ID K1P7T4_CRAGI Unreviewed; 1228 AA.
AC K1P7T4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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_10007692 {ECO:0000313|EMBL:EKC19757.1};
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:EKC19757.1};
RN [1] {ECO:0000313|EMBL:EKC19757.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC19757.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; JH816092; EKC19757.1; -; Genomic_DNA.
DR AlphaFoldDB; K1P7T4; -.
DR HOGENOM; CLU_000192_7_2_1; -.
DR InParanoid; K1P7T4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; 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 CDD; cd01379; MYSc_Myo3; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036083; MYSc_Myo3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46256; AGAP011099-PA; 1.
DR PANTHER; PTHR46256:SF3; MYOSIN III; 1.
DR Pfam; PF00612; IQ; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..722
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 600..622
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 92..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1228 AA; 139990 MW; CEF947A72E36E9C4 CRC64;
MRTYKALQTE SMETIVSQLD SRYSQGQIYT YIGDILLAVN PFRPLVIYTE EYSLKYKNAS
KEDNPPHIFA VADQSYQSMM HNKKNQCIVI SGESGAGKTE SANLLVQQLT QLGKAANRNL
EDRILQVNPL MEAFGNAKTV INDNSSRFGK YLEMFFTNNG MVVGAKITEY LLEKSRVISQ
AIGEQNFHVF YYIYNGLSPS ERAEYNLKEN TRYRYIDEYS SQNPDVSSLS VNRVKFKAIE
HCFDIIGFKP EEVKAVYSVI CAILHTGNID FDEKETTDHK GDACVITNMD LVNTISHLLG
IPAIDLVESL TTTGMVARGE LIVRDNSVPE AIDARDAMAK ALYGRLFSWI VNRINSLLKP
STMGRDDNQP IIGLLDIFGF ENFPKNSFEQ LLINIANEQI QYYFNQHIFA WELQEYRGEG
LEGVNISFVD NRPLLDMFLM KPLGLLALLD EESHFPKATD MSLVEKFHKN IQNNNYSRPK
GNNLTFSIDH YAGTVVYDAM GFLEKNRDRL PGDVVSMLRA SKNEVIRSLF STPLTKTGNL
ADGTIRSSRQ TPASSPGTSG PIQIMSYNSK SSSMGGSRGS GSTSMTKIQQ TVATYFRFSL
MDLLAKMVAG SPHFVRCIRP NEQKLPDDFE PDKVTTQLRY TGVLETTRIR REGYSHRIPF
GEFLKRYSML AFRWDEKVEH TRDCCFTLLD RLNMSMYQLG KTKVFLKYYH VEQLARLYEQ
RNKKITCIQA TIRRFLAINQ FHRLKWQREK AVTKIQALFR GYMVRKKMKP MIEERKKAAT
TIQARIRGYF VRNKQKKSQK EQESALKIQR AFRSHKAKKA SKKEQALRQG DREGAAVLIQ
SYVRMWQTRV KYLKLQDFEF QKEVQLSLFA QQVELYNKEK LDILMRNNSP VHSPSSKPSN
DDTAIYAQPQ KRRAPPPPIA PAKVEKPPPD VGEERLDHMK KMKELKPVMP TLETNYYDQI
NGVKSPVVNG YHDEEEVREI PQQPVEAPQT KKKEEIRHEA VPESSVRKDS PVLIVKAEVH
PQPQLPDHLR KRGSYEVPKD QVIDWDIPLV EAHNQSFRDR RKPKAGTEEF ERTRAARSIA
EAILANGSLT NGQQSMSGIS KDPASFREEF YKESNRQEMV KTLERQVSNS SVGQWNHRQR
QDGEQERDGV LQPPVPPPAP PPPPPMKRDP PTFFIPPPPT DPPPPIPTSV TPPFSIEIPL
TNGNPPMNNG IPNGVASPTA LAKVKFQL
//
