ID A0A1I7T4Z7_9PELO Unreviewed; 1148 AA.
AC A0A1I7T4Z7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
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.Scaffold507.g2453.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold507.g2453.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR AlphaFoldDB; A0A1I7T4Z7; -.
DR STRING; 1561998.A0A1I7T4Z7; -.
DR WBParaSite; Csp11.Scaffold507.g2453.t1; Csp11.Scaffold507.g2453.t1; Csp11.Scaffold507.g2453.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF414; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 135..410
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 749..838
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 96..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 124550 MW; 50B0A03012ABBE7F CRC64;
MSQRLEETLN EAQMKTSPES LEYLSKLVKK LLMIVSRPAR LLECLEFDPD EFYHLLEEAE
GVVREQLGSG TARVPDLPQY IIGKLGLDRD PLLDSTEHVD TPEDSISATA SGTMASKGPG
STWQETNRAP CEDDFDTIRL VSNGAYGAVY LVRHRETRQR FALKKMNKQT LMLRNQVDQV
FAERDILTMA DNPFVVSFYG SFETRQYLCM LMEYVEGGDC AALLKSAGTL PVELARLYVA
ETILAIEYLH SYGIVHRDLK PDNLLITAMG HIKLTDFGLS KIGLMNRTTL VAEGYDAVAE
TQQFQDKQLC GTPEYIAPEV ILRRGYGKPV DWWALGIILY EFLVGIVPFF GETPEALFSK
VISEEVEYPE EDEALPPEAE DLCRRLLEKN PAERLGTVNG AAQLMAHAFF ILLDFTSLLR
QKAEFVPQLD NEEDTSYFDT RTDRYNHEAE SCGEEEMIGS SAASSMMFHS FSTASPRHSI
VSIDPAHLPH LLSTANAAAK EIERSHSVSI SSRSEIRPER SYSTGQAPPD LFNISDDNTS
TAVNLRRRFS AQRHNVSTTS SSGTGSGTCF ATAASSTDSS IDASTLPIFQ PPSRASIGER
GSRSPLPKFS ISCEGDAHVT RDEHKEDEDS KDSTIVSNAS SASGADETVR YRRTSSGRTA
AAQLQLVIPS ISSSQSAPSA EPARETCYVM YPSGPSTSAG SQLSPGGASV SSASSSNDIG
SPHPTIPNSN DHPLTSQDGS IASSSPSKTI TIRKGPFGFG FTLKSVRVYL GEHSEYYTIE
HIVTAVVDGS PAHEANLQPE DMITHVNGHP VHNLTHPQLM HRLLSNGNEL ILRLVPLAST
SIREGAARRT IGKMARKKPK RPQRRVVPLE KKTRKPSALL RRLSGKRATN DIVPGSSSQK
QAFMPRSASS QDGSILTHLP GAVKTVPDPQ EPSTSSQGIV RRSVNEIEAN RPSSLRSTSS
THSHHNPTSF SSITSAPAAV ASTSTSNLTR MTSSSPSSSA SNSGTSSPAA SSSATSSGVT
MVKQKSQSIA VSPLARDTRM RSPSPSHLHH QRPSSSTYTT RPDGGAIPAT SSSQNSSVSG
QDPISFRASP NLSARRRSYQ PTTTTSMIVP PTTHHSRGFS AAAQSAQNLL NRILPRHESN
DRGGSQNK
//
