GenomeNet

Database: UniProt
Entry: P09814
LinkDB: P09814
Original site: P09814 
ID   POLG_TVMV               Reviewed;        3023 AA.
AC   P09814; Q84898; Q84899; Q84900; Q84901; Q84902;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   18-SEP-2019, entry version 154.
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   Tobacco vein mottling virus (TVMV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12228;
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH   NCBI_TaxID=3618; Rumex.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3737407; DOI=10.1093/nar/14.13.5417;
RA   Domier L.L., Franklin K.M., Shahabuddin M., Hellmann G.M.,
RA   Overmeyer J.H., Hiremath S.T., Siaw M.F.E., Lomonossoff G.P.,
RA   Shaw J.G., Rhoads R.E.;
RT   "The nucleotide sequence of tobacco vein mottling virus RNA.";
RL   Nucleic Acids Res. 14:5417-5430(1986).
RN   [2]
RP   SEQUENCE REVISION.
RA   Shaw J.G.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1874-1888, COVALENT RNA LINKAGE AT TYR-1878 (VPG),
RP   AND URIDYLYLATION AT TYR-1878.
RX   PubMed=1702164;
RA   Murphy J.F., Rychlik W., Rhoads R.E., Hunt A.G., Shaw J.G.;
RT   "A tyrosine residue in the small nuclear inclusion protein of tobacco
RT   vein mottling virus links the VPg to the viral RNA.";
RL   J. Virol. 65:511-513(1991).
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
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.
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=P09814-1; Sequence=Displayed;
CC         Note=Produced by conventional translation.;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CK10-1; 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.
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; X04083; CAA27720.1; -; Genomic_RNA.
DR   PIR; A23647; GNVSTV.
DR   RefSeq; NP_056867.1; NC_001768.1. [P09814-1]
DR   PDB; 3MMG; X-ray; 1.70 A; A/B=2002-2242, C/D=2753-2760.
DR   PDBsum; 3MMG; -.
DR   SMR; P09814; -.
DR   MEROPS; C04.003; -.
DR   PRIDE; P09814; -.
DR   GeneID; 1494056; -.
DR   KEGG; vg:1494056; -.
DR   PMAP-CutDB; P09814; -.
DR   Proteomes; UP000007549; 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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; PS51195; Q_MOTIF; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 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   3023       Genome polyprotein.
FT                                /FTId=PRO_0000420031.
FT   CHAIN         1    274       P1 proteinase. {ECO:0000255}.
FT                                /FTId=PRO_0000040483.
FT   CHAIN       275    731       Helper component proteinase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000040484.
FT   CHAIN       732   1078       Protein P3. {ECO:0000250}.
FT                                /FTId=PRO_0000040485.
FT   CHAIN      1079   1130       6 kDa protein 1. {ECO:0000250}.
FT                                /FTId=PRO_0000040486.
FT   CHAIN      1131   1765       Cytoplasmic inclusion protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040487.
FT   CHAIN      1766   1818       6 kDa protein 2. {ECO:0000250}.
FT                                /FTId=PRO_0000040488.
FT   CHAIN      1819   2001       Viral genome-linked protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040489.
FT   CHAIN      2002   2242       Nuclear inclusion protein A.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040490.
FT   CHAIN      2243   2758       Nuclear inclusion protein B.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040491.
FT   CHAIN      2759   3023       Capsid protein. {ECO:0000250}.
FT                                /FTId=PRO_0000040492.
FT   DOMAIN      132    274       Peptidase S30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01219}.
FT   DOMAIN      609    731       Peptidase C6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01080}.
FT   DOMAIN     1202   1354       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1367   1532       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2002   2218       Peptidase C4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00766}.
FT   DOMAIN     2484   2608       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1215   1222       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       325    328       Involved in interaction with stylet and
FT                                aphid transmission. {ECO:0000250}.
FT   MOTIF       583    585       Involved in virions binding and aphid
FT                                transmission. {ECO:0000250}.
FT   MOTIF      1304   1307       DEFH box.
FT   MOTIF      1856   1863       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   ACT_SITE    183    183       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    192    192       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    225    225       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    617    617       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE    690    690       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE   2047   2047       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2082   2082       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2152   2152       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   SITE        274    275       Cleavage; by P1 proteinase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   SITE        731    732       Cleavage; by autolysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   SITE       1078   1079       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1130   1131       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1765   1766       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1818   1819       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2001   2002       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2242   2243       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2758   2759       Cleavage; by NIa-pro. {ECO:0000250}.
FT   MOD_RES    1878   1878       O-(5'-phospho-RNA)-tyrosine.
FT                                {ECO:0000269|PubMed:1702164}.
FT   MOD_RES    1878   1878       O-UMP-tyrosine; transient.
FT                                {ECO:0000269|PubMed:1702164}.
FT   HELIX      2013   2016       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2019   2026       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2029   2038       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2041   2044       {ECO:0000244|PDB:3MMG}.
FT   HELIX      2046   2049       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2055   2060       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2063   2069       {ECO:0000244|PDB:3MMG}.
FT   HELIX      2070   2072       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2075   2077       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2080   2082       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2084   2087       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2110   2117       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2122   2130       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2138   2143       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2155   2158       {ECO:0000244|PDB:3MMG}.
FT   TURN       2159   2161       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2164   2172       {ECO:0000244|PDB:3MMG}.
FT   TURN       2173   2175       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2178   2182       {ECO:0000244|PDB:3MMG}.
FT   HELIX      2187   2191       {ECO:0000244|PDB:3MMG}.
FT   HELIX      2206   2208       {ECO:0000244|PDB:3MMG}.
FT   STRAND     2754   2757       {ECO:0000244|PDB:3MMG}.
SQ   SEQUENCE   3023 AA;  342285 MW;  299FDED15C0E5B87 CRC64;
     MAATMIFGSF THDLLGKAMS TIHSAVTAEK DIFSSIKERL ERKRHGKICR MKNGSIYIKA
     ASSTKVEKIN AAAKKLADDK AAFLKAQPTI VDKIIVNEKI QVVEAEEVHK REDVQTVFFK
     KTKKRAPKLR ATCSSSGLDN LYNAVANIAK ASSLRVEVIH KKRVCGEFKQ TRFGRALFID
     VAHAKGHRRR IDCRMHRREQ RTMHMFMRKT TKTEVRSKHL RKGDSGIVLL TQKIKGHLSG
     VRDEFFIVRG TCDDSLLEAR ARFSQSITLR ATHFSTGDIF WKGFNASFQE QKAIGLDHTC
     TSDLPVEACG HVAALMCQSL FPCGKITCKR CIANLSNLDF DTFSELQGDR AMRILDVMRA
     RFPSFTHTIR FLHDLFTQRR VTNPNTAAFR EILRLIGDRN EAPFAHVNRL NEILLLGSKA
     NPDSLAKASD SLLELARYLN NRTENIRNGS LKHFRNKISS KAHSNLALSC DNQLDQNGNF
     LWGLAGIAAK RFLNNYFETI DPEQGYDKYV IRKNPNGERK LAIGNFIIST NLEKLRDQLE
     GESIARVGIT EECVSRKDGN YRYPCCCVTL EDGSPMYSEL KMPTKNHLVI GNSGDPKYLD
     LPGEISNLMY IAKEGYCYIN IFLAMLVNVD EANAKDFTKR VRDESVQKLG KWPSLIDVAT
     ECALLSTYYP AAASAELPRL LVDHAQKTIH VVDSYGSLNT GYHILKANTV SQLEKFASNT
     LESPMAQYKV GGLVYSENND ASAVKALTQA IFRPDVLSEL IEKEPYLMVF ALVSPGILMA
     MSNSGALEFG ISKWISSDHS LVRMASILKT LASKVSVADT LALQKHIMRQ NANFLCGELI
     NGFQKKKSYT HATRFLLMIS EENEMDDPVL NAGYRVLEAS SHEIMEKTYL ALLETSWSDL
     SLYGKFKSIW FTRKHFGRYK AELFPKEQTD LQGRYSNSLR FHYQSTLKRL RNKGSLCRER
     FLESISSARR RTTCAVFSLL HKAFPDVLKF INTLVIVSLS MQIYYMLVAI IHEHRAAKIK
     SAQLEERVLE DKTMLLYDDF KAKLPEGSFE EFLEYTRQRD KEVYEYLMME TTEIVEFQAK
     NTGQASLERI IAFVSLTLML FDNERSDCVY KILTKFKGIL GSVENNVRFQ SLDTIVPTQE
     EKNMVIDFEL DSDTAHTPQM QEQTFSDWWS NQIANNRVVP HYRTEGYFMQ FTRNTASAVS
     HQIAHNEHKD IILMGAVGSG KSTGLPTNLC KFGGVLLLEP TRPLAENVTK QMRGSPFFAS
     PTLRMRNLST FGSSPITVMT TGFALHFFAN NVKEFDRYQF IIFDEFHVLD SNAIAFRNLC
     HEYSYNGKII KVSATPPGRE CDLTTQYPVE LLIEEQLSLR DFVDAQGTDA HADVVKKGDN
     ILVYVASYNE VDQLSKMLNE RGFLVTKVDG RTMKLGGVEI ITKGSSIKKH FIVATNIIEN
     GVTLDVDVVV DFGLKVVPNL DSDNRLVSYC KIPISLGERI QRFGRVGRNK PGVALRIGET
     IKGLVEIPSM IATEAAFLCF VYGLPVTTQN VSTSILSQVS VRQARVMCQF ELPIFYTAHL
     VRYDGAMHPA IHNALKRFKL RDSEINLNTL AIPTSSSKTW YTGKCYKQLV GRLDIPDEIK
     IPFYTKEVPE KVPEQIWDVM VKFSSDAGFG RMTSAAACKV AYTLQTDIHS IQRTVQIIDR
     LLENEMKKRN HFNLVVNQSC SSHFMSLSSI MASLRAHYAK NHTGQNIEIL QKAKAQLLEF
     SNLAIDPSTT EALRDFGYLE AVRFQSESEM ARGLKLSGHW KWSLISRDLI VVSGVGIGLG
     CMLWQFFKEK MHEPVKFQGK SRRRLQFRKA RDDKMGYIMH GEGDTIEHFF GAAYTKKGKS
     KGKTHGAGTK AHKFVNMYGV SPDEYSYVRY LDPVTGATLD ESPMTDLNIV QEHFGEIRRE
     AILADAMSPQ QRNKGIQAYF VRNSTMPILK VDLTPHIPLK VCESNNIAGF PEREGELRRT
     GPTETLPFDA LPPEKQEVAF ESKALLKGVR DFNPISACVW LLENSSDGHS ERLFGIGFGP
     YIIANQHLFR RNNGELTIKT MHGEFKVKNS TQLQMKPVEG RDIIVIKMAK DFPPFPQKLK
     FRQPTIKDRV CMVSTNFQQK SVSSLVSESS HIVHKEDTSF WQHWITTKDG QCGSPLVSII
     DGNILGIHSL THTTNGSNYF VEFPEKFVAT YLDAADGWCK NWKFNADKIS WGSFTLVEDA
     PEDDFMAKKT VAAIMDDLVR TQGEKRKWML EAAHTNIQPV AHLQSQLVTK HIVKGRCKMF
     ALYLQENADA RDFFKSFMGA YGPSHLNKEA YIKDIMKYSK QIVVGSVDCD TFESSLKVLS
     RKMKEWGFEN LEYVTDEQTI KNALNMDAAV GALYSGKKKQ YFEDLSDDAV ANLVQKSCLR
     LFKNKLGVWN GSLKAELRPF EKLIENKTRT FTAAPIETLL GGKVCVDDFN NHFYSKHIQC
     PWSVGMTKFY GGWNELLGKL PDGWVYCDAD GSQFDSSLSP YLINAVLRLR LSSMEEWDVG
     QKMLQNLYTE IVYTPISTPD GTIVKKFKGN NSGQPSTVVD NTLMVVLAMY YALSKLGVDI
     NSQEDVCKFF ANGDDLIIAI SPELEHVLDG FQQHFSDLGL NYDFSSRTRD KKELWFMSHR
     ALSKDGILIP KLEPERIVSI LEWDRSAEPH HRLEAICASM IEAWGYTDLL QNIRRFYKWT
     IEQEPYRSLA EQGLAPYLSE VALRRLYTSQ IATDNELTDY YKEILANNEF LRETVRFQSD
     TVDAGKDKAR DQKLADKPTL AIDRTKDKDV NTGTSGTFSI PRLKKAAMNM KLPKVGGSSV
     VNLDHLLTYK PAQEFVVNTR ATHSQFKAWH TNVMAELELN EEQMKIVLNG FMIWCIENGT
     SPNISGVWTM MDGDEQVEYP IEPMVKHANP SLRQIMKHFS NLAEAYIRMR NSEQVYIPRY
     GLQRGLVDRN LAPFAFDFFE VNGATPVRAR EAHAQMKAAA LRNSQQRMFC LDGSVSGQEE
     NTERHTVDDV NAQMHHLLGV KGV
//
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