ID G3P248_GASAC Unreviewed; 390 AA.
AC G3P248;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=phosphorylase kinase {ECO:0000256|ARBA:ARBA00012432};
DE EC=2.7.11.19 {ECO:0000256|ARBA:ARBA00012432};
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:ENSGACP00000011671.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000011671.1, 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:ENSGACP00000011671.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.;
CC EC=2.7.11.19; Evidence={ECO:0000256|ARBA:ARBA00001674};
CC -!- SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha,
CC beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB)
CC are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic
CC subunit, and delta is calmodulin. {ECO:0000256|ARBA:ARBA00025890}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR AlphaFoldDB; G3P248; -.
DR STRING; 69293.ENSGACP00000011671; -.
DR Ensembl; ENSGACT00000011695.1; ENSGACP00000011671.1; ENSGACG00000008802.1.
DR eggNOG; KOG0599; Eukaryota.
DR GeneTree; ENSGT00940000160435; -.
DR InParanoid; G3P248; -.
DR OMA; YHERHAP; -.
DR TreeFam; TF320349; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000008802; Expressed in diencephalon and 13 other cell types or tissues.
DR GO; GO:0005964; C:phosphorylase kinase complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0004689; F:phosphorylase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002291; Phosph_kin_gamma.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24347:SF390; PHOSPHORYLASE B KINASE GAMMA CATALYTIC CHAIN, LIVER_TESTIS ISOFORM; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01049; PHOSPHBKNASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Kinase {ECO:0000256|RuleBase:RU000304};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|RuleBase:RU000304}.
FT DOMAIN 24..291
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 390 AA; 45175 MW; 6C8632952EF1A5F4 CRC64;
MTKDFVVGDE LPDWVGAKEF YQKYDPKEVI GRGVSSVVRR CVHRHTGQEL AVKIIEITAE
KMTVLQLEEV KTSTLKEIQV LNMVKGHSSI ITLIDSYEST TFIFLVFDLM RRGELFDYLT
EKVTLSEKET RSMMRALLEA VQYLHSFNIV HRDLKPENIL LDDQGHIKLS DFGFSVQLPP
GEKLRELCGT PGYLAPEILK CSMDEMHPGY GQEVDLWACG VILFTLLAGS PPFWHRKQML
MLRMIMEGRY QFSSPEWDDR SDTVKDLISR LLVVEPAVRL TAEQALAHPF FRQYQREDVR
LFSPRKTFRV LIVSVLACIR MYGRYRRTRP LTREVLARDP YSLRGVRKLI DGCAFRIYGH
WVKKGEQQNR AALFQNTAKI MLLGLEDFET
//