POL_IPMA
ID POL_IPMA Reviewed; 867 AA.
AC P11368;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 109.
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;
GN Name=pol;
OS Mouse intracisternal a-particle MIA14 (IAP-MIA14).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Intracisternal A-particles.
OX NCBI_TaxID=11753;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3041022; DOI=10.1128/jvi.61.10.3020-3029.1987;
RA Mietz J.A., Grossman Z., Lueders K.K., Kuff E.L.;
RT "Nucleotide sequence of a complete mouse intracisternal A-particle genome:
RT relationship to known aspects of particle assembly and function.";
RL J. Virol. 61:3020-3029(1987).
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=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}.
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DR PIR; B26787; GNMSIA.
DR SMR; P11368; -.
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.
PE 3: Inferred from homology;
KW DNA integration; DNA recombination; DNA-binding; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; RNA-directed DNA polymerase; Transferase;
KW Transposable element; Viral genome integration; Virus entry into host cell.
FT CHAIN <1..867
FT /note="Intracisternal A-particle Pol-related polyprotein"
FT /id="PRO_0000125487"
FT CHAIN <1..592
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000443271"
FT CHAIN 593..867
FT /note="Integrase"
FT /id="PRO_0000443272"
FT DOMAIN 52..240
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 454..585
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 643..802
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT DNA_BIND 807..862
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 847..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 577
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 654
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 711
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT SITE 592..593
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03365"
FT NON_TER 1
SQ SEQUENCE 867 AA; 97779 MW; 7394B47ED63235B6 CRC64;
WKPRQTGSGF SLAAIGAARP IPWKTGDPVW VPQWHLSSEK LEAVIQLVEE QLKLGHIDPS
TSPWNTPIFV IKKKSGKWRL LHDLRPINEQ MNLFGPVQRG LPVLSALPRG WNLIIIDIKD
CFFSIPLCPR DRPRFAFTIP SINSDEPDNR YQWKVLPQGM SNSPTMCQLY VQEALLPVRE
QFPSLILLLY MDDILLCHKE LTMLQKAYPF LLKTLSQWGL QIATEKVQIS DTGQFLGSVV
SPDKIVPQKV EIRRDHLHTL NNFQKLLGDI NWLRPFLKIP SAELRPLFWY LEGDPHISSP
RTLTLAANQA LQKVEKALQN AQLQAIEDSQ PFSLCVFKTA QLPTAVLWQN GPLLWIHPNV
SPAKIIDWYP DAIAQLALKG LKAAITHFGR SPYLLIVPYT AAQVQTLAAT SNDWAVLVTS
FSGKIDNHYP KHPILQFAQN QSVVFPQITV RNPLKNGIVV YTDGSKTGIG AYVANGKVVS
KQYNENSPRM VECLVVLEVL KTFLEPLNIV SDSCYVVNAV NLLEGGWSDK PSSRVANIFQ
QIQLVLLSRS PVYITHVRAH SGLPTSAPWL SGNDLADKAT SGGCSLSSPV EAAQEIFITT
FHVTAEHYRS RNSLTRKEAR DIVTQCQSCC EFLPVPHVGI NPRGIRPLQV WQMDVTHVSS
FGKLQYLHVS IDTCSGIMFA SPLTGEKASH VIQHCLEAWS AWGKPRLLKT DNGPAYTSQK
FQQFCRQMDV THLTGLPYNP QGQGIVERAH RTLKTYLIKQ KRELEEILPQ HQESLSMALF
TLNFLNIDVH GHTAAERQCS EPDRPNEMVK WKNVLHNKWY GPDPILIRSR GAVCVFHRMK
TTHFGYQKDS PEKSRLTKGI PDVPRLW
