YG31B_YEAST
ID YG31B_YEAST Reviewed; 1547 AA.
AC Q99315; D6VUP1; Q07096;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Transposon Ty3-G Gag-Pol polyprotein;
DE AltName: Full=Gag3-Pol3;
DE AltName: Full=Transposon Ty3-1 TYA-TYB polyprotein;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CA;
DE AltName: Full=p24;
DE Contains:
DE RecName: Full=Spacer peptide p3;
DE Contains:
DE RecName: Full=Nucleocapsid protein p11;
DE Short=NC;
DE Contains:
DE RecName: Full=Ty3 protease;
DE Short=PR;
DE EC=3.4.23.-;
DE AltName: Full=p16;
DE Contains:
DE RecName: Full=Spacer peptide J;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE Short=RT;
DE Short=RT-RH;
DE EC=2.7.7.49;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
DE AltName: Full=p55;
DE Contains:
DE RecName: Full=Integrase p61;
DE Short=IN;
DE Contains:
DE RecName: Full=Integrase p58;
DE Short=IN;
GN Name=TY3B-G; Synonyms=YGRWTy3-1 POL; OrderedLocusNames=YGR109W-B;
GN ORFNames=G5984;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AB950;
RX PubMed=2159534; DOI=10.1128/jvi.64.6.2599-2607.1990;
RA Hansen L.J., Sandmeyer S.B.;
RT "Characterization of a transpositionally active Ty3 element and
RT identification of the Ty3 integrase protein.";
RL J. Virol. 64:2599-2607(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8905931;
RX DOI=10.1002/(sici)1097-0061(19960930)12:12<1273::aid-yea21>3.0.co;2-j;
RA Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
RA Schreer A., Schaefer B., Zimmermann M., Wolf K.;
RT "The sequence of a 23.4 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3
RT element and 11 new open reading frames.";
RL Yeast 12:1273-1277(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=2447089; DOI=10.1016/s0021-9258(19)57319-7;
RA Clark D.J., Bilanchone V.W., Haywood L.J., Dildine S.L., Sandmeyer S.B.;
RT "A yeast sigma composite element, TY3, has properties of a
RT retrotransposon.";
RL J. Biol. Chem. 263:1413-1423(1988).
RN [6]
RP FUNCTION OF REVERSE TRANSCRIPTASE, AND SUBCELLULAR LOCATION.
RX PubMed=1371165; DOI=10.1128/jvi.66.3.1414-1424.1992;
RA Hansen L.J., Chalker D.L., Orlinsky K.J., Sandmeyer S.B.;
RT "Ty3 GAG3 and POL3 genes encode the components of intracellular
RT particles.";
RL J. Virol. 66:1414-1424(1992).
RN [7]
RP RIBOSOMAL FRAMESHIFT SITE.
RX PubMed=8267715; DOI=10.1016/0092-8674(93)90297-4;
RA Farabaugh P.J., Zhao H., Vimaladithan A.;
RT "A novel programmed frameshift expresses the POL3 gene of retrotransposon
RT Ty3 of yeast: frameshifting without tRNA slippage.";
RL Cell 74:93-103(1993).
RN [8]
RP ERRATUM OF PUBMED:8267715.
RA Farabaugh P.J., Zhao H., Vimaladithan A.;
RL Cell 75:826-826(1993).
RN [9]
RP PROTEOLYTIC PROCESSING, AND CLEAVAGE SITES.
RX PubMed=7677953; DOI=10.1128/jvi.67.1.19-28.1993;
RA Kirchner J., Sandmeyer S.B.;
RT "Proteolytic processing of Ty3 proteins is required for transposition.";
RL J. Virol. 67:19-28(1993).
RN [10]
RP FUNCTION OF NUCLEOCAPSID, AND MUTAGENESIS OF CYS-267 AND HIS-275.
RX PubMed=7515969; DOI=10.1128/jvi.68.7.4152-4166.1994;
RA Orlinsky K.J., Sandmeyer S.B.;
RT "The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3
RT polyproteins.";
RL J. Virol. 68:4152-4166(1994).
RN [11]
RP NOMENCLATURE.
RX PubMed=9582191; DOI=10.1101/gr.8.5.464;
RA Kim J.M., Vanguri S., Boeke J.D., Gabriel A., Voytas D.F.;
RT "Transposable elements and genome organization: a comprehensive survey of
RT retrotransposons revealed by the complete Saccharomyces cerevisiae genome
RT sequence.";
RL Genome Res. 8:464-478(1998).
RN [12]
RP FUNCTION OF REVERSE TRANSCRIPTASE.
RX PubMed=10593967; DOI=10.1074/jbc.274.51.36643;
RA Cristofari G., Gabus C., Ficheux D., Bona M., Le Grice S.F.J.,
RA Darlix J.-L.;
RT "Characterization of active reverse transcriptase and nucleoprotein
RT complexes of the yeast retrotransposon Ty3 in vitro.";
RL J. Biol. Chem. 274:36643-36648(1999).
RN [13]
RP CHARACTERIZATION OF PEPTIDE J.
RX PubMed=11152529; DOI=10.1128/jvi.75.3.1557-1560.2001;
RA Claypool J.A., Malik H.S., Eickbush T.H., Sandmeyer S.B.;
RT "Ten-kilodalton domain in Ty3 Gag3-Pol3p between PR and RT is dispensable
RT for Ty3 transposition.";
RL J. Virol. 75:1557-1560(2001).
RN [14]
RP REVIEW.
RX PubMed=16093660; DOI=10.1159/000084940;
RA Lesage P., Todeschini A.L.;
RT "Happy together: the life and times of Ty retrotransposons and their
RT hosts.";
RL Cytogenet. Genome Res. 110:70-90(2005).
RN [15]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, CLEAVAGE SITE
RP GLY-207-208-ALA, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15956549; DOI=10.1128/jvi.79.13.8032-8045.2005;
RA Kuznetsov Y.G., Zhang M., Menees T.M., McPherson A., Sandmeyer S.B.;
RT "Investigation by atomic force microscopy of the structure of Ty3
RT retrotransposon particles.";
RL J. Virol. 79:8032-8045(2005).
CC -!- FUNCTION: Capsid protein (CA) is the structural component of the virus-
CC like particle (VLP), forming the shell that encapsulates the genomic
CC RNA-nucleocapsid complex.
CC -!- FUNCTION: Nucleocapsid protein p11 (NC) forms the nucleocore that coats
CC the retro-elements dimeric RNA. Binds these RNAs through its zinc
CC fingers (By similarity). Promotes primer tRNA(i)-Met annealing to the
CC multipartite primer-binding site (PBS), dimerization of Ty3 RNA and
CC initiation of reverse transcription. {ECO:0000250,
CC ECO:0000269|PubMed:10593967, ECO:0000269|PubMed:1371165,
CC ECO:0000269|PubMed:2159534, ECO:0000269|PubMed:7515969}.
CC -!- FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages
CC of the Gag and Gag-Pol polyproteins after assembly of the VLP.
CC -!- FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a
CC multifunctional enzyme that catalyzes the conversion of the retro-
CC elements RNA genome into dsDNA within the VLP. The enzyme displays a
CC DNA polymerase activity that can copy either DNA or RNA templates, and
CC a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-
CC DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA
CC primers. The conversion leads to a linear dsDNA copy of the
CC retrotransposon that includes long terminal repeats (LTRs) at both
CC ends.
CC -!- FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a
CC subparticle preintegration complex (PIC) containing at least integrase
CC and the newly synthesized dsDNA copy of the retrotransposon must
CC transit the nuclear membrane. Once in the nucleus, integrase performs
CC the integration of the dsDNA into the host genome.
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 -!- SUBUNIT: The protease is a homodimer, whose active site consists of two
CC apposed aspartic acid residues.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1371165}. Nucleus
CC {ECO:0000269|PubMed:1371165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=The Gag-Pol polyprotein is generated by a +1 ribosomal
CC frameshift. {ECO:0000269|PubMed:8267715};
CC Name=Transposon Ty3-G Gag-Pol polyprotein;
CC IsoId=Q99315-1; Sequence=Displayed;
CC Name=Transposon Ty3-G Gag polyprotein;
CC IsoId=Q12173-1; Sequence=External;
CC -!- DOMAIN: Integrase core domain contains the D-x(n)-D-x(35)-E motif,
CC named for the phylogenetically conserved glutamic acid and aspartic
CC acid residues and the invariant 35 amino acid spacing between the
CC second and third acidic residues. Each acidic residue of the D,D(35)E
CC motif is independently essential for the 3'-processing and strand
CC transfer activities of purified integrase protein.
CC -!- PTM: Initially, virus-like particles (VLPs) are composed of the
CC structural unprocessed proteins Gag and Gag-Pol, and also contain the
CC host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer
CC for minus-strand DNA synthesis, and a dimer of genomic Ty RNA.
CC Processing of the polyproteins occurs within the particle and proceeds
CC by an ordered pathway, called maturation. First, the protease (PR) is
CC released by autocatalytic cleavage of the Gag-Pol polyprotein, and this
CC cleavage is a prerequisite for subsequent processing at the remaining
CC sites to release the mature structural and catalytic proteins.
CC Maturation takes place prior to the RT reaction and is required to
CC produce transposition-competent VLPs. {ECO:0000269|PubMed:15956549,
CC ECO:0000269|PubMed:7677953}.
CC -!- MISCELLANEOUS: Retrotransposons are mobile genetic entities that are
CC able to replicate via an RNA intermediate and a reverse transcription
CC step. In contrast to retroviruses, retrotransposons are non-infectious,
CC lack an envelope and remain intracellular. Ty3 retrotransposons belong
CC to the gypsy-like elements (metaviridae).
CC -!- MISCELLANEOUS: [Isoform Transposon Ty3-G Gag-Pol polyprotein]: Produced
CC by +1 ribosomal frameshifting between codon Ala-285 and Val-286 of the
CC YGR109W-A ORF.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98435.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA97115.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA97117.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=DAA08202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M34549; AAA98435.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z72894; CAA97115.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z72895; CAA97117.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M18353; AAA66936.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08202.1; ALT_SEQ; Genomic_DNA.
DR PIR; S22875; S22875.
DR PIR; S69842; S69842.
DR RefSeq; NP_011624.1; NM_001184381.2.
DR PDB; 4OL8; X-ray; 3.10 A; A/B/E/F=536-1011.
DR PDB; 7Q5B; EM; 3.98 A; A/B/C/D=1-1547.
DR PDBsum; 4OL8; -.
DR PDBsum; 7Q5B; -.
DR AlphaFoldDB; Q99315; -.
DR SMR; Q99315; -.
DR BioGRID; 33356; 2.
DR STRING; 4932.YGR109W-B; -.
DR MEROPS; A02.022; -.
DR iPTMnet; Q99315; -.
DR PaxDb; Q99315; -.
DR PRIDE; Q99315; -.
DR GeneID; 853006; -.
DR KEGG; sce:YGR109W-B; -.
DR SGD; S000007347; YGR109W-B.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_000384_9_7_1; -.
DR InParanoid; Q99315; -.
DR ChiTaRS; YGR109W-B; yeast.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q99315; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000943; C:retrotransposon nucleocapsid; ISS:SGD.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISS:SGD.
DR GO; GO:0008233; F:peptidase activity; ISS:SGD.
DR GO; GO:0004540; F:ribonuclease activity; ISS:SGD.
DR GO; GO:0003723; F:RNA binding; ISS:SGD.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; ISS:SGD.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0032197; P:transposition, RNA-mediated; ISS:SGD.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR024650; Peptidase_A2B.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR InterPro; IPR045358; Ty3_capsid.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF12384; Peptidase_A2B; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF19259; Ty3_capsid; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aspartyl protease; ATP-binding; Cytoplasm;
KW DNA integration; DNA recombination; DNA-binding;
KW DNA-directed DNA polymerase; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Protease; Reference proteome;
KW Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Transposable element; Viral release from host cell;
KW Virion maturation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15956549"
FT CHAIN 2..1547
FT /note="Transposon Ty3-G Gag-Pol polyprotein"
FT /id="PRO_0000279356"
FT CHAIN 2..207
FT /note="Capsid protein"
FT /id="PRO_0000279357"
FT PEPTIDE 208..233
FT /note="Spacer peptide p3"
FT /id="PRO_0000279358"
FT CHAIN 234..309
FT /note="Nucleocapsid protein p11"
FT /id="PRO_0000279359"
FT CHAIN 310..442
FT /note="Ty3 protease"
FT /id="PRO_0000279360"
FT PEPTIDE 443..535
FT /note="Spacer peptide J"
FT /evidence="ECO:0000255"
FT /id="PRO_0000279361"
FT CHAIN 536..1011
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000279362"
FT CHAIN 1012..1547
FT /note="Integrase p61"
FT /id="PRO_0000279363"
FT CHAIN 1038..1547
FT /note="Integrase p58"
FT /id="PRO_0000279364"
FT DOMAIN 620..797
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 893..1011
FT /note="RNase H Ty3/gyspy-type"
FT DOMAIN 1159..1324
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 265..282
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1106..1145
FT /note="Integrase-type zinc finger-like"
FT ACT_SITE 336
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 686
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 893
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 936
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 961
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT BINDING 1236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT SITE 207..208
FT /note="Cleavage; by Ty3 protease"
FT SITE 233..234
FT /note="Cleavage; by Ty3 protease"
FT SITE 309..310
FT /note="Cleavage; by Ty3 protease"
FT SITE 442..443
FT /note="Cleavage; by Ty3 protease"
FT /evidence="ECO:0000255"
FT SITE 535..536
FT /note="Cleavage; by Ty3 protease"
FT SITE 1011..1012
FT /note="Cleavage; by Ty3 protease"
FT SITE 1037..1038
FT /note="Cleavage; by Ty3 protease; partial"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:15956549"
FT MUTAGEN 267
FT /note="C->S: Reduces level of VLP formation and
FT maturation."
FT /evidence="ECO:0000269|PubMed:7515969"
FT MUTAGEN 275
FT /note="H->Q: Reduces level of VLP formation and
FT maturation."
FT /evidence="ECO:0000269|PubMed:7515969"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 558..563
FT /evidence="ECO:0007829|PDB:4OL8"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 608..621
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 636..640
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 646..650
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 653..656
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 669..673
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 681..687
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 690..693
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 698..704
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 725..737
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 749..756
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 757..773
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 806..809
FT /evidence="ECO:0007829|PDB:4OL8"
FT TURN 810..814
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 821..832
FT /evidence="ECO:0007829|PDB:4OL8"
FT TURN 833..837
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 841..844
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 849..853
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 863..871
FT /evidence="ECO:0007829|PDB:4OL8"
FT TURN 876..878
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 884..891
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 899..906
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 908..911
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 913..921
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 932..944
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 948..951
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 957..959
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 965..969
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 970..972
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 976..986
FT /evidence="ECO:0007829|PDB:4OL8"
FT STRAND 997..1000
FT /evidence="ECO:0007829|PDB:4OL8"
FT HELIX 1001..1008
FT /evidence="ECO:0007829|PDB:4OL8"
SQ SEQUENCE 1547 AA; 178307 MW; 0E327D91E0575F78 CRC64;
MSFMDQIPGG GNYPKLPVEC LPNFPIQPSL TFRGRNDSHK LKNFISEIML NMSMISWPND
ASRIVYCRRH LLNPAAQWAN DFVQEQGILE ITFDTFIQGL YQHFYKPPDI NKIFNAITQL
SEAKLGIERL NQRFRKIWDR MPPDFMTEKA AIMTYTRLLT KETYNIVRMH KPETLKDAME
EAYQTTALTE RFFPGFELDA DGDTIIGATT HLQEEYDSDY DSEDNLTQNG YVHTVRTRRS
YNKPMSNHRN RRNNNPSREE CIKNRLCFYC KKEGHRLNEC RARKAVLTDL ELESKDQQTP
FIKTLPIVHY IAIPEMDNTA EKTIKIQNTK VKTLFDSGSP TSFIRRDIVE LLKYEIYETP
PLRFRGFVAT KSAVTSEAVT IDLKINDLHI TLAAYILDNM DYQLLIGNPI LRRYPKILHT
VLNTRESPDS LKPKTYRSET VNNVRTYSAG NRGNPRNIKL SFAPTILEAT DPKSAGNRGD
SRTKTLSLAT TTPAAIDPLT TLDNPGSTQS TFAQFPIPEE ASILEEDGKY SNVVSTIQSV
EPNATDHSNK DTFCTLPVWL QQKYREIIRN DLPPRPADIN NIPVKHDIEI KPGARLPRLQ
PYHVTEKNEQ EINKIVQKLL DNKFIVPSKS PCSSPVVLVP KKDGTFRLCV DYRTLNKATI
SDPFPLPRID NLLSRIGNAQ IFTTLDLHSG YHQIPMEPKD RYKTAFVTPS GKYEYTVMPF
GLVNAPSTFA RYMADTFRDL RFVNVYLDDI LIFSESPEEH WKHLDTVLER LKNENLIVKK
KKCKFASEET EFLGYSIGIQ KIAPLQHKCA AIRDFPTPKT VKQAQRFLGM INYYRRFIPN
CSKIAQPIQL FICDKSQWTE KQDKAIDKLK DALCNSPVLV PFNNKANYRL TTDASKDGIG
AVLEEVDNKN KLVGVVGYFS KSLESAQKNY PAGELELLGI IKALHHFRYM LHGKHFTLRT
DHISLLSLQN KNEPARRVQR WLDDLATYDF TLEYLAGPKN VVADAISRAV YTITPETSRP
IDTESWKSYY KSDPLCSAVL IHMKELTQHN VTPEDMSAFR SYQKKLELSE TFRKNYSLED
EMIYYQDRLV VPIKQQNAVM RLYHDHTLFG GHFGVTVTLA KISPIYYWPK LQHSIIQYIR
TCVQCQLIKS HRPRLHGLLQ PLPIAEGRWL DISMDFVTGL PPTSNNLNMI LVVVDRFSKR
AHFIATRKTL DATQLIDLLF RYIFSYHGFP RTITSDRDVR MTADKYQELT KRLGIKSTMS
SANHPQTDGQ SERTIQTLNR LLRAYASTNI QNWHVYLPQI EFVYNSTPTR TLGKSPFEID
LGYLPNTPAI KSDDEVNARS FTAVELAKHL KALTIQTKEQ LEHAQIEMET NNNQRRKPLL
LNIGDHVLVH RDAYFKKGAY MKVQQIYVGP FRVVKKINDN AYELDLNSHK KKHRVINVQF
LKKFVYRPDA YPKNKPISST ERIKRAHEVT ALIGIDTTHK TYLCHMQDVD PTLSVEYSEA
EFCQIPERTR RSILANFRQL YETQDNPERE EDVVSQNEIC QYDNTSP
