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Database: UniProt
Entry: A0A0N0LJ70_9FLAO
LinkDB: A0A0N0LJ70_9FLAO
Original site: A0A0N0LJ70_9FLAO 
ID   A0A0N0LJ70_9FLAO        Unreviewed;       224 AA.
AC   A0A0N0LJ70;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=AMQ68_01510 {ECO:0000313|EMBL:KPH14225.1};
OS   Chryseobacterium sp. ERMR1:04.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1705393 {ECO:0000313|EMBL:KPH14225.1, ECO:0000313|Proteomes:UP000037945};
RN   [1] {ECO:0000313|EMBL:KPH14225.1, ECO:0000313|Proteomes:UP000037945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERMR1:04 {ECO:0000313|EMBL:KPH14225.1,
RC   ECO:0000313|Proteomes:UP000037945};
RX   PubMed=26543128;
RA   Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT   "Genome Assembly of Chryseobacterium polytrichastri ERMR1:04, a
RT   Psychrotolerant Bacterium with Cold Active Proteases, Isolated from East
RT   Rathong Glacier in India.";
RL   Genome Announc. 3:e01305-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000037945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERMR1:04 {ECO:0000313|Proteomes:UP000037945};
RA   Swarnkar M.K., Kumar R., Singh A.K., Singh D.;
RT   "Genome Sequencing of Chryseobacterium sp. ERMR1:04 isolated from Glacier
RT   Moraine Ridge soil.";
RL   Submitted (AUG-2015) 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:KPH14225.1}.
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DR   EMBL; LIRF01000003; KPH14225.1; -; Genomic_DNA.
DR   RefSeq; WP_054508873.1; NZ_LIRF01000003.1.
DR   AlphaFoldDB; A0A0N0LJ70; -.
DR   STRING; 1705393.AMQ68_01510; -.
DR   PATRIC; fig|1705393.3.peg.316; -.
DR   OrthoDB; 9807434at2; -.
DR   Proteomes; UP000037945; 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|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00238};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00238};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00238}.
FT   DOMAIN          6..222
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   224 AA;  25317 MW;  C0D090DE178DB758 CRC64;
     MKKPVIAIDG YSSTGKSSIS KVIADKLELV HLDTGALYRG VTWFGLQHCM DDKGAINLEK
     LFSSLDQIQL EFKNNEGELV LYLNQTDISK QIRTNQVSDN VSLVAKQKEV RDFLLQSQRT
     LAEKGGIIMD GRDIGTVVLP NADFKFFLTA SIDERTKRRY NELLSLGIEA NEQQVKENLI
     IRDKIDSERE IAPLKQAHDA IVIDNTNLTK KETIESILSY IKNF
//
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