POLG_SPMMV
ID POLG_SPMMV Reviewed; 3456 AA.
AC P89201;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
DE AltName: Full=N-terminal protein;
DE Contains:
DE RecName: Full=Helper component proteinase;
DE Short=HC-pro;
DE EC=3.4.22.45 {ECO:0000250|UniProtKB:P04517};
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 Sweet potato mild mottle virus (isolate Salazar) (SPMMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Ipomovirus.
OX NCBI_TaxID=652105;
OH NCBI_TaxID=4120; Ipomoea batatas (Sweet potato) (Convolvulus batatas).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9620210; DOI=10.1016/s0168-1702(97)00148-2;
RA Colinet D., Kummert J., Lepoivre P.;
RT "The nucleotide sequence and genome organization of the whitefly
RT transmitted sweetpotato mild mottle virus: a close relationship with
RT members of the family Potyviridae.";
RL Virus Res. 53:187-196(1998).
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. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It
CC may be involved in replication.
CC -!- FUNCTION: [6 kDa protein 1]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P13529}.
CC -!- FUNCTION: [6 kDa protein 2]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P09814}.
CC -!- FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent,
CC EIF4E-dependent translation of viral genomic RNAs (By similarity).
CC Binds to the cap-binding site of host EIF4E and thus interferes with
CC the host EIF4E-dependent mRNA export and translation (By similarity).
CC VPg-RNA directly binds EIF4E and is a template for transcription (By
CC similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are
CC templates for translation (By similarity).
CC {ECO:0000250|UniProtKB:P18247}.
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA
CC polymerase that plays an essential role in the virus replication.
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. {ECO:0000250|UniProtKB:P04517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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; Evidence={ECO:0000250|UniProtKB:P04517};
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 Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle.
CC Note=Probably colocalizes with 6K2-induced vesicles associated with
CC host chloroplasts. {ECO:0000250|UniProtKB:P13529}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with
CC host chloroplasts. {ECO:0000250|UniProtKB:P09814}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC -!- DOMAIN: [Helper component proteinase]: The N-terminus 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: [Viral genome-linked protein]: VPg is uridylylated by the
CC polymerase and is covalently attached to the 5'-end of the genomic RNA.
CC This uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.
CC -!- PTM: [Genome polyprotein]: Genome polyprotein of potyviruses undergoes
CC post-translational proteolytic processing by the main proteinase NIa-
CC pro resulting in the production of at least ten individual proteins.
CC The P1 proteinase and the HC-pro cleave only their respective C-termini
CC autocatalytically. 6K1 is essential for proper proteolytic separation
CC of P3 from CI (By similarity). {ECO:0000250}.
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DR EMBL; Z73124; CAA97466.1; -; mRNA.
DR RefSeq; NP_620656.1; NC_003797.1.
DR MEROPS; C04.013; -.
DR GeneID; 944381; -.
DR KEGG; vg:944381; -.
DR Proteomes; UP000007084; 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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.150; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR025910; P1_Ser_Pept_dom.
DR InterPro; IPR002540; Pept_S30_P1_potyvir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF13611; Peptidase_S76; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 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; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Helical capsid protein; Helicase; Host cytoplasmic vesicle; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Reference proteome; Repeat; RNA-directed RNA polymerase; Serine protease;
KW Suppressor of RNA silencing; Thiol protease; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..3456
FT /note="Genome polyprotein"
FT /id="PRO_0000420024"
FT CHAIN 1..743
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_5000147693"
FT CHAIN 744..1196
FT /note="Helper component proteinase"
FT /id="PRO_5000147694"
FT CHAIN 1197..1489
FT /note="Protein P3"
FT /evidence="ECO:0000255"
FT /id="PRO_5000147695"
FT CHAIN 1490..1541
FT /note="6 kDa protein 1"
FT /id="PRO_5000147696"
FT CHAIN 1542..2181
FT /note="Cytoplasmic inclusion protein"
FT /id="PRO_5000147697"
FT CHAIN 2182..2234
FT /note="6 kDa protein 2"
FT /id="PRO_0000402492"
FT CHAIN 2235..2411
FT /note="Viral genome-linked protein"
FT /id="PRO_0000402493"
FT CHAIN 2412..?2642
FT /note="Nuclear inclusion protein A"
FT /id="PRO_0000402494"
FT CHAIN ?2643..?3180
FT /note="Nuclear inclusion protein B"
FT /id="PRO_0000402495"
FT CHAIN ?3181..3456
FT /note="Capsid protein"
FT /id="PRO_5000147698"
FT DOMAIN 600..743
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 1075..1196
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT REPEAT 1094..1126
FT /note="HAT 1"
FT DOMAIN 1617..1768
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1787..1947
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2412..2636
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT REPEAT 2597..2629
FT /note="HAT 2"
FT DOMAIN 2891..3011
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REPEAT 3082..3115
FT /note="HAT 3"
FT ACT_SITE 640
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 652
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 689
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 1083
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 1155
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2457
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2494
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2566
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1630..1637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 743..744
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 1196..1197
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1489..1490
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000255"
FT SITE 1541..1542
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000255"
FT SITE 2181..2182
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000255"
FT SITE 2234..2235
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000255"
FT SITE 2411..2412
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000255"
FT MOD_RES 2304
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3456 AA; 390285 MW; C8D758543597C72A CRC64;
MGKSKLTYKQ CIAKWGKAAL EAQNNGSRRS VSVGTHQIAA NIFAFYDAKD YHLFAMGKRG
GLTPAAEQLR IAIARGTIYK VQYNCHFCPD CDVIVDSEEG WFCEDCGSQF NKRDDNVLDN
KNDVARALGG WNEYEDATWA LFEAARADML EVAPTVGQLE KEIRAIEKSA GKKLTAYEEE
MLEELAYKLD VAKMNEEKQE EVLEETNFSI SNDEFPALNG PQDEEVNVVI EETTEESAIE
VAKEAEKSVE FEIIHEKTDE PISDAVNARM VATPVVATSV TKSGTVIDGK ELVEKPKTTM
WVTKPKTTAA IPATSSKSAV WVAKPKPASA IFIAEPVVKP AVRACNDVMN IGAMVCPIMV
SANAQVEDAT KEEEPVIKYN ITFGSFNYEV STKGERIQAA VQLDEIIEGP DIEPILICQT
GSSHKSETKK AAKGLFVQDK FSVIGNKVLC KSFPAFNNFM NETRLGGIYR TRKGNYKNAA
LRLLKATKVQ VFYDGIKDIF ECPYCHVSSN ELEGLNGDNC EKCKDLFYKH IDDPRKVEEE
YLMVPLVPID QHVHEEHSII SKAKWEAHES ICEGEVNIVK IFDGKPTASK KKFKTMQAPN
VANIPLDDFM QELVEICLER NTPIEIIGGV KSFNVVKLRH ATRDISKSGE DDMYPTEREW
FCHKNKLCLC GGIEREKKVR SFEVRPGWSG VILHKNQVAE CDWDKFVFID DICVVQGRNL
ITNKIENALE KKGATRLKQI QFYASSVVPN FKDEFDRASR LKADHEPYES SNNELIGRLA
RLVAAVIPKG HLYCKTCCLR VIKSKRADIV NALSKAKQRG ERDEFIYDEL IKLFELQAPP
PYKIATITSD DDMFAHIRIG WKPYSGRLSL IMQHLQGLHT SISMLHQSLA GAQNDQQIDR
QALHNQVRIL HQRNEEHMPF LKKAVDEIQL LNATDQVANA RELYLDTRAT STGDFDILRK
YQSIYEFFPN IMSRANKVGM AVIKSETSLS KAFALMDNAK SMNAIHTLIG EDVIDNTSGA
CLMKNDKTFF SIGCKQGVDG SKMYGPLCPT KQHVRIHRVE SNMQIPLPTF HDATVWEFNE
GYCYANQLAI MVGFINEDEM EFYKNQMNQI VLNLGAWPTF EQYLVELRAI SLDYPKVRGC
PAAIHLVSHA NKLIHVLGQF GTINQGWHAL EVATVGELVD LCHKKVEGEM LTYKVGGIYD
WVTKKNAFID LFEHHPENIF KICTSPSVLW LFARSCEKHD FINDIMARDH SLVGLFIKLE
YVGKHLHIFQ SVDDVCVEYA ASMREIIEEH ADIHGLRDSV VDRMVHAYHN EVREANKYEL
VDRILEKNIG LIAKEISSRK LITMYHRDLF SWHEWQRLKL MPHSSNAQKL FEEANERAYG
KQSWNLRVIW GACKEVLYAA THGVYVRVKG TTVRCADAVV YGFYGRTRAM VSSWASEAWG
AIFTSCLRAL VVMVVTAYIS TWIPKIRKMI KREKKQFEDL GDGELYVEQH GKKEEAFLFK
ICAIFALIAG IVDYEWGAAA CATMNKVRSI CTVLGSVGIE SHANEPNDKV EQDLKESLKF
TSFEIEVPTW FYHNDMTFER WFQHQIQYGN VCADPIYSGP LRMLAITESS AREVAMNIRT
SGETDVRVYS GVGGGKSTRL PKELSMFGHV LICVPTRVLA ESLLTSFMVL FNMDVNVAYR
GRIHTGNAPI TIMTYGYALN FLVHKPMELN RYDYVLLDEI NTNPVEFAPL FSFIKTTDPK
KKIVKLSATH AGMDCECETR HKIKVETLSE MPIESWVSMQ GSGVVGDATS VGDVILVFVA
SFKDVDTCAN GLRSKGFKVL KVDSRNFRRD ADVDKQIQSL GEGKKFIVAT NIIENGVTFN
IDVVVDFGEK ISPNLSSDER CITLGRQRIS RAERIQRFGR AGRIKPGTVL RFGRGNLVDA
LPSVLTATES ALLCFAHGIK PVCDRVDVAA IGTLTRQQAL VSGQFELNKL LVAHSATPSG
QIPRVVYELF KPLLLRTDAV PICSSYNAIA ACNWLPLSTY MRRNEKNEHV LATKIPWYCS
DLSEDFNIKL AECVKSCMST SNARFIVDNV NFITVAHKIS VGEKTVGQAK LMVGELLENS
KSWRDGLLHV QSSSVTRSLV GLCTSWYQRR AKAALDRLDL QVNRLQLLYD QLGQVEITSD
YDKLVEFFTE NGECAAYLES QSKTDFLEKH VLELRQPAIT KNVVGTAMFA VALTGCLFWW
WMKRNEKYEF IEQHGKKIRL NRDKRNACFV FSGTDDAMVE EYGVEYSQDV IHGRMSKAQK
ARQMKLKGKK PGSDTRVKPF KVLYGIDPND YDTVALSAGG LTTEAVPVGE ASLIDLMLEL
DDETGIFRKQ VVNELKLKYT NNANGEQAMV RLTPHDSRRA TIGSFMPSGF PDHHGEWRQT
GAAEIIKEKN VAVDSHVGTP TVDAEDKHIA SRLAIVRTHK GETHGIFHGD KLITPFHTFK
NACGNDTLTV QSLRGLYDYG ILSRQKMEQV PKQDIMVLVN PIDVTPFKQS QIFRPPIQCE
VAYMIVCRRT PNGLRFEKTQ ETEIFPLGKQ YGGVWKHGCD TRLGDCGGPI IACRDRKIVG
FNGGRLMQMK YNTVLAHIFE PVNETFIEML AKMEYAKGFW KFNPELVEWS RLLPTTTSFP
IQKQIQGVES HGKPGDKCCG GNLISVGFAN VTRISKHVIK GKRPSFVEYC NTYPDNIFMR
DNLCEHYGPS ILSKAAFYKD FTKYDDPVKV GRLDCYAFDT ALAMVHDTLS QLGFHGNSGS
QWDIAEIFDD LNKKSSMGAL YSGKKGQWMH GLTPEDAISL AVESYALLNS GHLGVWSGSL
KAELRHVDKL KEGKTRVFTG APIDTLLAGK ILVDNFNNYF YKCHLQGPWT VGINKFNRGW
NKLANYFNHD WVFIDCDGSR FDSSIPPIMF NAVCMLRSVF GDLDPDENQT LSNLYTEIVN
TPILTIEGNI IRKFRGNNSG QPSTVVDNTL ILMIAMEYAI AKVFVTRPDI KYVCNGDDLL
INCPRSTANA ISEHFKDVFA DLSLNYDFDH VCDKITDVDF MSHSFMWLDT EQMYIPKLDK
ERIVAILEWE RSDEQFRTRS ALNAAYIESF GYEDLMTEIE KFAHFWAKKH GLNDVLMERE
KVRSLYVDEN FDASRFEKFY PESFSPFDVY VEPHASTSKT IEELQQEMED LDSDTTITVV
QRETQKAGIR DQIEALRAQQ IVRPPEAQLQ PDVTPAQIVT FEPPRVTGFG ALWIPRQQRN
YMTPSYIEKI KAYVPHSNLI ESGLASEAQL TSWFENTCRD YQVSMDVFMS TILPAWIVNC
IINGTSQERT NEHTWRAVIM ANMEDQEVLY YPIKPIIINA QPTLRQVMRH FGEQAVAQYM
NSLQVGKPFT VKGAVTAGYA NVQDAWLGID FLRDTMKLTT KQMEVKHQII AANVTRRKIR
VFALAAPGDG DELDTERHVV DDVARGRHSL RGAQLD
