GenomeNet

Database: UniProt
Entry: Q85197
LinkDB: Q85197
Original site: Q85197 
ID   POLG_PVMA               Reviewed;        3059 AA.
AC   Q85197;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-NOV-2019, entry version 130.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE              EC=3.4.-.-;
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
DE   Contains:
DE     RecName: Full=Protein P3;
DE   Contains:
DE     RecName: Full=6 kDa protein 1;
DE              Short=6K1;
DE   Contains:
DE     RecName: Full=Cytoplasmic inclusion protein;
DE              Short=CI;
DE              EC=3.6.4.-;
DE   Contains:
DE     RecName: Full=6 kDa protein 2;
DE              Short=6K2;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein A;
DE              Short=NI-a;
DE              Short=NIa;
DE              EC=3.4.22.44;
DE     AltName: Full=49 kDa proteinase;
DE              Short=49 kDa-Pro;
DE     AltName: Full=NIa-pro;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein B;
DE              Short=NI-b;
DE              Short=NIb;
DE              EC=2.7.7.48;
DE     AltName: Full=RNA-directed RNA polymerase;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
OS   Potato virus A (PVA).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12215;
OH   NCBI_TaxID=45843; Solanum betaceum (Tamarillo) (Cyphomandra betacea).
OH   NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8113771; DOI=10.1099/0022-1317-75-2-457;
RA   Puurand U., Makinen K., Paulin L., Saarma M.;
RT   "The nucleotide sequence of potato virus A genomic RNA and its
RT   sequence similarities with otherpotyviruses.";
RL   J. Gen. Virol. 75:457-461(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2667-3059.
RX   PubMed=1604933; DOI=10.1016/0168-1702(92)90070-p;
RA   Puurand U., Mkinen K., Baumann M., Saarma M.;
RT   "Nucleotide sequence of the 3'-terminal region of potato virus A
RT   RNA.";
RL   Virus Res. 23:99-105(1992).
RN   [3]
RP   PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX   PubMed=11961277; DOI=10.1099/0022-1317-83-5-1211;
RA   Merits A., Rajamaeki M.-L., Lindholm P., Runeberg-Roos P.,
RA   Kekarainen T., Puustinen P., Maekelaeinen K., Valkonen J.P.T.,
RA   Saarma M.;
RT   "Proteolytic processing of potyviral proteins and polyprotein
RT   processing intermediates in insect and plant cells.";
RL   J. Gen. Virol. 83:1211-1221(2002).
RN   [4]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
RN   [5]
RP   COVALENT RNA LINKAGE OF VPG, AND URIDYLYLATION.
RX   PubMed=15218030; DOI=10.1074/jbc.m402910200;
RA   Puustinen P., Makinen K.;
RT   "Uridylylation of the potyvirus VPg by viral replicase NIb correlates
RT   with the nucleotide binding capacity of VPg.";
RL   J. Biol. Chem. 279:38103-38110(2004).
CC   -!- FUNCTION: Capsid protein: involved in aphid transmission, cell-to-
CC       cell and systemis movement, encapsidation of the viral RNA and in
CC       the regulation of viral RNA amplification.
CC   -!- FUNCTION: Nuclear inclusion protein B: an RNA-dependent RNA
CC       polymerase that plays an essential role in the virus replication.
CC   -!- FUNCTION: Helper component proteinase: required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a
CC       Gly-Gly dipeptide at its own C-terminus. Interacts with virions
CC       and aphid stylets. Acts as a suppressor of RNA-mediated gene
CC       silencing, also known as post-transcriptional gene silencing
CC       (PTGS), a mechanism of plant viral defense that limits the
CC       accumulation of viral RNAs. May have RNA-binding activity (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Cytoplasmic inclusion protein: has helicase activity. It
CC       may be involved in replication (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Both 6K peptides are indispensable for virus
CC       replication.
CC   -!- FUNCTION: Nuclear inclusion protein A: has RNA-binding and
CC       proteolytic activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC         restricted by preferences for the amino acids in P6 - P1' that
CC         vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-
CC         Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The
CC         natural substrate is the viral polyprotein, but other proteins
CC         and oligopeptides containing the appropriate consensus sequence
CC         are also cleaved.; EC=3.4.22.44;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus,
CC         commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the
CC         processing of the potyviral polyprotein.; EC=3.4.22.45;
CC   -!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome polyprotein;
CC         IsoId=Q85197-1; Sequence=Displayed;
CC         Note=Produced by conventional translation.;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CK05-1; Sequence=External;
CC         Note=Produced by -1 ribosomal frameshifting in P3 ORF.;
CC   -!- DOMAIN: The N-terminus of helper component proteinase is involved
CC       in interaction with stylets. The central part is involved in
CC       interaction with virions and the C-terminus is involved in cell-to
CC       cell movement of the virus.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently
CC       attached to the 5'-end of the genomic RNA. This uridylylated form
CC       acts as a nucleotide-peptide primer for the polymerase.
CC   -!- PTM: Potyviral RNA is expressed as two polyproteins which undergo
CC       post-translational proteolytic processing. Genome polyprotein is
CC       processed by NIa-pro, P1 and HC-pro proteinases resulting in the
CC       production of at least ten individual proteins. P3N-PIPO
CC       polyprotein is cleaved by P1 and HC-pro proteinases resulting in
CC       the production of three individual proteins. The P1 proteinase and
CC       the HC-pro cleave only their respective C-termini
CC       autocatalytically. 6K1 is essential for proper proteolytic
CC       separation of P3 from CI (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: 6K1 and 6K2 are involved in infectivity, as their
CC       deletion renders PVA non-infectious.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; Z21670; CAA79766.1; -; Genomic_RNA.
DR   MEROPS; C04.014; -.
DR   PRIDE; Q85197; -.
DR   Proteomes; UP000008484; Genome.
DR   GO; GO:0019029; C:helical 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:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.90.70.150; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR039560; Potyvirid-P3.
DR   InterPro; IPR013648; PP_Potyviridae.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF13608; Potyvirid-P3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Capsid protein; Complete proteome;
KW   Covalent protein-RNA linkage; Helical capsid protein; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Protease; Ribosomal frameshifting; RNA-directed RNA polymerase;
KW   Serine protease; Suppressor of RNA silencing; Thiol protease;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN         1   3059       Genome polyprotein.
FT                                /FTId=PRO_0000420014.
FT   CHAIN         1    298       P1 proteinase. {ECO:0000255}.
FT                                /FTId=PRO_0000040385.
FT   CHAIN       299    755       Helper component proteinase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000040386.
FT   CHAIN       756   1102       Protein P3.
FT                                /FTId=PRO_0000040387.
FT   CHAIN      1103   1154       6 kDa protein 1.
FT                                /FTId=PRO_0000040388.
FT   CHAIN      1155   1789       Cytoplasmic inclusion protein.
FT                                /FTId=PRO_0000040389.
FT   CHAIN      1790   1842       6 kDa protein 2.
FT                                /FTId=PRO_0000040390.
FT   CHAIN      1843   2031       Viral genome-linked protein.
FT                                /FTId=PRO_0000040391.
FT   CHAIN      2032   2274       Nuclear inclusion protein A.
FT                                /FTId=PRO_0000040392.
FT   CHAIN      2275   2790       Nuclear inclusion protein B.
FT                                /FTId=PRO_0000040393.
FT   CHAIN      2791   3059       Capsid protein.
FT                                /FTId=PRO_0000040394.
FT   DOMAIN      154    298       Peptidase S30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01219}.
FT   DOMAIN      633    755       Peptidase C6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01080}.
FT   DOMAIN     1226   1378       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1397   1556       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2032   2250       Peptidase C4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00766}.
FT   DOMAIN     2516   2640       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1239   1246       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       349    352       Involved in interaction with stylet and
FT                                aphid transmission. {ECO:0000250}.
FT   MOTIF       607    609       Involved in virions binding and aphid
FT                                transmission. {ECO:0000250}.
FT   MOTIF      1328   1331       DEFH box.
FT   MOTIF      1883   1890       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   ACT_SITE    207    207       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    216    216       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    249    249       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    641    641       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE    714    714       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE   2077   2077       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2112   2112       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2182   2182       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   SITE        298    299       Cleavage; by P1 proteinase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   SITE        755    756       Cleavage; by autolysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   SITE       1102   1103       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1154   1155       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1789   1790       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1842   1843       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2031   2032       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2274   2275       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2790   2791       Cleavage; by NIa-pro. {ECO:0000250}.
FT   MOD_RES    1905   1905       O-(5'-phospho-RNA)-tyrosine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   3059 AA;  346080 MW;  EFE897679595693A CRC64;
     MATQVIMVGE FKILEVNCKP HAPVAAIHVP TQTPKTNDIK WADLEFTLAK SLQRQAHGVV
     KVDKHGTARI KRASKHHMSC LEQQMADEVA EKEAFMAAPT QLVTSIIFAG TTPPSMMETE
     TIVKKIHTVG KRAKVMRKRS YITPPTDKSL RNHGVTPYSV QQLCRTLGNL SKRTGISLEV
     VGKTSKATKL RFTKTSFGHM ARVQLKHHDG RMHRRDLVVD TSTTTIMQTL FLKTARTNAN
     LDVLTHGSSG LVFWNYLVTG QRMRTRDNFI IVRGRCNGIL VDARAKLSES TMLSTHHYST
     GDVFWRGFNR TFLENKPINL DHVCSSDFSV EECGSIAALI CQSLLPCGKI TCRACAAKNL
     NMDEDTFKEF QTQRAREISA VIISEHPNFA CVSQFIDRYF SHQRVLNPNV NAYREILKIV
     GGFTQSPYTH IQELNEILVL GGRATPEQLG SASAHLLEIT RFVRNRTDNI KKGSLALFRN
     KISAKAHVNT ALMCDNQLDR NGNLIWGERG YHAKRFFSNY FDIITPGGGY KQYIERRVPN
     GIRKLAIGNL IVTTNLEALR EQLEGESIEK KAVTKACVSM SDNNYKYPCC CVTLDDGTPL
     YSTFIMPTKN HLVIGNSGDP KFLDLPADIS TQMYIAKSGY CYINIFLAML VNVDESDAKD
     FTKKVRDIIV PDLGEWPTLI DVATSCSLLS AFYPATSAAE LPRILVDHDL KTMHVIDSYG
     SLNTGYHVLK ANTIRQLIQF ASNSLDSEMK HYRVGGTSNS QINGYATIKM LAKAVYRPKL
     MKEIIHEQPF MLVMSLMSPG ILIALANSGA LEMGIHHWIR EGDSLVKMAH MLRTVAQNVS
     VARATWVQQE IISDSAQQML ETILNGTIPN VSYFQAIQYL TMLAASKEVD AEVRVTGYYT
     FKLQTSELLE KTYLSLLEDS WQELSYFGRF QAIRHSRRYC TAGTIVVKPE RHVDLGGIYA
     TSYQFALAKQ MEYSKKAVCQ AVNGLQARFN NITSQIYCKI LNWPKRLFPD LVKFINTMLA
     ITVALQLYIA FATILRHHQQ CKQDSLELEY CKKERQLITL YDFFIAKQPY ATEEEFMAHV
     DEQNPDLSNF AREYCAEVVL FQAKASEQVN FERIIAFISL VLMMFDRERS DCVYRSLTKL
     KSLMSTVENT VQFQSLDDIG PTLEEKNMTI DFDLDTDTIV GKSIIGHTFK EWWDVQLNTN
     RIVPHYRTEG HFMEFTRANA PTIAHQIAHD LHTDIMLRGA VGSGKSTGLP YHLSKKGTVL
     LLEPTRPLAE NVTKQLKSDP FHVSPTLRMR GMAVFGSTPI HVMTTGFALH YLANNLKMLS
     TYDFIIIDEF HVHDSNAIAL RNLLHEHNYQ GKLIKVSATP PGREVEFSTQ YPVEIRVEDQ
     VSFQDFVKAQ GNGSNLDLTS KCDNLLVYVA SYNEVDQLSK LLLERHFLVT KVDGRSMKLG
     QVEIITKGSA NKKHFIVATN IIENGVTLDI DAVIDFGMKV VPFLDSDNRM ISYNKVSISY
     GERIQRLGRV GRNKAGVALR IGHTEKGISD VPVVIATQAA FLGFVYGLPI STQSVTTQVL
     SNVTLKQART MVQFELPIFY MAHLVRYDGT MHPAIHNELK KYKLRDSEIQ LRKLAIPSKC
     VPIWMTGKAY RLLTHNSQIP DDVRVPFLTK EIPDKLHENV WAIVEKFKCD AGIGRMTSAQ
     ASKVAYTLET DIHSVQRTIL IIDQLLEREM QKQSHFEMVT NQSCSSGMLS LQTMMNAIQS
     RYAKNHTAGN IEILQRAKAQ LLEFSNLSGD ISTESALREF GYLEAVQFQS GTQVSNFLGL
     EGHWKKSLIT KDLLIVGGVC VGAAWMIGEY FFKKSKGVVA FQGIISDRGK KLKFARARDE
     KMGHYVEAPD STLEHYFGSA YTKKGKTKGK THGMGKKNHR FVNMYGFDPS DYTFIRYVDP
     LTGYTLDESP YTDIRLIQSQ FSDIREQQLL NDELERNMVH YKPGVQGYLV KDKTSQILKI
     DLTPHIPLKV CDATNNIAGH PDREGELRQT GKGQLLDYAE LPQKKESVEF ESTSMFRGVR
     DYNPISSVIC QLENESEGRT TQLFGLGFGP FIITNQHLFV RNNGSLTVRS QMGVFKVNST
     VALQMRPVEG RDVLIIKMPK DFPPFPQRLK FRQPTHSEKV CLILTNFQQK SSSSMVSETS
     ILYQRKNTYF WKHWISTKEG HCGSPIVSTT DGAILGIHSL SNMTNTSNYF ACFPKGFTET
     YLATESVHEW VKGWKFNANN VCWGSFHLQD SKPTKEFKTV KLVTDLLGEA VYTQGCDSKW
     LFNAAHTNIQ AVAQLESNLV TKHTVKGKCK LFETYLNVDK AAHDFFSKYM GFYKPSKLNR
     EAYTQDLMKY SKVIQVGEVD CGVFESALTG LLHNLGRWGF TTACYTTDED SIYTALNMKA
     AVGALYRGKK RDYFDAMSPS EREHLLFLSC KRLYFGQLGV WNGSLKAELR PKEKVDLNKT
     RTFTAAPIET LLGGKVCVDD FNNMFYSLHL KAPWSVGMTK FYGTWNQLMC KLPDDWVYCD
     ADGSQFDSSI SPYMINAVLR IRLHFMEDWD IGSQMLQNLY TEIGTHQSQH QMAQLLKKFK
     GNNSGQPSTV VDNTLLVVLA LHYALLKSGI PLEEQDSVCA YGVNGDDLLI AIRPDMEHKL
     DGFQALFSEL GLNYEFNSRS KDKKDLWFMS HKAIQCGEIL IPKLEEERIV SILEWDRSHE
     PIHRLEAICA SMVESWGYPE LTHEIRRFYA WVLEQSPYNA LATTGLAPYI AESALKTLYT
     NVHPTSTELE KYSIQFDEQM DEEDDMVYFQ AETLDASEAL AQKSEGRKKE RESNSSKAVA
     VKDKDVDLGT AGTHSVPRLK SMTSKLTLPM LKGKSVVNLD HLLSYKPKQV DLSNARATHE
     QFQNWYDGVM ASYELEESSM EIILNGFMVW CIENGTSPDI NGVWTMMDNE EQVSYPLKPM
     LDHAKPSLRQ IMRHFSALAE AYIEMRSREK PYMPRYGLQR NLRDQSLARY AFDFYEITAT
     TPIRAKEAHL QMKAAALKNS NTNMFGLDGN VTTSEEDTER HTATDVNRNM HHLLGVKGV
//
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