3.5.4.B9	metabolism	the APOBEC3 family has many roles, such as restricting endogenous and exogenous retrovirus replication and retrotransposon insertion events and reducing DNA-induced inflammation	755694	
3.5.4.B9	metabolism	the enzyme generates cytidine to deoxyuridine mutations in single-stranded DNA, and is capable of restricting replication of HIV-1 by generating mutations in viral genome	757774	
3.5.4.B9	physiological function	APOBEC3G is a single-stranded DNA cytidine deaminase capable of restricting retroviral replication	723285	
3.5.4.B9	physiological function	APOBEC3G protein inhibits HCV replication through direct binding at non-structural protein NS3 at its C-terminus, which is responsible for NS3's helicase and NTPase activities	735015	
3.5.4.B9	physiological function	the enzyme causes C to T mutations in the cDNA copy of the HIV-1 genome	719342	
3.5.4.B9	physiological function	the enzyme causes mutational diversity by initiating mutations on regions of single-stranded DNA. The enzyme enters the cytoplasm of the targeted T cell and catalyzes C deaminations on reverse transcribed cDNA causing HIV-1 retroviral inactivation. Enzyme-initiated mutations boost human fitness and restricts HIV-1 replication in the absence of the viral infectivity factor. The enzyme is involved in hepatic metastasis of colorectal cancer	721999	
3.5.4.B9	physiological function	the enzyme exhibits anti-human immunodeficiency virus-1 (HIV-1) activity by deaminating cytidines of the minus strand of HIV-1. Virus infectivity factor of HIV-1 counteracts the anti-HIV-1 activity of the enzyme	722114	
3.5.4.B9	physiological function	the enzyme inhibits HIV replication and inhibits retroviral infection by deaminating first strand cDNA, generating viral DNA mutations and potential viral elimination	722103	
3.5.4.B9	physiological function	the enzyme is a single-stranded DNA cytosine deaminase that functions in innate immunity against retroviruses and retrotransposons. The enzyme can potently restrict virus infectivity factor-deficient HIV-1 replication by catalyzing excessive levels of G->A hypermutation. Sublethal levels of enzyme-catalyzed mutation may contribute to the high level of HIV-1 fitness and its incurable prognosis	722064	
3.5.4.B9	physiological function	the enzyme is an endogenous inhibitor of human immunodeficiency virus type 1 (HIV-1) replication, able to induce G to A hypermutation in newly synthesized viral DNA	723260	
3.5.4.B9	physiological function	the enzyme is an important component of the cellular innate immune response to retroviral infection. The enzyme APOBEC3G can extinguish HIV-1 infectivity by its incorporation into virus particles and subsequent cytosine deaminase activity that attacks the nascent viral cDNA during reverse transcription, causing lethal mutagenesis. The enzyme can also induce sublethal mutagenesis, which maintains virus infectivity and contribute to HIV-1 variation	723071	
3.5.4.B9	physiological function	the enzyme is capable of blocking retrovirus replication by editing viral cDNA and impairing reverse transcription	721668	
3.5.4.B9	physiological function	the enzyme is encapsulated by the HIV virion and facilitates restriction of HIV-1 infection in T cells by deaminating cytosines in nascent minus-strand complementary DNA	723256	
3.5.4.B9	physiological function	the enzyme mutates the human immunodeficiency virus (HIV) genome by converting deoxycytidine to deoxyuridine in signature trinucleotides (CCC, TCC) on minus strand viral DNA during reverse transcription. The enzyme restricts viral propagation by degrading or incapacitating the coding ability of the HIV genome. The enzyme contributes to the evasion of adaptive immunity by HIV	723754	
3.5.4.B9	physiological function	the enzyme restricts replication of HIV-1 by inducing viral genome mutagenesis through deamination of cytosine to uracil on HIV-1 cDNA processively through jumping and sliding. The jumping and sliding of Apo3G is needed for efficient mutational inactivation of HIV-1	722698	
3.5.4.B9	physiological function	the single-stranded DNA-dependent cytosine deaminase inactivates HIV-1 in T cells by C to T hypermutation	720014