ID V8P2C4_OPHHA Unreviewed; 1946 AA.
AC V8P2C4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=Wnk2 {ECO:0000313|EMBL:ETE68664.1};
GN ORFNames=L345_05539 {ECO:0000313|EMBL:ETE68664.1};
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:ETE68664.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE68664.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE68664.1};
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:ETE68664.1}.
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DR EMBL; AZIM01000965; ETE68664.1; -; Genomic_DNA.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR PANTHER; PTHR13902:SF10; SERINE_THREONINE-PROTEIN KINASE WNK2; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETE68664.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..298
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1778..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE68664.1"
SQ SEQUENCE 1946 AA; 211842 MW; 5B4975EF79CACC8B CRC64;
MDDGSGSASR RGGGVDPAAV PKGGRTAAPA PFPRVPYAKD PKTAHQRFLR RSVVDSDQEE
PPFESAEPEQ QQQPKKILIL SKTRRIIAER AKAGQRPVVV EETRPGEEPA GQDQGKSKKE
EAEEEEEEAD MKAVATSPDG RFLKFDIELG RGSFKTVYKG LDTETWVEVA WCELQDRKLT
KMERQRFKEE AEMLKDGFFL FCSGTPEFMA PEMYEEHYDE SVDVYAFGMC MLEMATSEYP
YSECQNAAQI YRKVTSGVKP ASFDKVTDPE IKEIIGECIC KNKEERYEIK DLLSHAFFAE
DTGVRVELAE EDDGRKSSIA LRLWVEDAKK LKGKSKDNGA IEFTFELEKE TPDDVAQEMV
DAGFFHESDV KIIAKSIRDR VALIQWRRER IWPMLHSEDH RDPESLEKTK ATQAQPLQIT
HPSHAGHQIP SEPDEPEVDQ HLSQQNLPTS ITSLASDSTF DSGQGSTVYS DSQSSQQSVI
YSSVPDAIPP AVQRVYSPPL SESQTLPHGL QQIGPYQQPS VPGLPVVQGP TAVVPPRPQL
YPEPAIPFPI VHPTSVAPVQ MRQPQPVLVS QQQSISSPAP LQQVLSNQPV CSVQQPAPHL
LSQFQMPSSH MAATSAPLAP LQVPSAQSLP PVPPAQIPQF PIIPAVTPLA GLDTHPSNLS
DIPAANMTPI PAPSQYFPSA VIIPSLPVNS TLPLSSNSPA LPMQAVNLPH TTVASLVLPC
QTIVPNMPAA TVPLISMPLP GVSALPTHHA AAQLSQQQMY QATLQQIIQN EAMSSPLHTQ
NMQAVSQQQQ QMLSSLPQSL QPSIIHPSEQ AMSASGAGNQ IIGHPQYAVD IGTHIPALPV
QASAIISPPL QLQPEAMLPH IASDGLSQSN LGTTNSAMLA DHGLPLQCSA YPQSQSESHQ
LPGQQVPTKG PAVPLASEPP QEVVWAVHDN SYCLRVNEQA VLEKQQSLSQ SCESYMSPDV
ASGKEMSDSF EGTSGGGKQE GKPIKKHKKS ARARSRQEKS NRPKLTILNV CNTGDKMVEC
QLETHNHKMV TFKFDLDGDA PEEIATYMVE NEFILPTEKE IFIEQLKEII DKAEDMLSED
TEGERSSDQG VSPQQDTYKL EINENFGCFG DEFEQIPNVL HTGKRWFIIC PVVENQAAEV
PEFSSHAPQS TKQSEAPGLE LLDDQQQSSA VTEKQTSLAY QHISNQLGSN ECPRGTPPPS
SLTQVSVQSS LTSLSQVHPM LASTTLEKIA ESTSQLECPL PQPVSASQCD TPAHTTATSE
EHFEDKVPLN TSQHTVQKKD EKTCFPSMEH EHSTAGLPKQ FQSIPVQTTE NSFPVISDAP
VLELQSSTQT PSLSDNTQLG QIPHSFVDQI PPLPAISELP VSATSQLSSP PHLSTAVSQL
HMPTQSQPVA STGSAMTAPQ PPCMVESDGE GPPRVDFTDN TIKSLDEKLR NLLYQEYIPT
SSASAATPDQ VDGEFNLAPL PALVLDLKIP GVGLDAHVAE DQPSPILASQ TIHLEVMWMP
IKTAVVLIDI FNIADQKDIA KRNEKENVNV LLEKRNKSQQ DGTIDSNVKE AETPAKTIGR
FSVISTQDEL TLSSVHSLRY SAPPDVYLDN QPSSPDIKSS LRRVQTASSF DILYGKDSSD
SGDESLSGKQ IASPLSPQIS RLGNDNIKKT SCILQKSVKS SSQGLNSPNG HGSKIPTINV
TSFHSQSSYV SSDNDSEFED ADMKKELQNL REKHMKEITE LQSQQKKEIE ALYVRLGKPL
PPNVGFLHSA PPSGRRRRTS KHKLKTGKLL NPVVQQLKTS STSNISEHKD PLAKGSTRAQ
ADSAEATGLT VSTSAILESS VQTQQPCSVK ASLSSDICSG VASEGGDVRG NSGQGSSANS
LVAYPDPLPQ TTIQVQVQAN NSNNKKGTFT DDLHKLVDQW TNKTVGTVQA KPSLNQLKQN
QKRQDMEPKA NPMQTQNETC GVSGTP
//
