ID A0A3Q3FBK9_KRYMA Unreviewed; 423 AA.
AC A0A3Q3FBK9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine/threonine-protein kinase Sgk1-like {ECO:0000313|Ensembl:ENSKMAP00000010737.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000010737.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000010737.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR RefSeq; XP_017297621.1; XM_017442132.1.
DR AlphaFoldDB; A0A3Q3FBK9; -.
DR Ensembl; ENSKMAT00000010899.1; ENSKMAP00000010737.1; ENSKMAG00000008030.1.
DR GeneID; 108251730; -.
DR KEGG; kmr:108251730; -.
DR GeneTree; ENSGT00940000164496; -.
DR OrthoDB; 3028764at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05575; STKc_SGK; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 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; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF188; SERINE_THREONINE-PROTEIN KINASE SGK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 91..348
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 349..423
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 423 AA; 48132 MW; 056209ACAE6639C6 CRC64;
MAVTEAGCDL TYCKMRGIVA VLTAFIKERK MGLNDFIQKL VSTPHICQHV EVNNFLKIDE
NQNEEDEDGG PMCLNPRSSL AEDFQTKPCD FDYLKIIGKG SFGKVLLARH KETAKYYAVK
VLQKKIILKK KEQKHIMAER SVLMKNIKHP FLVGLHYCFQ TADKLYFVLD YVNGGELFYH
LQRERIFLEP RARFYAAEIA SALGYLHSLH IVYRDLKPEN ILLDSQGHIV LTDFGLCKEG
LEPNGTTTTF CGTPEYLAPE VLQKQAYDRT VDWWCLGSVL YEMLYGLPPF YSRNTAEMYN
NILHKAPVLK PNVSNAGREL LEGLLQKDCT KRLGARDDFL ELKYHSFFSP INWDDLMARK
ITPPFIPSVS GPTDLRHFDP EFTHLPVSSS LCSDTVMVTS SLKEAAGAFP GFSYGPPEEH
SFM
//
