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Database: UniProt
Entry: A0A158Q2K0_DRAME
LinkDB: A0A158Q2K0_DRAME
Original site: A0A158Q2K0_DRAME 
ID   A0A158Q2K0_DRAME        Unreviewed;       831 AA.
AC   A0A158Q2K0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000029801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000029801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-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};
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DR   AlphaFoldDB; A0A158Q2K0; -.
DR   WBParaSite; DME_0000029801-mRNA-1; DME_0000029801-mRNA-1; DME_0000029801.
DR   Proteomes; UP000038040; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd20809; C1_MRCK; 1.
DR   CDD; cd00132; CRIB; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   PANTHER; PTHR22988:SF66; SERINE_THREONINE-PROTEIN KINASE GENGHIS KHAN; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00285; PBD; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          69..119
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          307..592
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   DOMAIN          669..682
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   REGION          645..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  91957 MW;  FF59205D4B7EEA7D CRC64;
     LNIIDLNAKI FLYFLNFSAS TSHSSATYEN AHVGTPTPST ASTLVLGTQG RGASPKVIQS
     LNNALNGKGH RFSHVHLQTP SKCAHCTSIL IGLDRQGLFC QDCQYACHVH CAPKVPTSCP
     VPPEARRPLG IDPQKGVGTA YEGLVKTPKP AGVKRGWQST YVVVCDFKLY LYDCNIDKHG
     KAIDIHPMIR QVFFVLDMRD PDFNVSSVIE SDVIHASKSD LPKIFRVTTS QIHSMLPTVT
     VNTTGSNSSN GSAGSDTPIA RHLTFQEKTK WVIALNELKN LLRKSKLVDK SAFLVKEVFD
     SLTFRELRNA QCATVLDKSK IVMGFADYGL YAIDLDREIL VPIGGERENN KRTVEQIEYN
     ADEQLFVAMV GVVKERHIRL IPTAALDGRD LKWIKVADTK GCHLLTLGAG SSNDPHNYFC
     VAVKKTVLVY QIDRSEKRHR KVRDLAMPGH PQTISIMRGK LCVGYPSGFR MWDLADNSTT
     ALVNLEDASL QFLNQTLYDA HLIINVSGYE QKEFLLIFSR LGVYVDAQGR RCRSQELMFP
     SEASSGGFSC IMPHLCVYSE NEIDVFNVNS AEWVQTINLR KASPLTSDGR LTVCVINDLP
     YVVLLSDVLS DEDVLSLPDW TQPSIANIPS SSSLIKGITA KRRRKFSMKT PREDDRYGRS
     GDRRSQLPIS GPSDFVHIVH MGPGAGLELQ NLIDLKNSNP SHVTSSSSLG SGAADKVRQL
     INPIMRSTSS TTTNLHGVHQ LTNTSRREIE LMQSKSRPLS SHSKGSDGIG VLPKASITST
     NSHFLELKAV QKDAVKTNQL HWDTTTEPCL PSRSRSSLQI KQKRHNSQHD F
//
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