ID A0A1I0P4S8_9EURY Unreviewed; 191 AA.
AC A0A1I0P4S8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00239};
DE Short=CK {ECO:0000256|HAMAP-Rule:MF_00239};
DE EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00239};
DE AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00239};
DE Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00239};
GN Name=cmk {ECO:0000256|HAMAP-Rule:MF_00239};
GN ORFNames=SAMN05216285_2135 {ECO:0000313|EMBL:SEW09207.1};
OS Natrinema salifodinae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1202768 {ECO:0000313|EMBL:SEW09207.1, ECO:0000313|Proteomes:UP000183275};
RN [1] {ECO:0000313|Proteomes:UP000183275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12284 {ECO:0000313|Proteomes:UP000183275};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001097, ECO:0000256|HAMAP-
CC Rule:MF_00239};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001115, ECO:0000256|HAMAP-
CC Rule:MF_00239};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00239}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00011005, ECO:0000256|HAMAP-Rule:MF_00239}.
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DR EMBL; FOIS01000003; SEW09207.1; -; Genomic_DNA.
DR RefSeq; WP_049989569.1; NZ_JROF01000007.1.
DR AlphaFoldDB; A0A1I0P4S8; -.
DR STRING; 1202768.SAMN05216285_2135; -.
DR eggNOG; arCOG01037; Archaea.
DR OrthoDB; 31096at2157; -.
DR Proteomes; UP000183275; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd02020; CMPK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00239; Cytidyl_kinase_type2; 1.
DR InterPro; IPR011892; Cyt_kin_arch.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02173; cyt_kin_arch; 1.
DR Pfam; PF13189; Cytidylate_kin2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00239};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00239};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00239, ECO:0000313|EMBL:SEW09207.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000183275};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00239}.
FT REGION 108..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00239"
SQ SEQUENCE 191 AA; 21668 MW; CB5ABCE548FE188D CRC64;
MLLTVSGPPG SGKSTTAELL ADAFDLDHVS GGDIFRELAD ERGYTPLEFN KLAEENDQID
RDLDRRLREI AVEEDDLVLE SRLAGWLAGD QADFRFWLDA PARVRGERIA EREDKDPERA
TEETKAREAS EAQRYEEYYG IDIRDLTIYD LSVNTARWEP AAVLDMLVTA VERYEADGDE
GQALVNTDYE F
//
