ID   POLR_TYMV               Reviewed;        1844 AA.
AC   P10358;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   13-SEP-2023, entry version 121.
DE   RecName: Full=RNA replicase polyprotein;
DE   AltName: Full=206 kDa polyprotein;
DE   AltName: Full=206K;
DE   Contains:
DE     RecName: Full=Methyltransferase/Protease/Ubiquitinyl hydrolase;
DE              EC=2.1.1.-;
DE              EC=3.4.19.12 {ECO:0000269|PubMed:22117220, ECO:0000269|PubMed:23345508, ECO:0000269|PubMed:23966860};
DE              EC=3.4.22.-;
DE     AltName: Full=98 kDa protein;
DE     AltName: Full=MET/PRO;
DE   Contains:
DE     RecName: Full=Putative helicase;
DE              EC=3.6.4.-;
DE     AltName: Full=42 kDa protein;
DE     AltName: Full=HEL;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE     AltName: Full=66 kDa protein;
DE     AltName: Full=POL;
OS   Turnip yellow mosaic virus.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Tymoviridae; Tymovirus; Tymovirus brassicae.
OX   NCBI_TaxID=12154;
OH   NCBI_TaxID=3705; Brassica.
OH   NCBI_TaxID=51351; Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis).
OH   NCBI_TaxID=82359; Cardamine lilacina.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3399388; DOI=10.1093/nar/16.13.6157;
RA   Morch M.D., Boyer J.C., Haenni A.L.;
RT   "Overlapping open reading frames revealed by complete nucleotide sequencing
RT   of turnip yellow mosaic virus genomic RNA.";
RL   Nucleic Acids Res. 16:6157-6173(1988).
RN   [2]
RP   SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=11222099; DOI=10.1006/viro.2000.0769;
RA   Prod'homme D., Le Panse S., Drugeon G., Jupin I.;
RT   "Detection and subcellular localization of the turnip yellow mosaic virus
RT   66K replication protein in infected cells.";
RL   Virology 281:88-101(2001).
RN   [3]
RP   PROTEOLYTIC CLEAVAGE (RNA REPLICASE POLYPROTEIN), AND SUBCELLULAR LOCATION.
RX   PubMed=17686855; DOI=10.1128/jvi.01428-07;
RA   Jakubiec A., Drugeon G., Camborde L., Jupin I.;
RT   "Proteolytic processing of turnip yellow mosaic virus replication proteins
RT   and functional impact on infectivity.";
RL   J. Virol. 81:11402-11412(2007).
RN   [4]
RP   FUNCTION (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE), AND CATALYTIC
RP   ACTIVITY (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE).
RX   PubMed=22117220; DOI=10.1038/emboj.2011.424;
RA   Chenon M., Camborde L., Cheminant S., Jupin I.;
RT   "A viral deubiquitylating enzyme targets viral RNA-dependent RNA polymerase
RT   and affects viral infectivity.";
RL   EMBO J. 31:741-753(2012).
RN   [5]
RP   CATALYTIC ACTIVITY (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE),
RP   FUNCTION (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE),
RP   BIOPHYSICOCHEMICAL PROPERTIES (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL
RP   HYDROLASE), AND MUTAGENESIS OF GLU-10; SER-101 AND THR-128.
RX   PubMed=23345508; DOI=10.1128/jvi.03252-12;
RA   Capodagli G.C., Deaton M.K., Baker E.A., Lumpkin R.J., Pegan S.D.;
RT   "Diversity of ubiquitin and ISG15 specificity among nairoviruses' viral
RT   ovarian tumor domain proteases.";
RL   J. Virol. 87:3815-3827(2013).
RN   [6] {ECO:0007744|PDB:4A5U}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 728-879, FUNCTION
RP   (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE), ACTIVE SITE
RP   (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE), AND CATALYTIC ACTIVITY
RP   (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE).
RX   PubMed=23966860; DOI=10.1371/journal.ppat.1003560;
RA   Lombardi C., Ayach M., Beaurepaire L., Chenon M., Andreani J., Guerois R.,
RA   Jupin I., Bressanelli S.;
RT   "A compact viral processing proteinase/ubiquitin hydrolase from the OTU
RT   family.";
RL   PLoS Pathog. 9:e1003560-e1003560(2013).
RN   [7] {ECO:0007744|PDB:5LW5, ECO:0007744|PDB:5LWA}
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 728-874, ACTIVE SITE
RP   (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE), MUTAGENESIS OF ASP-843;
RP   ILE-847; GLY-865 AND 866-PRO-PRO-867, DOMAIN
RP   (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE), AND FUNCTION
RP   (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE).
RX   PubMed=29117247; DOI=10.1371/journal.ppat.1006714;
RA   Jupin I., Ayach M., Jomat L., Fieulaine S., Bressanelli S.;
RT   "A mobile loop near the active site acts as a switch between the dual
RT   activities of a viral protease/deubiquitinase.";
RL   PLoS Pathog. 13:e1006714-e1006714(2017).
RN   [8] {ECO:0007744|PDB:6YPT}
RP   X-RAY CRYSTALLOGRAPHY (3.66 ANGSTROMS) OF 728-879 IN COMPLEX WITH
RP   UBIQUITIN, AND FUNCTION (METHYLTRANSFERASE/PROTEASE/UBIQUITINYL HYDROLASE).
RX   PubMed=32732284; DOI=10.1074/jbc.ra120.014628;
RA   Fieulaine S., Witte M.D., Theile C.S., Ayach M., Ploegh H.L., Jupin I.,
RA   Bressanelli S.;
RT   "Turnip yellow mosaic virus protease binds ubiquitin suboptimally to fine-
RT   tune its deubiquitinase activity.";
RL   J. Biol. Chem. 295:13769-13783(2020).
CC   -!- FUNCTION: Acts as a cysteine protease, methyltransferase and
CC       deubiquitinase (PubMed:22117220, PubMed:23966860, PubMed:29117247,
CC       PubMed:32732284) (Probable). The cysteine protease activity cleaves the
CC       polyprotein giving rise to mature proteins (PubMed:23966860). The
CC       methyltransferase domain is probably involved in viral RNA capping
CC       (Probable). The deubiquitylating activity counteracts the degradation
CC       of the viral polymerase mediated by the host ubiquitin-proteasome
CC       system (PubMed:22117220). The polymerase is thus stabilized and
CC       infectivity is increased (PubMed:22117220). Favors K63 poly-Ub linkage
CC       (PubMed:23345508). {ECO:0000269|PubMed:22117220,
CC       ECO:0000269|PubMed:23345508, ECO:0000269|PubMed:23966860,
CC       ECO:0000269|PubMed:29117247, ECO:0000269|PubMed:32732284, ECO:0000305,
CC       ECO:0000305|PubMed:23345508}.
CC   -!- FUNCTION: RNA-directed RNA polymerase is responsible for the
CC       replication and transcription of the genome. {ECO:0000255|PROSITE-
CC       ProRule:PRU00539, ECO:0000269|PubMed:22117220}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:22117220,
CC         ECO:0000269|PubMed:23345508};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=70.2 uM for Ub-AMC {ECO:0000269|PubMed:23345508};
CC   -!- SUBUNIT: Interacts with host ubiquitin. {ECO:0000269|PubMed:32732284}.
CC   -!- SUBCELLULAR LOCATION: [Methyltransferase/Protease/Ubiquitinyl
CC       hydrolase]: Host chloroplast envelope.
CC   -!- SUBCELLULAR LOCATION: [Putative helicase]: Host chloroplast envelope.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host chloroplast
CC       envelope {ECO:0000269|PubMed:11222099}.
CC   -!- DOMAIN: [Methyltransferase/Protease/Ubiquitinyl hydrolase]: The viral
CC       OTU domain (vOTU) is responsible for the deubiquitination activity
CC       (PubMed:23345508). Both protease (PRO) and deubiquitination (DUB)
CC       activities rely on the single catalytic site of the cysteine proteinase
CC       (PubMed:29117247). The switch in the PRO/DUB activities is due to the
CC       mobility of a GPP flap (PubMed:29117247). {ECO:0000269|PubMed:23345508,
CC       ECO:0000269|PubMed:29117247}.
CC   -!- MISCELLANEOUS: The deubiquitinase activity is low compared to that of
CC       Bunyaviruses or coronaviruses. {ECO:0000269|PubMed:22117220,
CC       ECO:0000269|PubMed:23345508, ECO:0000269|PubMed:23966860}.
CC   -!- SIMILARITY: Belongs to the tymovirus NS35 RNA replicase polyprotein
CC       family. {ECO:0000305}.
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DR   EMBL; X07441; CAA30322.1; ALT_SEQ; Genomic_RNA.
DR   PIR; S01956; S01956.
DR   RefSeq; NP_663297.1; NC_004063.1.
DR   PDB; 4A5U; X-ray; 2.00 A; A=728-879.
DR   PDB; 5LW5; X-ray; 1.65 A; A/B=728-874.
DR   PDB; 5LWA; X-ray; 1.65 A; A/B=728-879.
DR   PDB; 6YPT; X-ray; 3.66 A; A/C=728-879.
DR   PDBsum; 4A5U; -.
DR   PDBsum; 5LW5; -.
DR   PDBsum; 5LWA; -.
DR   PDBsum; 6YPT; -.
DR   SMR; P10358; -.
DR   MEROPS; C21.001; -.
DR   GeneID; 951158; -.
DR   KEGG; vg:951158; -.
DR   Proteomes; UP000000401; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23247; Tymoviridae_RdRp; 1.
DR   Gene3D; 3.90.70.100; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008043; Peptidase_C21.
DR   InterPro; IPR001788; RNA-dep_RNA_pol_alsuvir.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR043629; Salyut_dom.
DR   InterPro; IPR043181; TYMV_endopept_dom.
DR   Pfam; PF05381; Peptidase_C21; 1.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF19227; Salyut; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51738; PEPTIDASE_C21; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Host-virus interaction; Hydrolase;
KW   Methyltransferase;
KW   Modulation of host ubiquitin pathway by viral deubiquitinase;
KW   Modulation of host ubiquitin pathway by virus; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW   RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1844
FT                   /note="RNA replicase polyprotein"
FT                   /id="PRO_0000222938"
FT   CHAIN           1..879
FT                   /note="Methyltransferase/Protease/Ubiquitinyl hydrolase"
FT                   /id="PRO_0000418048"
FT   CHAIN           880..1259
FT                   /note="Putative helicase"
FT                   /id="PRO_0000418049"
FT   CHAIN           1260..1844
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000418050"
FT   DOMAIN          58..219
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          728..879
FT                   /note="OTU"
FT                   /evidence="ECO:0000269|PubMed:23345508"
FT   DOMAIN          730..884
FT                   /note="Peptidase C21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   DOMAIN          946..1103
FT                   /note="(+)RNA virus helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   DOMAIN          1104..1236
FT                   /note="(+)RNA virus helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   DOMAIN          1572..1678
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          571..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          859..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           865..867
FT                   /note="GPP flap"
FT                   /evidence="ECO:0000269|PubMed:29117247"
FT   COMPBIAS        571..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..623
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..698
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        783
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074,
FT                   ECO:0000269|PubMed:23966860, ECO:0000269|PubMed:29117247"
FT   ACT_SITE        869
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074,
FT                   ECO:0000269|PubMed:23966860, ECO:0000269|PubMed:29117247"
FT   BINDING         976..983
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            879..880
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:17686855"
FT   SITE            1259..1260
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:17686855"
FT   MUTAGEN         843
FT                   /note="D->A: 70% loss of deubiquitinase activity."
FT                   /evidence="ECO:0000269|PubMed:29117247"
FT   MUTAGEN         847
FT                   /note="I->A: 80% loss of deubiquitinase activity."
FT                   /evidence="ECO:0000269|PubMed:29117247"
FT   MUTAGEN         847
FT                   /note="I->D: Almost complete loss of deubiquitinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29117247"
FT   MUTAGEN         865
FT                   /note="G->A: 70% loss of deubiquitinase activity."
FT                   /evidence="ECO:0000269|PubMed:29117247"
FT   MUTAGEN         866..867
FT                   /note="PP->GG: Almost complete loss of deubiquitinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29117247"
FT   HELIX           734..737
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   STRAND          742..748
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   HELIX           749..752
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   STRAND          765..769
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   HELIX           783..792
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   HELIX           796..804
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   HELIX           809..811
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   HELIX           815..820
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   HELIX           824..833
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   STRAND          836..842
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   STRAND          845..850
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   STRAND          855..863
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   STRAND          865..867
FT                   /evidence="ECO:0007829|PDB:5LW5"
FT   STRAND          869..872
FT                   /evidence="ECO:0007829|PDB:5LW5"
SQ   SEQUENCE   1844 AA;  206641 MW;  A016D758C83D128C CRC64;
     MAFQLALDAL APTTHRDPSL HPILESTVDS IRSSIQTYPW SIPKELLPLL NSYGIPTSGL
     GTSHHPHAAH KTIETFLLCT HWSFQATTPS SVMFMKPSKF NKLAQVNSNF RELKNYRLHP
     NDSTRYPFTS PDLPVFPTIF MHDALMYYHP SQIMDLFLRK PNLERLYASL VVPPEAHLSD
     QSFYPKLYTY TTTRHTLHYV PEGHEAGSYN QPSDAHSWLR INSIRLGNHH LSVTILESWG
     PVHSLLIQRG TPPPDPSLQA PPTLMTSDLF RSYQEPRLDV VSFRIPDAIE LPQATFLQQP
     LRDRLVPRAV YNALFTYTRA VRTLRTSDPA AFVRMHSSKP DHDWVTSNAW DNLQTFALLN
     VPLRPNVVYH VLQSPIASLS LYLRQHWRRL TATAVPILSF LTLLQRFLPL PIPLAEVKSI
     TAFRRELYRK KEPHHPLDVF HLQHRVRNYH SAISAVRPAS PPHQKLPHAL QKAALLLLRP
     ISPLLTATPF FRSEQKSMLP NAELSWTLKR FALPWQASLV LLALSESSIL LHKLFSPPTL
     QAQHDTYHRH LHPGSYSLQW ERTPLSIPRT TAFLPFTPTT STAPPDRSEA SLPPAFASTF
     VPRPPPAASS PGAQPPTTTA APPTPIEPTQ RTHQNSDLAL ESSTSTEPPP PPIRSPDMTP
     SAPVLFPEIN SPRRFPPQLP ATPDLEPAHT PPPLSIPHQD PTDSADPLMG SHLLHHSLPA
     PPTHPLPSSQ LLPAPLTNDP TAIGPVLPFE ELHPRRYPEN TATFLTRLRS LPSNHLPQPT
     LNCLLSAVSD QTKVSEEHLW ESLQTILPDS QLSNEETNTL GLSTEHLTAL AHLYNFQATV
     YSDRGPILFG PSDTIKRIDI THTTGPPSHF SPGKRLLGSQ PSAKGHPSDP LIRAMKSFKV
     SGNYLPFSEA HNHPTSISHA KNLISNMKNG FDGVLSLLDV STGQRTGPTP KERIIQIDHY
     LDTNPGKTTP VVHFAGFAGC GKTYPIQQLL KTKLFKDFRV SCPTTELRTE WKTAMELHGS
     QSWRFNTWES SILKSSRILV IDEIYKMPRG YLDLSILADP ALELVIILGD PLQGEYHSQS
     KDSSNHRLPS ETLRLLPYID MYCWWSYRIP QCIARLFQIH SFNAWQGVIG SVSTPHDQSP
     VLTNSHASSL TFNSLGYRSC TISSSQGLTF CDPAIIVLDN YTKWLSSANG LVALTRSRSG
     VQFMGPSSYV GGTNGSSAMF SDAFNNSLII MDRYFPSLFP QLKLITSPLT TRGPKLNGAT
     PSASPTHRSP NFHLPPHIPL SYDRDFVTVN PTLPDQGPET RLDTHFLPPS RLPLHFDLPP
     AITPPPVSTS VDPPQAKASP VYPGEFFDSL AAFFLPAHDP STREILHKDQ SSNQFPWFDR
     PFSLSCQPSS LISAKHAPNH DPTLLPASIN KRLRFRPSDS PHQITADDVV LGLQLFHSLC
     RAYSRQPNST VPFNPELFAE CISLNEYAQL SSKTQSTIVA NASRSDPDWR HTTVKIFAKA
     QHKVNDGSIF GSWKACQTLA LMHDYVILVL GPVKKYQRIF DNADRPPNIY SHCGKTPNQL
     RDWCQEHLTH STPKIANDYT AFDQSQHGES VVLEALKMKR LNIPSHLIQL HVHLKTNVST
     QFGPLTCMRL TGEPGTYDDN TDYNLAVIYS QYDVGSCPIM VSGDDSLIDH PLPTRHDWPS
     VLKRLHLRFK LELTSHPLFC GYYVGPAGCI RNPLALFCKL MIAVDDDALD DRRLSYLTEF
     TTGHLLGESL WHLLPETHVQ YQSACFDFFC RRCPRHEKML LDDSTPALSL LERITSSPRW
     LTKNAMYLLP AKLRLAITSL SQTQSFPESI EVSHAESELL HYVQ
//