ID W7FCN8_PLAF8 Unreviewed; 699 AA.
AC W7FCN8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=PFBG_03314 {ECO:0000313|EMBL:EUR70084.1};
OS Plasmodium falciparum (isolate 7G8).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57266 {ECO:0000313|EMBL:EUR70084.1, ECO:0000313|Proteomes:UP000030688};
RN [1] {ECO:0000313|Proteomes:UP000030688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7G8 {ECO:0000313|Proteomes:UP000030688};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Daily J.P., Sarr O., Ndiaye D., Ndir O., Mboup S., Lukens A.,
RA Stange-Thomann N., Mauceli E., Gnerre S., Jaffe D., Zainoun J.,
RA Wiegand R.C., Birren B., Galagan J., Lander E., Wirth D.F.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EUR70084.1, ECO:0000313|Proteomes:UP000030688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7G8 {ECO:0000313|EMBL:EUR70084.1,
RC ECO:0000313|Proteomes:UP000030688};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum 7G8.";
RL Submitted (FEB-2013) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00023596}.
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DR EMBL; KE123623; EUR70084.1; -; Genomic_DNA.
DR AlphaFoldDB; W7FCN8; -.
DR SMR; W7FCN8; -.
DR EnsemblProtists; EUR70084; EUR70084; PFBG_03314.
DR VEuPathDB; PlasmoDB:Pf7G8_110018300; -.
DR Proteomes; UP000030688; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14135; STKc_PRP4; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR044092; STKc_PRP4.
DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR PANTHER; PTHR24058:SF103; MITOGEN-ACTIVATED PROTEIN KINASE-RELATED; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:EUR70084.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:EUR70084.1}.
FT DOMAIN 365..687
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 110..151
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 227..254
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 699 AA; 81092 MW; 89309AD3A64A8FE4 CRC64;
MSKDKRNSFA SNSFDSSNDE KKSKNGNKIY KSKHEENSPD GDSYKINNNE KEKSKEKLKK
DQKKKSKEIY NSFNSPNSTS SDSDGNGLHL NFSNASSSSS ENGFKILRTQ ENEDKLLEER
RRKREALKEK LKNMVKENEQ NNDANEILQN DQINKDYNNE TFLLSENKND NDIITNEIPS
NPSYIDQNDA ACIFAPNNDV IEDTCSSLSS DHEIIEEKQN KEKPEAVKEC SDLYNDLKKK
IDEEKAKIRS FIIKQKELHE RLKMNVDDSL YVNKSKGNAD THNNLTNKKS PLENEEDEMQ
EEYDEDNDDF DMFSCVQANK KRKVEKVHIT DYYTTGNNAN LSDNWNDSEG YYKAMVGEVI
DKRYSVVCEL VGKGVFSNVL KCYDMVNKIP VAVKVIRDND MMKKAAEKEI SILKKLNQYD
KDNKRHIIRL LSSIKYKNHL CLVFEWMWGN LRIALKKYGN GHGLNATAVH CYTKQLFIAL
RHMRKCRIMH ADLKPDNILI NEKFNALKVC DLGSASDISE NEITSYLVSR FYRAPEIILG
FRYDAQIDVW SAAATVFELA TGKILFPGKS NNHMIKLMME YKGKFSHKMI KGGQFYSQHF
NENLDFLYVD RDHYSKKEVV RVISDLRPTK NITCDLLEHQ YWLKGNSPKM QFLKKKIKQL
GDLLEKCLIL DPSKRYTPDQ ALQHPYLRES IHFSKSQNE
//