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Database: UniProt
Entry: A0A162GH71_9MICO
LinkDB: A0A162GH71_9MICO
Original site: A0A162GH71_9MICO 
ID   A0A162GH71_9MICO        Unreviewed;       279 AA.
AC   A0A162GH71;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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:KZX21059.1};
GN   ORFNames=ACH61_01802 {ECO:0000313|EMBL:KZX21059.1}, EV639_107184
GN   {ECO:0000313|EMBL:TCO36504.1};
OS   Rathayibacter tanaceti.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=1671680 {ECO:0000313|EMBL:KZX21059.1, ECO:0000313|Proteomes:UP000076717};
RN   [1] {ECO:0000313|EMBL:TCO36504.1, ECO:0000313|Proteomes:UP000295366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO36504.1,
RC   ECO:0000313|Proteomes:UP000295366};
RX   PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA   Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA   De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA   Kyrpides N.C.;
RT   "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT   the genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Stand. Genomic Sci. 10:26-26(2015).
RN   [2] {ECO:0000313|EMBL:KZX21059.1, ECO:0000313|Proteomes:UP000076717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:KZX21059.1,
RC   ECO:0000313|Proteomes:UP000076717};
RA   Vasilenko O.V., Starodumova I.P., Tarlachkov S.V., Dorofeeva L.V.,
RA   Evtushenko L.I.;
RT   "Draft Genome Sequence of Rathayibacter sp. Strain VKM Ac-2596 Isolated
RT   from Leaf Gall Induced by Plant-Parasitic Nematodes.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:TCO36504.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO36504.1};
RA   Whitman W., Huntemann M., Clum A., Pillay M., Palaniappan K., Varghese N.,
RA   Mikhailova N., Stamatis D., Reddy T., Daum C., Shapiro N., Ivanova N.,
RA   Kyrpides N., Woyke T.;
RL   Submitted (MAR-2019) 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:KZX21059.1}.
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DR   EMBL; LIIN01000056; KZX21059.1; -; Genomic_DNA.
DR   EMBL; SLWP01000007; TCO36504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162GH71; -.
DR   PATRIC; fig|1671680.3.peg.1916; -.
DR   Proteomes; UP000076717; Unassembled WGS sequence.
DR   Proteomes; UP000295366; 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:0004127; F:cytidylate kinase activity; IEA:UniProtKB-UniRule.
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:KZX21059.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00238}; Reference proteome {ECO:0000313|Proteomes:UP000076717};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:KZX21059.1}.
FT   DOMAIN          53..264
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF02224"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   279 AA;  30288 MW;  A6F27A7F512F6996 CRC64;
     MSTEQNRQEG GLNRMTPARR AQQSIPEEGG PAPERADRPE SDESADFGAA TVVAIDGPAG
     SGKSSVSREA ARRLGFEFLD TGAAYRALAW HGLDRGLDFG DEDEIVDALD GFDYSIGTDP
     ESYSVWVGPT EVTAAIREPR VTERVSAVAK VPEVRRRITL LFRRIIGETR REGIIVEGRD
     ITTVVAPTAP VRILLTASEE ARMARRSREV TTESAEATGQ ALRSRDRADS QVVDFMNAAE
     GVTLLDSTHL DFEQTVDAVV AEVRTSRARA GHGTGHARR
//
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