ID   POLG_AEVCA              Reviewed;        2134 AA.
AC   Q9YLS4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein VP0;
DE     AltName: Full=VP4-VP2;
DE   Contains:
DE     RecName: Full=Capsid protein VP4;
DE     AltName: Full=P1A;
DE     AltName: Full=Virion protein 4;
DE   Contains:
DE     RecName: Full=Capsid protein VP2;
DE     AltName: Full=P1B;
DE     AltName: Full=Virion protein 2;
DE   Contains:
DE     RecName: Full=Capsid protein VP3;
DE     AltName: Full=P1C;
DE     AltName: Full=Virion protein 3;
DE   Contains:
DE     RecName: Full=Capsid protein VP1;
DE     AltName: Full=P1D;
DE     AltName: Full=Virion protein 1;
DE   Contains:
DE     RecName: Full=Protein 2A;
DE              Short=P2A;
DE   Contains:
DE     RecName: Full=Protein 2B;
DE              Short=P2B;
DE   Contains:
DE     RecName: Full=Protein 2C;
DE              Short=P2C;
DE              EC=3.6.1.15;
DE   Contains:
DE     RecName: Full=Protein 3A;
DE              Short=P3A;
DE   Contains:
DE     RecName: Full=Protein 3B;
DE              Short=P3B;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Protease 3C;
DE              Short=P3C;
DE              EC=3.4.22.28;
DE     AltName: Full=Picornain 3C;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE              Short=P3D-POL;
DE              EC=2.7.7.48;
OS   Avian encephalomyelitis virus (strain Calnek vaccine) (AEV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Heptrevirinae; Tremovirus; Tremovirus A.
OX   NCBI_TaxID=475778;
OH   NCBI_TaxID=8835; Anas (ducks).
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
OH   NCBI_TaxID=9005; Phasianidae (turkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10092005; DOI=10.1099/0022-1317-80-3-653;
RA   Marvil P., Knowles N.J., Mockett A.P., Britton P., Brown T.D.K.,
RA   Cavanagh D.;
RT   "Avian encephalomyelitis virus is a picornavirus and is most closely
RT   related to hepatitis A virus.";
RL   J. Gen. Virol. 80:653-662(1999).
CC   -!- FUNCTION: Capsid proteins VP1, VP2, and VP3 form a closed capsid
CC       enclosing the viral positive strand RNA genome. All these proteins
CC       contain a beta-sheet structure called beta-barrel jelly roll. Together
CC       they form an icosahedral capsid (T=3) composed of 60 copies of each
CC       VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1
CC       is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at
CC       the quasi-sixfold axes (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of
CC       immature procapsids. The N-terminal domain of VP0, protein VP4, is
CC       needed for the assembly of 12 pentamers into the icosahedral structure.
CC       Unlike other picornaviruses, AEV VP4 may not be myristoylated (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Protein 2B and 2BC precursor affect membrane integrity and
CC       cause an increase in membrane permeability. {ECO:0000250}.
CC   -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC       rearrangements of intracellular membranes. It displays RNA-binding,
CC       nucleotide binding and NTPase activities (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane
CC       anchor. {ECO:0000250}.
CC   -!- FUNCTION: Protein 3B is covalently linked to the 5'-end of both the
CC       positive-strand and negative-strand genomic RNAs. It acts as a genome-
CC       linked replication primer (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC       proteins from the precursor polyprotein. In addition to its proteolytic
CC       activity, it binds to viral RNA, and thus influences viral genome
CC       replication. RNA and substrate bind cooperatively to the protease (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and
CC       antigenomic RNA by recognizing replications specific signals.
CC       {ECO:0000255|PROSITE-ProRule:PRU00539}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC         polyprotein. In other picornavirus reactions Glu may be substituted
CC         for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum. May associate with membranes through a N-
CC       terminal amphipathic helix (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Protein 3B]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host
CC       cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Interacts with
CC       membranes in a complex with viral protein 3AB. Probably localizes to
CC       the surface of intracellular membrane vesicles that are induced after
CC       virus infection as the site for viral RNA replication. These vesicles
CC       are derived from the endoplasmic reticulum (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages by the viral protease in vivo yield a
CC       variety of precursors and mature proteins. During virion maturation,
CC       non-infectious particles are rendered infectious following cleavage of
CC       VP0. This maturation cleavage is followed by a conformational change of
CC       the particle (By similarity). {ECO:0000250}.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC       the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC       peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ225173; CAA12416.1; -; mRNA.
DR   RefSeq; NP_653151.1; NC_003990.1.
DR   SMR; Q9YLS4; -.
DR   MEROPS; C03.005; -.
DR   TCDB; 1.A.122.1.2; the avian encephalomyelitis virus protein 3a (aev-3a) family.
DR   GeneID; 944582; -.
DR   KEGG; vg:944582; -.
DR   Proteomes; UP000000357; Segment.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR   CDD; cd23193; ps-ssRNA_Picornaviridae; 1.
DR   CDD; cd00205; rhv_like; 2.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR024354; Hepatitis_A_VP1-2A.
DR   InterPro; IPR007053; LRAT_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001676; Picornavirus_capsid.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR033703; Rhv-like.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF12944; HAV_VP; 1.
DR   Pfam; PF04970; LRAT; 1.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 2.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 3.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51934; LRAT; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Capsid protein; Covalent protein-RNA linkage; Helicase;
KW   Host cytoplasm; Host cytoplasmic vesicle; Host membrane;
KW   Host-virus interaction; Hydrolase; Ion channel; Ion transport; Membrane;
KW   Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW   Reference proteome; RNA-binding; RNA-directed RNA polymerase;
KW   Thiol protease; Transferase; Transport; Viral attachment to host cell;
KW   Viral ion channel; Viral RNA replication; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..2134
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000310495"
FT   CHAIN           1..242
FT                   /note="Capsid protein VP0"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310496"
FT   CHAIN           1..19
FT                   /note="Capsid protein VP4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310497"
FT   CHAIN           20..242
FT                   /note="Capsid protein VP2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310498"
FT   CHAIN           243..487
FT                   /note="Capsid protein VP3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310499"
FT   CHAIN           488..757
FT                   /note="Capsid protein VP1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310500"
FT   CHAIN           758..806
FT                   /note="Protein 2A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310501"
FT   CHAIN           807..1021
FT                   /note="Protein 2B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310502"
FT   CHAIN           1022..1347
FT                   /note="Protein 2C"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310503"
FT   CHAIN           1348..1412
FT                   /note="Protein 3A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310504"
FT   CHAIN           1413..1433
FT                   /note="Protein 3B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310505"
FT   CHAIN           1434..1648
FT                   /note="Protease 3C"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310506"
FT   CHAIN           1649..2134
FT                   /note="RNA-directed RNA polymerase 3D-POL"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310507"
FT   TOPO_DOM        1..1377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1378..1392
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1393..2134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          781..882
FT                   /note="LRAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   DOMAIN          1127..1289
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1431..1643
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1880..2001
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ACT_SITE        791
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   ACT_SITE        802
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   ACT_SITE        863
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   ACT_SITE        1477
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1515
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1603
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         1153..1160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   SITE            19..20
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            242..243
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            487..488
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            757..758
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000255"
FT   SITE            806..807
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250"
FT   SITE            1021..1022
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1347..1348
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1412..1413
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1433..1434
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1648..1649
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1415
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   2134 AA;  238980 MW;  5BD829687E1ED30D CRC64;
     MSKLFSTVGK TVDEVLSVLN DENTESYAGP DRTAVVGGGF LTTVDQSSVS TATMGSLQDV
     QYRTAVDIPG SRVTQGERFF LIDQREWNST QSEWQLLGKI DIVKELLDQS YAVDGLLKYH
     SYARFGLDVI VQINPTSFQA GGLIAALVPY DQVDIESIAA MTTYCHGKLN CNINNVVRMK
     VPYIYSRGCY NLRNSAYSIW MLVIRVWSQL QLGSGTSTQI TVTTLARFVD LELHGLSPLV
     AQMMRNEFRL SSSSNIVNLA NYEDARAKVS LALGQEEFSR DSSSTGGELL HHFSQWTSIP
     CLAFTFTFPG TVGPGTQIWS TTVDPFSCNL RASSTVHPTN LSSIAGMFCF WRGDIVFEFQ
     VFCTKYHSGR LMFVYVPGDE NTKISTLTAK QASSGLTAVF DINGVNSTLV FRCPFISDTP
     YRVNPTTHKS LWPYATGKLV CYVYNRLNAP ASVSPSVSIN VYKSAVDLEL YAPVYGVSPT
     NTSVFAQGKE DEGGFSSVPE VEQHVVEDKE PQGPLHVTPF GAVKAMEDPQ LARKTPGTFP
     ELAPGKPRHT VDHMDLYKFM GRAHYLWGHK FTKTDMQYTF QIPLSPIKEG FVTGTLRWFL
     SLFQLYRGSL DITMTFAGKT NVDGIVYFVP EGVAIETERE EQTPLLTLNY KTSVGAIRFN
     TGQTTNVQFR IPFYTPLEHI ATHSKNAMDS VLGAITTQIT NYSAQDEYLQ VTYYISFNED
     SQFSVPRAVP VVSSFTDTSS KTVMNTYWLD DDELVEESSH SSFDEIEEAQ CSKCKMDLGD
     IVSCSGEKAK HFGVYVGDGV VHVDPEGNAT NWFMKRKATV KKSKNLDKWC FALSPRIDRT
     LICETANLMV GREVEYDIFV KNCETYARGI ASGDYGTKEG EKWKTLLSAV GVAAMTTTMM
     AMRHELLDTS LTKLPQKVGE VTNEVRKILE DTSAGVREFK EKVSSILRKT WPGKTSIKIM
     KWTCRIVKMC VGVGLCYAHG WDSKTVTAVV TMFSMDFLDL VIDGIEIGRM IIDELTTPKA
     QGLSEINQVL SIAKNAKDVI KMLIEIFCKV IERITGEHGK KIQWAQDKKE EIMNVLERAE
     KWITTSDDHS EGIECLKLVR SIQSVIRGEE SLKELAGELR AVGTHVLNKL GRLDKPNAPI
     LVRAEPTVLY LYGNRGGGKS LASMAIAVKL CKELGISHVE GIYTKPIMSD FWDGYAGQPV
     VIMDDLGQST SDEDWTNFCQ LVSSCPLRLN MANLEKKGTQ FNSPFIIASS NLSHPCPKTV
     YCTDAIARRL HIKVKVSPKE EFSTHAMLDV AKAKKAGAYC NLDCLDFQKI SDLASTPVSV
     QDIVLEMLHT NVDKQTLMGD IIQYWAQSNP REVFDTMAEG KNSGKYLWLF EKIKTSKWYI
     LGCVGAVLSV SVLGVFAYHM IKNHFRDQQH DQSAYSAAIK PLRVVRLEQS DAQSVVDISN
     VVHGNLVRVG VGPNEARIHW LYNGLGVYDT YILMPYHGIK DADVDDDLYI ERAGTIYSTN
     MKMVQVLFLE SREGDLVLIN VPRLPKFRDI RNHFSTEENI RRAEGMPGTL CTLDHERFTL
     VTESDLKMVE AATYVCEDDK GVRTDISVGR SWKAKACTVA GMCGGALVTS NNKMQNAIVG
     IHVAGGAHAI SRVITKEMIE EMLKTRAQCS RIWKTEFVEE KISVGSKTKY HKSPLYDFCP
     QEVIKCPTKL FYQGEIDVMQ VMLAKYSSPI VSEPLGYATV VEAYTNRMVS FFSEPRQLTY
     DECINGIEGL DAIDLKTSAG FPYNTLGLRK SDLIINGKMA QRLQQDVEKM EEDLHMNRSI
     QVVFTTCAKD ELRPLSKVML GKTRAIEACP VSFTILFRRY LGYALAQIQS HPGFHTGIAV
     GVDPDQDWHC MWYSIVTQCD LVVGLDFSNY DASLSPFMIY HAGRVLGQIC GLDPRLVDRI
     MEPIVNSVHQ LGSMRYYVHG SMPSGTPATS VLNSIINVVN ICHVLCALEK ISVFEVFKLF
     KILTYGDDVL LCIKKEYLDQ KSFPLSSFVQ GLEELGLSPT GADKMEVKVT PVHKMSFLKR
     TFYVDEWSIC HPRISEETVY SMLAWKSDNA SMKDLIETSI WFMFHHGPRK YVRFCTWLRG
     VLCRVGIGLY IPTYKELEVR YDRLVKYRFI DDSF
//