ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q668V1 | MGASATNSVTHPAFTLNVRPDNIGIITIDVVGDKVNTLKAEFADQIATILQQAHALPKLQGLVIVSGKPDSFIAGADITMIAACRTAHDARVLAQKGQSILAQIAAFPVPVVAAIHGACLGGGLELALACHSRICSLDDKTVLGLPEVQLGLLPGSGGTQRLPRLVGVSKALDMILTGKQIRPRQALKMGLVDDVVPRDILLDVAIQRAKAGWLNRRALPWQERLLSGPLGKALLFRIVRKKTLAKTRGHYPAAERIIDVVRKGLDQGGPSGYEAEARAFGELAMSPQSAALRSLFFATTSLKKETGSAATARAIHRVGV... | 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 metaboli... |
P38135 | MHPTGPHLGPDVLFRESNMKVTLTFNEQRRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADL... | 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... |
B4YQU1 | MASATPAMSENAVLRHKAASTTGIDYESSAAVSPAESPRTSASSTSLSSLSSLDANEKKDEYAGLLDTYGNAFTPPDFSIKDIRAAIPKHCYERSTIKSYAYVLRDLLCLSTTFYLFHNFVTPENIPSNPLRFVLWSIYTVLQGLFATGLWVIGHECGHCAFSPSPFISDLTGWVIHSALLVPYFSWKFSHSAHHKGIGNMERDMVFLPRTREQQATRLGRAVEELGDLCEETPIYTALHLVGKQLIGWPSYLMTNATGHNFHERQREGRGKGKKNGFGGGVNHFDPRSPIFEARQAKYIVLSDIGLGLAIAALVYLGNR... | 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... |
Q05AM4 | MGLTLGERVQHCLLVLVSGLFLALFRLLSPGTKRPKHLPPITNPLLTLSAVQLAEKIRRGEVSSVEVVQAYIDRIQEVNPLLNALIKDRFSAALLEAARADKLIKEENGGEEVLRNQFPLLGVPMSVKESFGLQGMPNSGGLKSRGKVLASVDAPPVALLKRAGAIPLGVTNTSELCMWMESNNHLYGITSNPYNLERICGGSSGGEGSIIGGGASVFGIGSDIGGSIRMPCFFNGIFGHKPSRGVVSNDNQFPRCSGLQNEYTGSGPMCRYAEDLLPLLKIMAGPTADKLTLSKAVDLKKLRFFTIVDDGGSPLTSPVD... | 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)... |
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 | MSRIVFICLAAILTDALTWAQVNVEPNTALLNEGDRTELLCRYGRSINYCRIEIPGEQKVLNLSPEWSKTPGFTYFGAGLTAGQCGVSIERVKASNNGQVKCSLGVEGEELSGTIDLVVALRPQQPIIELLSRPNREGYFNEGTEFRARCSVRDGRPPANISWYIDNMPANKRTTPLEVMSSTNDNVELSTSVQEIQWHLSPEDSNRKLVCRSHHQTDRESVPPQEAAYIINVRYAPVHQPDAAVYGLYLEHTAIVNITIRASPQPKIEWTIDGAIVGQGRTDGRYSAYEPQYLGNDEYNVTLAIAGLTLEDTTKIYNLR... | 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 | MNKYPPLLTMLIIGIGSNAVAGDYFDPSLLATDIGNNDKLDLSLFSHPGGGVKGEREVSVYINDFFYKNVTLDFENGISGALEPIFPSGFFDNILASPYRSIKEKELISTADFLSLVPYGMVRFDQAIARVDISIPQAYLGRDAQMKSAPESWNQGVPALLIDYRLSGSKNKYNYGSSQNFYANAFLGFNLMGWRLRTTTNYMSYNSKDLYNKGERQGSFNFYNTYLEKDIGYLRSTLRLGELSTRGMILESFNFKGGKIYSNDEMLNDRLRSYTPTVRGIASSQAVVTIKQGGVVILQKNVPPGPFEINDFSLSGYSGD... | 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 | MSFGLHPWDVAFRPSPPHNLEKKVVPPGADREKSLPSPKEDSDGAREPDSTVDLRKKNKKKKNYQRYAKPPYSYLAMISLVIQNSPEKRLKLSQILQDISSLFPFFKGNYQGWKDSIRHNLSSNDCFRKVLKDPLKPQAKGNYWTVDVTRIPPDALKLQNTAVTRQDLFPLDLAPYILHGQPYRSLERLSANHTRGRTTPRMEPEVQIPVSDPAVSFPMILWNLPTSYSKCVAPNVVAPPSIHPLLLYSNFPSISIYNYLPPPYGSPVYSDRRDLLASGLHPQIPLTPKPPELKNAPSDFPPNKTVFDIPVYTGHPGFLA... | 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 ... |
Q14296 | MRRPRGEPGPRAPRPTEGATCAGPGESWSPSPNSMLRVLLSAQTSPARLSGLLLIPPVQPCCLGPSKWGDRPVGGGPSAGPVQGLQRLLEQAKSPGELLRWLGQNPSKVRAHHYSVALRRLGQLLGSRPRPPPVEQVTLQDLSQLIIRNCPSFDIHTIHVCLHLAVLLGFPSDGPLVCALEQERRLRLPPKPPPPLQPLLRGGQGLEAALSCPRFLRYPRQHLISSLAEARPEELTPHVMVLLAQHLARHRLREPQLLEAIAHFLVVQETQLSSKVVQKLVLPFGRLNYLPLEQQFMPCLERILAREAGVAPLATVNILM... | 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... |
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 ... |
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 ... |
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; ... |
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-phosphogly... |
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 + e... |
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 + e... |
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 + e... |
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 + e... |
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 + e... |
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 + e... |
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 + e... |
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 + e... |
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 + e... |
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 + e... |
O55058 | MLPFASCLPGSLLLWALLLLLLGAASPQDSEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDEQESCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKVGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECSYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYV... | 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 i... |
O95967 | MLPCASCLPGSLLLWALLLLLLGSASPQDSEEPDSYTECTDGYEWDPDSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDDQDSCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCHQGYELHRDGFSCSDIDECSYSSYLCQYRCINEPGRFSCHCPQGYQLLATRLCQDIDECESGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYI... | 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 i... |
Q9WVJ9 | MLPFASCLPGSLLLWAFLLLLLGAASPQDPEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVISDLHGEGPPPPAAHAQQPNPCPQGYEPDEQESCVDVDECTQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECGYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYV... | 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 i... |
Q9UBX5 | MPGIKRILTVTILALCLPSPGNAQAQCTNGFDLDRQSGQCLDIDECRTIPEACRGDMMCVNQNGGYLCIPRTNPVYRGPYSNPYSTPYSGPYPAAAPPLSAPNYPTISRPLICRFGYQMDESNQCVDVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCLDIDECRYGYCQQLCANVPGSYSCTCNPGFTLNEDGRSCQDVNECATENPCVQTCVNTYGSFICRCDPGYELEEDGVHCSDMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRSCQDINECEHRNHTCNLQQTCYNLQGGFKCIDPIRC... | 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... |
Q53RD9 | MVPSSPRALFLLLLILACPEPRASQNCLSKQQLLSAIRQLQQLLKGQETRFAEGIRHMKSRLAALQNSVGRVGPDALPVSCPALNTPADGRKFGSKYLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCRGISECSSQPCQNGGTCVEGVNQYRCICPPGRTGNRCQHQAQTAAPEGSVAGDSAFSRAPRCAQVERAQHCSCEAGFHLSGAAGDSVCQDVNECELYGQEGRPRLCMHACVNTPGSYRCTCPGGYRTLADGKSCEDVDECVGLQPVCPQGTTCINTGGSFQCVSPECPEGSGNVSYVKTSPFQCER... | 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 | MGPGSQRALFLLLLLLASPGARAFQSCLNKQQLLTTIRQLQQLLKGQETRFTEGIRNMKSRLAALQNTVNKMTPDAPPVSCPALEAPPDGKKFGSKYLVDHEVYFTCNPGFQLVGPSSVVCLANGSWTGEQPRCRDISECSSQPCHNGGTCVEGINHYRCICPPGKTGNRCQHQTQAAAPDGGEAGDPAFSRAPRCAQVEREQHCSCEAGFHLSSTTGGHSVCQDVNECEIYGQKGRPRLCMHACVNTPGSYRCTCPSGYRILADGKSCEDVDECAGPQHMCPRGTTCINTGGGFQCVNPECPEGSGNISYVKTSPFQCE... | 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 | MLPRLLLLICAPLCEPAELFLIASPSHPTEGSPVTLTCKMPFLQSSDAQFQFCFFRDTRALGPGWSSSPKLQIAAMWKEDTGSYWCEAQTMASKVLRSRRSQINVHRVPVADVSLETQPPGGQVMEGDRLVLICSVAMGTGDITFLWYKGAVGLNLQSKTQRSLTAEYEIPSVRESDAEQYYCVAENGYGPSPSGLVSITVRIPVSRPILMLRAPRAQAAVEDVLELHCEALRGSPPILYWFYHEDITLGSRSAPSGGGASFNLSLTEEHSGNYSCEANNGLGAQRSEAVTLNFTVPTGARSNHLTSGVIEGLLSTLGPA... | 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 | MLPWLLLLICALPCEPAGISDVSLKTRPPGGWVMEGDKLVLICSVDRVTGNITYFWYRGALGFQLETKTQPSLTAEFEISDMKQSDADQYYCAANDGHDPIASELVSIHVRVPVSRPVLTFGDSGTQAVLGDLVELHCKALRGSPPIFYQFYHESIILGNSSAPSGGGASFNFSLTAEHSGNFSCEASNGQGAQRSEVVALNLTGLSLVPTENGISHLSLGLTGWLLGCLSPITMALIFCYWLKRKIGRQSEDPVRSPPQTVLQGSTYPKSPDSRQPEPLYENVNVVSGNEVYSLVYHTPQVLEPAAAQHVRTHGVSESF... | 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 membra... |
Q96LA5 | MLLWSLLVIFDAVTEQADSLTLVAPSSVFEGDSIVLKCQGEQNWKIQKMAYHKDNKELSVFKKFSDFLIQSAVLSDSGNYFCSTKGQLFLWDKTSNIVKIKVQELFQRPVLTASSFQPIEGGPVSLKCETRLSPQRLDVQLQFCFFRENQVLGSGWSSSPELQISAVWSEDTGSYWCKAETVTHRIRKQSLQSQIHVQRIPISNVSLEIRAPGGQVTEGQKLILLCSVAGGTGNVTFSWYREATGTSMGKKTQRSLSAELEIPAVKESDAGKYYCRADNGHVPIQSKVVNIPVRIPVSRPVLTLRSPGAQAAVGDLLELH... | 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 th... |
Q96P31 | MLLWLLLLILTPGREQSGVAPKAVLLLNPPWSTAFKGEKVALICSSISHSLAQGDTYWYHDEKLLKIKHDKIQITEPGNYQCKTRGSSLSDAVHVEFSPDWLILQALHPVFEGDNVILRCQGKDNKNTHQKVYYKDGKQLPNSYNLEKITVNSVSRDNSKYHCTAYRKFYILDIEVTSKPLNIQVQELFLHPVLRASSSTPIEGSPMTLTCETQLSPQRPDVQLQFSLFRDSQTLGLGWSRSPRLQIPAMWTEDSGSYWCEVETVTHSIKKRSLRSQIRVQRVPVSNVNLEIRPTGGQLIEGENMVLICSVAQGSGTVTF... | 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, po... |
Q96PJ5 | MLLWASLLAFAPVCGQSAAAHKPVISVHPPWTTFFKGERVTLTCNGFQFYATEKTTWYHRHYWGEKLTLTPGNTLEVRESGLYRCQARGSPRSNPVRLLFSSDSLILQAPYSVFEGDTLVLRCHRRRKEKLTAVKYTWNGNILSISNKSWDLLIPQASSNNNGNYRCIGYGDENDVFRSNFKIIKIQELFPHPELKATDSQPTEGNSVNLSCETQLPPERSDTPLHFNFFRDGEVILSDWSTYPELQLPTVWRENSGSYWCGAETVRGNIHKHSPSLQIHVQRIPVSGVLLETQPSGGQAVEGEMLVLVCSVAEGTGDTT... | 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 mem... |
Q96RD9 | MLLWVILLVLAPVSGQFARTPRPIIFLQPPWTTVFQGERVTLTCKGFRFYSPQKTKWYHRYLGKEILRETPDNILEVQESGEYRCQAQGSPLSSPVHLDFSSASLILQAPLSVFEGDSVVLRCRAKAEVTLNNTIYKNDNVLAFLNKRTDFHIPHACLKDNGAYRCTGYKESCCPVSSNTVKIQVQEPFTRPVLRASSFQPISGNPVTLTCETQLSLERSDVPLRFRFFRDDQTLGLGWSLSPNFQITAMWSKDSGFYWCKAATMPYSVISDSPRSWIQVQIPASHPVLTLSPEKALNFEGTKVTLHCETQEDSLRTLYR... | 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... |
Q68SN8 | MSGSFSPCVVFTQMWLTLLVVTPVNGQHEAAQQSVVSLQPPWTTFFRGEVVTLTCYRFGFSVPQKTKWYQKRKTVKQTPGALVIKAHTLKVHESGEYWCQADSLLPSMHVNVEFSEDFLVLQAPPAVFEGDSVVLRCYAKKGIEAETLTFYKDGKALTLHPQSSEFYIHRANLKDNGQYKCTSKKKWSFGSLYTSNTVVVQVQELFPRPVLRARPSHPIDGSPVTLTCQTQLSAQKSDARLQFCFFRNLQLLGSGCSRSSEFHIPAIWTEESKRYQCKAETVNSQVSKQSTAFIIPVQRASARFQTHIIPASKLVFEGQL... | 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 | MLLWTAVLLFVPCVGKTVWLYLQAWPNPVFEGDALTLRCQGWKNTPLSQVKFYRDGKFLHFSKENQTLSMGAATVQSRGQYSCSGQVMYIPQTFTQTSETAMVQVQELFPPPVLSAIPSPEPREGSLVTLRCQTKLHPLRSALRLLFSFHKDGHTLQDRGPHPELCIPGAKEGDSGLYWCEVAPEGGQVQKQSPQLEVRVQAPVSRPVLTLHHGPADPAVGDMVQLLCEAQRGSPPILYSFYLDEKIVGNHSAPCGGTTSLLFPVKSEQDAGNYSCEAENSVSRERSEPKKLSLKGSQVLFTPASNWLVPWLPASLLGLM... | 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 phos... |
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 Leng... |
A0A2P1BT06 | MGERRFSNQQIDRLLRPKSVAVIGASDRKGALGATLLNNLVQYEFSGDIYPVNPKRDELLGLKVYHEVAELPEGIDCAVLAIPRPFVIDTVRQLAQRGCGAVVIYSAGFSEAGEEGMKDQLELAAIAAEYGMVIEGPNCLGCTNYVERVPLTFVETNMQTPPKGTRAVGIASQSGALAAVLATALHPRGLYVSSSVSTGNEAASGVEDYVEWLVDDEDTHVIAMYVESLRRPKAFIAAARRAHAAGKPIVMLHPGKSNKAQESAATHTGAMAGDYALMKTKLAREGVIFADTLEELADITEIALRCRALPGANMAVLGES... | 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 | MSSLSTKTDLLGDPDFIRLQSVEVDGSEVIPGETRPRRNTKFPKLTNSPDGKTFTLYDVYRINKDSDSNFLGIRELLADGKRGDYKWISYKQACIRANNIGSALVQLGLNKGDRIGIFSINRPEWVLSDMAAMNHSLVPVALYATLGANAIEYVVNHSEISVLLCEGKNVEKILSMPGTTIKTIVSYDPLPQATLDKFKDNENVKLYLLSDFEKLGEQNPAQHEVPSPEDLCTLLYTSGSTGNPKGVMLTHTNMVSEVAGANFSPAGVIPEDVHMSYLPLAHSFERAVVSLMCYVGGQIGFFSGLIPELFNDIQVLRPTF... | 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-c... |
Q1ZXQ4 | MINNWLAVGLLVVSGILAFNWKRKHPYGQTVEIGEKPENGGRIRRNSACADHLISFLEDDEIYTLYDSLVKSCKKYGERKCFGERKKDSNGNLGKFEWISYNTYLERCEYIQQGLCELGLKPKSKVGIFSKNRLEWLIVHSASFIQSYCVVSFYETLGVESLSYVTEHAEIGLAFCSAETLQKTLDIAKGVKVLKTIICFDSIDKEHYNIAKELGVTLYTYDEIMKKGKEANGKHKHTPPTPDTLSTIMYTSGTTGPPKGVMITHKNLTSVVCAVSDFIKVYDTDVHYSYLPYAHVLERVVILAAFHFGAAIGIFSGDIS... | 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... |
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 | MLTATPLPHQLLATFLLVLASATQPAVPASTDRAALLAFRASLSPPSRAALSSWSGPLSPSWLGVSLHPATAPAPSVTTPSVAELSLRGLNLTGVIPAAPLALLRRLRTLDLSANALSGELPCSLPRSLLALDLSRNALSGAVPTCLPSSLPALRTLNLSANFLRLPLSPRLSFPARLAALDLSRNAISGAVPPRIVADPDNSALLLLDLSHNRFSGEIPAGIAAVRSLQGLFLADNQLSGDIPPGIGNLTYLQVLDLSNNRLSGSVPAGLAGCFQLLYLQLGGNQLSGALRPELDALASLKVLDLSNNKISGEIPLPLA... | 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
Sequen... |
P80668 | MTEPHVAVLSQVQQFLDRQHGLYIDGRPGPAQSEKRLAIFDPATGQEIASTADANEADVDNAVMSAWRAFVSRRWAGRLPAERERILLRFADLVEQHSEELAQLETLEQGKSIAISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLSIPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTMLRVAELASEAGIPDGVFNVVTGSGAVCGAALTSHPHVAKISFTGSTATGKGIARTAADHLTRVTLELGGKNPAIVLKDADPQWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFD... | 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... |
P13036 | MTPLRVFRKTTPLVNTIRLSLLPLAGLSFSAFAAQVNIAPGSLDKALNQYAAHSGFTLSVDASLTRGKQSNGLHGDYDVESGLQQLLDGSGLQVKPLGNNSWTLEPAPAPKEDALTVVGDWLGDARENDVFEHAGARDVIRREDFAKTGATTMREVLNRIPGVSAPENNGTGSHDLAMNFGIRGLNPRLASRSTVLMDGIPVPFAPYGQPQLSLAPVSLGNMDAIDVVRGGGAVRYGPQSVGGVVNFVTRAIPQDFGIEAGVEGQLSPTSSQNNPKETHNLMVGGTADNGFGTALLYSGTRGSDWREHSATRIDDLMLKS... | 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 | MTAIKHPVLLWGLPVAALIIIFWLSLFCYSAIPVSGADATRALLPGHTPTLPEALVQNLRLPRSLVAVLIGASLALAGTLLQTLTHNPMASPSLLGINSGAALAMALTSALSPTPIAGYSLSFIAACGGGVSWLLVMTAGGGFRHTHDRNKLILAGIALSAFCMGLTRITLLLAEDHAYGIFYWLAGGVSHARWQDVWQLLPVVVTAVPVVLLLANQLNLLNLSDSTAHTLGVNLTRLRLVINMLVLLLVGACVSVAGPVAFIGLLVPHLARFWAGFDQRNVLPVSMLLGATLMLLADVLARALAFPGDLPAGAVLALIG... | 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 tr... |
Q6C116 | MGIKGLNKLLMEHCPAALRSSEIKNFGGRKVAIDASMSLYQFVIAVRQADGQQLTNENGETTSHLMGMFYRTLRMVDNGIKPVYVFDGKPPVLKSGELAKRKERREEALKKIEELKQQVEDGEEGEETKEAQEDVTRFEKRTVRVTPEQNDEAKKLLTLMGIPIVEAPCEAEAQCAKLAEAGKVYAAASEDMDTLCFGSPVLLRHLTFSEAKKMPISEINFAKILEGLEMTHAQFIDLCILLGCDYADTIRGVGPQTALKLMKEHGSLEKIVEHIEKNPSGKLKVPENWPYQEVRALLQAPDVLDSSSCDIKWNNPDVEG... | 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. Du... |
P25621 | MMKESKSITQHEVERESVSSKRAIKKRLLLFKIDLFVLSFVCLQYWINYVDRVGFTNAYISGMKEDLKMVGNDLTVSNTVFMIGYIVGMVPNNLMLLCVPPRIWLSFCTFAWGLLTLGMYKVTSFKHICAIRFFQALFESCTFSGTHFVLGSWYKEDELPIRSAIFTGSGLVGSMFSGFMQTSIFTHLNGRNGLAGWRWLFIIDFCITLPIAIYGFIFFPGLPDQTSAVSKFSMTRYIFNEQELHYARRRLPARDESTRLDWSTIPRVLKRWHWWMFSLVWVLGGENLGFASNSTFALWLQNQKYTLAQRNNYPSGIFAV... | 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 | MFHSLVLMACALAALSVAQGAGSARSKSLPLSLSLSVSVSSSLASASSPGAAADPTAAFTVTATAPTPASAPFAGKQLNRCRQSCYQQLSKDWHYCKDSVDCTNCCQKLVAPFELRILKAQRQESLVLTDIGWDEMIANASRQCLITWEVSGGGLIGNLLTDTARAELSLWPDTVYNIQVKCKHKLTGLMRRSIKLNVDTSQLVGTTTTTTTSKSSIQRQHLEQPVDHTDALEHSQHIRIPRPTDRVYIISALPTPSELGGVVYPAFGALAFFLALLVMFLFLRPQRKRFPLDADSADTATLIGRSSSSSRNSMDASTLH... | 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 | MNNLAFLFPGQGSQFVGMGKSFWNDFVLAKRLFEEASDAISMDVKKLCFDGDMTELTRTMNAQPAILTVSVIAYQVYMQEIGIKPHFLAGHSLGEYSALVCAGVLSFQEAVKLIRQRGILMQNADPEQLGTMAAITQVYIQPLQDLCTEISTEDFPVGVACMNSDQQHVISGHRQAVEFVIKKAERMGANHTYLNVSAPFHSSMMRSASEQFQTALNQYSFRDAEWPIISNVTAIPYNNGHSVREHLQTHMTMPVRWAESMHYLLLHGVTEVIEMGPKNVLVGLLKKITNHIAAYPLGQTSDLHLLSDSAERNENIVNLR... | 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 | MQEKEMFDLTIIGGGPAGLYSTFYAGMRDLKVKLVEYNKELGGKILFYPEKIIWDVGGMPPTTGRTLINQLVEQATTFNPTICLNEHIVRMVREPDNTYTLFNEQGKAHYTRAVMLASGHGIPVMQKLEIEGADRYEVSNLHYTVTQMDIFANKRVLISGGGNAAVDWANELANISKEVVVCHRRDEFGGHEKNVEQMKSVTKIHTPYQIKELHGVGSAIEAVTLAHCDTGEQRQIEVDAVIVNHGMKLDGCFLIEAGLALEEDGFLRVSACMETSQPGIFAAGDVTRHEGKLQLISGAFVEGATAVNGVKQFLDPKADK... | 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 | MTEQLELFDVTIIGGGPAGMYTAFYSGMRDLKTKVLEYNESLGGKILLYPEKVIWDVGGLPPTRGEQLIQQLEKQAKTFEPEIALNQKITSFERDEHQNILLTAENGDRHLTKTLILAMGHGIPVQRKLEIEHADRYEVTNLYYTVQELKTFAGKRVVISGGGDSAVDWANALVPIAESVTVVHRRDMFGGHEKNVANMKASCARILTPHELTDLHGQGDKIDAVTIQHLETGEIERIETDAVIVNHGMKGDLSVLSEWGLKQGEWGLIEVNEKMETNLPGVYAVGDLCTHKSKVRLIAGTFVDGVNALNSAKLYIEPEA... | 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 | MAENQEVYDVTIIGGGPIGLFTAFYCGMRELKTKVIEFLPKLGGKVSLFFPEKIIRDIGGIPGIAGKQLIEQLKEQAATFDPDIVLNQRVTGFERLDDGTIVLTGSEGKKHYTRTVILACGMGTLEVNEFDSEDAARYAGKNLHYGVEKLDAFKGKRVVISGGGDTAVDWANELEPIAASVTVVHRREEFGGMESSVTKMKQSSVRVLTPYRLEQLNGDEEGIKSVTVCHTESGQRKDIEIDELIINHGFKIDLGPMMEWGLEIEEGRVKADRHMRTNLPGVFVAGDAAFYESKLRLIAGGFTEGPTAVNSAKAYLDPKA... | 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 | MEEEKLTSEKEIYDITVIGGGPVGLFTAFYAGLRGISVKVIESLSELGGQPAILYPEKVIYDIPAFPAITGADLVDNLIEQLERFKDKTTICLKEEVKTFEKENAIFTITTNKGNHFSKAIIIACGNGAFAPRRLGLDDEERYADHNLFYNVHKLDQFAGKKVVICGGGDSAVDWANALDKIAESVTLVHRRDAFRAHEHSVEVLKTSHVNIMTPYVPLELKGEGDEATSLVIQKVKSEETKELSLDSLIVSFGFSTSNKNLKSWNIDYKRSSINVSPLFETSQTGVFAIGDAAEYEGKIDLIATGFGEAPTAVNQAIKY... | 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 | MIYVSRRLLITCLLLVSACVVAGIWGLRSGAVTLETSQVFAALMGDAPRSMTMVVTEWRLPRVLMALLIGAALGVSGAIFQSLMRNPLGSPDVMGFNTGAWSGVLVAMVLFGQDLTAIALSAMVGGIVTSLLVWLLAWRNGIDTFRLIIIGIGVRAMLVAFNTWLLLKASLETALTAGLWNAGSLNGLTWAKTSPSAPIIILMLIAAALLVRRMRLLEMGDDTACALGVSVERSRLLMMLVAVVLTAAATALAGPISFIALVAPHIARRISGTARWGLTQAALCGALLLLAADLCAQQLFMPYQLPVGVVTVSLGGIYLI... | 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 ... |
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 | MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCMVFQTQPVSSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTF... | 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 | LVLLLSLAQLWSCHLVTAVPLLGYREHNCDDPEAEQVALLAVDHINNHLQQGYKHILNRIDKVKVWPRRPTGEVYELEIDTLETTCHALDPTPLANCSVRQVTQHAVEGDCDFHVLKQDGQFTVLSAKCDSTPDSAEDILKLCPDCPLLTPLNDTRVAQAAEAALTAFNEKNNGAYLQLVEIARAQLVPLPASTYVEFTVAATDCVAKEVTDPAKCNLLADKQYGFCKATVAEKVAREEVEVTCTIFPAQPVVPQPQPGVAGAAAVEPAPAVDPASPVSPPDGQSPSSLVVGPVLVAQAPAPPRAHYDLRQTFAGVPSME... | 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 | MKSLVLLLCFAQLWSCQSAPQGAGLGFRELACDDPETEHVALIAVDYLNKHLLQGFRQILNQIDKVKVWSRRPFGEVYELEIDTLETTCHALDPTPLANCSVRQQAEHAVEGDCDFHILKQDGQFRVLHAQCHSTPDSAEDVRKFCPRCPILIRFNDTNVVHTVKTALAAFNAQNNGTYFKLVEISRAQNVPFPVSTLVEFVIAATDCTGQEVTDPAKCNLLAEKQYGFCKATLIHRLGGEEVSVACKLFQTQPQPANANPAGPAPTVGQAAPVAPPAGPPESVVVGPVAVPLGLPDHRTHHDLRHAFSPVASVESASGE... | 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 ... |
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 ... |
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 co... |
P96809 | MTGISRRTFGLAAGFGAIGAGGLGGGCSTRSGPTPTPEPASRGVGVVLSHEQFRTDRLVAHAQAAEQAGFRYVWASDHLQPWQDNEGHSMFPWLTLALVGNSTSSILFGTGVTCPIYRYHPATVAQAFASLAILNPGRVFLGLGTGERLNEQAATDTFGNYRERHDRLIEAIVLIRQLWSGERISFTGHYFRTDELKLYDTPAMPPPIFVAASGPQSATLAGRYGDGWIAQARDINDAKLLAAFAAGAQAAGRDPTTLGKRAELFAVVGDDKAAARAADLWRFTAGAVDQPNPVEIQRAAESNPIEKVLANWAVGTDPGV... | 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) activit... |
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... |
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 membr... |
Q59MV9 | MTVEYETKQLTPAQIKIILDTVPILEEAGETLTQKFYQRMIGNYDEVKPFFNTTDQKLLRQPKILAFALLNYAKNIEDLTPLTDFVKQIVVKHIGLQVLPEHYPIVGTCLIQTMVELLPPEIANKDFLEAWTIAYGNLAKLLIDLEAAEYAKQPWRWFKDFKVTRIVQECKDVKSVYFTPVDKDLLPLPKPERGQYLCFRWKLPGEEFEISREYSVSEFPKENEYRISVRHVPGGKISGYIHNNLKVGDILKVAPPAGNFVYDPATDKELIFVAGGIGITPLLSMIERALEEGKNVKLLYSNRSAETRAFGNLFKEYKSK... | 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... |
Q03331 | MSAAKQLFKIVPLTPTEINFLQSLAPVVKEHGVTVTSTMYKYMFQTYPEVRSYFNMTNQKTGRQPKVLAFSLYQYILHLNDLTPISGFVNQIVLKHCGLGIKPDQYPVVGESLVQAFKMVLGEAADEHFVEVFKKAYGNLAQTLIDAEASVYKTLAWEEFKDFRVTKLVKEAEDVTSVYLTPVDGFKLKPIIPGEYISFRWDIHNPDITDIQPREYSISQDVKENEYRISVRDIGIVSDYINKKLQVGDIVPVHAPVGTMKYDSISKKGKVAVLAGGIGITPMIPIIEHALKDGKDVELYYSNRSYQSEPFREFFSNLEK... | 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... |
Q9URY5 | MSSVEVNRENADVANTNRQANLAEGYEIKELNESQKQYIRSSIPILESSGVNLTKAFYQKMLGNYPEVLPYFNKAHQISLSQPRILAFALLNYAKNIDDLTSLSAFMDQIVVKHVGLQIKAEHYPIVGHCLLSTMQELLPSDVATPAFLEAWTTAYGNLAKILIDSEKKVYQSQPWNGFVEFKVTELINESSDVKSVYLGPKDPAFRISHAHPGQYVSVLWEIPGLSHKTLREYSLSNRVDTCRNQFRISVRRVAGGVVSNFVHDNLKVGDIVGVSPPAGNFVYKRSEENVNRPLLCFAGGIGITPLIPIIETALLDGRK... | 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... |
P39676 | MLAEKTRSIIKATVPVLEQQGTVITRTFYKNMLTEHTELLNIFNRTNQKVGAQPNALATTVLAAAKNIDDLSVLMDHVKQIGHKHRALQIKPEHYPIVGEYLLKAIKEVLGDAATPEIINAWGEAYQAIADIFITVEKKMYEEALWPGWKPFDITAKEYVASDIVEFTVKPKFGSGIELESLPITPGQYITVNTHPIRQENQYDALRHYSLCSASTKNGLRFAVKMEAARENFPAGLVSEYLHKDAKVGDEIKLSAPAGDFAINKELIHQNEVPLVLLSSGVGVTPLLAMLEEQVKCNPNRPIYWIQSSYDEKTQAFKKH... | 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... |
A7LXW1 | MRNTRYGFLVLLSSLLMLTGCSRRDILDDYPVSGVDIKLDWDGVTDQLPEGVRVIFYPKNGDGRKVDKYLSVRGGEMKVPPGRYSVVVYNYNTESIRIRGEESYETIEAYTGNCNGLGIEGTEKMVWSPDSLYVLNIDELKIEKSEEVLRLDWKLESVVKKYSFAVEAKGLEYVATVVGSIDGLSDCYCIGKGRGVCSSQPIYFEVKKGDNKVTAFFTAFKQVKEMTMPTRMSTSERETSSEKGAIILILKFIKTDNTVQEATIDVTEIIGTLENAGTGEDGKPTPPPEIELPPDDKIEVDKPETPPNPDGGGGMGGNVD... | 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).
... |
P33410 | MKQIPLILAMSLAFAAAAKGESAPDMQAAVNFDSAMLWGGANGADLSRFNYSNALRPGNYIVDIYANNYPLIRQQVRFVAAQTSGQGLKTAPAVACFTYGQLEAMQVRLRALDPALVADLKSSGRCEVLGKLFPDSRESFDFGENRLEVSIPQAYTINRFRRDISPDEWDSGITAFRLGYQYNYADYIGGLRAGRRLDLNLYSGFNFKGWYLRNSSTLGWGQGRFTRRSQRTSLQTDIPSWRARLVFGDVFSSGEYFAPYSMRGMLVGSDTAMLPYSERLYRPTIRGVARTRANVKVYQAGVLVFQDAVPPGPFAIDDYS... | 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 f... |
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 necessa... |
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 function... |
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 function... |
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 necessa... |
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 assem... |
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 necessa... |
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 necessa... |
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 necessa... |
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 T... |
Q59207 | MHVTRDFSHYVRTAGEGIKHIDLAVEGVHCAGCMAKIERGLSAIPDVTLARVNLTDRRVALEWKAGTLDPGRFIDRLEELGYKAYPFETESAEVAEVAESRFLLRCLGVAAFATMNVMMLSIPVWSGNVSDMLPEQRDFFHWLSALIALPAAAYAGQPFFRSAWRALSAKTTNMDVPISIGVILALGMSVVETIHHAEHAYFDAAIMLLTFLLVGRFLDQNMRRRTRAVAGNLAALKAETAAKFVGPDEISQVPVAAISPGDIVLLRPGERCAVDGTVIEGRSEIDQSLITGETLYVTAEQGTPVYAGSMNISGTLRVRV... | 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: ... |
P18398 | MSCCASSAAIMVAEGGQASPASEELWLASRDLGGGLRQTELSVPNAYCGTCIATIEGALRAKPEVERARVNLSSRRVSIVWKEEVGGRRTNPCDFLHAIAERGYQTHLFSPGEEEGDDLLKQLILAVAVSGFAATNIMLLSVSVWSGADAATRDLFHWISALIAGPALIYAGRFFYKSAWNAIRHGRTNMDVPIALAVSLSYGMSLHETIGHGEHAWFDASVTLLFFLLIGRTLDHMMRGRARTAISGLARLSPRGATVVHPDGSREYRAVDEINPGDRLIVAAGERVPVDGRVLSGTSDLDRSVVNGESSPTVVTTGDT... | 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: ... |
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: Cytopla... |
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: Cytopla... |
P26489 | MTDTPTQALPPKAPQAGPTVPGTVRRAVPGSAAAALVIAASHFAALSAFDPRILLVLLVIVVLASSGGLFAGLAATAVSALGLALRGLLSGDTVVADWQSLGLLTIAGAGIAVLGERLRRTRLDAVARDRALLAREAHLSSILDTVPDAMIVIDERGIMQSFSITAERLFGYSPSEVIGRNVSMLMPNPHRDQHDLYLSRYLTTGERRIIGIGRVVTGERKDGATFPMELAVGEMHSVSGRFFTGFIRDLTERQNTEARLQELQAELVHISRLTALGEMASTLAHELNQPLSAIANYIKGSRRLLDDGDPKRIPMLQGAL... | 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 T... |
P23222 | MAPTRVTHPPDDGRGEHFRVRIEGFGVGTWDLDLKTWALDWSDTARTLLGIGQDQPASYDLFLSRLEPDDRERVESAIKRVSERGGGFDVSFRVAGTSNAGQWIRARAGLIRDEAGTARHLSGIFLDIDEEKQVEGALRTRETHLRSILHTIPDAMIVIDGHGIIQLFSTAAERLFGWSELEAIGQNVNILMPEPDRSRHDSYISRYRTTSDPHIIGIGRIVTGKRRDGTTFPMHLSIGEMQSGGEPYFTGFVRDLTEHQQTQARLQELQSELVHVSRLSAMGEMASALAHELNQPLAAISNYMKGSRRLLAGSSDPNTP... | 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 M... |
P10955 | MLSKSGIERTQWGRRVVRWRGDGVAAYIVAAIVTSSVLAIRMIRAEPIGEGLLLFSFIPAILVVALIGGRNPILFAAGLSLVAAVSHQQISSADGPSVVELLVFGSAVLLIVALGEVLEAARRAIDRTEDVVRARDAHLRSILDTVPDATVVSATDGTIVSFNAAAVRQFGYAEEEVIGQNLRILMPEPYRHEHDGYLQRYMATGEKRIIGIDRVVSGQRKDGSTFPMKLAVGEMRSGGERFFTGFIRDLTEREESAARLEQIQAELARLARLNEMGEMASTLAHELNQPLSAIANYSHGCTRLLRDMDDAVATRIREAL... | 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 T... |
P98055 | MNYTLETADRALGAFPALLGAAFAHDSLFAAHMWVLFFTLVVSTLLLLRRVSFLPPVAGPPCRRTEYFDEVVKYGVMATVFWGVVGFLVGVVVALQLAFPDLNIAPYFNFGRMRPLHTSAVIFAFGGNALIATSFYVVQRTCRARLFGGNLGWFVFWGYNLFIIMAATGYLLGITQGREYAEPEWYVDLWLTIVWVAYLATFLGTILTRKEPHISVANWFYLSFIVTIAMLHIVNNLAVPVSFLGVKSYSAFSGVQAALTQWWYGHNAVGFFLTAGFLGMMYYFIPKQVNRPVYSYRLSIIHFWALIFMYIWAGPHHLHY... | 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 cyto... |
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