POL_IPMAI
ID POL_IPMAI Reviewed; 814 AA.
AC P12894;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Intracisternal A-particle Pol-related 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 Flags: Fragment;
OS Mouse intracisternal a-particle IL3 (IAP-IL3).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Intracisternal A-particles.
OX NCBI_TaxID=11754;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3016667; DOI=10.1093/nar/14.14.5901;
RA Ymer S., Tucker W.Q.J., Campbell H.D., Young I.G.;
RT "Nucleotide sequence of the intracisternal A-particle genome inserted 5' to
RT the interleukin-3 gene of the leukemia cell line WEHI-3B.";
RL Nucleic Acids Res. 14:5901-5918(1986).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
CC Note=The RT polymerase active site binds 2 magnesium ions.
CC {ECO:0000255|PROSITE-ProRule:PRU00405};
CC -!- MISCELLANEOUS: [Intracisternal A-particle Pol-related polyprotein]:
CC Intracisternal A particles (IAPs) are defective retroviral elements.
CC Due to extensive mutations in the envelope coding sequence, IAPs can
CC only form defective viral particles confined to the intracisternae of
CC the Golgi. IAPs are an important class of transposable elements that
CC induce genomic mutations and cell transformation by disrupting gene
CC expression. {ECO:0000305}.
CC -!- MISCELLANEOUS: Reverse transcriptase/ribonuclease HThe reverse
CC transcriptase is an error-prone enzyme that lacks a proof-reading
CC function. High mutations rate is a direct consequence of this
CC characteristic. RT also displays frequent template swiching leading to
CC high recombination rate. Recombination mostly occurs between homologous
CC regions of the two copackaged RNA genomes. If these two RNA molecules
CC derive from different viral strains, reverse transcription will give
CC rise to highly recombinated proviral DNAs. {ECO:0000255|PROSITE-
CC ProRule:PRU00405}.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
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DR EMBL; X04120; CAA27732.1; -; Genomic_DNA.
DR PIR; A23597; GNMSIP.
DR SMR; P12894; -.
DR PRIDE; P12894; -.
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: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; IPR000721; Gag_p24_N.
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; IPR008919; Retrov_capsid_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; PF00607; Gag_p24; 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; PF00078; RVT_1; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF47943; SSF47943; 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-binding; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleotidyltransferase;
KW RNA-directed DNA polymerase; Transferase; Transposable element;
KW Viral genome integration; Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN <1..814
FT /note="Intracisternal A-particle Pol-related polyprotein"
FT /id="PRO_0000125488"
FT CHAIN <1..511
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000443273"
FT CHAIN 512..814
FT /note="Integrase"
FT /id="PRO_0000443274"
FT DOMAIN 1..159
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 373..503
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 561..733
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 507..548
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 727..776
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 411
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 572
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 629
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT SITE 512..513
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03365"
FT NON_TER 1
SQ SEQUENCE 814 AA; 91001 MW; A369620A450F729A CRC64;
MALTPADWQM IAKAALPNMG KYLEWRSLWR EAAQAQARAN AAALTPEQRD WTFDLLTGQR
AYSAKPDKRY QWKVLPQGMS NSPTMCQLYV QKALLPVREQ FPSLILLLYM DDILLCHKDL
TMLQKAYPFL LKTLSQWGLQ IATEKVQISD TGQFLGSVVS PDKIVPQKVE IRRDHLHTLN
DFQKLLGDIN WLRPFLKIPS AELRPLFSIL EGDPHISSPR TLTLAANQAL QKVEKALQNA
QLQRIEDSQP FSLCVFKTAQ LPTAVLWQNG PLLWIHPNVS PAKIIDWYPD AIAQLALKGL
KAAITHFGQS PYLLIVPYTA AQVQTLAAAS NDWAVLVTSF SGKIDNHYPK HPILQFAQNQ
SVVFPQITVR NPLKNGIVVY TDGSKTGIGA YVANGKVVSK QYNENSPQVV ECLVVLEVLK
TFLKPLNIVS DSYYVVNAVN LLEVAGVIKP SSRVANIFQQ IQLVLLSRRS PVYITHVRAH
SGLPGPMALG NDLADKATKV VAAALSSPVE AARNFHNNFH VTAETLRSRF SLTRKEARDI
VTQCQSCCEF LPVPHVGINP RGIRPLQVWQ MDVTHVSSFG KLQYLHVSID TCSGIMFASP
LTGEKASHVI QHCLEAWSAW GKPRLLKTDN GPAYTSQKFQ QFCRQMDVTH LTGLPYNPQG
QGIVERAHRT LKAYLIKQKR GTFEETVPRA PRVSVSLALF TLNFLNIDAH GHTAAERHCS
EPDRPNEMVK WKNVLDNKWY GPDPILIRSR GAICVFPQNE DNPFWVPERL TRKIQTDQGN
TNVPRLGDVQ GVNNKERAAL GDNVDISTPN DGDV
