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Database: UniProt
Entry: A0A3M0IT00_HIRRU
LinkDB: A0A3M0IT00_HIRRU
Original site: A0A3M0IT00_HIRRU 
ID   A0A3M0IT00_HIRRU        Unreviewed;       152 AA.
AC   A0A3M0IT00;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=DUI87_31995 {ECO:0000313|EMBL:RMB91765.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB91765.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMB91765.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMB91765.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMB91765.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) 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}.
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:RMB91765.1}.
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DR   EMBL; QRBI01000235; RMB91765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0IT00; -.
DR   STRING; 333673.A0A3M0IT00; -.
DR   Proteomes; UP000269221; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProt.
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:UP000269221};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364006}.
FT   DOMAIN          20..147
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
SQ   SEQUENCE   152 AA;  16525 MW;  4E2900AD9EC1169E CRC64;
     MEGGGQHPVP AVAPSQPQGD HLQLLLRRSW EAKNCAYCPY SHFPVGAALL TTGGEIFSGC
     NVENACYSLG VCAERTAIQK AISEGHTSFK AMAITSDMGD HFITPCGACR QVMREFGTDW
     DVYLTKADGT YIVKRLEELL PLSFGPEDLK KV
//
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