GenomeNet

Database: UniProt
Entry: Q01901
LinkDB: Q01901
Original site: Q01901 
ID   POLG_PRSVH              Reviewed;        3344 AA.
AC   Q01901;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   11-DEC-2019, entry version 144.
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   Papaya ringspot virus (strain P / mutant HA).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=31731;
OH   NCBI_TaxID=3649; Carica papaya (Papaya).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   AGRICOLA=IND20450567;
RA   Wang C.H., Bau H.J., Yeh S.D.;
RT   "Comparison of the nuclear inclusion b protein and coat protein genes of
RT   five papaya ringspot virus strains distinct in geographic origin and
RT   pathogenicity.";
RL   Phytopathology 84:1205-1210(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1402799; DOI=10.1099/0022-1317-73-10-2531;
RA   Yeh S.D., Jan F.J., Chiang C.H., Doong T.J., Chen M.C., Chung P.H.,
RA   Bau H.J.;
RT   "Complete nucleotide sequence and genetic organization of papaya ringspot
RT   virus RNA.";
RL   J. Gen. Virol. 73:2531-2541(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2561-3344.
RX   PubMed=1456896; DOI=10.1007/bf01309597;
RA   Wang C.H., Yeh S.D.;
RT   "Nucleotide sequence comparison of the 3'-terminal regions of severe, mild,
RT   and non-papaya infecting strains of papaya ringspot virus.";
RL   Arch. Virol. 127:345-354(1992).
RN   [4]
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=Q01901-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ98-1; 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; X67673; CAA47905.1; -; Genomic_RNA.
DR   EMBL; S46722; AAB23789.1; -; Genomic_RNA.
DR   EMBL; X67672; CAA47904.1; -; Genomic_RNA.
DR   PIR; JQ1899; JQ1899.
DR   RefSeq; NP_056758.1; NC_001785.1.
DR   MEROPS; C04.009; -.
DR   PRIDE; Q01901; -.
DR   GeneID; 1494043; -.
DR   KEGG; vg:1494043; -.
DR   Proteomes; UP000006688; Genome.
DR   Proteomes; UP000007380; 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; IPR022199; DUF3725.
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; PF12523; DUF3725; 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..3344
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420010"
FT   CHAIN           1..547
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040361"
FT   CHAIN           548..1004
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040362"
FT   CHAIN           1005..1349
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040363"
FT   CHAIN           1350..1401
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040364"
FT   CHAIN           1402..2036
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040365"
FT   CHAIN           2037..2093
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040366"
FT   CHAIN           2094..2282
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040367"
FT   CHAIN           2283..2520
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040368"
FT   CHAIN           2521..3057
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040369"
FT   CHAIN           3058..3344
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040370"
FT   DOMAIN          408..547
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          882..1004
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1473..1625
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1644..1803
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2283..2499
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2761..2885
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1486..1493
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           598..601
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           856..858
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1575..1578
FT                   /note="DECH box"
FT   MOTIF           2134..2141
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        456
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        465
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        499
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        890
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        963
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2327
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2362
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2431
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            547..548
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            1004..1005
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1349..1350
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1401..1402
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2036..2037
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2093..2094
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2282..2283
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2520..2521
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            3057..3058
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2156
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   3344 AA;  381046 MW;  E90CD7523AC5243D CRC64;
     MSSLYTLRAA AQYDRRLESK KGSGWVEHKL ERKGERGNTH YCSEFDISKG AKILQLVQIG
     NTEVGRTFLE GNRFVRANIF EIIRKTMVGR LGYDFESELW VCRNCDKTSE KYFKKCDCGE
     TYYYSERNLM RTMNDLMYQF DMTPSEINSV DLEYLANAVD YAEQLVKRSQ VPEPVELAMM
     EPIVASGEGI LMVSEPEVMP VTTKVEEAWT IQIGEIPVPL VVIKETPVIS GVEGTLNSTG
     FSLEADITKL VEKEILQEEV KEAVHLALEV GNEIAEKKPE LKLIPYWSAS LELHKRIRKH
     KEHAKIAAIQ VQKEREKDQK VFSALELRLN LKSRRRNQAV VCDKRGTLKW ETQRGHKKSK
     LMQQASDFVV TQIHCDFGCK TQYSEPHIPG IKQSTSKKIC KPRKHSRIVG NSKINYIMKN
     LCDTIIERGI PVELVTKRCK RRILQKEGRS YVQLRHMNGI RARQDVSSSP DMELLFTQFC
     KFLVGHKPLK SKNLTFGSSG LIFKPKFADN VGRYFGDYFV VRGRLGGKLF DGRSKLARSV
     YAKMDQYNDV AEKFWLGFNR AFLRHRKPTD HTCTSDMDVT MCGEVAALAT IILFPCHKIT
     CNTCMSKVKG RVIDEVGEDL NCELERLRET LSAYGGSFGH VSTLLDQLNR VLNARNMNDG
     AFKEIAKKID EKKESPWTHM TTINNTLYKG SLATGYEFER ASNSLREIVR WHLKRTESIK
     AGSVESFRNK RSGKAHFNPA LTCDNQLDKN GNFLWGERQY HAKRFFANYF EKIDHSKGYE
     YYSQRQNPNG IRKIAIGNLV FSTNLERFRQ QMVEHHIDQG PITRECIALR NNNYVHVCSC
     VTLDDGTPAT SELKTPTKNH IVLGNSGDPK YVDLPTLESD SMYIAKKGYC YMNIFLAMLI
     NIPENEAKDF TKRVRDLVGS KLGEWPTMLD VATCANQLVV FHPDAANAEL PQILVDHRQK
     TMHVIDSFGS VDSGYHILKA NTVNQLIQFA RDPLDSEMKH YIVGGEFDPT TNCLHQLIRV
     IYKPHELRSL LRNEPYLIVI ALMSPSVLLT LFNSGAVEHA LNYWIKRDQD VVEVIVLVEQ
     LCRKVTLART ILEQFNEIRQ NARDLHELMD RNNKPWISYD RSLELLSVYA NSQLTDEGLL
     KQGFSTLDPR LREAVEKTYA TLLQEEWRAL SLFQKLHLRY FAFKSQPSFS EYLKPKGRAD
     LKIVYDFSPK YCVHEVGKAF LLPVKAGAKI ASRIINGCGA FIRKSAAKGC AYIFKDLFQF
     VHVVLVLSIL LQIFRSAQGI ATEHLQLKQA KAEVERQKDF DRLEALYAEL CVKSGEQPTT
     EEFLDFVMER EPRLKDQAYN LIYIPVIHQA KSDNEKKLEQ VIAFITLILM MIDVDKSDCV
     YRILNKFKGV INSSNTNVYH QSLDDIRDFY EDKQLTIDFD ITGENQINRG PIDVTFEKWW
     DNQLSNNNTI GHYRIGGTFV EFSRVNAATV ASEIAHSPER EFLVRGAVGS GKSTNLPFLL
     SKHGSVLLIE PTRPLCENVC KQLRGEPFHC NPTIRMRGLT AFGSTNITIM TSGFALHYYA
     HNIQQLRLFD FIIFDECHVI DSQAMAFYCL MEGNAIEKKI LKVSATPPGR EVEFSTQFPT
     KIVTEQSISF KQLVDNFGTG ANSDVTAFAD NILVYVASYN EVDQLSKLLS DKGYLVTKID
     GRTMKVGKTE ISTSGTKFKK HFIVATNIIE NGVTLDIEAV IDFGMKVVPE MDSDNRMIRY
     SKQAISFGER IQRLGRVGRH KEGIALRIGH TEKGIQEIPE MAATEAAFLS FTYGLPVMTH
     NVGLSLLKNC TVRQARTMQQ YELSPFFTQN LVNFDGTVHP KIDVLLRPYK LRDCEVRLSE
     AAIPHGVQSI WLSARDYEAV GGRLCLEGDV RIPFLIKDVP ERLYKELWDI VQTYKRDFTF
     GRINSVSAGK IAYTLRTDVY SIPRTLITID KLIESENMKH AHFKAMTSCT GLNSSFSLLG
     VINTIQSRYL VDHSVENIRK LQLAKAQIQQ LEAHMQENNV ENLIQSLGAV RAVYHQSVDG
     FKHIKRELGL KGVWDGSLMI KDAIVCGFTM AGGAMLLYQH FRDKFTNVHV FHQGFSARQR
     QKLRFKSAAN AKLGREVYGD DGTIEHYFGE AYTKKGNKKG KMHGMGVKTR KFVATYGFKP
     EDYSYVRYLD PLTGETLDES PQTDISMVQD HFSDIRRKYM DSDSFDRQAL IANNTIKAYY
     VRNSAKAALE VDLTPHNPLK VCDNKLTIAG FPDREAELRQ TGPPRTIQVD QVPPPSKSVH
     HEGKSLCQGM RNYNGIASVV CHLKNTSGKG KSLFGIGYNS FIITNRHLFK ENNGELIVKS
     QHGKFIVKNT TTLQIAPVGK TDLLIIRMPK DFPPFHSRAR FRAMKAGDKV CMIGVDYQEN
     HIASKVSETS IISEGTGDFG CHWISTNDGD CGNPLVSVSD GFIVGLHSLS TSTGDQNFFA
     KIPAQFEEKV LRKIDDLTWS KHWSYNINEL SWGALKVWES RPEAIFNAQK EVNQLNVFEQ
     SGGRWLFDKL HGNLKGVSSA PSNLVTKHVV KGICPLFRNY LECDEEAKAF FSPLMGHYMK
     SVLSKEAYIK DLLKYSSDIV VGEVNHDVFE DSVAQVIELL NDHECPELEY ITDSEVIIQA
     LNMDAAVGAL YTGKKRKYFE GSTVEHRQAL VRKSCERLYE GRMGVWNGSL KAELRPAEKV
     LAKKTRSFTA APLDTLLGAK VCVDDFNNWF YSKNMECPWT VGMTKFYKGW DEFLKKFPDG
     WVYCDADGSQ FDSSLTPYLL NAVLSIRLWA MEDWDIGEQM LKNLYGEITY TPILTPDGTI
     VKKFKGNNSG QPSTVVDNTL MVLITMYYAL RKAGYDTKTQ EDMCVFYING DDLCIAIHPD
     HEHVLDSFSS SFAELGLKYD FAQRHRNKQN LWFMSHRGIL IDDIYIPKLE PERIVAILEW
     DKSKLPEHRL EAITAAMIES WGYGDLTHQI RRFYQWVLEQ APFNELAKQG RAPYVSEVGL
     RRLYTSERGS MDELEAYIDK YFERERGDSP ELLVYHESRG TDDYQLVCSN NTHVFHQSKN
     EAVDAGLNEK LKEKEKQKEK EKEKQKEKEK DGASDGNDVS TSTKTGERDR DVNVGTSGTF
     TVPRIKSFTD KMVLPRIKGK TVLNLNHLLQ YNPQQIDISN TRATHSQFEK WYEGVRNDYG
     LNDNEMQVML NGLMVWCIEN GTSPDISGVW VMMDGETQVD YPIKPLIEHA TPSFRQIMAH
     FSNAAEAYIA KRNATERYMP RYGIKRNLTD ISLARYAFDF YEVNSKTPDR AREAHMQMKA
     AALRNTSRRM FGMDGSVSNK EENTERHTVE DVNRDMHSLL GMRN
//
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