ID C8C6W0_9HIV1 Unreviewed; 911 AA.
AC C8C6W0;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACU55265.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACU55265.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACU55265.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACU55265.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D8572TOB8U {ECO:0000313|EMBL:ACU55265.1};
RX PubMed=19690614; DOI=10.1371/journal.pone.0006687;
RA Brumme Z.L., John M., Carlson J.M., Brumme C.J., Chan D., Brockman M.A.,
RA Swenson L.C., Tao I., Szeto S., Rosato P., Sela J., Kadie C., Frahm N.,
RA Brander C., Haas D.W., Riddler S., Haubrich R., Walker B.D., Harrigan P.R.,
RA Heckerman D., Mallal S.;
RT "HLA-associated immune escape pathways in HIV-1 subtype B Gag, Pol and Nef
RT proteins.";
RL PLoS ONE 4:e6687-e6687(2009).
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; GQ371833; ACU55265.1; -; 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: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 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; 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; 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; 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; 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; 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 78..147
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 201..391
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 591..714
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT DOMAIN 720..761
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS50876"
FT DOMAIN 771..871
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 27..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACU55265.1"
FT NON_TER 911
FT /evidence="ECO:0000313|EMBL:ACU55265.1"
SQ SEQUENCE 911 AA; 102799 MW; 77CF87EC511EA3F2 CRC64;
FFRENLAFPQ XKARXFSSEQ TRALSPTRRE LQVWGRDNNS PSEAGAGTDR QGTVSFSFPQ
ITLWQRPLVT IRIGGQLKEA LLDTGADDTV LEDMSLPGKW KPKMIGGIGG FIKVRQYDQI
LXEICGHKVT GTVLVGPTPV NIIGRNLLTQ LGCTLNFPIX PIETVPVKLK XXXXXXXXXX
XXLTEEKXXA LXEICTEMXK EGKISKIGPE NPXNTPVXAI KKKXSTKWRK LVDFXELXKR
TQDFWEVQLG IPHPAGLKKK KSVTVLDVGD AYFSVPLXKD FRKYTAFTIP SINNETPGIR
YQYNVLPQGW KGSPAIFQCS MTKILEXFRK QNPDIVIYQY MDDLYVGSDL EIGXHRTXIE
ELRQHLLSWG FTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IQLPEKDSWT VNDIQKLVGK
LNWASQIYAG IKVKQLCKLL RGTKALTEVV PLTXEAELEL AENKEILKEP VHGVYYDPSK
DLVAEVQKQG QGQWTYQIYQ EPFKNLKTGK YARMRGAHTN DVKQLTEAVQ KIAAESIVIW
GKTPKFKLPI QKETWEAWWM EYWQATWIPE WEFVNTPPLV KLWYQLEKEP IAGAETFYVD
GAANRETXLG KAGYVTDRGR QKVVPLADTT NQKTELQAIH LALQDXGLEG NMVTDSQYAL
GIIQAQPDKS ESEIVSQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDKLVS XGIRXVLFLD
GIDKAQEDHE KYHSNWRAMA SEFNLPPIVA KEIVASCDKC QLKGEAMHGQ VDCSPGIWQL
DCTHLEGKII LVAVHVASGY IEAEVIPAET GQETAYFLLK LAGRWPVTTI HTDNGPNFIS
NTVKAACWWA GIKQEFGIPY NPQSQGVVES MXXXXXXXXX XXXXXXXXXX XXXXXXXFIH
NFKRKGGIGG Y
//
