ID POL_HV1Z6 STANDARD; PRT; 148 AA. AC P04586; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Pol polyprotein [Contains: Protease (Retropepsin) (EC 3.4.23.16); DE Reverse transcriptase (EC 2.7.7.49); Ribonuclease H (EC 3.1.26.4)] DE (Fragment). GN Name=POL; OS Human immunodeficiency virus type 1 (Zaire 6 isolate) (HIV-1). OC Viruses; Retroid viruses; Retroviridae; Lentivirus. OX NCBI_TaxID=11708; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87248097; PubMed=3036660; RA Srinivasan A., Anand R., York D., Ranganathan P., Feorino P., RA Schochetman G., Curran J., Kalyanaraman V.S., Luciw P.A., RA Sanchez-Pescador R.; RT "Molecular characterization of human immunodeficiency virus from RT Zaire: nucleotide sequence analysis identifies conserved and variable RT domains in the envelope gene."; RL Gene 52:71-82(1987). CC -!- CATALYTIC ACTIVITY: Specific for a P1 residue that is hydrophobic, CC and P1' variable, but often Pro. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. CC -!- CATALYTIC ACTIVITY: N deoxynucleoside triphosphate = N diphosphate CC + {DNA}(N). CC -!- PTM: Cleavage sites that yield the mature proteins remain to be CC determined. CC -!- SIMILARITY: The protease belongs to peptidase family A2; also CC known as the retropepsin family. 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; K03458; AAA45376.1; -. DR PIR; A26192; A26192. DR PDB; 1IHV; NMR; A/B=79-130. DR PDB; 1IHW; NMR; A/B=79-130. DR MEROPS; A02.001; -. DR HIV; K03458; POL$Z6. DR InterPro; IPR001037; Integrase_C. DR InterPro; IPR001969; Pept_Asp_AS. DR InterPro; IPR001584; Rve. DR Pfam; PF00552; Integrase; 1. DR Pfam; PF00665; rve; 1. DR PROSITE; PS00141; ASP_PROTEASE; PARTIAL. KW 3D-structure; AIDS; Aspartyl protease; Endonuclease; Hydrolase; KW Nuclease; Polyprotein; RNA-directed DNA polymerase; Transferase. FT NON_TER 1 1 FT STRAND 83 88 FT STRAND 95 104 FT STRAND 108 112 FT STRAND 117 121 FT HELIX 122 124 FT STRAND 125 129 SQ SEQUENCE 148 AA; 16840 MW; A0DD31618CF0FC0E CRC64; IPYNPQSQGV VESMNKELKK IIGQVRDQAE HLKTAVQMAV FIHNFKRKGG IGGYSAGERI IDIIATDIQT KELQKQITKI QNFRVYYRDS RDPIWKGPAK LLWKGEGAVV IQDNSDIKVV PRRKVKIIRD YGKQMAGDDC VASRQDED //