ID F8QME5_TOXGO Unreviewed; 554 AA.
AC F8QME5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:ADH04619.1};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000313|EMBL:ADH04619.1};
RN [1] {ECO:0000313|EMBL:ADH04619.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TgCtGZ7 {ECO:0000313|EMBL:ADH04619.1};
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; GQ243215; ADH04619.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QME5; -.
DR SMR; F8QME5; -.
DR VEuPathDB; ToxoDB:TGARI_205250; -.
DR VEuPathDB; ToxoDB:TGCOUG_205250; -.
DR VEuPathDB; ToxoDB:TGDOM2_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; 62680 MW; 9FBDA4ED1E6A5734 CRC64;
MFSVQRPPLT RTVVRMGLAT LLPKTACLAV LNVALVFLLF QVQDETGITL DPSKLDSKPT
SLDSQQHVAD KRWPATVGHY 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 RPFQTTGITY TFTTDAWQLG ITLYCIWCKE
RPTPADGIWD YLHFADCPST PELVQDLIRN LLNREPQKRM LPLQALETAA FNEMDSVVKR
AAQNFEQQEH LHTE
//
