YP13B_YEAST
ID YP13B_YEAST Reviewed; 1756 AA.
AC P0C2J0; D6W4F5;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Transposon Ty1-PR2 Gag-Pol polyprotein;
DE AltName: Full=Gag-Pol-p199;
DE AltName: Full=TY1A-TY1B;
DE AltName: Full=Transposon Ty1 TYA-TYB polyprotein;
DE AltName: Full=p190;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CA;
DE AltName: Full=Gag-p45;
DE AltName: Full=p54;
DE Contains:
DE RecName: Full=Ty1 protease;
DE Short=PR;
DE EC=3.4.23.-;
DE AltName: Full=Pol-p20;
DE AltName: Full=p23;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE AltName: Full=Pol-p71;
DE AltName: Full=p84;
DE AltName: Full=p90;
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=Pol-p63;
DE AltName: Full=p60;
GN Name=TY1B-PR2; Synonyms=YPRWTy1-3 POL; OrderedLocusNames=YPR158W-B;
GN ORFNames=P9584.3c;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP REVIEW, AND DOMAINS.
RX PubMed=16093680; DOI=10.1159/000084960;
RA Wilhelm F.-X., Wilhelm M., Gabriel A.;
RT "Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1
RT element.";
RL Cytogenet. Genome Res. 110:269-287(2005).
CC -!- FUNCTION: Capsid protein (CA) is the structural component of the virus-
CC like particle (VLP), forming the shell that encapsulates the
CC retrotransposons dimeric RNA genome. The particles are assembled from
CC trimer-clustered units and there are holes in the capsid shells that
CC allow for the diffusion of macromolecules. CA has also nucleocapsid-
CC like chaperone activity, promoting primer tRNA(i)-Met annealing to the
CC multipartite primer-binding site (PBS), dimerization of Ty1 RNA and
CC initiation of reverse transcription (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages
CC of the Gag and Gag-Pol polyproteins after assembly of the VLP.
CC {ECO:0000250}.
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 ends
CC (By similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
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;
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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- SUBUNIT: The capsid protein forms a homotrimer, from which the VLPs are
CC assembled. The protease is a homodimer, whose active site consists of
CC two apposed aspartic acid residues (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=The Gag-Pol polyprotein is generated by a +1 ribosomal
CC frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By
CC similarity). {ECO:0000250};
CC Name=Transposon Ty1-PR2 Gag-Pol polyprotein;
CC IsoId=P0C2J0-1; Sequence=Displayed;
CC Name=Transposon Ty1-PR2 Gag polyprotein;
CC IsoId=P0CX60-1; Sequence=External;
CC -!- DOMAIN: The C-terminal RNA-binding region of CA is sufficient for all
CC its nucleocapsid-like chaperone activities. {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
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 yielding
CC capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a
CC prerequisite for subsequent processing of Pol-p154 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 (By similarity). {ECO:0000250}.
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. Ty1 retrotransposons belong
CC to the copia elements (pseudoviridae).
CC -!- MISCELLANEOUS: [Isoform Transposon Ty1-PR2 Gag-Pol polyprotein]:
CC Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-
CC 436 of the YPR158W-A ORF.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U28371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006949; DAA11571.1; -; Genomic_DNA.
DR PIR; S69983; S69983.
DR RefSeq; NP_058193.1; NM_001184398.2. [P0C2J0-1]
DR AlphaFoldDB; P0C2J0; -.
DR BioGRID; 36327; 6.
DR IntAct; P0C2J0; 2.
DR MINT; P0C2J0; -.
DR STRING; 4932.YPR158W-B; -.
DR iPTMnet; P0C2J0; -.
DR PaxDb; P0C2J0; -.
DR GeneID; 856283; -.
DR KEGG; sce:YPR158W-B; -.
DR SGD; S000007364; YPR158W-B.
DR VEuPathDB; FungiDB:YPR158W-B; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_244151_0_0_1; -.
DR InParanoid; P0C2J0; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P0C2J0; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; 3.30.420.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR013103; RVT_2.
DR InterPro; IPR015820; TYA.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF07727; RVT_2; 1.
DR Pfam; PF01021; TYA; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; ATP-binding; Cytoplasm; DNA integration;
KW DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Protease;
KW Reference proteome; Ribosomal frameshifting; RNA-binding;
KW RNA-directed DNA polymerase; Transferase; Transposable element;
KW Transposition; Viral release from host cell; Virion maturation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1756
FT /note="Transposon Ty1-PR2 Gag-Pol polyprotein"
FT /id="PRO_0000279179"
FT CHAIN 1..401
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279180"
FT CHAIN 402..582
FT /note="Ty1 protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279181"
FT CHAIN 583..1218
FT /note="Integrase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279182"
FT CHAIN 1219..1756
FT /note="Reverse transcriptase/ribonuclease H"
FT /evidence="ECO:0000250"
FT /id="PRO_0000279183"
FT DOMAIN 660..836
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT DOMAIN 1339..1477
FT /note="Reverse transcriptase Ty1/copia-type"
FT DOMAIN 1611..1753
FT /note="RNase H Ty1/copia-type"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..401
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 352..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..640
FT /note="Integrase-type zinc finger-like"
FT REGION 957..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1179..1213
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 461
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 671
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 736
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1653
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1686
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT SITE 401..402
FT /note="Cleavage; by Ty1 protease"
FT /evidence="ECO:0000250"
FT SITE 582..583
FT /note="Cleavage; by Ty1 protease"
FT /evidence="ECO:0000250"
FT SITE 1218..1219
FT /note="Cleavage; by Ty1 protease"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1756 AA; 198639 MW; ECBC18448B722BF6 CRC64;
MESQQLSNYP HISHGSACAS VTSKEVHTNQ DPLDVSASKI QEYDKASTKA NSQQTTTPAS
SAVPENPHHA SPQPASVPPP QNGPYPQQCM MTQNQANPSG WSFYGHPSMI PYTPYQMSPM
YFPPGPQSQF PQYPSSVGTP LSTPSPESGN TFTDSSSADS DMTSTKKYVR PPPMLTSPND
FPNWVKTYIK FLQNSNLGGI IPTVNGKPVR PITDDELTFL YNTFQIFAPS QFLPTWVKDI
LSVDYTDIMK ILSKSIEKMQ SDTQEANDIV TLANLQYNGS TPADAFETKV TNIIDRLNNN
GIHINNKVAC QLIMRGLSGE YKFLRYTRHR HLNMTVAELF LDIHAIYEEQ QGSRNSKPNY
RRNPSDEKND SRSYTNTTKP KVIARNPQKT NNSKSKTARA HNVSTSNNSP STDNDSISKS
TTEPIQLNNK HDLHLGQKLT ESTVNHTNHS DDELPGHLLL DSGASRTLIR SAHHIHSASS
NPDINVVDAQ KRNIPINAIG DLQFHFQDNT KTSIKVLHTP NIAYDLLSLN ELAAVDITAC
FTKNVLERSD GTVLAPIVKY GDFYWVSKKY LLPSNISVPT INNVHTSEST RKYPYPFIHR
MLAHANAQTI RYSLKNNTIT YFNESDVDWS SAIDYQCPDC LIGKSTKHRH IKGSRLKYQN
SYEPFQYLHT DIFGPVHNLP KSAPSYFISF TDETTKFRWV YPLHDRREDS ILDVFTTILA
FIKNQFQASV LVIQMDRGSE YTNRTLHKFL EKKNGITPCY TTTADSRAHG VAERLNRTLL
DDCRTQLQCS GLPNHLWFSA IEFSTIVRNS LASPKSKKSA RQHAGLAGLD ISTLLPFGQP
VIVNDHNPNS KIHPRGIPGY ALHPSRNSYG YIIYLPSLKK TVDTTNYVIL QGKESRLDQF
NYDALTFDED LNRLTASYHS FIASNEIQES NDLNIESDHD FQSDIELHPE QPRNVLSKAV
SPTDSTPPST HTEDSKRVSK TNIRAPREVD PNISESNILP SKKRSSTPQI SNIESTGSGG
MHKLNVPLLA PMSQSNTHES SHASKSKDFR HSDSYSENET NHTNVPISST GGTNNKTVPQ
ISDQETEKRI IHRSPSIDAS PPENNSSHNI VPIKTPTTVS EQNTEESIIA DLPLPDLPPE
SPTEFPDPFK ELPPINSHQT NSSLGGIGDS NAYTTINSKK RSLEDNETEI KVSRDTWNTK
NMRSLEPPRS KKRIHLIAAV KAVKSIKPIR TTLRYDEAIT YNKDIKEKEK YIEAYHKEVN
QLLKMNTWDT DKYYDRKEID PKRVINSMFI FNRKRDGTHK ARFVARGDIQ HPDTYDSGMQ
SNTVHHYALM TSLSLALDNN YYITQLDISS AYLYADIKEE LYIRPPPHLG MNDKLIRLKK
SLYGLKQSGA NWYETIKSYL IKQCGMEEVR GWSCVFKNSQ VTICLFVDDM ILFSKDLNAN
KKIITTLKKQ YDTKIINLGE SDNEIQYDIL GLEIKYQRGK YMKLGMENSL TEKIPKLNVP
LNPKGRKLSA PGQPGLYIDQ DELEIDEDEY KEKVHEMQKL IGLASYVGYK FRFDLLYYIN
TLAQHILFPS RQVLDMTYEL IQFMWDTRDK QLIWHKNKPT EPDNKLVAIS DASYGNQPYY
KSQIGNIYLL NGKVIGGKST KASLTCTSTT EAEIHAISES VPLLNNLSHL VQELNKKPIT
KGLLTDSKST ISIIISNNEE KFRNRFFGTK AMRLRDEVSG NHLHVCYIET KKNIADVMTK
PLPIKTFKLL TNKWIH
