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Database: UniProt
Entry: D9SN16_CLOC7
LinkDB: D9SN16_CLOC7
Original site: D9SN16_CLOC7 
ID   D9SN16_CLOC7            Unreviewed;       215 AA.
AC   D9SN16;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE            Short=CK {ECO:0000256|HAMAP-Rule:MF_00238};
DE            EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00238};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE            Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00238};
GN   Name=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN   OrderedLocusNames=Clocel_2139 {ECO:0000313|EMBL:ADL51882.1};
OS   Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL51882.1, ECO:0000313|Proteomes:UP000002730};
RN   [1] {ECO:0000313|EMBL:ADL51882.1, ECO:0000313|Proteomes:UP000002730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC   {ECO:0000313|Proteomes:UP000002730};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium cellulovorans 743B.";
RL   Submitted (AUG-2010) 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_00238};
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_00238};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009427, ECO:0000256|HAMAP-Rule:MF_00238}.
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DR   EMBL; CP002160; ADL51882.1; -; Genomic_DNA.
DR   RefSeq; WP_010076899.1; NC_014393.1.
DR   AlphaFoldDB; D9SN16; -.
DR   STRING; 573061.Clocel_2139; -.
DR   KEGG; ccb:Clocel_2139; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_0_2_9; -.
DR   OrthoDB; 9807434at2; -.
DR   Proteomes; UP000002730; Chromosome.
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_00238; Cytidyl_kinase_type1; 1.
DR   InterPro; IPR003136; Cytidylate_kin.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00017; cmk; 1.
DR   PANTHER; PTHR21299:SF2; CYTIDYLATE KINASE; 1.
DR   PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00238}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:ADL51882.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00238}; Reference proteome {ECO:0000313|Proteomes:UP000002730};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00238}.
FT   DOMAIN          6..211
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF02224"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   215 AA;  24361 MW;  54557A6754A57210 CRC64;
     MINRSIAIDG PAGSGKSTIA KIIAKENNLM YINTGAMYRA VTYYAIKAGI SYDEVSKLID
     LIDNLEMHFE GDRLIVNGTD ITDELTYPEI SNNVSNYAAV KEVREKLVSF QQKMSQKYEV
     IMDGRDIGTV VLKDAKYKFF LTAKAEERAK RRCKELIEKG IEVDFNNILE EIEKRDYIDT
     HREINPLTKA DDAMEIDTSS MTIDEVVKKI SGLLN
//
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