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Database: UniProt
Entry: B3GJB5_9HIV1
LinkDB: B3GJB5_9HIV1
Original site: B3GJB5_9HIV1 
ID   B3GJB5_9HIV1            Unreviewed;       390 AA.
AC   B3GJB5;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ACD80599.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ACD80599.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ACD80599.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACD80599.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21158SASA4100XXxxxxxiDDDD1ccLK39XXXX
RC   {ECO:0000313|EMBL:ACD80599.1};
RA   Rousseau C.M., Daniels M.G., Carlson J.M., Kadie C., Crawford H.,
RA   Prendergast A., Matthews P., Payne R., Rolland M., Raugi D.N., Maust B.S.,
RA   Learn G.H., Nickle D.C., Coovadia H., Ndung'u T., Frahm N., Brander C.,
RA   Walker B.D., Goulder P.J.R., Bhattacharya T., Heckerman D.E., Korber B.T.,
RA   Mullins J.I.;
RT   "HLA Class-I Driven Evolution of Human Immunodeficiency Virus Type 1
RT   Subtype C Proteome: Immune Escape and Viral Load.";
RL   Submitted (MAY-2008) 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};
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DR   EMBL; EU698852; ACD80599.1; -; Genomic_DNA.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; 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   Gene3D; 3.30.70.270; -; 3.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
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:SF5; RIBONUCLEASE H; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF06815; RVT_connect; 1.
DR   Pfam; PF06817; RVT_thumb; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   4: Predicted;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   DNA integration {ECO:0000256|ARBA:ARBA00022908};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..90
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          290..390
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACD80599.1"
FT   NON_TER         390
FT                   /evidence="ECO:0000313|EMBL:ACD80599.1"
SQ   SEQUENCE   390 AA;  45254 MW;  7A3A899711A5A819 CRC64;
     QYNVLPQGWK GSPAIFQSSM TKILEPFRAK NPEIVIYQYM DDLYVGSDLE IGQHRAKIEE
     LRTHLLKWGL TTPDKKHQKE PPFLWMGYEL HPDKWTVQPI QLPEKDSWTV NDIQKLVGKL
     NWASQIYAGI KVRQLCKLLR GTKALTDIVP LTEEAELELA ENREILKEPV HGVYYDPSKD
     LIAEIQKQGD DQWTYQIYQE PFKNLKTGKY AKMRTAHTND VKQLTEAVQK IALESIVIWG
     KTPKFRLPIQ KETWEIWWTD YWQATWIPEW EFVNTPPLVK LWYQLEKEPI IGAETFYVDG
     AANRETKLGK AGYVTDRGRQ KIISLAETTN QKTELQAIQL ALQDSGSEVN IVTDSQYALG
     IIQAQPDKSE SELVNQIIEQ LIRKERVYLS
//
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