ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q668V1 | MGASATNSVTHPAFTLNVRPDNIGIITIDVVGDKVNTLKAEFADQIATILQQAHALPKLQGLVIVSGKPDSFIAGADITMIAACRTAHDARVLAQKGQSILAQIAAFPVPVVAAIHGACLGGGLELALACHSRICSLDDKTVLGLPEVQLGLLPGSGGTQRLPRLVGVSKALDMILTGKQIRPRQALKMGLVDDVVPRDILLDVAIQRAKAGWLNRRALPWQERLLSGPLGKALLFRIVRKKTLAKTRGHYPAAERIIDVVRKGLDQGGPSGYEAEARAFGELAMSPQSAALRSLFFATTSLKKETGSAATARAIHRVGVLGGGLMGGGIANVTATRAGLPVRIKDINPQGINQALKYTWDALGKRVRSKRMRPTEQQRQMMLISGSTDYRGFERVDIVVEAVFEDLSLKQQMVADIERFGAAHTIFASNTSSLPISQIAALAQRPEQVIGLHYFSPVDKMPLVEVIPHEKTSEETIATTVALARKQGKTAIVVADRAGFYVNRILAPYINEAARCLLDGEPIESVDNALVDFGFPVGPMMLLDEVGIDVATKIMPILVEQLGPRFAAPPSFDVILKDGRKGRKNGRGFYLYSNPTLHSNSTKNSSPTKNGNSPAKRNSFKWRKNKVKPVDSSIYTLLGVTPKAHLGAGVITQRCTMLMLNEAVRCLDESIIRNPRDGDIGAVFGIGFPPFLGGPFRYLDSLGADKVVQALRLLVQQYGERFEPCQRLVTMAEQQQQFYPVDANIDEVTDVAS | Function: Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 81350
Sequence Length: 753
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Cytoplasm
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P38135 | MHPTGPHLGPDVLFRESNMKVTLTFNEQRRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLTQDVCEEIE | Function: Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Is maximally active on C6:0, C8:0 and C12:0 fatty acids, while has a low activity on C14-C18 chain length fatty acids . Is involved in the anaerobic beta-oxidative degradation of fatty acids, which allows anaerobic growth of E.coli on fatty acids as a sole carbon and energy source in the presence of nitrate or fumarate as a terminal electron acceptor . Can functionally replace FadD under anaerobic conditions .
Catalytic Activity: ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62759
Sequence Length: 566
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Cell membrane
EC: 6.2.1.-
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B4YQU1 | MASATPAMSENAVLRHKAASTTGIDYESSAAVSPAESPRTSASSTSLSSLSSLDANEKKDEYAGLLDTYGNAFTPPDFSIKDIRAAIPKHCYERSTIKSYAYVLRDLLCLSTTFYLFHNFVTPENIPSNPLRFVLWSIYTVLQGLFATGLWVIGHECGHCAFSPSPFISDLTGWVIHSALLVPYFSWKFSHSAHHKGIGNMERDMVFLPRTREQQATRLGRAVEELGDLCEETPIYTALHLVGKQLIGWPSYLMTNATGHNFHERQREGRGKGKKNGFGGGVNHFDPRSPIFEARQAKYIVLSDIGLGLAIAALVYLGNRFGWANMAVWYFLPYLWVNHWLVAITFLQHTDPTLPHYNREEWNFVRGGACTIDRDLGFIGRHLFHGIADTHVVHHYVSRIPFYNADEASEAIKPIMGKHYRSDTAHGPVGFLHALWKTARWCQWVEPSADAQGAGKGILFYRNRNKLGTKPISMKTQ | Function: Oleate hydroxylase involved in the biosynthesis of ricinoleate . Exhibits delta(12) hydroxylase activity on 16C and 18C monounsaturated fatty acids (e.g. oleic and palmitoleic acids), and, to a lower extent, gamma(3) hydroxylase activity on ricinoleic acid . It uses cytochrome b5 as an electron donor. May act on both oleic acid (18:1(9cis)) and eicosenoic acid (20:1(11cis)) (By similarity).
Catalytic Activity: (9Z)-octadecenoate + AH2 + O2 = (12R)-hydroxy-(9Z)-octadecenoate + A + H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53452
Sequence Length: 477
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Pathway: Lipid metabolism; monounsaturated fatty acid biosynthesis.
Subcellular Location: Microsome membrane
EC: 1.14.-.-
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Q05AM4 | MGLTLGERVQHCLLVLVSGLFLALFRLLSPGTKRPKHLPPITNPLLTLSAVQLAEKIRRGEVSSVEVVQAYIDRIQEVNPLLNALIKDRFSAALLEAARADKLIKEENGGEEVLRNQFPLLGVPMSVKESFGLQGMPNSGGLKSRGKVLASVDAPPVALLKRAGAIPLGVTNTSELCMWMESNNHLYGITSNPYNLERICGGSSGGEGSIIGGGASVFGIGSDIGGSIRMPCFFNGIFGHKPSRGVVSNDNQFPRCSGLQNEYTGSGPMCRYAEDLLPLLKIMAGPTADKLTLSKAVDLKKLRFFTIVDDGGSPLTSPVDRQLVEVQKRVAARLEADLGVTVQEVNFPQLKYSYQIWDTFLALPDKDGKPPEAFVELMADGGSVWPVWELIKRIFGRSEHTVAAIGLALMESSHSSKSSEFILKQKEDLQREMEDLLGTDGVLLYPSHPLLAPKHHHPLFMPFNFSYTGILNILGLPVTQCPLGLSKERLPLGVQVVAGLCQDHLTLAMALYLEKAFGGWVDPGVV | Catalytic Activity: H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57026
Sequence Length: 526
Subcellular Location: Membrane
EC: 3.5.1.99
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Q9SUC5 | MVAERYTVDLNKPLVFQVGHLGEEYQEWIHQPIVCVEGPRFFESDFWEFLTRTVWWAIPTIWLPVVCYVLSISASKGLTFPQIGLIVAFGVLTWTLLEYTLHRFLFHIQTKSYWANTAHYLLHGCHHKHPQDGLRLVFPPTATAILLVPLWKLLHLLATPATAPAILGGILFGYVMYDITHYYLHHGQPKEPTFKHLKKYHLNHHFRIQDKGYGITSSLWDKVFGTLPGIKAAAKKS | Cofactor: Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Function: Fatty acid 2-hydroxylase involved in the alpha-hydroxylation of the long-chain fatty acid (LCFA) palmitic acid. Probably involved in the resistance response to oxidative stress.
Catalytic Activity: an N-(1,2-saturated acyl)sphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-[(2'R)-hydroxyacyl]sphinganine + 2 Fe(III)-[cytochrome b5] + H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27311
Sequence Length: 237
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.18.7
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Q93ZE5 | MATSMIQRMFKQGTKIVCVGRNYAAHAKELGNAVPKEPVIFLKPTSSYLENGGTIEIPHPLDSLHHEVELALVIGQKARDVPESIAMDYIGGYAVALDMTARELQASAKASGLPWTVAKGQDTFTPISSVLPKAMVRDPDNLELWLKVDGETRQKGLTKDMIFKVPYLISYISSIMTLYEGDVILTGTPEGVGPVKIGQKITAGITGLSEVQFDVERRVKPLS | Function: Probable acylpyruvase. Binds copper in vitro.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24283
Sequence Length: 223
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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P15278 | MSRIVFICLAAILTDALTWAQVNVEPNTALLNEGDRTELLCRYGRSINYCRIEIPGEQKVLNLSPEWSKTPGFTYFGAGLTAGQCGVSIERVKASNNGQVKCSLGVEGEELSGTIDLVVALRPQQPIIELLSRPNREGYFNEGTEFRARCSVRDGRPPANISWYIDNMPANKRTTPLEVMSSTNDNVELSTSVQEIQWHLSPEDSNRKLVCRSHHQTDRESVPPQEAAYIINVRYAPVHQPDAAVYGLYLEHTAIVNITIRASPQPKIEWTIDGAIVGQGRTDGRYSAYEPQYLGNDEYNVTLAIAGLTLEDTTKIYNLRASNELGLTDYQVRISSSSKPPSSSLDVAAIVGIVVAVAVLVLVVLLIVFARATGRWCFGGKSIKTPTNETSDTESADIKATSTATATTTMGGVGVSAEEEETVNEQESPQEQQQQQQKKAKRLPAFAAAILRRFNEKDSRKYKDNQESLNIVEGSVQEIPATNNAIDGNDNEPKAIVWQSTSPVWTFK | Function: Mediates cell adhesion in a Ca(2+)-independent manner. It plays a role in axon outgrowth, guidance and fasciculation of the developing nervous system.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 55884
Sequence Length: 508
Subcellular Location: Membrane
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P46000 | MNKYPPLLTMLIIGIGSNAVAGDYFDPSLLATDIGNNDKLDLSLFSHPGGGVKGEREVSVYINDFFYKNVTLDFENGISGALEPIFPSGFFDNILASPYRSIKEKELISTADFLSLVPYGMVRFDQAIARVDISIPQAYLGRDAQMKSAPESWNQGVPALLIDYRLSGSKNKYNYGSSQNFYANAFLGFNLMGWRLRTTTNYMSYNSKDLYNKGERQGSFNFYNTYLEKDIGYLRSTLRLGELSTRGMILESFNFKGGKIYSNDEMLNDRLRSYTPTVRGIASSQAVVTIKQGGVVILQKNVPPGPFEINDFSLSGYSGDLYVNIKEADGSEHSFIQPFSTLPEMKREGVSGYEISLGHYNNSGATQYYNESPFLYASWSRGYRNGMTLYSETIQSRKYQLLGVGSTLSLGDFGAVSGDASLSRANKYDKIHSGQSYGLKYSKNKVDTGTTVTLATYRYSTKDFYSFNDFVSKNDSVQYVWDNRLKNRITLSLNQSLDDYGSLSLIASQQNYWTSDYVSRSFSLSHSFGWNDIFFSTSFSLDQKEGDNALRNNNKVFGFYSSIPLSKLIGKNESTYSTLSYNVTKINNQVRNTATLAGKVPGSMAQYRFSSGWANTEQSSNKALSVNWDGDLLDGSLGYTSSGKNRITDYSLSGSAILYPWRLAIGSDSVINGAAVVETEFISGIKVRQGGETSLLGTAIVTSMQPYTENRIDLDTQNIPDDLFISNASKKIVPEKGAVVPVKYNLFKGKQIVFSLKRYDGTPLPFGSVVSLVGSDSEITGIIDDAGRVYLAGIPSKGILHGAWGYNKSCEVSFNLNGKPSNNSNEIIEYEGVCK | Function: Involved in the export and assembly of the 987P fimbriae subunits across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92354
Sequence Length: 835
Subcellular Location: Cell outer membrane
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Q8JIT7 | MSFGLHPWDVAFRPSPPHNLEKKVVPPGADREKSLPSPKEDSDGAREPDSTVDLRKKNKKKKNYQRYAKPPYSYLAMISLVIQNSPEKRLKLSQILQDISSLFPFFKGNYQGWKDSIRHNLSSNDCFRKVLKDPLKPQAKGNYWTVDVTRIPPDALKLQNTAVTRQDLFPLDLAPYILHGQPYRSLERLSANHTRGRTTPRMEPEVQIPVSDPAVSFPMILWNLPTSYSKCVAPNVVAPPSIHPLLLYSNFPSISIYNYLPPPYGSPVYSDRRDLLASGLHPQIPLTPKPPELKNAPSDFPPNKTVFDIPVYTGHPGFLASQSLFSPHLPTATPPLVGYRPSGL | Function: Transcriptional activator. Upon TGF-beta induction, forms a transcriptionally active complex with smad2 and smad4 called activin-responsive factor 2 (ARF2), which binds a site on the mix-B/mix.2 promoter called the activin response element (ARE). Binds to activated smads and the ARE with much higher affinity than foxh1/fast-1. Acts with foxh1/fast-1 to control the convergent extension movements of gastrulation.
Sequence Mass (Da): 38658
Sequence Length: 344
Domain: The FM region is required for binding smad2/smad4 complexes. FM2 is more effective than FM1 and only interacts with phosphorylated smad2 that is in an activated smad complex.
Subcellular Location: Nucleus
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Q14296 | MRRPRGEPGPRAPRPTEGATCAGPGESWSPSPNSMLRVLLSAQTSPARLSGLLLIPPVQPCCLGPSKWGDRPVGGGPSAGPVQGLQRLLEQAKSPGELLRWLGQNPSKVRAHHYSVALRRLGQLLGSRPRPPPVEQVTLQDLSQLIIRNCPSFDIHTIHVCLHLAVLLGFPSDGPLVCALEQERRLRLPPKPPPPLQPLLRGGQGLEAALSCPRFLRYPRQHLISSLAEARPEELTPHVMVLLAQHLARHRLREPQLLEAIAHFLVVQETQLSSKVVQKLVLPFGRLNYLPLEQQFMPCLERILAREAGVAPLATVNILMSLCQLRCLPFRALHFVFSPGFINYISGTPHALIVRRYLSLLDTAVELELPGYRGPRLPRRQQVPIFPQPLITDRARCKYSHKDIVAEGLRQLLGEEKYRQDLTVPPGYCTDFLLCASSSGAVLPVRTQDPFLPYPPRSCPQGQAASSATTRDPAQRVVLVLRERWHFCRDGRVLLGSRALRERHLGLMGYQLLPLPFEELESQRGLPQLKSYLRQKLQALGLRWGPEGG | Function: Phosphorylates the splicing regulator TIA1, thereby promoting the inclusion of FAS exon 6, which leads to an mRNA encoding a pro-apoptotic form of the receptor.
PTM: Autophosphorylated on serine/threonine residues. Activated by dephosphorylation.
Catalytic Activity: ATP + L-seryl-[Fas-activated protein] = ADP + H(+) + O-phospho-L-seryl-[Fas-activated protein]
Sequence Mass (Da): 61104
Sequence Length: 549
Domain: The RAP domain is essential for RNA-binding.
Subcellular Location: Mitochondrion matrix
EC: 2.7.11.1
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P08757 | MGLRPDGIIGHSLGEVARAYYNGRISQEEAILSAY | Function: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein.
Catalytic Activity: acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+)
Sequence Mass (Da): 3808
Sequence Length: 35
Subcellular Location: Cytoplasm
EC: 2.3.1.85
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P07855 | AEGEGQRDLLKAVAHILGIRDLAGINLDSSLADLGLDSLMGVEVRQTLEREHDLVLSMREVRQL | Function: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein.
Catalytic Activity: acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+)
Sequence Mass (Da): 7037
Sequence Length: 64
Subcellular Location: Cytoplasm
EC: 2.3.1.85
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Q9FZ32 | MALYCRDTLIIIFQKLTVADLARASCVCKVWNSVATEDDLVVSAFTAPWRIKELVGRPASVSFWRDNGIWKFAISHRICRGDSVTSLAVKYAVQVMDIKRLNNMMSDHGIYSRDRLLIPISNPEILANTTCYVELDKYAKREVAVLYLEGAPKREQPVPGTNQQSNLSADGKRRLIESLRRSMQVDDGTALYYLAIAEGDPRSALSEFSADLRWERQAGLN | Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 24904
Sequence Length: 221
Domain: The F-box is necessary for the interaction with ASK proteins.
Pathway: Protein modification; protein ubiquitination.
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B4RGP0 | MAEAILAVRGGLGAKSRLAAVFSDAERAALVEAMLLDMLDALAGAGAGAVRRVWVVTPTERLERLAAAAGARVIREPRPAGLNAAFRCGLAAAAEEAPYADIVLLPGDLPTLRAQDVDAALLLLRTHDLVLALASRDGGTGLLAVRAGVPFTPQFGAQSCARHRRQARARGLSCALVEAGSLALDLDRPEDAVEVARGPCGRRTAEVLSDLKSRWRAQ | Function: Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor coenzyme F420, 3PG-F420.
Catalytic Activity: (2R)-3-phosphoglycerate + GTP + H(+) = 3-[(R)-glyceryl]-diphospho-5'-guanosine + diphosphate
Sequence Mass (Da): 22786
Sequence Length: 218
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.106
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A5USE3 | MVIHAIVPVKELHRAKQRLARVLDAHERRALSLAMLNDVLVALSYSPVSRIIVIGRDVETGHTARAHGAAFVIDQSAALNDALHQAAADIPDHAAALVAPSDLPLLGAEDVIALTCISGDKPGVAIAPAHDGGTNLLLVSPVVGWTFLFGPDSLTHHIAAARQRHLPVHLLRLPHLERDIDDIDDLIWLAQQPGDTSAQRLARMFLERKGAQLWQSSDMPPH | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 23996
Sequence Length: 222
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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Q1AXF2 | MSVFAVVPVKELRGAKSRLGAVLDPVGRAGLTLHMLRRVVPALRGAGLRRVLVVSPDPAVLEEARLLGAAGLRQEGFGLNAALEEGRRRALEEGAGALLALPADLPLIEPADVAALLEVAGEGPCAVISPDDARSGTNALLLRPPGALPFSFGPGSFGVHLQAALRRGVRVRVCERPNVAFDLDSPEDLARLEASGGVQYRPRRA | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 21464
Sequence Length: 205
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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D1BJD0 | MSAEQQAVVSAEQQAVVSAEQPAVVSADQPAVTWTVVVPVKVTSQAKTRLAGDLSPTQRVELVRAMVVDTVAAARATPTVDRVVVVTDDPDVVADLSADEPAGTDAERRADPSAENRASTSAQHPCLRAHLDVVPEPSPAAGLNAAIRAGVASARSGGGLAAVSVAVLLGDLPALRPGDLGAALEAASAHHRAVVTDADGSGTTLLTARSGVELYPAFGPGSAAEHAARGHVVLDVADVPAVSGLRQDVDLARDLAAVAALGPGPRTTEVLDRWARLGEGSSAA | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 28596
Sequence Length: 284
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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D1C883 | MTTIAVVPVQRLSTAKSRLAARLAPDERRTLVLSLLDHVLTALNAARQVDAVILVSPDPEVLEHAARRGAIALLQPGVGLNEGLRLGRDEALRRGADTLLIVLADLPWITADEIDALVAALPERGIALAPDRHDHGTNAAALRPPDAIEPAFGAGSFARHQAQARSRGLPLRELRVQGLAFDIDTPADLEELAGHAPVGASSDESGT | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 21837
Sequence Length: 207
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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Q9ZBS2 | MQWTLVVPVKALARAKSRLSDTADDGLRPGLALAFAQDTVAAALACPAVADVAVVTDDARAGRELAALGAGVVADEPGGGLNAALAHGAAVVRAARPESPVAALNADLPALRPAELARVLAAATQFPRAFLPDAAGIGTTLLTVAPGQELAPAFGADSRARHRASGAVELRLDAVDSVRQDVDTGGDLRSALALGVGPRTAAVAARLLIAGQ | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 21151
Sequence Length: 212
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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D2AVM1 | MLKAMPASESSGWTLVVPVKTLVAAKTRLSEAAGPHRAALAVAIACDTVEAALSCVIVARIVVVTGDPLAAEALGGVGAHVVGDPEAGLNAALRRGAQEAVRLAPGDAVGALQADLPALRPAELALVLTAAAEFEQAFLPDAADVGTTFYGVRPGVPFTPGFGGESRDRHLRRGAKEICLDGIDSVRRDVDTPDDLRAALALGLGPRTLAMVERIRGGFPSP | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 22725
Sequence Length: 222
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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C9Z3U4 | MQWTLVVPVKPLARAKSRLSDTAADAVRPGLALAFAQDTVAAALAATAVRGVVVVTDDPLAARELTALGARAVPEDPGGGPGDGLNAALRHGAALVRDVRPQSPVAALNADLPALRPGELTRVLGAAAAFPRAFLADAAGTGTTLLAAAPGHGLSPAFGPGSRTRHRRSGAVELDLTAVDSVRQDVDTGDDLRAALGLGVGPRTAAAAARLLIPGQ | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 21607
Sequence Length: 216
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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D1AB53 | MAVETSHDAELTWSLVLPVKPLARAKTRMAEAAGPLRQALALAVAADTVAAALRCAAVAEVIVVTDDPLAAAELSALGARVVPDEPDCGLNPALAHGAALARAARPRAGVGAMSADLPALRPAELGRALAAAAGFAESFVADAQGVGTTLYAVRPGVPFSPAFGPGSRARHAAQGARELAIEGLDSLRRDVDTPGDLRAALALGTGPRTAALAARMPAFSPGAETSRG | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 22845
Sequence Length: 228
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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B9L4T8 | MQVLAVVPVQRLEQAKSRLAPALEPAARQALVRELAERTIRILRSVPAVAVIGLLTPDPSLASLASRWGVRTLRDAAHGLNDAVRLAQAEACRLHLPALLIVLGDLPLLDPHAIRHALALLESPGVVLAPDRHGTGTNLLALAPPDVIAPAFGPFSRWRHRRAAAGARCTIRELWSRALVLDLDTPEDLALVHRVREGER | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 21668
Sequence Length: 200
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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D1CDA4 | MSAMNIAVLVPVKKLDKAKMRMADTLDRSQRRQLMMVTLRRVLSALQKAQIGDVYLVASDPQVKNIACDLCVKFIPDQGDELNPSLELARGELCQNYDALLVVFGDLPMISDKDIKTIVRLGSSKPSCVIAPDKRNVGTNVLFLHPPYLLPFTFGGNSYERFRSNCEKLGVQFLVYQSQNTALDLDYPQDILDLAALRGHKISGLEEILDPGVLAQISQVTSMSGAKMGA | Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Mass (Da): 25358
Sequence Length: 230
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.7.105
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O55058 | MLPFASCLPGSLLLWALLLLLLGAASPQDSEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDEQESCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKVGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECSYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYVQVSDNRCFCPVSNPLCREQPSSIVHRYMSITSERSVPADVFQIQATSVYPGAYNAFQIRAGNTQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF | Function: Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta. In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin. Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction. Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling.
PTM: N-glycosylated; contains mostly complex-type glycans. Not O-glycosylated.
Sequence Mass (Da): 49432
Sequence Length: 443
Subcellular Location: Secreted
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O95967 | MLPCASCLPGSLLLWALLLLLLGSASPQDSEEPDSYTECTDGYEWDPDSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDDQDSCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCHQGYELHRDGFSCSDIDECSYSSYLCQYRCINEPGRFSCHCPQGYQLLATRLCQDIDECESGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYIQVSENRCLCPASNPLCREQPSSIVHRYMTITSERSVPADVFQIQATSVYPGAYNAFQIRAGNSQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF | Function: Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta . In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin (By similarity). Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction . Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling .
PTM: N-glycosylated; contains mostly complex-type glycans . Not O-glycosylated .
Sequence Mass (Da): 49405
Sequence Length: 443
Subcellular Location: Secreted
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Q9WVJ9 | MLPFASCLPGSLLLWAFLLLLLGAASPQDPEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVISDLHGEGPPPPAAHAQQPNPCPQGYEPDEQESCVDVDECTQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECGYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYVQVSDNRCLCPASNPLCREQPSSIVHRYMSITSERSVPADVFQIQATSVYPGAYNAFQIRSGNTQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF | Function: Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta . In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin . Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction . Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling .
PTM: N-glycosylated; contains mostly complex-type glycans. Not O-glycosylated.
Sequence Mass (Da): 49425
Sequence Length: 443
Subcellular Location: Secreted
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Q9UBX5 | MPGIKRILTVTILALCLPSPGNAQAQCTNGFDLDRQSGQCLDIDECRTIPEACRGDMMCVNQNGGYLCIPRTNPVYRGPYSNPYSTPYSGPYPAAAPPLSAPNYPTISRPLICRFGYQMDESNQCVDVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCLDIDECRYGYCQQLCANVPGSYSCTCNPGFTLNEDGRSCQDVNECATENPCVQTCVNTYGSFICRCDPGYELEEDGVHCSDMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRSCQDINECEHRNHTCNLQQTCYNLQGGFKCIDPIRCEEPYLRISDNRCMCPAENPGCRDQPFTILYRDMDVVSGRSVPADIFQMQATTRYPGAYYIFQIKSGNEGREFYMRQTGPISATLVMTRPIKGPREIQLDLEMITVNTVINFRGSSVIRLRIYVSQYPF | Function: Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN . Stabilizes and organizes elastic fibers in the skin, lung and vasculature (By similarity). Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling . May act as an adapter that mediates the interaction between FBN1 and ELN .
PTM: N-glycosylated.
Sequence Mass (Da): 50180
Sequence Length: 448
Subcellular Location: Secreted
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Q53RD9 | MVPSSPRALFLLLLILACPEPRASQNCLSKQQLLSAIRQLQQLLKGQETRFAEGIRHMKSRLAALQNSVGRVGPDALPVSCPALNTPADGRKFGSKYLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCRGISECSSQPCQNGGTCVEGVNQYRCICPPGRTGNRCQHQAQTAAPEGSVAGDSAFSRAPRCAQVERAQHCSCEAGFHLSGAAGDSVCQDVNECELYGQEGRPRLCMHACVNTPGSYRCTCPGGYRTLADGKSCEDVDECVGLQPVCPQGTTCINTGGSFQCVSPECPEGSGNVSYVKTSPFQCERNPCPMDSRPCRHLPKTISFHYLSLPSNLKTPITLFRMATASAPGRAGPNSLRFGIVGGNSRGHFVMQRSDRQTGDLILVQNLEGPQTLEVDVDMSEYLDRSFQANHVSKVTIFVSPYDF | Function: An adhesion molecule that interacts with extracellular matrix molecules in developing teeth and may play important roles in differentiation and maintenance of odontoblasts as well as in dentin formation.
PTM: N-glycosylated.
Sequence Mass (Da): 47376
Sequence Length: 439
Subcellular Location: Secreted
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Q501P1 | MGPGSQRALFLLLLLLASPGARAFQSCLNKQQLLTTIRQLQQLLKGQETRFTEGIRNMKSRLAALQNTVNKMTPDAPPVSCPALEAPPDGKKFGSKYLVDHEVYFTCNPGFQLVGPSSVVCLANGSWTGEQPRCRDISECSSQPCHNGGTCVEGINHYRCICPPGKTGNRCQHQTQAAAPDGGEAGDPAFSRAPRCAQVEREQHCSCEAGFHLSSTTGGHSVCQDVNECEIYGQKGRPRLCMHACVNTPGSYRCTCPSGYRILADGKSCEDVDECAGPQHMCPRGTTCINTGGGFQCVNPECPEGSGNISYVKTSPFQCERNPCPMDSRPCRHLPKTISFHYLSLPSKLKTPITLFRMATASIPGHPGPNSLRFGIVGGNSRGHFVMQRSDRQTGELILTQTLEGPQTLEVDVDMSEYLERSFQANHVSKVTIFVSRYDF | Function: An adhesion molecule that interacts with extracellular matrix molecules in developing teeth and may play important roles in differentiation and maintenance of odontoblasts as well as in dentin formation.
PTM: N-glycosylated.
Sequence Mass (Da): 47927
Sequence Length: 440
Subcellular Location: Secreted
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Q96LA6 | MLPRLLLLICAPLCEPAELFLIASPSHPTEGSPVTLTCKMPFLQSSDAQFQFCFFRDTRALGPGWSSSPKLQIAAMWKEDTGSYWCEAQTMASKVLRSRRSQINVHRVPVADVSLETQPPGGQVMEGDRLVLICSVAMGTGDITFLWYKGAVGLNLQSKTQRSLTAEYEIPSVRESDAEQYYCVAENGYGPSPSGLVSITVRIPVSRPILMLRAPRAQAAVEDVLELHCEALRGSPPILYWFYHEDITLGSRSAPSGGGASFNLSLTEEHSGNYSCEANNGLGAQRSEAVTLNFTVPTGARSNHLTSGVIEGLLSTLGPATVALLFCYGLKRKIGRRSARDPLRSLPSPLPQEFTYLNSPTPGQLQPIYENVNVVSGDEVYSLAYYNQPEQESVAAETLGTHMEDKVSLDIYSRLRKANITDVDYEDAM | Function: May function as an activating coreceptor in B-cells. May function in B-cells activation and differentiation.
PTM: Phosphorylated on tyrosines upon activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46936
Sequence Length: 429
Subcellular Location: Cell membrane
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Q8R4Y0 | MLPWLLLLICALPCEPAGISDVSLKTRPPGGWVMEGDKLVLICSVDRVTGNITYFWYRGALGFQLETKTQPSLTAEFEISDMKQSDADQYYCAANDGHDPIASELVSIHVRVPVSRPVLTFGDSGTQAVLGDLVELHCKALRGSPPIFYQFYHESIILGNSSAPSGGGASFNFSLTAEHSGNFSCEASNGQGAQRSEVVALNLTGLSLVPTENGISHLSLGLTGWLLGCLSPITMALIFCYWLKRKIGRQSEDPVRSPPQTVLQGSTYPKSPDSRQPEPLYENVNVVSGNEVYSLVYHTPQVLEPAAAQHVRTHGVSESFQVSSGLYSKPRINIAHMDYEDAM | Function: May function as an activating coreceptor in B-cells. May function in B-cells activation and differentiation (By similarity).
PTM: Phosphorylated on tyrosines upon activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37277
Sequence Length: 343
Subcellular Location: Cell membrane
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Q96LA5 | MLLWSLLVIFDAVTEQADSLTLVAPSSVFEGDSIVLKCQGEQNWKIQKMAYHKDNKELSVFKKFSDFLIQSAVLSDSGNYFCSTKGQLFLWDKTSNIVKIKVQELFQRPVLTASSFQPIEGGPVSLKCETRLSPQRLDVQLQFCFFRENQVLGSGWSSSPELQISAVWSEDTGSYWCKAETVTHRIRKQSLQSQIHVQRIPISNVSLEIRAPGGQVTEGQKLILLCSVAGGTGNVTFSWYREATGTSMGKKTQRSLSAELEIPAVKESDAGKYYCRADNGHVPIQSKVVNIPVRIPVSRPVLTLRSPGAQAAVGDLLELHCEALRGSPPILYQFYHEDVTLGNSSAPSGGGASFNLSLTAEHSGNYSCEANNGLGAQCSEAVPVSISGPDGYRRDLMTAGVLWGLFGVLGFTGVALLLYALFHKISGESSATNEPRGASRPNPQEFTYSSPTPDMEELQPVYVNVGSVDVDVVYSQVWSMQQPESSANIRTLLENKDSQVIYSSVKKS | Function: May have an regulatory role in normal and neoplastic B cell development.
PTM: Isoform 2 is N- and O-glycosylated, and phosphorylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 55542
Sequence Length: 508
Domain: Contains 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif bind the SH2 domain of PTPN6.
Subcellular Location: Cell membrane
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Q96P31 | MLLWLLLLILTPGREQSGVAPKAVLLLNPPWSTAFKGEKVALICSSISHSLAQGDTYWYHDEKLLKIKHDKIQITEPGNYQCKTRGSSLSDAVHVEFSPDWLILQALHPVFEGDNVILRCQGKDNKNTHQKVYYKDGKQLPNSYNLEKITVNSVSRDNSKYHCTAYRKFYILDIEVTSKPLNIQVQELFLHPVLRASSSTPIEGSPMTLTCETQLSPQRPDVQLQFSLFRDSQTLGLGWSRSPRLQIPAMWTEDSGSYWCEVETVTHSIKKRSLRSQIRVQRVPVSNVNLEIRPTGGQLIEGENMVLICSVAQGSGTVTFSWHKEGRVRSLGRKTQRSLLAELHVLTVKESDAGRYYCAADNVHSPILSTWIRVTVRIPVSHPVLTFRAPRAHTVVGDLLELHCESLRGSPPILYRFYHEDVTLGNSSAPSGGGASFNLSLTAEHSGNYSCDADNGLGAQHSHGVSLRVTVPVSRPVLTLRAPGAQAVVGDLLELHCESLRGSFPILYWFYHEDDTLGNISAHSGGGASFNLSLTTEHSGNYSCEADNGLGAQHSKVVTLNVTGTSRNRTGLTAAGITGLVLSILVLAAAAALLHYARARRKPGGLSATGTSSHSPSECQEPSSSRPSRIDPQEPTHSKPLAPMELEPMYSNVNPGDSNPIYSQIWSIQHTKENSANCPMMHQEHEELTVLYSELKKTHPDDSAGEASSRGRAHEEDDEENYENVPRVLLASDH | Function: Promotes TLR9-induced B-cell proliferation, activation and survival but inhibits antibody production and suppresses plasma cell differentiation. Enhances activation of NF-kappa-B and MAPK signaling pathways in TLR9 stimulated B-cells . Has inhibitory potentional on B-cell receptor (BCR)-mediated signaling, possibly through association with SH2 domain-containing phosphatases. Inhibits cell tyrosine phosphorylation, calcium mobilization and activation-induced cell death induced through BCR signaling . Regulatory T-cells expressing FCRL3 exhibit a memory phenotype, are relatively nonresponsive to antigenic stimulation in presence of IL2 and have reduced capacity to suppress the proliferation of effector T-cells . Acts as a human-specific epitope on the cell surface of oocytes (oolemma) and plays a role during sperm-egg adhesion and fusion . Interacts with the IZUMO1-IZUMO1R/JUNO sperm-egg complex and replaces IZUMO1R/JUNO as IZUMO1 receptor during fertilization, thereby permitting species-specific gamete fusion .
PTM: Phosphorylated on cytoplasmic tyrosines; required for interaction with protein tyrosine phosphatases and protein tyrosine kinases.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 80856
Sequence Length: 734
Subcellular Location: Cell membrane
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Q96PJ5 | MLLWASLLAFAPVCGQSAAAHKPVISVHPPWTTFFKGERVTLTCNGFQFYATEKTTWYHRHYWGEKLTLTPGNTLEVRESGLYRCQARGSPRSNPVRLLFSSDSLILQAPYSVFEGDTLVLRCHRRRKEKLTAVKYTWNGNILSISNKSWDLLIPQASSNNNGNYRCIGYGDENDVFRSNFKIIKIQELFPHPELKATDSQPTEGNSVNLSCETQLPPERSDTPLHFNFFRDGEVILSDWSTYPELQLPTVWRENSGSYWCGAETVRGNIHKHSPSLQIHVQRIPVSGVLLETQPSGGQAVEGEMLVLVCSVAEGTGDTTFSWHREDMQESLGRKTQRSLRAELELPAIRQSHAGGYYCTADNSYGPVQSMVLNVTVRETPGNRDGLVAAGATGGLLSALLLAVALLFHCWRRRKSGVGFLGDETRLPPAPGPGESSHSICPAQVELQSLYVDVHPKKGDLVYSEIQTTQLGEEEEANTSRTLLEDKDVSVVYSEVKTQHPDNSAGKISSKDEES | Function: May function as an inhibitor of the B-cell receptor signaling. May function in the B-cell-mediated immune response.
PTM: Phosphorylated on cytoplasmic tyrosines upon activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 57224
Sequence Length: 515
Subcellular Location: Cell membrane
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Q96RD9 | MLLWVILLVLAPVSGQFARTPRPIIFLQPPWTTVFQGERVTLTCKGFRFYSPQKTKWYHRYLGKEILRETPDNILEVQESGEYRCQAQGSPLSSPVHLDFSSASLILQAPLSVFEGDSVVLRCRAKAEVTLNNTIYKNDNVLAFLNKRTDFHIPHACLKDNGAYRCTGYKESCCPVSSNTVKIQVQEPFTRPVLRASSFQPISGNPVTLTCETQLSLERSDVPLRFRFFRDDQTLGLGWSLSPNFQITAMWSKDSGFYWCKAATMPYSVISDSPRSWIQVQIPASHPVLTLSPEKALNFEGTKVTLHCETQEDSLRTLYRFYHEGVPLRHKSVRCERGASISFSLTTENSGNYYCTADNGLGAKPSKAVSLSVTVPVSHPVLNLSSPEDLIFEGAKVTLHCEAQRGSLPILYQFHHEGAALERRSANSAGGVAISFSLTAEHSGNYYCTADNGFGPQRSKAVSLSVTVPVSHPVLTLSSAEALTFEGATVTLHCEVQRGSPQILYQFYHEDMPLWSSSTPSVGRVSFSFSLTEGHSGNYYCTADNGFGPQRSEVVSLFVTVPVSRPILTLRVPRAQAVVGDLLELHCEAPRGSPPILYWFYHEDVTLGSSSAPSGGEASFNLSLTAEHSGNYSCEANNGLVAQHSDTISLSVIVPVSRPILTFRAPRAQAVVGDLLELHCEALRGSSPILYWFYHEDVTLGKISAPSGGGASFNLSLTTEHSGIYSCEADNGLEAQRSEMVTLKVAVPVSRPVLTLRAPGTHAAVGDLLELHCEALRGSPLILYRFFHEDVTLGNRSSPSGGASLNLSLTAEHSGNYSCEADNGLGAQRSETVTLYITGLTANRSGPFATGVAGGLLSIAGLAAGALLLYCWLSRKAGRKPASDPARSPSDSDSQEPTYHNVPAWEELQPVYTNANPRGENVVYSEVRIIQEKKKHAVASDPRHLRNKGSPIIYSEVKVASTPVSGSLFLASSAPHR | Function: May be involved in B-cell development and differentiation in peripheral lymphoid organs and may be useful markers of B-cell stages. May have an immunoregulatory role in marginal zone B-cells. May play a role in fertilization (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 106437
Sequence Length: 977
Domain: Contains 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM).
Subcellular Location: Cell membrane
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Q68SN8 | MSGSFSPCVVFTQMWLTLLVVTPVNGQHEAAQQSVVSLQPPWTTFFRGEVVTLTCYRFGFSVPQKTKWYQKRKTVKQTPGALVIKAHTLKVHESGEYWCQADSLLPSMHVNVEFSEDFLVLQAPPAVFEGDSVVLRCYAKKGIEAETLTFYKDGKALTLHPQSSEFYIHRANLKDNGQYKCTSKKKWSFGSLYTSNTVVVQVQELFPRPVLRARPSHPIDGSPVTLTCQTQLSAQKSDARLQFCFFRNLQLLGSGCSRSSEFHIPAIWTEESKRYQCKAETVNSQVSKQSTAFIIPVQRASARFQTHIIPASKLVFEGQLLLLNCSVKGVPGPLKFSWYKKDMLNKETKILKSSNAEFKISQVNISDAGEYYCEANNSRRSFVSRAFPITIKVPVSQPVLTLSTGKTQALEGDLMTLHCQSQRGSPCILYEFFYENVSLGNSSILSGGGAYFNFSMSTERSGNYYCTADNGLGAQCSEAIRISIFDMTKNRSVPMAAGITVGLLIMAVGVFLFYCWFSRKAGGKPTSDDSRNPSDSEPQEPTYYNVPACIELQPVYSNEPEENVIYTEVRRTQPRQKHADQESESPRSRCQMAEKK | Function: May play a role in fertilization.
PTM: Phosphorylated on cytoplasmic tyrosines; required for interaction with protein tyrosine phosphatases and protein tyrosine kinases.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 66779
Sequence Length: 596
Subcellular Location: Cell membrane
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Q6DN72 | MLLWTAVLLFVPCVGKTVWLYLQAWPNPVFEGDALTLRCQGWKNTPLSQVKFYRDGKFLHFSKENQTLSMGAATVQSRGQYSCSGQVMYIPQTFTQTSETAMVQVQELFPPPVLSAIPSPEPREGSLVTLRCQTKLHPLRSALRLLFSFHKDGHTLQDRGPHPELCIPGAKEGDSGLYWCEVAPEGGQVQKQSPQLEVRVQAPVSRPVLTLHHGPADPAVGDMVQLLCEAQRGSPPILYSFYLDEKIVGNHSAPCGGTTSLLFPVKSEQDAGNYSCEAENSVSRERSEPKKLSLKGSQVLFTPASNWLVPWLPASLLGLMVIAAALLVYVRSWRKAGPLPSQIPPTAPGGEQCPLYANVHHQKGKDEGVVYSVVHRTSKRSEARSAEFTVGRKDSSIICAEVRCLQPSEVSSTEVNMRSRTLQEPLSDCEEVLC | Function: Acts as a MHC class II receptor . When stimulated on its own, does not play a role in cytokine production or the release of cytotoxic granules by NK cells and cytotoxic CD8(+) T cells . Does not act as an Fc receptor .
PTM: Phosphorylated on Tyr residues. Tyrosine phosphorylation induces association with phosphatase PTPN11, PTPN6, INPP5D, INPPL1 and GRB2.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 47748
Sequence Length: 434
Domain: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif is involved in PTPN11 binding.
Subcellular Location: Cell membrane
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A1YIY0 | MLLWMVLLLCESMAEAQELFPNPELTEFTNSETMDVILKCTIKVDPKNPTLQLFYTFYKNNHVIQDRSPHSVFSAEAKEENSGLYQCMVDTEDGLIQKKSGYLDIQFWTPVSHPVLTLQHEATNLAVGDKVEFLCEAHQGSLPIFYSFYINGEILGKPLAPSGRAASLLASVKAEWSTKNYSCEAKNNISREISELKKFPLVVSGTAWIKSNMLPIWLPASLLGGMVIAAVVLMYFFKPCKKHARPETPTLKEPDSFLYVSVDNQRYK | Function: Acts as a MHC class II receptor. When stimulated on its own, does not play a role in cytokine production or the release of cytotoxic granules by NK cells and cytotoxic CD8(+) T cells. Does not act as an Fc receptor.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 30237
Sequence Length: 268
Subcellular Location: Cell membrane
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A0A2P1BT06 | MGERRFSNQQIDRLLRPKSVAVIGASDRKGALGATLLNNLVQYEFSGDIYPVNPKRDELLGLKVYHEVAELPEGIDCAVLAIPRPFVIDTVRQLAQRGCGAVVIYSAGFSEAGEEGMKDQLELAAIAAEYGMVIEGPNCLGCTNYVERVPLTFVETNMQTPPKGTRAVGIASQSGALAAVLATALHPRGLYVSSSVSTGNEAASGVEDYVEWLVDDEDTHVIAMYVESLRRPKAFIAAARRAHAAGKPIVMLHPGKSNKAQESAATHTGAMAGDYALMKTKLAREGVIFADTLEELADITEIALRCRALPGANMAVLGESGALRGLAFDIAEDIGLDLIHLDDDNSPALRAILPDFVPVSNPTDITALGLSEPEIYTKVLTALLEDERIGSVVASIIQSDPITSGIKFPHIIKVLDGGTFAKPLVFAGVDEGATVPKEYIDGLRKVGIPWFPSTERAYRAIARLADLSKRDLADNSGDPIVVPGLDAVSGVVPEYKAKELLRPLGIAFPPSQFAANAEAAAAAARAIGYPVVMKAQAAALGHKSDAGGVILNLKTDDEVRDAFARIYGNVEAYDRSIALDGVLIEKMGKMGTEMIVGAKNDPQWGPVVLAGFGGVTAEILKDVKLFTPEMDAAAVQRGLLELKQAPILKGYRGAPALDVAALAELIVQIGRVMAGNPSIREIDLNPVIIHPAGEGVAALDALMLVER | Function: Catalyzes the formation of feruloyl-CoA, ADP and phosphate from ferulate, CoA and ATP.
Catalytic Activity: (E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + ADP + phosphate
Sequence Mass (Da): 74923
Sequence Length: 707
EC: 6.2.1.34
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Q55DR6 | MSSLSTKTDLLGDPDFIRLQSVEVDGSEVIPGETRPRRNTKFPKLTNSPDGKTFTLYDVYRINKDSDSNFLGIRELLADGKRGDYKWISYKQACIRANNIGSALVQLGLNKGDRIGIFSINRPEWVLSDMAAMNHSLVPVALYATLGANAIEYVVNHSEISVLLCEGKNVEKILSMPGTTIKTIVSYDPLPQATLDKFKDNENVKLYLLSDFEKLGEQNPAQHEVPSPEDLCTLLYTSGSTGNPKGVMLTHTNMVSEVAGANFSPAGVIPEDVHMSYLPLAHSFERAVVSLMCYVGGQIGFFSGLIPELFNDIQVLRPTFLCGAPRVWQRLHDKLWFTVNNDSWLKKFLFNWGLNSKQSALRLGSTTPIWDKLVFSKTKDRLGGRVKFILSGSAPLDPKLAEFLRACFCCPVVSGYGLSENVGGASVAYPEDNNVGHVGPPLSACEMKLIDVPEMNYFSTDKPCPRGEVCIRGFNVFKGYFKDPEKTKEDLKEDGWFHTGDIGRWNENGTLSIIDRKKNIFKLSQGEYVAAEYLESVFVRSPFASQVFVYGDSLNSFLVGVVVPDFEVVQKLFASKYPELDVSNHATLAKSKELYKEILSSFDACAAEAKLHGFEKLKHIYVEHEPFTEENNLLTPSFKPKRPQLKERYQTIIDTLYAEYKRDHPDV | Function: Long chain fatty acid acyl-CoA synthetases catalyze the formation of a thiester bond between a free fatty acid and coenzyme A during fatty acid metabolic process. May mediate fatty acid retrieval from the lumen of endosomes into the cytoplasm.
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74609
Sequence Length: 667
Subcellular Location: Endosome membrane
EC: 6.2.1.3
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Q1ZXQ4 | MINNWLAVGLLVVSGILAFNWKRKHPYGQTVEIGEKPENGGRIRRNSACADHLISFLEDDEIYTLYDSLVKSCKKYGERKCFGERKKDSNGNLGKFEWISYNTYLERCEYIQQGLCELGLKPKSKVGIFSKNRLEWLIVHSASFIQSYCVVSFYETLGVESLSYVTEHAEIGLAFCSAETLQKTLDIAKGVKVLKTIICFDSIDKEHYNIAKELGVTLYTYDEIMKKGKEANGKHKHTPPTPDTLSTIMYTSGTTGPPKGVMITHKNLTSVVCAVSDFIKVYDTDVHYSYLPYAHVLERVVILAAFHFGAAIGIFSGDISNILVEVKLLSPTLFIGVPRVFERIKTNVFKEISKKPALLRTLFNGAYNLKYLSIQHGFKLPIIEKVLDLVFFSKIKQALGGKVRVILSGSAPLSFDTEVFLRVVMCCCVLQGYGASEGCGGDACKRLDDESVGTIGPPFASNEIKLVDVPELGYDSNGEVQTGEVCLRGPSISSGYYKDEEKTREEFKDGWFHTGDIGRWNRDGSLSIVDRKKNIFKLSQGEYVAVEKIETIVVKSEYVEQVCIYGDSQKSCVIAIIHPHPESCSEWAGSKKTDKDIKEICKNQDFIKVVLDDIIKNCKKSGLHGFEIPKAIHLTPEAFSDQNNLLTPSFKLKRHEIKKYFEDEIKKLYSKLD | Function: Long chain fatty acid acyl-CoA synthetases catalyze the formation of a thiester bond between a free fatty acid and coenzyme A during fatty acid metabolic process.
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 75581
Sequence Length: 673
Subcellular Location: Endoplasmic reticulum
EC: 6.2.1.3
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Q84JK2 | MLSSAKHQRNHRLSATNKNQTLTKVSSISSSSPSSSSSSSSTSSSSPLPSQDSQAQKRSLVTMEEVWNDINLASIHHLNRHSPHPQHNHEPRFRGQNHHNQNPNSIFQDFLKGSLNQEPAPTSQTTGSAPNGDSTTVTVLYSSPFPPPATVLSLNSGAGFEFLDNQDPLVTSNSNLHTHHHLSNAHAFNTSFEALVPSSSFGKKRGQDSNEGSGNRRHKRMIKNRESAARSRARKQAYTNELELEVAHLQAENARLKRQQDQLKMAAAIQQPKKNTLQRSSTAPF | Function: Transcription factor required for the transition to flowering promoted by FT.
PTM: Phosphorylated at Thr-282 in a calcium-dependent manner by CPK6 and CPK33.
Sequence Mass (Da): 31377
Sequence Length: 285
Subcellular Location: Nucleus
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Q940E8 | MLTATPLPHQLLATFLLVLASATQPAVPASTDRAALLAFRASLSPPSRAALSSWSGPLSPSWLGVSLHPATAPAPSVTTPSVAELSLRGLNLTGVIPAAPLALLRRLRTLDLSANALSGELPCSLPRSLLALDLSRNALSGAVPTCLPSSLPALRTLNLSANFLRLPLSPRLSFPARLAALDLSRNAISGAVPPRIVADPDNSALLLLDLSHNRFSGEIPAGIAAVRSLQGLFLADNQLSGDIPPGIGNLTYLQVLDLSNNRLSGSVPAGLAGCFQLLYLQLGGNQLSGALRPELDALASLKVLDLSNNKISGEIPLPLAGCRSLEVVDLSGNEISGELSSAVAKWLSLKFLSLAGNQLSGHLPDWMFSFPLLQWLDLSSNKFVGFIPDGGFNVSEVLNGGGGQGTPSESVLPPQLFVSASVDTVSWQLDLGYDVQATTGIDLSGNELCGEIPEGLVDMKGLEYLNLSCNYLAGQIPAGLGGMGRLHTLDFSHNGLSGEVPPGIAAMTVLEVLNLSYNSLSGPLPTTKFPGALAGNPGICSGKGCSENARTPEGKMEGSNHRGWLGGWHGENGWVSLGAFCISTMTSFYVSLATLLCSSNARNFVFRPVRVEY | Function: Receptor-like protein that regulates shoot meristem proliferation. Based on additive and synergistic phenotypes of double mutants, it is probable that unlike CLV1 and CLV2 in A.thaliana, FAE2 and TD1 do not function exclusively in a single pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63951
Sequence Length: 613
Subcellular Location: Cell membrane
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P80668 | MTEPHVAVLSQVQQFLDRQHGLYIDGRPGPAQSEKRLAIFDPATGQEIASTADANEADVDNAVMSAWRAFVSRRWAGRLPAERERILLRFADLVEQHSEELAQLETLEQGKSIAISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLSIPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTMLRVAELASEAGIPDGVFNVVTGSGAVCGAALTSHPHVAKISFTGSTATGKGIARTAADHLTRVTLELGGKNPAIVLKDADPQWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLQVGPGMSPVAQINPLVSRAHCDKVCSFLDDAQAQQAELIRGSNGPAGEGYYVAPTLVVNPDAKLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNLSQALEYSDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCVRY | Function: Acts almost equally well on phenylacetaldehyde, 4-hydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetaldehyde.
Catalytic Activity: 2-phenylacetaldehyde + H2O + NAD(+) = 2-phenylacetate + 2 H(+) + NADH
Sequence Mass (Da): 53699
Sequence Length: 499
Pathway: Amino-acid degradation; L-phenylalanine degradation; phenylacetate from L-phenylalanine: step 3/3.
EC: 1.2.1.39
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P13036 | MTPLRVFRKTTPLVNTIRLSLLPLAGLSFSAFAAQVNIAPGSLDKALNQYAAHSGFTLSVDASLTRGKQSNGLHGDYDVESGLQQLLDGSGLQVKPLGNNSWTLEPAPAPKEDALTVVGDWLGDARENDVFEHAGARDVIRREDFAKTGATTMREVLNRIPGVSAPENNGTGSHDLAMNFGIRGLNPRLASRSTVLMDGIPVPFAPYGQPQLSLAPVSLGNMDAIDVVRGGGAVRYGPQSVGGVVNFVTRAIPQDFGIEAGVEGQLSPTSSQNNPKETHNLMVGGTADNGFGTALLYSGTRGSDWREHSATRIDDLMLKSKYAPDEVHTFNSLLQYYDGEADMPGGLSRADYDADRWQSTRPYDRFWGRRKLASLGYQFQPDSQHKFNIQGFYTQTLRSGYLEQGKRITLSPRNYWVRGIEPRYSQIFMIGPSAHEVGVGYRYLNESTHEMRYYTATSSGQLPSGSSPYDRDTRSGTEAHAWYLDDKIDIGNWTITPGMRFEHIESYQNNAITGTHEEVSYNAPLPALNVLYHLTDSWNLYANTEGSFGTVQYSQIGKAVQSGNVEPEKARTWELGTRYDDGALTAEMGLFLINFNNQYDSNQTNDTVTARGKTRHTGLETQARYDLGTLTPTLDNVSIYASYAYVNAEIREKGDTYGNLVPFSPKHKGTLGVDYKPGNWTFNLNSDFQSSQFADNANTVKESADGSTGRIPGFMLWGARVAYDFGPQMADLNLAFGVKNIFDQDYFIRSYDDNNKGIYAGQPRTLYMQGSLKF | Function: FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85322
Sequence Length: 774
Subcellular Location: Cell outer membrane
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P15030 | MTAIKHPVLLWGLPVAALIIIFWLSLFCYSAIPVSGADATRALLPGHTPTLPEALVQNLRLPRSLVAVLIGASLALAGTLLQTLTHNPMASPSLLGINSGAALAMALTSALSPTPIAGYSLSFIAACGGGVSWLLVMTAGGGFRHTHDRNKLILAGIALSAFCMGLTRITLLLAEDHAYGIFYWLAGGVSHARWQDVWQLLPVVVTAVPVVLLLANQLNLLNLSDSTAHTLGVNLTRLRLVINMLVLLLVGACVSVAGPVAFIGLLVPHLARFWAGFDQRNVLPVSMLLGATLMLLADVLARALAFPGDLPAGAVLALIGSPCFVWLVRRRG | Function: Part of the binding-protein-dependent transport system for citrate-dependent Fe(3+). Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34893
Sequence Length: 332
Subcellular Location: Cell inner membrane
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P15029 | MKIALVIFITLALAGCALLSLHMGVIPVPWRALLTDWQAGHEHYYVLMEYRLPRLLLALFVGAALAVAGVLIQGIVRNPLASPDILGVNHAASLASVGALLLMPSLPVMVLPLLAFAGGMAGLILLKMLAKTHQPMKLALTGVALSACWASLTDYLMLSRPQDVNNALLWLTGSLWGRDWSFVKIAIPLMILFLPLSLSFCRDLDLLALGDARATTLGVSVPHTRFWALLLAVAMTSTGVAACGPISFIGLVVPHMMRSITGGRHRRLLPVSALTGALLLVVADLLARIIHPPLELPVGVLTAIIGAPWFVWLLVRMR | Function: Part of the binding-protein-dependent transport system for citrate-dependent Fe(3+). Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34131
Sequence Length: 318
Subcellular Location: Cell inner membrane
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P15031 | MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEIHPEPVSGRPMCLMR | Function: Part of the binding-protein-dependent transport system for citrate-dependent Fe(3+). Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28191
Sequence Length: 255
Subcellular Location: Cell inner membrane
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P23485 | MNPLLTDSRRQALRSASHWYAVLSGERVSPQQEARWQQWYEQDQDNQWAWQQVENLRNQLGGVPGDVASRALHDTRLTRRHVMKGLLLLLGAGGGWQLWQSETGEGLRADYRTAKGTVSRQQLEDGSLLTLNTQSAADVRFDAHQRTVRLWYGEIAITTAKDALQRPFRVLTRQGQLTALGTEFTVRQQDNFTQLDVQQHAVEVLLASAPAQKRIVNAGESLQFSASEFGAVKPLDDESTSWTKDILSFSDKPLGEVIATLTRYRNGVLRCDPAVAGLRLSGTFPLKNTDAILNVIAQTLPVKIQSITRYWINISPL | Function: Required for transcriptional activation of the fecABCDE operon by sigma factor FecI . Undergoes sequential cleavage to produce an N-terminal cytoplasmic fragment which is released from the membrane and binds to FecI, allowing it to activate transcription of the fecABCDE operon which mediates ferric citrate transport . In the absence of citrate, FecR inactivates FecI .
PTM: Sequentially cleaved starting with cleavage immediately after translation to generate CL(a). CL(a) is then cleaved by an unknown protease in the periplasm to yield CL(b). Finally, CL(b) undergoes intramembrane proteolysis by RseP to produce the N-terminal cytoplasmic fragment CL(c) which is released from the membrane and binds to sigma factor FecI, allowing it to activate transcription of the fecABCDE operon.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35532
Sequence Length: 317
Subcellular Location: Cell inner membrane
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Q6C116 | MGIKGLNKLLMEHCPAALRSSEIKNFGGRKVAIDASMSLYQFVIAVRQADGQQLTNENGETTSHLMGMFYRTLRMVDNGIKPVYVFDGKPPVLKSGELAKRKERREEALKKIEELKQQVEDGEEGEETKEAQEDVTRFEKRTVRVTPEQNDEAKKLLTLMGIPIVEAPCEAEAQCAKLAEAGKVYAAASEDMDTLCFGSPVLLRHLTFSEAKKMPISEINFAKILEGLEMTHAQFIDLCILLGCDYADTIRGVGPQTALKLMKEHGSLEKIVEHIEKNPSGKLKVPENWPYQEVRALLQAPDVLDSSSCDIKWNNPDVEGLVDFLVRDKGFSEDRVRAGAARLMKQVKVKPQARLDGFFKVMPKEGGEKRKADDKKTKGKKPATKKAKK | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
PTM: Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
Sequence Mass (Da): 43446
Sequence Length: 389
Subcellular Location: Nucleus
EC: 3.1.-.-
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P25621 | MMKESKSITQHEVERESVSSKRAIKKRLLLFKIDLFVLSFVCLQYWINYVDRVGFTNAYISGMKEDLKMVGNDLTVSNTVFMIGYIVGMVPNNLMLLCVPPRIWLSFCTFAWGLLTLGMYKVTSFKHICAIRFFQALFESCTFSGTHFVLGSWYKEDELPIRSAIFTGSGLVGSMFSGFMQTSIFTHLNGRNGLAGWRWLFIIDFCITLPIAIYGFIFFPGLPDQTSAVSKFSMTRYIFNEQELHYARRRLPARDESTRLDWSTIPRVLKRWHWWMFSLVWVLGGENLGFASNSTFALWLQNQKYTLAQRNNYPSGIFAVGIVSTLCSAVYMSKIPRARHWHVSVFISLVMVIVAVLIRADPLNPKVVFSAQYLGGVAYAGQAVFFSWANIICHADLQERAIVLASMNMFSGAVNAWWSILFFASDMVPKFERGCYALLATAISSGIVSVVIRSLQIKENLSKKQVPYIDANDMPGEDDDDDNQDNENDGDDESMEVELHNEEMAEISNPFR | Function: Transports pantothenate into the cell. Also involved in the catabolite repression-mediated regulation of ergosterol biosynthesis and in fenpropimorph resistance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58256
Sequence Length: 512
Subcellular Location: Cell membrane
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Q9GNL3 | MFHSLVLMACALAALSVAQGAGSARSKSLPLSLSLSVSVSSSLASASSPGAAADPTAAFTVTATAPTPASAPFAGKQLNRCRQSCYQQLSKDWHYCKDSVDCTNCCQKLVAPFELRILKAQRQESLVLTDIGWDEMIANASRQCLITWEVSGGGLIGNLLTDTARAELSLWPDTVYNIQVKCKHKLTGLMRRSIKLNVDTSQLVGTTTTTTTSKSSIQRQHLEQPVDHTDALEHSQHIRIPRPTDRVYIISALPTPSELGGVVYPAFGALAFFLALLVMFLFLRPQRKRFPLDADSADTATLIGRSSSSSRNSMDASTLHV | Function: Involved in the normal targeting of ventral muscle, muscle 12, by motoneurons. May function as an axon guidance molecule involved in neuromuscular specificity.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 34626
Sequence Length: 321
Subcellular Location: Membrane
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Q9R9J2 | MNNLAFLFPGQGSQFVGMGKSFWNDFVLAKRLFEEASDAISMDVKKLCFDGDMTELTRTMNAQPAILTVSVIAYQVYMQEIGIKPHFLAGHSLGEYSALVCAGVLSFQEAVKLIRQRGILMQNADPEQLGTMAAITQVYIQPLQDLCTEISTEDFPVGVACMNSDQQHVISGHRQAVEFVIKKAERMGANHTYLNVSAPFHSSMMRSASEQFQTALNQYSFRDAEWPIISNVTAIPYNNGHSVREHLQTHMTMPVRWAESMHYLLLHGVTEVIEMGPKNVLVGLLKKITNHIAAYPLGQTSDLHLLSDSAERNENIVNLRKKQLNKMMIQSIIARNYNKDAKTYSNLTTPLFPQIQLLKERVERKEVELSAEELEHSIHLCQLICEAKQLPTWEQLRILK | Function: Is involved in the mycosubtilin synthetase assembly, by catalyzing the transfer of malonyl groups to a specific acyl-carrier-protein domain on MycA.
Catalytic Activity: holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]
Sequence Mass (Da): 45222
Sequence Length: 400
EC: 2.3.1.39
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Q5WAF1 | MQEKEMFDLTIIGGGPAGLYSTFYAGMRDLKVKLVEYNKELGGKILFYPEKIIWDVGGMPPTTGRTLINQLVEQATTFNPTICLNEHIVRMVREPDNTYTLFNEQGKAHYTRAVMLASGHGIPVMQKLEIEGADRYEVSNLHYTVTQMDIFANKRVLISGGGNAAVDWANELANISKEVVVCHRRDEFGGHEKNVEQMKSVTKIHTPYQIKELHGVGSAIEAVTLAHCDTGEQRQIEVDAVIVNHGMKLDGCFLIEAGLALEEDGFLRVSACMETSQPGIFAAGDVTRHEGKLQLISGAFVEGATAVNGVKQFLDPKADKQAYVSSHNEKFKKKNEQLKQEKQAQLMN | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38586
Sequence Length: 348
EC: 1.18.1.2
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A8FB45 | MTEQLELFDVTIIGGGPAGMYTAFYSGMRDLKTKVLEYNESLGGKILLYPEKVIWDVGGLPPTRGEQLIQQLEKQAKTFEPEIALNQKITSFERDEHQNILLTAENGDRHLTKTLILAMGHGIPVQRKLEIEHADRYEVTNLYYTVQELKTFAGKRVVISGGGDSAVDWANALVPIAESVTVVHRRDMFGGHEKNVANMKASCARILTPHELTDLHGQGDKIDAVTIQHLETGEIERIETDAVIVNHGMKGDLSVLSEWGLKQGEWGLIEVNEKMETNLPGVYAVGDLCTHKSKVRLIAGTFVDGVNALNSAKLYIEPEAEKVAYVSSHNERFKEKNKELQTVGAR | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38418
Sequence Length: 346
EC: 1.18.1.2
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O31475 | MAENQEVYDVTIIGGGPIGLFTAFYCGMRELKTKVIEFLPKLGGKVSLFFPEKIIRDIGGIPGIAGKQLIEQLKEQAATFDPDIVLNQRVTGFERLDDGTIVLTGSEGKKHYTRTVILACGMGTLEVNEFDSEDAARYAGKNLHYGVEKLDAFKGKRVVISGGGDTAVDWANELEPIAASVTVVHRREEFGGMESSVTKMKQSSVRVLTPYRLEQLNGDEEGIKSVTVCHTESGQRKDIEIDELIINHGFKIDLGPMMEWGLEIEEGRVKADRHMRTNLPGVFVAGDAAFYESKLRLIAGGFTEGPTAVNSAKAYLDPKAENMAMYSTHHKKLVHK | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36967
Sequence Length: 336
EC: 1.18.1.2
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P24134 | TXIVIIGGGPGGYEAA | Function: Couples electron transfer from NADH to cytochrome P450(soy) in the presence of ferredoxin.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 1486
Sequence Length: 16
EC: 1.18.1.3
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Q8DUN5 | MEEEKLTSEKEIYDITVIGGGPVGLFTAFYAGLRGISVKVIESLSELGGQPAILYPEKVIYDIPAFPAITGADLVDNLIEQLERFKDKTTICLKEEVKTFEKENAIFTITTNKGNHFSKAIIIACGNGAFAPRRLGLDDEERYADHNLFYNVHKLDQFAGKKVVICGGGDSAVDWANALDKIAESVTLVHRRDAFRAHEHSVEVLKTSHVNIMTPYVPLELKGEGDEATSLVIQKVKSEETKELSLDSLIVSFGFSTSNKNLKSWNIDYKRSSINVSPLFETSQTGVFAIGDAAEYEGKIDLIATGFGEAPTAVNQAIKYIYPERDNRVVHSTSLIK | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 37155
Sequence Length: 337
EC: 1.18.1.2
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P23877 | MIYVSRRLLITCLLLVSACVVAGIWGLRSGAVTLETSQVFAALMGDAPRSMTMVVTEWRLPRVLMALLIGAALGVSGAIFQSLMRNPLGSPDVMGFNTGAWSGVLVAMVLFGQDLTAIALSAMVGGIVTSLLVWLLAWRNGIDTFRLIIIGIGVRAMLVAFNTWLLLKASLETALTAGLWNAGSLNGLTWAKTSPSAPIIILMLIAAALLVRRMRLLEMGDDTACALGVSVERSRLLMMLVAVVLTAAATALAGPISFIALVAPHIARRISGTARWGLTQAALCGALLLLAADLCAQQLFMPYQLPVGVVTVSLGGIYLIVLLIQESRKK | Function: Part of the ABC transporter complex FepBDGC involved in ferric enterobactin uptake . Responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34910
Sequence Length: 330
Subcellular Location: Cell inner membrane
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P17007 | MAVYKVRLICEEQGLDTTIECPDDEYILDAAEEQGIDLPYSCRAGACSTCAGKVVEGTVDQSDQSFLDDAQLAAGYVLTCVAYPSSDCTVKTHQEESLY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10726
Sequence Length: 99
Subcellular Location: Plastid
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P00239 | SYMVTLKTPSGEQKVEVSPDSYILDAAEEAGVDLPYSCRAGSCSSCAGKVESGTVDQSDQSFLDDDQMDSGFVLTCVAYATSDCTIVTHQEENLY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10162
Sequence Length: 95
Subcellular Location: Plastid
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O78510 | MATYKVKLSGEGVDKTIDCPDDQYILDAAEEQGIDLPYSCRAGACSTCAGKVAAGSVDQSDQSFLDDSQIGDGFVLTCVAYPTSDCTILTHQEEGLY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10281
Sequence Length: 97
Subcellular Location: Plastid
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D0LZ73 | MSSEQLHEPAELLSEETKNMHRALVTLIEELEAVDWYQQRADACSEPGLHDVLIHNKNEEVEHAMMTLEWIRRRSPVFDAHMRTYLFTERPILELEEEDTGSSSSVAASPTSAPSHGSLGIGSLRQEGKED | Function: Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like ferroxidase that converts Fe(2+) to Fe(3+) iron inside the encapsulin nanocompartment . Mineralized Fe(3+) is released to the exterior of the decameric complex for deposition in the encapsulin nanocompartment. In solution the decamer binds 10-15 iron cations; in the encapsulin nanocompartment the decamer can bind up to 48 ions, perhaps via its internal channel, and on its exterior. The cargo-loaded nanocompartment maximally sequesters up to 4150 Fe ions (By similarity).
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 14799
Sequence Length: 131
Domain: The decamer has negatively charged patches on its exterior, and a negatively charged tunnel at the center, the charges are probably metal-binding sites.
Subcellular Location: Encapsulin nanocompartment
EC: 1.16.3.1
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P00225 | AFKVKLLTPDGPKEFECPDDVYILDQAEELGIELPYSCRAGSCSSCAGKLVEGDLDQSDQSFLDDEQIEEGWVLTCAAYPRSDVVIETHKEEELTG | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10588
Sequence Length: 96
Subcellular Location: Plastid
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P09735 | TFKVTLNTPTGQSVIDVEDDEYILDAAEEAGLSLPYSCRAGACSSCAGKVTAGEVDQSDESFLDDDQMDEGYVLTCIAYPTSDLTIDTHQEEALI | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10174
Sequence Length: 95
Subcellular Location: Plastid
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Q8TQQ5 | MVWHYTNDVALYCRAFRSMPHCLRERQYFMVKDHDLLLKLTGELVSVNINRYKCGYCGACVGVCPKGALELVETWIEVDESTCIKCGICDRICPVGAIEVMK | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Ferredoxin that is the specific electron donor for the geranylgeranyl reductase GGR involved in the biosynthesis of archaeal membrane lipids.
Sequence Mass (Da): 11624
Sequence Length: 102
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
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P02765 | MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCMVFQTQPVSSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKV | Function: Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions.
PTM: Phosphorylated by FAM20C in the extracellular medium.
Sequence Mass (Da): 39341
Sequence Length: 367
Subcellular Location: Secreted
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P80191 | LVLLLSLAQLWSCHLVTAVPLLGYREHNCDDPEAEQVALLAVDHINNHLQQGYKHILNRIDKVKVWPRRPTGEVYELEIDTLETTCHALDPTPLANCSVRQVTQHAVEGDCDFHVLKQDGQFTVLSAKCDSTPDSAEDILKLCPDCPLLTPLNDTRVAQAAEAALTAFNEKNNGAYLQLVEIARAQLVPLPASTYVEFTVAATDCVAKEVTDPAKCNLLADKQYGFCKATVAEKVAREEVEVTCTIFPAQPVVPQPQPGVAGAAAVEPAPAVDPASPVSPPDGQSPSSLVVGPVLVAQAPAPPRAHYDLRQTFAGVPSMESGSGEAFHPGKVPVVVQPSVGAAPGPVITPCPGKVRYFKI | Function: A cell adhesion protein that binds immature cells of the granulocyte lineage.
PTM: Phosphorylated by FAM20C in the extracellular medium.
Sequence Mass (Da): 38387
Sequence Length: 360
Subcellular Location: Secreted
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P24090 | MKSLVLLLCFAQLWSCQSAPQGAGLGFRELACDDPETEHVALIAVDYLNKHLLQGFRQILNQIDKVKVWSRRPFGEVYELEIDTLETTCHALDPTPLANCSVRQQAEHAVEGDCDFHILKQDGQFRVLHAQCHSTPDSAEDVRKFCPRCPILIRFNDTNVVHTVKTALAAFNAQNNGTYFKLVEISRAQNVPFPVSTLVEFVIAATDCTGQEVTDPAKCNLLAEKQYGFCKATLIHRLGGEEVSVACKLFQTQPQPANANPAGPAPTVGQAAPVAPPAGPPESVVVGPVAVPLGLPDHRTHHDLRHAFSPVASVESASGEVLHSPKVGQPGDAGAAGPVAPLCPGRVRYFKI | Function: Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma cells.
PTM: Undergoes complex post-translational modification involving N-glycosylation, and addition of fucose and sialic acid residues. Phosphorylation occurs at a serine residue.
Sequence Mass (Da): 37982
Sequence Length: 352
Subcellular Location: Secreted
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P37237 | MGSPRSALSCLLLHLLVLCLQAQVRSAAQKRGPGAGNPADTLGQGHEDRPFGQRSRAGKNFTNPAPNYPEEGSKEQRDSVLPKVTQRHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR | Function: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. Required for normal brain, eye, ear and limb development during embryogenesis. Required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Plays a role in neurite outgrowth in hippocampal cells (By similarity). Cooperates with Wnt-1 in mouse mammary tumor virus-induced murine mammary tumorigenesis .
PTM: The N-terminus is blocked.
Sequence Mass (Da): 30420
Sequence Length: 268
Subcellular Location: Secreted
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A8MR65 | MDDADKSCSPSLDHSDINDPMIVAVESLDTSKKRKLHAEESDLLPLPKHFCSEHQASLVNSSCPSSVIDYAECSYAMENTKTSDEASSSASFTGPSLYMFKDSIYSTGSSSSGYAATSSIEQCFSKVDHKTQEDTQDFTHMEFIYHDSEFAVEDLQEVLNPVESYILSSARWSVSNQDSKEATTKPTIDQEFEQYFSTLMM | Function: Can activate transcription (By similarity). Essential for light-regulated PHYA nuclear accumulation and subsequent PHYA phototropic signaling processes . PHYA-specific signal transducer in response to continuous FR lights. Mediates the association of PHYA with HFR1 and LAF1 in the nucleus in response to FR conditions . Contributes to inhibition of hypocotyl elongation in continuous blue light (B) .
PTM: Inactivated by rapid reversible PHYA-mediated phosphorylation.
Sequence Mass (Da): 22376
Sequence Length: 201
Subcellular Location: Nucleus
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P96809 | MTGISRRTFGLAAGFGAIGAGGLGGGCSTRSGPTPTPEPASRGVGVVLSHEQFRTDRLVAHAQAAEQAGFRYVWASDHLQPWQDNEGHSMFPWLTLALVGNSTSSILFGTGVTCPIYRYHPATVAQAFASLAILNPGRVFLGLGTGERLNEQAATDTFGNYRERHDRLIEAIVLIRQLWSGERISFTGHYFRTDELKLYDTPAMPPPIFVAASGPQSATLAGRYGDGWIAQARDINDAKLLAAFAAGAQAAGRDPTTLGKRAELFAVVGDDKAAARAADLWRFTAGAVDQPNPVEIQRAAESNPIEKVLANWAVGTDPGVHIGAVQAVLDAGAVPFLHFPQDDPITAIDFYRTNVLPELR | Function: Catalyzes the coenzyme F420-dependent oxidation of hydroxymycolic acids (H-MAs) to ketomycolic acids (K-MAs), a lipid class making up the mycobacterial pseudo-outer membrane and over one-third of the dry weight of M.tuberculosis . Does not exhibit F420-dependent glucose-6-phosphate dehydrogenase (FGD) activity .
PTM: Is exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 38445
Sequence Length: 360
Pathway: Lipid metabolism; mycolic acid biosynthesis.
Subcellular Location: Cell envelope
EC: 1.1.98.-
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Q988C8 | MIRNIAIIGLGTMGPGMAARLARGGLQVVAYDVAPAAIERARSMLSVAETVLDALGIALPSAGVGTVRFTDDIGDAVSGADLVIENVPENISIKADVYRTIDGLIGQDTIVASDTSGIPITKLQAHISYPERMVGMHWSNPPHIIPMIEVIAGEKTAPQTVATIRDLIRSIGLLPVVVKKDVPGFVENRVLYALLREAVDLVERGVIDPEDLDTCVSWGIGYKIAVIGPMALLDMAGLDIYKSVSSFLNADLSNRDDVAPMVLEKTSASKFGIKSGEGMFCYTPEQTKALQAERARKLVAVRRILEGRE | Function: Involved in the degradation of pyridoxine (vitamin B(6)). Catalyzes the oxidation of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate (FHMPC) by NAD(+) to 5-hydroxy-6-methylpyridine-3,4-dicarboxylate (HMPDC) . Can also catalyze the reduction of FHMPC by NADH to 4-pyridoxic acid .
Catalytic Activity: 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + H2O + NAD(+) = 5-hydroxy-6-methylpyridine-3,4-dicarboxylate + 2 H(+) + NADH
Sequence Mass (Da): 33061
Sequence Length: 309
Pathway: Cofactor degradation; B6 vitamer degradation.
EC: 1.2.1.100
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P53279 | MLSAADNLVRIINAVFLIISIGLISGLIGTQTKHSSRVNFCMFAAVYGLVTDSLYGFLANFWTSLTYPAILLVLDFLNFIFTFVAATALAVGIRCHSCKNKTYLEQNKIIQGSSSRCHQSQAAVAFFYFSCFLFLIKVTVATMGMMQNGGFGSNTGFSRRRARRQMGIPTISQV | Function: Involved in membrane organization. Required for the formation of membrane compartments of CAN1 (MCCs), localization of CAN1 at the MCCs and subsequent invagination of the plasma membrane at the MCCs sites. Involved in eisosome organization and might act as a sensor of sphingolipids that regulates plasma membrane function. Involved in a novel pathway of export of proteins that lack a cleavable signal sequence. Non-classical export pathway functions also as an alternative clearance/detoxification pathway to eliminate damaged material, when the basic repair pathway is not sufficient.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19152
Sequence Length: 174
Subcellular Location: Cell membrane
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Q59MV9 | MTVEYETKQLTPAQIKIILDTVPILEEAGETLTQKFYQRMIGNYDEVKPFFNTTDQKLLRQPKILAFALLNYAKNIEDLTPLTDFVKQIVVKHIGLQVLPEHYPIVGTCLIQTMVELLPPEIANKDFLEAWTIAYGNLAKLLIDLEAAEYAKQPWRWFKDFKVTRIVQECKDVKSVYFTPVDKDLLPLPKPERGQYLCFRWKLPGEEFEISREYSVSEFPKENEYRISVRHVPGGKISGYIHNNLKVGDILKVAPPAGNFVYDPATDKELIFVAGGIGITPLLSMIERALEEGKNVKLLYSNRSAETRAFGNLFKEYKSKFGDKFQAIEYFSEDNNTDDKIVIDKAFNRKLTTDDLDFIAPEHDVYLVGPREFMKDIKEHLGKKNVPVKLEYFGPYDP | Cofactor: Binds 1 FAD per subunit.
Function: Nitric oxide dioxygenase involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Plays a role in virulence since nitric oxide is generated by macrophages of the host immune system.
Catalytic Activity: NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate
Sequence Mass (Da): 45819
Sequence Length: 398
Domain: Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Subcellular Location: Cytoplasm
EC: 1.14.12.17
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Q03331 | MSAAKQLFKIVPLTPTEINFLQSLAPVVKEHGVTVTSTMYKYMFQTYPEVRSYFNMTNQKTGRQPKVLAFSLYQYILHLNDLTPISGFVNQIVLKHCGLGIKPDQYPVVGESLVQAFKMVLGEAADEHFVEVFKKAYGNLAQTLIDAEASVYKTLAWEEFKDFRVTKLVKEAEDVTSVYLTPVDGFKLKPIIPGEYISFRWDIHNPDITDIQPREYSISQDVKENEYRISVRDIGIVSDYINKKLQVGDIVPVHAPVGTMKYDSISKKGKVAVLAGGIGITPMIPIIEHALKDGKDVELYYSNRSYQSEPFREFFSNLEKENNGKFKLNNYISAENQKLQVKDLEHINPDEYDVYLLGPVAYMHEFKTYLVGKGVSDLKMEFFGPTDPDC | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity).
Catalytic Activity: NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate
Sequence Mass (Da): 44363
Sequence Length: 390
Domain: Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Subcellular Location: Cytoplasm
EC: 1.14.12.17
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Q9URY5 | MSSVEVNRENADVANTNRQANLAEGYEIKELNESQKQYIRSSIPILESSGVNLTKAFYQKMLGNYPEVLPYFNKAHQISLSQPRILAFALLNYAKNIDDLTSLSAFMDQIVVKHVGLQIKAEHYPIVGHCLLSTMQELLPSDVATPAFLEAWTTAYGNLAKILIDSEKKVYQSQPWNGFVEFKVTELINESSDVKSVYLGPKDPAFRISHAHPGQYVSVLWEIPGLSHKTLREYSLSNRVDTCRNQFRISVRRVAGGVVSNFVHDNLKVGDIVGVSPPAGNFVYKRSEENVNRPLLCFAGGIGITPLIPIIETALLDGRKVNFCYSSRNYVSRPFKQWLEQLKLKYKENLKLKEFFSEESSVTKEQIVDEVMTRIINEEDLEKLDLSECDIYMLGPNNYMRFVKQELVKLGVEPNKVQSEFFGPYIP | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity).
Catalytic Activity: NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate
Sequence Mass (Da): 48459
Sequence Length: 427
Domain: Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Subcellular Location: Cytoplasm
EC: 1.14.12.17
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P39676 | MLAEKTRSIIKATVPVLEQQGTVITRTFYKNMLTEHTELLNIFNRTNQKVGAQPNALATTVLAAAKNIDDLSVLMDHVKQIGHKHRALQIKPEHYPIVGEYLLKAIKEVLGDAATPEIINAWGEAYQAIADIFITVEKKMYEEALWPGWKPFDITAKEYVASDIVEFTVKPKFGSGIELESLPITPGQYITVNTHPIRQENQYDALRHYSLCSASTKNGLRFAVKMEAARENFPAGLVSEYLHKDAKVGDEIKLSAPAGDFAINKELIHQNEVPLVLLSSGVGVTPLLAMLEEQVKCNPNRPIYWIQSSYDEKTQAFKKHVDELLAECANVDKIIVHTDTEPLINAAFLKEKSPAHADVYTCGSLAFMQAMIGHLKELEHRDDMIHYEPFGPKMSTVQV | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
Catalytic Activity: NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate
Sequence Mass (Da): 44646
Sequence Length: 399
Domain: Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Subcellular Location: Cytoplasm
EC: 1.14.12.17
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A7LXW1 | MRNTRYGFLVLLSSLLMLTGCSRRDILDDYPVSGVDIKLDWDGVTDQLPEGVRVIFYPKNGDGRKVDKYLSVRGGEMKVPPGRYSVVVYNYNTESIRIRGEESYETIEAYTGNCNGLGIEGTEKMVWSPDSLYVLNIDELKIEKSEEVLRLDWKLESVVKKYSFAVEAKGLEYVATVVGSIDGLSDCYCIGKGRGVCSSQPIYFEVKKGDNKVTAFFTAFKQVKEMTMPTRMSTSERETSSEKGAIILILKFIKTDNTVQEATIDVTEIIGTLENAGTGEDGKPTPPPEIELPPDDKIEVDKPETPPNPDGGGGMGGNVDGWGPEDNVELPVN | Function: Putative fimbrium anchoring subunit.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36725
Sequence Length: 333
Subcellular Location: Cell outer membrane
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A0PA81 | MNDAKKYIVSVLILLVAGMFGGCIKEDYSDCPRPFRLTVRAWDADMQDITETGAVQRVVIFVFDETGRRIDRLMMDAAQVAARKPIPLEYDGPTTVSFVAWANPDDHMLEETANVQNVKDLFFRLSSTDGIAQSPGDLFSGVLTCPIEYGSIEQGTDQTVDIYRRTAQVHIIIRGYQEWLEANGPRQLPDYADILLGETPDTYTGLAELIGNAVQYRPDGQIQNGDFISPIIRVYPTLDTTPLHLKLYAYGQELLNISTGSDGVPFIPVIGKMLNIYIDLRGANLNVLVSVTPWDVVQQYAEY | Function: Anchoring subunit of the major fimbriae. Regulates fimbrial length . These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. Fimbriae of P.gingivalis are major virulence factors (Probable).
Location Topology: Lipid-anchor
Sequence Mass (Da): 33805
Sequence Length: 303
Subcellular Location: Cell outer membrane
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P33410 | MKQIPLILAMSLAFAAAAKGESAPDMQAAVNFDSAMLWGGANGADLSRFNYSNALRPGNYIVDIYANNYPLIRQQVRFVAAQTSGQGLKTAPAVACFTYGQLEAMQVRLRALDPALVADLKSSGRCEVLGKLFPDSRESFDFGENRLEVSIPQAYTINRFRRDISPDEWDSGITAFRLGYQYNYADYIGGLRAGRRLDLNLYSGFNFKGWYLRNSSTLGWGQGRFTRRSQRTSLQTDIPSWRARLVFGDVFSSGEYFAPYSMRGMLVGSDTAMLPYSERLYRPTIRGVARTRANVKVYQAGVLVFQDAVPPGPFAIDDYSPASYGGDLRVVVTEANGAVQTFTVPYASAVRLILPGQTQWSFSAGRYRNYRNDGQDRPWVTQLTGRHGVADGVNLYGGLLIAQAYQAGLAGLSWNTPWGAMAADATLSRSQLSTTGNANGSSLRFSYSKTLSGTNTAIRLATLRYSSSGFWNFADAVNAGPVETNGRNGRFGLYSLLGRERPRGDFSVTLSQPLGGYGSLYVSALRRTYWGSSRVDQQTQLGYSTQVGRVGVNLDVSRTENRRSTEHQVMLNLSIPLYGATSSGVVTGSLARTGSAPVQQSVNYSGMSGERDQYTYGLGVQRAGTSAQYALNGSWSGTYGEVSGQLTHGRSYSQYQINGSGGLVAHAGGVTFGQYQAGTIGLIQAEAAAGAKVVNTRNAAVDRSGYGLVSLTPYSLNEVELSPQDLPLDVQLESTVEQVIPRAGAVVALRFPTRHDVAAMLVAEPGSEGALVFGTEVRDGAGKVVGVAGQGASALVRGVSASGTLEVTRADGSICRATYDLKSAGQAVHGLPRIALACAPQGGGERGARAAGQAVAQPSAISISGKDHEPDIR | Function: Probable porin-like protein necessary for the assembly of a pilin-type protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93369
Sequence Length: 873
Subcellular Location: Cell outer membrane
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B7YZT2 | MEDLLNEVVPQEDLERFEKKYHHELELDGEVTTDTKFEYAFCLVRSRYTNDVRKGIMILEELARTHPDGRRDYIYYLAFGNARIKEYTSGLKYCRAFLDIESNDQVRSLEEYIKKEIDKEVAKGMVVAGGAALVLGGILGLGIAMARNKQKREK | Function: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering . Functions downstream of Pink1 and upstream of Drp1 to regulate mitochondrial fission .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17771
Sequence Length: 154
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Subcellular Location: Mitochondrion outer membrane
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Q4IBU4 | MVTELPYALDAETPLNPSELNVLKAQYDREGEMVGVQTKFNYAWGLVKSNQRNDQQLGVRLLSDIFRVSPERRRECLYYLALGNYKLGNYGEARRYNDLLLDKEPANLQASNLRSLIDDKVAREGLMGVAILSGVGVAAGVVGAFLLRNARKR | Function: Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17134
Sequence Length: 153
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Subcellular Location: Mitochondrion outer membrane
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Q9Y3D6 | MEAVLNELVSVEDLLKFEKKFQSEKAAGSVSKSTQFEYAWCLVRSKYNDDIRKGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS | Function: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering . Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission . May not be essential for the assembly of functional fission complexes and the subsequent membrane scission event . Also mediates peroxisomal fission . May act when the products of fission are directed toward mitochondrial homeostasis, mitophagy, or apoptosis . Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis .
PTM: Ubiquitinated by MARCHF5.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16938
Sequence Length: 152
Domain: The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L.
Subcellular Location: Mitochondrion outer membrane
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Q9CQ92 | MEAVLNELVSVEDLKNFERKFQSEQAAGSVSKSTQFEYAWCLVRSKYNEDIRRGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS | Function: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering . Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission . May not be essential for the assembly of functional fission complexes and the subsequent membrane scission event (By similarity). Also mediates peroxisomal fission (By similarity). May act when the products of fission are directed toward mitochondrial homeostasis, mitophagy, or apoptosis (By similarity). Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis (By similarity).
PTM: Ubiquitinated by MARCHF5.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17009
Sequence Length: 152
Domain: The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L.
Subcellular Location: Mitochondrion outer membrane
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Q7S8M1 | MTQLPYAVDAETPLNPAELNVLRAQYEKEGEMVGVQTKFNYAWGLVKSNVRADQHLGVMLLSEIFRTSPERRRECLYYLALGNYKLGNYAQARKYNDALLENEPANLQAANLRALIDDKVTKEGLMGVAIISGVAVAAGVIGGVLLRNLGRKR | Function: Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16924
Sequence Length: 153
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Subcellular Location: Mitochondrion outer membrane
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P84817 | MEAVLNELVSVEDLKNFERKFQSEQAAGSVSKSTQFEYAWCLVRSKYNDDIRRGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS | Function: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering . Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission (By similarity). May not be essential for the assembly of functional fission complexes and the subsequent membrane scission event (By similarity). Also mediates peroxisomal fission (By similarity). May act when the products of fission are directed toward mitochondrial homeostasis, mitophagy, or apoptosis (By similarity). Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis (By similarity).
PTM: Ubiquitinated by MARCHF5.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16995
Sequence Length: 152
Domain: The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L.
Subcellular Location: Mitochondrion outer membrane
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Q9USZ8 | MTEKHTLRLADPSAIDSIISVDEFLQIKEQYDAEQPLITLQTKFNLAWALVRSDSTQHVQQGLSLFCSIYKDSPERRLECLYYIALSHYKLKQYEESRRYLNMLLSKDPNSPEALKLKNRLYDAVTKEGYIGMVVVAGAVVSVAALVGWASKRLFSKRRP | Function: Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18329
Sequence Length: 160
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Subcellular Location: Mitochondrion outer membrane
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Q4P7J4 | MSLPYAADAETSLSPSELQVLKSQYETELASGHVTTQTKFNYAWGLVKSKQRAEMSIGVGLLTEIYRSDPPRRRECLYYLSLGHYKMGNYDEARRFNALLIEREPNNLQAQSLNQLIEKGVAREGYIGMALIGGAAAVASIAIAGLMRRGRR | Function: Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16900
Sequence Length: 152
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Subcellular Location: Mitochondrion outer membrane
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Q6CFJ0 | MKKEDYLPNLVDIESPLSDEELYVLSQQYNNEGDFVSVQTRFNYAWGLIKSRKVEDQQLGVQILAQVYKDTPSRRRECLYYLAIGSYKLGEYTDARKYCDLLLQIEPDDPQSAKLRQIIEDKLAKEGMIGIAIVGGVIAVGAAVLGAVLSQKKR | Function: Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17392
Sequence Length: 154
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Subcellular Location: Mitochondrion outer membrane
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P40515 | MTKVDFWPTLKDAYEPLYPQQLEILRQQVVSEGGPTATIQSRFNYAWGLIKSTDVNDERLGVKILTDIYKEAESRRRECLYYLTIGCYKLGEYSMAKRYVDTLFEHERNNKQVGALKSMVEDKIQKETLKGVVVAGGVLAGAVAVASFFLRNKRR | Function: Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17733
Sequence Length: 155
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Subcellular Location: Mitochondrion outer membrane
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Q59207 | MHVTRDFSHYVRTAGEGIKHIDLAVEGVHCAGCMAKIERGLSAIPDVTLARVNLTDRRVALEWKAGTLDPGRFIDRLEELGYKAYPFETESAEVAEVAESRFLLRCLGVAAFATMNVMMLSIPVWSGNVSDMLPEQRDFFHWLSALIALPAAAYAGQPFFRSAWRALSAKTTNMDVPISIGVILALGMSVVETIHHAEHAYFDAAIMLLTFLLVGRFLDQNMRRRTRAVAGNLAALKAETAAKFVGPDEISQVPVAAISPGDIVLLRPGERCAVDGTVIEGRSEIDQSLITGETLYVTAEQGTPVYAGSMNISGTLRVRVSAASEATLLAEIARLLDNALQARSRYMRLADRASRLYAPVVHATALITILGWVIAGASWHDAIVTGVAVLIITCPCALGLAIPTVQTVASGAMFKSGVLLNSGDAIERLAEADHVIFDKTGTLTLPDLEVMNAADIPADIFELAGRLALSSHHPVAAAVAQAAGARSPIVGAVEEAGQGVRADVDGAEIRLGRPSFCGAEALVGDGTRLDPEASIVAFSKGAEKFILWVRQGLRPDAQAVIAALKARNIGIEILSGDREPAVKAAAHALAIPEWRAGVTPADKIARIEELKRRGARVLMVGDGMNDAPSLAAAHVSMSPISAAHLSQATADLVFLGRPLAPVAAAIDSARKALHLMRQNLWLAIGYNVLAVPVAISGVVTPLIAAAAMSGSSILVMLNSLRARSDSREIV | Function: FixI is a pump of a specific cation involved in symbiotic nitrogen fixation. The four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalyzed by FixG.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77339
Sequence Length: 730
Subcellular Location: Cell membrane
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P18398 | MSCCASSAAIMVAEGGQASPASEELWLASRDLGGGLRQTELSVPNAYCGTCIATIEGALRAKPEVERARVNLSSRRVSIVWKEEVGGRRTNPCDFLHAIAERGYQTHLFSPGEEEGDDLLKQLILAVAVSGFAATNIMLLSVSVWSGADAATRDLFHWISALIAGPALIYAGRFFYKSAWNAIRHGRTNMDVPIALAVSLSYGMSLHETIGHGEHAWFDASVTLLFFLLIGRTLDHMMRGRARTAISGLARLSPRGATVVHPDGSREYRAVDEINPGDRLIVAAGERVPVDGRVLSGTSDLDRSVVNGESSPTVVTTGDTVQAGTLNLTGPLTLEATAAARDSFIAEIIGLMEAAEGGRARYRRIADRAARYYSPAVHLLALLTFVGWMLVEGDVRHAMLVAVAVLIITCPCALGLAVPVVQVVAAGRLFQGGVMVKDGSAMERLAEIDTVLLDKTGTLTIGKPRLVNAHEISPGRLATAAAIAVHSRHPIAVAIQNSAGAASPIAGDIREIPGAGIEVKTEDGVYRLGSRDFAVGGSGPDGRQSEAILSLDFRELACFRFEDQPRPASRESIEALGRLGIATGILSGDRAPVVAALASSLGISNWYAELSPREKVQVCAAAAEAGHKALVVGDGINDAPVLRAAHVSMAPATAADVGRQAADFVFMHERLSAVPFAIETSRHAGQLIRQNFALAIGYNVIAVPIAILGYATPLVAAVAMSSSSLVVVFNALRLKRSLAAGRGATPGTLIHSGAVTS | Function: FixI is a pump of a specific cation involved in symbiotic nitrogen fixation. The four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalyzed by FixG.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79559
Sequence Length: 757
Subcellular Location: Cell membrane
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P23221 | MTTKGHIYVIDDDAAMRDSLNFLLDSAGFGVTLFDDAQAFLDALPGLSFGCVVSDVRMPGLDGIELLKRMKAQQSPFPILIMTGHGDVPLAVEAMKLGAVDFLEKPFEDDRLTAMIESAIRQAEPAAKSEAVAQDIAARVASLSPRERQVMEGLIAGLSNKLIAREYDISPRTIEVYRANVMTKMQANSLSELVRLAMRAGMLND | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: FixJ, when activated by FixL, induces the expression of both nifA, required for activation of classical nif and fix genes, and fixK, required for FixN activation.
PTM: Phosphorylated by FixL.
Sequence Mass (Da): 22318
Sequence Length: 205
Subcellular Location: Cytoplasm
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P10958 | MTDYTVHIVDDEEPVRKSLAFMLTMNGFAVKMHQSAEAFLAFAPDVRNGVLVTDLRMPDMSGVELLRNLGDLKINIPSIVITGHGDVPMAVEAMKAGAVDFIEKPFEDTVIIEAIERASEHLVAAEADVDDANDIRARLQTLSERERQVLSAVVAGLPNKSIAYDLDISPRTVEVHRANVMAKMKAKSLPHLVRMALAGGFGPS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: FixJ, when activated by FixL, induces the expression of both nifA, required for activation of classical nif and fix genes, and fixK, required for FixN activation.
PTM: Phosphorylated by FixL.
Sequence Mass (Da): 22219
Sequence Length: 204
Subcellular Location: Cytoplasm
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P26489 | MTDTPTQALPPKAPQAGPTVPGTVRRAVPGSAAAALVIAASHFAALSAFDPRILLVLLVIVVLASSGGLFAGLAATAVSALGLALRGLLSGDTVVADWQSLGLLTIAGAGIAVLGERLRRTRLDAVARDRALLAREAHLSSILDTVPDAMIVIDERGIMQSFSITAERLFGYSPSEVIGRNVSMLMPNPHRDQHDLYLSRYLTTGERRIIGIGRVVTGERKDGATFPMELAVGEMHSVSGRFFTGFIRDLTERQNTEARLQELQAELVHISRLTALGEMASTLAHELNQPLSAIANYIKGSRRLLDDGDPKRIPMLQGALDKAAEQALRAGQIIRRLRDFVSRGETERRVESLSKLIEEASALALVGAKEHGIQVRYQIDTSCDLVLADKVQVQQVLLNLMRNALEAMMDASRRQLLVQTTPAEDDMVTVSVCDTGHGISDEMRAQLFTPFVTTKAQGMGVGLSISRTIIEAHGGRIWAEPNAGGGTIFRFTLRTVDEEAMNDA | Cofactor: Binds 1 heme group per subunit.
Function: Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54319
Sequence Length: 504
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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P23222 | MAPTRVTHPPDDGRGEHFRVRIEGFGVGTWDLDLKTWALDWSDTARTLLGIGQDQPASYDLFLSRLEPDDRERVESAIKRVSERGGGFDVSFRVAGTSNAGQWIRARAGLIRDEAGTARHLSGIFLDIDEEKQVEGALRTRETHLRSILHTIPDAMIVIDGHGIIQLFSTAAERLFGWSELEAIGQNVNILMPEPDRSRHDSYISRYRTTSDPHIIGIGRIVTGKRRDGTTFPMHLSIGEMQSGGEPYFTGFVRDLTEHQQTQARLQELQSELVHVSRLSAMGEMASALAHELNQPLAAISNYMKGSRRLLAGSSDPNTPKVESALDRAAEQALRAGQIIRRLRDFVARGESEKRVESLSKLIEEAGALGLAGAREQNVQLRFSLDPGADLVLADRVQIQQVLVNLFRNALEAMAQSQRRELVVTNTPAADDMIEVEVSDTGSGFQDDVIPNLFQTFFTTKDTGMGVGLSISRSIIEAHGGRMWAESNASGGATFRFTLPAADEN | Cofactor: Binds 1 heme group per subunit.
Function: Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 55652
Sequence Length: 505
EC: 2.7.13.3
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P10955 | MLSKSGIERTQWGRRVVRWRGDGVAAYIVAAIVTSSVLAIRMIRAEPIGEGLLLFSFIPAILVVALIGGRNPILFAAGLSLVAAVSHQQISSADGPSVVELLVFGSAVLLIVALGEVLEAARRAIDRTEDVVRARDAHLRSILDTVPDATVVSATDGTIVSFNAAAVRQFGYAEEEVIGQNLRILMPEPYRHEHDGYLQRYMATGEKRIIGIDRVVSGQRKDGSTFPMKLAVGEMRSGGERFFTGFIRDLTEREESAARLEQIQAELARLARLNEMGEMASTLAHELNQPLSAIANYSHGCTRLLRDMDDAVATRIREALEEVASQSLRAGQIIKHLREFVTKGETEKAPEDIRKLVEESAALALVGSREQGVRTVFEYLPGAEMVLVDRIQVQQVLINLMRNAIEAMRHVDRRELTIRTMPADPGEVAVVVEDTGGGIPEEVAGQLFKPFVTTKASGMGIGLSISKRIVEAHGGEMTVSKNEAGGATFRFTLPAYLDERIVAND | Cofactor: Binds 1 heme group per subunit.
Function: Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55073
Sequence Length: 505
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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P98055 | MNYTLETADRALGAFPALLGAAFAHDSLFAAHMWVLFFTLVVSTLLLLRRVSFLPPVAGPPCRRTEYFDEVVKYGVMATVFWGVVGFLVGVVVALQLAFPDLNIAPYFNFGRMRPLHTSAVIFAFGGNALIATSFYVVQRTCRARLFGGNLGWFVFWGYNLFIIMAATGYLLGITQGREYAEPEWYVDLWLTIVWVAYLATFLGTILTRKEPHISVANWFYLSFIVTIAMLHIVNNLAVPVSFLGVKSYSAFSGVQAALTQWWYGHNAVGFFLTAGFLGMMYYFIPKQVNRPVYSYRLSIIHFWALIFMYIWAGPHHLHYTALPDWAQTLGMVFSIMLWMPSWGGMINGLMTLSGAWDKIRTDPIVRMMVMAVAFYGMATFEGPMMSIKAVNSLSHYTDWTIGHVHSGALGWNGMITFGAIYYLTPKLWGRDRLYSLQLVNWHFWLATLGIVVYAAVMWVAGIQQALMWREYDSQGFLVYSFAESVAALFPYYVMRALGGLMFLSGALIMAYNVTMTILGHQREEGASKGAAPSLQPAE | Cofactor: Binds 1 copper ion per subunit, denoted as copper B.
Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60651
Sequence Length: 539
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Cell membrane
EC: 7.1.1.9
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