GenomeNet

Database: UniProt
Entry: P89876
LinkDB: P89876
Original site: P89876 
ID   POLG_LMVE               Reviewed;        3255 AA.
AC   P89876;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   18-SEP-2019, entry version 143.
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   Lettuce mosaic virus (strain E) (LMV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=117131;
OH   NCBI_TaxID=4222; Carthamus tinctorius (Safflower).
OH   NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH   NCBI_TaxID=114280; Cichorium endivia (Endive).
OH   NCBI_TaxID=13427; Cichorium intybus (Chicory).
OH   NCBI_TaxID=52518; Eustoma exaltatum subsp. russellianum (Bluebells) (Eustoma grandiflorum).
OH   NCBI_TaxID=4235; Lactuca.
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9085548; DOI=10.1016/s0168-1702(96)01411-6;
RA   Revers F., Yang S.J., Walter J., Souche S., Lot H., Le Gall O.,
RA   Candresse T., Dunez J.;
RT   "Comparison of the complete nucleotide sequences of two isolates of
RT   lettuce mosaic virus differing in their biological properties.";
RL   Virus Res. 47:167-177(1997).
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
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=P89876-1; Sequence=Displayed;
CC         Note=Produced by conventional translation.;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CW79-1; 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; X97705; CAA66281.1; -; Genomic_RNA.
DR   RefSeq; NP_619667.1; NC_003605.1.
DR   PRIDE; P89876; -.
DR   GeneID; 940180; -.
DR   KEGG; vg:940180; -.
DR   Proteomes; UP000008378; 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   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Complete proteome;
KW   Covalent protein-RNA linkage; Helical capsid protein; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Protease; Ribosomal frameshifting; RNA-directed RNA polymerase;
KW   Serine protease; Suppressor of RNA silencing; Thiol protease;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN         1   3255       Genome polyprotein.
FT                                /FTId=PRO_0000420000.
FT   CHAIN         1    437       P1 proteinase. {ECO:0000255}.
FT                                /FTId=PRO_0000040279.
FT   CHAIN       438    895       Helper component proteinase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000040280.
FT   CHAIN       896   1273       Protein P3. {ECO:0000250}.
FT                                /FTId=PRO_0000040281.
FT   CHAIN      1274   1325       6 kDa protein 1. {ECO:0000250}.
FT                                /FTId=PRO_0000040282.
FT   CHAIN      1326   1968       Cytoplasmic inclusion protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040283.
FT   CHAIN      1969   2021       6 kDa protein 2. {ECO:0000250}.
FT                                /FTId=PRO_0000040284.
FT   CHAIN      2022   2214       Viral genome-linked protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040285.
FT   CHAIN      2215   2457       Nuclear inclusion protein A.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040286.
FT   CHAIN      2458   2977       Nuclear inclusion protein B.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040287.
FT   CHAIN      2978   3255       Capsid protein. {ECO:0000250}.
FT                                /FTId=PRO_0000040288.
FT   DOMAIN      292    437       Peptidase S30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01219}.
FT   DOMAIN      773    895       Peptidase C6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01080}.
FT   DOMAIN     1397   1549       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1568   1727       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2215   2433       Peptidase C4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00766}.
FT   DOMAIN     2699   2823       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1410   1417       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       489    492       Involved in interaction with stylet and
FT                                aphid transmission. {ECO:0000250}.
FT   MOTIF       747    749       Involved in virions binding and aphid
FT                                transmission. {ECO:0000250}.
FT   MOTIF      1499   1502       DECH box.
FT   MOTIF      2062   2069       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   COMPBIAS   1266   1271       Poly-Glu.
FT   COMPBIAS   2965   2972       Poly-Asp.
FT   ACT_SITE    345    345       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    354    354       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    388    388       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    781    781       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE    854    854       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE   2260   2260       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2295   2295       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2365   2365       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   SITE        437    438       Cleavage; by P1 proteinase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   SITE        895    896       Cleavage; by autolysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   SITE       1273   1274       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1325   1326       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1968   1969       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2021   2022       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2214   2215       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2457   2458       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2977   2978       Cleavage; by NIa-pro. {ECO:0000250}.
FT   MOD_RES    2084   2084       O-(5'-phospho-RNA)-tyrosine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   3255 AA;  367624 MW;  B3E8582927E01628 CRC64;
     MATLDNCTQV HHMFAYNREH GTNYTRNHFR RYLAAQRIGF YYDWDDDVYE CPTCEAIYHS
     LDEIKNWHEC DPPAFDLNDF ITDARLKSAP VPDLGPVIVE TPKVEEKQEL NFFAATPAPE
     VLQWKCRGLQ FGSFTELETS EPVVSAPKPN CEEPARTIAK PEEPVEQETC GDGKRLLQAQ
     MEVDKAEQDL AFAYLSASLK PRLEGRTTAT IARRRDGCLV YKTKPSWSQR KGTKKILKVD
     TLACKNPYIP AVVDKISIAG GSSASVMHEQ QKPKILHTTP SRKVATHYKR TVMNQQTLTA
     LINQVGTIIL NAEKEFEVVG CRKQKVTGKG TRHNGVRLVK LKTAHEEGHR RKVDIRIPNG
     LRSIVTRISA RGGWHKTWTD SELSPGSSGY VLNSSKIIGE FGLRRHSIFV VRGRVYGKII
     DSQSKVTHTL THRMVQYSDV ARNFWNGYST CFMHNTPKDI LHTCTSDFDV KDCGTVAALL
     TQTLFQFGKI TCGKCAIEYK NLTRDELATR VNKEIDGTII SIQTQHPRFV HVLNFLRLIK
     QVLNAKNGNF GAFQETERII GDRMDAPFSH VNKLNAIVIK GNQATSDEMA QASNHVLEIA
     RYFKNRTENI QKGSLKSFRN KISGKAHLNP SLMCDNQLDK NGGFEWGQRS YHAKRFFDGY
     FETIDPSDGY SKYTIRRNPN GHRKLAIGNL IVSTNFESHR RSMVGEPIED PGLTNQCVSK
     EGGAFIYPCC CVTDEYGKPT LSEIKMPTKH HLVLGNAGDP KYVDLPKEAE GKMFVAKDGY
     CYINIFLAML VDVPEDQAKD FTKMAREIAV KQLGEWPSMM DVATACNILA TFHPDTRRSE
     LPRILVDHAT KTFHVIDSYG SITTGYHILK ANTVTQLVKF AHESLESEMQ HYRVGGEPDK
     APRKPAGNVP TLGISDLKNL GVESENEEHS IRPNLQRLIK AIYRPRMMRS LLTEEPYLLI
     LSIVSPGVLM ALYNSGSLER TMHEFLQTDQ RLSATAQILK HLAKKVSLAK TLTIQNAILE
     GGAGSLNEIL DAPAGRSLSY RLAKQTVEVM MARSDMDKEL VDVGFSVLRD QKNELIEKSY
     LMDLEDSWRA LPLCGKLSAM RVSRRWRDTS TPEAIPTGAA DLKGRYSISV GSVSKSAILH
     LKGICSGAVK RVKDKWVGVQ VQGVKWLAKS VHYMIPELTN ILNVGTLLLT LISLGVRFRS
     LTGQFKEMKY KETLAREEEL RKRIRTYNST YYEIHGKHAD AKQITKFITH HDPKLLEVVE
     FYEGPEEEEV EHQAKREDQA NLERIIAFTA LVMMMFDSER SDCVYRSLSK LKSLVSTCDD
     DVRHQSVDEI IDLFDEKKET IDFEIEGKEL YSSRVVDSTF SKWWDNQLVR GNTMAHYRTE
     GHFMTFTRET AASVAAEIAH NEYRDILLQG GVGSGKSTGL PFHLHKKGGV LLIEPTRPLA
     QNVYKQLGSN PFHLSPNLRM RGACKFGSSQ VTVATSGYAL HFIANNAQSL KMFDFIIFDE
     CHVLDASAMA FRCLLQEFEY QGKIIKVSAT PPGRKLDFKP MHMVDITTEN ELSIQQFVQG
     QGTGVNCDAT KKGDNILVYV SSYNEVDMLS KMLNDKGYKV TKVDGRTMKL GSVEVETVGT
     PQRKHFVVAT NIIENGVTLD VDVVVDFGQK VVPILDSEHR MIRYTKKSIT YGERIQRVGR
     VGRNKAGSAI RIGSTEMGTE EIPASIATEA AFLCFTYGLP VMTSNVSTSV LGNCTVRQAR
     TMQKFELSPF FMVDLVHHDG TVHPAINSLL RQFKLKESDT KLSTLAIPNA VTTFWKSARE
     YNSLGARTTI DDAAKIPFMI KDVPEHLQEK LWETIQQYKG DAGFGRCTSA NACKIAYTLS
     VSPFMIPATI NKIDALMAEE RQKLEYFQTV TANTCTISNF SISSLGDMIR SRYSTNHSRE
     NLQKLQTVRD TIINFECQAG TSDGGTFDME TAQKLAEEYG CIDVIYHQSK GALSKRLGLK
     GRWNQSLICK DLLIFCGVAI GGTWMMFQSF KDGMADVIRH QGKGKRQRQK LRYRQARDNK
     MGIEVYGDDA TMEHYFGAAY TEKGKKSGKT KGMGTKNRRF VNMYGYNPED YSFIRFLDPL
     TGKTMDEQVF TDISLVQDAF GKERLKLLSE GEIESEHMRN GIRAYLVKNL TTAALEIDMT
     PHNSCQLGTK TNNIAGFVDR EYELRQTGEA RVVAPALIPK DNPITDEDIP VKHESKTLFR
     GLRDYNPIAS AICLLTNESD GMKETMYGIG FGNTIITNQH LFRRNNGVLR VQSRHGEYVL
     PNTTQLKVLP CEGRDIMVII LTPDFPPFPQ KLKFRPPIKG EKICLVGSLF QDKSITSTVS
     ETSVTTPVDN SFLWKHWITT KDGHCGLPLV SSNDGYIVGI HSATSSRQTQ NYHAAMPEDF
     HQTHLIDPVS KSWVKHWKYN PDNMVWGGIN LINSTPREPF KINKLVTDLF GDAVQFQSKQ
     DEWFASQLKG NLKAVGKSTS QLVTKHTVKG KCMMFELYLQ THEEEKEFFK PLMGAYQKSR
     LNREAFTKDI MKYSTPITVG IVDCDTFLKA EKGVIKRLEK LGFSGCEYVT DEEAIFQALN
     MKAAVGALYS GKKRDYFESY GPEEKENILR ESCKRLYTGK FGVWNGSLKS ELRPMEKVMA
     NKTRVFTAAP LDTLLAGKVC VDDFNNYFYS KNIEAPWTVG MTKFYGGWNE LLTKLPDGWV
     YCDADGSQFD SSLSPFLINS VLRIRLKFME DWDLGEQMLK NLYTEIVYTA ILTPDSTIVK
     KFKGNNSGQP STVVDNTLMV VLAMTYTLHK LGFEDEEQDS MCKYFVNGDD LIIAIKPEYE
     SLLDQFQHCF KSLGLNYDFN SRTRKREELW FMSHCGIKKD GIFIPKLEPE RIVSILEWDR
     SDQPVHRLEA ICAAMIESWG YDKLTHEIRK FYKWCLDEAP YADLAKAGKA PYIAECALKR
     LYTSKEASEA ELEKYMEAIR SLVNDEDDDD MDEVYHQVDT KLDAGQGSKN DDKQKSSADS
     KDNVITEKGS GSGQVRKDDD INAGLHGKHT IPRTKAITQK MKLPMIRGKV ALNLDHLLEY
     EPNQRDISNT RATQKQYESW YDGVKNDYDV DDNGMQLILN GLMVWCIENG TSPNINGTWV
     MMDSEEQVEY ALKPIIEHAK PTFRQIMAHF SDAAEAYIEM RNKKKPYMPR YGRLRGLNDM
     GLARYAFDFY ETTSATPNRA REAHNQMKAA ALVGTQNRLF GMDGGGSTQE ENTERHTAAD
     VNQNMHTLLG VRGLH
//
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