ID A0A1B8GN76_9PEZI Unreviewed; 333 AA.
AC A0A1B8GN76;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Deoxycytidine monophosphate (dCMP) deaminase {ECO:0000313|EMBL:OBT97301.1};
GN Name=DCD1 {ECO:0000313|EMBL:OBT97301.1};
GN ORFNames=VE01_04630 {ECO:0000313|EMBL:OBT97301.1};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT97301.1, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBT97301.1, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT97301.1,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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; KV460223; OBT97301.1; -; Genomic_DNA.
DR RefSeq; XP_018131034.1; XM_018274101.1.
DR AlphaFoldDB; A0A1B8GN76; -.
DR STRING; 342668.A0A1B8GN76; -.
DR GeneID; 28838016; -.
DR OrthoDB; 178124at2759; -.
DR Proteomes; UP000091956; Unassembled WGS sequence.
DR GO; GO:0019239; F:deaminase activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01286; deoxycytidylate_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR015517; dCMP_deaminase-rel.
DR InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
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 SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Reference proteome {ECO:0000313|Proteomes:UP000091956};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 176..314
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 333 AA; 37192 MW; C6EB6AB5533126DE CRC64;
MFVGLCGGIC SGKRTVAQYL IEHHGFTRLR LQHSANEPLT DDKHTFRTID DLVNFVTTQW
QRRWVTTDVY CEAVLDILVR RPFFILISVD APVNVRWKRF QRRLTSPTSS PQLDEDLSLE
DFVLRSDDHL FNPNGGLLPL ISRATIRLLN TSSDLAHLYA TLGKLDLTNE DRLRPSWDQY
FMQLASLAAQ RSNCMKRRVG CVLVREKRVI STGYNGTPRG LKNCGEGGCP RCNDAQGSGV
GLSTCLCIHA EENALLEAGR ERIREGAILY CDTCPCLTCS IKIAQVGISE VVYSQGYSMD
GETAAVFREA GVQLRQFSPP PNGLVHLEKQ AIA
//
