ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q93ZA0 | MTTLTKIQVYPQVLEHRLFFRDPIRVGSRLTCRERSNRVYVHRCEKKVERKRKVEKFKGNGSWDSLKSGFLGFSKLGFLSKDEYNQKVENLEMVFSSVAVQIARYIVTMTSTGAILLIGFQLSGGDSSMNSLVWYSWLGGIIIGTMTGANMVLEDHYRAGPRNVVITGSTRGLGKALAREFLLSGDRVIVTSRSSESVDMTVKELEQNLKEIMSNASESARKKLSDAKVVGIACDVCKPEDVEKLSNFAVKELGSINIWINNAGTNKGFRPLLEFTEEDITQIVSTNLIGSILCTRGAMDVMSRQHSGGHIFNMDGAGSG... | Function: Involved in chlorophyll b degradation. Belongs to the chlorophyll catabolic enzymes (CCEs).
Catalytic Activity: 7(1)-hydroxychlorophyllide a + NAD(+) = chlorophyllide b + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54845
Sequence Length: 496
Subcellular Location: Plastid
EC:... |
Q5N800 | MAAAAVVHLSVHGRLRRSPELHARPYHRPSLLRCRAFKQEADNGGEEASSSPPPPTTAEARRRRKGPLYKLKAAIQGLAGSRSAAAEAYGGEYQRAVEKAEEIFFSVATQVGRYVITMMSSGVVLGVGFQLSGGDSQMNTLIWYSWLGGVIIGTMIGANSVLEEHCKAGPRNVVITGSTRGLGKALAREFLLSGDRVVIASRSPESVLQTINELEENIQEGLSVAKKKQREILLHAKVVGTSCDVCKPEDVKKLVNFAKDELGSIDIWINNAGTNKGFRPLVNFSDEDISQIVSTNLVGSLLCTREAMNVMQHQQKGGHV... | Function: Required for proper chloroplast degradation. Involved in chlorophyll b degradation.
Catalytic Activity: 7(1)-hydroxychlorophyllide a + NAD(+) = chlorophyllide b + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54716
Sequence Length: 504
Subcellular Location: Plastid
EC: 1.1.1.2... |
P13398 | MSKVDLWQDATAQAELVRSGEISRTELLEATIAHVQAVNPEINAVIIPLFEKARRESELASGPFAGVPYLLKDLTVVSQGDINTSSIKGMKESGYRADHDAYFVQRMRAAGFVLLGKTNTPEMGNQVTTEPEAWGATRNPWNLGRSVGGSSGGSGAAVAAALSPVAHGNDAAGSVRIPASVCGVVGLKPTRGRISPGPLVTDSDNVAGAAHEGLFARSVRDIAALLDVVSGHRPGDTFCAPTASRPYAQGISENPGSLRVGVLTHNPVGDFALDPECAAAARGAAAALAALGHDVNDAYPEALGDRSFLKDYSTICDVAI... | Function: Specifically catalyzes the hydrolysis of 6-aminohexanoic acid cyclic dimer (1,8-diazacyclotetradecane-2,9-dione) to form the linear dimer 6-aminohexanoyl-6-aminohexanoic acid. Is inactive on 6-aminohexanoic acid oligomers (degree of polymerization 2 to 6), various other cyclic amides, cyclic diamides, linear ... |
P07061 | MNARSTGQHPARYPGAAAGEPTLDSWQEAPHNRWAFARLGELLPTAAVSRRDPATPAEPVVRLDALATRLPDLEQRLEETCTDAFLVLRGSEVLAEYYRAGFAPDDRHLLMSVSKSLCGTVVGALIDEGRIDPAQPVTEYVPELAGSVYDGPSVLQVLDMQISIDYNEDYVDPASEVQTHDRSAGWRTRRDGDPADTYEFLTTLRGDGGTGEFQYCSANTDVLAWIVERVTGLRYVEALSTYLWAKLDADRDATITVDQTGFGFANGGVSCTARDLARVGRMMLDGGVAPGGRVVSQGWVESVLAGGSREAMTDEGFTSA... | Function: Involved in nylon oligomer degradation.
Catalytic Activity: [N-(6-aminohexanoyl)](n) + H2O = 6-aminohexanoate + [N-(6-aminohexanoyl)](n-1)
Sequence Mass (Da): 42693
Sequence Length: 392
Pathway: Xenobiotic degradation; nylon-6 oligomer degradation.
EC: 3.5.1.46
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Q79F77 | MNTTPVHALTDIDGGIAVDPAPRLAGPPVFGGPGNDAFDLAPVRSTGREMLRFDFPGVSIGAAHYEEGPTGATVIHIPAGARTAVDARGGAVGLSGGYDFNHAICLAGGAGYGLEAGAGVSDALLERLEHRTGFAELQLVSSAVIYDFSARSTAVYPDKALGRAALEFAVPGEFPQGRAGAGMSASAGKVDWDRTEITGQGAAFRRLGDVRILAVVVPNPVGVIVDRAGTVVRGNYDAQTGVRRHPVFDYQEAFAEQVPPVTEAGNTTISAIVTNVRMSPVELNQFAKQVHSSMHRGIQPFHTDMDGDTLFAVTTDEIDL... | Function: Involved in the degradation of nylon-6 oligomers . Degrades cyclic and linear oligomers of 6-aminohexanoate (Ahx) with a degree of polymerization greater than three by an endo-type mode . Cannot use Ahx cyclic dimer or the Ahx linear dimer .
PTM: Expressed as an inactive precursor that is cleaved autocatalyti... |
P0DTZ4 | MKLTCVLIVSVLILTACQFTAAVDCHSTGYLCFWWHECCSNFCIPLQQRCF | Function: Probable neurotoxin.
Sequence Mass (Da): 5848
Sequence Length: 51
Domain: The cysteine framework is VI/VII (C-C-CC-C-C).
Subcellular Location: Secreted
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P0DTZ6 | MKLTCVLIVAVLILTACQVIAADSSCWFCSTGFNKCCESTGDCMTYPSEYNASCPEA | Function: Probable neurotoxin.
Sequence Mass (Da): 6094
Sequence Length: 57
Domain: The cysteine framework is VI/VII (C-C-CC-C-C).
Subcellular Location: Secreted
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P0DUA0 | MKLTFVLIVAVLVLAVCNFTVADKANNAEAPEQEKRACTPNGSYCNILSGKLNCCSGWCLALICAG | Function: Probable neurotoxin.
Sequence Mass (Da): 6965
Sequence Length: 66
Domain: The cysteine framework is VI/VII (C-C-CC-C-C).
Subcellular Location: Secreted
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P0DJB2 | DDCTTYCYGVHCCPPAFKCAASPSCKQT | Function: Probable neurotoxin with unknown target. Possibly targets ion channels.
Sequence Mass (Da): 3000
Sequence Length: 28
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P0C1C8 | TCKQKGEGCSLDVECCSSSCKPGGPLFDFDC | Function: Gamma-conotoxins may act on voltage-gated non-specific cation pacemaker channels (HCN) (By similarity). Elicits toxic effects in the freshwater snail Pomacea paludosa after intramuscular injection, but it has no effect when injected intracerebrally into mice.
Sequence Mass (Da): 3245
Sequence Length: 31
Domai... |
P0C1C9 | ACKPKNNLCAITEMAECCSGFCLIYRCS | Function: Gamma-conotoxins may act on voltage-gated non-specific cation pacemaker channels (HCN).
Sequence Mass (Da): 3073
Sequence Length: 28
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P56633 | MKLTCVVIVVVLFLTACQLITADDSRRTQKHRALRSTTKLSLSTRCRIPNQKCFQHLDDCCSRKCNRFNKCV | Function: Kappa-conotoxins bind and inhibit voltage-gated potassium channels (Kv). This toxin inhibits the drosophila Shaker channel (IC(50)=57-80 nM) . In vivo, when tested in fish, this toxin induces hyperactivity, followed by continuous contraction and extension of major fins, without immobilization or death . Injec... |
P0CY69 | ACQLITAEDSRGTQLHRALRSTSKVSKSTSCVEAGSYCRPNVKLCCGFCSPYSKICMNFPKN | Function: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav).
Sequence Mass (Da): 6778
Sequence Length: 62
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q8VGS3 | MDKENHSVVTEFVFMGITQDPQLQIIFFVVFLLVYLVNVIGNVGMIILIITDSQLHTPMYFFLCNLSFVDLGYSSAIAPRMLADFLTKHKVISFSSCATQFAFFVGFVDAECYVLAAMAYDRFVAICRPLHYSTLMSKKVCLVLMLGSYFAGLVSLVAHTSLTFSLSYCGSNIINHFFCEIPPLLALSCSDTYISEILLFSLCGFIEFSTILIIFISYAFILIAIIRIRSAEGRLKAFSTCGSHLTGVTLFYGTVMFMYLRPTSSYSLDQDKWASVFYTIIIPMLNPLIYSLRNKDVKAAFKKLIGKKPQ | Function: Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanethiol (MTMT). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 348... |
Q8NGC0 | MTEFHLQSQMPSIRLIFRRLSLGRIKPSQSPRCSTSFMVVPSFSIAEHWRRMKGANLSQGMEFELLGLTTDPQLQRLLFVVFLGMYTATLLGNLVMFLLIHVSATLHTPMYSLLKSLSFLDFCYSSTVVPQTLVNFLAKRKVISYFGCMTQMFFYAGFATSECYLIAAMAYDRYAAICNPLLYSTIMSPEVCASLIVGSYSAGFLNSLIHTGCIFSLKFCGAHVVTHFFCDGPPILSLSCVDTSLCEILLFIFAGFNLLSCTLTILISYFLILNTILKMSSAQGRFKAFSTCASHLTAICLFFGTTLFMYLRPRSSYSLT... | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40658
Sequence Length: 362
Subcellular Location: Cell membrane
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Q8VF76 | MEEKNQTIVMEFFFLGLTDHLYQKIALFITILFVYLVTLGGNLGMITLIWADPRLHTPMYFFLSHLSFVDMCSSSSIAPKMLCDIFAEEKRISFMGCAAQMWFFGFFVGTECFLLASMAYDRYTAICKPLLYTLLMSQRVCVHLVVGPYVFAIINITTHTTLAFCLPFCGSNTINHFFCDVSPLLSLACADSWVNKVVLFVLSGAIGVFSGLIIIVSYVSILMTIFKIQTADGKQKAFSTCSSHLSAVSILYGTLFFIYVRPSASFSLNINKMISLFYTVVIPMLNPLIYSLRNKEVKGAFRRKVQKKHFPAGR | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35374
Sequence Length: 314
Subcellular Location: Cell membrane
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Q8VEX5 | MEDGNTTLLTEFVLTGLTDHQGLQVPLFLLFLMIYLITVVGNLGLIALIWSDPHLHIPMYLFLGSLAFVDAWISSAVTPNMLFDLLSKNKMISLSECMIQFFAFAFGGTTECFLLGTMAYDRYVAICKPLLYPVIMTNRLCIRLLVSVFIGGFLHSLFHVLFLLRLTFCNSNIIHHFYCDIIPLYNISCTDPTLNLLLVFILSGSIQVFTIMTVLVSYTLVLFTILKMKSLQGIRKAFSTCGAHLLSVSLYYGPLLFMYVLPASQQTDGQGMMDSLFYTVIIPVLNPIIYSLRNKQVTDSLKKRLERHV | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34902
Sequence Length: 309
Subcellular Location: Cell membrane
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Q8VG43 | MEAENHTTVAELIILGLTEDPKLCIVFFVIFLGVYIITLVGNISIITLIRISSQLHTPMYLFLSHLAFVDIVFSTSVSVIMLMELLGHGLVLSVATCAAQLCMTVSFGSAECFLLAAMAYDRYVAICSPLLYSTLMSSRVCFLLLGISYVGGFVNGWTFTGCVLSLSFCGPTQINHFFCDFSPLLKVSCSDVSIIGIIPSISSGSIIVVTVFVIAVSYIYILITILKMRSTEGRHKAFSTCTSHLTAVTLFYGTITVIYVMPKSSYSTEQNKVISLFYTVVIPMLNPLIYSLRNRDVKDALRKAIVRVYS | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34090
Sequence Length: 310
Subcellular Location: Cell membrane
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Q8VG44 | MEAENHTTVAELIILGLTEDPKLCIVFFVIFLGVYIVTLVGNISIITLIRISSQLHTPMYLFLSHLAFVDILYSTSVSVIMHMELLGHGLALPVAACAAQLCITVSFGSAECFLLAAMAYDRYVAICSPLLYSTLMSPRVCFLLLGMSYVGGCMNGWTFTGCLLSLSFCGPNQIDHFFCDFSPLLKLSCSDVSIIGIIPSISSGSIIVVTVFVIAVSYIYILITILNMRSTEGRHKAFSTCTSHLTAVTLYYGTITFIYVMPKSNYSTEQNKVLSVFYTVVIPMLNPLIYSLRNRDVKEALRKATVRVYS | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34187
Sequence Length: 310
Subcellular Location: Cell membrane
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Q8DC44 | MTNIGSLLVDAAALMVTGMGVVFIFLTILIFLVRLMSKLVPQEVPPPITAPKAVKNQANHTSTVSPQVVAAISAAIHQHRASVAK | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8943
Sequence Length: 85
Subcellular Location: Cell membrane
EC: 7.2.4.2
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A0LSX1 | MTTFVDRVVVHVRGGDGGNGCASIRREKFKPLGGPDGGNGGRGGDVVFVVDPGTTTLLDLHRRPHRRAAPGSPGQGNNKHGADGADLLIPVPDGTVVKDLDGQVLADLVGAGTRYVAARGGRGGLGNAALASARRKAPGFALRGEPGEERDVVVEVKSVADIALVGYPNAGKSSLIAAISAARPKIADYPFTTLAPNLGVVEAGEIRFTVADVPGLVRGASQGRGLGLEFLRHIERCAAVVHVVDCAAAEPDRSPLADLAAIRAELAAYASLDLGGPPLHERPQLVVLNKIDIPEARARAEAAARQIADAPVFLVSAVTR... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A5FV29 | MKFLDQAKIYVRSGDGGNGVVAFRREKYIEFGGPDGGNGGRGGDIVFEAVENLNTLIDFRYTQHFRARKGGNGAGSDRTGAAAPPVVIKVPVGTQILDDDRETLLADLDAPGKRIVLLRGGDGGHGNAMFKTSTNRAPRRADPGWPGEERWVWLRLKLIADAGLVGLPNAGKSTFLSVASAARPKIADYPFTTLHPQLGVVRLSMTEEFVLADIPGLIEGAHDGAGLGDRFLGHVERCAALIHLIDGAAGDVVDAWRTIRGELEAYGGGLADKPELIVLNKMDAMTPHQIAGRRSALERASGCKVMVISAAAHQGVDAVL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
B7J427 | MKFIDEVRIHVASGNGGHGAVSFRREKFIPFGGPDGGDGGRGGSVYLVAQASLNTLIDFRYQRRYRAENGHGGAGRQMTGRAGHDLEIKVPVGTLVYDDDTHELLGDLRFEGERLLIARSGRGGHGNLFYKSSTNRAPRQFEKGGAGEERDLRLELRLLADVGLLGLPNAGKSTLIRAVSAARPKVADYPFTTLYPNLGVVRVAAHESFVLADIPGLIPGASEGAGLGTRFLKHLSRTRLLLHLVDMAPVDGSDPAMNIRALEMELAAYSPTLAARPRWLVVNKSDLLPGEEAEARFQQICTALQWESPAFLISAASGAG... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
Q7CW97 | MKFLDEAKVYIKSGDGGAGAVSFRREKFIEFGGPDGGDGGRGGDVWVEVVNGLNTLIDFRFQQHFKASIGQHGMGKTRTGAKGSDVVLKVPVGTQIFEEDNETLIMDLTKEGQRFRLAAGGNGGFGNAYFKSSTNQAPTHANPGLAGEEKTIWLRLKLIADAGLVGLPNAGKSTFLATVTRARPKIANYPFTTLHPNLGVATIDGREFVLADIPGLIEGAHEGVGIGDRFLGHVERTRVLLHLVSAQEEKVGKAYKTVKAELDAYGGGLTDKPEIVALSQIDVLDEKELKKKAKELEKACGRPPLLLSAAAHIGMTEALR... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
B2UQ30 | MFVDNIRIFARAGKGGNGLVSFRRAKFVPKGGPDGGDGGDGGSVILEVDPHTNDLRSFFYDPKLIATDGVGGQSAKKHGKNGKSVIGKVPPGTIIYRSNASSMAEATWLEREGEGIELEKIADLTEIGTRFTLCQGGLGGKGNWHFRSATNQAPTEAEMGTEGEEGVFFMELRRIADAGLVGYPNAGKSTLLGDISEAKPKVASYPFTTLQPIIGVVEFDSFRRCVVADIPGIIEGAHNNRGLGHEFLRHITRCKVLVFVLDMAGSEGRDPIEDLQNLRTEIKLYSEDLAKQPWFVVANKMDLEGAEENLANFRMRFPKV... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A0M5C6 | MTEGNFVDYVKIHVFSGKGGKGSAHLHREKYITKGGPDGGDGGRGGHVILKGSKNLWTLFHLKFKRHVKAEHGGNGSKQRSSGSQGSDEYIDVPLGTVIRDTETNEIIKEITEDGQEFIVAEGGMGGRGNWHFKSSTNQTPRYAQPGVDGQQIDVTLELKVLADVGLVGFPNAGKSTLLSVITAAKPKIANYEFTTLKPNLGIVEYRDFKTFVVADIPGIIEGAAEGKGLGHRFLRHIERNSTLLFLIPSDARDIKKQYDILLDELKRYNPELMDKDRLVAISKSDLLDEELKAEMAKELDKELQLPYIFISSVAQSGLT... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
Q1R0C0 | MQFVDEASIIVEAGKGGNGCLSFRREKYVPKGGPDGGDGGHGGSVYLIGDESLNTLIDFKYQRFYKAPNGQPGQGRQMSGRNGEDLHVKVPVGTTVIDEDTLEVIADVTEAGQVVLVAQAGRRGLGNIHFKSSTNRAPRKTTPGTEGERRNLRFEMKVMADVGLLGVPNAGKSTLIRAVSAAKPKVANYPFTTLVPNLGVVKLGTHEHFVMADVPGLIEGASDGAGLGLRFLKHLTRTRLLLHVVDVAPFDESDPVDSARAIAHELEQFSATLAERPRWLVLNKLDLLPEEERPSTVDDIVERLAWSGPVYKISAISGDG... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
B5E958 | MSFIDEVKINVKSGDGGAGCVSFRREKFIPLGGPDGGDGGKGGDVIVKVSSHLSTLLDLRQHPHQKAGRGKNGMGSDRHGANGHTLEILVPQGTVIKDAETGEILADLAEPDSSMVLLKGGRGGQGNARFKTATHKAPKFAQPGEPGEERWIRMELKLMADVGLLGMPSVGKSSLIAKISAARPKIAEYHFTTLKPSLGVVQYKNYRSFVMADIPGLIEGASEGAGLGHRFLKHLERTGQLLHLLDLSWMPDRDPIAEYEAINRELALFNPELADKRQTVVVNKIDLPHVRENLKEILPYFEERGIKVFPISAATGEGIP... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
Q72NQ7 | MESFVDEVAIEVFAGHGGAGSVHFRREKYVEFGGPDGGDGGIGGNVVIRPNLSMYTLDKYLSKRKFKAQAGFPGVGDNCSGKKGEDLVLFVPLGTQIYDEETGDLLFDFVSDSQEFVVARGGRGGKGNAHFKTSTNQTPRFAQPGEEGEYKFLRLSLKLLADVGIVGLPNAGKSTLISKITDAHPKIAGYAFTTLSPNLGVVKRRGDIFRFTIADIPGIIEGASMGIGLGLSFLRHIERVKGILYLFDASSLDIEEDLKMLRNELSTYNPELLNRPYLIVLNKIDIWNDPEFTKDVIAKVSHLGKVVAISADQEVNLEEL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
Q2S3C0 | MKFLDQVDLRVSSGDGGKGVVAWRREKYVPKGGPSGGDGGDGGSVYVEADENLYTLMDLSHNTQVFAEDGEPGGRREQTGASGEDKVIRVPPGTVVKTQTGEVLGEVVEPGQRICVAEGGQGGRGNAFFKSSTNQAPRESQPGEPGEERDLTFELKLMADVGLVGFPNAGKSTLVSSVSAAEPEVADYPFTTLTPQLGMVYVSEYETFVMADIPGIIEDAHEGKGLGLQFLRHIERTSVLLFVIPITSQDLGEEYEALLHELESHEASLLDKPRVVALSKIDILAPDERALLPDVVADEFPDDVPLLPISAVADVGLDQL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A4XAG1 | MTTFVDRVVLHLQAGDGGHGCVSVHREKFKPFGGPDGGNGGHGGSVSLVVDPQVHTLLDFHFRPHVKAANGRGGAGSNRDGANGANLVLKVPNGTVVQSGDGTVLADLVGVGTTFEVARGGRGGRGNASLANARRKAPGFAELGEPGDQIDVVLELKSVADVGLVGYPSAGKSSLISVISAAKPKIADYPFTTLVPNLGVVRVDNHTFTVADVPGLIPGAATGKGLGLEFLRHIERCAVLLHVVDTAALETERDPVADIDAIEAELVAYGGLVDRPRLVALNKVDVPDGRDLAEIVRPDLEARGFRVFEVSAATRAGLKE... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
C4L3W2 | MGESSNVHEKSQAFYGPNLGYIIELYEQYLEDPSSVDEETRRYFDEFGAPETSTPTEVPVSGPSFDLEKVVSATRLINDIRAFGHKAADIYPLKDHPREQELFELSRYDLTEEDLKQIPARLLSDDAPKPNASALELFRHLLDVYTGTVAIELRHLDDMEEKKWIRRQVEQGALQQTFSKEEKIELFKRLAETELFESFLHKTYVGQKRFSIEGLDAMVPLLDAMVGGLISSGSEHINIGMAHRGRLNVLAHVLGKPYEMIFAEFQHAPNKELIPSEGSIGINFGWSGDVKYHLGLDRKVVEQQKEVRLNLANNPSHLEF... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
Q5L172 | MAKQTNYAQPWSQFYGPNLGYVIEMYEQYLDDPNSIDPELKQLFEQWGAPVLEEPVSPADDETAKTHQTFRLPETPTIFSKLVAAVKLADSIRHYGHLVADTNPLVKKEKKLRRLELDEYDLTEEDLKRIPVAFLCPHAPAHVKNGWDAILHLRKIYTDKIAFEFSQVHNLEERNWLIQQIESGAYYPSLANKERVALLRRLTEVEGFEKFIHRTYVGQKRFSIEGLDSMVPLLDELVRQAIEHEIDAVNIGMAHRGRLNVLAHVLGKPYEMIFAEFQHAESKNFIPSEGSVAITYGWTGDVKYHLGAARRLRNQSAHTM... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
P45303 | MQQNKAFDDWLASTALGGANQSYIEELYESYLSDPQSVEESWRKTFDSLPKTTALEQPHTPVRDYFRRLARENHNEAVTVIDPAAGAKLVKVLQFINAYRFRGHLEANLDPLNYYRWKVSFVPELDYRHHGFTEQDLNETFNINHYVYKRDTIKLGELAQMLKETYCGSIGLEFMHVQDMEQKMWLQSKMESLLDKPLFTSEERVNFLRELTAADGLERYLGAKFPGAKRFSLEGSDAFIPLMKEIIRHSSRQGVNDVVMGMAHRGRLNMLVNVLGKKPENLFDEFAGKHSSERTGDVKYHQGFSSDFAVDDKRVHLTLA... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
Q9KAT1 | MSSKEHTSEEPWQGFYGPNLGVAVELYEEYQKDPNAVDDELREAFEKWGPPPATAPERTQSTFTAASITDPDVIKKFVGAVKLADHIRAFGHLAADIQPILKEQRREDMFDLDRFGLTESDIRSVPVDLLCPYAPAHVKNGLDAINHLKEVYTKTIAFEFVHVTDEEERKWLNRMIESGLYLPNLSTEQRKSLLKRLTDVEGFEKFLHRTFVGQKRFSIEGLDTLVPMLDEVVREAVHEGTTNVMIGMAHRGRLNVLAHVLNKPYEMIFAEFLHSLNKDLFPSEGSIGINYGWTGDVKYHLGADRQIRDENTAEARLTLA... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
Q02218 | MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEEMYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNVDKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDESDLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFETPGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSENGVDYVIMGMPHRGRLNVLAN... | Function: 2-oxoglutarate dehydrogenase (E1o) component of the 2-oxoglutarate dehydrogenase complex (OGDHC) . Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC . Catalyzes the irreversible decarboxylation of 2-oxoglutarate (a... |
Q72PJ7 | MKIEKLMALYGENGALLEELYNQYKLNPETLDKEWKSFFQEVDTNGLANGSGYTNGNGKSAVATSFTDAQAASIREMGIINLLNAYRRQGHLAAKLDPLGIQKPNRTFIDSKLHNISPADIDTVVDSETLGRVKLAEIVDLYEKVYCNTIGAEHFYLVNDEEREWLQKKMESPEFLAPLPRGIKLRLFEKLFQADYFETFLAKKYVGKKRFSLEGGESFIPLLDTIVEEAGYHQMDGLVIGMAHRGRLNVLVNIIEKPASLIFAEFEEKTDKDNLSYADVKYHLGYSNSRMTTSGKEVKLSLAFNPSHLECVDPVVTGSV... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
P86231 | MFHLRTCAAKSVHKSWDIFFRNTNAGAPPGTAYQSPLSLSRLGFYGLHESDLDKSTRFEEFLQRGRLNVLANVIRYHLGMYHRRSSPYPTDVARICEEAFTRRQILLPFRKPLIVFTPKSLLRHPEARTSFDEMLPGTHFQRVYYDLTRAKPVWYAGRKTHLTELQRFLDTAFDLDAFKK | Function: 2-oxoglutarate dehydrogenase (E1) component of the 2-oxoglutarate dehydrogenase complex (OGDHC), which mediates the decarboxylation of alpha-ketoglutarate. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate dehydrogenase co... |
Q4UKI8 | MEEDLKKTGYLFGGNAVFVDELYRQYLANPASVDQTWQEFFAGIKDNSTVLNKSTAKIIIPYEIKKEPLNNNLSSEVLNNRHLAKPAYREEFKGDTERSTAAYIDIREDASTGSTSKLPLEAKFGKMSSLKAKEMINTYRKHAHYLANLDPLGLELRKTKNDLKLNIETFGLDNSQLEKNINITDEFVGNWNCKLSELVTKLDKTYTGSIGVEFEQIENVEEKNWLYNKLESEVTFSSEDKKTILNDLVEVEGFEQYLHTKFPGAKRFSVEGGDASIVAMSKAIDLSMNQGVEEIVIGMAHRGRLNTLTKVVGKPYKAVI... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
P32473 | MFSRLPTSLARNVARRAPTSFVRPSAAAAALRFSSTKTMTVREALNSAMAEELDRDDDVFLIGEEVAQYNGAYKVSKGLLDRFGERRVVDTPITEYGFTGLAVGAALKGLKPIVEFMSFNFSMQAIDHVVNSAAKTHYMSGGTQKCQMVFRGPNGAAVGVGAQHSQDFSPWYGSIPGLKVLVPYSAEDARGLLKAAIRDPNPVVFLENELLYGESFEISEEALSPEFTLPYKAKIEREGTDISIVTYTRNVQFSLEAAEILQKKYGVSAEVINLRSIRPLDTEAIIKTVKKTNHLITVESTFPSFGVGAEIVAQVMESEA... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] +... |
Q32RM2 | MAEVLLFEALRQGLQEEMDRDPRVMVMGEDVGHYGGSYKVTKGFAERYGDLRLLDTPIAENSFTGMAIGAAMTGLRPVVEGMNMGFLLLAFNQIANNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQMVACSTPYNAKGLIKSAIRSDNPIILFEHVLLYNLKEDLAEEEYLVCLEKAEVVRPGNDITILTYSRMRHNVLQATKSLVYKGYDPEIIDIVSLKPFDLGTIGASVCKTHKVLIVEECMRTGGIGATLRAAIMEHFFDYLDAPILCLSSQDVPTPYSSPLEELTVIQPNQIIQVVE... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6... |
O66113 | MAIELKMPALSPTMEEGTLTRWLVKEGDSIKAGEILAEIETDKAIMEFEAVDEGVITKILIPEGSENVKVGTAIAYLGTDANDVTLDGASAETKAEESAPVASPAKTEAAAVEEAATPSLGKVINSAPEIPEGTEFFQQTLREALRDAMAEEMRRDDRVFVMGEEVAEYQGAYKVTQGLLQEFGARRVVDTPISEYGFSGIGVGAAMEGLRPVIEFMTMNFSMQAIDHIINSAAKTHYMSGGQVRCPIVFRGPNGAAPRVGAQHTQNFGPWYAAVPGLVVLAPYDAIDAKGLLKAAIRSDDPVVFLECELLYGKTFDVPK... | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3... |
P26268 | SNIFKGPTVGSSVVAMSARLASTEATFQAKPFKLHKLDSGPDVNMHVTKEDALRYYTQMQTIRRMETAAGNLYKEKKVRGFCHLYSGQEACAVGMKAAMEPGDAAITAYRCHGWTYLSGSPVAKVLCELTGRITGNVYGKGGSMHMYGENFYGGNGIVGAQQPLGTGIAFAMKYKKQKNVCITLFGDGATNQGQLYESMNMAKLWELPVLYVCENNGYGMGTSAARSSASTDYYTRGDYVPGFWVDGMDVLAVRQAIRWGKEWCNAGKGPLMIEMATYRYGGHSMSDPGTSYRTREEIQEVRKTRDPITGFKDKIVTAGL... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldih... |
P22439 | MAASWRLGCDPRLLRCLLGFGSRRSPELVKGAARWSVGRGASWRWFHSTQWLRADPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVAEGSKNIRLGSLIGLLVEEGEDWKHVEIPKDTGPPPPAAKPSVPPPSAEPQIATPVKKEHPPGKVQFRLSPAARNILEKHALDANQGTATGPRGIFTKEDALKLVQLKQTGKITEPRPTAALPTTPAAPLPPQAAATASYPRPMIPPVSTPGQPNVEGTFTEIPASNIRRVIAKRLTESKSTIPHAYATTDCDLGAVLTARQNLV... | Function: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex acti... |
G0S5Q0 | MASLAAACRVSARLAARKLQHDAAVRGFRSSAAALAAQNFMMPALSPTMTEGNIASWRVKEGERFSAGDVLLEIETDKATMDVEAQEDGILMKIIQPDGSKGVQVGTRIAVVAEEGDDITKLEIPPDEGPQQLKAAAPAPAPTPAPAPASPQPQFAAPTPSPPKASTKVPARKYPLLPSVHQLIKENGLDESAVSNITPTGPGGRILKGDVLAYLGKINPNTPAQISARFEKASHLDLSNVKVAKPVEPEKPQEEKASAPAPAPRAPEPPAKAVVSLPISLSAVLEAQQRINKKLGIFLPLSTFISRATELANEELPLPT... | Function: The 10-megadalton pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) and catalyzes the overall oxidative decarboxylation of pyruvate to form acetyl-CoA and CO(2) . E3BP is ... |
O00330 | MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLRGDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTATPTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLV... | Function: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex acti... |
Q18807 | MSGELWITLVDTADIVGVTLTFCVNIVLLGLLKTRGKNLGTYKYLMAFFSVFSIFYAIIEFILRPIMHIENTTFFLISRKRFNYSTKLGKINSAFYCACFATSFVVSGVHFVYRYFATCKPNLLRLFNLPTLLLWPLGCSVPVTMWASVSYFLYPDTEYTEAAVTNVLNNHYNWIKKENVSYIAYVYYQYENGVRHIYLKNLLGCFVHYFVMSMTFVVMFYCGYATWKTMNEHKDVSDRTRALQKQLFKALVLQTLIPTIFMYAPTGVMFIAPFFDVNLNANANFIVFCSFLYPGLDPLILILIIRDFRRTIFNFLCGKK... | Function: An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39227
Sequence Length: 339
Subcellular Location: Cell projection
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Q8I7F8 | MTRNRRKSKTTATSHPELHLEKVDPMKTVTESMILFDVQLQEWVTKSAKNHEFVLSDKGIPASAYFLLGSFCSDGDIHVAYASKCPVHSSALEENATESSKMLEDEWMSDHAERLLRMLPGGIHVVGIAWFSDKKTFSDRKSHIHKTLGRIQKMNNQITTANVDDSISDNMITVFFETPSTTPIGAIIDVTNRGNDSAQKVQFQKLEWISLVTNASARIVHNVPVDTGRPTDFYSDLVVATKNFVNNLFQCEFTLLDGEIRDDKEPLIKDIKKNKKTTIEAQLFLNPLYNRELGAIDDIASNMHEVLFDIEVRAAVPIRS... | Function: Required, with oct-8, for the localization of a subset of 7 transmembrane domain odorant receptors, including odr-10, to the cilia of olfactory neurons AWA and AWC . Regulates chemotaxis responses to benzaldehyde, diacetyl and 2,4,5-trimethylthiazole in AWA and AWC neurons . Plays a role in nociceptive neuron... |
Q54QH3 | MIINSNIKITLEERSNKLEQSHIEIGLLIGQESEISEQQTFVLGLFPTPLNISNTDDDNNNKPINIDSISSIDKEWILEYCHQVNIMLYGGIDIVGIYMIIPDSDTLNEKNNESFIMKLLKSIHTIINSKSLQFISYSKKTGLINGKATNSTQLYRLKSTEIKVINNLENEFLSLHCILPIDIKLKSKNGMISFENLKKDIIEIFENQLFKESTLLIENEFVSGNEIISQQFKSKSKLNIDLLINQLDSISTSSLEFNFNNNNNTHCIAYIHQLEQIKTAFKFIKKDIIKSVESRFDLLFNEISSNNNNNDNDQDNIKLS... | Function: May play a role in the trafficking of a subset of G-protein coupled receptors.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 52246
Sequence Length: 456
Subcellular Location: Membrane
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Q9VTX8 | MRTVLLSKHDELYLEKCAQENQFSYGIIVGHQADLTKSVVVHLARNNEEDADLEDLSEVRLTISDINSQALASQWLSASKMCPGSFDVIGIFVSSVRSDVVNEQSAEFKNAKKLFSDIYDLLLKSNSSFGVYTTDIAQTDFVFLSYSLADKKVLCKNYSYGNGGTFTNMEFRFVDKPFEWIQLECSYDFDDVLPILDSSRRVNIEDQFQSMIVSVRKNLLASEVFLQNEVVEDTIDLQAYIKKKKTKVDKLQPTSTTGGTATASSNTTDSLPRLASEGIIGGTETIRASIVLPMKCQLSKPTDIKVREFSGTLHMSGIIT... | Function: May play a role in the trafficking of a subset of G-protein coupled receptors.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54587
Sequence Length: 492
Subcellular Location: Membrane
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Q5SWX8 | MGRTYIVEETVGQYLSNINLQGKAFVSGLLIGQCSSQKDYVILATRTPPKEEQSENLKHPKAKLDNLDEEWATEHACQVSRMLPGGLLVLGVFIITTLELANDFQNALRRLMFAVEKSINRKRLWNFTEEEVSERVTLHICASTKKIFCRTYDIHDPKSSARPADWKYQSGLSSSWLSLECTVHINIHIPLSATSVSYTLEKNTKNGLTRWAKEIENGVYLINGQVKDEDCDLLEGQKKSSRGNTQATSHSFDVRVLTQLLLNSDHRSTATVQICSGSVNLKGAVKCRAYIHSSKPKVKDAVQAVKRDILNTVADRCEML... | Function: May play a role in the trafficking of a subset of G-protein coupled receptors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51103
Sequence Length: 454
Subcellular Location: Membrane
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Q8TZ11 | MLEVTLPGEGTPPAEGFRTLHSLKRDLERYFRGYPVDFDDVPVRINVSGKPREVLELVREIPYGTVVTYGDIAQKANTHPRVVGVSLARNRVPIIVACHRVVAADGLGGFRWGLEWKRRLLELEGALPSRR | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
O26715 | MKQFECMYTLINIHEAETFKCMYTLMHPLIDIGVVWGDDGVTAIILLEGVKKYSNDSSPPMAIKKLLDSIRMFLDGCEVDFDLSVLDFGGCTEYQRRVLDVVSSIPRGSTLTYSEVAARAGGSPRSAAGALSRNPFPLVIPCHRVIRSDGNAGGYQGGVKLKKRLLEMEGVSLEGQ | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
P0A697 | MIHYRTIDSPIGPLTLAGHGSVLTNLRMLEQTYEPSRTHWTPDPGAFSGAVDQLNAYFAGELTEFDVELDLRGTDFQQRVWKALLTIPYGETRSYGEIADQIGAPGAARAVGLANGHNPIAIIVPCHRVIGASGKLTGYGGGINRKRALLELEKSRAPADLTLFD | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
P52982 | MIHCRSMDSPIGPLILAGHGSVLTNLQMVDQTYEPSRVGWLPENGAFAEAVSQLDAYFAGELTEFAIELDLCGTEFQQRVWQALLTIPYGETRSYGEIAEQVGAPGAARAVGLANSRNPIAIIVPCHRVIGASGQLIGYGGGLNRKLTLLELEKHQVLTSLTLFD | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
Q9ZET8 | MIEYRTVDSPIGLLTLAGRDPVLTNLRMVDQTYEPSRTGWTENPRAFAGAVEQLGAYFAGELTEFDIELDLRGSEFQRRVWRALQTIPYGETRSYGEIAEQIGAPGAARAVGLANGHNPIAIVVPCHRVIGASGKLTGYGGGLDRKQTLLALERRHSPASLTLFD | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
O93728 | MICSQYGPVVVGWDGSKTFVNPSRCSKRVGLAEFLELINIDEIDKRLLYLLGIPRGYVTTYKLYAEVLGTSPRHVGWLMARNPLPVILPCHRVVKSDFSLGGYTGGVEVKKKLLAYEGALCGDRPCRVVRPRMIDDVRDALFKSLGLA | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
Q8TZV2 | MILEVRKFQVKNKAVYIGTLSEDKIFGIIFSIDEPEVIRHRIPTLINFLEKRLNKKLEIKEGNSGFSDVVFKTLIGKISNEEAAEFIEVSYLTKFERKLYIYLVENVKRGEVITYGELAKILNTSSRAVGAAVKRNPYPIIVPCHRVIGRKNPYLYTPKPEYKKFLLEVEGWTS | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
Q97VW7 | MLVYGLYKSPLGYITVAKDDKGFIMLDFCDCVEGNSRDDSSFTEFFHKLDLYFEGKPINLREPINLKTYPFRLSVFKEVMKIPWGKVMTYKQIADSLGTSPRAVGMALSKNPILLIIPCHRVIAENGIGGYSRGVKLKRALLELEGVKIPE | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
Q6Z1J6 | MPPKASKKDAAPAERPILGRFSSHLKIGIVGLPNVGKSTFFNIVTKLSIPAENFPFCTIDPNEARVYVPDERFDWLCQLYKPKSEVSAYLEINDIAGLVRGAHAGEGLGNAFLSHIRAVDGIFHVLRAFEDKEVTHIDDSVDPVRDLETIGEELRLKDIEFVQNKIDDLEKSMKRSNDKQLKLEHELCEKVKAHLEDGKDVRFGDWKSADIEILNTFQLLTAKPVVYLVNMSEKDYQRKKNKFLPKIHAWVQEHGGETIIPFSCAFERLLADMPPDEAAKYCAENQIASVIPKIIKTGFAAIHLIYFFTAGPDEVKCWQI... | Function: Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP (Potential). Exhibits GTPase activity . Exhibits similar binding affinities and hydrolytic activities toward both GTP and ATP . Binds to the 26 S ribosomal RNA in vitro, but not to the 5.8 S or 18 S rRNA . Confers sen... |
P9WEQ1 | MLNLLLLSLSVCLLYVFITAFWNLYIHPLHHIPGPRQWIAFPILRHLSAIRGTLDSDLRRWHFRYGSAVRFGPDEASFITAEAWKDIYGSTRPQLPRVISSGSNTSDIINANDANHARYRKALAHAFSTNGVRDQEPLVIDYIVKLVGRLKEVAESKLPTDMVKWYKLTTFDMIGDLAFGEHFGGLEKSEYHHWVATVGRFTRIIPFLKIMDAYPVLFKVFLAVMPQSFWKAQAEQAEYTKLTVQKRLNSSIAQDRPDFMDSMLRHRNEKDKLSEHELESNASVLVLAGSETPADLLSGVTYWLLKTPEALEKATGEVRS... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4... |
P9WEQ3 | MESLDFTKAPPEFQEVKYLSDILLVTLASGWLVCYFATIRTAFCDRACWMPLLPLSCNVAWELVFITLYPPPGSPILGFWLLVNLGVIYSALRFAPSKASHLAVEKHYLPVLFVLAVGFWAWGHLALIEQLNPLPAFYYGGMACQLMTSAAALSGLVDQGSTQGASYTIWLSRVIGTSSALAGLFFRAHYWPSLWAWADNELMRWLAAAFGILDGVYGVQFWRLRRSENQLTIDHAHRKTE | Function: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-... |
P9WEQ4 | MEPKDFKVIIIGGSVAGLTLALSLNKIGIDYVVLEKRAHIAPQEGASIGILPHGGRILEQLGLFEAVERSIEPLHTAHIRFPDGFEYTTASPSVLNDRFGLPLAFLERQKMLQILFDAQTEKSKILCGKKVTKIEDFEESMTVYTEDGSTYTGDLVVGADGVHSQVRTEMWRLAEKMQPGIVSNTEKSSMTVQYTCVFGISAAVPGLVPGEQVASFNDKRSFLTFPGKNGRVFWFLINRLDQEHSYSSAPRFSMKDTETICHQFLEDIIYGDVRFNDLWSRKEVCSVTALEEGAFRTWSYRRIVCIGDSMHKMAPNTGQG... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-h... |
P9WEQ6 | MLQGVIDTHQASLRGILATGALVIFVALFLATFQFQVLCLPLINGRKRFELSLTNSKKRYYADAKGFIQSGFSQSKNGFYAITENGRELILAPKFADDIRNDKRFNFHTYREHTMLPNVAGLDLFQLNDLGKKILSHVIGYRLTHNLEWHEVPLRNSLLAVISQQSSRVFLGKKFCRDPTWLKINTDITVLAFRAVQELRVYPNLLRPVVGWFLPACRVLRSEVRKARKIVEPIVQKRRDYKAACLREQTNPEQFLDTIEWAEECAGSQAYDPTVTQLTIALSAMHNTSDFLTQLVFDLCERPNLIEDLRQEIISVRKKH... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4... |
P80443 | VTVYDAEGTKVQLDGSIRLVM | Function: Structural rigidity of the outer membrane of elementary bodies and porin forming, permitting diffusion of solutes through the intracellular reticulate body membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 2295
Sequence Length: 21
Subcellular Location: Cell outer membrane
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P80368 | VTVYDAEGTKVQIDGSLRVEL | Function: Structural rigidity of the outer membrane of elementary bodies and porin forming, permitting diffusion of solutes through the intracellular reticulate body membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 2293
Sequence Length: 21
Subcellular Location: Cell outer membrane
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P80442 | VTVYDAEGTKVQVDGSLRLVE | Function: Structural rigidity of the outer membrane of elementary bodies and porin forming, permitting diffusion of solutes through the intracellular reticulate body membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 2279
Sequence Length: 21
Subcellular Location: Cell outer membrane
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Q83EK8 | METTTKLAIGVSALCCLASAAFAGGPDIPMIDMNGFHIGLGFGYKSYTYDQVGTVTVTTNGGTVLSVLHPVSASITQFGPVGELGYTFASDWWIAGVKAQYQYDNVRSVHIMDAPLVGSNYSYRTRLGSHLTAMLLAGIKVNEANAVYLEAGYSTVWGKTTLFGPGPVAVSMKNRLNGGIAGIGWRHYFMNNVFLDLSYDYALYRSKSNSVTLSSATASAEGTAIGVSGTVQNPKRVAINGITATVNYLFNI | Function: Able to form a pore in lipid bilayers.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26771
Sequence Length: 252
Subcellular Location: Cell outer membrane
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A8ABZ0 | MEAREVEEMRRSRLLTLGGIGYTAVIALAALVLVMGALGLVLKVAAAAGALPSEVAKVANALPGLKASVDANPAAGSLSSVSVST | Function: The most abundant protein of the outer membrane, it forms a pore through it.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8388
Sequence Length: 85
Subcellular Location: Cell outer membrane
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B2SAB9 | MNIKSLLLGSAAALVAASGAQAADAIVAPEPEAVEYVRVCDAYGAGYFYIPGTETCLRVHGYVRYDVKGGDDVYSGTDRNGWDKGARFALMFNTNSETELGTLGTYTQLRFNYTSNNSRHDGQYGDFSDDRDVADGGVSTGKIAYTFTGGNGFSAVIALEQGGEDVDNDYTIDGYMPHVVGGLKYAGGWGSIAGVVAYDSVIEEWATKVRGDVNITDRFSVWLQGAYSSAATPNQNYGQWGGDWAVWGGAKFIAPEKATFNLQAAHDDWGKTAVTANVAYQLVPGFTITPEVSYTKFGGEWKDTVAEDNAWGGIVRFQRS... | Function: Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34535
Sequence Length: 321
Domain: Consists of 16-stranded beta-barrel sheets, with large surface-exposed loops, that form a trans... |
Q04064 | MKKTLLAAALLAGFAGAAQAETSVTLYGIIDTGIGYNDVDFKVKGANADDSDFKYNHSRFGMINGVQNGSRWGLRGTEDLGDGLQAVFQLESGFNSGNGNSAQDGRLFGRQATIGLQSESWGRLDFGRQTNIASKYFGSIDPFGAGFGQANIGMGMSAMNTVRYDNMVMYQTPSYSGFQFGIGYSFSANDKDADAVNRVGFATADNVRAITTGLRYVNGPLNVALSYDQLNASNNQAQGEVDATPRSYGLGGSYDFEVVKLALAYARTTDGWFGGQGYPVAVTLPSGDKFGGFGVNTFADGFKANSYMVGLSAPIGGASN... | Function: Forms anion selective channels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41046
Sequence Length: 385
Subcellular Location: Cell outer membrane
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S7ZC62 | MRGYRSSQRTFFRGFDPRHAYRFRGDGRHGGMGGALKIVFLGMMTYFIAKKAFRSSQHPPTDFNAPVQSVPQRAQRPSDTRLQGPVLLASNHPSGDSASPE | Function: Part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid . Does not seem to play a role in oxopyrrolidines A and B biosynthesis .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11253
Sequenc... |
S8AKG0 | MSETRDPRTHSESSLEKGTHPPHQDELATNSTTKDASPVITSTPKKQGAKAWLSLAAGFMGMFASFGWVNCVAIFQAEYEMNQLRDYSSSQVGWISSVLFFFMLGVSPVAGRLYDGYGPRLPIMIGCFFHVFGLMMTSLATRYYQFILSQSVCSGIGTSLIITPAMTAPTTYFHDRRALAGGVTIAGSSLGGVVFPFMVNHLLSSIGFAWTMRACAFLILVLMVITYTLISSNVTHIPKEFKLKNYLTPLRECNFLLLCLVSFFMYWGMFIPYVYMVISSIHYGMSVQMGYNLIPILNGISFFGRIVPQFWARKYGICNV... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48262
Sequence Length: 443
Subcellular Location: Membrane
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S7Z6Y2 | MSEDSQPRLLESDPNPGDRDLKAVNSNPSDNRLNNQSDDYEPEWVEGITLVMVISGITLVVFLMLLDMSIVSTAIPKITTQFDSLGDVAWYGSAYTISSAAFQPLTGKFYNYLSSKWTFLSFFGIFEVGSLVCGVANSSKMLIIGRAVAGVGSSGMMNGALSILAGAVPIKRRPTMIGIIMGVGQLGLVGGPLVGGAFTTYSTWRWCFYMNLPVGALVGVLLLFTRVPDQKPKQPAREVLRSVVLRRFDFIGFVLFAPASIMLLLALQYGGNEYSWDSATVIGLICGSVATFVVFGLWERHMGIEAMIPGHLVRDKIVFF... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60325
Sequence Length: 560
Subcellular Location: Membrane
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S7ZC75 | MSDELKDNAAKEASFGAFLTRQLMKSVPAVTGNLDGKVAIVTGANVGLGLACARQLLSLQLSHLILAVRSLRKGEAAALELQASFPHARVEVWALEMESYASIQAFVSRCHSELGRVDIAILNAGLALKRFQTCTNPQTTPREITLQVNFLSTVFLALLLLPILGAKKEKKDAVFIPGRLTLVGSDTVYWVNARELKSRPLLQAANSSEGFDGFEQYKMSKLFVLMFVAKLARDLVSPDQVIVNVACPGLCKGTAFVREPDSNWAKQAIVSSLIRLVGRTPEQGARVYLAAAILQGPKSHGSMISEGDILP | Function: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid . Does not seem to play a role in oxopyrrolidines A and B biosynthesis . May be involved in further modifications of these oxop... |
P0A434 | MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no d... |
P20401 | MSNSLPVPMSLNEYLAHLPMSDEQRAELAGCTTFAELHERLSAQPVTDPAEAAQASVGRRLTLTPRDQLEDAEMLGVDASGRLCLKATPPIRRTKVVPEPWRTNILVRGWRRLTGKGNPPKPEHDDLPRDLPKARWRTVGSIRRYILLILMLGQTIVAGWYMKGILPYQGWSLVSLDEITRQTFVQTALQVMPYALQTSILLLFGILFCWVSAGFWTALMGFLELLTGRDKYRISGASAGNEPIEKGARTALVMPICNEDVPRVFAGLRATFESVAATGDLDRFDFFVLSDTNETDIAVAEQQAWLDVCRETKGFGKIFY... | Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91130
Sequence Length: 804
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.-
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Q6N5U3 | MDAVIAPRHEDCRDVERRAEPLPANAPLPMPVQSLLQSPRAAAVRSPAAWRRVLIMVATAVLSAAGIYEMYQVLQVGGITVLEGVVLVLFAALFAWVALSFVSALAGFTVLCCGWRDDVGISTDGSLPSVSSRIAMLLPTYNEDAPVVFARLQATRQSVDETGRGAQFDWFVLSDSTDPSVWIDEERCYAELAATHDRLYYRHRPHNTARKSGNIADWVERFGGAYDFMVILDADSVMTGDVLVRVAAAMETNSDVGLIQTLPVVVQARTLFARVQQFAGSIYGPMIAAGTAWWHGSESNYWGHNAIIRVSAFAGSAGLP... | Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79058
Sequence Length: 721
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.-
|
Q8ZQ26 | MNKTTEYIDALLLSEREKAALPKTDIRAVHQALDAEHRTYSREDDSPQGSVKARLEHAWPDSLAKGQLIKDDEGRDQLQAMPKATRSSMFPDPWRTNPVGRFWDRLRGRDVTPRYVSRLTKEEQASEQKWRTVGTIRRYILLILTLAQTVVATWYMKTILPYQGWALINPMDMVGQDIWVSFMQLLPYMLQTGILILFAVLFCWVSAGFWTALMGFLQLLIGRDKYSISASTVGDEPLNPEHRTALIMPICNEDVSRVFAGLRATWESVKATGNAAHFDVYILSDSYNPDICVAEQKAWMELIAEVQGEGQIFYRRRRRR... | Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 97101
Sequence Length: 847
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.-
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Q8EF78 | MTVSESSVLDTEVLVGGSAMPNERPGPMEPQSLSQMPEGFPRRSTVANGVRSRASRRFFVVGGALLLSSFAIYEMGAVFSIGGITPLEYLMLALFAINFCWIALAFCSGIAGFLLLLKKPKPNELAQTELHTRTAILMPTYNESPDRVFSAVSVMAEALSQTGHGHAFDWFILSDTTDPEIALLEEQAFLVLRQETHKHSRVYYRRRRKNVARKAGNVADFCRRWGSRYDHLLVLDADSLMESSTITGLAQRMQADPDAGLIQTIPSLINGTTLMARLQQFAARIYGPVIGTGLGWWVQKEGNFWGHNAIIRTEAFMGAA... | Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81034
Sequence Length: 727
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.-
|
O02464 | MDPGPGLAALQAWAAKSPAYGAANQTVVDKVPPDMMHMIDPHWYQFPPMNPLWHALLGFTIGVLGFVSISGNGMVIYIFMSTKSLKTPSNLLVVNLAFSDFLMMCAMSPAMVVNCYYETWVWGPFACELYACAGSLFGCASIWTMTMIAFDRYNVIVKGIAAKPMTSNGALLRILGIWVFSLAWTLLPFFGWNRYVPEGNMTACGTDYLSKSWVSRSYILIYSVFVYFLPLLLIIYSYFFIVQAVAAHEKAMREQAKKMNVASLRSSEAANTSAECKLAKVALMTISLWFMAWTPYLVINYTGVFESAPISPLATIWGSL... | Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May play a role in photoperiodic photoreception.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41432
Sequence Length: 377
Subcellular Location: Me... |
J5J924 | MRFLAGGASASVAAVGAGTVADLWEVKRRGTAMGYFFLGPMLGPLVSPIIGGILTQRFGWRSTQWGAVVYGGLVWLSMIFLLPETSSKAVKGKEPAVAENSDDGNVQPVPESCVSRFFKALGRMLVEPFRLVGYLRSPPLFMTCYYASISFACYYILNLAIQRTFSRDPYSFRAIILGLLYIPSALGSIVASVVGGRWTDYVMRREAKAAGRFDESGNPKFRPSDRMCENAWIPAFVFPAALLVFGWTTHEGIFWFAPIVVTFFFGLGNSLIFNTATTMLTEILPGKASNAVALNNLMRNTLSCAAAVATDPLLGAIGTQ... | Function: MFS transporter; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects . The function of this putative MFS transporter remains unclear since its delet... |
Q26495 | MVNTTDFYPVPAAMAYESSVGLPLLGWNVPTEHLDLVHPHWRSFQVPNKYWHFGLAFVYFMLMCMSSLGNGIVLWIYATTKSIRTPSNMFIVNLALFDVLMLLEMPMLVVSSLFYQRPVGWELGCDIYAALGSVAGIGSAINNAAIAFDRYRTISCPIDGRLTQGQVLALIAGTWVWTLPFTLMPLLRIWSRFTAEGFLTTCSFDYLTDDEDTKVFVGCIFAWSYAFPLCLICCFYYRLIGAVREHEKMLRDQAKKMNVKSLQSNADTEAQSAEIRIAKVALTIFFLFLCSWTPYAVVAMIGAFGNRAALTPLSTMIPAV... | Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass ... |
P04950 | MESGNVSSSLFGNVSTALRPEARLSAETRLLGWNVPPEELRHIPEHWLTYPEPPESMNYLLGTLYIFFTLMSMLGNGLVIWVFSAAKSLRTPSNILVINLAFCDFMMMVKTPIFIYNSFHQGYALGHLGCQIFGIIGSYTGIAAGATNAFIAYDRFNVITRPMEGKMTHGKAIAMIIFIYMYATPWVVACYTETWGRFVPEGYLTSCTFDYLTDNFDTRLFVACIFFFSFVCPTTMITYYYSQIVGHVFSHEKALRDQAKKMNVESLRSNVDKNKETAEIRIAKAAITICFLFFCSWTPYGVMSLIGAFGDKTLLTPGAT... | Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass ... |
J4VWM7 | MGSIREPLHLVVIGGGLAGLSAAIATRLEGHRCTLLEKAPEFNEVGAGLQLTPNSTRLLRRWGVLDKLRSKAGIPTQLTVRRYDGSKVLSRADGWDETMQSQYDAPFWDMHRADLQAAMVARARHLGVDVRTGAEVESIDTDGVAVILAGTRERLQGDVVLAADGLWSRTRAALFPDLGTAPQPTGDLAYRIILRLENLQHDPELAAWVAKPTVNFWVGADAHAVAYSVRGGSELNLVLLCPDDLPEGCARAQADLEEMRARFQGWDPLLCRFLDNVKTVEKWRLMHMPSLPKWNHESGYFTMAGDSCHPMLPYLAQGAN... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects . The non-reducing polyketide synthase OpS1 produces orsellinic aci... |
J5JH35 | MMRPWTILIASSWLSLAAASASASACAAKPSVAAEIASIDHDNCEHGPNSRGCWGDYSINTNYYEQAPDTGVTREYWFVVENITMAPDGYEQHVLAINRSIPGPLIEANWGDEVVIHVTNNMERNGTAIHWHGIRQLNNNAHDGVPGVTQCPIPPGGSYTYRWKAEQYGTSWYHSHFSLQYSVGLQGPMIIHGPATANYDEDLGTVMLQDWSHVSPFAMWWYARVPSGPPSLSNSLINGKNIFRCTDPLDKNCLGTGERSEWHFEKGKRYRMRLVNTGLYSNFRFAIDGHNLTVIANDFVPIEPYTTDNVIISMGQRYDV... | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects . The non-reducing polyketide synthase OpS1 produces orsellinic acid by condensi... |
P91657 | MHINGPSGPQAYVNDSLGDGSVFPMGHGYPAEYQHMVHAHWRGFREAPIYYHAGFYIAFIVLMLSSIFGNGLVIWIFSTSKSLRTPSNLLILNLAIFDLFMCTNMPHYLINATVGYIVGGDLGCDIYALNGGISGMGASITNAFIAFDRYKTISNPIDGRLSYGQIVLLILFTWLWATPFSVLPLFQIWGRYQPEGFLTTCSFDYLTNTDENRLFVRTIFVWSYVIPMTMILVSYYKLFTHVRVHEKMLAEQAKKMNVKSLSANANADNMSVELRIAKAALIIYMLFILAWTPYSVVALIGCFGEQQLITPFVSMLPCLA... | Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass ... |
J4UHQ8 | MASLQPIKLYAHKKGPNPWKVALILEELGLPYETTYLEFPDAKVEPYISLNPNGKLPAIQDPNHSIELFESGAIIEYLIEQYDKDGKLSHESLQDKSLARAWLHLQMSAQAPVIGYKVWMGRTYDASQIVSANEFLTLEIKRVLGVLDKHLAKMGGPYLLGSKVSYADLAFVPHYMMLPLFVPDYDPATEYPHFAAWLAALKERPAVKKIAATKAALA | Function: Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects . The non-reducing polyketide synthase OpS1 produces ors... |
O61303 | MSNDSIHWEARYLPAGPPRLLGWNVPAEELIHIPEHWLVYPEPNPSLHYLLALLYILFTFLALLGNGLVIWIFCAAKSLRTPSNMFVVNLAICDFFMMIKTPIFIYNSFNTGFALGNLGCQIFAVIGSLTGIGAAITNAAIAYDRYSTIARPLDGKLSRGQVILFIVLIWTYTIPWALMPVMGVWGRFVPEGFLTSCSFDYLTDTNEIRIFVATIFTFSYCIPMILIIYYYSQIVSHVVNHEKALREQAKKMNVDSLRSNANTSSQSAEIRIAKAAITICFLYVLSWTPYGVMSMIGAFGNKALLTPGVTMIPACTCKAV... | Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to 11-cis-retinal.
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Ma... |
Q90309 | MDAWTYQFGNLSKISPFEGPQYHLAPKWAFYLQAAFMGFVFFVGTPLNAIVLFVTMKYKKLRQPLNYILVNISLGGFIFDTFSVSQVFFSALRGYYFFGYTLCAMEAAMGSIAGLVTGWSLAVLAFERYVVICKPFGSFKFGQSQALGAVALTWIIGIGCATPPFWGWSRYIPEGIGTACGPDWYTKNEEYNTESYTYFLLVSCFMMPIMIITFSYSQLLGALRAVAAQQAESASTQKAEKEVSRMVVVMVGSFVVCYGPYAITALYFSYAEDSNKDYRLVAIPSLFSKSSCVYNPLIYAFMNKQFNACIMETVFGKKID... | Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass ... |
Q57336 | MPLFTEAPKSLCILRLSAVGDVCHALAVVQHIQEYYPQTEMTWIVGKTEMGLLSSIPNITLIPYDKKTGWKGVLSLWKQLKNKQFDALLNMQTAFRASILSLGIKAKFKIGFGEKRSREGQWLFVNRRIRDPFSPHVLDGFMAFAEYIGVPKAEPKWELAISQDDYKFADQFIDFSRKNLLISPCSSKAEKDWLIEGYAEVANIAHQHNINVIFCSSPAKRELEIVEKITALCHFTPTNIAGKTNLKQLTALISKVDLVLSPDSGPAHIATTQGTPVIGLYAYHNPLRTAPYNNLDNVVSVYEENAQKEFGKPSSELPWA... | Function: Catalyzes heptose transfer to the lipopolysaccharide core. It transfers the first L-glycero-D-manno-heptose to the phosphorylated 3-deoxy-alpha-D-manno-octulosonic acid (Kdo-P) of the inner core.
Sequence Mass (Da): 38938
Sequence Length: 347
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis... |
O14718 | MLRNNLGNSSDSKNEDGSVFSQTEHNIVATYLIMAGMISIISNIIVLGIFIKYKELRTPTNAIIINLAVTDIGVSSIGYPMSAASDLYGSWKFGYAGCQVYAGLNIFFGMASIGLLTVVAVDRYLTICLPDVGRRMTTNTYIGLILGAWINGLFWALMPIIGWASYAPDPTGATCTINWRKNDRSFVSYTMTVIAINFIVPLTVMFYCYYHVTLSIKHHTTSDCTESLNRDWSDQIDVTKMSVIMICMFLVAWSPYSIVCLWASFGDPKKIPPPMAIIAPLFAKSSTFYNPCIYVVANKKFRRAMLAMFKCQTHQTMPVT... | Function: May play a role in rpe physiology either by detecting light directly or by monitoring the concentration of retinoids or other photoreceptor-derived compounds.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37423
Sequence Length: 337
Subcellular Location: Membrane
|
O35214 | MLSEASDFNSSGSRSEGSVFSRTEHSVIAAYLIVAGITSILSNVVVLGIFIKYKELRTPTNAVIINLAFTDIGVSSIGYPMSAASDLHGSWKFGHAGCQIYAGLNIFFGMVSIGLLTVVAMDRYLTISCPDVGRRMTTNTYLSMILGAWINGLFWALMPIIGWASYAPDPTGATCTINWRNNDTSFVSYTMMVIVVNFIVPLTVMFYCYYHVSRSLRLYAASDCTAHLHRDWADQADVTKMSVIMILMFLLAWSPYSIVCLWACFGNPKKIPPSMAIIAPLFAKSSTFYNPCIYVAAHKKFRKAMLAMFKCQPHLAVPEP... | Function: May play a role in rpe physiology either by detecting light directly or by monitoring the concentration of retinoids or other photoreceptor-derived compounds.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37209
Sequence Length: 337
Subcellular Location: Membrane
|
Q9SS80 | MNPATDPVSAAAAALAPPPQPPQPHRLSTSCNRHPEERFTGFCPSCLCERLSVLDQTNNGGSSSSSKKPPTISAAALKALFKPSGNNGVGGVNTNGNGRVKPGFFPELRRTKSFSASKNNEGFSGVFEPQRRSCDVRLRSSLWNLFSQDEQRNLPSNVTGGEIDVEPRKSSVAEPVLEVNDEGEAESDDEELEEEEEEDYVEAGDFEILNDSGELMREKSDEIVEVREEIEEAVKPTKGLSEEELKPIKDYIDLDSQTKKPSVRRSFWSAASVFSKKLQKWRQNQKMKKRRNGGDHRPGSARLPVEKPIGRQLRDTQSEI... | Function: Potentiates primary root protophloem differentiation . Required, together with VCC, for embryo provasculature development and cotyledon vascular complexity and connectivity . Regulates roots architecture . Mediates the recruitment of ASK7/BIN2 to the plasma membrane .
PTM: Phosphorylation at Ser-318 amplifies... |
Q9FG72 | MTSVFDEHKPSDDSHESKIVINGEEEVLEEENDNPIEEVRLTVPITDDPTLPVLTFRTWTLGLFSCILLAFVNQFFGFRSNQLWVSSVAAQIVTLPLGKLMAKTLPTKKFGFPGTNWSWSFNPGPFNMKEHVLITIFANTGAGGVYATSIITIVKAFYNRQLNVAAAMLLTQTTQLLGYGWAGIFRKFLVDSPYMWWPSNLVQVSLFRALHEKEDLQKGQQTRFRFFIIVFCVSFAYYIIPGYLFPSISAISFVCWIWKSSVTAQIVGSGLKGLGIGSFGLDWSTVAGFLGSPLAVPFFAIANFFGGFFIFLYIVLPIFY... | Function: Involved in the translocation of tetra- and pentapeptides across the cellular membrane in an energy-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85349
Sequence Length: 755
Subcellular Location: Membrane
|
P40897 | MSTIYRESDSLESEPSPTPTTIPIQINMEEEKKDAFVKNIDEDVNNLTATTDEEDRDPESQKFDRHSIQEEGLVWKGDPTYLPNSPYPEVRSAVSIEDDPTIRLNHWRTWFLTTVFVVVFAGVNQFFSLRYPSLEINFLVAQVVCYPIGRILALLPDWKCSKVPFFDLNPGPFTKKEHAVVTIAVALTSSTAYAMYILNAQGSFYNMKLNVGYQFLLVWTSQMIGYGAAGLTRRWVVNPASSIWPQTLISVSLFDSLHSRKVEKTVANGWTMPRYRFFLIVLIGSFIWYWVPGFLFTGLSYFNVILWGSKTRHNFIANTI... | Function: High affinity transporter for glutathione. Also transports tetra- and pentapeptides like the opioids leucine enkephalin (Tyr-Gly-Gly-Phe-Leu) and methionine enkephalin (Tyr-Gly-Gly_Phe-Met) across the cell membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91616
Sequence Length: 799
... |
Q06593 | MSETVKDKVIIDEKVSTKGTVDYAEGAEYSERLSNHSSDFSQWYTDEQILHFMKKLGYENRTLYDIPEDVAYILKKMPELTLEDSFKILKDSIIYFKDDENIPHDQYEEWKRLVDLEDLDSKEGIDEYDSFDIRAFASAIKFHSPYQEVRAVVDPEDDPTIPVETFRAYFLAIIWSVIGSGFNEFFSHRVVSISLNTPIIQMFLYICGKAWAKTIPCWTITIRGRKYGINIDKPWTQKEQMFSTLLYAICQGAFYTHYNILTQKLFYHSAFSFGYQFLLSLSVQFIGFGFAGILRKFVVYPARALWPTVMPTIAINKALL... | Function: Transports tetra- and pentapeptides. Does not transport glutathione.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101261
Sequence Length: 877
Subcellular Location: Membrane
|
O23482 | MDAEKATDKTNVHLSSDHERCPVEEVALVVPETDDPSLPVMTFRAWFLGLTSCVLLIFLNTFFTYRTQPLTISAILMQIAVLPIGKFMARTLPTTSHNLLGWSFSLNPGPFNIKEHVIITIFANCGVAYGGGDAYSIGAITVMKAYYKQSLSFICGLFIVLTTQILGYGWAGILRRYLVDPVDMWWPSNLAQVSLFRALHEKENKSKGLTRMKFFLVALGASFIYYALPGYLFPILTFFSWVCWAWPNSITAQQVGSGYHGLGVGAFTLDWAGISAYHGSPLVAPWSSILNVGVGFIMFIYIIVPVCYWKFNTFDARKFP... | Function: May be involved in the translocation of tetra- and pentapeptides across the cellular membrane in an energy-dependent manner. Acts also as a metal transporter that could be a component of the copper transport machinery. Essential for early embryo development.
Location Topology: Multi-pass membrane protein
Sequ... |
Q9FME8 | MATADEFSDEDTSPIEEVRLTVTNTDDPTLPVWTFRMWFLGLISCSLLSFLNQFFSYRTEPLVITQITVQVATLPIGHFLAKVLPKTRFGLPGCGSARFSLNPGPFNMKEHVLISIFANAGSAFGSGSAYAVGIITIIKAFYGRSISFIAGWLLIITTQVLGYGWAGLLRKYVVEPAHMWWPSTLVQVSLFRALHEKDDQRMTRAKFFVIALVCSFGWYIVPGYLFTTLTSISWVCWAFPRSVTAQQIGSGMRGLGLGAFTLDWTAVASFLFSPLISPFFAIANVFIGYVLLIYFVLPLAYWGFDSYNATRFPIFSSHLF... | Function: Involved in the translocation of tetra- and pentapeptides across the cellular membrane in an energy-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81793
Sequence Length: 729
Subcellular Location: Membrane
|
Q9SUA4 | MVGSLEVSKPPEHKVESKIVIADEEEEDENDSPIEEVRLTVPITDDPSLPVLTFRTWFLGMVSCVVLAFVNNFFGYRSNPLTVSSVVAQIITLPLGKLMATTLPTTKLRLPGTNWSCSLNPGPFNMKEHVLITIFANTGAGGAYATSILTIVKAFYHRNLNPAAAMLLVQTTQLLGYGWAGMFRKYLVDSPYMWWPANLVQVSLFRALHEKEEKREGKQTKLRFFLIVFFLSFTYYIVPGYLFPSISYLSFVCWIWTRSVTAQQIGSGLHGLGIGSFGLDWSTVAGFLGSPLAVPFFAIANSFGGFIIFFYIILPIFYWS... | Function: Involved in the translocation of tetra- and pentapeptides across the cellular membrane in an energy-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84890
Sequence Length: 753
Subcellular Location: Membrane
|
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