TY1AB_YEASX
ID TY1AB_YEASX Reviewed; 1755 AA.
AC Q07163; Q07169;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Transposon TyH3 Gag-Pol polyprotein;
DE AltName: Full=Gag-Pol-p199;
DE AltName: Full=TY1A-TY1B;
DE AltName: Full=Transposon Ty1-H3 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; Synonyms=POL, TYB1;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LEU-602.
RC STRAIN=JB84A;
RX PubMed=2837641; DOI=10.1128/mcb.8.4.1432-1442.1988;
RA Boeke J.D., Eichinger D., Castrillon D., Fink G.R.;
RT "The Saccharomyces cerevisiae genome contains functional and nonfunctional
RT copies of transposon Ty1.";
RL Mol. Cell. Biol. 8:1432-1442(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-480, AND VARIANTS TY1-15 ILE-12;
RP 74-THR--SER-79 AND ARG-142.
RX PubMed=2982101; DOI=10.1038/313243a0;
RA Mellor J., Fulton S.M., Dobson M.J., Wilson W., Kingsman S.M.,
RA Kingsman A.J.;
RT "A retrovirus-like strategy for expression of a fusion protein encoded by
RT yeast transposon Ty1.";
RL Nature 313:243-246(1985).
RN [3]
RP PROTEIN SEQUENCE OF 402-408, CLEAVAGE SITE HIS-401-402-ASN, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11435555; DOI=10.1128/jvi.75.15.6769-6775.2001;
RA Lawler J.F. Jr., Merkulov G.V., Boeke J.D.;
RT "Frameshift signal transplantation and the unambiguous analysis of
RT mutations in the yeast retrotransposon Ty1 Gag-Pol overlap region.";
RL J. Virol. 75:6769-6775(2001).
RN [4]
RP RIBOSOMAL FRAMESHIFT SITE.
RX PubMed=2164889; DOI=10.1016/0092-8674(90)90371-k;
RA Belcourt M.F., Farabaugh P.J.;
RT "Ribosomal frameshifting in the yeast retrotransposon Ty: tRNAs induce
RT slippage on a 7 nucleotide minimal site.";
RL Cell 62:339-352(1990).
RN [5]
RP PROTEOLYTIC PROCESSING.
RX PubMed=1714514; DOI=10.1128/jvi.65.9.4573-4581.1991;
RA Garfinkel D.J., Hedge A.M., Youngren S.D., Copeland T.D.;
RT "Proteolytic processing of pol-TYB proteins from the yeast retrotransposon
RT Ty1.";
RL J. Virol. 65:4573-4581(1991).
RN [6]
RP CLEAVAGE SITES ASN-582-583-ASN AND ALA-1217-1218-ALA.
RX PubMed=8127892; DOI=10.1073/pnas.91.5.1843;
RA Moore S.P., Garfinkel D.J.;
RT "Expression and partial purification of enzymatically active recombinant
RT Ty1 integrase in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1843-1847(1994).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-1178; LYS-1179;
RP ARG-1180; 1183-GLU--GLU-1188; LYS-1210; LYS-1211 AND ARG-1212.
RX PubMed=9448008; DOI=10.1128/mcb.18.2.1105;
RA Moore S.P., Rinckel L.A., Garfinkel D.J.;
RT "A Ty1 integrase nuclear localization signal required for
RT retrotransposition.";
RL Mol. Cell. Biol. 18:1105-1114(1998).
RN [8]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10766747; DOI=10.1074/jbc.m001371200;
RA Cristofari G., Ficheux D., Darlix J.-L.;
RT "The Gag-like protein of the yeast Ty1 retrotransposon contains a nucleic
RT acid chaperone domain analogous to retroviral nucleocapsid proteins.";
RL J. Biol. Chem. 275:19210-19217(2000).
RN [9]
RP FUNCTION.
RX PubMed=11595735; DOI=10.1074/jbc.m106067200;
RA Wilhelm M., Uzun O., Mules E.H., Gabriel A., Wilhelm F.-X.;
RT "Polypurine tract formation by Ty1 RNase H.";
RL J. Biol. Chem. 276:47695-47701(2001).
RN [10]
RP PROTEOLYTIC PROCESSING.
RX PubMed=11134277; DOI=10.1128/jvi.75.2.638-644.2001;
RA Merkulov G.V., Lawler J.F. Jr., Eby Y., Boeke J.D.;
RT "Ty1 proteolytic cleavage sites are required for transposition: all sites
RT are not created equal.";
RL J. Virol. 75:638-644(2001).
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.
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;
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 {ECO:0000269|PubMed:9448008}. Nucleus
CC {ECO:0000269|PubMed:9448008}.
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.
CC {ECO:0000269|PubMed:2164889};
CC Name=Transposon TyH3 Gag-Pol polyprotein;
CC IsoId=Q07163-1; Sequence=Displayed;
CC Name=Transposon TyH3 Gag polyprotein;
CC IsoId=P08405-1; Sequence=External;
CC -!- DOMAIN: The C-terminal RNA-binding region of CA is sufficient for all
CC its nucleocapsid-like chaperone activities.
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 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. {ECO:0000269|PubMed:11134277,
CC ECO:0000269|PubMed:11435555, ECO:0000269|PubMed:1714514,
CC ECO:0000269|PubMed:8127892}.
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 TyH3 Gag-Pol polyprotein]: Produced
CC by +1 ribosomal frameshifting between codon Leu-435 and Gly-436.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA66938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA25874.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; M18706; AAA66938.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X01736; CAA25874.1; ALT_SEQ; Genomic_DNA.
DR PIR; B22671; B22671.
DR PIR; B28097; B28097.
DR AlphaFoldDB; Q07163; -.
DR PRIDE; Q07163; -.
DR VEuPathDB; FungiDB:YPR137C-B; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
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:0032196; P:transposition; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Aspartyl protease; ATP-binding; Cytoplasm; Direct protein sequencing;
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; Phosphoprotein; Protease;
KW Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Transposable element; Transposition;
KW Viral release from host cell; Virion maturation; Zinc; Zinc-finger.
FT CHAIN 1..1755
FT /note="Transposon TyH3 Gag-Pol polyprotein"
FT /id="PRO_0000278970"
FT CHAIN 1..401
FT /note="Capsid protein"
FT /id="PRO_0000278971"
FT CHAIN 402..582
FT /note="Ty1 protease"
FT /id="PRO_0000278972"
FT CHAIN 583..1217
FT /note="Integrase"
FT /id="PRO_0000278973"
FT CHAIN 1218..1755
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000278974"
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 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 COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..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 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 SITE 582..583
FT /note="Cleavage; by Ty1 protease"
FT SITE 1217..1218
FT /note="Cleavage; by Ty1 protease"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99231"
FT VARIANT 12
FT /note="N -> I (in Ty1-15)"
FT /evidence="ECO:0000269|PubMed:2982101"
FT VARIANT 74..79
FT /note="PASVPP -> TAQSHS (in Ty1-15)"
FT VARIANT 142
FT /note="S -> R (in Ty1-15)"
FT /evidence="ECO:0000269|PubMed:2982101"
FT MUTAGEN 602
FT /note="L->I: In Ty173; reduces transposition frequency 60-
FT fold."
FT /evidence="ECO:0000269|PubMed:2837641"
FT MUTAGEN 1178
FT /note="K->G: Partially prevents nuclear localization of
FT integrase and reduces transposition efficiency by 30%.
FT Prevents nuclear localization of integrase and reduces
FT transposition efficiency by 99.6%; when associated with
FT Gly-1179. Prevents nuclear localization of integrase; when
FT associated with Gly-1179 and Thr-1180."
FT /evidence="ECO:0000269|PubMed:9448008"
FT MUTAGEN 1179
FT /note="K->G: Prevents nuclear localization of integrase and
FT reduces transposition efficiency by 99.6%; when associated
FT with Gly-1178. Prevents nuclear localization of integrase;
FT when associated with Gly-1178 and Thr-1180."
FT /evidence="ECO:0000269|PubMed:9448008"
FT MUTAGEN 1180
FT /note="R->T: Prevents nuclear localization of integrase;
FT when associated with Gly-1178 and Gly-1179."
FT /evidence="ECO:0000269|PubMed:9448008"
FT MUTAGEN 1183..1188
FT /note="EDNETE->QNNQTQ: Prevents nuclear localization of
FT integrase."
FT /evidence="ECO:0000269|PubMed:9448008"
FT MUTAGEN 1210
FT /note="K->G: Reduces transposition efficiency by 77%.
FT Reduces transposition efficiency by 98.4%; when associated
FT with Gly-1211. Reduces transposition efficiency by 99.8%;
FT when associated with Gly-1211 and Thr-1212."
FT /evidence="ECO:0000269|PubMed:9448008"
FT MUTAGEN 1211
FT /note="K->G: Reduces transposition efficiency by 98.4%;
FT when associated with Gly-1210. Reduces transposition
FT efficiency by 99.8%; when associated with Gly-1210 and Thr-
FT 1212."
FT /evidence="ECO:0000269|PubMed:9448008"
FT MUTAGEN 1212
FT /note="R->T: Reduces transposition efficiency by 99.8%;
FT when associated with Gly-1210 and Gly-1211."
FT /evidence="ECO:0000269|PubMed:9448008"
SQ SEQUENCE 1755 AA; 198662 MW; 595E431E836B5EA5 CRC64;
MESQQLSQHS PNSHGSACAS VTSKEVHTNQ DPLDVSASKT EECEKASTKA NSQQTTTPAS
SAVPENPHHA SPQPASVPPP 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 NSAPSYFISF 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 LPPINSRQTN SSLGGIGDSN AYTTINSKKR SLEDNETEIK VSRDTWNTKN
MRSLEPPRSK KRIHLIAAVK AVKSIKPIRT TLRYDEAITY NKDIKEKEKY IEAYHKEVNQ
LLKMKTWDTD EYYDRKEIDP KRVINSMFIF NKKRDGTHKA RFVARGDIQH PDTYDSGMQS
NTVHHYALMT SLSLALDNNY YITQLDISSA YLYADIKEEL YIRPPPHLGM NDKLIRLKKS
LYGLKQSGAN WYETIKSYLI QQCGMEEVRG WSCVFKNSQV TICLFVDDMV LFSKNLNSNK
RIIEKLKMQY DTKIINLGES DEEIQYDILG LEIKYQRGKY MKLGMENSLT EKIPKLNVPL
NPKGRKLSAP GQPGLYIDQD ELEIDEDEYK EKVHEMQKLI GLASYVGYKF RFDLLYYINT
LAQHILFPSR QVLDMTYELI QFMWDTRDKQ LIWHKNKPTE PDNKLVAISD ASYGNQPYYK
SQIGNIYLLN GKVIGGKSTK ASLTCTSTTE AEIHAISESV PLLNNLSYLI QELNKKPIIK
GLLTDSRSTI SIIKSTNEEK FRNRFFGTKA MRLRDEVSGN NLYVYYIETK KNIADVMTKP
LPIKTFKLLT NKWIH
