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KCY_PYRFU
ID   KCY_PYRFU               Reviewed;         192 AA.
AC   Q8U2L4;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=PF0820;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL80944.1; -; Genomic_DNA.
DR   RefSeq; WP_011011949.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U2L4; -.
DR   SMR; Q8U2L4; -.
DR   STRING; 186497.PF0820; -.
DR   EnsemblBacteria; AAL80944; AAL80944; PF0820.
DR   GeneID; 41712623; -.
DR   KEGG; pfu:PF0820; -.
DR   PATRIC; fig|186497.12.peg.868; -.
DR   eggNOG; arCOG01037; Archaea.
DR   HOGENOM; CLU_079959_1_0_2; -.
DR   OMA; FIFRDMA; -.
DR   OrthoDB; 110333at2157; -.
DR   PhylomeDB; Q8U2L4; -.
DR   Proteomes; UP000001013; 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; -; 1.
DR   HAMAP; MF_00239; Cytidyl_kinase_type2; 1.
DR   InterPro; IPR011892; Cyt_kin_arch.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
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_0000132020"
FT   BINDING         12..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ   SEQUENCE   192 AA;  21737 MW;  27BD125622E5CB26 CRC64;
     MPKGCLVITV SGLAGSGTTT LCRKLAEHYG FKHVYAGLIF RQMAKERGMT LEEFQKYAEL
     HPEIDREVDR RQIEAAKECN VVIEGRLAGW MVKNADLKIW LDAPIRVRAE RVARREGITV
     EEAFMKIAER EMQNRKRYLN LYGIDINDLS IYDLIIDTSK WSPDGVFAIV KAAIDHLDPV
     GDAGSKKEKE VG
 
 
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