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Database: UniProt
Entry: F8QMD6_TOXGO
LinkDB: F8QMD6_TOXGO
Original site: F8QMD6_TOXGO 
ID   F8QMD6_TOXGO            Unreviewed;       554 AA.
AC   F8QMD6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=rop18 {ECO:0000313|EMBL:ADH04610.1};
OS   Toxoplasma gondii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=5811 {ECO:0000313|EMBL:ADH04610.1};
RN   [1] {ECO:0000313|EMBL:ADH04610.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=QHO {ECO:0000313|EMBL:ADH04610.1};
RA   Liu M., Peng G., Yuan Z., He X., Zhu X.;
RT   "Genetic variation and phylogenetic relationship of Toxoplasma gondii
RT   isolated from Guangzhou in mainland China based on rop16 and rop18 genes.";
RL   Submitted (JUN-2009) 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};
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DR   EMBL; GQ243205; ADH04610.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8QMD6; -.
DR   VEuPathDB; ToxoDB:TGARI_205250; -.
DR   VEuPathDB; ToxoDB:TGCOUG_205250; -.
DR   VEuPathDB; ToxoDB:TGDOM2_205250; -.
DR   VEuPathDB; ToxoDB:TGMAS_205250; -.
DR   VEuPathDB; ToxoDB:TGME49_205250; -.
DR   VEuPathDB; ToxoDB:TGP89_205250; -.
DR   VEuPathDB; ToxoDB:TGPRC2_205250; -.
DR   VEuPathDB; ToxoDB:TGVEG_205250; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR027916; Kinase-like_dom_Apicomplexa.
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   PANTHER; PTHR24349:SF569; MAP KINASE-ACTIVATED PROTEIN KINASE 2; 1.
DR   PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF14531; Kinase-like; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          252..531
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   554 AA;  62637 MW;  C038ACBF64B44E0C CRC64;
     MFSVQRPPLT RTVVRMGLAT LLPKTACLAV LNVALVFLLF QVQDGTGITL DPSKLDSKPT
     SLDSQQHVAD KRWPATAGHY KYLAGATEST RDVSLLEERA QHRVNAQETN QRRTIFQRLL
     NLLRRRERDG EVSGSAADSS SRPRLSVRQR LAQLWRKAKS FFTRGIPRYF SQGRNRLRSL
     RAQRRRSELF FEKADSGCVI GKRILAHMQE QIGQPQALGN SERLDRILTV AAWPPDVPER
     FVSVTTGETR TLVRGAPLGS GGFATVYEAT DVETNEELAV KVFMSEKEPT DETMRDLQRE
     SFCYRNFSLA KTAKDAQERC RFMVPSDVVM LEGQPASTEV VIGLTTRWVP NYFLLMMRAE
     TDMSKVISWV FGDASVNNSE LGLVVRMYLS SQAIRLVANV QAQGIVHTDI KPANFLLLKD
     GRLFLGDFGT YRINNSVGPA IGTPGYEPPE RPFQTTDITY TFTTDAWQLG ITLYCIWCKE
     RPTPADGIWD YLHFADCPST PELVQDLIRN LLNREPQKRM LPLQALETAA FNEMDSVVKR
     AAQNFEQQEH LHTE
//
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