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KCY_HALWD
ID   KCY_HALWD               Reviewed;         192 AA.
AC   Q18GM4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00239};
DE            Short=CK {ECO:0000255|HAMAP-Rule:MF_00239};
DE            EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00239};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00239};
DE            Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00239};
GN   Name=cmk {ECO:0000255|HAMAP-Rule:MF_00239}; OrderedLocusNames=HQ_2765A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; Evidence={ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00239};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00239}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00239}.
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DR   EMBL; AM180088; CAJ52873.1; -; Genomic_DNA.
DR   RefSeq; WP_011571987.1; NC_008212.1.
DR   AlphaFoldDB; Q18GM4; -.
DR   SMR; Q18GM4; -.
DR   STRING; 362976.HQ_2765A; -.
DR   EnsemblBacteria; CAJ52873; CAJ52873; HQ_2765A.
DR   GeneID; 4193843; -.
DR   KEGG; hwa:HQ_2765A; -.
DR   eggNOG; arCOG01037; Archaea.
DR   HOGENOM; CLU_079959_1_0_2; -.
DR   OMA; ADFRFWL; -.
DR   Proteomes; UP000001975; 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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00239; Cytidyl_kinase_type2; 1.
DR   InterPro; IPR011892; Cyt_kin_arch.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02173; cyt_kin_arch; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..192
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_1000005667"
FT   BINDING         7..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ   SEQUENCE   192 AA;  21488 MW;  E9D8B6C8C974E494 CRC64;
     MLLTVSGPPG AGKSTTADTL AATFGLEHVS GGDIFRELAA ERGLTAVELN QQAEEDDQID
     RDLDQRLRTI ALERDDILLE SRLAGWLAGD AADIRVWLDA PLNVRAGRIA DREDKSISTA
     QEETRTREES EALRYQNYYN IDIHDHSIYD LRVNTARWPK TEVPDILEAA IAAYEPASDE
     GRFPIEDIIY DF
 
 
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