ID B7T153_BOVIN Unreviewed; 185 AA.
AC B7T153;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G {ECO:0000256|ARBA:ARBA00020239};
DE EC=3.5.4.38 {ECO:0000256|ARBA:ARBA00029489};
DE AltName: Full=Deoxycytidine deaminase {ECO:0000256|ARBA:ARBA00032972};
GN Name=APOBEC3Z1 {ECO:0000313|EMBL:ACH69762.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:ACH69762.1};
RN [1] {ECO:0000313|EMBL:ACH69762.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19017397; DOI=10.1186/1471-2199-9-104;
RA LaRue R.S., Jonsson S.R., Silverstein K.A., Lajoie M., Bertrand D.,
RA El-Mabrouk N., Hotzel I., Andresdottir V., Smith T.P., Harris R.S.;
RT "The artiodactyl APOBEC3 innate immune repertoire shows evidence for a
RT multi-functional domain organization that existed in the ancestor of
RT placental mammals.";
RL BMC Mol. Biol. 9:104-104(2008).
RN [2] {ECO:0000313|EMBL:ACH69762.1}
RP NUCLEOTIDE SEQUENCE.
RA LaRue R.S., Harris R.S.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-
CC deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948,
CC Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:133902; EC=3.5.4.38;
CC Evidence={ECO:0000256|ARBA:ARBA00029350};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR EMBL; EU864534; ACH69762.1; -; mRNA.
DR RefSeq; NP_001157408.1; NM_001163936.1.
DR AlphaFoldDB; B7T153; -.
DR GeneID; 507162; -.
DR KEGG; bta:507162; -.
DR CTD; 610245; -.
DR OrthoDB; 5355962at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF20; DNA DC-DU-EDITING ENZYME APOBEC-3G; 1.
DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1.
DR Pfam; PF18782; NAD2; 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 2: Evidence at transcript level;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 15..137
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 185 AA; 21675 MW; 61A7EBD4DDCF2922 CRC64;
MDEYTFTENF NNQGRPSKTY LCYEMERLDG NATIPLDEYK GFVRNKGLDQ PEKPCHAELY
FLGKIRSWNL DRNQHYRLTC FISWSPCYDC AQKLTTFLKE NHHISLHILA SRIYTRNHFG
CHQSGLCELQ AAGARITIMT FEDFKHCWET FVDHKGKPFQ PWEGLNVKSQ ALCAELQAIL
KTQQN
//
