ID H6X4V2_9CAUD Unreviewed; 156 AA.
AC H6X4V2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=dCMP deaminase {ECO:0000313|EMBL:AFA44768.1};
GN Name=cd {ECO:0000313|EMBL:AFA44768.1};
GN ORFNames=RaK2_00495 {ECO:0000313|EMBL:AFA44768.1};
OS Klebsiella phage vB_KleM_RaK2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Alcyoneusvirus; Alcyoneusvirus RaK2.
OX NCBI_TaxID=1147094 {ECO:0000313|EMBL:AFA44768.1, ECO:0000313|Proteomes:UP000007524};
RN [1] {ECO:0000313|EMBL:AFA44768.1, ECO:0000313|Proteomes:UP000007524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22492928; DOI=10.1128/JVI.00347-12;
RA Simoliunas E., Kaliniene L., Truncaite L., Klausa V., Zajanckauskaite A.,
RA Meskys R.;
RT "Genome of Klebsiella sp.-Infecting Bacteriophage vB_KleM_RaK2.";
RL J. Virol. 86:5406-5406(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006019-2};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR EMBL; JQ513383; AFA44768.1; -; Genomic_DNA.
DR RefSeq; YP_007007650.1; NC_019526.1.
DR GeneID; 14013083; -.
DR KEGG; vg:14013083; -.
DR OrthoDB; 10605at10239; -.
DR Proteomes; UP000007524; Genome.
DR GO; GO:0004132; F:dCMP deaminase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:InterPro.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR016473; dCMP_deaminase.
DR InterPro; IPR015517; dCMP_deaminase-rel.
DR PANTHER; PTHR11086:SF18; CYTIDINE AND DCMP DEAMINASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR11086; DEOXYCYTIDYLATE DEAMINASE-RELATED; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR PIRSF; PIRSF006019; dCMP_deaminase; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR006019-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007524};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006019-2}.
FT DOMAIN 1..142
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-1"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
SQ SEQUENCE 156 AA; 17366 MW; DE93A8F588F3830A CRC64;
MKHKTWLNIA KAVAEESKCI SHKVGAVIVK NNRILSTGYN GTSSGAVNCC DANSHLIHNN
EFQNWVSDEA KHEHHEWSNI HEIHAEMNAL LYSSPQERQG ATLYSTMQPC YTCSKLIAGS
GITNVIYEKE YPRTPPEAIE VLKDAGITVN KLSDLE
//
