ID   YP12B_YEAST             Reviewed;        1755 AA.
AC   P0C2I9; D6W4D4;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Transposon Ty1-PR1 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-PR1; Synonyms=YPRCTy1-2 POL; OrderedLocusNames=YPR137C-B;
GN   ORFNames=P9659.6c;
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-PR1 Gag-Pol polyprotein;
CC         IsoId=P0C2I9-1; Sequence=Displayed;
CC       Name=Transposon Ty1-PR1 Gag polyprotein;
CC         IsoId=P0CX58-1; 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-PR1 Gag-Pol polyprotein]:
CC       Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-
CC       436 of the YPR137C-A ORF.
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DR   EMBL; U40829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006949; DAA11550.1; -; Genomic_DNA.
DR   PIR; S69980; S69980.
DR   RefSeq; NP_058191.1; NM_001184394.2. [P0C2I9-1]
DR   AlphaFoldDB; P0C2I9; -.
DR   SMR; P0C2I9; -.
DR   BioGRID; 36304; 11.
DR   IntAct; P0C2I9; 1.
DR   iPTMnet; P0C2I9; -.
DR   PaxDb; 4932-YPR137C-B; -.
DR   PeptideAtlas; P0C2I9; -.
DR   GeneID; 856257; -.
DR   KEGG; sce:YPR137C-B; -.
DR   AGR; SGD:S000007360; -.
DR   SGD; S000007360; YPR137C-B.
DR   VEuPathDB; FungiDB:YPR137C-B; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_244151_0_0_1; -.
DR   InParanoid; P0C2I9; -.
DR   OrthoDB; 2039326at2759; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P0C2I9; 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:0003723; F:RNA binding; ISS:SGD.
DR   GO; GO:0004540; F:RNA nuclease activity; 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:retrotransposition; ISS:SGD.
DR   CDD; cd09272; RNase_HI_RT_Ty1; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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   PANTHER; PTHR42648; TRANSPOSASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR42648:SF11; TRANSPOSON TY4-P GAG-POL POLYPROTEIN; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF07727; RVT_2; 1.
DR   Pfam; PF01021; TYA; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 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; Phosphoprotein;
KW   Protease; 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..1755
FT                   /note="Transposon Ty1-PR1 Gag-Pol polyprotein"
FT                   /id="PRO_0000279174"
FT   CHAIN           1..401
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279175"
FT   CHAIN           402..582
FT                   /note="Ty1 protease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279176"
FT   CHAIN           583..1217
FT                   /note="Integrase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279177"
FT   CHAIN           1218..1755
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279178"
FT   DOMAIN          660..835
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   DOMAIN          1338..1476
FT                   /note="Reverse transcriptase Ty1/copia-type"
FT   DOMAIN          1610..1752
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          956..1087
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1092..1111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1130..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1178..1212
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..93
FT                   /note="Polar 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        969..983
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1018
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1056
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1080
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1148
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1178
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         1346
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         1427
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         1610
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         1652
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         1685
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            1217..1218
FT                   /note="Cleavage; by Ty1 protease"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99231"
SQ   SEQUENCE   1755 AA;  198568 MW;  40AB2AF6024026F6 CRC64;
     MESQQLSQHS PISHGSACAS VTSKEVHTNQ DPLDVSASKT EECEKASTKA NSQQTTTPAS
     SAVPENPHHA SPQTAQSHSP QNGPYPQQCM MTQNQANPSG WSFYGHPSMI PYTPYQMSPM
     YFPPGPQSQF PQYPSSVGTP LSTPSPESGN TFTDSSSADS DMTSTKKYVR PPPMLTSPND
     FPNWVKTYIK FLQNSNLGGI IPTVNGKPVR QITDDELTFL 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 EKNGITPCYT TTADSRAHGV AERLNRTLLD
     DCRTQLQCSG LPNHLWFSAI EFSTIVRNSL ASPKSKKSAR QHAGLAGLDI STLLPFGQPV
     IVNDHNPNSK IHPRGIPGYA LHPSRNSYGY IIYLPSLKKT VDTTNYVILQ GKESRLDQFN
     YDALTFDEDL NRLTASYHSF IASNEIQESN DLNIESDHDF QSDIELHPEQ PRNVLSKAVS
     PTDSTPPSTH TEDSKRVSKT NIRAPREVDP NISESNILPS KKRSSTPQIS NIESTGSGGM
     HKLNVPLLAP MSQSNTHESS HASKSKDFRH SDSYSENETN HTNVPISSTG GTNNKTVPQI
     SDQETEKRII HRSPSIDASP PENNSSHNIV PIKTPTTVSE QNTEESIIAD LPLPDLPPES
     PTEFPDPFKE LPPINSHQTN SSLGGIGDSN AYTTINSKKR SLEDNETEIK VSRDTWNTKN
     MRSLEPPRSK KRIHLIAAVK AVKSIKPIRT TLRYDEAITY NKDIKEKEKY IEAYHKEVNQ
     LLKMNTWDTD KYYDRKEIDP KRVINSMFIF NKKRDGTHKA RFVARGDIQH PDTYDTGMQS
     NTVHHYALMT SLSLALDNNY YITQLDISSA YLYADIKEEL YIRPPPHLGM NDKLIRLKKS
     HYGLKQSGAN WYETIKSYLI KQCGMEEVRG WSCVFKNSQV TICLFVDDMI LFSKDLNANK
     KIITTLKKQY DTKIINLGES DNEIQYDILG LEIKYQRGKY MKLGMENSLT EKIPKLNVPL
     NPKGRKLSAP GQPGLYIDQD ELEIDEDEYK EKVHEMQKLI GLASYVGYKF RFDLLYYINT
     LAQHILFPSR QVLDMTYELI QFMWDTRDKQ LIWHKNKPTE PDNKLVAISD ASYGNQPYYK
     SQIGNIFLLN GKVIGGKSTK ASLTCTSTTE AEIHAVSEAI PLLNNLSHLV QELNKKPIIK
     GLLTDSRSTI SIIKSTNEEK FRNRFFGTKA MRLRDEVSGN NLYVYYIETK KNIADVMTKP
     LPIKTFKLLT NKWIH
//