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Transposon Ty3-G Gag-Pol polyprotein (Gag3-Pol3) (Transposon Ty3-1 TYA-TYB polyprotein) [Cleaved into: Capsid protein (CA) (p24); Spacer peptide p3; Nucleocapsid protein p11 (NC); Ty3 protease (PR) (EC 3.4.23.-) (p16); Spacer peptide J; Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (p55); Integrase p61 (IN); Integrase p58 (IN)]

 YG31B_YEAST             Reviewed;        1547 AA.
Q99315; D6VUP1; Q07096;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 3.
27-SEP-2017, entry version 129.
RecName: Full=Transposon Ty3-G Gag-Pol polyprotein;
AltName: Full=Gag3-Pol3;
AltName: Full=Transposon Ty3-1 TYA-TYB polyprotein;
Contains:
RecName: Full=Capsid protein;
Short=CA;
AltName: Full=p24;
Contains:
RecName: Full=Spacer peptide p3;
Contains:
RecName: Full=Nucleocapsid protein p11;
Short=NC;
Contains:
RecName: Full=Ty3 protease;
Short=PR;
EC=3.4.23.-;
AltName: Full=p16;
Contains:
RecName: Full=Spacer peptide J;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
Short=RT-RH;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.4;
AltName: Full=p55;
Contains:
RecName: Full=Integrase p61;
Short=IN;
Contains:
RecName: Full=Integrase p58;
Short=IN;
Name=TY3B-G; Synonyms=YGRWTy3-1 POL; OrderedLocusNames=YGR109W-B;
ORFNames=G5984;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=AB950;
PubMed=2159534;
Hansen L.J., Sandmeyer S.B.;
"Characterization of a transpositionally active Ty3 element and
identification of the Ty3 integrase protein.";
J. Virol. 64:2599-2607(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8905931;
DOI=10.1002/(SICI)1097-0061(19960930)12:12<1273::AID-YEA21>3.0.CO;2-J;
Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
Schreer A., Schaefer B., Zimmermann M., Wolf K.;
"The sequence of a 23.4 kb segment on the right arm of chromosome VII
from Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57
genes, a Ty3 element and 11 new open reading frames.";
Yeast 12:1273-1277(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=2447089;
Clark D.J., Bilanchone V.W., Haywood L.J., Dildine S.L.,
Sandmeyer S.B.;
"A yeast sigma composite element, TY3, has properties of a
retrotransposon.";
J. Biol. Chem. 263:1413-1423(1988).
[6]
FUNCTION OF REVERSE TRANSCRIPTASE, AND SUBCELLULAR LOCATION.
PubMed=1371165;
Hansen L.J., Chalker D.L., Orlinsky K.J., Sandmeyer S.B.;
"Ty3 GAG3 and POL3 genes encode the components of intracellular
particles.";
J. Virol. 66:1414-1424(1992).
[7]
RIBOSOMAL FRAMESHIFT SITE.
PubMed=8267715; DOI=10.1016/0092-8674(93)90297-4;
Farabaugh P.J., Zhao H., Vimaladithan A.;
"A novel programed frameshift expresses the POL3 gene of
retrotransposon Ty3 of yeast: frameshifting without tRNA slippage.";
Cell 74:93-103(1993).
[8]
ERRATUM.
Farabaugh P.J., Zhao H., Vimaladithan A.;
Cell 75:826-826(1993).
[9]
PROTEOLYTIC PROCESSING, AND CLEAVAGE SITES.
PubMed=7677953;
Kirchner J., Sandmeyer S.B.;
"Proteolytic processing of Ty3 proteins is required for
transposition.";
J. Virol. 67:19-28(1993).
[10]
FUNCTION OF NUCLEOCAPSID, AND MUTAGENESIS OF CYS-267 AND HIS-275.
PubMed=7515969;
Orlinsky K.J., Sandmeyer S.B.;
"The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3
polyproteins.";
J. Virol. 68:4152-4166(1994).
[11]
NOMENCLATURE.
PubMed=9582191;
Kim J.M., Vanguri S., Boeke J.D., Gabriel A., Voytas D.F.;
"Transposable elements and genome organization: a comprehensive survey
of retrotransposons revealed by the complete Saccharomyces cerevisiae
genome sequence.";
Genome Res. 8:464-478(1998).
[12]
FUNCTION OF REVERSE TRANSCRIPTASE.
PubMed=10593967; DOI=10.1074/jbc.274.51.36643;
Cristofari G., Gabus C., Ficheux D., Bona M., Le Grice S.F.J.,
Darlix J.-L.;
"Characterization of active reverse transcriptase and nucleoprotein
complexes of the yeast retrotransposon Ty3 in vitro.";
J. Biol. Chem. 274:36643-36648(1999).
[13]
CHARACTERIZATION OF PEPTIDE J.
PubMed=11152529; DOI=10.1128/JVI.75.3.1557-1560.2001;
Claypool J.A., Malik H.S., Eickbush T.H., Sandmeyer S.B.;
"Ten-kilodalton domain in Ty3 Gag3-Pol3p between PR and RT is
dispensable for Ty3 transposition.";
J. Virol. 75:1557-1560(2001).
[14]
REVIEW.
PubMed=16093660; DOI=10.1159/000084940;
Lesage P., Todeschini A.L.;
"Happy together: the life and times of Ty retrotransposons and their
hosts.";
Cytogenet. Genome Res. 110:70-90(2005).
[15]
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, CLEAVAGE SITE
GLY-207-208-ALA, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15956549; DOI=10.1128/JVI.79.13.8032-8045.2005;
Kuznetsov Y.G., Zhang M., Menees T.M., McPherson A., Sandmeyer S.B.;
"Investigation by atomic force microscopy of the structure of Ty3
retrotransposon particles.";
J. Virol. 79:8032-8045(2005).
-!- FUNCTION: Capsid protein (CA) is the structural component of the
virus-like particle (VLP), forming the shell that encapsulates the
genomic RNA-nucleocapsid complex.
-!- FUNCTION: Nucleocapsid protein p11 (NC) forms the nucleocore that
coats the retro-elements dimeric RNA. Binds these RNAs through its
zinc fingers (By similarity). Promotes primer tRNA(i)-Met
annealing to the multipartite primer-binding site (PBS),
dimerization of Ty3 RNA and initiation of reverse transcription.
{ECO:0000250, ECO:0000269|PubMed:10593967,
ECO:0000269|PubMed:1371165, ECO:0000269|PubMed:2159534,
ECO:0000269|PubMed:7515969}.
-!- FUNCTION: The aspartyl protease (PR) mediates the proteolytic
cleavages of the Gag and Gag-Pol polyproteins after assembly of
the VLP.
-!- FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a
multifunctional enzyme that catalyzes the conversion of the retro-
elements RNA genome into dsDNA within the VLP. The enzyme displays
a DNA polymerase activity that can copy either DNA or RNA
templates, and a ribonuclease H (RNase H) activity that cleaves
the RNA strand of RNA-DNA heteroduplexes during plus-strand
synthesis and hydrolyzes RNA primers. The conversion leads to a
linear dsDNA copy of the retrotransposon that includes long
terminal repeats (LTRs) at both ends.
-!- FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a
subparticle preintegration complex (PIC) containing at least
integrase and the newly synthesized dsDNA copy of the
retrotransposon must transit the nuclear membrane. Once in the
nucleus, integrase performs the integration of the dsDNA into the
host genome.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester.
-!- SUBUNIT: The protease is a homodimer, whose active site consists
of two apposed aspartic acid residues.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1371165}.
Nucleus {ECO:0000269|PubMed:1371165}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=The Gag-Pol polyprotein is generated by a +1 ribosomal
frameshift. {ECO:0000269|PubMed:8267715};
Name=Transposon Ty3-G Gag-Pol polyprotein;
IsoId=Q99315-1; Sequence=Displayed;
Note=Produced by +1 ribosomal frameshifting between codon
Ala-285 and Val-286 of the YGR109W-A ORF.;
Name=Transposon Ty3-G Gag polyprotein;
IsoId=Q12173-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: Integrase core domain contains the D-x(n)-D-x(35)-E motif,
named for the phylogenetically conserved glutamic acid and
aspartic acid residues and the invariant 35 amino acid spacing
between the second and third acidic residues. Each acidic residue
of the D,D(35)E motif is independently essential for the 3'-
processing and strand transfer activities of purified integrase
protein.
-!- PTM: Initially, virus-like particles (VLPs) are composed of the
structural unprocessed proteins Gag and Gag-Pol, and contain also
the host initiator methionine tRNA (tRNA(i)-Met) which serves as a
primer for minus-strand DNA synthesis, and a dimer of genomic Ty
RNA. Processing of the polyproteins occurs within the particle and
proceeds by an ordered pathway, called maturation. First, the
protease (PR) is released by autocatalytic cleavage of the Gag-Pol
polyprotein, and this cleavage is a prerequisite for subsequent
processing at the remaining sites to release the mature structural
and catalytic proteins. Maturation takes place prior to the RT
reaction and is required to produce transposition-competent VLPs.
{ECO:0000269|PubMed:15956549, ECO:0000269|PubMed:7677953}.
-!- MISCELLANEOUS: Retrotransposons are mobile genetic entities that
are able to replicate via an RNA intermediate and a reverse
transcription step. In contrast to retroviruses, retrotransposons
are non-infectious, lack an envelope and remain intracellular. Ty3
retrotransposons belong to the gypsy-like elements (metaviridae).
-!- SEQUENCE CAUTION:
Sequence=AAA98435.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA97115.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA97117.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=DAA08202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; M34549; AAA98435.1; ALT_SEQ; Genomic_DNA.
EMBL; Z72894; CAA97115.1; ALT_SEQ; Genomic_DNA.
EMBL; Z72895; CAA97117.1; ALT_SEQ; Genomic_DNA.
EMBL; M18353; AAA66936.1; -; Genomic_DNA.
EMBL; BK006941; DAA08202.1; ALT_SEQ; Genomic_DNA.
PIR; S22875; S22875.
PIR; S69842; S69842.
RefSeq; NP_011624.1; NM_001184381.2.
PDB; 4OL8; X-ray; 3.10 A; A/B/E/F=536-1011.
PDBsum; 4OL8; -.
ProteinModelPortal; Q99315; -.
SMR; Q99315; -.
BioGrid; 33356; 1.
IntAct; Q99315; 11.
STRING; 4932.YGR109W-B; -.
MEROPS; A02.022; -.
iPTMnet; Q99315; -.
PRIDE; Q99315; -.
GeneID; 853006; -.
KEGG; sce:YGR109W-B; -.
EuPathDB; FungiDB:YGR109W-B; -.
SGD; S000007347; YGR109W-B.
HOGENOM; HOG000172599; -.
InParanoid; Q99315; -.
KO; K07497; -.
OrthoDB; EOG092C0KYC; -.
PMAP-CutDB; Q99315; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0000943; C:retrotransposon nucleocapsid; ISS:SGD.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISS:SGD.
GO; GO:0008233; F:peptidase activity; ISS:SGD.
GO; GO:0004540; F:ribonuclease activity; ISS:SGD.
GO; GO:0003723; F:RNA binding; ISS:SGD.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; ISS:SGD.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0032197; P:transposition, RNA-mediated; ISS:SGD.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 1.
Gene3D; 4.10.60.10; -; 1.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR024650; Peptidase_A2B.
InterPro; IPR021109; Peptidase_aspartic_dom.
InterPro; IPR012337; RNaseH-like_dom.
InterPro; IPR000477; RT_dom.
InterPro; IPR001878; Znf_CCHC.
Pfam; PF12384; Peptidase_A2B; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00078; RVT_1; 1.
SMART; SM00343; ZnF_C2HC; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Aspartyl protease; ATP-binding;
Complete proteome; Cytoplasm; DNA integration; DNA recombination;
DNA-binding; DNA-directed DNA polymerase; Endonuclease; Hydrolase;
Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Nucleus; Protease;
Reference proteome; Ribosomal frameshifting; RNA-binding;
RNA-directed DNA polymerase; Transferase; Transposable element;
Virion maturation; Virus exit from host cell; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:15956549}.
CHAIN 2 1547 Transposon Ty3-G Gag-Pol polyprotein.
/FTId=PRO_0000279356.
CHAIN 2 207 Capsid protein.
/FTId=PRO_0000279357.
PEPTIDE 208 233 Spacer peptide p3.
/FTId=PRO_0000279358.
CHAIN 234 309 Nucleocapsid protein p11.
/FTId=PRO_0000279359.
CHAIN 310 442 Ty3 protease.
/FTId=PRO_0000279360.
PEPTIDE 443 535 Spacer peptide J. {ECO:0000255}.
/FTId=PRO_0000279361.
CHAIN 536 1011 Reverse transcriptase/ribonuclease H.
/FTId=PRO_0000279362.
CHAIN 1012 1547 Integrase p61.
/FTId=PRO_0000279363.
CHAIN 1038 1547 Integrase p58.
/FTId=PRO_0000279364.
DOMAIN 620 797 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 893 1011 RNase H Ty3/gyspy-type.
DOMAIN 1159 1324 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 265 282 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 1106 1145 Integrase-type zinc finger-like.
ACT_SITE 336 336 For protease activity; shared with
dimeric partner. {ECO:0000250}.
METAL 686 686 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 748 748 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 749 749 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 893 893 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 936 936 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 961 961 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1175 1175 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1236 1236 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
SITE 207 208 Cleavage; by Ty3 protease.
SITE 233 234 Cleavage; by Ty3 protease.
SITE 309 310 Cleavage; by Ty3 protease.
SITE 442 443 Cleavage; by Ty3 protease. {ECO:0000255}.
SITE 535 536 Cleavage; by Ty3 protease.
SITE 1011 1012 Cleavage; by Ty3 protease.
SITE 1037 1038 Cleavage; by Ty3 protease; partial.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:15956549}.
MUTAGEN 267 267 C->S: Reduces level of VLP formation and
maturation. {ECO:0000269|PubMed:7515969}.
MUTAGEN 275 275 H->Q: Reduces level of VLP formation and
maturation. {ECO:0000269|PubMed:7515969}.
TURN 552 555 {ECO:0000244|PDB:4OL8}.
HELIX 558 563 {ECO:0000244|PDB:4OL8}.
TURN 565 567 {ECO:0000244|PDB:4OL8}.
HELIX 608 621 {ECO:0000244|PDB:4OL8}.
STRAND 636 640 {ECO:0000244|PDB:4OL8}.
STRAND 646 650 {ECO:0000244|PDB:4OL8}.
HELIX 653 656 {ECO:0000244|PDB:4OL8}.
HELIX 669 673 {ECO:0000244|PDB:4OL8}.
STRAND 681 687 {ECO:0000244|PDB:4OL8}.
HELIX 690 693 {ECO:0000244|PDB:4OL8}.
STRAND 694 696 {ECO:0000244|PDB:4OL8}.
HELIX 698 704 {ECO:0000244|PDB:4OL8}.
STRAND 712 717 {ECO:0000244|PDB:4OL8}.
HELIX 725 737 {ECO:0000244|PDB:4OL8}.
STRAND 743 746 {ECO:0000244|PDB:4OL8}.
STRAND 749 756 {ECO:0000244|PDB:4OL8}.
HELIX 757 773 {ECO:0000244|PDB:4OL8}.
HELIX 780 782 {ECO:0000244|PDB:4OL8}.
STRAND 795 797 {ECO:0000244|PDB:4OL8}.
STRAND 802 804 {ECO:0000244|PDB:4OL8}.
HELIX 806 809 {ECO:0000244|PDB:4OL8}.
TURN 810 814 {ECO:0000244|PDB:4OL8}.
HELIX 821 832 {ECO:0000244|PDB:4OL8}.
TURN 833 837 {ECO:0000244|PDB:4OL8}.
HELIX 841 844 {ECO:0000244|PDB:4OL8}.
HELIX 849 853 {ECO:0000244|PDB:4OL8}.
HELIX 863 871 {ECO:0000244|PDB:4OL8}.
TURN 876 878 {ECO:0000244|PDB:4OL8}.
STRAND 884 891 {ECO:0000244|PDB:4OL8}.
STRAND 899 906 {ECO:0000244|PDB:4OL8}.
STRAND 908 911 {ECO:0000244|PDB:4OL8}.
STRAND 913 921 {ECO:0000244|PDB:4OL8}.
HELIX 932 944 {ECO:0000244|PDB:4OL8}.
HELIX 948 951 {ECO:0000244|PDB:4OL8}.
STRAND 957 959 {ECO:0000244|PDB:4OL8}.
HELIX 965 969 {ECO:0000244|PDB:4OL8}.
STRAND 970 972 {ECO:0000244|PDB:4OL8}.
HELIX 976 986 {ECO:0000244|PDB:4OL8}.
STRAND 997 1000 {ECO:0000244|PDB:4OL8}.
HELIX 1001 1008 {ECO:0000244|PDB:4OL8}.
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


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