GenomeNet

Database: UniProt
Entry: A0A1Q2CI41_9ACTN
LinkDB: A0A1Q2CI41_9ACTN
Original site: A0A1Q2CI41_9ACTN 
ID   A0A1Q2CI41_9ACTN        Unreviewed;       152 AA.
AC   A0A1Q2CI41;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Cell division protein DedD {ECO:0000313|EMBL:AQP45725.1};
DE   SubName: Full=dCMP deaminase {ECO:0000313|EMBL:SDZ12858.1};
GN   ORFNames=RPIT_13650 {ECO:0000313|EMBL:AQP45725.1}, SAMN05428934_11169
GN   {ECO:0000313|EMBL:SDZ12858.1};
OS   Tessaracoccus flavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1610493 {ECO:0000313|EMBL:AQP45725.1, ECO:0000313|Proteomes:UP000188324};
RN   [1] {ECO:0000313|EMBL:AQP45725.1, ECO:0000313|Proteomes:UP000188324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RP1T {ECO:0000313|EMBL:AQP45725.1,
RC   ECO:0000313|Proteomes:UP000188324};
RX   PubMed=26869509; DOI=10.1099/ijsem.0.000958;
RA   Kumari R., Singh P., Schumann P., Lal R.;
RT   "Tessaracoccus flavus sp. nov., isolated from the drainage system of a
RT   lindane-producing factory.";
RL   Int. J. Syst. Evol. Microbiol. 66:1862-1868(2016).
RN   [2] {ECO:0000313|EMBL:SDZ12858.1, ECO:0000313|Proteomes:UP000199635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RP1 {ECO:0000313|EMBL:SDZ12858.1,
RC   ECO:0000313|Proteomes:UP000199635};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AQP45725.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RP1T {ECO:0000313|EMBL:AQP45725.1};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|PIRSR:PIRSR006019-2};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000256|ARBA:ARBA00006576}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP019605; AQP45725.1; -; Genomic_DNA.
DR   EMBL; FNPU01000011; SDZ12858.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2CI41; -.
DR   STRING; 1610493.RPIT_13650; -.
DR   KEGG; tfl:RPIT_13650; -.
DR   OrthoDB; 9788517at2; -.
DR   Proteomes; UP000188324; Chromosome.
DR   Proteomes; UP000199635; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:InterPro.
DR   CDD; cd01286; deoxycytidylate_deaminase; 1.
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   InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
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   Cell cycle {ECO:0000313|EMBL:AQP45725.1};
KW   Cell division {ECO:0000313|EMBL:AQP45725.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR006019-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188324};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006019-2}.
FT   DOMAIN          12..152
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-1"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT   BINDING         122
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;  16057 MW;  15FB638A7A3C80B3 CRC64;
     MDSSPVTHTV PGWDEYFLQI ADAVSARAKC TRRRVGAVLV VERRIIATGY NGAASGEPDC
     LEGACPRGAL DYGTVPGLGD YDRPGTPGFC IAIHAEVNAL LFATRDTAGA TAYITDPPCP
     GCRKALAAAG IARVVWPDGV YDGRGEIMDW SR
//
DBGET integrated database retrieval system