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Database: UniProt
Entry: C9KVJ5_9BACE
LinkDB: C9KVJ5_9BACE
Original site: C9KVJ5_9BACE 
ID   C9KVJ5_9BACE            Unreviewed;       247 AA.
AC   C9KVJ5;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
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   ECO:0000313|EMBL:EEX45838.1};
GN   ORFNames=BACFIN_06344 {ECO:0000313|EMBL:EEX45838.1};
OS   Bacteroides finegoldii DSM 17565.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=483215 {ECO:0000313|EMBL:EEX45838.1, ECO:0000313|Proteomes:UP000003768};
RN   [1] {ECO:0000313|EMBL:EEX45838.1, ECO:0000313|Proteomes:UP000003768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17565 {ECO:0000313|EMBL:EEX45838.1,
RC   ECO:0000313|Proteomes:UP000003768};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2009) 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}.
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:EEX45838.1}.
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DR   EMBL; ABXI02000032; EEX45838.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9KVJ5; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_0_2_10; -.
DR   Proteomes; UP000003768; 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_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:EEX45838.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00238};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:EEX45838.1}.
FT   DOMAIN          23..240
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF02224"
FT   BINDING         27..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   247 AA;  28143 MW;  CEA8AFE0A4A7CE47 CRC64;
     MIFKINVSLA DKSEELNMKK ITIAIDGFSS CGKSTMAKDL AREVGYIYID SGAMYRAVTL
     YSIENGIFDG NDIDTEKLRK EIRNIRISFR LNPATGRPDT YLNDVNVENR IRTMEVSSKV
     SPISALDFVR TEMVAQQQAM GKEKGIVMDG RDIGTTVFPE AELKIFVTAT PEIRAQRRYD
     ELKAKGQEAS FDEILENVKQ RDYIDQHREV SPLRKAEDAL LLDNTNLTIE QQKEWLFEQF
     NKVSGIQ
//
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