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Database: UniProt
Entry: A0A0D0D215_9AGAM
LinkDB: A0A0D0D215_9AGAM
Original site: A0A0D0D215_9AGAM 
ID   A0A0D0D215_9AGAM        Unreviewed;       165 AA.
AC   A0A0D0D215;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Cytidine deaminase {ECO:0000256|ARBA:ARBA00012783, ECO:0000256|RuleBase:RU364006};
DE            EC=3.5.4.5 {ECO:0000256|ARBA:ARBA00012783, ECO:0000256|RuleBase:RU364006};
DE   AltName: Full=Cytidine aminohydrolase {ECO:0000256|ARBA:ARBA00032005, ECO:0000256|RuleBase:RU364006};
GN   ORFNames=PAXRUDRAFT_832397 {ECO:0000313|EMBL:KIK82103.1};
OS   Paxillus rubicundulus Ve08.2h10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK82103.1, ECO:0000313|Proteomes:UP000054538};
RN   [1] {ECO:0000313|EMBL:KIK82103.1, ECO:0000313|Proteomes:UP000054538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK82103.1,
RC   ECO:0000313|Proteomes:UP000054538};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC       2'-deoxycytidine for UMP synthesis. {ECO:0000256|ARBA:ARBA00003949,
CC       ECO:0000256|RuleBase:RU364006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+);
CC         Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC         Evidence={ECO:0000256|RuleBase:RU364006};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine + H(+) + H2O = NH4(+) + uridine;
CC         Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000393,
CC         ECO:0000256|RuleBase:RU364006};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU364006};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000256|ARBA:ARBA00006576, ECO:0000256|RuleBase:RU364006}.
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DR   EMBL; KN825678; KIK82103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0D215; -.
DR   STRING; 930991.A0A0D0D215; -.
DR   HOGENOM; CLU_097262_2_1_1; -.
DR   InParanoid; A0A0D0D215; -.
DR   OrthoDB; 102874at2759; -.
DR   Proteomes; UP000054538; Unassembled WGS sequence.
DR   GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01283; cytidine_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; IPR006262; Cyt_deam_tetra.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   NCBIfam; TIGR01354; cyt_deam_tetra; 1.
DR   PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1.
DR   PANTHER; PTHR11644:SF2; CYTIDINE DEAMINASE; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364006};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054538};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364006}.
FT   DOMAIN          9..149
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
SQ   SEQUENCE   165 AA;  17685 MW;  4E62FB50C60AA2AA CRC64;
     MQSDTSTSSD RQRLIEGAIR AKQYAYSRYS NFRVGAALLD EDRTIITGAS IDNACYSATI
     CAERTAILKA ISENIRTFKA LAVTSDVLSP ISPCGLCREV IREFCAREMP VLLIPADYPK
     QGDNGLEVED GGIVTLTVGQ LLPHSPGPGY LEQAISSGPC VGSRA
//
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