ID V8PIQ8_OPHHA Unreviewed; 855 AA.
AC V8PIQ8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN Name=stk10 {ECO:0000313|EMBL:ETE73851.1};
GN ORFNames=L345_00298 {ECO:0000313|EMBL:ETE73851.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE73851.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE73851.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE73851.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE73851.1}.
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DR EMBL; AZIM01000027; ETE73851.1; -; Genomic_DNA.
DR AlphaFoldDB; V8PIQ8; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46538:SF2; SERINE_THREONINE-PROTEIN KINASE 10; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ETE73851.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..200
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 224..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 524..599
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 359..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE73851.1"
SQ SEQUENCE 855 AA; 99241 MW; 65351A7BE91BC0D6 CRC64;
MLQSLILAED LEIIMIEFCP GGAVDATMLE LDRGLTESQI QVICRQMLEA LNYLHGKKII
HRDLKAGNVL LTLDGDIKLA DFGVSAKNMK TVQKRDSFIG TPYWMAPEVV MCETMKDTPY
DYKADIWSLG ITLIEMAQIE PPHHELNPMR VLLKIAKSDP PTLNYPSKWS PAFRDFLKTA
LDKNPETRPT ATQLLEHPFV SKITTNKALR ELVAEAKAEV MEEIEDNREE VEEEDSSESA
SPHDVQKRDS SLASQLGLGG EKLQENRLSL VTNGPKLPLE QAKEAVNGQD SRLLEEEART
EALVKTAEHS DSLGIESYSV LPGAKQKLST SPQALQPNEN IKPAEDEAVN HQKESTETAN
SEDSNWGSQT VNSLLETPTE EKLPNGSLNS SQFENDSFKR DSDSGSTSAS ESMDLNISLS
TDLSLNRGSE SHSLKNAKMQ NMTLKRTRRF VVDGVEVSVT TSKIISEDEK KDEEMRFLRQ
AKTVFCLRQE LRELRLLQKE EHRNQTQLTN KHQLLLEQML KRFEQEMNSK KRFYDTELEN
LERQQKQQIE KMEQDHALHR RDEAKRIRAE QERDLVKFQE LLKQRKKELK NDIEKLPRQQ
RKSSMKVKMD EFVQKKQVME QDFIAKQSED LEQAMKNITA QNRKEICDKE RDCLNKKQQL
MRDREATIWD LEEHHLQEKH QILKQQLKDQ YFLQRHELLR KHEKEREQMQ RYNQRMIEQL
KVRQQQERAR LPKIQRSEGK TRMAMYKKSL HINSSGSASE QREKIKQFAQ QEDKRQKAER
VQQQQKHEMQ MKEMLAQCES NMNELQQLQA LEDELNQKKR EQEMFFKLSE ETDGLSPMSP
NKPAKFVPFS SAEAS
//
