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Database: UniProt
Entry: H6CYU5_9HIV1
LinkDB: H6CYU5_9HIV1
Original site: H6CYU5_9HIV1 
ID   H6CYU5_9HIV1            Unreviewed;      1006 AA.
AC   H6CYU5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:AFB38374.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:AFB38374.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AFB38374.1, ECO:0000313|Proteomes:UP000151763};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AFB38374.1, ECO:0000313|Proteomes:UP000151763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USPI90770EI129y95111pcWG2B10 {ECO:0000313|EMBL:AFB38374.1};
RX   PubMed=21593162; DOI=10.1128/JVI.02697-10;
RA   Herbeck J.T., Rolland M., Liu Y., McLaughlin S., McNevin J., Zhao H.,
RA   Wong K., Stoddard J.N., Raugi D., Sorensen S., Genowati I., Birditt B.,
RA   McKay A., Diem K., Maust B.S., Deng W., Collier A.C., Stekler J.D.,
RA   McElrath M.J., Mullins J.I.;
RT   "Demographic processes affect HIV-1 evolution in primary infection before
RT   the onset of selective processes.";
RL   J. Virol. 85:7523-7534(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC         hybrid.; EC=3.1.13.2; Evidence={ECO:0000256|ARBA:ARBA00000379};
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; JN024323; AFB38374.1; -; Genomic_RNA.
DR   Proteomes; UP000151763; Genome.
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:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
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:0008270; F:zinc ion binding; 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   CDD; cd01645; RT_Rtv; 1.
DR   Gene3D; 1.10.10.200; -; 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; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR017856; Integrase-like_N.
DR   InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR   InterPro; IPR001037; Integrase_C_retrovir.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR003308; Integrase_Zn-bd_dom_N.
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:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR   Pfam; PF00552; IN_DBD_C; 1.
DR   Pfam; PF02022; Integrase_Zn; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF00665; rve; 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; SSF50122; DNA-binding domain of retroviral integrase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS51027; INTEGRASE_DBD; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50876; ZF_INTEGRASE; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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   Viral release from host cell {ECO:0000256|ARBA:ARBA00023113};
KW   Virion maturation {ECO:0000256|ARBA:ARBA00023113};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00450}.
FT   DOMAIN          79..148
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          202..392
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          592..715
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   DOMAIN          721..762
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50876"
FT   DOMAIN          772..922
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   DOMAIN          941..988
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51027"
FT   DNA_BIND        941..988
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00506"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFB38374.1"
SQ   SEQUENCE   1006 AA;  113804 MW;  FFB796BFF075A586 CRC64;
     FFREDLAFPQ GEAREFSSEQ TRANSPNSPT RGELQVWGRD NDSLSEAGAD RQGNVSFNLP
     QITLRQRPLV TVKIGGQLKE ALLDTGADDT VLEEMNLPGR WKPKMIGGIG GFIKVRQYDQ
     ILIEICGHKA IGTVLIGPTP VNIIGRNLLT QIGCTLNFPI SPIETVPVKL KPGMDGPKVK
     QWPLTEEKIK ALVEICTEME KEGKISKIGP ENPYNTPVFA IKKKDGTKWR KLVDFRELNK
     RTQDFWEVQL GIPHPAGLKK KKSVTVLDVG DAYFSVPLDE DFRKYTAFTI PSTNNETPGI
     RYQYNVPPQG WKGSPAIFQS SMTKILEPFR KQNPDIVIYQ YMDDLYVGSD LEIGQHRIKI
     EELRQHLLGW GFTTPDKKHQ KEPPFLWMGY ELHPDKWTVQ PIVLPEKDSW TVNDIQKLVG
     KLNWASQIYA GIKVKQLCKL LRGTKALTDV IPLTEEAELE LAENRKILKE PVHGVYYDPS
     KELISEIQKQ GQGQWTYQIY QEPFKNLKTG KYARTRGAHT NDVKQLTEAV QKIASESIII
     WGKTPKFRLP ILRETWDTWW TEYWQATWIP EWEFVNTPPL VKLWYQLEKE PIVGAETFYV
     DGAANRETKL GKAGYVTNRG RQKVVSLTDT TNQKTELQAI HLALQDSGLE VNIVTDSQYA
     LGIIQAQPDK SESELVNQII EQLIKKEKVY LAWVPAHKGI GGNEQVDKLV SAGIRKILFL
     DGIDKAQEEH EKYHNNWRAM ASDFNIPPIV AKEIVACCDK CQLKGEAMHG QVDCSPGIWQ
     LDCTHLEGKV IVVAVHVASG YIEAEVIPAE TGQETAYFIL KLAGRWPVKT IHTDSGPNFT
     STAVKAACWW AGIKQEFGIP YNPQSQGVVE SMNKELKKII GQVRDQAEQL KTAVQMAVLI
     HNFKRKGGIG GYSAGERIID IIATDIQTKE LQKRITKIRN FRVYYRDSRD PLWKGPAKLL
     WKGEGAVVIQ DNSDIKAVPR RKAKIIRDYG KQMAGDDCVA SRQDED
//
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