ID A0A3B4YLA2_SERLL Unreviewed; 1075 AA.
AC A0A3B4YLA2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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 Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000031355.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000031355.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B4YLA2; -.
DR STRING; 1841481.ENSSLDP00000031355; -.
DR Ensembl; ENSSLDT00000032251.1; ENSSLDP00000031355.1; ENSSLDG00000024081.1.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000261360; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR CDD; cd11638; HR1_ROCK2; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR Gene3D; 1.20.5.340; -; 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; 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; IPR037311; ROCK2_HR1.
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; PF00433; Pkinase_C; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01206};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 48..310
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 311..381
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 908..962
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT REGION 606..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1075 AA; 124413 MW; 115891B1EB949F5F CRC64;
LLHDSMNALV LDLDYPALRK NKNIETFLNR YEKVIGQIRD LQMKSEDFDR VKVIGRGAFG
EVQLVRHKAS QKVYAMKLLS KFEMIKRSDS AFFWEERDIM AFANSPWVVQ LCCAFQDEHF
LYMVMEYMPG GDLVNLTSTY DVPEKWAKFY TAEVVMALDA IHSMGFIHRD VKPDNMLLDR
LGHLKLADFG TCMKMDATGM VHCDTAVGTP DYISPEVLKS QGGDGYYGRE CDWWSVGVFI
FEMLVGDTPF YADSLVGTYS KIMDHKNSLN FPDDVEISKD AKNIICAFLT DREVRLGRNG
VEEIKRHPFF KNDQWTFNTI RETVAPVVPE LSSDIDTSNF DEIEDDKGDV ETFPKPKAFV
GNQLPFVGFT YFKEDHSPSH KDLCDWLIFF FLQSAALQKK LRHLEVQINN DKQVKDDLEH
KYRYSSCCSN NTLEHSGSNC QNGRKNLESS MRQLEREKAL LQHKSLESHR KAESEADRKR
CLENEVNSLR DQLDDMKRRN QNSHISNEKN IHLQKQLEEA NTLLRAESEA ATRLRKTQTE
SSKQLQQLEA NVRELQDKCC LLERSKLSLE KECISLQAAL ETERREHSQG SETISDLMGR
ISGLEEEARQ QRQTLSKAEA EKRQLQEKHT DLEKSNKEID LTYKLKVLQQ ELEQEESSHK
ATRALLADKS KIKVTIEGAK SESMKEMEQK LAEERVAKLR LENRILELEK HSSMMDCDYK
QALQKLDELR RHKDRLTEEV KNLTLKIEQE TQKRTLTQND LKAQNQQLST LRTSEKQLKQ
ETNHLLDIKR SLEKQNQELR KSTLYKTQVR ELKEECEERN KLTKDVQQSL QELQEERDSL
AAQLEITLTK ADSEQLARSI AEEQYSDLEK EKIMKELELK EMMARHRQEL AEKDITISSL
EEANRTLTSD VANLANEKEE LNNKLREAIE DPEALLQPDN SETHVRLQAV NKLAEIMNRK
EVRGGGSRRG NDTDMRRKEK ENRKLQLELR SEKEKLNSTI IKYQREINEM QAQLADESQM
RIELQMALDS KDSDIEQLRN LLQSLSVQSM DSASVSSGPE FDADDAFAGK SLTTV
//
