ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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Q4UQV0 | MSTSLPLRDDGAVRASFALALFVLLGLGLGYSLVATGITSALMPDQAHGSLLRADGRVIGSSLVAQPFADARYFQPRPSAAKYDPTAAAGSNQARSNPELLARIATARAEIAQRDGIAPDAVPGELLTQSGSGLDPHLSPAGAQVQLRRVAAARGWPEQRVAALLQAATEQPQFGLLGQPRINVLALNLALDRAGDGVPGTENGVEQQR | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21691
Sequence Length: 209
Subcellular Location: Cell inner membrane
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P94608 | MDINYERPDPYYLLNKIDKEEKNKNRGKLKIFFGYAAGVGKTYAMLRAAHYMKELGKDIVIGYIEPHARMDTMSLTKGLPQIPVKNIDYKGVILREFDVDKALLRKPEIILVDELAHTNAKSQRNKKRWKDIEELLDAGIDVYTTLNVQHIESLNDIVANITHVSVRETIPDKVFDDADKVELIDIEPDELLKRFTDGKIYRKEQVKRAFNNFFTKNNLYALREIALRRTADRVNFEIEIARLSKGQITVMATSDQILACIGTSPSSARIIRTAARMAESYHSKWIALYVDTGRSLGKADKETLNANFNLVELLGGELVTVHGENVADQIIRYAELRNTTKIVIGKNHKRTGTLLHFYAKDVVDKLMDSNSYIDVYMIPNSSYYRDHKNSILSKISIQHKGSVKDVLKAIIIMAITTDIAELFSYMGFKDVNVIMIFILGVIIVYMATKGQIMGIISSIAAVLVFNYRFTEPKNSFIVYDKSYLVTFPIMMIVAFIIGSLTNKVQKEAQDSNMREKRTQTLYIVSGKLLSAVGTSEVVSIGIKYISRLVNRNVICYLADTSNKLSTPFVYKKDKGAKEEIIMSKDENAAAYWTFLNGKESGCGTSTFYRAKGYYIPIKIKNKVLGVIGVSCPSGPLRPQKKAVVDTVTGQIAIALDREILSKEQEKSKVEIERERLRSNLLRSISHDLRSPLAGIKGAASTILENGELIDEKRKQELINGIYEDTEWLIRLIENLLSMTKFDEGNTKIKKDVELVEEVVSEAVQRSSKYFKNHKIKVSVPEDVIMVSMDGSLIEQVIINLLDNASKFSPKGSTIEIKVYEKKKDVVFEIIDEGQGISEDILPNIFDRFFTNGSKISDSRRGVGLGLAICKSIVEAHGGKIEAVNKGSGGAIFKFNIPKEL | Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals (By similarity).
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101360
Sequence Length: 900
Subcellular Location: Cell membrane
EC: 2.7.13.3
|
P21865 | MNNEPLRPDPDRLLEQTAAPHRGKLKVFFGACAGVGKTWAMLAEAQRLRAQGLDIVVGVVETHGRKDTAAMLEGLAVLPLKRQAYRGRHISEFDLDAALARRPALILMDELAHSNAPGSRHPKRWQDIEELLEAGIDVFTTVNVQHLESLNDVVSGVTGIQVRETVPDPFFDAADDVVLVDLPPDDLRQRLKEGKVYIAGQAERAIEHFFRKGNLIALRELALRRTADRVDEQMRAWRGHPGEEKVWHTRDAILLCIGHNTGSEKLVRAAARLASRLGSVWHAVYVETPALHRLPEKKRRAILSALRLAQELGAETATLSDPAEEKAVVRYAREHNLGKIILGRPASRRWWRRETFADRLARIAPDLDQVLVALDEPPARTINNAPDNRSFKDKWRVQIQGCVVAAALCAVITLIAMQWLMAFDAANLVMLYLLGVVVVALFYGRWPSVVATVINVVSFDLFFIAPRGTLAVSDVQYLLTFAVMLTVGLVIGNLTAGVRYQARVARYREQRTRHLYEMSKALAVGRSPQDIAATSEQFIASTFHARSQVLLPDDNGKLQPLTHPQGMTPWDDAIAQWSFDKGLPAGAGTDTLPGVPYQILPLKSGEKTYGLVVVEPGNLRQLMIPEQQRLLETFTLLVANALERLTLTASEEQARMASEREQIRNALLAALSHDLRTPLTVLFGQAEILTLDLASEGSPHARQASEIRQHVLNTTRLVNNLLDMARIQSGGFNLKKEWLTLEEVVGSALQMLEPGLSSPINLSLPEPLTLIHVDGPLFERVLINLLENAVKYAGAQAEIGIDAHVEGENLQLDVWDNGPGLPPGQEQTIFDKFARGNKESAVPGVGLGLAICRAIVDVHGGTITAFNRPEGGACFRVTLPQQTAPELEEFHEDM | Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 98718
Sequence Length: 894
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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P61656 | MKDNTCTKRDFLNGTKIGGDEPFFLISGPCVMENRDLLDRVCAEMIEVCGELKIPYIFKSSFDKANRSSVNSYRGPGLAEGIKNLEYIKNKYNVPVLTDIHETSQISPLKDVIDVYQIPAFLCRQTDLISQSAQTGKWVNVKKGQFLAPADTRHIAVKMNESGNNKLLVTERGTSFGYGNLIFDGRAIPIIHGFDIPLVFDATHSAQLPGAAGNSTGGQREFIPSILRSAVSFGIEGIFMEVHPDPPNALSDATTQYPLSQIKSLLKEMIGLDRYIKKEILISRSSL | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 31703
Sequence Length: 287
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.5.1.55
|
Q604M5 | MSNVETSARPFELCGFPVGLEHPLFLIAGPCVIETEQLALDTAGALKEITDGLGIPFIYKSSFDKANRSSHASYRGPGMEEGLRILAEVKRQIGVPVLTDVHEDTPLQEVASVVDVLQTPAFLCRQTNFIQNVANTGKPVNLKKGQFLAPWDMKHVAAKALATGNRHIMVCERGVSFGYNNLVSDMRSLSIMRETGCPVVYDATHSVQLPGGQGTASGGQREFVPALARAAVAVGISGLFMETHPDPDRALSDGPNSWPLDRMKALLELLSTLDRTVKASPLL | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 30506
Sequence Length: 283
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.5.1.55
|
Q9JZ55 | MDIKINDITLGNNSPFVLFGGINVLESLDSTLQTCAHYVEVTRKLGIPYIFKASFDKANRSSIHSYRGVGLEEGLKIFEKVKAEFGIPVITDVHEPHQCQPVAEVCDVIQLPAFLARQTDLVVAMAKTGNVVNIKKPQFLSPSQMKNIVEKFHEAGNGKLILCERGSSFGYDNLVVDMLGFGVMKQTCGNLPVIFDVTHSLQTRDAGSAASGGRRAQALDLALAGMATRLAGLFLESHPDPKLAKCDGPSALPLHLLEDFLIRIKALDDLIKSQPILTIE | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 30483
Sequence Length: 280
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.5.1.55
|
Q3SRK0 | MNQPVSASPVVSVGSVTFGQDRPLSIIAGPCQMESRAHALEVAGALKDIAARLNVGLVFKTSFDKANRTSASGARGIGLKQALPVFADIRSSLGLPVLTDVHEAAQCAEVAQVVDVLQIPAFLCRQTDLLLAAAATGKVVNVKKGQFLAPWDMGNVVAKITGGGNRNILVTERGASFGYNTLVSDMRALPILARTTGAPVIFDATHSVQQPGGKGASTGGEREFVPVLARAAVAVGVAGVFIETHPDPDHAPSDGPNMVPLREFEALVRRLMAFDALAKAADPACPE | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 29822
Sequence Length: 287
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.5.1.55
|
O66914 | MRRAVIIPARLGSTRLKEKPLKNLLGKPLIRWVVEGLVKTGERVILATDSERVKEVVEDLCEVFLTPSDLPSGSDRVLYVVRDLDVDLIINYQGDEPFVYEEDIKLIFRELEKGERVVTLARKDKEAYERPEDVKVVLDREGYALYFSRSPIPYFRKNDTFYPLKHVGIYGFRKETLMEFGAMPPSKLEQIEGLEQLRLLENGIKIKVLITENYYHGVDTEEDLKIVEEKLKNL | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27173
Sequence Length: 234
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q9C920 | MSVCSSSSSSQKTWIVNGILAGTAIAAAIGARAYLGRSKKFRSRVVGIIPARYASSRFEGKPLVQILGKPMIQRTWERSKLATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEALEKLEKKYDVVVNIQGDEPLIEPEIIDGVVKALQVTPDAVFSTAVTSLKPEDGLDPNRVKCVVDNRGYAIYFSRGLIPYNKSGKVNPDFPYMLHLGIQSFDSKFLKVYSELQPTPLQQEEDLEQLKVLENGYKMKVIKVDHEAHGVDTPDDVEKIESLMRERNMS | Function: Catalyzes the production of the sugar nucleotide CMP-3-deoxy-D-manno-octulosonate (CMP-KDO). CTP is the preferred nucleotide donor, but it can partially be replaced with UTP. Activates KDO during the biosynthesis of rhamnogalacturonan II (RG-II), a structurally complex pectic polysaccharide of the primary cell wall. RG-II is essential for the cell wall integrity of rapidly growing tissues and pollen tube growth and elongation.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32245
Sequence Length: 290
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Mitochondrion outer membrane
EC: 2.7.7.38
|
A8IGU8 | MAFSASDVLVLIPARLAASRLPGKPLADVGGRPMIVEVARRAVAAGIGRVAVATDAVEIADAVRAAGFEAVMTRADHPSGSDRIFEALGVLDPDGAVQVVVNVQGDLPTIAPETIRAALVPLEEGPADIATLTAVITEEGERTDPNVVKVVGTPIGENRLRALYFTRATAPTGEGPLYHHIGLYAYRRAALERFVSLPPSPLEKRERLEQLRALEAGMRIDVAVVDAVPLGVDTPEHLERARALLASNDN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 26436
Sequence Length: 250
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q8A9S0 | MKFLGIIPARYASTRFPAKPLAMLGGKTVIQRVYEQVAGILDDAYVATDDERIEAAVKAFGGKVVMTSIDHKSGTDRCYEACTKIGGDFDVVVNIQGDEPFIQPSQLNAVKACFEDPTTQIATLVKPFTADEPFAVLENVNSPKVVLNKNWNALYFSRSIIPFQRNADKEDWLKGHTYYKHIGLYAYRTEVLKEITALPQSSLELAESLEQLRWLENGYKIKVGISDVETIGIDTPQDLKHAEEFLKNRS | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27994
Sequence Length: 250
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
Q6G4U6 | MALEPIILIPARIGSTRLPQKALAEIAGKPMIVHVAEQAKKAAFGRIIVATDHNNIAKVVTAYGHECIITCRDHKSGSDRIYEALTHIDPERRYNVILNVQGDLPTITPHEIISALRPLENSLTDIATLGAKIVEENEKTDPNIVKIIGTPLSHNRFRALYFTRATAPYGDGPLYHHIGIYAYRREALEKFVALKPSPLEQREKLEQLRALEHNMRIDVEIVDTIPLGVDTQRDLERVRKILA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27280
Sequence Length: 243
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
Q6MPP1 | MKIVGVIPARFGSTRFPGKPLVNLKGRPLIQWTVEGAKKSKLLSEVIVATDHEGIKAAAEAVGVKVVMTDSDLPTGSDRINAAIKDVACDVVVNIQGDEPLVTGELIDRLAQVFVDDPKMDMATLAHPISAEELQSMNSVKVVVNCRDEALYFSRYPMPYSRMSAQEAGSMDGCLKHIGMYAYSRNFLKQFCEAPPALIEKAESLEQLRALYLGAKIKVIRVKEASVGVDTPEDLARLEKLLSSQGM | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 26921
Sequence Length: 247
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
Q492T2 | MNFVVIIPVRFFSTRFPGKALADINGKPMIVRVMENALDSGANKVIIATDSSCIARVIESEQSESEVCLTRSTHQSGTERLAEVAINYKFSDDQIIVHLQGDEPLLSSTMIRQVASILCSMSSTISMATLATPLSSFKEARDDNVVKVVINMNSNALYFSRSMIPWNTGDFVNHLDSKFSKTLLRHIGIYAYRVKFLRRYIAWTKSPLEQIEHLEQLRVLWHGEAIHVSVIDDVFNISVDTPESLSRVNTVFKKNKYATVHN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 29527
Sequence Length: 262
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
Q129C7 | MRFTVLIPARLASTRLPNKPLADMGGAPMVVRVAQRAMQSTAARTVVATDSTDIIDKCAAFGVAAVLTRADHPSGSDRLAEACTALGLADDDIVVNVQGDEPLIDPALIDAVARLLNERPDCAMSTAAHSIDQMADLLNPNVVKVVLDARQTALYFSRSPIPAARDFAGKPWWEDGEKGCKLPKPLRHVGIYGYRVGFLRQFPTLPQAPLEQLESLEQLRALWHGHRIAVHITDEAPGPGVDTPEDLARARQFFP | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27656
Sequence Length: 255
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
B2RLM4 | MNTEVIAIIPARFASSRFPGKPLADMLGKSMIQRVHERIAGVVPRAVVATDDERIRQAVEDFGGEVVMTSPECSSGTERCREAFDKVGRGEKIVLNLQGDEPFIQKEQIDLLISAFDKPETDIATLAEVFSSDASFERLNNPNSPKIVLDHGGYALYFSRSVIPYLRGVQPDSWCRRHTYYKHIGIYAFRPTVLRKITSLPQSTAEQAESLEQLRWLEYGYRIRVLQTQQSTIGIDTPEDMDKAIAYLRSQGME | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28660
Sequence Length: 254
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
Q9HZM5 | MTQAFTVVIPARYASTRLPGKPLQDIAGQPMIQRVWNQARKSAASRVVVATDDERILAACQGFGAEALLTRAEHNSGTDRLEEVASRLGLASDAIVVNVQGDEPLIPPALIDQVAANLAAHPEAAIATLAEPIHEVSALFNPNVVKVATDIDGLALTFSRAPLPWARDAFARDRDSLPEGVPYRRHIGIYAYRVGFLADFVAWGPCWLENAESLEQLRALWHGVRIHVADARENMLPGVDTPEDLERVRRVLGG | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27646
Sequence Length: 254
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
Q4KFT3 | MSSAFTVVIPARYASTRLPGKPLQLIAGKPMIQWVWEQARKSSAERVVVATDDQRIVEACQGFGAEALLTREDHNSGTDRLAEVAAQLGLAADAIVVNVQGDEPLIPPSVIDQVAANLAAHTEARMATLAEPIEDVQTLFNPNVVKVVSDLNGLALTFSRATLPWARDAFAQSREQLPEGVPYRRHIGIYAYRAGFLHDFVSWGPCWLENTESLEQLRALWHGVRIHVADALEAPPTGVDTAEDLERVRRLLEA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27862
Sequence Length: 254
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
Q46222 | MMLRGVHRIFKCFYDVVLVCAFVIALPKLLYKMLVYGKYKKSLAVRFGLKKPHVPGEGPLVWFHGASVGEVRLLLPVLEKFCEEFPGWRCLVTSCTELGVQVASQVFIPMGATVSILPLDFSIIIKSVVAKLRPSLVVFSEGDCWLNFIEEAKRIGATTLVINGRISIDSSKRFKFLKRLGKNYFSPVDGFLLQDEVQKQRFLSLGIPEHKLQVTGNIKTYVAAQTALHLERETWRDRLRLPTDSKLVILGSMHRSDAGKWLPVVQKLIKEGVSVLWVPRHVEKTKDVEESLHRLHIPYGLWSRGANFSYVPVVVVDEIGLLKQLYVAGDLAFVGGTFDPKIGGHNLLEPLQCEVPLIFGPHITSQSELAQRLLLSGAGLCLDEIEPIIDTVSFLLNNQEVREAYVQKGKVFVKAETASFDRTWRALKSYIPLYKNS | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of three 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the trisaccharide alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 49187
Sequence Length: 437
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.99.12
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P0CE14 | MIRRWLTSRLYDAFLVCAFFVSAPRIFYKVFFHGKYIDSWKIRFGVQKPFVKGEGPLVWFHGASVGEVSLLAPLLNRWREEFPEWRFVVTTCSEAGVHTARRLYESLGATVFVLPLDLSCIIKSVVRKLAPDIVIFSEGDCWLHFLTESKRLGAKAFLINGKLSEHSCKRFSFLKRLGRNYFAPLDLLILQDELYKQRFMQIGISSDKIHVTGNMKTFIESSLATNRRDFWRAKLQISSQDRLIVLGSMHPKDVEVWAEVVSHFHNSSTKILWVPRHLEKLKEHAKLLEKAGILFGLWSQGASFRQYNSLIMDAMGVLKDIYSAADIAFVGGTFDPSVGGHNLLEPLQKEVPLMFGPYIYSQSVLAEKLREKEAGLSVNKETLLDVVTDLLQNEKNRQAYIEKGKSFLKQEENSFQQTWEILKSQITCMKI | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of three 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the trisaccharide alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 49497
Sequence Length: 431
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.99.12
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P0AC77 | MLELLYTALLYLIQPLIWIRLWVRGRKAPAYRKRWGERYGFYRHPLKPGGIMLHSVSVGETLAAIPLVRALRHRYPDLPITVTTMTPTGSERVQSAFGKDVQHVYLPYDLPDALNRFLNKVDPKLVLIMETELWPNLIAALHKRKIPLVIANARLSARSAAGYAKLGKFVRRLLRRITLIAAQNEEDGARFVALGAKNNQVTVTGSLKFDISVTPQLAAKAVTLRRQWAPHRPVWIATSTHEGEESVVIAAHQALLQQFPNLLLILVPRHPERFPDAINLVRQAGLSYITRSSGEVPSTSTQVVVGDTMGELMLLYGIADLAFVGGSLVERGGHNPLEAAAHAIPVLMGPHTFNFKDICARLEQASGLITVTDATTLAKEVSSLLTDADYRSFYGRHAVEVLYQNQGALQRLLQLLEPYLPPKTH | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47291
Sequence Length: 425
Pathway: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step 1/4.
Subcellular Location: Cell inner membrane
EC: 2.4.99.12
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P44806 | MWRFFYTSLLLICQPLILCFIGLLSVKSPRYRQRLAERYGFYGNASCPPPQGIFIHAASVGEVIAATPLVRQLQQDYPHLSITFTTFTPTGSERVKATFGDSVFHYYLPLDLPFSIHRFINFVQPKLCIVMETELWPNLIHQLFLRNIPFVIANARLSARSAHRYGKIKAHLQTMWSQISLIAAQDNISGKRYATLGYPKEKLNITGNIKYDLNTNDELLRKIDSLRTLWKQDRPIWIAASTHNGEDEIILKSHRALLAKYPNLLLLLVPRHPERFNVVADLLKKEKFQFIRRSTNELPNENTQVILGDSMGELMLMYGISDIAFVGGSLVKHGGHNPLEPLAFKMPVITGKHTFNFPEIFRMLVEVQGVLEVNSTADALERAVEALLNSKESRERLGNAGYEVLMENRGALQRLLDLLKPYLERNV | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the acceptor lipid.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 48743
Sequence Length: 427
Domain: The N-terminal half of KdtA, especially the first 30 amino acid residues, is responsible for determining the number of Kdo residues that are transferred to lipid IVA.
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.99.12
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Q9ZE58 | MMLLYYTLSFILLPVYFIIIFIRLLIGKEDIRRIQERFAIGKQRQNSALDFIQMSVNKEGFTDHKTTSYVDMHRNASLMYKLSLERSYAHSLVWIHAASVGEVMTALTLIHNISKLAPNVRFLITSWTNASAKILSTKLPKIATHQFLPIDNVIFTRKFLRNWQPDLGIFIESELWPCTINEGAKYCKLLLINARISNKSFKAWLKRKRFFQLIIKNFSKIIVQSERDLQKFNALGISDAMNLGNIKFANEKLLVNQEKLSKLILHLDNRRVLVFASTHPEDEEVILPIINNLKEQFIDCYIILIPRHPERIKSIINNCKLHHLSATAKSQNDLPVLNNDLYIVDRFGEMGLFFSVATISFIGGSFKQGGHNILEAAYFSNCIIFGPDMSKNTDIAKGILQNNAAIQIKNGKDLLNTLTSLLNANNALKLKTYRENALKFVENNQKKILDEYLQIIKQFLP | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 52976
Sequence Length: 461
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.99.12
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P50842 | MGYLHDAFSLKGKTALVTGPGTGIGQGIAKALAGAGADIIGTSHTSSLSETQQLVEQEGRIFTSFTLDMSKPEAIKDSAAELFENRQIDILVNNAGIIHREKAEDFPEENWQHVLNVNLNSLFILTQLAGRHMLKRGHGKIINIASLLSFQGGILVPAYTASKHAVAGLTKSFANEWAASGIQVNAIAPGYISTANTKPIRDDEKRNEDILKRIPAGRWGQADDIGGTAVFLASRASDYVNGHILAVDGGWLSR | Function: Catalyzes the reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH.
Catalytic Activity: 2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + NADH
Sequence Mass (Da): 27186
Sequence Length: 254
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 5/5.
EC: 1.1.1.127
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P37769 | MILSAFSLEGKVAVVTGCDTGLGQGMALGLAQAGCDIVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLDRAVAEFGHIDILVNNAGLIRREDALEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGRWGLPSDLMGPIVFLASSASDYVNGYTIAVDGGWLAR | Function: Catalyzes the reversible reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH (Ref.4). To a lesser extent, can also reduce 5-keto-D-gluconate and oxidize D-gluconate and 1,2-propanediol . Together with KduI, seems to play a role in the catabolism of hexuronates under osmotic stress conditions, substituting for the regular hexuronate degrading enzymes UxaABC and UxuAB whose expression is repressed in these conditions . In vitro, also exhibits NADH-dependent 20-ketosteroid reductase activity against eukaryotic steroid hormone 11-deoxycorticosterone (11-DOC), which is converted into the product 4-pregnen-20,21-diol-3-one. In addition to 11-DOC, five other C21 steroid compounds (11-deoxycortisol, cortisol, corticosterone, cortisone, and 21-hydroxypregnenolone) are reduced by KduD, but steroids lacking the hydroxyl group at C21 position, such as pregnenolone, testosterone propionate, cortisone acetate, or progesterone, cannot be used as substrate .
Catalytic Activity: 2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + NADH
Sequence Mass (Da): 27070
Sequence Length: 253
EC: 1.1.1.127
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Q8A2S4 | MKTNYEIRYAAHPEDAKSYDTARIRRDFLIEKIFVPNEVNMVYSMYDRMVVGGALPVGEVLTLEAIDPLKAPFFLTRREMGIYNVGGPGVVKAGDAVFELDYKEALYLGSGDRVVTFESKDASNPAKFYFNSLTAHRNYPDRKVTKADAVVAEMGSLEGSNHRNINKMLVNQVLPTCQLQMGMTELAPGSVWNTMPAHVHSRRMEAYFYFEIPEEHAICHFMGEVDETRHVWMKGDQAVLSPEWSIHSAAATHNYTFIWGMGGENLDYGDQDFSLITDLK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
Catalytic Activity: 5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-hexodiulosonate
Sequence Mass (Da): 31666
Sequence Length: 280
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 4/5.
EC: 5.3.1.17
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Q9X756 | MDSHTLIQALIYLGAAALIVPIASVLGLGSVLGYLIAGCIIGPWALRLVNDAEAILHFAEIGVVLMLVAMGLELDPQRLWKLRASVFDGGALQMVACGVLIGLFCMLLGLRWQVAELIGMTLALSSTAIAMQAMNERNLTVSQMGRSAFAVLLFQDIAAIPLVAMIPLLAASGGATSLMAFALSALKVAAALALVVVLGRYLTRPLLRFVARSGLREVFSAVACSWSSALGLLLEEVGLSMAMGAFLAGVLLASSEYRHALENDIEPVKGLLLGLFFIGVGMSIDFAPWSPNPLRIVILLVGFPAIKMLMLWLIAQPLGVPRAQHRWFAVLLGQGSEFAFVVFGPARMADVLDGEWPKALTLAVALSMATTPILLVLLTRLEKSSSGQARDADEIDEEQPRVIVAGFGRFGQIAGRLLLSSGVKMVILDHDPDHVDTLRKFDMKVFYGDATRVDLLESAGAEKAEVLINAIDDPHVSLELVARVKEHFPHLQIISRARDVDHYIQLRQAGVEAPERETFEAALKSGRMTLEALGLGAYEARERPDLFRRFNLQMVEEMVAMAENDPRRGVAVFKRTSDMLTGIINEDRHHLSLVQRHGWQGTEEGRHTGDIADEPENKPSA | Function: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67353
Sequence Length: 621
Subcellular Location: Cell inner membrane
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Q8ZRW2 | MDSHTLLQALIYLGSAALIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDAESILHFAEIGVVLMLFVIGLELDPQRLWKLRASVFGGGALQMGVCGGLIGLFCMFLGLRWQVAELIGMTLALSSTAIAMQAMNERNLTVSQVGRSAFAVLLFQDIAAIPLVAMIPLLAASGASTTLGAFALSALKVAGALALVVLLGRYVTRPALRFVARSGLREVFSAVALFLVFGFGLLLEEVGLSMAMGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIGVGMSIDFGTLVENPLRILLLLAGFLAIKIVMLWLVARPLGVPAKQRRWFAVLLGQGSEFAFVVFGAAQMADVLEPEWAKALTLAVALSMAATPIFLVLLTRMEKTATGEAREADEIDEEQPRVIVAGFGRFGQIAGRLLLSSGVKMVVLDHDPDHIETLRKFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTNLQLSELVKSHFPHLQIIARARDVDHYIRLRQAGVAMPERETFEGALKSGRQALEALGLGRYEARERADLFRHFNTRMVEEMAKGENDPLSRAAAYKRTSAMLSEIITEDREHLSLIQRHGWQGTAEGKHSGEVADEPEVKPSI | Function: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67054
Sequence Length: 620
Subcellular Location: Cell inner membrane
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E7R7R2 | MSRYFLLACTLALQCVAASQEDYIVKDLPGLSNIPAVVRPVMHAGHLEIDEEHNTELFFWRFQNPKNNGTHQTLHRNELIVWLNGGPGCSSMDGAMMETGPLRVSDKLEVELNPGSWTQVADILFVDQPAGTGFSYTDSYDTELKQAAQHFWQFLKTYYQLFPEDRTKKLYLAGESYAGQYIPYFAKEIIENNSLNISLEGLLIGNGWIDPDIQSLSYVPFSLEAGFLDRQSPSMAQVLKQHEKCQQAIDDPSNHDFEKVECVKIFHSILAASRDETKPAKEQCVNMYDYRKHDYFPACGSNWPEGLPTVTKFLNLDAVQKALNLKSAKRWHECDGKVEFFFQPEHSVKSFDLLPKLLEKMKIALFAGDKDIICNHKSIEMVIEKLQITPGQFGFTNSRKSGWIYDGQEVGEVETQSNLTYIKVFNSSHMVPYDLPEVSRGLFDIITNSIEKRSTDIVTPVYDSRGNYKFVEEKQDTDQNEEEEKEKPPKHHHSLTFYVAEVAILAVLAYLLYSFYKSFAKSRKSAFLSLSSKKKKKQVHWFDESDIGMDQEAGEADHKPKSMLESVFNKLGYGGQYDTVQDGRDIEMAPVEEHEDQFIIQSDEEEFGHR | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 69724
Sequence Length: 610
Subcellular Location: Golgi apparatus
EC: 3.4.16.6
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B6H7A4 | MLLSALSLLLSPLVSASSAADYYVRSLPGAPEGPFLKMHAGHIEVDPDTNGNLFFWHFQNRHIANRQRTVIWLNGGPGCSSMDGAFMEVGPYRLQDDHTLKYNEGRWDEFANLLFVDNPVGTGFSYANTNSYLHELDEMAAHFVIFLEKFFELFPEYANDDLYIAGESYAGQHIPYIAKAIQDRNKGITENGGTKWPLKGLLIGNGWISPADQYPSYFKFIEREGLAKPGTSLHHNINALNEVCLSKLETPGAKNKLDVGACELVLQQFLDLTTEDHQCYNMYDVRLKDEAKSCGMNWPPDLKNIEPYLQRPDVVKALNINPAKKSGWTECAGMVHMAFTAKNSIPSVHLLPGLIESGINVLLFSGDKDLICNHIGTETLIHNMDWKGGTGFETSPGVWAPRHDWSFEGEPAGIYQSARNLTYVLFYNSSHMVPFDNPRQSRDMLDRFMKVDIASIGGQPSDSRIDGEKLPQTAVGGQANSTAAEQNEKERLKQTEMHAYTKSGEAVLIIVIIGVIAWGFFIWRSRRTRRGYKGVSNNDMSDSTSVLSRFQNKHSGRDVEAGDFDEAELDQLHSPSIEREDYAVGEASDDDDHIISHPETGGNRQSS | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 67721
Sequence Length: 607
Subcellular Location: Golgi apparatus
EC: 3.4.16.6
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Q0USX0 | MLLTHTSSRWRTAAVCALAATASWLPSVQAAEKTQADYFVSSLPGAPEGPLLKMHAGHIEVDAEHNSNLFFWHYENRHIADRQRTVLWLNGGPGCSSMDGAMMEIGPYRVKHGGHLEYNNGSWDEFANMLFIDQPVGTGFSYVNTDSYLTDLDQMAEHMMIFLEKWFKLFPEYENDDLYIAGESYAGQHIPYIARAILNRNKNQNTDPKPWNLKGLLIGNGWISPADQYLAYLPFAYQNGMIQADSDSAKRVEQQQSICIQKLQDGGHDKVDTSECEQIMVAILEETKDRKADRMNQCLNMYDIRLRDDSSCGMNWPPDLTDVTPYLRRPDVIKALHINSDKKTGWSECNGAVSGHFRAKNSVPTVKFLPELLTEVPILLFSGDKDFICNHVGTEAMIENMSWNGGKGWEVSPGVWAPKQDWTFEGEPAGTYQEVRNLTYVVFYNSSHMVPFDYPKRTRDMLDRFMNVDISAIGGDPADSRIDGEKGPLTSVGDHPNSTKAEEDKAQQLKEAEWKAYYRSGEVVLVILIIVACLWGAFLWRTRRSTSLYKGVDGDEGRESLLTGMGLDNFRRGARRHDVEAADFDERELDDLDDAPKKPANGYSNVNSEKERQPHNDSTFSLGADSDDEAEGSERGRRKEHS | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72415
Sequence Length: 642
Subcellular Location: Golgi apparatus
EC: 3.4.16.6
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D0MVS1 | MVTRHVLAAALAGSMTSAQRLHPTSQRASDDLIQNLPGLDPAAKVTQHAGRIALHDNDKNKMFYWHFQAAQDPEKAPLVIWLNGGPGCTSMQGLFLGNSPFTLKDDSTIGKNEHSWHEFANLLFVDQPIGTGMSYTKGNDYRLDEETIAQDFYEFLTKFLQRHNKYLSDGDDGVSNSRAVYMFGESHAGRWIPEFSDHIMKQNNDPKNQIKINLDGVGIGNGWVHPRIQYEYSDYAHGLGLLTFGQVRSLKASYAECLAALDAGTYYSRSCLDNMDSITGSVKPGNGGNSLNFYDVRQYLRNVGSYPSGQSNIAKYMNKMEVRKAVHGNEDKNFRFDLCSNGVFRALSKFDGVSTLDKVESLLQQGLRMIFYNGQWDMMCNHYGTEKLLLNLNWNGSDAYQQADKYTWRVQGRKEPAGFAQQGGNLTYLVVTGAGHMVPMDVPDVAADILRRFVNRLEFNDKVQTVVTTRLNATDMEVSFCYSPSVSADPDTSLSTRDQTGANSSQVHIGIAWLWVALVIAVVSSVLAVCVTIVCIRNKRNGKQEHEMITQVSDDEEVNQIEDESEEGFSDEDVGVHVLVSNVSQRATSPRSRVTEV | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 66514
Sequence Length: 597
Subcellular Location: Golgi apparatus
EC: 3.4.16.6
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E3L8A5 | MSSFQSATTRQGLHRRNMNSETPQSEFIQRLRRSPPSESSSSTPSSSTTTSSTTTTSNTSGKKKKTAPSASDFYVPSLPGQPKDSQLILYAGHLSFSPPDTTIEPEKDSYGFFFLNKARHIANRPVLLVWLNGGPGCSSFDGSLMEVGPLRMVLKGDGTLKEVDAAWNEYANMLFIDQPTGTGYSYGPKPNYVHELDVSSANLVNLLARFFKIFPEYQQMDLYICGESFAGQYIPYLAQAILDTNIISAPLKGIMIGNGWIDPINQYLAYPEFAFKVGLVNPSSKAADLVNEELKKCTEWIDSNSTTPIHIEACEGILSAITDSTVQTVNSQKMCLNMYDVRLVDSYPACGLTWPPDLADITPYLSRTDVKQALHAQDHAADWVECEAKVGNNFWAKTSQPSVTLFPKLLDKIKILLFSGDQDLICCHTGTERMIDHLTWAGHQGWTSQAINQPWKVNGSYAGLWKEERNLTYVLVANASHMAPYDVPYVTQDMLVRFLGIDVMTAAGPAAQITSRIGEETATKVNRVVMNETKLGQEGSGTTGLAMTSGPVHDENYYNASSAMLFLTLVGLVVGLIFFVRRRLRRDGHGDFAHHPSDETEIILKNHHHHHLSPDSSLPRSARDRQFQPVPTDDLDDHHLHPNLPSNNTSYQDLPR | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72697
Sequence Length: 656
Subcellular Location: Golgi apparatus
EC: 3.4.16.6
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B6K7U7 | MSLSFLLRVAGLFFLQFNSAQAKSQVHEQWHVSSIPNVPAGYTGSLHSGYLNLTDKLEGDLFFTLYGSENEVHQNRTIIWLNGGPGCSSEDGSMLELGPLRLTNDSLVYYNAASWVRLGNVLFVDQPMGTGFSFADTRDAILNDNEKMSNDFAYFLQEFVKAFPEYATDTWYIAGESFAGQYIPAIAKKVIDSDIVNLSGIAIGNGWIEPASHYLTYLDYLVERGLLERGSALFEALTAVQAKCLMSLEQSASGMLEDENSCDKYLFDILFSVSDKSGEFCFNMYDVTLTSPYPSCGMEWPLELPALTDFLSSPDVMKALHVASDKVSRWEECSSLVSNFYADTNVFRTRFTIAELLEEIPVMLFYGENDFLCNYVSGEFLISNLEWSGKRGFENASNADWYPRYSEANTLEYGQYAAAAGIIHSERNLTYATIRNSSHMVPYDHPYEMLALVSAFFDNDFSQILMLPDPVTIVPNHSFLSIFLWVMAGILAFSAIGAICYYSYRHIRSRYDSYTPIQEESA | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58658
Sequence Length: 522
Subcellular Location: Golgi apparatus
EC: 3.4.16.6
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O60123 | MISKLLKIVLLTAGVIGNTLADSRIHEQYLVKAFPNEPVDYEGRMHAGHLNQTDQLDGDLFFWMFESVKPEYEHRSILWLNGGPGCSSEDGSLMEVGPFRLDDNNTFQLNPGRWDELGNLLFVDQPLGTGYSYSLAKDFQSNNEKMANDFSIFFEKFLEEFPERANDEWFIAGESFAGQYIPHIAAKLKEKNLVNLGGLAIGNGWINPLSHYETYLNYLVEKGMVDFESELGQYLHHSWAECLLAFDKIGSGSGDLSKCESFLGDILYMVSKEPGKACMNMYDISLESTYPTCGMDWPYDLSYLTEFLSTREAMTSLNVNLEKVHDWEECNDDVALQYAREGIESSSKLIQDLVSTVPILLFYGENDFLCNYLSGEKLTRSLEWNGAVGFQNQSAQPFYLPGYSDQPSGSYVSSRNLTFARIVEASHMVPYDHPNEMKTLITAFFNNDFASLPSVPKPSPDLGNGNYKWLYLGLIPVALTIIILFSIYLCRRFGLFGLSKQRYQPISPTP | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 57644
Sequence Length: 510
Subcellular Location: Golgi apparatus
EC: 3.4.16.6
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A7EYY7 | MRSLTTKTSSALLTVWGLLSVSLMPSVGQADKTAGDYFVHSLPGAPAGPLLKMHAGHIEVTPEHHGNIFFWHFQNRHIANKQRTVIWLNGGPGCSSEDGALMEIGPYRVKDGSNGPKLEYNPGSWDEFANVMFVDNPVGTGFSFVDSDSYIHDLPEMADQFVQFLEKWFALFPEYEHDDLYLAGESYAGQHIPYITKAILERNKKPDAKHKWPVKGMLIGNGWISPVEQYMSYLPFAYEKGLVKKDSEKAKKLESQQAICTKMLNENGGRDKVDNSQCEQILQEILSTTQSKGSDGNMQCYNMYDVRLKDSYPSCGMNWPPDLVNVTPYLRRSDVVAALHISPEKRTGWTECNGAVGSAFRAANSKPSIQILPELLAEVPTILFSGAEDLICNHIGTEELISNMEWNGGKGFELGSGTWAPRRDWEFEGEPAGFWQEARNLTYVLFYNSSHMVPFDYARRTRDMLDRFMKVDIASIGGAPTDSRIDGEKGLETSVGGHPNSTAAAEAEEERLEAAKWNAYYKSGEIVLVIVVIAASAWGYYIWRERRQRAGYAGIFGGDTPMALAGARSGSRGAAGLEDFRNKRNARDVEAADFDESELDELHVRSPTDDMDRDRYSVGSASDDESIGKRNGNGKGKEKSYS | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 71339
Sequence Length: 642
Subcellular Location: Golgi apparatus
EC: 3.4.16.6
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Q9PNB8 | MKLQGFVLLISGPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLKHTQNALDNGKIVVFDIDVQGFKIARKKMADKIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSEYDYLIINDELKQSYEALRAILIAHKFRTKGQNLGQIQNIWNEGE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24025
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q3AC14 | MHKGMLVVVSGPSGAGKGTICQEIRKRNPNLFYSISATTREKRVGEIDGVHYYFIDRQQFEKMIANDEFLEWADVYGNYYGTPKKPVFEALARGQDVILEIDIKGARQVKKTYPEGVFVFILPPSISILEERLRKRGTDKEEIIVKRMQMAWEEIANCDWYDYLILNDDLETAVNDLEAVLTAEKLKPKRVNYRVLLEGGVLER | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23494
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q9A7N9 | MNKSHHPHRGLLLMVVAPSGVGKTSLTRRLVSDHGDLHLSISATTRDPRPGEHDGRDYHFVSRDKFQGMLAEDAFLEWAEVYGNFYGSPKAPIMDALSRGESVLFDIDFQGAMKVHKQAGADSVLVYILPPSLAEMSRRLHTRSQDSEEVIHRRLSRAKDEVAAWEQFDYVILNDDFDRAYADLAHIYHAERLKRARNPWIGDLVSDLLKEEI | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24219
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q3J2A5 | MARRGLLLILSSPSGAGKSTLSKRLTAWDPSIRFSVSATTRAPRPGEVDGRDYYFRTRDEFIAAVEAGEMLEHAEVFGNFYGSPKAPVEKALEQGHDTLFDIDWQGGQQIRNSSLGRDVVSIFVLPPSIGELDRRLRSRAQDSEEVIATRMARSKDEISHWAEYDYVLVNRDLDLAEEQLKMILSAERLRRDRQPDLMDFVRGLNGEFETR | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23948
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q11HG8 | MESASPSATIRRRGVMLVLSSPSGAGKSTIARSLLENDHEFELSVSVTTRPRRPSEIEGVHYHFKTQRDFEMMRDGGDLLEWAEVHGNCYGTPRGPVERAIAGGRDMLFDIDWQGAAQLREKMPDDIVSVFILPPTMKELLARLTRRAEDTPEIIERRLRNAHHEIEQWRDYDYVVINDDLDRAFASVRAIVSAERLRHERRPGLEDFVAGLLAERPE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24890
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q3AQL3 | MAVEPSGKLIVFSAPSGAGKTTIATMVLQRIANLSFSVSATTRKQREGEQDGVNYYFLDKATFEKKIEQGGFIEHEFFFGNYYGTLLDATESVLASGKNLLLDVDVKGALNVRKLFGERSLLIFIQPPSMEVLIERLQGRGSEDDAALQERLERARFEMSFADQFDTIIVNNNLTAAVDDVEAAIVNFIG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 20968
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q822M8 | MKDKVRVPFSPDHPSCAPKLFTISAPAGAGKTTLVRMLAQEFPDSFQKTLSLTTRAPRPEEVSGIDYWFVSQEEFKQRLDSNNFLEWVLLFGEYYGTSRLEIDEIWKSGKHAVAVIDVEGALSLKSKIPTVTIFISAPSQEELERRLKYRGSEQDSQRQERLQHSLIEQAASNQFEYVIINDDLQKSYEILKSIFIAEEHRNVL | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23398
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q9Z961 | MNKILVDSPFSPDHQKCCPKLFTISAPAGVGKTTLVRMLEQEFSSAFAETISVTTRKPREGEVPGKDYHFVSHEEFQRLLDRQALLEWVFLFGECYGTSMLEIERIWSLGKHAVAVIDIQGALFIRSRMPSVSIFIAPPSQEELERRLASRGSEEGSQRKERLEHSLIELAAANQFDYVIINDDLNQAYRVLKSIFIAEEHRNIL | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23368
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q8KFS5 | MSAEQVLDQGRLIVFSAPSGTGKSTVAKLVMERLGSLEFSVSATTRQMRAGERDGVDYHFLSREEFEKKIAENGFIEHEFFFGNFYGTLLDKTIDAIKAGHNLLFDLDVKGALNLKRIFGDQALLVFLKPPSMEELARRLQARDSESAEALKSRLERAEMELSHAGEFDFVVVNDDLGRTVDAVATRIAEFLPQP | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 21773
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9HTM2 | MSGTLYIVSAPSGAGKTSLVKALLDAAPEVRVSVSHTTRGMRPGEVDGVNYHFTSREEFLAMLERNEFLEHAEVFGNLYGTSQRWVEKTLAEGLDLILEIDWQGAQQVRRLMPEAQSIFILPPSQEALRQRLTNRGQDSDEVIERRMREAVSEMSHYVEYDHLVINDDFAHALDDLKAIFRARQLRQDAQQQRHAELLGRLLA | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23102
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q4K3R4 | MTHSTGTLYIISAPSGAGKSSLVKALTDAKPEIRVSVSHTTRAMRPGEVDGVNYHFVSRETFVKMGEHGDFLERAEVFGNLYGTSQSHLQQTLDAGHDLILEIDWQGAEQVRKLMPQARSIFILPPSLQALHQRLTNRGQDSDEVIDGRMREAVSEMSHYVDYDYLIINDDFAHALGDLKAIFRANQLQQKRQQQRFGKLLAELLG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23121
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q88C87 | MNHSSGTLYIVSAPSGAGKTSLVTALTKDDQQIRVSVSHTTRAMRPGEQHGVNYHFVVHEEFKALIAQGDFLEHAEVFGNFYGTSRSALQQTLDQGYDLILEIDWQGAQQVRKLMPQALSVFILPPSQEALRHRLDGRGQDSEEIIAGRMKEAVSEMVHYDEYDYVIINDDFDTALADLKAVFRSNRLLLKKQQQRHAALLKQMIG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23184
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q4FQY7 | MTGSLFIITAASGTGKTSLVKQLLATTNDLTVSVSHTTRDPRPGEIDGHHYHFTDVDNFVTAISESQFLEHAEVFGNYYGTSEQSVRAQLDAGVDVILEIDWQGALQVKKIFTDAIMIFILPPSIATLRQRLSTRGQDSMEVIEQRLAGAVNEMAQYINFDYVIINDNFEVALTELKAIIVADRQTLKRQQQRYQRTITNLLSNIVDK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23293
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q984S9 | MVPRDLGSRIRRRGLMLVLSSPSGAGKSTIARNLLESDSSLELSVSVTTRPRRGSEIEGVHYHFRTMREFERLRDSDALLEWAEVHGNCYATPREPAELALAQGRDMLFDIDWQGAQQLKEKMRADIVSIFILPPSMKELKARLKRRAEDQEAVIETRLKNARNEIEHWKEYDFVIVNDDLDRAFAEVRGIVVAERLRRDRRPGLFDFVSGLLDEKTV | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 25105
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q7UP92 | MNDPSCSSADETAHPGRLVIISGPSGAGKSTVVKQLMKRCDVPLQLSVSATTREPRPGEIHGQDYFFLSHEEFERRRKLNDFVECKQVFSMGQWYGTLKDQVATGLNAGKWVILEIDVQGAMAVLDDPHYRPVTIFVHPGSMEELERRLRNRGTESESSLTARLETAAAEMQCLSRYQYEIINESVDNAVTEICQILLDQRKTTPCSKN | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23450
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q2IX83 | MKDGAAGSLNGIERRGLMFVLSSPSGAGKTTLSRMLVDEAPGLRMSVSATTRPKRPGEVDGRDYYFVDRPKFDAMVEAGEFLEWANVFDNCYGTPRAPVEAALSAGNDVLFDIDWQGTQQLRSRASNDVVSVFILPPSVQDLEHRLHTRAQDSDEVIRGRMKKAGDEMSHFDAYDYIVVNDNIGVAFESVKAILRAEQLKRERQIGIDAFVREMRRELEK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24616
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q6A8B2 | MDNSVRVRVPATSANLGPGYDCIGLALDLWDEVSVGVLDRPGVMIDVTGEGADTVPHDESHLVMATLRQGLVELGYPHPDAGLHLTAINSIPQSRGLGSSAAAVVSGLALAWGLARPGFPLDRSALLTMAAAIEGHPDNAAPAILGGAQLAWLDGEAVNHIGLTVNPSIVFRVYVPDRLVPTALARQVLPEQVDRVDAVHQVLAASLLVTALTTSPEHLLAATQDWIHQPYRRALMPESAALTDRLRGRGVATVISGAGPTVLALGSRDQLEKVSDVDTAGFVAHDLVLGEGVHFF | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 31006
Sequence Length: 296
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
Q9RRU5 | MSSPARPFTVRAPASSANLGPGFDSLGLSVPLYTTLRVTPQDKAEVVPLGTELADTPADESNYVYRAMTLAAKRAGRTLPPARVEIETEVPLARGLGSSAAALVAGVVAGNELLGRPLDDETVLDVTAREEGHPDNVAPALFGGIVVATLDKLGTHYVRLDPPAHLGVTVLVPDFELSTSKARAVLPREYSRADTVHALSHAALLAAALAQGRLDLLRHAMQDYVHQVWRAPLVPGLSDILEHAHEYGALGAALSGAGPTVLCFHDQRGSTATLHHYLHDVMTKNGLSGRVMDFPIDAAGTVVEHAK | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32390
Sequence Length: 307
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
Q24XU1 | MVRVRIPATSANLGPGFDCLGMALSLYNVVQIEAADSFQIALKGDYTAGIPGDETNLVWQSMCNLWEAIGFEIPTVSLELENNIPPTRGMGSSSAAIVGGLVAANEYAGGVLSKQQILQIANRIEGHPDNVAPALLGGVTLAVTAEASVIARTVHSQPQFMALAIVPDFYLSTEKSRNVLPASISRADAVYNLSRTALLVEALIHENHELLKEGMQDRLHQNQRAGLVPGLGETLQVALDSGAYGSALSGSGPTILALVSSHRAEQVSQAMVDSLAAHGLTAKAYLLSVDSEGAAVI | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 31093
Sequence Length: 297
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
Q21017 | MAAPRRRMGLEKIGLYDVGRAIGKGNFATVRIARHKIAKTKVAIKSIDVSALDRENLIKLEREVKIVKVIDHPHIVKSYEIMRVDNMLYIVSEYCSSGELYETLIEKGRVAENVARKWFSETASAVAYLHSQGIVHRDLKAENILLGKNSNIKIIDFGFSNFQTGDQLLNTWCGSPPYAAPELLLGNSYDGMKADIWSMGVLLYILVAGGFPFPSDSVNKLKRSVLSGLVKIPYWVSVECADFIRKMLVLNPGKRYTIQNVLQHRWMHIRDDVQKNQAAQLLEAIPSSSIEIRQQSTKLNPTIMMFMQQHGKWSEEQIIDAVLGRDFESPIFATYELLADKVKKGTLEGTGEEFPRRGSRGSILSGKANVDEQPLTPTISAHQLAQLNLSSPDCDSDDSSNSDLCDDSPMSSMGPMNHERQFGTPHGLDIIGNRFENRRHTLCASEQLLSPNMMGQFPPPNLLLNNFSMNPPLGFPPMPEGQAAEFPLPSLHPAFATIPIADLSKMLPVPKSERRASAGETLLPTNFDLTQHLANLPAPPISFPTVEEEGKSYLSKYGGKRNTVHCLGNQLGGGIQNPIPRYQRTPYTKAPPAERRSSWASPSLSAQQQNHLEKLFKQALQTNNDMTRLHKEFKGLSHGCAQSQITNEGSSLACPQISITDEYNRQHNIAPSASSFDPVSIFQKNAQEVVFGQRPATAIGFSSTSFSGMSTPEQTTRSIDDRVRSIVCTLPFTEVIDELKASLNILKIPFSESHEMVYEPQVTEMRRLSLPSGVEIGVAVLPPEHKAHVEFAIINNDSPTSEYLCDQLICRLRMIDPSWSSE | Function: Regulates chemoreceptor expression by phosphorylating the hda-4 class II histone deacetylase (HDAC) and inhibiting the gene repression functions of hda-4 and the mef-2 transcription factor, enabling the correct sensing and transduction of food signals. Role in determining body size, the dauer decision and serotonin-mediated egg laying. May modulate the Sma/Mab pathway and regulates development in the later larval stages.
PTM: Autophosphorylated. Elevated cAMP levels appears to act via PKA to directly or indirectly phosphorylate multiple sites on kin-29 and inhibit function.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 91365
Sequence Length: 822
Subcellular Location: Cytoplasm
EC: 2.7.11.1
|
P22209 | MHRRQFFQEYRSPQQQQGHPPRSEYQVLEEIGRGSFGSVRKVIHIPTKKLLVRKDIKYGHMNSKERQQLIAECSILSQLKHENIVEFYNWDFDEQKEVLYLYMEYCSRGDLSQMIKHYKQEHKYIPEKIVWGILAQLLTALYKCHYGVELPTLTTIYDRMKPPVKGKNIVIHRDLKPGNIFLSYDDSDYNINEQVDGHEEVNSNYYRDHRVNSGKRGSPMDYSQVVVKLGDFGLAKSLETSIQFATTYVGTPYYMSPEVLMDQPYSPLSDIWSLGCVIFEMCSLHPPFQAKNYLELQTKIKNGKCDTVPEYYSRGLNAIIHSMIDVNLRTRPSTFELLQDIQIRTARKSLQLERFERKLLDYENELTNIEKILEKQAIEYERELSQLKEQFTQAVEERAREVISGKKVGKVPESINGYYGKKFAKPAYHWQTRYR | Function: This protein is probably a serine/threonine protein kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 51203
Sequence Length: 435
EC: 2.7.11.1
|
Q01919 | MASVPKRHTYGGNVVTDRDRHSLQRNNEILHPIHKNQRKHATFGPYIIGSTLGEGEFGKVKLGWTKASSSNEVPKQVAIKLIRRDTIKKDADKEIKIYREINALKHLTHPNIIYLEEVLQNSKYIGIVLEFVSGGEFYKYIQRKRRLKESSACRLFAQLISGVNYMHYKGLVHRDLKLENLLLDKHENLVITDFGFVNEFFEDNELMKTSCGSPCYAAPELVVSTKAYEARKADVWSCGVILYAMLAGYLPWDDDHENPTGDDIARLYKYITQTPLKFPEYITPIPRDLLRRILVPNPRRRINLQTIKRHVWLKPHEAFLSIQPNYWDEHLQKERPKPPNKGDVGRHSTYSSSASSYSKSRDRNSLIIESTLEQHRMSPQLATSRPASPTFSTGSKVVLNDTKNDMKESNINGERTSASCRYTRDSKGNGQTQIEQVSARHSSRGNKHTSVAGLVTIPGSPTTARTRNAPSSKLTEHVKDSSQTSFTQEEFHRIGNYHVPRSRPRPTSYYPGLSRNTADNSLADIPVNKLGSNGRLTDAKDPVPLNAIHDTNKATISNNSIMLLSEGPAAKTSPVDYHYAIGDLNHGDKPITEVIDKINKDLTHKAAENGFPRESIDPESTSTILVTKEPTNSTDEDHVESQLENVGHSSNKSDASSDKDSKKIYEKKRFSFMSLYSSLNGSRSTVESRTSKGNAPPVSSRNPSGQSNRSNIKITQQQPRNLSDRVPNPDKKINDNRIRDNAPSYAESENPGRSVRASVMVSTLREENRSELSNEGNNVEAQTSTARKVLNFFKRRSMRV | Function: This protein is probably a serine/threonine protein kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 90088
Sequence Length: 800
EC: 2.7.11.1
|
P25341 | MTQQEYRSPSQRLSKGRSMSLPKIFARNLRSLQNNAPPGKNINVNCLNVNSCSLSASPSSQINMACNGNKQDLPIPFPLHVECNDSWSSSKLNKFKSMFNHNRSKSSGTTDASTSEKGTHKREPRSTIHTELLQSSIIGEPNVHSTTSSTLIPNEAICSTPNEISGSSSPDAELFTFDMPTDPSSFHTPSSPSYIAKDSRNLSNGSLNDINENEELQNFHRKISENGSASPLANLSLSNSPIDSPRKNSETRKDQIPMNITPRLRRAASEPFNTAKDGLMREDYIALKQPPSLGDIVEPRRSRRLRTKSFGNKFQDITVEPQSFEKIRLLGQGDVGKVYLVRERDTNQIFALKVLNKHEMIKRKKIKRVLTEQEILATSDHPFIVTLYHSFQTKDYLYLCMEYCMGGEFFRALQTRKSKCIAEEDAKFYASEVVAALEYLHLLGFIYRDLKPENILLHQSGHVMLSDFDLSIQATGSKKPTMKDSTYLDTKICSDGFRTNSFVGTEEYLAPEVIRGNGHTAAVDWWTLGILIYEMLFGCTPFKGDNSNETFSNILTKDVKFPHDKEVSKNCKDLIKKLLNKNEAKRLGSKSGAADIKRHPFFKKVQWSFLRNQDPPLIPALNDNGCELPFILSCNKHPKRNSVSEQETKMFCEKVANDDEIDEADPFHDFNSMSLTKKDHNILTYSENYTYGKILYKATCTRPRHNSSHRSFFKDIIPEL | Function: Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 81462
Sequence Length: 720
EC: 2.7.11.1
|
P16497 | MEQDTQHVKPLQTKTDIHAVLASNGRIIYISANSKLHLGYLQGEMIGSFLKTFLHEEDQFLVESYFYNEHHLMPCTFRFIKKDHTIVWVEAAVEIVTTRAERTEREIILKMKVLEEETGHQSLNCEKHEIEPASPESTTYITDDYERLVENLPSPLCISVKGKIVYVNSAMLSMLGAKSKDAIIGKSSYEFIEEEYHDIVKNRIIRMQKGMEVGMIEQTWKRLDGTPVHLEVKASPTVYKNQQAELLLLIDISSRKKFQTILQKSRERYQLLIQNSIDTIAVIHNGKWVFMNESGISLFEAATYEDLIGKNIYDQLHPCDHEDVKERIQNIAEQKTESEIVKQSWFTFQNRVIYTEMVCIPTTFFGEAAVQVILRDISERKQTEELMLKSEKLSIAGQLAAGIAHEIRNPLTAIKGFLQLMKPTMEGNEHYFDIVFSELSRIELILSELLMLAKPQQNAVKEYLNLKKLIGEVSALLETQANLNGIFIRTSYEKDSIYINGDQNQLKQVFINLIKNAVESMPDGGTVDIIITEDEHSVHVTVKDEGEGIPEKVLNRIGEPFLTTKEKGTGLGLMVTFNIIENHQGVIHVDSHPEKGTAFKISFPKK | Function: Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. It also autophosphorylates in the presence of ATP.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 69171
Sequence Length: 606
EC: 2.7.13.3
|
Q84VQ1 | MGNANGKDEDAAAGSGGADVTSSSARSNGGDPSARSRHRRPSSDSMSSSPPGSPARSPSPFLFAPQVPVAPLQRANAPPPNNIQWNQSQRVFDNPPEQGIPTIITWNQGGNDVAVEGSWDNWRSRKKLQKSGKDHSILFVLPSGIYHYKVIVDGESKYIPDLPFVADEVGNVCNILDVHNFVPENPESIVEFEAPPSPDHSYGQTLPAAEDYAKEPLAVPPQLHLTLLGTTEETAIATKPQHVVLNHVFIEQGWTPQSIVALGLTHRFESKYITVVLYKPLTR | Function: Regulatory subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and in assimilation of nitrogen by phosphorylating nitrate reductase.
PTM: Sumoylated by SIZ1.
Sequence Mass (Da): 30724
Sequence Length: 283
Domain: Kinase-interacting sequence (KIS) is specific for the alpha catalytic subunit interaction and Association with SNF1 Complex (ASC) is specific for the gamma non-catalytic regulatory subunit interaction.
Subcellular Location: Cell membrane
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Q9SCY5 | MGNVNAREEANSNNASAVEDEDAEICSREAMSAASDGNHVAPPELMGQSPPHSPRATQSPLMFAPQVPVLPLQRPDEIHIPNPSWMQSPSSLYEEASNEQGIPTMITWCHGGKEIAVEGSWDNWKTRSRLQRSGKDFTIMKVLPSGVYEYRFIVDGQWRHAPELPLARDDAGNTFNILDLQDYVPEDIQSISGFEPPQSPENSYSNLLLGAEDYSKEPPVVPPHLQMTLLNLPAANPDIPSPLPRPQHVILNHLYMQKGKSGPSVVALGSTHRFLAKYVTVVLYKSLQR | Function: Regulatory subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and in assimilation of nitrogen by phosphorylating nitrate reductase.
PTM: Sumoylated.
Sequence Mass (Da): 31993
Sequence Length: 289
Domain: Kinase-interacting sequence (KIS) is specific for the alpha catalytic subunit interaction and Association with SNF1 Complex (ASC) is specific for the gamma non-catalytic regulatory subunit interaction.
Subcellular Location: Cell membrane
|
Q08430 | MEILKDYLLHICFILFPILLYQVFWLGKPAILVPKINSGLVTLFACGASVLCIIFPIHEMDYIQYGLQMIPVIICLFYISTASGLTVAASVLCFELLFYEPSAMFVFTLLPFLIIIPILFQKKWPFMSKAKKLLLSLLISCVEIFLFFASSWILSALNILNFQKSGIFVYEAAVSGLFRSSVLLLSIYIIESIAENIALRSQLIHSEKMTIVSELAASVAHEVRNPLTVVRGFVQLLFNDETLQNKSSADYKKLVLSELDRAQGIITNYLDMAKQQLYEKEVFDLSALIKETSSLMVSYANYKSVTVEAETEPDLLIYGDATKLKQAVINLMKNSIEAVPHGKGMIHISAKRNGHTIMINITDNGVGMTDHQMQKLGEPYYSLKTNGTGLGLTVTFSIIEHHHGTISFNSSFQKGTTVTIKLPADLPH | Function: Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. Spo0F is required for the KinB activity.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47812
Sequence Length: 428
Subcellular Location: Cell membrane
EC: 2.7.13.3
|
O34206 | MSMPLPMKLRTRLFLSISALITVSLFGLLLGLFSVMQLGRAQEQRMSHHYATIEVSQQLRQLLGDQLVILLRETPDGQALERSQNDFRRVLEQGRANTVDSAEQAALDGVRDAYLQLQAHTPALLEAPMVDNDGFSEAFNGLRLRLQDLQQLALAGISDAETSARHRAYLVAGLLGLVGVAILLIGFVTAHSIARRFGAPIETLARAADRIGEGDFDVTLPMTNVAEVGQLTRRFGLMAEALRQYRKTSVEEVLSGERRLQAVLDSIDDGLVIFDNQGRIEHANPVAIRQLFVSNDPHGKRIDEILSDVDVQEAVEKALLGEVQDEAMPDLVVDVAGESRLLAWSLYPVTHPGGHSVGAVLVVRDVTEQRAFERVRSEFVLRASHELRTPVTGMQMAFSLLRERLDFPAESREADLIQTVDEEMSRLVLLINDLLNFSRYQTGMQKLELASCDLVDLLTQAQQRFIPKGEARRVSLQLELGDELPRLQLDRLQIERVIDNLLENALRHSSEGGQIHLQARRQGDRVLIAVEDNGEGIPFSQQGRIFEPFVQVGRKKGGAGLGLELCKEIIQLHGGRIAVRSQPGQGARFYMLLPV | Function: Member of the two-component regulatory system AlgB/KinB involved in regulation of alginate biosynthesis genes. KinB functions as a membrane-associated protein kinase that phosphorylates AlgB, probably in response to environmental signals.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 66072
Sequence Length: 595
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
|
P39764 | MRKYQARIISIILAMIFIMFWDYLFYFIGKNPINWPVDIVYTAVTLVSVWMLAYYIDEKQQLVKKMKDNEWKYKQLSEEKNRIMDNLQEIVFQTNAKGEITYLNQAWASITGFSISECMGTMYNDYFIKEKHVADHINTQIQNKASSGMFTAKYVTKNGTIFWGEVHYKLYYDRDDQFTGSLGTMSDITERKEAEDELIEINERLARESQKLSITSELAAGIAHEVRNPLTSVSGFLQIMKTQYPDRKDYFDIIFSEIKRIDLVLSELLLLAKPQAITFKTHQLNEILKQVTTLLDTNAILSNIVIEKNFKETDGCMINGDENQLKQVFINIIKNGIEAMPKGGVVTISTAKTASHAVISVKDEGNGMPQEKLKQIGKPFYSTKEKGTGLGLPICLRILKEHDGELKIESEAGKGSVFQVVLPLKSDS | Function: Phosphorylates the sporulation-regulatory protein Spo0A a transcription factor that also controls biofilm formation (Probable). Requires FloT and FloA for localization to DRMs and for activity .
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48846
Sequence Length: 428
Subcellular Location: Cell membrane
EC: 2.7.13.3
|
O31671 | MLERCKLKILKGACGRVKLYIILVVIPAIVISFFVYEKEKDTIAAEHKQEASVLLNLHRNKINYLIGETMARMTSLSIAIDRPVDIKKMQSILEKTFDSEPRFSGLYFLNAKGDVTASTTELKTKVNLADRSFFIKAKETKKTVISDSYSSRITGQPIFTICVPVLDSKRNVTDYLVAAIQIDYLKNLINLLSPDVYIEVVNQDGKMIFASGQASHAEDQKPVSGYLDDISWNMKVYPNPVTIEELSKSLVLPLSCIIVLLNILFILVLYYLLKRQTQLERSENEAQKLELIGTLAASTAHEIRNPLTGISGFIQLLQKKYKGEEDQLYFSIIEQEIKRINQIVSEFLVLGKPTAEKWELNSLQDIIGEIMPIIYSEGNLYNVEVELQYLTEQPLLVKCTKDHIKQVILNVAKNGLESMPEGGKLTISLGALDKKAIIKVVDNGEGISQEMLDHIFLPFVTSKEKGTGLGLVVCKRIVLMYGGSIHIESEVRRGTEVTITLPVSAS | Function: Phosphorylates the sporulation-regulatory protein spo0F and, to a minor extent, is responsible for heterogeneous expression of spo0A during logarithmical growth. Also phosphorylates spo0A under biofilm growth conditions.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56704
Sequence Length: 506
Subcellular Location: Cell membrane
EC: 2.7.13.3
|
O31661 | METLGVQTNSELREELNRLKEENARLKKELNQHQVIVNNTLDAIFICDNEMRIVQANEATERMLQVDSEDLKKRSVLDFLFSIPKDELNLSVKKFFKKGFLWKEVPIRLDCGATKYIEFLAKRGIGEDFFFVVMRDISSKKILEREFSMNEQLFKDLFDRAVDGIVLFDKDGGFIDANLSFCKSFEINHNELSHLSLYEFIDSGSRKDFDNIWKALNRKGKAKGELPVKLRSGVQKLFEFTITSNIISGFYMSIMRDITEKRSMELQLFKSEERFREIFENAMDAIIIWSNDGRIVKANQSACKIFELPMNLLLKRKLCDFLVDSQQKYSITKRKYAKYGEIREELLFQMGNGQFKELEFTSKRTILENQHLTILRNVSDRKRMEKELRESELKFRKVFNGSMDGNVLFDNQYRIIDANPLASHILGLSHEEIKQHSLLDIISAYEIENLASPARQINFDEMDNEIPFLLSSGDNRKLEFSFKRNIIQNMNLAIFKDVTERKELEERLRKSDTLHVVGELAAGIAHEIRNPMTALKGFIQLLKGSVEGDYALYFNVITSELKRIESIITEFLILAKPQAIMYEEKHVTQIMRDTIDLLNAQANLSNVQMQLDLIDDIPPIYCEPNQLKQVFINILKNAIEVMPDGGNIFVTIKALDQDHVLISLKDEGIGMTEDKLKRLGEPFYTTKERGTGLGLMVSYKIIEEHQGEIMVESEEGKGTVFHITLPVRQNAEERRNDE | Function: Phosphorylates the sporulation-regulatory protein spo0A under biofilm growth conditions. Also able to weakly phosphorylate spo0F.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 85513
Sequence Length: 738
EC: 2.7.13.3
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Q8LBB2 | MATVPEIKIMRSESLGHRSDVSSPEAKLGMRVEDLWDEQKPQLSPNEKLNACFESIPVSAFPLSSDSQDIEIRSDTSLAEAVQTLSKFKVLSAPVVDVDAPEDASWIDRYIGIVEFPGIVVWLLHQLEPPSPRSPAVAASNGFSHDFTTDVLDNGDSAVTSGNFFEVLTSSELYKNTKVRDISGTFRWAPFLALQKENSFLTMLLLLSKYKMKSIPVVDLGVAKIENIITQSGVIHMLAECAGLLWFEDWGIKTLSEVGLPIMSKDHIIKIYEDEPVLQAFKLMRRKRIGGIPVIERNSEKPVGNISLRDVQFLLTAPEIYHDYRSITTKNFLVSVREHLEKCGDTSAPIMSGVIACTKNHTLKELILMLDAEKIHRIYVVDDFGNLEGLITLRDIIARLVHEPSGYFGDFFDGVMPLPENYRV | Function: Regulatory subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and in assimilation of nitrogen by phosphorylating nitrate reductase.
PTM: Sumoylated by SIZ1.
Sequence Mass (Da): 47423
Sequence Length: 424
Subcellular Location: Mitochondrion
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P34540 | MEPRTDGAECGVQVFCRIRPLNKTEEKNADRFLPKFPSEDSISLGGKVYVFDKVFKPNTTQEQVYKGAAYHIVQDVLSGYNGTVFAYGQTSSGKTHTMEGVIGDNGLSGIIPRIVADIFNHIYSMDENLQFHIKVSYYEIYNEKIRDLLDPEKVNLSIHEDKNRVPYVKGATERFVGGPDEVLQAIEDGKSNRMVAVTNMNEHSSRSHSVFLITVKQEHQTTKKQLTGKLYLVDLAGSEKVSKTGAQGTVLEEAKNINKSLTALGIVISALAEGTKSHVPYRDSKLTRILQESLGGNSRTTVIICASPSHFNEAETKSTLLFGARAKTIKNVVQINEELTAEEWKRRYEKEKEKNTRLAALLQAAALELSRWRAGESVSEVEWVNLSDSAQMAVSEVSGGSTPLMERSIAPAPPMLTSTTGPITDEEKKKYEEERVKLYQQLDEKDDEIQKVSQELEKLRQQVLLQEEALGTMRENEELIREENNRFQKEAEDKQQEGKEMMTALEEIAVNLDVRQAECEKLKRELEVVQEDNQSLEDRMNQATSLLNAHLDECGPKIRHFKEGIYNVIREFNIADIASQNDQLPDHDLLNHVRIGVSKLFSEYSAAKESSTAAEHDAEAKLAADVARVESGQDAGRMKQLLVKDQAAKEIKPLTDRVNMELTTLKNLKKEFMRVLVARCQANQDTEGEDSLSGPAQKQRIQFLENNLDKLTKVHKQLVRDNADLRVELPKMEARLRGREDRIKILETALRDSKQRSQAERKKYQQEVERIKEAVRQRNMRRMNAPQIVKPIRPGQVYTSPSAGMSQGAPNGSNA | Function: Microtubule-dependent motor protein required for organelle transport . Plays a role in endosome transport . Required for the transport of mitochondria along the axon of motor neurons . Involved in the nuclear migration of hyp7 hypodermal precursor cells . Required for the formation of dendritic branches of PVD sensory neurons . In non-ciliated neurons such as the PVD and PHC neurons, required for the organization of minus-end out microtubules in dendrites . Also required for the minus-end out orientation of microtubules in dendrites of AQR gas-sensing neurons . Involved in the localization of unc-33 to neurites . Positively regulates cilium position and dendrite morphogenesis in the postembryonic AQR and PQR gas-sensing neurons . Plays a more prominent role in regulating dendrite morphogenesis in AQR than in PQR neurons . Plays a role in regulating the localization of grdn-1 to the distal dendrites of AQR sensory neurons .
Sequence Mass (Da): 91894
Sequence Length: 815
Domain: Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.
Subcellular Location: Cytoplasm
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A7NI79 | MTRLSSGGRIEVICGCMFSGKTEELIRRLNHVRLARQRLIAFTPRRDTRYRLGSLVSHNGLSVEARVIDSIRDTPAHLNTDIHVVAVDELHLLDDPPDAAREVCQDLADRGLRVIVAGLDQDFRAQPFPAMAQLMAVAEQVDKLYAICVRCGAYATRSQRLIDGKPAPADAPTIVVGGQELYEARCRACYEPAR | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 21494
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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Q5LUY8 | MAKLYFNYSTMNAGKSTVLLQASHNYRERGMQTYLMTAAIDGRAGTGRIASRIGIGAEADIFTPRDDVFAMIRDRLGAGPVACVFVDEAQFLSPEQVWQLARVVDDLDVPVLAYGLRVDFQGKLFPGSATLLALADEMREVRTICKCGRKATMVIRQDASGRAITEGAQVQIGGNETYVSLCRKHWREATGDPGAKGH | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 21618
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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Q2RZH4 | MDRDRTTGWMEVICGSMFSGKTEELIRRLRRARIARQHTRVFKPALDERYSEDEVVSHNENSVTTTPVEAPPQIQELVQEADVVGIDEAQFFDDDLVPTCQALAEDGHRVIVVGLDTDYRAEPFDPMPQLMAVAEHVTKLHAVCVVCGAPANHSQRIVPGEDRVLVGATEAYEPRCRACFEPEPVTVTRPRPHTEALRAVATDDADASTNEADPEAADAASADGTAA | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 24876
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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Q07866 | MYDNMSTMVYIKEDKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSNMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDTDSTKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGTSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPENMEKRRSRESLNVDVVKYESGPDGGEEVSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR | Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport . The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity).
PTM: Phosphorylation at Ser-460 by ERK inhibits interaction with CLSTN1 and localization to cytoplasmic vesicles.
Sequence Mass (Da): 65310
Sequence Length: 573
Subcellular Location: Cell projection
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Q9H0B6 | MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEDASPNEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGDNKPIWMHAEEREESKDKRRDSAPYGEYGSWYKACKVDSPTVNTTLRSLGALYRRQGKLEAAHTLEDCASRNRKQGLDPASQTKVVELLKDGSGRRGDRRSSRDMAGGAGPRSESDLEDVGPTAEWNGDGSGSLRRSGSFGKLRDALRRSSEMLVKKLQGGTPQEPPNPRMKRASSLNFLNKSVEEPTQPGGTGLSDSRTLSSSSMDLSRRSSLVG | Function: Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68935
Sequence Length: 622
Subcellular Location: Cytoplasm
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O88448 | MATMVLPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLASHEAGEAEPGSQERCLLLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEMLPQEEKGDVPKDSLDDLFPNEDEQSPAPSPGGGDVAAQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGENKPIWMHAEEREESKDKRRDRRPMEYGSWYKACKVDSPTVNTTLRTLGALYRPEGKLEAAHTLEDCASRSRKQGLDPASQTKVVELLKDGSGRGHRRGSRDVAGPQSESDLEESGPAAEWSGDGSGSLRRSGSFGKLRDALRRSSEMLVRKLQGGGPQEPNSRMKRASSLNFLNKSVEEPVQPGGRVFLTAAL | Function: Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66662
Sequence Length: 599
Subcellular Location: Cytoplasm
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Q6P597 | MSVQVAAPGSAGLGPERLSPEELVRQTRQVVQGLEALRAEHHGLAGHLAEALAGQGPAAGLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHVGALEAEKQRLRSQARRLAQENVWLREELEETQRRLRASEESVAQLEEEKRHLEFLGQLRQYDPPAESQQSESPPRRDSLASLFPSEEEERKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATDLLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFEDVERHYARALSIYEALGGPHDPNVAKTKNNLASAYLKQNKYQQAEELYKEILHKEDLPAPLGAPNTGTAGDAEQALRRSSSLSKIRESIRRGSEKLVSRLRGEAAAGAAGMKRAMSLNTLNVDAPRAPGTQFPSWHLDKAPRTLSASTQDLSPH | Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Plays a role during spermiogenesis in the development of the sperm tail midpiece and in the normal function of spermatozoa (By similarity). May play a role in the formation of the mitochondrial sheath formation in the developing spermatid midpiece (By similarity).
Sequence Mass (Da): 55364
Sequence Length: 504
Domain: The heptad repeat (HR) motif is sufficient for interaction with kinesin heavy (KHL) chains and ODF1. The TPR region is involved in mitochondrial binding (By similarity).
Subcellular Location: Cytoplasm
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Q9UH77 | MEGESVKLSSQTLIQAGDDEKNQRTITVNPAHMGKAFKVMNELRSKQLLCDVMIVAEDVEIEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKETRLEHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECYDFEEDRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLRVRTVDVYDGVKDQWTSIASMQERRSTLGAAVLNDLLYAVGGFDGSTGLASVEAYSYKTNEWFFVAPMNTRRSSVGVGVVEGKLYAVGGYDGASRQCLSTVEQYNPATNEWIYVADMSTRRSGAGVGVLSGQLYATGGHDGPLVRKSVEVYDPGTNTWKQVADMNMCRRNAGVCAVNGLLYVVGGDDGSCNLASVEYYNPVTDKWTLLPTNMSTGRSYAGVAVIHKSL | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron . The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two activators of Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney, thereby regulating NaCl reabsorption . The BCR(KLHL3) complex also mediates ubiquitination and degradation of WNK3 . The BCR(KLHL3) complex also mediates ubiquitination of CLDN8, a tight-junction protein required for paracellular chloride transport in the kidney, leading to its degradation (By similarity).
PTM: Phosphorylation at Ser-433 by PKA or PKC decreases the interaction with WNK1 and WNK4, leading to inhibit their degradation by the BCR(KLHL3) complex . Phosphorylated at Ser-433 by PKC in response to angiotensin II signaling, decreasing ability to promote degradation of WNK1 and WNK4, leading to activation of Na-Cl cotransporter SLC12A3/NCC . Phosphorylation at Ser-433 is increased by insulin . Dephosphorylated at Ser-433 by calcineurin PPP3CA, promoting degradation of WNK1 and WNK4 .
Sequence Mass (Da): 64970
Sequence Length: 587
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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E0CZ16 | MEGESVKPSPQPTAQAEDEEKNRRTVTVNAAHMGKAFKVMNELRSKRLLCDVMIVAEDVEVEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKETRLDHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECYDFEEGRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLRVRTVDVYDGVKDQWTSIASMQERRSTLGAAVLNDLLYAVGGFDGSTGLASVEAYSYKTNEWFFVAPMNTRRSSVGVGVVEGKLYAVGGYDGASRQCLSTVEQYNPATNEWIYVADMSTRRSGAGVGVLSGQLYATGGHDGPLVRKSVEVYDPGTNTWKQVADMNMCRRNAGVCAVNGLLYVVGGDDGSCNLASVEYYNPVTDKWTLLPTNMSTGRSYAGVAVIHKSL | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron . The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two activators of Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney, thereby regulating NaCl reabsorption . The BCR(KLHL3) complex also mediates ubiquitination of CLDN8, a tight-junction protein required for paracellular chloride transport in the kidney, leading to its degradation .
PTM: Phosphorylation at Ser-433 by PKA or PKC decreases the interaction with WNK1 and WNK4, leading to inhibit their degradation by the BCR(KLHL3) complex (By similarity). Phosphorylated at Ser-433 by PKC in response to angiotensin II signaling, decreasing ability to promote degradation of WNK1 and WNK4, leading to activation of Na-Cl cotransporter SLC12A3/NCC . Phosphorylation at Ser-433 is increased by insulin (By similarity). Dephosphorylated at Ser-433 by calcineurin PPP3CA, promoting degradation of WNK1 and WNK4 (By similarity).
Sequence Mass (Da): 64922
Sequence Length: 587
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q5REP9 | MEGESVKLSSQTLIQAGDDEKNQRTITVNPAHMGKAFKVMNELRSKQLLCDVMIVAEDVEIEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYVYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKGTRLEHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECYDFEEDRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLRVRTVDVYDGVKDQWTSIASMQERRSTLGAAVLNDLLYAVGGFDGSTGLASVEAYSYKTNEWFFVAPMNTRRSSVGVGVVEGKLYAVGGYDGASRQCLSTVEQYNPATNEWIYVADMSTRRSGAGVGVLSGQLYATGGHDGPLVRKSVEVYDPGTNTWKQVADMNMCRRNAGVCAVNGLLYVVGGDDGSCNLASVEYYNPVTDKWTLLPTNMSTGRSYAGVAVIHKSL | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron. The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two activators of Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney, thereby regulating NaCl reabsorption. The BCR(KLHL3) complex also mediates ubiquitination and degradation of WNK3 (By similarity). The BCR(KLHL3) complex also mediates ubiquitination of CLDN8, a tight-junction protein required for paracellular chloride transport in the kidney, leading to its degradation (By similarity).
PTM: Phosphorylation at Ser-433 by PKA or PKC decreases the interaction with WNK1 and WNK4, leading to inhibit their degradation by the BCR(KLHL3) complex. Phosphorylated at Ser-433 by PKC in response to angiotensin II signaling, decreasing ability to promote degradation of WNK1 and WNK4, leading to activation of Na-Cl cotransporter SLC12A3/NCC. Phosphorylation at Ser-433 is increased by insulin. Dephosphorylated at Ser-433 by calcineurin PPP3CA, promoting degradation of WNK1 and WNK4.
Sequence Mass (Da): 64884
Sequence Length: 587
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q5ZI33 | MAAPGSEKSSKKKTEKKLAAREEAKLLAGFMGVMNSMRKQRTLCDVILMVQERRIPAHRVVLASASHFFNLMFTTNMLESKSFEVELKDAEPDIIEQLVEFAYTARISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLNQDTLTVRAEDQVYDAAVRWLKYDEPNRQPYMVDILAKVRFPLISKNFLSKTVQAEPLIQDNPECLKMVISGMRYHLLSPEDREELVEGTRPRRKKHDYRIALFGGSQPQSCRYFNPKDYSWTDIRCPFEKRRDAACVFWDNVVYILGGSQLFPIKRMDCYNVVKDSWYSKLGPPTPRDSLAACAAEGKIYTSGGSEVGNSALYLFECYDTRTESWHTKPSMLTQRCSHGMVEANGLIYVCGGSLGNNVSRRVLNSCEVYDPATETWTELCPMIEARKNHGLVFVKDKIFAVGGQNGLGGLDNVEYYDIKMNEWKMVSPMPWKGVTVKCAAVGSIVYVLAGFQGVGRLGHILEYNTETDKWIANSKVRAFPVTSCLICVVDTCGANEETLET | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination (By similarity).
Sequence Mass (Da): 66196
Sequence Length: 586
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q8IXQ5 | MAASGVEKSSKKKTEKKLAAREEAKLLAGFMGVMNNMRKQKTLCDVILMVQERKIPAHRVVLAAASHFFNLMFTTNMLESKSFEVELKDAEPDIIEQLVEFAYTARISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLNQDTLTVRAEDQVYDAAVRWLKYDEPNRQPFMVDILAKVRFPLISKNFLSKTVQAEPLIQDNPECLKMVISGMRYHLLSPEDREELVDGTRPRRKKHDYRIALFGGSQPQSCRYFNPKDYSWTDIRCPFEKRRDAACVFWDNVVYILGGSQLFPIKRMDCYNVVKDSWYSKLGPPTPRDSLAACAAEGKIYTSGGSEVGNSALYLFECYDTRTESWHTKPSMLTQRCSHGMVEANGLIYVCGGSLGNNVSGRVLNSCEVYDPATETWTELCPMIEARKNHGLVFVKDKIFAVGGQNGLGGLDNVEYYDIKLNEWKMVSPMPWKGVTVKCAAVGSIVYVLAGFQGVGRLGHILEYNTETDKWVANSKVRAFPVTSCLICVVDTCGANEETLET | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination.
Sequence Mass (Da): 65992
Sequence Length: 586
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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G5ED84 | MPVYAKAIFGSFPSVQQVRVENGERCLIEAMDELNKNEKGLYRPVRLENGDQISTTDDVLNGKLARVSYTPFEEFELVSNSKGSCMEYENQEQSSKIMEQMRILRQTEELCDVELLVAGSVIRAHRYILAAASPYFKAMFTNGMVEMKKLTIELQDIPEESVRIIVDYIYTDKIAITMNNVHQLIFTATVLQMDVIVVACQQFLATMITSHNCMSLYHFSDIYNCTNLISSIEDFASSQFRCIRKSPEFNSISFHHLKSLLNRSDLNVSEEQDVFETIVQWVSSNPRDRQHHFVQLFKTLRLHLVGWNFLCEAVNSNSYVKNSQECREIISAMVLDAMTPSKRKHPESNHENTSEYSASMACPSLTASSSSSTSTFRKSVAGAIFCAGGRGKAGGPFSSVEAYDWRRNQWIEVPDMMSQRRHVGVVSANGNLYAIGGHDGTAHLATAEAFQPSIRQWKRIASMKTARRGIAVASIENVIYAVGGLDDTTCYKTVERYDIEEDEWSTVADMDVQRGGVGVAVIGRYLFAIGGNDGTSSLETCERFDPMIDKWKRIASMKNRRAGSGVCVLDGYLYAIGGFDDNAPLETCERYDPDADKWITLDKMSSPRGGVGVAALGGKVYAIGGHDGSDYLNTVECYDPIANRWQPAAEIKECRAGAGVAWANVRMHQLSRTPEKCDSGCAPSGGSYCI | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates degradation of glutamate receptors in neurons. The BCR(kel-8) ubiquitin ligase complex mediates ubiquitination and subsequent degradation of rpy-1. Indirectly regulates the protein turnover of glr-1, possibly via ubiquitination and degradation of rpy-1.
Sequence Mass (Da): 76763
Sequence Length: 690
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Synapse
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O43240 | MRAPHLHLSAASGARALAKLLPLLMAQLWAAEAALLPQNDTRLDPEAYGSPCARGSQPWQVSLFNGLSFHCAGVLVDQSWVLTAAHCGNKPLWARVGDDHLLLLQGEQLRRTTRSVVHPKYHQGSGPILPRRTDEHDLMLLKLARPVVLGPRVRALQLPYRCAQPGDQCQVAGWGTTAARRVKYNKGLTCSSITILSPKECEVFYPGVVTNNMICAGLDRGQDPCQSDSGGPLVCDETLQGILSWGVYPCGSAQHPAVYTQICKYMSWINKVIRSN | Function: Has a tumor-suppressor role for NES1 in breast and prostate cancer.
Sequence Mass (Da): 30170
Sequence Length: 276
Subcellular Location: Secreted
EC: 3.4.21.-
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Q07970 | MASRNQNRPPRSPNAKKEGLGGISFDKRRKVETQGGTGRRQAFSAVNKQDVTMNSDVGSIEECGKVDFTKDEILALLSERAKAGKFDTKAKIEQMTDIIKRLKVCVKWFQQADETHVQEKENLKVSLESSEQKYNHKELEARTKEEELQATISKLEENVVSLHEKLAKEESSTQDAIECHRREKEARVAAEKVQASLGEELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNSKLQTDLETVRAALTRAEKEKSSILENLSTLRGHSKSLQDQLSSSRVLQDDAIKQKDSLLSEVTNLRNELQQVRDDRDRQVVQSQKLSEEIRKYQENVGKSSQELDILTAKSGSLEETCSLQKERLNMLEQQLAIANERQKMADASVSLTRTEFEEQKHLLCELQDRLADMEHQLCEGELLRKKLHNTILELKGNIRVFCRVRPLLPDDGGRHEATVIAYPTSTEAQGRGVDLVQSGNKHPFTFDKVFNHEASQEEVFFEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPEAPDQKGLIPRSLEQIFQASQSLGAQGWKYKMQVSMLEIYNETIRDLLSTNRTTSMDLVRADSGTSGKQYTITHDVNGHTHVSDLTIFDVCSVGKISSLLQQAAQSRSVGKTQMNEQSSRSHFVFTMRISGVNESTEQQVQGVLNLIDLAGSERLSKSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNISPDPTSAGESLCSLRFAARVNACEIGIPRRQTSTKLLDSRLSYG | Function: Kinesin that supports microtubule movement in an ATP-dependent manner and has a minus-end directed polarity. Plays a crucial role in spindle morphogenesis in male meiosis. In mitosis, is required for normal microtubule accumulation at the spindle poles during prophase and may play a role in spindle assembly during prometaphase.
Sequence Mass (Da): 89047
Sequence Length: 793
Domain: Composed of three structural domains; a small globular N-terminal, a central alpha-helical coiled coil and a large globular C-terminal which is responsible for the motor activity (it hydrolyzes ATP and binds microtubules).
Subcellular Location: Cytoplasm
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F4JGP4 | MPLRNQNRAPLPSPNVKKEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDTKGKIEQMTDIIKKLKVCVRWYQQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKKLHNTILELKGNIRVFCRVRPLLPDDGGRQEASVIAYPTSTESLGRGIDVVQSGNKHPFTFDKVFDHGASQEEVFFEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPETPEQKGLIPRSLEQIFKTSQSLSTQGWKYKMQVSMLEIYNESIRDLLSTSRTIAIESVRADSSTSGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNESTEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARVNACEIGIPRRQTSAKLLDSRLSYG | Function: Kinesin that supports microtubule movement in an ATP-dependent manner and that functions as a minus-end directed motor as well as a plus-end tracking protein. During mitosis, is involved in early spindle assembly. Participates in the capture of antiparallel interpolar microtubules and helps in generating force to coalign microtubules.
Sequence Mass (Da): 89194
Sequence Length: 790
Domain: Composed of three structural domains; a small globular N-terminal, a central alpha-helical coiled coil and a large globular C-terminal which is responsible for the motor activity (it hydrolyzes ATP and binds microtubules).
Subcellular Location: Cytoplasm
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P34885 | MLFTGTVRVRVLEARQLRPTEWSRRFRQDEAATAAIDSYVNVDWDEYHIGKTQVRPKTNEPRWNEEFTASGVHQGKAIGFSVFHSCVMPPDDFVANTRIAFDQLKIGSANDIWVDLEPHGQLHVVVEMHGTNVEDVHSHNKTRVFKERTNAFNDRQRRGAMRRKIHEVTGHKFMALFLRQPTFCAHCKEFIWGIGKQGYQCQICTVVVHKRCHEDVVWKCPGNKADAVEELGKEIQETGAGRFNINMPHRFSVHSYKRPTFCDHCGSMLYGLINQGLQCSTCKLNVHKRCQRNVANNCGINAKQMAAELAQLGLTGDKMSIRSKKKPSIMTDTSTDISGSSNSENSGYLQQISEDDSGTTSSRSASKVPGGTLSIHDFTFMKVLGKGSFGKVMLAERKGTDEVYAIKILKKDVIVQDDDVECTMCEKRILSLAAKHPFLTALHSSFQTSDRLFFVMEYVNGGDLMFQIQRARKFDESRARFYAAEVTCALQFLHRNDVIYRDLKLDNILLDAEGHCRLADFGMCKEGINKDNLTSTFCGTPDYIAPEILQEMEYGVSVDWWALGVLMYEMMAGQPPFEADNEDDLFEAILNDDVLYPVWLSKEAVNILKAFMTKNAGKRLGCVVSQGGEDAIRAHPFFREIDWDALESRQVKPPFKPKIKSKRDANNFDSDFTKEEPVLTPSDPAVVRAINQDEFRGFSFINPHFTY | Function: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. Involved in neuropeptide secretion in motor axons. Likely to act via the extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) pathway in the signaling response to various sensory neurons; temperature, odor, taste, and osmolality. Its role in regulation differs depending on the neuron in which it is acting; thermosensation in AFD neurons, osmolality in ASH neurons, olfactory perception in AWA and AWC neurons. Promotes dauer formation mediated by the insulin/IGF pathway. Required for resistance to antimitotic toxins.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80151
Sequence Length: 707
Subcellular Location: Membrane
EC: 2.7.11.13
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Q16974 | MEKRVARRGALRQKNVHEVKNHKFLARFFKQPTFCSHCKDFIWGFGKQGFQCQVCSLVVHKRCHEFVCFICPGADKGPDSDATNLHKFKLHSYGSPTFCDHCGSLLYGLLHQGLKCDSCDMNVHKRCEKNVPLLCGTDHTERRGRILIKGAVKGSKVLVEILEAKNLCPMDPNGLADPYVKVKLIPYDAHKLKLKTKTIKASLNPVWNESFTVDIGPEDNSKRLSLEVWDWDRTSRNDFMGSLSFGISELIKSPVEGWFKLLNQEEGEFYGVPVTDDITESIQEIKSKMHRSSISSEKRYPEPDKVQNMSKQDIVRASDFNFLTVLGKGSFGKVVLAERKGTDELYAIKILKKDVIIQDDDVECTMIEKRVLALPDKPPFLVQLHSCFQTMDRLYFVMEYVNGGDLMYRIQQEGKFKEPVAAFYAAEIAIGLFYLHTQGIVYRDLKLDNVMLDAEGHIKIADFGMCKENIMGDKTTRTFCGTPDYIAPEIVLYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEEELFTSITDHNVSYPKALSREAVSLCKGLLTKTPAKRLGCGPNGERDIKDRAFFRPIQWERIELREVQPPYKPRIKSRKDVSNFDREFTSEAPNVTPTDKLFIMNLDQCEFSGFSYVNPEFVVTV | Cofactor: Binds 3 Ca(2+) ions per C2 domain.
Function: This is calcium-dependent, phospholipid-dependent, serine- and threonine-specific enzyme. Activation of PKC by serotonin results in presynaptic facilitation of depressed sensory-to-motor neuron synapses, which is thought to underlie behavioral dishabituation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 74079
Sequence Length: 649
Subcellular Location: Cytoplasm
EC: 2.7.11.13
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P34722 | MAQAENACRLKLLRADVPVDLLPAGCSATDLQPAVNVKEKIEVNGESRLVQKKKTLYPEWEKCWDTAVAEGRILQIVLMFNQTPVVEATMRLEDIISKCKSDAITHIWINTKPNGRILAQTRHLKNAPDDDHPVEDIMTSRSNSGPGIQRRRGAIKHARVHEIRGHQFVATFFRQPHFCSLCSDFMWGLNKQGYQCQLCSAAVHKKCHEKVIMQCPGSAKNTKETMALKERFKVDIPHRFKTYNFKSPTFCDHCGSMLYGLFKQGLRCEVCNVACHHKCERLMSNLCGVNQKQLSEMYHEIKRGTHATASCPPNIANLHLNGETSKNNGSLPNKLKNLFKSHQYSVEEQKETDEYMDNIWGGGDGPVKKFALPHFNLLKVLGKGSFGKVMLVELKGKNEFYAMKCLKKDVILEDDDTECTYIERRVLILASQCPFLCQLFCSFQTNEYLFFVMEYLNGGDLMHHIQQIKKFDEARTRFYACEIVVALQFLHTNNIIYRDLKLDNVLLDCDGHIKLADFGMAKTEMNRENGMASTFCGTPDYISPEIIKGQLYNEAVDFWSFGVLMYEMLVGQSPFHGEGEDELFDSILNERPYFPKTISKEAAKCLSALFDRNPNTRLGMPECPDGPIRQHCFFRGVDWKRFENRQVPPPFKPNIKSNSDASNFDDDFTNEKAALTPVHDKNLLASIDPEAFLNFSYTNPHFSK | Function: Diacylglycerol (DAG)-dependent serine/threonine-protein kinase that phosphorylates a range of cellular proteins (Probable). Phosphorylates mlk-1, a component of the JNK pathway. Involved in axon regeneration after injury probably by activating the JNK pathway . Plays a role in resistance to fungal infection and in wound healing by promoting expression of antimicrobial peptide nlp-29 in the epidermis downstream of gpa-12 and plc-3 and upstream of tir-1-p38-like pathway . Probably by regulating neuronal transmission in ALA neurons, regulates the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt, downstream of lin-3 and receptor let-23 and phospholipase plc-3 .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 80298
Sequence Length: 704
EC: 2.7.11.13
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Q6ZFT5 | MEVVVARQPKAKKQINLFYCSECEELALKVAASSDTIHLQSINWRSFDDGFPNLFINNAHDIRGQHVAFLASFSSPSVIFEQISVIFALPKLFIASFTLVLPFFPTGSFERVEEEGDVATAFTLARILSMIPKSRGGPTSVVIYDIHALQERFYFGDDVLPCFETGIPLLLQRLRQLPDADNITIAFPDDGAWKRFHKLLLNFPMVVCAKVREGDKRIVRIKEGNPEGRHVVIVDDLVQSGGTLRECQKVLAAHGAAKVSAYVTHAVFPKQSYERFTHTNSAGSADKFAYFWITDSCPQTVKAINQQPPFEVLSLAGSIADALQI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 36149
Sequence Length: 325
EC: 2.7.6.1
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Q9XGA1 | MEKPNTKQVLLFYCVEAEELARKVAAQSPLITLQSINWRSFDDGFPNLFINNAQDIRGQHVAFLAAFSSPAVIFEQLSVIYALPRLFVASFTLVLPFFPTGSFERMEEEGDVATAFTMARILSNIPVSRGGPTSVVIYDIHALQERFYFSDNVLPLFETGIPLLKQRLDQLPDADKIVVAFPDDGAWKRFHKQLDHFPMVVCAKVREGDKRIVRLKEGNPAGCHVVIVDDLVQSGGTLIECQKVLAAHGATKVSAYVTHAVFPKNSFERFTHKDDGSDKAFTYFWITDSCPRTVKSIANKAPFEVLSLAGSIADALQI | Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 35385
Sequence Length: 318
Subcellular Location: Cytoplasm
EC: 2.7.6.1
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Q9YAW0 | MEGPEQWVIVGGWGSASAEFSEGLSRNMGLKLVKPVFKLFPDEEEYVRIEGDISGFTGAIVVQSFERPASRSLVYSLLIADALKEAGVGRIVLMAPYMGYTRQDRVFLPGEPVSVRAVMRALASSGYNALASIEVHKEYVLDYFDGSTLNIFPFTYMLKETGISCGDNTIIVAPDKGSLPRVERLARETGCRSYGYLVKERDRITGEVRLAKSTVDPRGKNAIVVDDIISTGGTIALASQWLLENGANSVFVLAAHYLGIGNAEEKMMKAGVSRVVTGNTLPRKPSKIVTYVDLTGLAAGQLTKLVSNL | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 33508
Sequence Length: 309
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.6.1
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P14193 | MSNQYGDKNLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLEDIVIVSPDHGGVTRARKLADRLKAPIAIIDKRRPRPNVAEVMNIVGNIEGKTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVLSGPAVERINNSTIKELVVTNSIKLPEEKKIERFKQLSVGPLLAEAIIRVHEQQSVSYLFS | Cofactor: Binds 2 Mg(2+) ions per subunit. Each Mg(2+) binds only one residue (His-136 and Asp-175, respectively) of this protein, however the magnesium ions also bind substrates and water molecules to complete their coordination spheres . Can also use Mn(2+) and Cd(2+) ions, but the activity is less than that obtained with Mg(2+) ions .
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 34868
Sequence Length: 317
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.6.1
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Q8G5P2 | MVSAILEGKPDKNLILVTGRIHPKLAEDVAEQLGIDVLETTAYDFANGEMYVRYTESVRGADVFVLQSHYKPINKAIMEQLIMIDALKRASARSITAVCPLLGYSRQDKKHRGREPISCRLVFDLLKTAGADRIMSVDLHAAQSQGFFDGPVDHLVAMPVLVDYIRDRFQGHLDNVAVVSPDAGRIRVAEQWAQRLGGGPLAFVHKTRDITRPNQAVANRVVGDVAGKDCVLVDDLIDTAGTIAGACHVLQDAGAKSVTVVATHGVLSGPAVERLKNCGAREVVLTDTVPIPEEKRWDGLTVLSIAPLLASAIRAVFEDGSVAELFDTYPEHHGQGFLFA | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 36863
Sequence Length: 340
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.6.1
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Q89DJ1 | MSAKNGSIKLVAGNSNPALAQAIAQGLHLPLTKAVVRRFADMEIFVEIQENVRGSDAFIIQSTSFPANDHLMELLIITDALRRSSARRITAVLPYFGYARQDRKSGSRTPISAKLVANLITQAGVDRVMTLDLHAGQIQGFFDIPTDNLYAAPLMVRDIKDKFDLSKTMVISPDVGGVARARGLAKRINTPLAIVDKRRERPGESEVMNVIGDVAGYTCILVDDIVDSGGTLVNAADALIAKGAKDVYAYITHGVLSGGAAARITNSKLKELVITDSILPTDAVSKAPNIRTLPIASLISDAIARTAAEESVSSLFD | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 33868
Sequence Length: 317
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.6.1
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P11980 | MPKPDSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVEMLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRAATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKEKGADYLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAVFHRLLFEELARASSQSTDPLEAMAMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDAVLDAWAEDVDLRVNLAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP | Function: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.
PTM: ISGylated.
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 57818
Sequence Length: 531
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.40
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P30613 | MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS | Function: Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis.
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 61830
Sequence Length: 574
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
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A0A1X9ISP7 | MSLLLSNSALVGPKFRSSRISHASASLDIGLQRATSPQNASVATCFEETKGRIAKLFHKNELSVSTYDTAWVAMVPSPTSSEEPCFPACLNWLLENQCHDGSWARPHHHHMLKKDVLSSTLACILALKKWGVGEEQISRGLHFVELNFASATEKGQITPMGFDIIFPAMLDNARGLSLNLQLEPTTLNDLIYKRDLELKRCNQSNSAEKEVYWAHIAEGMGKLQDWESVMKYQRKNGSLFNSPSTTAAAFIALRNSDCLNYLYSAMNKFGSAVPAVYPLDIYSQLCLVDNLERLGISRFFSTEIQSVLDDTYRCWLDGDEEIFMDASTCALAFRTLRMNGYSVTSDSFTKAVQDCFSSSIPSHMRDVNTTLELYRASEIMLYPDEIELEKQHSRLRSLLEHELSSGSIQSSQLNAVVKHALDYPFYAILDRMAKKKTIEHYEFDDTRILKTSFCSPTFGNKDFLSLSVEDYNRCQAIHRKEFRELDRWFKETKLDELKFARQKYTYSYCTAAASFASPELSDARMSWAKNSVLIGIVDDLFDVKGSVEEKQNLIKLVELWDVDVSTQCCSQSVQIIFSALRSTICEIGDKGFKIQGRSITDHIIAIWLDVLYNMMKESEWAENKSVPTIDEYMKISHVSSGLGPVVLPSLYLVGPKLSQEMVNHSEYHSLFKLMSTCCRLLNDIRSYEREVEGGKPNALALYRVSSGGEMMMSKEAAISELERLIERQRRELMRTILEESVIPKCCKEIFGH | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities . Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-isopimaradiene like compounds .
Sequence Mass (Da): 85257
Sequence Length: 752
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 4.2.3.-
|
Q0JA81 | MVPALRRGGGGPRFPQCVAWIQRNQRGDGSWRHAAAAHQQLGSSPEIVTERDLSSTLACVLALARWDAGSEHVRRGLQFIGRNMSVAMDDQTAAPASGSVVSFAAMLRMAMEMGLEVPAVSQADVRDRDAGVICHGGRTEYTAYVSEGLGNIQNWNEVMKFQRKNGSLFNSPYTTAAALVHNYDAKALQYLDMLLDKFGSAVPAAYPANIQSQLYMVDVLEKMGISRHFVGEIKSILDMTYSCWKQRDEEIVLDMQTCGMAFRMLRMNGYDVSSDELSHFSEPSSFHNSLQGYLNDTRSLLELHKASKVSIAEKEVILDNIGSWTGCLLKEQLLSSAMKRNPLSEEVEYALEFPFYTILDRLDHKRNIEHFDITSSQMLETAYLPCHSNEEIMALGVRDFSSSQFIFQEELQQLNSWVKESRLDQLQFARQKLDYFYFSAAATIFTPELSDVRILWAKNGVLTTVVDDFFDVGGSKEELENLVALVEKWDKNDKTEYYSEQVEIVFSAIYTSTNQLGSMASVVQGRDVTKHLVEIWQELLRSMMTEVEWRQSRYVPTAEEYMENAVVTFALGPVVLPALYLVGPKMPDSVIRSQECSELFRLMSKCGRLLNDVQSYEREGSQGKLNSVSLLALHSGGSVSMEEAVKQIQRPIEKCRRELLKLVVSRGGAVPRPCRELFWSMCKVCHFFYSGGDGFSSPTAKAGALDAIPICFVECDEKKKNEEERIVIFWAEKKEKEKEKERVNNKKMVLLLFTWVTGDDGGGAAEVAGATGGLGHLPVAVEGVGGVGEHDPGVLGVKPGVDDAGGLGSNDGGVKPPMGGSGGGWSSGANGVEAKGGVGVGVVVGVEDDGGAFGGLTQYGELEPSPVASARLAASPSGFAGEGDEEGSCIGSTVLMKLSLYSAFSSVFLLLRLIRALASAPSTTTTTTQSNAHQKPN | Cofactor: Binds 3 Mg(2+) ions per subunit.
Sequence Mass (Da): 102596
Sequence Length: 937
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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A0A1X9ISH5 | MSTLKLIPFSTSIDKQFSGRTSILGGKCCLQIDGPKTTKKQSKILVEKIRERISNGKVVEISASAYDTAWVAMVPSREMSGRPSFPECLDWIVENQNPDGSWGLNPFLVKDSLSCTLACLLALRKWGLPNHLLHKGIEFIESNISRAATDDENQVAPIGFNIIFPAMISYAKELDLTLTLPPSSLNALLRARDSEMIRREGKWEYVGEGLGDSCNWNQIIQKHQSRNGSLFNSPATTAAAAIHCRDHKCFDYLISVVNKCNGWAPTVYPMDIYARLCMIDTLQRLGIDCHFRVELDAIFDEIYRNWQEREEEIFSDVTCQALAFRLLRVKGYDVSSDGLEEFVEQEGFFNSVSMQHSNVGTVLELYRASQTRINEEENTLQKIHAWTKPFLTQQLLNKTIRHKPLQMQVEYDLKNFYGTVDRFQHRRTIDLYDAQASQILKTAYRCSAIHNEDFIRFSVQNFKICRAEYQKELDEINKWYAYFGMDLLSKGRNACEQAYVVTAGLIADVELSMARISFAQVILLITVFDDVFDRYGTREEALAVIHLIKEILTHYRWKAAPKECSQLVKTTFTALYDTVNETAAKAHALQGFCFKQQIISLWEELLECAVREKESLSGKNVSTLDEYLSFAPVTIGCELCVLTAVHFLGIQVSEEMLTSAEMLTLCWHGNVVCRLLNDLKTYSREREEKTVNSVSVQVGVSEEEAVAKVKEVLEYHRRKVVEMVYQSQGSNVPRECKELVWKTCKVAHCFYGYDGDEFSSPRDIVDDIKAMMFLGLPHLSTH | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities . Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to nezukol and miltiradiene . The reaction mechanism proceeds via the ionization of the diphosphate group of (+)-CPP, followed by formation of an intermediary pimar-15-en-8-yl(+) carbocation and neutralization of the carbocation by water capture at C-8 to yield nezukol . Can interact with ent-copalyl diphosphate (ent-CPP) but seems unable to use it as substrate .
Catalytic Activity: (+)-copalyl diphosphate = diphosphate + miltiradiene
Sequence Mass (Da): 89155
Sequence Length: 782
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.183
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Q0JA83 | MFQLELVNVVMHQRKAIEDTMRKKKKQQLHKFEMLPSPYDTAWVAMVPLPGSSSQLPCFPQCVEWILQNQQSNGSWDLNQLDSITKDALLSTLACVLALRRGLLFIGRNFSIAMDEQLAAPIGFNITFPGMLSSVIEMGLEVPIGQTDVERVLHLQETELKREYEENYRGRNTYMAYVSEGLGNAQDWNEVMNFQRKNGSLFNSLSITAAVLVHNYDAKAHRYLNLLLNKFGTAVYTKNIHRQLSMLDALENMGISRHFDGEIKSILDMTYSCWLQRDEEVMLDITTCAMAFRILRMNGYDVSSDDLCHIAEVSDFHSSHQGYLSDTRTLLELYKASEVSVADNEFILDRIGSWSGRLLKEQLSSGALQRTSSIFEEVEHALDCPFYATLDRLVHKRNIEHFAAMSYISYAQNNIPDELERIDSWVKENRLHELKFARQKSAYFYLSAAGTVFDPEMSDARIWWAINGVLTTVVDDFFDVGGSREELENLISLVEMWDEHHKEELYSEQVEIVFFAIFNSVNQLGAKVSAVQGRDVTKHLIEIWLDLLRSMMTEVEWRISNYVPTPEEYMENAAMTFALGPIVLPALYLVGPKIPESVVRDSEYNELFRLMSTCGRLLNDVQTYEREDGEGKVNSVSLLVIQSGGSVSIEEARREIMKPIERCRRELLGLVLRRGSAVPGPCKELFWKMCKVCYFFYSRGDGFSSPTAKSAAVDAVIRDPLDLAAVVASQEPIYIIPAS | Cofactor: Binds 3 Mg(2+) ions per subunit.
Sequence Mass (Da): 84125
Sequence Length: 739
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
|
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