GenomeNet

Database: UniProt
Entry: O56075
LinkDB: O56075
Original site: O56075 
ID   POLG_PEMVM              Reviewed;        3099 AA.
AC   O56075;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   11-DEC-2019, entry version 137.
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   Peanut mottle virus (strain M).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=103926;
OH   NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH   NCBI_TaxID=108216; Arachis pintoi.
OH   NCBI_TaxID=53851; Cassia.
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH   NCBI_TaxID=35627; Stylosanthes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Flasinski S., Gonzales R.A., Cassidy B.G.;
RT   "The complete nucleotide sequence of peanut mottle virus (M strain) genomic
RT   RNA.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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).
CC   -!- FUNCTION: [Capsid protein]: involved in aphid transmission, cell-to-
CC       cell and systemis movement, encapsidation of the viral RNA and in the
CC       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 Gly-Gly
CC       dipeptide at its own C-terminus. Interacts with virions and aphid
CC       stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC       known as post-transcriptional gene silencing (PTGS), a mechanism of
CC       plant viral defense that limits the accumulation of viral RNAs. May
CC       have RNA-binding activity (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Cytoplasmic inclusion protein]: has helicase activity. It
CC       may be involved in replication.
CC   -!- FUNCTION: Both 6K peptides are indispensable for virus replication.
CC       {ECO:0000250}.
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 vary
CC         with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC         Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC         the viral polyprotein, but other proteins and oligopeptides
CC         containing the appropriate consensus sequence are also cleaved.;
CC         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, ChEBI:CHEBI:83400;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC         the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC         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=O56075-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CK00-1; Sequence=External;
CC   -!- DOMAIN: The N-terminus of helper component proteinase is involved in
CC       interaction with stylets. The central part is involved in interaction
CC       with virions and the C-terminus is involved in cell-to cell movement of
CC       the virus.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC       to the 5'-end of the genomic RNA. This uridylylated form acts as a
CC       nucleotide-peptide primer for the polymerase (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Potyviral RNA is expressed as two polyproteins which undergo post-
CC       translational proteolytic processing. Genome polyprotein is processed
CC       by NIa-pro, P1 and HC-pro proteinases resulting in the production of at
CC       least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1
CC       and HC-pro proteinases resulting in the production of three individual
CC       proteins. The P1 proteinase and the HC-pro cleave only their respective
CC       C-termini autocatalytically. 6K1 is essential for proper proteolytic
CC       separation of P3 from CI (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC       translation.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; AF023848; AAB94595.1; -; Genomic_RNA.
DR   RefSeq; NP_068348.2; NC_002600.1.
DR   MEROPS; C06.001; -.
DR   PRIDE; O56075; -.
DR   GeneID; 912241; -.
DR   KEGG; vg:912241; -.
DR   Proteomes; UP000000471; 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   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW   Helical capsid protein; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Ribosomal frameshifting;
KW   RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW   Thiol protease; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..3099
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420004"
FT   CHAIN           1..322
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040305"
FT   CHAIN           323..779
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040306"
FT   CHAIN           780..1128
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040307"
FT   CHAIN           1129..1180
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040308"
FT   CHAIN           1181..1814
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040309"
FT   CHAIN           1815..1867
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040310"
FT   CHAIN           1868..2057
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040311"
FT   CHAIN           2058..2303
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040312"
FT   CHAIN           2304..2821
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040313"
FT   CHAIN           2822..3099
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040314"
FT   DOMAIN          180..322
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          657..779
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1252..1404
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1423..1582
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2058..2276
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2545..2669
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1265..1272
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           374..377
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           631..633
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1354..1357
FT                   /note="DESH box"
FT   MOTIF           1906..1915
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        233
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        242
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        275
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        665
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        738
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2103
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2138
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2208
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            322..323
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            779..780
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1128..1129
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1180..1181
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1814..1815
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1867..1868
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2057..2058
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2303..2304
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2821..2822
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1930
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   3099 AA;  351038 MW;  0D8E9FC7603F0A4B CRC64;
     MASITFGNAC TVVFGQVRKE EVTAGPVAVN LNEGTRMVVV PTAAQMATPT PSVSIKIINR
     WSNKAVSSYE RQVEDVFANF FAKKERSDEL LTRYYGKVVQ KGNKLMVKRA PLHVARVLEK
     QRLQDIEDEK AFLQYRDAGV HVAGSVKFTD TRSRGQTVSF RTEHYKPTGK IVQKKKAQKQ
     RANADVDHLI DEVMKICSAD CKQVEFISMG KRRLTAKFKL FGKSVIPCIH LAHEQGRRLR
     RELDPRIHEQ VIAHLVTGRK VRELIKDDMV TYGWSGAILN KNLFKRTPFR WDEVVIRGRL
     YGKLVDARSK LSECSKDKIH QYSSFEAQFW KGWKNKFDTL HPHNKDHICE PTINNEKCGE
     IVATIFQAIH PVIKVSCSTC RERLTKASNE ELNEYLATNL ACHKATFDDM RQQHATVNTV
     LNKIEQTSLA NPNLKDSMEI VRLLQNLNQT QARQLMKVNN TLLKGNVATS EEFSDATTQL
     LEVTRWYAKH LSLVDEGSIS SFRNKATSKS LINPSLLCDN QLDRNGNFVW GERGRHSKRF
     FENFFEEVVP GGGYKKYQIR NSPNCTRKLA IGNLIVPMSL ERARNALIGE SVERLPVTEA
     CVSRVNGAFM HVASCVTSDN GSAHFSPLYS PTKRHLVVGT TGDSKYIDLP ATESDKMYVA
     KEGYCYINIF LAMLVNVNED SAKDFTKMIR DTIVPMLGTW PSMMDVATAC YILTVFHPET
     KSAELPRILV DHTNKTMHVI DSFGSISTGY HILKAGTVSQ LIHFASNELV SEMKHYVVGG
     EAPHARRMRM EKALIQGIFK PKQLVYLIEE DPYILMMSLV SPTLLINLFN VGGLEVAMKH
     WIKKEMNIGL IFSMLSSLAQ KVSRADLVNE QITMIDANAA QFIETLAGID VENPMRNELV
     SALTMMLARS DVDSTLNKTG FTGFSDTLLE MREKIIGDEL NKVWSELSWW EKFSSIIFSR
     RARKHIMAPL PNTKLHAIDD RYAISCTWLH GKIKARFNGA KSATLEVCKK VTSILKRNTV
     DSILYICRKC YSDIFYFVNV MLISSMILSV IYTMHKMVIE SRAHKQAMVI MKMREDELVV
     KQMYDQYCKL ANETPTKEEF FQYVCKMNKE LGERIAPEFE EGSLVVYQAK TETELGLEKV
     VAYLALIAMI FDGERSDAVF RALSKLKTVF GTLGETVRYQ SLDEIESVAD EKKMTIDFEL
     EGSEASSSTV MSAKFSDWWY KQLETNRVVP HYRIGGEFVE FTRKTAAEVV NNMRASNASE
     FLVRGAVGSG KSTGLPHLLA QKGRVLLLEP TRPLAENVCK QLRQAPFQQN PTLRMRGLTT
     FGSSNIVIMT SGFALHYYAN NPTKLQEYDF VMIDESHTMD ASAMAFYCLV REYNFQGKII
     KVSATPPGKE CEFKTQFDVA LLIEEDLSFQ QFAQSQGQGG NADMTKHGDN ILVYVASYND
     VDQLAELLIR GNHFVTKVDG RTMKMGSTEI VSKGTASKKH YIIATNIIEN GVTLDVDVVV
     DFGQKVVAEL DGDSRCMRYR KVAVSYGERI QRLGRVGRVK KGTALRIGHT EHGISEIPAS
     ISTEAAFLCF AYGLPVITHN VTVSILANCT VQQARTMMLF ELSPFFLADL VKYNGSMHPE
     VHKLLKPYKL RDSEIELCKL AIPNSSIGRW LSVHEYAKLG IKIHAVDSVR IPFAGRGIPD
     KLYSELWHII QEHKHEAGFG RLTSASASTI AYTLSTDPEA IPRTIALLDN LIAEEMQKKA
     HFEALNSTLC SQRFTLKNIV DTVRQRYMKD HSKHNIEVLQ SARSQILEFN SATHDFKKVA
     SLLGYGFLDT VQYQSKNELS KRLGLKGRWN KSLVTNDLLV CGMVLFGGVW MVWEYAKSAM
     NEPVRYQGKR QNQKLKFRDA RDRKVGREVY GDDGTIEHFF GEAYTKKGKS KGNHTVKGMG
     RKTRRFIHMY GFDPTEYSFV RFVDPLTGYA IDENITCDIS LVQDEVAEVR KQFINEDEIS
     AQSIAENPGI IAYYMSRNAD KALKIDLTPH NPLAVGRGGS SIAGFPEREY ELRQTGKPLE
     VKKSEVPPVS KDVVATEGKS MCRGLRNYNP IATSICKLVN ESDGHSETIH GIGFGPVIIT
     NSHLFRRNNG TLQIQTHHGV FRVKNSTQLQ VSHMAKKDMI IIKMPCDVPP FPSKLRFRQP
     EQGEKAVLVG SLFQQKSITS SVSESTMVMP VNDSGYWRHW VSTKDGDCGL PLVSTVDGAI
     LGLHGLTSTK SDRNYFVPFD EQFERDILAN LEKLDWKRHW LHSSDLIAWG GMSLKENHPH
     DCFRTSKLVT DLLGLTKDSV EYQSGQDKWV LAGLENNLKA VAQSESQLVT KHVVKGQCMY
     FQEYLATHST AEKFFKPLMG AYQPSKLNKE AFTKDLYKYQ NEIIVGEVDK DAFDNAVEAV
     IYLLDDLGFG ECAYVTDEEA ILDSLNMKAA VGALYKGKKK EYFESLSEPE KHHIVQASCE
     RLFYGEMGVW NGSLKAELRP KEKVALNKTR TFTAAPIDTL LGGKCCVDDF NNRFYSLNIE
     GPWTVGMTKF YGGWDKLMRK LPDGWRYCHA DGSQFDSSLT PFLLNAVLAV RLMFMEDWWV
     GEQMLRNFYT EIIYTPILTP DGTIVKKFKG NNSGQPSTVV DNTLMVMIAM FYGMKKLNWT
     DEQIKERIVF FAXGDDLIIA VQPEHEGILD TLQRSLGELG LKYDFSERCD DRQELWFMSH
     QGHLVDGMYI PKLEQERIVS ILEWDRSTVI EHRAEAICAA MIEAWGYPEL LKQIRLFYAW
     ILDHDMFKSL VAEGKLPYIA ETALRKLYTD ADATDVELEE YILRFTEVDE DEDHNDEVRY
     QSGENKSKVE VDAAAAKLKE KEKEKHKKTE EGTSEGTSQT KEPDVDTGSQ GIVYVPKLAK
     ITKKMRMPMV GGQVILHIPH LLDYKPEQVD LSNTRSSQQQ FTAWYNGLKE AYEITDDTSM
     SVLMNGLMVW CIENGTSPNI NGNWTMMDGH EQNEYPLKPV IENAKPTFRQ IMHHFSDAAE
     AYIEMRNAEK PYMPRYGLQR NLRDFSYARI AFDFYEITSR TSAKAREIHM QMKAAALNNV
     AIKTFGLDGN VGTQDEDTER HTANDVNRNM HSLLGMRQM
//
DBGET integrated database retrieval system