ID E9N760_9HIV1 Unreviewed; 659 AA.
AC E9N760;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ADV56940.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ADV56940.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ADV56940.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADV56940.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ADRT-T48-AFMC {ECO:0000313|EMBL:ADV56940.1};
RA Patil R.T., Gupta R.M., Sen S., Chaturbhuj D.N., Hingankar N.K.,
RA Tripathy S.P., Paranjape R.S.;
RT "Emergence of drug resistance amongst human immunodeficiency virus type 1
RT infected individuals at the end of 12 months of first line ART initiation
RT in India.";
RL Submitted (NOV-2010) 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}.
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DR EMBL; HQ456680; ADV56940.1; -; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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:0046718; P:viral entry into host cell; 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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; 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; 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 SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 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:ARBA00022908};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004064};
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, 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:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 20..89
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 143..333
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 533..656
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT UNSURE 616
FT /note="I or L"
FT /evidence="ECO:0000313|EMBL:ADV56940.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADV56940.1"
FT NON_TER 659
FT /evidence="ECO:0000313|EMBL:ADV56940.1"
SQ SEQUENCE 659 AA; 75137 MW; 2022F014201153D1 CRC64;
PQITLWQRPL VSIKIGGQIK EALLDTGADD TVLEEINLPG KWKPKMIGGI GGFIKVRQYD
QISIEICGKK AIGTVLVGPT PVNIIGRNML TQLGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALTXICXEM EKEGKITKIG PENPYNTPIF AIKKKDSTKW RKLVDFRELN
KRTQDFWEVQ LGIPHPAGLK KXKSXTVLDV GDAYFSVPLX EDFRKYTAFT IPSTNNETPG
IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RAQNPEIVIY QYMDDLYVGS DLEIGQHRAK
XEELRXHLLK WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIQLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVRQLCX LLRGAKALTD IVPLTDEAEL ELAENREILK EPVHGAYYDP
SKDLIAEIQK QGQDQWTYQI YQEPFKNLKT GKYAKMRTAH TNDVKQLTEA VQKIAMESIV
IWGKTPKFRL PIQKETWEAW WTDYWQATWI PEWEFVNTPP LVKLWYQLEK DPIAGVETFY
VDGAANRETK QGKAGYVTDR GRQKIVSLTE TTNQKTELQA IYLALQDSGS EVNIVTDSQY
ALGIIQAQPD KSESEXVNQI IEELIXKERV YLSWVPAHKG IGGNEQVDKL VSSGIRKVL
//
