ID A0A0L8ICJ6_OCTBM Unreviewed; 551 AA.
AC A0A0L8ICJ6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=OCBIM_22023314mg {ECO:0000313|EMBL:KOF98750.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF98750.1};
RN [1] {ECO:0000313|EMBL:KOF98750.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF98750.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF98750.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; KQ416087; KOF98750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8ICJ6; -.
DR STRING; 37653.A0A0L8ICJ6; -.
DR EnsemblMetazoa; Ocbimv22023314m; Ocbimv22023314m.p; Ocbimv22023314m.g.
DR EnsemblMetazoa; XM_014924703.1; XP_014780189.1; LOC106876226.
DR OMA; WRISAKN; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd20813; C1_ROCK; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.730; Single helix bin; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF73; RHO-ASSOCIATED PROTEIN KINASE; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF103652; G protein-binding domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01206, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 136..202
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 416..471
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 201..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..192
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 551 AA; 62817 MW; A441E9241FEB5B40 CRC64;
MKFDQWKPTI LQNAGKLGNC TRSQADLAWF LQLDALPNTK SFLVPKAPKG SGQCPSLNYI
ARQERPVTYK LEPLSSCSDV GSAKHSCPMN SQLRQLVFSM CVNKGLLIGE QQYQCMYAHV
CGGRKTELED SKREYGKNNE QLQNEKDDLI NKMNKMADDL KNEKSENNIS EIEQLRKLLQ
DERLKKIQAV NKLAEVMNRK EFADKSKKPT NSNSGALRKR DKECRRLQQE LTMEREKYTK
MVEKFQRDIS EMVTQMNDEM QAKAKLQMEL DAKDSEIEQL QQKLANPDNT SVNSGSVEEF
GAEDGLTDNV MEGRLAIPHK PSTKKLIWKK QFVVASSRKI LFYNTPNDKQ NSDPVMVLDI
DKLFHVRPVT QGDVYRADSK DIPRIFQILY ATEGENIKPG ETAQESQDRT GFSYKGHDLI
PIHYRIPATC DSCNKPVWHV IHPPAALECK RCHVKVHREH YEKEEEFIGY CKVNYDIQAK
ELLLLAESSE KQKSWVQHLG RKIPKKGITP AGSSSSSVVP SRSLRQYSSY GPLHRHSSVG
KSATLPPNTR P
//
