GenomeNet

Database: UniProt
Entry: Q89330
LinkDB: Q89330
Original site: Q89330 
ID   POLG_ZYMVR              Reviewed;        3083 AA.
AC   Q89330;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-DEC-2019, entry version 134.
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   Zucchini yellow mosaic virus (strain Reunion Island) (ZYMV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=117129;
OH   NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH   NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH   NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7844540; DOI=10.1099/0022-1317-76-1-37;
RA   Wisler G.C., Purcifull D.E., Hiebert E.;
RT   "Characterization of the P1 protein and coding region of the zucchini
RT   yellow mosaic virus.";
RL   J. Gen. Virol. 76:37-45(1995).
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 (By similarity). {ECO:0000250}.
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=Q89330-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CK14-1; 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; L29569; AAA65558.1; -; Genomic_RNA.
DR   PRIDE; Q89330; -.
DR   Proteomes; UP000008611; 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; IPR011492; DEAD_Flavivir.
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; PF07652; Flavi_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..3083
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420036"
FT   CHAIN           1..313
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040510"
FT   CHAIN           314..769
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040511"
FT   CHAIN           770..1115
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040512"
FT   CHAIN           1116..1167
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040513"
FT   CHAIN           1168..1801
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040514"
FT   CHAIN           1802..1854
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040515"
FT   CHAIN           1855..2044
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040516"
FT   CHAIN           2045..2287
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040517"
FT   CHAIN           2288..2804
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040518"
FT   CHAIN           2805..3083
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040519"
FT   DOMAIN          173..313
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          647..769
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1239..1391
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1410..1569
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2045..2263
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2529..2653
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1252..1259
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           365..368
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           621..623
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1341..1344
FT                   /note="DECH box"
FT   MOTIF           1894..1903
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        226
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        235
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        267
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        655
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        728
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2090
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2125
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2195
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            313..314
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            769..770
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1115..1116
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1167..1168
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1801..1802
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2044..2045
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2287..2288
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2804..2805
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1918
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   3083 AA;  351161 MW;  55E51B455C20C537 CRC64;
     MAAIMIGSIS VPIVESARCA TVQTGNRVNI VAPGHVAVCK PQMKSHSYYK HASEKLSKQA
     SESINILNSF FDTDPEMRFR LTRNEMSKVK KGPNGRMILR KPRAQRVLER ISFEKIEKGA
     ERQVLPWRVY ATVTSIINTF TDERNGIANS SLRSPFYKRS CRKEKKKIVC ENVVRSASVN
     NLCDRVLKIA REKNIPVEMI GKKKNRHTLT FKNFKGSFIG KVSLAHERGQ MRHVEMSYEQ
     FGFILQAICR VTNTRCVRDE DIKPGCSGWV LGDDHELTQK FSRLPCLVIR GRDDEGIVNA
     LEPVFFYDDV DHYSSQPEVQ FFQGWRRMFD NFKPSSDHVC KVDHGNEECG ELAAIFSQAL
     FPVVKLSCQT CREKLSRVSF EEFKDSLAIN FTVHKSEWDS LKENPHHDNV LKLIKGATQA
     TQNLKLSSEV MKLVQNHTST HMKQIQDINR ALMKGSLVTQ DELDLALKQL LEMTQWFKNH
     MHLTGEEALK TFRNKRSSKA MINPSLLCDN QLDKNGNFVW GERGYHSKRL FKNFFEEVIP
     SEGYTKYIVR NFPNGTRKLA IGSLIVPLNL DRARTALLGE SIEKEPLTSA CVSQQNGNYI
     HSCCCVTMDD GTPMYSDVKS PTKRHLVIGA SGDPKYIDLP ASEADRMYIA KEGYCYLNIF
     LAMLVNVNEN EAKDFTKMIR DVLIPMLGQW PSLMDVATAA YILGVFHPET RCAELPRILV
     DHATQTMHVI DSYGSLTVGY HVLKAGTVNH LIQFASNDLQ SEMKHYRVGG TPTQRIKLEE
     QLIKGIFKPK LMMQLLQDDP YVLILGMVSP TILVHMYRMR HFERGIEMWI KRDHEVGKIF
     VILEQLTRKV ALTEVLVDQL DLISEASPHL LEIMKGCQDN QRAYVPALDL LTVQVEREFS
     NKELKVNGYP DLQQTLYDMR EKIYAKQLHD SWQELSLLEK SCVTVRLKRF SIFTERKLTQ
     QAKDGKRVSS LQFVHECFIT TRVHAKSIRD VGMRKFNEAL VGTCKFLFTC GFKIFARCYS
     DIIYLVNVCL IFSLVLQMSN TVRSMISATR EEKERALANK ADENERTLMH MYHIFSKKQD
     DAPLYSEFLE HVRNVRPDLE ETLLYMAGAE IVTPQAKSAV QVQFEKIIAV VALLTMCFDA
     ERSDAIFKIL TKLKTVFGTV GETVRLQGLE DIENLEDDKK LTIDFDINTN EAQSSTTFDV
     HFDDWWNRQL QQNRTVPHYR TTGKFLEFTR NTAAFVANEI ASSNEGEFLV RGAVGSGKST
     SLPAHLAKKG KVLLLEPTRP LAENVSRQLA GDPFFQNVTL RMRGLSCFGS SNITVMTSGY
     AFHYYVNNPH QMMEFDFIII DECHVTDSAT IAFNCALKEY NFAGKLIKVS ATPPGRECDF
     DTQFAVKVKT EDHLSFQAFV GAQRTGSNAD MIQHGNNILV YVASYNEVDM LSKLLTERQF
     SVTKVDGRTM QLGKTTIETH GTSQKPHFIV ATNIIENGVT LDVDCVVDFG LKVVAELDSE
     SRCVRYSKKP VNYGERIQRL GRVGRSKPGT ALRIGHTEKG IENIPEFIAT EAAALSFAYG
     LSVTTHGVST NILGKCTVKQ MKCALNFELT PFFTTHLIRH DGSMHPLIHE ELKQFKLRDS
     EMVLNKVALP HQFVSQWMTQ GDYEHIGVHI QCNENTRIPF YTNGIPDRVY EKIWKCIQEN
     KNDALFGRLS SACSTKVSYT LSTDPAALPR TIAIIDHLLA EEMMKRNHFD MISSAVTGYS
     FSLAGIADSF RKRYMRDHTA HNIAILQQAR AQLLEFDSKN VNINNLSDLE GIGVIKSVVL
     QSKQEVSNFL GLRGKWDGRK FANDVILAIM TLLGGGWFMW EYFTKKVNEP VRVESKKRRS
     QKLKFRDAYD RKVGREIFGD DETIGRTFGE AYTKRGKVKG NNSTKGMGRK TRNFVHLYGV
     EPENYSFIRF VDPLTGHTLD ESTHTDISLV QEEFGNIREK FLENDLISRQ SIINKPGIQA
     YFMGKGTAEA LKFDFTPHVP SLSCSNSNAH AGYPERENEL RQTGTPVKVS LKDVPEKNEH
     VELESKSIYK GVRDYNGIST IVCQLTNDSD RLKETMYGIG YGPIIITNGH LFRKNNGTIL
     VRSWHGEFTV KNTTTLKVHF IEGKDVVLVR MPKTFPPFKS NASFRAPKRE ERACLVGTNF
     QEKSLRSTVS ESSMTNPRRT GSYWIHWIST NEGDCGLPMV STTDGKLIGL HGKASTVSSK
     NYFVPFTDDF MATHLSKLDD LTWTQHWLWQ PSKIAWGLLN LVDEQPGPEF RISNLVKDLF
     NSGVETQSKR ERWVYESCEG NLRAVGSAQS ALVTKHVVKG KCPFFEEYLQ THAEASAYFR
     PLMGEYQPSK LNKEAFKKDF FKYNKPVIVN QLDHDKFLEA VDGVIRMMCD FEFNECRFIT
     DPEEIYSSLN MKAAIGAQYR GKKKEYFEGL DNFDMERLLF QSCERLFNGY KGLWNGSLKA
     ELRPLEKVQA NKTRTFTAAP IDTLLGAKVC VDDFNNEFYS KNLKCPWTVG MSKFYGGWDK
     LMRALPDGWL YCHADGSQFD SSLTPALLNA VLIIRSFYME DWWVGQEMLE NLYAEIVYTP
     ILAPDGTIFK KFRGNNSGQP STVVDNTLMV VISIYYACIK FGWGYDEIEN RLVFFANGDD
     LILAVKDEDS GLLDNMSASF SELGLNYDFS ERTHKREDLW FMSHQAMLVD GMYIPKLERE
     RIVSILEWDR SKEVMHRTEA ICAAMIEAWG HTELLHEIRK FYLWFVEKEE VRELAALGKA
     PYIAETALRK LYTDKGAETS ELARYLQALH QDVFFEQRDT VMLQSDTQTK EADAGAAKRD
     KDEEKEKKKD VASSSANEKT MTATAKDKDV NAGSHGKIVP RLSKITKKMS LPRVKGSVIL
     DIDHLLEYKP DQIELYNTRA SHQQFASWFN QVKAEYDLNE QQMGVVMNGF MVWCIENGTS
     PDINGVWFMM DGDEQVEYPL KPIVENAKPT LRQIMHHFSD AAEAYIEMRN AEAPYMPRYG
     LLRNLRDRSL ARYAFDFYEV NSKTPDRARE AVAQMKAAAL SNVSSRLFGL DGNVATNSED
     TERHTARDVN RNMHTLLGVN TMQ
//
DBGET integrated database retrieval system