ID A0A0H5BN33_9HIV1 Unreviewed; 584 AA. AC A0A0H5BN33; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 28-JUN-2023, entry version 32. DE SubName: Full=Gag-pol polyprotein {ECO:0000313|EMBL:CDG41821.1}; DE Flags: Fragment; OS HIV-1 M:CRF08_BC. OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus. OX NCBI_TaxID=1385608 {ECO:0000313|EMBL:CDG41821.1}; RN [1] {ECO:0000313|EMBL:CDG41821.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YN254 {ECO:0000313|EMBL:CDG41821.1}; RA Chen S., Chen Y.Y., Lu W.; RT "Changing subtype dominance and shift in resistance of HIV-1 in the RT southwest border of China."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human CC immunodeficiency virus type 1 and Moloney murine leukemia virus CC enzymes prefer to cleave the RNA strand one nucleotide away from the CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides CC away from the primer terminus.; EC=3.1.26.13; CC Evidence={ECO:0000256|ARBA:ARBA00023415}; CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family. CC {ECO:0000256|RuleBase:RU004064}. 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; HG421589; CDG41821.1; -; Genomic_RNA. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW. DR CDD; cd05482; HIV_retropepsin_like; 1. DR Gene3D; 3.30.70.270; -; 3. DR Gene3D; 2.40.70.10; Acid Proteases; 1. DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR001995; Peptidase_A2_cat. DR InterPro; IPR021109; Peptidase_aspartic_dom_sf. DR InterPro; IPR034170; Retropepsin-like_cat_dom. DR InterPro; IPR018061; Retropepsins. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR000477; RT_dom. DR InterPro; IPR010659; RVT_connect. DR InterPro; IPR010661; RVT_thumb. DR PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1. DR PANTHER; PTHR41694:SF3; INTEGRASE-RELATED; 1. DR Pfam; PF00077; RVP; 1. DR Pfam; PF00078; RVT_1; 1. DR Pfam; PF06815; RVT_connect; 1. DR Pfam; PF06817; RVT_thumb; 1. DR SUPFAM; SSF50630; Acid proteases; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR PROSITE; PS50175; ASP_PROT_RETROV; 1. DR PROSITE; PS00141; ASP_PROTEASE; 1. DR PROSITE; PS50878; RT_POL; 1. PE 3: Inferred from homology; KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750, KW ECO:0000256|RuleBase:RU004064}; KW DNA integration {ECO:0000256|ARBA:ARBA00023195}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004064}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Protease {ECO:0000256|RuleBase:RU004064}; KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Viral genome integration {ECO:0000256|ARBA:ARBA00023195}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195}. FT DOMAIN 72..141 FT /note="Peptidase A2" FT /evidence="ECO:0000259|PROSITE:PS50175" FT DOMAIN 195..385 FT /note="Reverse transcriptase" FT /evidence="ECO:0000259|PROSITE:PS50878" FT REGION 1..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..48 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CDG41821.1" FT NON_TER 584 FT /evidence="ECO:0000313|EMBL:CDG41821.1" SQ SEQUENCE 584 AA; 67204 MW; 82ACDA6F31FF5E9F CRC64; FFRENLACPQ GEAREFPPEQ TRANSPASRE LQVRGDNPSS EAGTERQGTL NFPQITLWQR PLVSIKIGGQ IKEALLDTGA DDTVLEEINL PGKWKPKMIG GIGGFIKVRQ YEQIPIEICG KRATGTVLVG PTPVNIIGRN MLTQLGCTLN FPISPIETVP VKLKPGMDGP KVKQWPLTEE KIKALTAICD EMEKEGKITK IGPDNPYNTP IFAIKKKDST KWRKLVDFRE LNKRTQDFWE VQLGIPHPAG LKKKRSVTVL DVGDAYFSVP LDKDFRKYTA FTIPSINNAT PGIRYQYNVL PQGWKGSPAI FQCSMTKILE PFRKQNPDIV IYQYMDDLYV GSDLEIGQHR TKIEELREHL LKWGFTTPDK KHQKEPPFLW MGYELHPDKW TVQPIQLPDK DSWTVNDIQK LVGKLNWASQ IYPGIKVRQL CRLLRGAKAL TDIVPLTEEA ELELAENREI LKEPVHGAYY DPSKELIAEI QKQGQDQWTY QIYQEPFKNL KTGKYAKMRT AHTNDVKQLT EAVQKISMES IVIWGKIPKF RLPIQKETWE TWWTDYWQAT WIPEWEFVNT PPLVKLWYQL EKDP //