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Database: UniProt
Entry: W6LGL5_9TRYP
LinkDB: W6LGL5_9TRYP
Original site: W6LGL5_9TRYP 
ID   W6LGL5_9TRYP            Unreviewed;       342 AA.
AC   W6LGL5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=GSHART1_T00008325001 {ECO:0000313|EMBL:CCW70666.1};
OS   Phytomonas sp. Hart1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW70666.1};
RN   [1] {ECO:0000313|EMBL:CCW70666.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW70666.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW70666.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW70666.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; HF955207; CCW70666.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6LGL5; -.
DR   EnsemblProtists; CCW70666; CCW70666; GSHART1_T00008325001.
DR   OrthoDB; 168943at2759; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44899; CAMK FAMILY PROTEIN KINASE; 1.
DR   PANTHER; PTHR44899:SF3; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..156
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          223..340
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
SQ   SEQUENCE   342 AA;  38595 MW;  AA8919C9F408C287 CRC64;
     MIHRDVKSAN MFLTSHGIIK LGDFGFSKRF ETTISSETVT GTFLGTPFYL SPEMWEGKRY
     GKKADIWAAG IILYEMLMDG ARPFSAVGPT ELRDSVLHQD VGLVEAPPAS LGASPDPGPP
     RRGPFSLEMR ELVRSIFTKD PHERPDAGRL LRTPVMQYYL HVFERHVQSL MALDARALEQ
     DADALDGLAF RDPSERDLVL RNIEEAKHLI EAAMPRGLHE RDSLRYEGVV YKRNNDGSWK
     ERYLILSEDF FIISLSRTKE AADGTERSRK VPLKLIKSVS RCAVTDLLSK SSEAGEGGKK
     VHPAYAFTLF MIESSQPIFF GVQKEEELYH WTNCLTKALK ID
//
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