ID A0A1Q4VC86_9ACTN Unreviewed; 152 AA.
AC A0A1Q4VC86;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=CMP/dCMP-type deaminase domain-containing protein {ECO:0000259|PROSITE:PS51747};
GN ORFNames=AB852_00835 {ECO:0000313|EMBL:OKH95437.1};
OS Streptomyces uncialis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1048205 {ECO:0000313|EMBL:OKH95437.1, ECO:0000313|Proteomes:UP000186455};
RN [1] {ECO:0000313|EMBL:OKH95437.1, ECO:0000313|Proteomes:UP000186455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCA2648 {ECO:0000313|EMBL:OKH95437.1,
RC ECO:0000313|Proteomes:UP000186455};
RA Yan X., Huang T., Ge H., Shen B.;
RT "Cloning and characterization of the uncialamcin biosynthetic gene
RT cluster.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:OKH95437.1}.
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DR EMBL; LFBV01000001; OKH95437.1; -; Genomic_DNA.
DR RefSeq; WP_073782578.1; NZ_LFBV01000001.1.
DR AlphaFoldDB; A0A1Q4VC86; -.
DR STRING; 1048205.AB852_00835; -.
DR Proteomes; UP000186455; Unassembled WGS sequence.
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:UP000186455};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006019-2}.
FT DOMAIN 23..152
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-1"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
SQ SEQUENCE 152 AA; 16264 MW; 551A3DF52388B834 CRC64;
MPTTEYDLVH GTLRSYPQQQ RPGWDEYFLG IATAVAARGD CLRSQVGAVL VGGDHRIRAT
GYNGSEPGGP SCLRGECARC QSQVPAGTAY DECVETHAEA NALLHAAWSD CQGATLYITR
PPCQGCSKLI RSAGIDHVLW PQGALSFTQE VA
//
