ID Q8A5K5_BACTN PRELIMINARY; PRT; 147 AA. AC Q8A5K5; DT 01-JUN-2003 (TrEMBLrel. 24, Created) DT 01-JUN-2003 (TrEMBLrel. 24, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Putative cytosine/adenosine deaminase. GN OrderedLocusNames=BT2234; OS Bacteroides thetaiotaomicron. OC Bacteria; Bacteroidetes; Bacteroides (class); Bacteroidales; OC Bacteroidaceae; Bacteroides. OX NCBI_TaxID=818; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VPI-5482 / ATCC 29148; RX MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., RA Chiang H.C., Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) that mediates a form CC of innate resistance to retroviral infections by triggering G-to-A CC hypermutation in the newly synthetized viral DNA. The replacements CC C-to-U in the minus strand DNA during reverse transcription, leads CC to G-to-A transitions in the plus strand. The inhibition of viral CC replication is either due to the degradation of the minus strand CC before its integration or to the lethality of the hypermutations. CC Modification of both DNA strands is not excluded. APOBEC3G binds a CC variety of RNAs, but does not display detectable APOB, NF1 and CC NAT1 mRNA editing (By similarity). CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: Zinc (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mainly cytoplasmic. Small amount are found CC in the nucleus (By similarity). 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; AE016935; AAO77341.1; -; Genomic_DNA. DR GO; GO:0016787; F:hydrolase activity; IEA. DR GO; GO:0008270; F:zinc ion binding; IEA. DR InterPro; IPR002125; dCMP/cyt_deam. DR Pfam; PF00383; dCMP_cyt_deam; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; UNKNOWN_1. KW Complete proteome; Hydrolase; Zinc. SQ SEQUENCE 147 AA; 15970 MW; 3A072D8ED1686443 CRC64; MMTLDDTYFM KQALIEAGKA AERGEVPVGA VVVCKERIIA RAHNLTETLN DVTAHAEMQA ITAAANVLGG KYLNECTLYV TVEPCVMCAG AIAWAQTGKL VFGAEDDKRG YQRYAAQALH PKTVVVKGIL ADECATLMKD FFASKRR //