ID A0A3B4DP37_PYGNA Unreviewed; 417 AA.
AC A0A3B4DP37;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000024876.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000024876.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily.
CC {ECO:0000256|ARBA:ARBA00005926}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_017561868.1; XM_017706379.1.
DR AlphaFoldDB; A0A3B4DP37; -.
DR Ensembl; ENSPNAT00000009030.1; ENSPNAP00000024876.1; ENSPNAG00000009710.1.
DR GeneID; 108432511; -.
DR CTD; 554152; -.
DR GeneTree; ENSGT00940000156470; -.
DR OMA; AANNKHK; -.
DR OrthoDB; 1534388at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14126; STKc_CK1_gamma; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR022247; Casein_kinase-1_gamma_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11909:SF157; CASEIN KINASE I ISOFORM GAMMA-2; 1.
DR PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR Pfam; PF12605; CK1gamma_C; 1.
DR Pfam; PF00069; Pkinase; 1.
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}; Kinase {ECO:0000256|RuleBase:RU000304};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|RuleBase:RU000304};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 48..318
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..382
FT /note="Polar residues"
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 417 AA; 47578 MW; 5B21E2D2C759AFFB CRC64;
MDFDKRGGGG GKGEVEEGKR MSKTASRAGH GGRSSATNSG VLMVGPNFRV GKKIGCGNFG
ELRLGKNLYT NEYVAIKLEP IKSRAPQLHL EYRFYKQLGN SEGVPQVYYF GPCGKYNAMV
LELLGPSLED LFDLCDRTFS LKTVLMIAIQ LITRMEYVHT RSLIYRDVKP ENFLVGRPGS
KRQHTIHIID FGLAKEYIDP ETKKHIPYRE HKSLTGTARY MSINTHLGKE QSRRDDLEAL
GHMFMYFLRG SLPWQGLKAD TLKERYQKIG DTKRATPIEV LCESFPEEMA TYLRYVRRLD
FFEKPDYDYL RKLFTDLFDR NGYVFDYEYD WVGKPLPTPI GPIPSDTPLQ PSSRDKAQQH
TKNQVMSSTN GEVNTDDPTA GHSNAPITAP AEVEVADDTK CCCFFKRRKR KALQRHK
//