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Database: UniProt
Entry: A0A3Q2C8I3_CYPVA
LinkDB: A0A3Q2C8I3_CYPVA
Original site: A0A3Q2C8I3_CYPVA 
ID   A0A3Q2C8I3_CYPVA        Unreviewed;      1285 AA.
AC   A0A3Q2C8I3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000000987.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000000987.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   STRING; 28743.ENSCVAP00000000987; -.
DR   Ensembl; ENSCVAT00000014177.1; ENSCVAP00000000987.1; ENSCVAG00000001937.1.
DR   GeneTree; ENSGT01030000234517; -.
DR   OMA; IGPACDW; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR   CDD; cd22250; ROCK_SBD; 1.
DR   CDD; cd05596; STKc_ROCK; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.20.5.730; Single helix bin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR015008; ROCK_Rho-bd_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   PANTHER; PTHR22988:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08912; Rho_Binding; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF103652; G protein-binding domain; 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.
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, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01206}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          44..306
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          307..377
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          888..956
FT                   /note="RhoBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51859"
FT   DOMAIN          1136..1191
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          1113..1132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1227..1285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          17..47
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          380..935
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          962..989
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1232..1260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1285 AA;  149221 MW;  1DB525ABA5ABFDAF CRC64;
     SMNALAHDLN YPVLRKNKNI EAFLKRYEKL VNELRELQVK LDDFEKVKLI GRGAYGEVQL
     VRHKASKKVY AMKQLSKFEM IKRSESAFFW EERHIMAFSN SPWIVQLCCA FQDDRHLYMV
     MEFMPGGDLV TLTINYDIPE KWARFYTAEV VLALDAIHSM GFIHRDVKPD NMLLDQQGHL
     KLADFGTCMR MDSTGMVHCE TAVGTPDYIS PEVLQSQGSD GIYGRECDWW SVGVFLYELL
     VGETPFYAES LIGTYGKIMN HHNSLVFPDD AEMSQDAKDL ICAFLTDRND RLGRTGVDEI
     KRHPFFKNEQ WNFDNIRDTV APVVPELHSD IDTSNFDDIA VDKGAAETFP TPRAFAGNQL
     PFIGFTYFKD DQHFFLSFPS EQLLEKVNQL EEQLDHEMQE LRLEASLRQL ERERALLQQQ
     SAENLRKVEM EADRKRILEN QINCLKDQLE DMKKKNRDSH IFNENNVQLQ KQLEEANSAL
     QAEQKATALL KKSQSEAQKQ AQNLEVSLKE MEKKCSSLEA NKAEQEKQIW ELQAELEEEK
     RERNLSTEAL ADLQVTISVL EDEVKEAKSS LSKVKDEKKE LQTKLNNLEK EKNKQEIDLT
     FKLKSLQQSL EQEEAEHKAT KAKLSDKKET YQSIEEAKSE ALKEMESTLE EERSLKQQVE
     ENLLQLKKDH SMLEWDHKQA QQKLDELQAQ KEKLSEEVMD LTLRLEQEIQ KRSKSQSELK
     AHKQQVSVLT SSEKQLKQEF NQLLDMKQSL EKQNQELRRE KQEADGQLKE LMDQLEDEQN
     FNTLYRKQIH ELKDENDEKN KMYQEAQQQL AEYQEERASM AAQLESSLKK ADSERLARSV
     AEEQYSDLEK EKIMKELEIK DMMARHKQEL NEKEATITSL EESNRTLTVD VGNLASEKEE
     LNNQLKELEQ ELQKAKETEK KIESQKLSLE KQIQTEKTLK IQAVNKLSEV MAKRKDQERG
     GIRIVNSEVH KTKQENRKLQ QDLKAERQKI NSILFKHQKE LEDVQALLVD ESHHCQELQM
     ILDSRESDIE HLRCQLTSLS VHSLDTTSIS SNNDLEIISP CIIEHLKILL HGFPFFLLKL
     FHVRPITQTD CYRADVKEIP RIFQILYANE GESKREQEEA EESSPSERSP FVSHKGHEFV
     GTIYHLPSSC DACSRPLWNV FKPPAALECR CCHAKFHRDH LDKKEEVIPP CKVNYDVSTA
     KDLLLLTGSQ TEQQRWVRHL LKRIPRKTST LSPPPAARNI SDDSLPRSSP QVSPHSSPRT
     SPRLSHRRAI KVQSTRHQQT SENSR
//
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