ID A0A125YI07_TOXGV Unreviewed; 462 AA.
AC A0A125YI07;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=UMP-CMP kinase {ECO:0000313|EMBL:ESS28568.1};
DE EC=2.7.4.14 {ECO:0000313|EMBL:ESS28568.1};
GN ORFNames=TGVEG_257740 {ECO:0000313|EMBL:ESS28568.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS28568.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESS28568.1}.
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DR EMBL; AAYL02000337; ESS28568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A125YI07; -.
DR STRING; 432359.A0A125YI07; -.
DR PaxDb; 5811-TGME49_057740; -.
DR EnsemblProtists; ESS28568; ESS28568; TGVEG_257740.
DR VEuPathDB; ToxoDB:TGVEG_257740; -.
DR eggNOG; KOG3079; Eukaryota.
DR OMA; QISMVRP; -.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR Pfam; PF00406; ADK; 2.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
SQ SEQUENCE 462 AA; 50995 MW; 41B9F13ECF99E648 CRC64;
MFLPLPMGSF QDTRRSHSST PVARIVSSVF RATWLSSLAL VPCLSFLGTF VPDAVHEVYV
HSSAAVLPAL QFYGQSQISM VRPAFLDTHK RILSSFFHKF SIRAPSQYFV PTGKPSSSLA
SNCGPSVPAV LCSVLPSISG RLACETEVPS ALSTWENQLP SGQRTERGFT AATYSSAPFA
QQFCTRLRMN PRISTLCGKR DAMAATNTIE SGTTRCEKKP KIVFVLGGPG AGKGTQCELL
TKHHRVFHIS AGDCLREERQ RPNSKDGELI QECIREGRIV PVEITLTLLL KKMLARGWSE
VFLIDGFPRN QDNLDGWLSF TKRENLMTKL EQISTTNPEL APQCKQVLEQ LQAEGKTAAD
GAANASQANG ACADSDSGVE ICFCLFLDCS EETMEARLLE RGKHSGRADD NAAAIKKRFR
TYKEETMPIV QYFEKQNKVK AIDAGQTVEQ VWSRVDQLFK NL
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