ID A0A1I7TFL6_9PELO Unreviewed; 831 AA.
AC A0A1I7TFL6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold601.g5456.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold601.g5456.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway.
CC {ECO:0000256|PIRNR:PIRNR038172}.
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 ECO:0000256|PIRNR:PIRNR038172};
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 ECO:0000256|PIRNR:PIRNR038172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000256|ARBA:ARBA00008874,
CC ECO:0000256|PIRNR:PIRNR038172}.
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DR AlphaFoldDB; A0A1I7TFL6; -.
DR STRING; 1561998.A0A1I7TFL6; -.
DR WBParaSite; Csp11.Scaffold601.g5456.t1; Csp11.Scaffold601.g5456.t1; Csp11.Scaffold601.g5456.
DR eggNOG; KOG0576; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06613; STKc_MAP4K3_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF18; HAPPYHOUR, ISOFORM A; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 2.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 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|PIRNR:PIRNR038172};
KW Kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT DOMAIN 15..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 481..800
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 831 AA; 92303 MW; DF5AEA7867ADA48C CRC64;
MSADVIKRSN PADDYELLQR VGSGTYGEVY KARDIRSDTL AAVKVVKLEA GDNFAVIQQE
IMVIRECSHP NIIAYFGSYI RRDRLWIVME YCGGGSLQDI YHLTGPLSEL QIAFVCRETL
RGLNYLHNIG KIHRDIKGAN ILLSSNGDVK LADFGVAAQI TATIGKRKSF IGTPYWMAPE
VACVEKRGGY GMQCDVWATG ITAIELGECQ PPLFDLHPMQ VLYLMTKSGY KPPHLKDKHR
WSPLFHDFVR QCLTKSAKKR PSPEKLLTTH PFVLGSLSSR MTRDLLDKVN GASPDVYDRM
SKTVDDLTEE ESDMDDAPSL LTPDAAPIRI GLPAHLNGLR LDARCLEQLS SSPHSSSSET
DRKTPTATPK GLNRGYHSER TLPAKEMPSL PDVVGGDALL HCGSGNGVII DDDETIRAPR
APPRTLRAAQ KAAASGSENR FSSTSIASTP SEDSLSTFFG MPIIPKVPMG ACFSKIIDGT
ELKINCAASW VHPLTGAHLL LFGTEQGIYS FDTNCMPDGN LTKIHHRRCS WMYVYSDRLT
AIQGNTPYLY RHDLVALTQK NLTLKMSKNL NKIPEKYVPK RLAITVRMPE TRGALQCTVK
QGEGAHANSI FLCCAVPKTA HLFQWYKPMN QFVLVRSEPL QDDIRFPIRP FSLVNSRTSD
FPELCIGVGK MSGSSEYQFN MINFCSSTRN SEASDGFNSS FGSLAEDEML EVNNMHQINR
DTLCFSFRNK VVLTDLEGFE RPKPSIFTFN FHIEYLHVVD GTVLAFHSNG VQGRDLKTNL
NTQDLSDVSR LYRVIGDDRV IVLRSQLMSA RNAGDTCDIS LLMGHSDTPV L
//
