GenomeNet

Database: UniProt
Entry: Q02597
LinkDB: Q02597
Original site: Q02597 
ID   POLG_TUMVQ              Reviewed;        3163 AA.
AC   Q02597;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   18-SEP-2019, entry version 148.
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   Turnip mosaic virus (strain Quebec) (TuMV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=36396;
OH   NCBI_TaxID=126269; Alliaria.
OH   NCBI_TaxID=3705; Brassica.
OH   NCBI_TaxID=38206; Calanthe.
OH   NCBI_TaxID=3719; Capsella bursa-pastoris (Shepherd's purse) (Thlaspi bursa-pastoris).
OH   NCBI_TaxID=264418; Hesperis matronalis.
OH   NCBI_TaxID=13274; Stellaria media (Common chickweed) (Alsine media).
OH   NCBI_TaxID=74517; Trifolium hybridum (Alsike clover).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1431807; DOI=10.1099/0022-1317-73-11-2785;
RA   Nicolas O., Laliberte J.F.;
RT   "The complete nucleotide sequence of turnip mosaic potyvirus RNA.";
RL   J. Gen. Virol. 73:2785-2793(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1534-3163, AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   PubMed=2254757; DOI=10.1099/0022-1317-71-11-2769;
RA   Tremblay M.F., Nicolas O., Sinha R., Lazure C., Laliberte J.F.;
RT   "Sequence of the 3'-terminal region of turnip mosaic virus RNA and the
RT   capsid protein gene.";
RL   J. Gen. Virol. 71:2769-2772(1990).
RN   [3]
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
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. {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
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=Q02597-1; Sequence=Displayed;
CC         Note=Produced by conventional translation.;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CK12-1; 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 (By
CC       similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; D10927; BAA01725.1; -; Genomic_RNA.
DR   EMBL; D10601; BAA01452.1; -; Genomic_RNA.
DR   PIR; JQ1895; JQ1895.
DR   MEROPS; C06.001; -.
DR   PRIDE; Q02597; -.
DR   Proteomes; UP000008263; 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; Direct protein sequencing;
KW   Helical capsid protein; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease;
KW   Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW   Suppressor of RNA silencing; Thiol protease; Transferase;
KW   Viral RNA replication; Virion.
FT   CHAIN         1   3163       Genome polyprotein.
FT                                /FTId=PRO_0000420030.
FT   CHAIN         1    362       P1 proteinase. {ECO:0000255}.
FT                                /FTId=PRO_0000040473.
FT   CHAIN       363    820       Helper component proteinase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000040474.
FT   CHAIN       821   1175       Protein P3. {ECO:0000250}.
FT                                /FTId=PRO_0000040475.
FT   CHAIN      1176   1227       6 kDa protein 1. {ECO:0000250}.
FT                                /FTId=PRO_0000040476.
FT   CHAIN      1228   1870       Cytoplasmic inclusion protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040477.
FT   CHAIN      1871   1923       6 kDa protein 2. {ECO:0000250}.
FT                                /FTId=PRO_0000040478.
FT   CHAIN      1924   2115       Viral genome-linked protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040479.
FT   CHAIN      2116   2358       Nuclear inclusion protein A.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040480.
FT   CHAIN      2359   2875       Nuclear inclusion protein B.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040481.
FT   CHAIN      2876   3163       Capsid protein. {ECO:0000250}.
FT                                /FTId=PRO_0000040482.
FT   DOMAIN      219    362       Peptidase S30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01219}.
FT   DOMAIN      698    820       Peptidase C6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01080}.
FT   DOMAIN     1300   1452       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1471   1630       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2116   2334       Peptidase C4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00766}.
FT   DOMAIN     2600   2724       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1313   1320       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       414    417       Involved in interaction with stylet and
FT                                aphid transmission. {ECO:0000250}.
FT   MOTIF       672    674       Involved in virions binding and aphid
FT                                transmission. {ECO:0000250}.
FT   MOTIF      1402   1405       DECH box.
FT   MOTIF      1964   1971       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   ACT_SITE    270    270       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    279    279       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    313    313       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    706    706       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE    779    779       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE   2161   2161       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2196   2196       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2266   2266       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   SITE        362    363       Cleavage; by P1 proteinase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   SITE        820    821       Cleavage; by autolysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   SITE       1175   1176       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1227   1228       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1870   1871       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2115   2116       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2358   2359       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2875   2876       Cleavage; by NIa-pro. {ECO:0000250}.
FT   MOD_RES    1986   1986       O-(5'-phospho-RNA)-tyrosine.
FT                                {ECO:0000250}.
FT   CONFLICT   2862   2862       E -> G (in Ref. 2; BAA01452).
FT                                {ECO:0000305}.
SQ   SEQUENCE   3163 AA;  357822 MW;  61B0F73B58DF6D59 CRC64;
     MAAVTFASAI TNAITNKTTS TGMVQFGSFP PMPLRSTTVT TVATPVGQPK LYTVRFGSLD
     PVIVKGGAGS LAKATRQQPS VEIDVSLSEA AALEVAKPKS SAVLRMHEEA NKERALFLDW
     EASLKRRSYG IAENEKVVMT TRGVSKIVPR SSRAMKQKRA RERRRAQQPI ILKWEPKLSG
     FSIGGGFSAS AIEAEEVRTK WPLHKTPSMK KRMVHKTCKM SDQGVDMLIR SLVKIFKAKS
     ANIEYIGKKP IKVDFIRKER TKFARIQVAH LLGKRAQRDL LAGMEENHFI DILSEYSGNG
     TTINPGVVCA GWSGIVVRNE TLTQKRSRSP SKAFVIRGEH EDKLYDARIK ITKTMSLKIV
     HFSARGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC
     VIDSELSQGQ ASGPSMKHRL TQLRDVIKSS YPRFKHAVQI LDRYEQSLSS ANENYQDFAE
     IQSISDGVEK AAFPHVNKLN AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL
     KSFRNKVSQK AHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
     RVVPNGSRKL AIGKLIVPTN FEVLREQMRG EPVEPYPVTV ECVSKSQGDF VHACCCVTTE
     SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
     SQAKEFTKVV RDKLVSELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
     VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWENAHGA DNIDNPQWCI
     KRLVKGVYRP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEHLMNHY ISADSNVAVL
     LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LIEAKANING PDDAATRACN RFMGMLLHMA
     EPNYELANGG YTFLRDHSIS ILEKSYLQIL DEAWNELSWS ERCVIRYYPS KQAIFTQKDL
     PMQSEADLGG RYSESVISSY EWSKQQAKGV KDSVVNKLRS SMSWTSSKVS NSVCRTINYL
     VPDVFKFMNV LVCISLLIKM TAEANHIITT QRRLKLDIEE TERKKIEWEL AFHHNILTHS
     ASQHPTLDEF TAYIAEKAPH LSEHIEPEEK EVVHQAKRQS EQELERVIAF VALVLMMFDA
     ERSDCVTKIL NKLKGLVATV EPTVYHQTLN EIEDDLNERN LFVDFELSSD SEMLQQLPAE
     KTFASWWSHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK IAHESDKDIL LMGAVGSGKS
     TGLPYHLSRK GNVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTAFG SAPISVMTSG
     FALNYFANNR SRIEEFDFVI FDECHVHDAN AMAMRCLIHE CDYSGKIIKV SATPPGREVE
     FSTQYPVSIS TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLIERD
     FKVTKVDGRT MKVGNIEITT SGTPSRKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT
     DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTER GLSEVPSCIA TEAALKCFTY
     GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD
     SEIVLTKLAI PNRGVNAGSQ PVSMHDSVQM LKIGVTLRIP FMCRDIPEKL HLDMWDVVVK
     FKGDAGFGRL SSSASKVAYT LQTDVNSIQR TVTIIDTLIA EERRKQEYFK TVTSNCVSSS
     NFSLQSITNA IKSRMMKDHP CENISVLEGA KSQLLEFRNL NSDHSFVTKT DGISRSFMRD
     YGALEAVNHQ STNEMSKFLQ LKGKWNKTLI TRDVLVICGV LGGGVWMVVQ HFRSKVSEPV
     THEAKGKKQR QKLKFRNARD NKMGREVYGD DDTIEHFFGD AYTKKGKSKG RTRGIGHKNR
     KFINMYGFDP EDFSAVRFVD PLTGATLDDN PFTDITLVQK HFGDIRMDLL GEDELDSNEI
     RMNKTIQAYY MNNKTGKALK VDLTPHIPLK VCDLHATIAG FPERENELRQ TGKAQPINID
     EVPRANNELV PVDHESNSMF RGLRDYNPIS NNICHLTNVS DGASNSLYGV GFGPLILTNR
     HLFERNNGEL IIKSRHGEFV IKNTTQLHLL PIPDRDLLLI RLPKDVPPFP QKLGFRQPEK
     GERICMVGSN FQTKSITSIV SETSTIMPVE NSQFWKHWIS TKDGQCGSPM VSTKDGKILG
     LHSLANFQNS INYFAAFPDD FTEKYLHTIE AHEWVKHWKY NTSAISWGSL NIQASQPVSL
     FKVSKLISDL DSTAVYAQTQ QNRWMFEQLT GNLKAIAHCP SQLVTKHTVK GKCQMFDLYL
     KLHDEAREYF QPMLGQYQKS KLNREAYAKD LLKYATPIEA GNIDCDLFEK TVEIVISDLR
     GYGFETCNYV TDENDIFEAL NMKSAVGALY KGKKKDYFAE FTPEVKEEIL KQSCERLFLG
     KMGVWNGSLK AELRPLEKVE ANKTRTFTAA PLDTLLGGKV CVDDFNNQFY DHNLRAPWDV
     GMTKFYCGWD RLLESLPDGW VYCDADGSQF DSSLSPYLIN AVLNIRLGFM EEWDVGEVML
     RNLYTEIVYT PISTPDGTLV KKFKGNNSGQ PSTVVDNTLM VILAVNYSLK KGGIPSELRD
     SIIRFFVNGD DLLLSVHPEY EYILDTMADN FRELGLKYTF DSRTREKGDL WFMSHQGHRR
     EGIWIPKLEP ERIVSILEWD RSKEPCHRLE AICAAMIESW GYDKLTHEIR KFYAWMIEQA
     PFSSLAQEGK APYIAETALR KLYLDKEPAQ EDLTQYLQAI FEDYEDGVEA CVYHQAGETL
     DADLTEEQKQ AEKEKKEREK AEKERERQKQ LAFKKGKDVA QEEGKRDKEV NAGTSGTFSV
     PRLKSLTSKM RVPRYEKRVA LNLDHLILYT PEQTDLSNTR STRKQFDTWF EGVMADYELT
     EDKMQIILNG LRVWCIENGT SPNINGMWVM MDGDDQVEFP IKPLIDHAKP TFRQIMAHFS
     DVAEAYIEKR NQDRPYMPRY GLQRNLTDMS LARYAFDFYE MTSRTPIRAR EAHIQMKAAA
     LRGANNNLFG LDGNVGTTVE NTERHTTEDV NRNMHNLLGV QGL
//
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