPTPLIVGLGTAANIAYNEMEKDTKHVNHLFDKFLDAINSQISEVYLNGDKDQRYKGNLNLSFAGVEGESII... | Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaff... |
Q4UL77 | MNPQLNNPNLPIYMDYQATTPLDPRVMEAMLPYFTTKFGNPHSRSHSFGWEAENAVEEARSRVARLIGADTKEIIFTSGATESNNLAIKGIAKFYGNKKNHIITVVSEHKCVLDACRHLEQEGIKITYLPIKPNGIIDLETLKNAITDQTMLVSVMAVNNEIGVVQPLKEIGKICRERGVFFHSDIAQGFGKIPIDVNEFNIDLASISGHKIYGPKGIGALYVRKKPRVRVTPLINGGGQERGMRSGTLPTPLIVGLGMAAEIAYSVMEKDTKHVNYLFDRFLNNIHNRISEVYLNGDKNQRYKGNINLSFAGVEGESII... | Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaff... |
Q2FXJ2 | MNKHHPKLRSFYSIRKSTLGVASVIVSTLFLITSQHQAQAAENTNTSDKISENQNNNATTTQPPKDTNQTQPATQPANTAKNYPAADESLKDAIKDPALENKEHDIGPREQVNFQLLDKNNETQYYHFFSIKDPADVYYTKKKAEVELDINTASTWKKFEVYENNQKLPVRLVSYSPVPEDHAYIRFPVSDGTQELKIVSSTQIDDGEETNYDYTKLVFAKPIYNDPSLVKSDTNDAVVTNDQSSSVASNQTNTNTSNQNISTINNANNQPQATTNMSQPAQPKSSTNADQASSQPAHETNSNGNTNDKTNESSNQSDVN... | Function: Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 100947
Sequence Length: 895
Domain: The NEAT 1 domain binds with higher... |
A7I1V2 | MKDITLVLLAAGDSTRFKAPFKKQWIRIGEIPLWQYVAKDLSQKCDFSDIIIVANEKEISYMKKIERNFKYAKGGKLRQNSLANALKKVKSEFVFVSDTARAEISKDLIGRLINECEKFDCVSPFLGVVDTTYLGRNQIDRNDLKLIQTPQISRANLLKKALESNEIFTDDSAAVAFAGGKLGFVEGDEKARKITFTSDLAHFDFTPASGTIFTGNGFDVHAFAKGEFITLGGVKIPCEYSLVGHSDADAAIHALMDAILGACGLGDIGELFPDTDDSFKGIDSKILLQKVVNFVHLLGFKIINADITIIAQKPKISPYK... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q9PM68 | MSEMSLIMLAAGNSTRFNTKVKKQFLRLGNDPLWLYATKNLSSFYPFKKIVVTSSNITYMKKFTKNYEFIEGGDTRAESLKKALELIDSEFVMVSDVARVLVSKNLFDRLIENLDKADCITPALKVADTTLFDNEALQREKIKLIQTPQISKTKLLKKALDQNLEFTDDSTAIAAMGGKIWFVEGEENARKLTFKEDLKKLDLPTPSFEIFTGNGFDVHEFGENRPLLLAGVQIHPTMGLKAHSDGDVLAHSLTDAILGAAGLGDIGELYPDTDMKFKNANSMELLKQAYDKVREIGFELINIDICVMAQSPKLKDFKQA... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q9A7I5 | MTFSVVIVAAGSGTRAGPGQAKQWRVLAGRPVLRWSVEAFLAAGAAEVVVVTTADGEAFLPRMLEGLQGWRSTLGGATRALSVQAGLAALSERPGAEPVMIHDAARPFVSRNVILALLGALSDADLALPALAVADTLKRQPTGEAAQTVSREHLWRAQTPQAARRDTLIAAYAAWTHGEPTDDAQVVEAAGGRIALTAGDPLLTKLTYPEDFAMAEHLAGVARVTRVGQGFDAHRWGPGEEVWLCGVAIKHDETLVGHSDADAGLHALTDAILGAIGEGDIGDHFPPTDPKWKGAASDQFLKHAVDLVTAKGGALVNVDV... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
A5CTY4 | MSHDPVVPSAPATDGGATDGPRLGVVVVAAGSGTRLGAGIPKALVEVGGVTLLARSLSSVLGLAEEAHVVVVAPDTHLAETSAVVDAVAGAARGSVAVVVGGATRQGSVRAGLAALVGSVDTVLVHDAARALTPTDLFAAVARAVRAEGAGVVPGLPVTDTVKRVDPAGECLGTVDRSDLVGVQTPQGFPRAALDAAYARAAAEHTDDAALFQASGGRVRVIPGDALAFKVTTAWDLRRAEELVARDAGAGSASSRLRSGIGTDVHAVDASQPLWLAGLHWPGEAGLAGHSDGDAVSHAMCDALLSAAGLGDIGGIFGTD... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
B1GYT4 | MKNAAIIAAAGSGKRFGSRVSKQFLNLSGKPVFLWSVEAFASIKSFKQIIVVVPSDMVEFLSLKYKTGFVCATGGNERFDSVKNGLALVGDDIDFIAVHDASRPLISKKDILLVLEKAAKTKVAVAVEKAKDTVKLVSADGYILKTLDRTILRNAQTPQIFKTELLKRAYSRKMSAGTTDDSQLVENLKIKVSAVETKFLNFKITTKQDFELAEKILKS | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 24065
Sequence Length: 219
Pathway: Isoprenoid bi... |
Q2J542 | MGEGHRLPVASPRVAAIVPAAGRGERLGGGTPKALRALGGRPMLVRTVESLRRSRLVTQIVVAAPPTLVDAVAQLLGGDVYVIAGGAERVDSVRRALRAVDDDVSVVLVHDAARPLTPPELVDAVAAAVLDGHPAVIPVVPLADTVKEVDADGRVVRTPPRDGLRAVQTPQGFRRDVLSAAYALEDIAVTDDAGLVEALGVPVTTIPGAQEAFKVTRPADLVLAEALLARCDPADDARSAEARSAEARSEEPQFAGARSTDARSGG | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 27498
Sequence Length: 266
Pathway: Isoprenoid bi... |
Q8R6H2 | MYSSNSEIKKKVTFILAAAGQGKRMNLNSPKQFLDYRGEPLFYSSLKLAFENKNINDIIIITNKENLNFMVKYCQNKNLFSKVKYIVEGGSERQYSIYNAIKKIKDTDIVIIQDAARPFLKDKYIEESLKILNDDCDGAIIGVKCKDTIKIIDENGIVLETPNRDNLIMVHTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKIKIIYGDYDNIKITVQEDLKFLK | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 26491
Sequence Length: 231
Pathway: Isoprenoid bi... |
Q9KUJ2 | MNNMTAIVPAAGVGSRMQADRPKQYLTLLDKTVLEHTVEHLLEHPLIEHVVVAVSADDPYFANLPLAHHPRVIRVDGGKERADSVLSALEYVCQHRLSEWVLVHDAARPCVTHADITQLITTALAHPIGAILASPVRDTMKRGDHLQQIVHTVDRTALWHALTPQMFRAQSLRERLFAALQQQVTITDEASAFEWRGEKPALVAGRADNLKITQPEDLALAEFYLSRNKEKS | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25902
Sequence Length: 232
Pathway: Isoprenoid bi... |
Q8PLR8 | MTGSIWAIVPAAGRGTRFGGPLPKQYLQAGGQPLMAYTLAALAAHPALAGIMVAIAPGDADWPGWTAVQSKPVLTCLGGATRAASVLSGLLALPESVRADDFVLVHDAARPNLALADLDRLLEIGRGDPVGAILAAPVRDTLKRAGDDGGIDGTEPRERLWRALTPQLFRRHQLIRGLTEASAAGVEVTDEAMAMERIGLRPLLVEGAEDNFKVTTPADLARFEFELANRDCGPGTRDPESAHPQSSVSASAFSGPGSRAPGPEEI | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 27793
Sequence Length: 266
Pathway: Isoprenoid bi... |
Q6AAD6 | MTVTVRVSAKVNLALGVGGLAPDGFHPLATVFEAICIYDEVAVTRRDDSRITLTVSGEDADQVPTDETNLAWRAVELVREEFASEWGKRGHGADIHIDKSIPVAGGMAGGSADAAGALMAAAALCRLPYSPEELQPLAAQLGSDVPFCLTGGVALGRGRGDRLAPVICRGRHRWVFATSNQGLSTPAVYRRFDELGGTPGGETVPNDLISALTRGDLDAVAASLSNDLQAAAIDLRPELEEVLTVGREVGALTALVSGSGPTCAFLVRDTAGAKKVSAAVSNLPQVHRTRTARGPAAGAQLLPGPVGSFA | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 32024
Sequence Length: 310
Pathway: Isoprenoid biosynthesis; isopente... |
Q11VT3 | MISFPNAKINLGLSVLSKRPDGYHNIETCFYPIPWNDMLEIIPAKETVFTSSGNNIPGTSASNLCLKTYTLLKEKYPLSPVHIHLHKRIPIGAGLGGGSSDAAFTCKLLNDVFALKLSAAEMEDIVRPVGSDCAFFIENTSILAHEKGDYFSHPGIVNLSGKWIYLIHPGIHVATKEAYDGVVPNTDRKPIGDILKQPLSVWKAELVNDFERSVFEKYPAIKTLKEQMYKQGAAYAAMSGSGSTVFGIFNTKPETFHENTSNIQSCIAPL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 29635
Sequence Length: 270
Pathway: Isoprenoid biosynthesis; isopente... |
Q3Z9E9 | MLTLLAPAKVNLSLEVLYRRNDGYHELRSIIQSLSLCDRLSFSPAKTVQISSDSPDWQAEHSLVSKAVALFSEKCGQGRGVNLTIAKRIPLVSGLGGDSSCAAAVLKGLNKLWGCGYPRWRLMELGAELGSDVPFFMMGGTAMMEGRGETVTPLPTLNQMWAVLLVPEIEMPPDKTAALYRNLHADSFSSGEISDKLLEDICQGKLSYSSCFNVFEKIAFTLFPDLAKYRWQFLEAGAYQIFLAGAGPTLFTLLKDKNMAEKIYHNLCQKGHQAYLVSTLGPLD | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31235
Sequence Length: 284
Pathway: Isoprenoid biosynthesis; isopente... |
Q9RR89 | MTHQPSPVIHHHFAPAKINLGLSVLGVRENGYHDLHSLMVPLTVGDELEIRPAGALTLRVEGADLPTDERNLVYRAARAYLDAAGAAGGADLVLHKRLPLASGLGGGSSDAASTLLALAELYPAPDHRPVDLPALALTLGADVPFFLLGGAALAEGVGERLTPVDDLPPVHLVLANAGAEVSAGDAYRWLDETGDFSGKLRLEAMRLALARGVEVPYFNSLQAGVLARVPSVLTTLEALADAGLHSVLMSGSGATCFGLAHDAAQAQAAAAALAQRCPGWWVTAAQVRLPLSDNSGGRT | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30919
Sequence Length: 299
Pathway: Isoprenoid biosynthesis; isopente... |
Q251V5 | MIRNQVEMFAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAEGGIQCSCGEWSGPENLAYRAAEAFLSGLGSSQGIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAPKINLVLIKPDQGVNTAEAYRAFDQEGKFSHLDYAGWQEALASGRAESLIPLLYNDLEPASMKLLPEIAWVKEELMKQNGCLGALMSGSGSAVFGIVQTEEQAEKIAAIWRERNYHVWVTHTMERGNIYG | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31504
Sequence Length: 290
Pathway: Isoprenoid biosynthesis; isopente... |
Q6AJL6 | MDRNEGELAQVATRLHMRAPAKVNLSLQVLSRRADGYHDLATHMQKVSLYDELELCLTKQSGVSLVCSDGDIPLDEKNLAVRAALAYLARSSRVGQRGVRISLEKNIPVGAGLGGGSSDAGTVLRGLNQLLDNEFSEEELIEMARPLGADVPFFASEMSAAFATGIGDILQPLESTKEFDFILVNPGIFISTKEIFERFSLTLSPKRNIFARPFRVHERASLLDYMHNDLEEIVSDLCPAIDEMKSLLEANGASAVMMSGSGSTVFGVFQRSVGQKKINQVCKVLSCKYGEKVFAVQAV | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 32616
Sequence Length: 299
Pathway: Isoprenoid biosynthesis; isopente... |
A4J0P1 | MGIRLKAHGKINLTLDVLDRRPDGYHEVEMIMQSISLHDVLEIEEQSKEISLTVSGISVTAEEDNLVLKAARLLQQVAGTGAGAKIHLQKNIPVAAGLAGGSTDAAATLKGLNALWGLGLSQEQLRQLATQLGADVPFCLAGGTAIARGIGEKLTTLEPAPPFGIILVKPSFGVSTAEVYQGLRLEHLGKRPNTEAMVKALKERDLGQVARELANVLESVTLRMHPKLEQIKEILRQIGCTGVLMSGSGPTVFGLTENREKAAELISGLPQAGCHVLAAWMV | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 29982
Sequence Length: 282
Pathway: Isoprenoid biosynthesis; isopente... |
Q72BQ8 | MNDAVTLRSGCKVNLDLHITSRRDDGYHEIDSLFLPLEEPHDELVVTVGDAPGITVTCAIQGIDPTRNTVTRAYDAYAEASGFRPPLRVELRKGVPHGAGLGGGSANAAAILNHLESIAPHPLGRETLCRLAARIGADVPFFIHAVPCRASGIGEIITPVAWPYKGFTLLLACPQVQVSTAWAYGALDAAEEKQLRVRGCLTTGGVADRNSFSRESWLHNSFEPVVFASHPELRSLKEALLRHGAAAALMSGSGASVFALFRRREDAEAAFEQLKGHGIRVYQHLL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30819
Sequence Length: 286
Pathway: Isoprenoid biosynthesis; isopente... |
A2BWR1 | MTKLSTTKICVKSPAKINLHLEIIGKREDGYHELAMIMQNIDLFDYIEFENNQIGDIELKSNNKDLSLKDDNLIIKAANYVKDISKKKDLGANIFLKKNIPIGAGLAGGSSNAAATIIGLNKLWDLDLDNETMLSLSSKLGSDVPFFINGGCQFCFGRGEILENYNSKFDYGVILLKNPNISISTADTYKKYSKEYCSNFLTESEKTNDIRNDLRINGFNDLNSSNQIIKVKNDLQIIVEKENDSVKKALYLLSNLQNCLSFSMSGSGPTCFALFKDINKANEVFEQNHKMFNNNGFEAWVCKLINSGITFL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 34941
Sequence Length: 312
Pathway: Isoprenoid biosynthesis; isopente... |
Q46L57 | MVPSKANEDFLIANAHAKINLHLEVLGIRSDGFHELAMVMQSINLSDQLKMIKRVDNTINLKSNNKEISNGDDNLIIKAAKLLRNKVENQELGVDIELEKNIPIGAGLAGGSTDAAATLLGLNKLWKLNLKIDELENLSKEIGSDIPFCISGGRQICFGRGEILEKLKFDQIQLGLVLVKDPSIQVSTPVAYKKYKEQFGESYLEDDRDFEIKRNSIRSIDWSDQSLFDNRKEIQNDLQKSIRPMTPEVEKSLNLLSSLPDSRLVSMSGSGPSCFALFQNYDQANKVLKEHVNEFERAGLSAWACSMMSNGVELRNEFT | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 35688
Sequence Length: 319
Pathway: Isoprenoid biosynthesis; isopente... |
P42805 | MSVRLSLPAPAKLNLFLHILGRRDDGYHELQTLFQFLDHGDELHFEARQDGQVRLHTEIAGVPHDSNLIVRAARGLQEASGSPQGVDIWLDKRLPMGGGIGGGSSDAATTLLALNHLWQLGWDEDRIAALGLRLGADVPVFTRGRAAFAEGVGEKLTPVDIPEPWYLVVVPQVLVSTAEIFSDPLLTRDSPAIKVRTVLEGDSRNDCQPVVERRYPEVRNALILLNKFVSARLTGTGGCVFGSFPNKAEADKVSALLPDHLQRFVAKGSNISMLHRKLETLV | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30843
Sequence Length: 282
Pathway: Isoprenoid biosynthesis; isopente... |
Q9CAK8 | MATSSTQLLLSSSSLFHSQITKKPFLLPATKIGVWRPKKSLSLSCRPSASVSAASSAVDVNESVTSEKPTKTLPFRIGHGFDLHRLEPGYPLIIGGIVIPHDRGCEAHSDGDVLLHCVVDAILGALGLPDIGQIFPDSDPKWKGAASSVFIKEAVRLMDEAGYEIGNLDATLILQRPKISPHKETIRSNLSKLLGADPSVVNLKAKTHEKVDSLGENRSIAAHTVILLMKK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP. Is essential for chloroplast development.
Catalytic Activi... |
Q5NYK0 | MKAPFRIGQGFDVHALVPGRALIVGGVHIPFERGLLGHSDADVLLHALTDALLGAAGLGDIGRLFPDTDAAHAGADSRVLLREAFAAVRAAGFGVVNVDATVICRAPRILPHAPAMVANIAADLGIDAAAVNIKGKTTEKLGFTGRGEGIAAQVVALLMRHGDET | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
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