POL_ALV
ID POL_ALV Reviewed; 895 AA.
AC Q7SQ98;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Pol polyprotein;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE Short=RT;
DE EC=2.7.7.49;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:Q04095};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q04095};
DE AltName: Full=pp32;
GN Name=pol;
OS Avian leukosis virus (ALV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=11864;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14993650; DOI=10.1099/vir.0.79778-0;
RA Tomioka Y., Ochiai K., Ohashi K., Ono E., Toyoda T., Kimura T., Umemura T.;
RT "Genome sequence analysis of the avian retrovirus causing so-called fowl
RT glioma and the promoter activity of the long terminal repeat.";
RL J. Gen. Virol. 85:647-652(2004).
CC -!- FUNCTION: During replicative cycle of retroviruses, the reverse-
CC transcribed viral DNA is integrated into the host chromosome by the
CC viral integrase enzyme. RNase H activity is associated with the reverse
CC transcriptase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 8 Mn(2+) or Mg(2+) ions per integrase homotetramer.
CC {ECO:0000250};
CC -!- SUBUNIT: The integrase forms a homotetramer. The reverse transcriptase
CC forms a heterodimer of alpha and beta subunits (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The integrase is composed of three domains. The N-terminal
CC domain is a zinc binding domain. The central domain is the catalytic
CC domain. The C-terminal domain is a non-specific DNA binding domain (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC pol-derived portion of gag-pol precursor is processed to yield the
CC reverse transcriptase beta subunit, which in turn is processed to yield
CC the reverse transcriptase alpha subunit and the integrase (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein is synthesized as a Gag-Pol polyprotein.
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DR EMBL; AB112960; BAC78443.1; -; Genomic_RNA.
DR SMR; Q7SQ98; -.
DR Proteomes; UP000149542; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase 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:UniProtKB-EC.
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: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; 2.30.30.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
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; 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; IPR010661; RVT_thumb.
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; PF00078; RVT_1; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 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 DNA integration; DNA recombination; DNA-binding; Endonuclease; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; RNA-directed DNA polymerase; Transferase;
KW Viral genome integration; Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..572
FT /note="Reverse transcriptase/ribonuclease H"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040978"
FT CHAIN 573..895
FT /note="Integrase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040979"
FT DOMAIN 42..230
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 441..572
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 625..788
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 573..613
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 794..842
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 843..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 612
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 636
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT BINDING 729
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 895 AA; 98588 MW; 768028C3E5830073 CRC64;
TVALHLAIPL KWKPDHTPVW IDQWPLPEGK LVALTQLVEK ELQLGHIEPS LSCWNTPVFV
IRKASGSYRL LHDLRAVNAK LVPFGAVQQG APVLSALPRG WPLMVLDLKD CFFSIPLAEQ
DREAFAFTLP SVNNQAPARR FQWKVLPQGM TCSPTICQLV VGQVLEPLRL KHPSLRMLHY
MDDLLLAASS HDGLEAAGEE VISTLERAGF TISPDKIQRE PGVQYLGYKL GSTYVAPVGL
VAEPRIATLW DVQKLVGSLQ WLRPALGIPP RLMGPFYEQL RGSDPNEARE WNLDMKMAWR
EIVQLSTTAA LERWDPALPL EGAVARCEQG AIGVLGQGLS THPRPCLWLF STQPTKAFTA
WLEVLTLLIT KLRASAVRTF GKEVDILLLP ACFREDLPLP EGILLALKGF AGKIRSSDTP
SIFDIARPLH VSLKVRVTDH PVPGPTVFTD ASSSTHKGVV VWREGPRWEI KEIADSGASV
QQLEARAVAM ALLLWPTTPT NVVTDSAFVA KMLLKMGQEG VPSTAAAFIL EDALSQRSAM
AAVLHVRSHS EVPGFFTEGN DVADSQATFQ AYPLREAKDL HTALHIGPRA LSKACNISMQ
QAREVVQTCP HCNSAPALEA GVNPRGLGPL QIWQTDFTLE PRMAPRSWLA VTVDTASSAI
VVTQHGRVTS VAAQHHWATA IAVLGRPKAI KTDNGSCFTS KSTREWLARW GIAHTTGIPG
NSQGQAMVER ANRLLKDKIR VLAEGDGFMK RIPTSKQGEL LAKAMYALNH FERGENTKTP
IQKHWRPTVL TEGPPVKIRI ETGEWEKGWN VLVWGRGYAA VKNRDTDKVI WVPSRKVKPD
ITQKDEVTKK DEASPLFAGI SDWAPWKGEQ EGLQEEVASN KQERPGEDTL AANES
