GenomeNet

Database: UniProt
Entry: P17766
LinkDB: P17766
Original site: P17766 
ID   POLG_PPVNA              Reviewed;        3125 AA.
AC   P17766;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   11-DEC-2019, entry version 153.
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   Plum pox potyvirus (isolate NAT) (PPV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12213;
OH   NCBI_TaxID=36596; Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OH   NCBI_TaxID=36595; Prunus cerasifera (cherry plum).
OH   NCBI_TaxID=3758; Prunus domestica (Garden plum).
OH   NCBI_TaxID=105665; Prunus glandulosa.
OH   NCBI_TaxID=3760; Prunus persica (Peach) (Amygdalus persica).
OH   NCBI_TaxID=88123; Prunus salicina.
OH   NCBI_TaxID=114937; Prunus spinosa (Blackthorn) (Prunus domestica var. spinosa).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2732699; DOI=10.1099/0022-1317-70-3-513;
RA   Maiss E., Timpe U., Brisske A., Jelkmann W., Casper R., Himmler G.,
RA   Mattanovich D., Katinger H.W.D.;
RT   "The complete nucleotide sequence of plum pox virus RNA.";
RL   J. Gen. Virol. 70:513-524(1989).
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: [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=P17766-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CK02-1; 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; D13751; BAA02898.1; -; Genomic_RNA.
DR   PIR; JQ0003; GNVSPP.
DR   RefSeq; NP_040807.1; NC_001445.1.
DR   PRIDE; P17766; -.
DR   GeneID; 1494049; -.
DR   KEGG; vg:1494049; -.
DR   BRENDA; 3.4.22.45; 4919.
DR   Proteomes; UP000006685; 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..3125
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420007"
FT   CHAIN           1..308
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040331"
FT   CHAIN           309..766
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040332"
FT   CHAIN           767..1116
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040333"
FT   CHAIN           1117..1168
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040334"
FT   CHAIN           1169..1803
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040335"
FT   CHAIN           1804..1856
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040336"
FT   CHAIN           1857..2049
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040337"
FT   CHAIN           2050..2292
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040338"
FT   CHAIN           2293..2810
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040339"
FT   CHAIN           2811..3125
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040340"
FT   DOMAIN          165..308
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          644..766
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1240..1392
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1411..1570
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2050..2268
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2534..2658
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1253..1260
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           360..363
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           618..620
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1342..1345
FT                   /note="DECH box"
FT   MOTIF           1897..1904
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        216
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        225
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        259
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        652
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        725
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2095
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2130
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2200
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            308..309
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            766..767
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1116..1117
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1168..1169
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1803..1804
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1856..1857
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2049..2050
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2292..2293
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2810..2811
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1919
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   3125 AA;  354266 MW;  ED0DD33C439CB712 CRC64;
     MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNA HLLCRRAAES LINTYESATA
     SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLRKQYQE ERERLQFLNG
     PDAIVNQISV DKCEASVRVP SPHIIEKPSF VTPSMKKKVV FKKVRMSEAS LQLFMRRVAA
     NAKANGQKVE IIGRKRVVGN YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
     NTSGFHHVHK KGEVTPGMSG FVVNPMNLSD PMQVYDTDLF IVRGKHNSIL VDSRCKVSKK
     QSNEIIHYSD PGKQFSDGFT NSFMQCKLRE TDHQCTSDLD VKECGYVAAL VCQAIIPCGK
     ITCLQCAQKY SYMSQQEIRD RFSTVIEQHE KTVMDNYPQF SHVLAFLKRY RELMRVENQN
     YEAFKDITHM IGERKEAPFS HLNKINELII KGGMMSAQDY IEASDHLREL ARYQKNRTEN
     IRSGSIKAFR NKISSKAHVN MQLMCDNQLD TNGNFVWGQR EYHAKRFFRN YFDVIDVSEG
     YRRHIVRENP RGIRKLAIGN LVMSTNLAAL RKQLLGEECI HFEVSKECTS KRGENFVYQC
     CCVTHEDGTP LESEIISPTK NHLVVGNSGD SKYVDLPTAK GGAMFIAKAG YCYINIFLAM
     LININEDEAK SFTKTVRDTL VPKLGTWPSM MDLATACHFL AVLYPETRNA ELPRILVDHE
     AKIFHVVDSF GSLSTGMHVL KANTINQLIS FASDTLDSNM KTYLVGGLEV DKCDEFKNVK
     LLIRSIYKPQ IMEQVLKEEP YLLLMSVLSP GVLMALFNSG SLEKATQYWI TRSHSLAAIT
     SMLSALAAKV SLASTLNAQM SVIDEHAAVL YDSVFVGTQP YASYMMAVKT LERMKARTES
     DHTLNDLGFS VLRQATPHLV EKSYLQELEQ AWKELSWSEK FSAILESQRW RKHIPKPFIP
     KDGADLGGRY DISVRSLLGN QYKRLRDVVR WKRDDVVCYT YQSMGKLFCK AIGISPSFLP
     STLKMLDMLI VFSLLLSIGA TCNSMVNEHK HLKQLAADRE DKKRFKRLQV LYTRLSEKVG
     CTPTADEFLE YVGDENPDLL KHAEDLIGDG QVVVHQSKRD SQANLERVVA FVALVMMLFD
     SERSDGVYKI LNKLKGIMGS VDRAVHHQSL DDIEDILDEK KLTVDFVLQS NEVAPTVPFD
     STFEKWWMNQ LETGNVIPHY RTEGHFLEFT RENAAHIANE VMHGSHQDIL IRGAVGSGKS
     TGLPFHLSKK GHVLLIEPTR PLAENVCKQL RGQPFNVNPT LRMRGMSTFG STPITVMTSG
     YALHFLANNP TYLDNYKCII FDECHVHDAS AMAFRCLLSE YSYPGKILKV SATPPGHEVE
     FKTQKEVKVI VEESLSFQQF VSNLGTGCNS DILKHGVNVL VYVASYNEVD TLSKLLTDRS
     FKVSKVDGRT MKVGNVEIPT SGTQAKPHFV VATNIIENGV TLDIDVVVDF GLKVVPVLDI
     DNRLVRYTKK SISYGERIQR LGRVGRNKPG AALRIGFTEK GLTQIPPIIA TEAAFLCFTY
     GLPVMTNGVS TSLLAMCTVK QARTMQQFEL SPFYTVALVR FDGTMHQEIF RLLKSYRLRD
     SEVILNKLAI PNSNVCGWMS VRDYKRQGCN LDLDENIRVP FYVKDIPETL HERIWQAVET
     HKSDAGFGRI CSSSACKIAY TLQTDIHSIP RTIKIIDALL EQERTKQAHF RAMTSQSCSS
     SNFSLSSITS AIRSKYAKDH TEENIGVLQM AKSQLLEFKN LNIDPSYPEL IRNFGALECV
     HHQTKEGVSK ALQLKGHWNK RLITRDATLM LGVLGGGAWM IFSYLRDSFK EEVIHQGFNR
     RQRQKLKFRQ ARDNRMAREV YGDDSTMEAY FGSAYSKKGK SKGKTRGMGT KTRKFVNMYG
     YDPTDYNFVR FVDPLTGHTL DESPLMDINL VQEHFSQIRN DYIGDDKITM QHIMSNPGIV
     AYYIKDATQK ALKVDLTPHN PLRVCDKTAT IAGFPEREFE LRQTGHPVFV EPNAIPKINE
     EGDEEVDHES KSLFRGLRDY NPIASSICQL NNSSGARQSE MFGLGFGGLI VTNQHLFKRN
     DGELTIRSHH GEFVVKDTKT LKLLPCKGRD IVIIRLPKDF PPFPRRLQFR TPTTEDRVCL
     IGSNFQTKSI SSTMSETSAT YPVDNSHFWK HWISTKDGHC GLPIVSTRDG SILGLHSLAN
     STNTQNFYAA FPDNFETTYL SNQDNDNWIK QWRYNPDEVC WGSLQLKRDI PQSPFTICKL
     LTDLDGEFVY TQSKTTHWLR DRLEGNLKAV GACPGQLVTK HVVKGKCTLF ETYLLTHPEE
     HEFFRPLMGA YQKSALNKDA YVKDLMKYSK PIVVGAVDCD QFERAVDVVI SMLISKGFEE
     CNYVTDPDDI FSALNMKAAV GALYSGKKRD YFENVSDQDK ESFVRASCKR LFMGKKGVWN
     GSLKAELRPK EKVEANKTRS FTAAPIDTLL GGKVCVDDFN NQFYSLNLHC PWSVGMTKFR
     GGWDKLLKAL PEGWIYCDAD GSQFDSSLSP YLINAVLNIR LAFMEEWDIG EQMLSNLYTE
     IVYTPIATPD GTIVKKFKGN NSGQPSTVVD NTLMVILAMT YSLLKLGHHP DTHDCICRYF
     VNGDDLVLAV HPAYESIYDE LQEHFSQLGL NYTFTTKTEN KEELWFMSHK GVLYDDMYIP
     KLEPERIVSI LEWDRSNEPI HRLEAICASM VEAWGYKELL REIRKFYSWV LEQAPYNALS
     KDGKAPYIAE TALKKLYTDT EASETEIERY LEAFYDNIND DGESNVVVHQ ADEREDEEEV
     DALQPPPVIQ PAPRTTAPML NPIFTPATTQ PATKPVSQVS GPQLQTFGTY SHEDASPSNS
     NALVNTNRDR DVDAGSTGTF TVPRLKAMTS KLSLPKVKGK AIMNLNHLAH YSPAQVDLSN
     TRAPQSCFQT WYEGVKRDYD VTDDEMSIIL NGLMVWCIEN GTSPNINGMW VMMDGETQVE
     YPIKPLLDHA KPTFRQIMAH FSNVAEAYIE KRNYEKAYMP RYGIQRNLTD YSLARYAFDF
     YEMTSTTPVR AREAHIQMKA AALRNVQNRL FGLDGNVGTQ EEDTERHTAG DVNRNMHNLL
     GMRGV
//
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