ID   YH11B_YEAST             Reviewed;        1793 AA.
AC   O13535; D3DLG6;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Transposon Ty1-H 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-H; Synonyms=YHRCTy1-1 POL; OrderedLocusNames=YHR214C-B;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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-H Gag-Pol polyprotein;
CC         IsoId=O13535-1; Sequence=Displayed;
CC       Name=Transposon Ty1-H Gag polyprotein;
CC         IsoId=P0C2I4-1; 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-H Gag-Pol polyprotein]: Produced
CC       by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the
CC       YHR214C-C ORF.
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DR   EMBL; U00029; AAB69744.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06910.1; -; Genomic_DNA.
DR   PIR; S40969; S40969.
DR   PIR; S52601; S52601.
DR   RefSeq; NP_012086.1; NM_001181431.2. [O13535-1]
DR   AlphaFoldDB; O13535; -.
DR   BioGRID; 36648; 9.
DR   IntAct; O13535; 3.
DR   MINT; O13535; -.
DR   iPTMnet; O13535; -.
DR   PaxDb; 4932-YHR214C-B; -.
DR   PeptideAtlas; O13535; -.
DR   GeneID; 856623; -.
DR   KEGG; sce:YHR214C-B; -.
DR   AGR; SGD:S000003534; -.
DR   SGD; S000003534; YHR214C-B.
DR   VEuPathDB; FungiDB:YHR214C-B; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_244151_0_0_1; -.
DR   InParanoid; O13535; -.
DR   OrthoDB; 2039326at2759; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; O13535; 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; 2.
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; 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..1793
FT                   /note="Transposon Ty1-H Gag-Pol polyprotein"
FT                   /id="PRO_0000279074"
FT   CHAIN           1..439
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279075"
FT   CHAIN           440..620
FT                   /note="Ty1 protease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279076"
FT   CHAIN           621..1255
FT                   /note="Integrase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279077"
FT   CHAIN           1256..1793
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279078"
FT   DOMAIN          698..873
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   DOMAIN          1376..1514
FT                   /note="Reverse transcriptase Ty1/copia-type"
FT   DOMAIN          1648..1790
FT                   /note="RNase H Ty1/copia-type"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..439
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          390..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..678
FT                   /note="Integrase-type zinc finger-like"
FT   REGION          996..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1216..1250
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        131..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1053
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1078..1094
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1095..1118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1132..1149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1187..1208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        499
FT                   /note="For protease activity; shared with dimeric partner"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   BINDING         709
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         774
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         1384
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         1465
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         1466
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         1648
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         1690
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         1723
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            439..440
FT                   /note="Cleavage; by Ty1 protease"
FT                   /evidence="ECO:0000250"
FT   SITE            620..621
FT                   /note="Cleavage; by Ty1 protease"
FT                   /evidence="ECO:0000250"
FT   SITE            1255..1256
FT                   /note="Cleavage; by Ty1 protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1793 AA;  202817 MW;  1DA6A07E10E0A2CB CRC64;
     MESQQLSNYP HISHGSACAS VTSKEVHTNQ DPLDVSASKI QEYDKASTKA NSQQTTTPAS
     SAVPENLHHA SPQPASVPPP QNGPYPQQCM MTQNQANPSG WSFYGHPSMI PYTPYQMSPM
     YFPPGPQSQF PQYPSSVGTP LSTPSPESGN TFTDSSSADS DMTSTKKYVR PPPMLTSPND
     FPNWVKTYIK FLQNSNLGGI IPTVNGKPVP PMLTSPNDFP NWVKTYIKFL QNSNLGGIIP
     TVNGKPVRQI TDDELTFLYN TFQIFAPSQF LPTWVKDILS VDYTDIMKIL SKSIEKMQSD
     TQEANDIVTL ANLQYNGSTP ADAFETKVTN IIDRLNNNGI HINNKVACQL IMRGLSGEYK
     FLRYTRHRHL NMTVAELFLD IHAIYEEQQG SRNSKPNYRR NPSDEKNDSR SYTNTTKPKV
     IARNPQKTNN SKSKTARAHN VSTSNNSPST DNDSISKSTT EPIQLNNKHD LHLGQKLTES
     TVNHTNHSDD ELPGHLLLDS GASRTLIRSA HHIHSASSNP DINVVDAQKR NIPINAIGDL
     QFHFQDNTKT SIKVLHTPNI AYDLLSLNEL AAVDITACFT KNVLERSDGT VLAPIVKYGD
     FYWVSKKYLL PSNISVPTIN NVHTSESTRK YPYPFIHRML AHANAQTIRY SLKNNTITYF
     NESDVDWSSA IDYQCPDCLI GKSTKHRHIK GSRLKYQNSY EPFQYLHTDI FGPVHNLPKS
     APSYFISFTD ETTKFRWVYP LHDRREDSIL DVFTTILAFI KNQFQASVLV IQMDRGSEYT
     NRTLHKFLEK NGITPCYTTT ADSRAHGVAE RLNRTLLDDC RTQLQCSGLP NHLWFSAIEF
     STIVRNSLAS PKSKKSARQH AGLAGLDIST LLPFGQPVIV NDHNPNSKIH PRGIPGYALH
     PSRNSYGYII YLPSLKKTVD TTNYVILQGK ESRLDQFNYD ALTFDEDLNR LTASYHSFIA
     SNEIQQSNDL NIESDHDFQS DIELHPEQLR NVLSKAVSPT DSTPPSTHTE DSKRVSKTNI
     RAPREVDPNI SESNILPSKK RSSTPQISDI ESTGSGGMHR LDVPLLAPMS QSNTHESSHA
     SKSKDFRHSD SYSDNETNHT NVPISSTGGT NNKTVPQTSE QETEKRIIHR SPSIDTSSSE
     SNSLHHVVPI KTSDTCPKEN TEESIIADLP LPDLPPEPPT ELSDSFKELP PINSHQTNSS
     LGGIGDSNAY TTINSKKRSL EDNETEIKVS RDTWNTKNMR SLEPPRSKKR IHLIAAVKAV
     KSIKPIRTTL RYDEAITYNK DIKEKEKYIQ AYHKEVNQLL MMKTWDTDRY YDRKEIDPKR
     VINSMFIFNR KRDGTHKARF VARGDIQHPD TYDPGMQSNT VHHYALMTSL SLALDNNYYI
     TQLDISSAYL YADIKEELYI RPPPHLGMND KLIRLKKSLY GLKQSGANWY ETIKSYLIKQ
     CGMEEVRGWS CVFKNSQVTI CLFVDDMILF SKDLNANKKI ITTLKKQYDT KIINLGESDN
     EIQYDILGLE IKYQRGKYMK LGMENSLTEK IPKLNVPLNP KGRKLSAPGQ PGLYIDQDEL
     EIDEDEYKEK VHEMQKLIGL ASYVGYKFRF DLLYYINTLA QHILFPSRQV LDMTYELIQF
     MWDTRDKQLI WHKNKPTEPD NKLVAISDAS YGNQPYYKSQ IGNIYLLNGK VIGGKSTKAS
     LTCTSTTEAE IHAISESVPL LNNLSHLVQE LNKKPITKGL LTDSKSTISI IISNNEEKFR
     NRFFGTKAMR LRDEVSGNHL HVCYIETKKN IADVMTKPLP IKTFKLLTNK WIH
//