KCY_ENCCU
ID KCY_ENCCU Reviewed; 220 AA.
AC Q8SS83;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable cytidylate kinase;
DE Short=CK;
DE EC=2.7.4.25;
DE AltName: Full=Cytidine monophosphate kinase;
DE Short=CMP kinase;
GN OrderedLocusNames=ECU03_1270;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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 -!- 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 -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL590443; CAD26270.1; -; Genomic_DNA.
DR RefSeq; NP_597635.1; NM_001040999.1.
DR PDB; 7L4A; X-ray; 1.50 A; A=1-220.
DR PDBsum; 7L4A; -.
DR AlphaFoldDB; Q8SS83; -.
DR SMR; Q8SS83; -.
DR STRING; 284813.Q8SS83; -.
DR GeneID; 858797; -.
DR KEGG; ecu:ECU03_1270; -.
DR VEuPathDB; MicrosporidiaDB:ECU03_1270; -.
DR HOGENOM; CLU_079959_0_2_1; -.
DR InParanoid; Q8SS83; -.
DR OMA; DIATIVC; -.
DR OrthoDB; 1366104at2759; -.
DR Proteomes; UP000000819; Chromosome III.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 CDD; cd02020; CMPK; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF02224; Cytidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00017; cmk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..220
FT /note="Probable cytidylate kinase"
FT /id="PRO_0000388422"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:7L4A"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:7L4A"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:7L4A"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:7L4A"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:7L4A"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 164..180
FT /evidence="ECO:0007829|PDB:7L4A"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:7L4A"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:7L4A"
FT HELIX 202..220
FT /evidence="ECO:0007829|PDB:7L4A"
SQ SEQUENCE 220 AA; 25208 MW; 26FC9F0D996E6528 CRC64;
MKTYKIAVDG PAASGKSSTS DLVARKLGFS HLISGNLYRA VTYGLVRRFG EVRPGDEEQK
RFVLELSIEV RNNRVFLDGE DVSESLRKEV VDRHVVSVAR EKYIREKVFT IQRSVIDLEK
RGIVVDGRDI ATRIMPNADL KVFLTASPET RARRRYMEGG SESYEELLES IKKRDHNDRT
REHDPLVATC DSIVIENDSM TLEETADEII RLFRRVESFN