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Database: UniProt
Entry: K1RJ07_CRAGI
LinkDB: K1RJ07_CRAGI
Original site: K1RJ07_CRAGI 
ID   K1RJ07_CRAGI            Unreviewed;       491 AA.
AC   K1RJ07;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000605};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000605};
GN   ORFNames=CGI_10022111 {ECO:0000313|EMBL:EKC41560.1};
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:EKC41560.1};
RN   [1] {ECO:0000313|EMBL:EKC41560.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC41560.1};
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         ECO:0000256|PIRNR:PIRNR000605};
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         ECO:0000256|PIRNR:PIRNR000605};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000605}.
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DR   EMBL; JH823226; EKC41560.1; -; Genomic_DNA.
DR   RefSeq; XP_011422352.1; XM_011424050.2.
DR   AlphaFoldDB; K1RJ07; -.
DR   GeneID; 105324844; -.
DR   KEGG; crg:105324844; -.
DR   HOGENOM; CLU_000288_63_5_1; -.
DR   InParanoid; K1RJ07; -.
DR   OMA; CWTAMPP; -.
DR   OrthoDB; 5489497at2759; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd05584; STKc_p70S6K; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016238; Ribosomal_S6_kinase.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000605; Ribsml_S6_kin_1; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000605};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000605};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000605};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000605};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000605}.
SQ   SEQUENCE   491 AA;  54815 MW;  DA8FCCB959E05494 CRC64;
     MAGVFDLELH DTPEGDEEIS DDEFFEPELE GGSGRGQNLM CEDGMETVEI TENTVNPGEL
     KVGPQDFELL KVLGKGGYGK VFQVRKISGA DNGKIFAMKV LKKATIARNA KDTAHTKAER
     NILECVKHPF IVDLIYAFQT GGKLYLILEY LPGGELFMQL EREGIFMEDT ACFYLAEITL
     AIEHLHSQGI IYRDLKPENI LLDNTGHVKL TDFGLCKESI NEGGLTHTFC GTIEYMAPEI
     LTRSGHGKAV DWWSLGALMY DMLTGAPPFT AENRKKTIDK ILKAKLSLPP YLTNEARGLI
     KRLLKKSPQE RLGGGVDDSK PIKQHAFFRH IDWNELHQHK VEPPFKPCVT SEEDVSQFDT
     KFTRQTPVDS PDDSVLSESA NQVFVGFTYV APSVLEELNK PWISEKEPRS PRKIGSSFKA
     SMSMSPHQIN LIEGFRVAGQ MNGMDDMEVM DTTTPTIPKR STSPAIATKN TTYKQAAYPG
     AQNRPPHLRM N
//
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