GenomeNet

Database: UniProt
Entry: Q01500
LinkDB: Q01500
Original site: Q01500 
ID   POLG_PEMVC              Reviewed;        3068 AA.
AC   Q01500;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   11-DEC-2019, entry version 145.
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   Pepper mottle virus (isolate California) (PeMV) (PepMoV C).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=31737;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=4075; Datura inoxia (Downy thornapple) (Datura meteloides).
OH   NCBI_TaxID=4107; Solanum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1413501; DOI=10.1016/0042-6822(92)90162-i;
RA   Vance V.B., Moore D., Turpen T.H., Bracker A., Hollowell V.C.;
RT   "The complete nucleotide sequence of pepper mottle virus genomic RNA:
RT   comparison of the encoded polyprotein with those of other sequenced
RT   potyviruses.";
RL   Virology 191:19-30(1992).
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=Q01500-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CK01-1; 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; M96425; AAA46903.1; -; Genomic_RNA.
DR   PIR; A44062; A44062.
DR   RefSeq; NP_041276.1; NC_001517.1.
DR   MEROPS; C04.002; -.
DR   PRIDE; Q01500; -.
DR   GeneID; 1494047; -.
DR   KEGG; vg:1494047; -.
DR   Proteomes; UP000008157; 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..3068
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420003"
FT   CHAIN           1..287
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040295"
FT   CHAIN           288..743
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040296"
FT   CHAIN           744..1104
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040297"
FT   CHAIN           1105..1156
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040298"
FT   CHAIN           1157..1790
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040299"
FT   CHAIN           1791..1842
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040300"
FT   CHAIN           1843..2030
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040301"
FT   CHAIN           2031..2276
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040302"
FT   CHAIN           2277..2795
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040303"
FT   CHAIN           2796..3068
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040304"
FT   DOMAIN          144..287
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          621..743
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1228..1380
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1399..1558
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2031..2249
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2518..2642
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1241..1248
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           337..340
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           595..597
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1330..1333
FT                   /note="DECH box"
FT   MOTIF           1884..1891
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        195
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        204
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        238
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        629
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        702
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2076
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2111
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2181
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            287..288
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            743..744
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1104..1105
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1156..1157
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1790..1791
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1842..1843
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2030..2031
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2276..2277
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2795..2796
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1906
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   3068 AA;  348656 MW;  FD3458B837FDA7C2 CRC64;
     MATSVIQFGS FVCNLPKSQP LCTTVHCPKQ SMSTNIVRPS DPFAELEKHL EPYLQKRMDA
     TIRQTKGGTL VYKHMSEAKR ARKLRKKQRE EEEVRLFMNA APYIVSNITI GGGEVPSKME
     EVSIKRPLNK TPSRKIKKSL TPVTFRDGHM NKFLRELRDC ATRNSMTVHL IGKRKTELAF
     KRRASLNAVY ATLHHMRGVD RKRDIVLEEW MNDYVLNLSK VSTWGSLFHA ESLKRGDSGL
     ILNARALRGK FGRCSRGFFI VRGKSDGVVL DARSKLSMAT VTHMEQYSTP EAFWSGLEKK
     WSVVRKPTAH TCKPTYSVSN CGEVAAIIAQ ALFPCHKLTC GECSKEICDL TSNECVQELY
     KNTSLALERM NNLHPEFQHI VKVLSVVRQL TEASNHGTET FDEIFKMIGS KTQSPFTHLN
     KLNEFMLKGN ENTSGEWLTA RQHLRELVRF QKNRTDNIKK GDLASFRNKL SARAQYNLYL
     SCDNQLDKNA SFLWGQREYH ARRFFLNFFQ QIDPSKGYLA YEDRTIPNGS RKLAIGNLIV
     PLDLAEFRKR MNGIDTQQPP IGKYCTSQLD GNFVYPCCCT TLDDGQPIRS AVYAPTKKHL
     VVGNTGDTKY INLPKGDTEM LYIALDGYCY INIYLAMLVN ISEEEAKDFT KKVRDIFMPK
     LGKWPTLMDL ATTCAQLRIF HPDVHDAELP RILVDHNTQT CHVVDSYGSI STGYHILKAA
     TVSQLVLFAD DNLESEIKHY RVGGIVENHK VQIDNQPSRC GVSEFHAIRM LIKGIYRPSV
     MYELLSEEPY LLVFSILSPS ILIAMYNDRA FELAVQIWLE KEQSIPLIAT ILTNLAAKVS
     VATTLVQQLQ LIELSADQLL NVTCDGFRVS FAYQSALTLL TRMRDQAKAN SELISGGFNE
     YDQDLAWTLE KNYQGLLHDQ WKELSSLEKF RYYWSSRKRK TRLRSNIKSR SSPVASAISS
     LSLKPFMGKV FSHMKAGAVC TKQGTKNFID ARCLGISTYF VGSLMRKFPS AKVLLSSLFV
     LGALLNITHA ANRIIIDNRI SREHAAALEL YRKEDTCHEL YTALERKLGE KPTWDEYCSY
     VAKINPAMLE FIKDSYDEKQ VVHQRSTEDL KKVEHIIAFV TLAIMLFDSE RSDCVFKTLN
     KFKGVVCSLG SGVRHQSLDD FVSTMDEKNF VVDFELNDSV QRKNLTTEIT FESWWDEQVA
     RGFTIPHYRT EGRFMEFTRA TAAKVASDIS ISSERDFLIR GAVGSGKSTG LPHHLSTYGR
     VLLIEPTRPL AENVFKQLSG GPFFLKPTMR MRGNSVFGSS PISVMTSGFA LHFFANNITQ
     LQEIQFIIID ECHVMDASSM AFRSLIHTYH TNCKVLKVSA TPPGREVEFT TQFPVKLVVE
     DSLSFKTFVE SQGTGSNCDM IQYGNNLLVY VASYNEVDQL SKLLVAREFN VTKVDGRTMK
     HGELEIVTRG TKSKPHFVVA TNIIENGVTL DIDVVIDFGM KVSPFLDVDN RSVAYNKVSI
     SYGERIQRLG RVGRIQKGTA LRIGHTEKGL IEIPQMISTE AALYCFAYNL PVMSSGVSTS
     MIKNCTIPQV RTMHTFELSP FFMYNFVSHD GTMHPVVHET LKRYKLRDSV IPLSESSIPY
     RASSDWITAG DYRRIGVKLD IPDETRIAFH IKTFHRKFTN NLWESVLKYK ASAAFPTLRS
     SSITKIAYTL STDLYAIPRT LAVVESLLED ERTKQYQFKS LIDNGCSSMF SVVGISNALR
     AKYSKDHTVE NINKLETVKA QLKEFHNLNG SGDELNLIKR FESLQFVHHQ SKSSLAKALG
     LRGVWNKSLI VRDAIIAAGV ACGGAWLLYT WFTAKMSEVS HQGRSKTKRI QALKFRKARD
     KRAGFEIDNN EDTIEEYFGS AYTKKGKGKG TTVGMGRTNR RFINMYGFEP GQFSYIKFVD
     PLTGAQMEEN VYADIVDVQE KFGDIRRQMI LDDELDRRQT DVHNTIHAYL IKDWSNKALK
     VDLTPHNPLR VSDKASAIMK FPEREGELRQ TGQAVEVDVC DIPKEVVKHE AKTLMRGLRD
     YNPIAQTVCK LTVKSELGET STYGLGFGGL IIANHHLFKS FNGSLEVKSH HGVFRVPNLM
     AISVLPLKGR DMIIIKMPKD FPVFPQRLKF REPASTDRVC LIGSNFQERY ISTTVSEISA
     THPVPRSTFW KHWISTDDGH CGLPIVSTTD GFILGLHSLA NNRNSENYYT AFDSDFEMKI
     LRSGENTEWV KNWKYNPDTV LWGPLQLTKG TPSGMFKTTK MIEDLLAFKS ESVREQAHTS
     SWMLEVLKEN LKAIAYMKSQ LVTKHVVKGE CMMFKQYLQE NPRANEFFQP KMWAYGKSML
     NKEAYIKDIM KYSKVIDVGV VDCDRHLRKL SLELLYTQIH GFRKCSYITD EEEIFKALNI
     TTAVGAMYGG KKKEYFEKFT TEDKAEILRQ SCLRLYTGKL GVWEWALKAE LRSKEKIEAN
     KTRTFTAAPI DTLLGGKVCV DDLNNQFYSK NIECCWTVGM TKFYGGWDKL LTALPAGWIY
     CDADGSQFDS SLTPYLINAV LTIRYAFMED WDIGYKMLQN LYTEIIYTPI STPDGTIVKK
     FRGNNSGQPS TVVDNSLMVV LAMHYAFVRE GIAFEEIDSI CKFFVNGDDL LIAVNPERES
     LLDTLSNHFS DLGLNYDFSS RTRNKSELWF MSHCGISVEG TYIPKLEEER IVSILQWDRA
     ELPEYRLEAI CAAMIESWGY PQLTHEIRRF YSWLIEKNPY ADLASEGKAP YISELALKKL
     YLNQDVQMMS FRSYLKYFAD ADEEFECGTY EVRHQSSSRS DTLDAGEEKK KNKEVATVSD
     GMGKKEVEST RDSDVNAGTV GTFTIPRIKS ITEKMRMPKQ KRKGVLNLAH LLEYKPSQVD
     ISNTRSTQAQ FDNWYCEVMK AYDLQEEAMG TVMNGLMVWC IENGTSPNIS GTWTMMDGDE
     QVEFPLKPVI ENAKPTFRQI MAHFSDVAEA YIEMRNKQEP YMPRYGLVRN LRDMGLARYA
     FDFYEVTSRT STRAREAHIQ MKAAALKSAQ TRLFGLDGGI GTQGENTERH TTEDVSPDMH
     TLLGVREM
//
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