ID L9WCX3_9EURY Unreviewed; 195 AA.
AC L9WCX3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=C496_01311 {ECO:0000313|EMBL:ELY46163.1};
OS Natronorubrum tibetense GA33.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1114856 {ECO:0000313|EMBL:ELY46163.1, ECO:0000313|Proteomes:UP000011599};
RN [1] {ECO:0000313|EMBL:ELY46163.1, ECO:0000313|Proteomes:UP000011599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA33 {ECO:0000313|EMBL:ELY46163.1,
RC ECO:0000313|Proteomes:UP000011599};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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:ELY46163.1}.
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DR EMBL; AOHW01000004; ELY46163.1; -; Genomic_DNA.
DR AlphaFoldDB; L9WCX3; -.
DR STRING; 1114856.GCA_000383975_03969; -.
DR PATRIC; fig|1114856.3.peg.270; -.
DR eggNOG; arCOG01037; Archaea.
DR Proteomes; UP000011599; 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; PF13238; AAA_18; 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:ELY46163.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00239};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00239, ECO:0000313|EMBL:ELY46163.1}.
FT BINDING 13..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00239"
SQ SEQUENCE 195 AA; 22023 MW; BCE66BFE10AC2C35 CRC64;
MEIDTTLFIT VSGPPGCGAT TLCEQLADAM GCPYVSGGDI FREIAEDQDM TLSQLTAQAD
SSEEIDRAID QRLQQIAEKW GTANKPFILE SRLAGWLAGE RADLRIWLDA PEDVRADRIE
DRVETEAEMR VREVSEAGRY QSYYQIDIDE REFYDLSINT ARWSKRGVFE LVRAALEEYD
PEIDEGAFST PDIDP
//
