ID A0A0M8MZ13_9BASI Unreviewed; 343 AA.
AC A0A0M8MZ13;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Deoxycytidylate deaminase {ECO:0000313|EMBL:KOS16580.1};
GN ORFNames=Malapachy_3127 {ECO:0000313|EMBL:KOS16580.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS16580.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS16580.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS16580.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KOS16580.1}.
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DR EMBL; LGAV01000001; KOS16580.1; -; Genomic_DNA.
DR RefSeq; XP_017994212.1; XM_018137605.1.
DR AlphaFoldDB; A0A0M8MZ13; -.
DR STRING; 77020.A0A0M8MZ13; -.
DR GeneID; 28729481; -.
DR VEuPathDB; FungiDB:Malapachy_3127; -.
DR OrthoDB; 178124at2759; -.
DR Proteomes; UP000037751; 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:UP000037751};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 197..332
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 343 AA; 37464 MW; 9FB883038E1199BF CRC64;
MLIAIVGLAC SGKSAVAEYL VARHGFQIIT LDASGGENDF ASPDAMLHHV TSNWRTNFVT
LALDSSPLIE MFEKRPFFLL LGVEAPLMQR WNRARMRATA AGETPASLES FVARDDAVLY
GVSTVTPGDV SDDLSNLSFT SHNGAMMSMS LPSAQLSLAG LLQRCQLRIT NTFVRVDELH
AHLDSLALPS MHRLRPTWDT YFVRLCTLAA MRSNCMKRRV GAVIVRNHRV LSTGYNGTPR
GLTNCNEGGC VRCNESAPCG SSLDECLCLH AEENALLELG RDRGGAEGTV LYCNTCPCLR
CAVKIVQTGV SEVVYQLEYS MDSRSAQIFA QAGVAFRKYL PPF
//
