ID C1JHV0_9HIV1 Unreviewed; 683 AA.
AC C1JHV0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACO50668.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACO50668.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACO50668.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACO50668.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BR021 {ECO:0000313|EMBL:ACO50668.1};
RA Kawashima Y., Pfafferott K., Frater J., Matthews P., Payne R., Addo M.,
RA Gatanaga H., Fujiwara M., Hachiya A., Koizumi H., Kuse N., Oka S., Duda A.,
RA Prendergast A., Crawford H., Leslie A., Brumme Z., Brumme C., Allen T.,
RA Brander C., Kaslow R., Tang J., Hunter E., Allen S., Mulenga J., Branch S.,
RA Roach T., John M., Mallal S., Ogwu A., Shapiro R., Prado J.G., Fidler S.,
RA Weber J., Pybus O.G., Klenerman P., Ndung'u T., Phillips R., Heckerman D.,
RA Harrigan P.R., Walker B.D., Takiguchi M., Goulder P.;
RT "Adaptation of HIV-1 to human leukocyte antigen class I.";
RL Nature 458:641-645(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 ---------------------------------------------------------------------------
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; FJ645511; ACO50668.1; -; Genomic_DNA.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; 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: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 Gene3D; 1.10.10.200; -; 1.
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; 2.
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; 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; 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; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 2.
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 4: Predicted;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
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};
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};
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 1..128
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 328..451
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT DOMAIN 457..498
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS50876"
FT DOMAIN 508..658
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACO50668.1"
FT NON_TER 683
FT /evidence="ECO:0000313|EMBL:ACO50668.1"
SQ SEQUENCE 683 AA; 77687 MW; 5AD69F32343F2C28 CRC64;
TVLDVGDAYF SVPLDKESGK YTAFTIPSVN NETPGIRYQY NVLPQGWKGS PAIFQCSMTK
ILEPFRKHNP EIVIYQYMDD LYVGSDLEIG QHRAKIEDLR AHLLKWGFTT PDKKHQKEPP
FLWMGYELHP DKWTVQPIVL PEKDSWTVND IQKLVGKLNW ASQIYSGIKV RQLCKLLRGT
KALTEVVPLT TEAELELAEN REILREPVHG VYYDPSKDLI AEIQKQEHGQ WSYQIYQEPF
KNLKTGKYAR MRGAHTNDVR QLTEAVQKIA AESIVIWGKI PKFKLPIQKE TWEAWWTEYW
QATWIPEWEF VNTPPLVKLW YQLEKEPIVG AETFYVDGAA NRETKLGKAG YVTDRGRQKV
VSLTDTSNQK TELQAIHLAL QDSGLEVNIV TDSQYALGII QAQPDKSESE LVNQIIEQLI
KKEKVYLAWV PAHKGIGGNE QVDKLVSAGI RKVLFLDGID KAQEEHEKYH NNWRAMASDF
NLPPVVAREI VASCDKCQLK GEAMHGQVDC SPGIWQLDCT HLEGKVILVA VHVASGYIEA
EVIPAETGQE TAYFLLKLAG RWPVKTIHTD NGSNFTSATV KAACWWAGIK QEFGIPYNPQ
SQGVVESMNK ELKKIIGQVR DQAEHLKTAV QMAVFIHNFK RKGGIGGYSA GERIIDIIAT
DMQTKELQKQ ITNIQKFRVY YRA
//
