ID G3NSL6_GASAC Unreviewed; 476 AA.
AC G3NSL6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000008334.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000008334.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000008334.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. RAC subfamily. {ECO:0000256|ARBA:ARBA00006935}.
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DR AlphaFoldDB; G3NSL6; -.
DR STRING; 69293.ENSGACP00000008334; -.
DR Ensembl; ENSGACT00000008353.1; ENSGACP00000008334.1; ENSGACG00000006298.1.
DR eggNOG; KOG0690; Eukaryota.
DR GeneTree; ENSGT00940000158752; -.
DR InParanoid; G3NSL6; -.
DR OMA; ITREAKN; -.
DR TreeFam; TF102004; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000006298; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01241; PH_PKB; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039026; PH_PKB.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF200; V-AKT MURINE THYMOMA VIRAL ONCOGENE HOMOLOG 1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..108
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 100..404
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 405..476
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 444..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 54812 MW; 73B50E8991D13381 CRC64;
IFEVAIKQSA TVHHRREYIK TWRPRYFLLK SDGTFIGYKE RPQDVDQLET PLNNFSVAQC
QLMKTERPKP NTFIIRCLQW TTVIERTFHV ETPEEREEWT KAIQAVAEGL QKQEEEMMDS
SPDPMDMEIY LTKPRQKVTF NSNAYSSQSL PSPPPLTPQL LFQTSAAGDL APDSVSTGFL
IPTCVDEVAH TLTENRVLQN SKHPFLTGLK YSFQTHDRLC FVMEYANGGE LFFHLSRDRV
FSEERARFYG AEIVSALDYL HAERNVVYRD LKLENLMLDK DGHIKITDFG LCKEGIKDGA
TMKTFCGTPE YLAPEVLEDN DYGRAVDWWG LGVVMYEMMC GRLPFYNQDH EKLFELILME
DIRFPRTLGP EARSLLSGLL KKEPTQRLGG GSEDAKEIMQ HKFFAGIEWQ DVYEKKLVPP
FKPQVTSETD TRYFDEEFTA QTITITPPGQ DDSMESFDSE RRPHFPQFSY SASGTA
//