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Database: UniProt
Entry: K1QUN1_CRAGI
LinkDB: K1QUN1_CRAGI
Original site: K1QUN1_CRAGI 
ID   K1QUN1_CRAGI            Unreviewed;       827 AA.
AC   K1QUN1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
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   ORFNames=CGI_10019662 {ECO:0000313|EMBL:EKC25276.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC25276.1};
RN   [1] {ECO:0000313|EMBL:EKC25276.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC25276.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   EMBL; JH817691; EKC25276.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1QUN1; -.
DR   HOGENOM; CLU_006347_1_1_1; -.
DR   InParanoid; K1QUN1; -.
DR   OMA; NDESVHC; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06613; STKc_MAP4K3_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR021160; MAPKKKK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR48012:SF18; HAPPYHOUR, ISOFORM A; 1.
DR   PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF038172; MAPKKKK; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:EKC25276.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000313|EMBL:EKC25276.1}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKC25276.1"
SQ   SEQUENCE   827 AA;  93327 MW;  A0B2302362B6C023 CRC64;
     ARNFSTGELA AIKVIKLEPG DDFAIIQQEI VMMKDCKHSN IVAYFGSYLR RDKLWIAMEY
     CGGGSMQDIY HITGPLTEPQ IGFICRETLK GLMYLHNRGK MHRDIKGANI LLTDEGDIKL
     ADFGVSAQIT QTMCKRKSFI GTPYWMAPEV AAVERKGGYN QQCDIWAVGI TAIEFAELQP
     PMFDLHPMRA LFLMSKSGFK PPQLKDKNKW SQVFQHFIKV ALTKNPKKRP TADKLLEHPF
     VLSDHLSRNS TRELLDRVHN PTSPGDFDLQ EDDDGVLQNV PRRISSQNSS QSSAARNSLE
     FQVNIPTEHD GDFKTAHSYL DDPVSEMGLL DSVNEELIQR GHENQMSVPA EDIPLSEQST
     LQIKPPPRLP KPLPQLPKDD KPEDDGSPRF DDHGPDLDAI LDRELTLVPG ARPPKEADDK
     PPELPPKLSK RQNGVLDLGT GAGGGGATEE PPPAVPRRKD RASNMNKADR PVSNGLPPTP
     KVHMGACFSK VFNGCPLQIN CTASWVHPDT RDQHILIGAN EGLYTLNLNE IHESSLELLH
     ARRCIWVYVI KDVLMTLSGK TTCLFRHDLK MLHSKQANRL SLPMNKIPEK LIPRKFNHTT
     KVPDTKGCTQ CCVGRNPYNG YRYLCGALPH GIILMQWYDP LNKFMLLKTF DWDSIPLQPS
     VFEMFISPEL EYPMVCMGVR QSSTEMNQLK FDIINLNSSS LWFTEQNDND QLLPVVNVTQ
     LEKDTILVCY DNFVRVVNLR GKLKSSRKQS SELHFDFKVE SLVCLQDSVL AFHKHGMQGR
     SFKANEVTQE ICDRTRNFRV ILLESRPSDS PSVESNLYVL AGHENNF
//
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