ID K1R5J3_CRAGI Unreviewed; 2293 AA.
AC K1R5J3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CGI_10026610 {ECO:0000313|EMBL:EKC38809.1};
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:EKC38809.1};
RN [1] {ECO:0000313|EMBL:EKC38809.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC38809.1};
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};
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DR EMBL; JH816764; EKC38809.1; -; Genomic_DNA.
DR HOGENOM; CLU_000987_0_0_1; -.
DR InParanoid; K1R5J3; -.
DR OMA; GEEVIWC; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF169; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKC38809.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKC38809.1}.
SQ SEQUENCE 2293 AA; 260322 MW; C0F7DFABD04FAD0C CRC64;
MDEIFMISMG DFTGEELIQA AIFNDAELMK CLLEGECVNF INFQDRRGRT AVYTSVSNNS
SRCLRILLEH GADPNIAALK TFNFMTPLHQ AIIDLKLDIF KLLLSYGADI TKPDGSGLSP
MALAENMELN DYLQEMEEEQ AFAEACRAAD TSKMATILET NTSPTMHAKL VLNTVTEDGL
TPVCWACKSG NVDMVDLLLR HHASTISCTS QEMTPIHIAC HFENTDCVKL LLQHCPDIVQ
RKMSNESLAL HLAIEAGNLS LVQLLLYHDY PEYALEDHRD EALGISYKLP FDVNTKDSIG
RSPLYVAAEK NQVEIVRCLL DFCVQCERKQ QPKKYEGRNR QASNVNFEPE LRREQLKASG
SHSGVFASNI YHPVDINLQG RNGFTPLHVA VSSSFYEVTD ILLKHKADVN ILANDNGKLI
STLMMACKKG DSIILDKLFK YGADDLDKQV FEYAVEKRPR MVFTLLKYRT FKDLENEYKI
NKMDMRLLYR QMSDLEDSYD GLNSLNLDFK KFKFPVNSVH IKWQDLQHID ALKEDTLVDI
SSHHNPELQA TSLSNPFALF AITKIDISGN KIGPMFPAVF FKLPSLHYLN LSKNQIKMFP
DVSDNDHLFV CLEELLLDRN KIEVLPDYLF KVSTLRFLSV SYNSVKDIPC DIWELQCLAF
LNLANNMIAS LPQPRPRQSR PPSQGNPSNV PNYFEDDSIP NQAPTPKSDV EETEVKHALI
WMSGSVHVSD NDFDIGSGPR NRGLQDLNLS KNRLKEIPFW LCCTSPFMEN LNLSSNQISS
VGRLFQLPQH LKTLDLSGNN LADTVNWQCF EDNDGLCYST RSVRPTNSPH SFSSYTSFTQ
LMTCAHRQHR ILERLDTLNL GGNRRLEKVV VSRATDNRQR RSSAASLSSL NSSLDEEKRR
LLFPNLTSLD LSYNIGLQEI PSEIGDLSSL KRLSLSFTGV KELPPNIGKL KSLFTLDLEK
CNLEGPILDI IHGSPMRTKD ILGFLLSVLE DQRIDKTATG MRQDGNTLST VGIDINEIVI
GERWANGPVT FRTWDFGGQK EYYATHQYFL SPRSLYLVMW KLTDGEQGIQ TIWQWLVSIQ
ARAPGSPVII IGTHRDFLTN RKTRSNFPAS FEDDMKEIIV RQFINVEEPD KCGLPFVIGQ
FNVSCKSGEN VKELVNFIYS RVFQLKHPRR NKEKLLQHKI PKKYLILKDI VQELAEERIH
EEKDPVLDKS SYMLKTMHKM MERSGTLFRD PEDVEQATRF LHENGILFHY EDLTLKDRYF
LDPQWLCDQL ARVVTVDQVN NFAQNDETLR RTKNSLPGSG SPNSSMYQRP GGSLGFVNSH
PSSNVIFSHC RLYVMTYFPS GFWPRLITRI LADKSLYEIV TDLFPIPSEV LEACPYLKTK
EPYWQPWQTG VQLLCHNTVL FRIKEVLPGL SGFCDYQRTA LKCWIDNRWS PIDMENSVVL
EIGFPCDSIE FTFADRGASQ HGMCAITKKI KVCLEERASA KFLVKMSEHI DNLLQDWYPE
IGESRFVQNC YGRYLITRVI PCPHCLFEVV RKERKNDTTL YWQFVDQNLD ITSTISLSEI
MLDESTLDQR EETSKNNMYC FLVEKCILNC LNDHNEICPL HGSMSPRFMM SQDGVARTLY
IAPEILFSDL DTSILIGPAD TLTLVKLVGK GAFGEVYQGK LRKVDEPIKD VAVKMLCGPF
KDASLQSKGQ TDLHMENATS AYLTARQEIS ILQTIDHQNI VPLLGLSLRP LALVLSLAPL
GSLGNKLLQI GNDGRRLSVY AIKQIVLQVA DALSYLHCRS IIYRDLKADN VLVWQMNGFD
FSEDTLDPIH VKLADYGVSR TVQSSGTKGF GGTPPFIAPE ILQFAGKAQY TEKELSYPSH
FLDLMSISWS HDPAERPSAE RIKQMVQCPQ FCHLIDAISM DTSVNILSAC CVSVEKEMDN
ENDDVFDDHD FLPTNTTKEI WLSTAPTNGN SRIEIYCYDR VFRSTINKLK ATLKDLIYVD
TVVLSSLAKE IKMITCGFDF KIRFLTSQIL RAESQSQVVF VLTSVKGGVL VIIEVDSVNL
TVSTRQNIVP GKCICACLVP KEDGNQEIWC GQTEGKILVQ DYKDLTKSEQ IVETNDIVNM
HRNCQFLESA MVGDRQYVWS YNYPGTTVSC WNVKTKEVEA ELNCADVVPI TESGSLHAYF
TNNLEARKYQ VTAMRVSDKY LYVGTTSGCV IVADAVELKP YTVFCCHSSE DFYVRTIVPM
QENEQSDSQF MKHGIPYGIV TVGKGYRDLI LKPETEMEHN FLQAFANRPG SPRKSVKNPT
YILSWHAKNW EYY
//
