ID G0N0M7_CAEBE Unreviewed; 567 AA.
AC G0N0M7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=Cbn-gck-3 {ECO:0000313|EMBL:EGT49130.1};
GN ORFNames=CAEBREN_17876 {ECO:0000313|EMBL:EGT49130.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; GL379825; EGT49130.1; -; Genomic_DNA.
DR AlphaFoldDB; G0N0M7; -.
DR STRING; 135651.G0N0M7; -.
DR EnsemblMetazoa; CBN17876.1; CBN17876.1; WBGene00156601.
DR eggNOG; KOG0582; Eukaryota.
DR HOGENOM; CLU_000288_111_2_1; -.
DR InParanoid; G0N0M7; -.
DR OMA; KMRTANC; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019901; F:protein kinase binding; IEA:EnsemblMetazoa.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0060562; P:epithelial tube morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0006972; P:hyperosmotic response; IEA:EnsemblMetazoa.
DR GO; GO:0050891; P:multicellular organismal-level water homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
DR CDD; cd06610; STKc_OSR1_SPAK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF16; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF12202; OSR1_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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 101..379
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 567 AA; 61992 MW; D71B6724F32AE3DC CRC64;
MSSTNLAGSG SAAGANNTVT SEYSTTQTTT GTYHTDTLSS VGGTSIASSA PSLSSQAPST
VHASGAAPPV SSPIAAAAAA SAALVAQLNP ADRWPTEPSA YKLDESIGVG ATATVFTAYC
LPRNEKVAIK CINLEKCQTS VDELSHEIQA MSQCNHPNVV NYYTSFIAQE ELWVVMRLLN
CGSMLDILKR KVKAIGKEQA QFGVLDEVSI ATVLREVLKG LEYFHLNGQI HRDIKAGNIL
LADDGTIQIA DFGVSGWLAS SGGDLSRQKV RHTFVGTPCW MAPEVMEQVQ GYDFKADIWS
LGILAIELAT GTAPYHKYPP MKVLMLTLQN DPPTLETNAE RKDQYKAYGK SFKTLIRDCL
QKDPAKRPTA SELLKYSFFK KAKDKKYLVH TLIENLASVP VVSHHSSKKV ASGKLRKDAH
GNWEFEYDSP QESDSDEDEE REKKKKSDQQ ATVTAQQSIQ DTSNQSTETL NMVLRVRNQQ
RELNDIKFDY TKSADTVEGI AHELVTAELI DCHDLVIVAA NLQKLIDFAE QKLDRRSITF
ALNSGVHANE VPDERTLTGF AQISLLD
//
