L_VSIVM
ID L_VSIVM Reviewed; 2109 AA.
AC Q98776;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=RNA-directed RNA polymerase L;
DE Short=Protein L;
DE AltName: Full=Large structural protein;
DE AltName: Full=Replicase;
DE AltName: Full=Transcriptase;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48 {ECO:0000250|UniProtKB:P28887};
DE Includes:
DE RecName: Full=GTP phosphohydrolase {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:P03523};
DE Includes:
DE RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000305};
DE EC=2.7.7.88 {ECO:0000269|PubMed:26512087};
DE AltName: Full=PRNTase {ECO:0000305};
DE Includes:
DE RecName: Full=mRNA cap methyltransferase {ECO:0000305};
DE EC=2.1.1.375 {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE Short=G-N7-MTase {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE Short=N1-2'-O-MTase {ECO:0000250|UniProtKB:P03523};
GN Name=L;
OS Vesicular stomatitis Indiana virus (strain Mudd-Summers) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11279;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=252607; Lutzomyia.
OH NCBI_TaxID=7370; Musca domestica (House fly).
OH NCBI_TaxID=7190; Simuliidae (black flies).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6086959; DOI=10.1128/jvi.51.2.505-514.1984;
RA Schubert M., Harmison G.G., Meier E.;
RT "Primary structure of the vesicular stomatitis virus polymerase (L) gene:
RT evidence for a high frequency of mutations.";
RL J. Virol. 51:505-514(1984).
RN [2]
RP INTERACTION WITH PHOSPHOPROTEIN.
RX PubMed=2845648; DOI=10.1016/0042-6822(88)90505-3;
RA Paul P.R., Chattopadhyay D., Banerjee A.K.;
RT "The functional domains of the phosphoprotein (NS) of vesicular stomatitis
RT virus (Indiana serotype).";
RL Virology 166:350-357(1988).
RN [3] {ECO:0007744|PDB:5CHS}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 36-380, MUTAGENESIS OF TYR-39;
RP LEU-41; ASP-236; GLU-290; ARG-356; HIS-357 AND TRP-358, AND CATALYTIC
RP ACTIVITY.
RX PubMed=26512087; DOI=10.1128/jvi.02317-15;
RA Qiu S., Ogino M., Luo M., Ogino T., Green T.J.;
RT "Structure and Function of the N-Terminal Domain of the Vesicular
RT Stomatitis Virus RNA Polymerase.";
RL J. Virol. 90:715-724(2016).
CC -!- FUNCTION: Responsible for RNA synthesis (replicase and transcriptase),
CC cap addition, and cap methylation (By similarity). Performs also the
CC polyadenylation of subgenomic mRNAs by a stuttering mechanism at a
CC slipery stop site present at the end of viral genes (By similarity).
CC The template is composed of the viral RNA tightly encapsidated by the
CC nucleoprotein (N) (By similarity). The viral polymerase binds to the
CC genomic RNA at the 3' leader promoter, thereby initiating either genome
CC replication or mRNA transcription. In the transcription mode, the
CC polymerase performs the sequential transcription of all mRNAs using a
CC termination-reinitiation mechanism responding to gene start and gene
CC end signals. Some polymerase disengage from the template at each gene
CC junction, resulting in a decreasing abundance of transcripts from the
CC 3' to the 5' end of the genome (By similarity). The first gene is the
CC most transcribed, and the last the least transcribed. The viral
CC phosphoprotein helps the polymerase to engage the N-RNA template and
CC acts as processivity factor. Polyribonucleotidyl transferase (PRNTase)
CC adds the cap structure when the nascent RNA chain length has reached
CC few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and
CC facilitates subsequent guanine-N-7 methylation, both activities being
CC carried by the viral polymerase (By similarity). In the replication
CC mode, the polymerase replicates the whole viral genome without
CC recognizing the gene end transcriptional signals. The ability of the
CC polymerase to override the gene end signals as it is producing the
CC antigenome is probably due to replicative RNA becoming encapsidated
CC with nucleoprotein as it is synthesized (By similarity).
CC {ECO:0000250|UniProtKB:P03523, ECO:0000250|UniProtKB:P28887}.
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=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in
CC mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-
CC adenylyl-cytidylyl-adenosine in mRNA + diphosphate;
CC Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl
CC 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-
CC triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156482, ChEBI:CHEBI:156484;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a
CC 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482,
CC ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- SUBUNIT: Interacts with the P protein; the association of P and L forms
CC the polymerase complex. {ECO:0000305|PubMed:2845648}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged
CC asymmetrically towards the blunt end of the virus.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- SIMILARITY: Belongs to the rhabdoviridae protein L family.
CC {ECO:0000305}.
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DR EMBL; K02378; AAA48441.1; -; Genomic_RNA.
DR PDB; 5CHS; X-ray; 1.80 A; A/B=36-380.
DR PDBsum; 5CHS; -.
DR SMR; Q98776; -.
DR BRENDA; 2.7.7.88; 14216.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR039530; L_methyltransferase_rhabdo.
DR InterPro; IPR039736; L_poly_C.
DR InterPro; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR InterPro; IPR025786; Mononega_L_MeTrfase.
DR InterPro; IPR017234; RNA-dir_pol_rhabdovirus.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF14314; Methyltrans_Mon; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF037546; RNA_pol_RhabdoV_sub; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Host cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
KW Viral RNA replication; Virion; Zinc.
FT CHAIN 1..2109
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000287265"
FT DOMAIN 598..784
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1640..1837
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT ACT_SITE 1227
FT /note="Nucleophile; for GDP polyribonucleotidyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1651
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1762
FT /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1795
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1833
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 605
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P28887"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P28887"
FT BINDING 1081
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1667..1676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 39
FT /note="Y->A: Almost complete loss of viral transcription."
FT /evidence="ECO:0000269|PubMed:26512087"
FT MUTAGEN 41
FT /note="L->A: Almost complete loss of viral transcription."
FT /evidence="ECO:0000269|PubMed:26512087"
FT MUTAGEN 236
FT /note="D->A: Almost complete loss of viral transcription."
FT /evidence="ECO:0000269|PubMed:26512087"
FT MUTAGEN 290
FT /note="E->A: Almost complete loss of viral transcription."
FT /evidence="ECO:0000269|PubMed:26512087"
FT MUTAGEN 356
FT /note="R->A: Almost complete loss of viral transcription."
FT /evidence="ECO:0000269|PubMed:26512087"
FT MUTAGEN 357
FT /note="H->A: Almost complete loss of viral transcription."
FT /evidence="ECO:0000269|PubMed:26512087"
FT MUTAGEN 358
FT /note="W->A: Almost complete loss of viral transcription."
FT /evidence="ECO:0000269|PubMed:26512087"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 107..131
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 149..171
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:5CHS"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5CHS"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:5CHS"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5CHS"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:5CHS"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:5CHS"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:5CHS"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 228..249
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 258..278
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 289..304
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 312..328
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:5CHS"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:5CHS"
FT TURN 354..358
FT /evidence="ECO:0007829|PDB:5CHS"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:5CHS"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5CHS"
SQ SEQUENCE 2109 AA; 240998 MW; 643A212A468E94DA CRC64;
MEVHDFETDE FNDFNEDDYA TREFLNPDER MTYLNHADYN LNSPLISDDI DNLIRKFNSL
PIPSMWDSKN WDGVLEMLTS CQANPISTSQ MHKWMGSWLM SDNHDASQGY SFLHEVDKEA
EITFDVVETF IRGWGNKPIE YIKKERWTDS FKILAYLCQK FLDLHKLTLI LNAVSEVELL
NLARTFKGKV RRSSHGTNIC RIRVPSLGPT FISEGWAYFK KLDILMDRNF LLMVKDVIIG
RMQTVLSMVC RIDNLFSEQD IFSLLNIYRI GDKIVERQGN FSYDLIKMVE PICNLKLMKL
ARESRPLVPQ FPHFENHIKT SVDEGAKIDR GIRFLHDQIM SVKTVDLTLV IYGSFRHWGH
PFIDYYTGLE KLHSQVTMKK DIDVSYAKAL ASDLARIVLF QQFNDHKKWF VNGDLLPHDH
PFKSHVKENT WPTAAQVQDF GDKWHELPLI KCFEIPDLLD PSIIYSDKSH SMNRSEVLKH
VRMNPNTPIP SKKVLQTMLD TKATNWKEFL KEIDEKGLDD DDLIIGLKGK ERELKLAGRF
FSLMSWKLRE YFVITEYLIK THFVPMFKGL TMADDLTAVI KKMLDSSSGQ GLKSYEAICI
ANHIDYEKWN NHQRKLSNGP VFRVMGQFLG YPSLIERTHE FFEKSLIYYN GRPDLMRVHN
NTLINSTSQR VCWQGQEGGL EGLRQKGWTI LNLLVIQREA KIRNTAVKVL AQGDNQVICT
QYKTKKSRNV VELQGALNQM VSNNEKIMTA IKIGTGKLGL LINDDETMQS ADYLNYGKIP
IFRGVIRGLE TKRWSRVTCV TNDQIPTCAN IMSSVSTNAL TVAHFAENPI NAMIQYNYFG
TFARLLLMMH DPALRQSLYE VQDKIPGLHS STFKYAMLYL DPSIGGVSGM SLSRFLIRAF
PDPVTESLSF WRFIHVHARS EHLKEMSAVF GNPEIAKFRI THIDKLVEDP TSLNIAMGMS
PANLLKTEVK KCLIESRQTI RNQVIKDATI YLYHEEDRLR SFLWSINPLF PRFLSEFKSG
TFLGVADGLI SLFQNSRTIR NSFKKKYHRE LDDLIVRSEV SSLTHLGKLH LRRGSCKMWT
CSATHADTLR YKSWGRTVIG TTVPHPLEML GPQHRKETPC APCNTSGFNY VSVHCPDGIH
DVFSSRGPLP AYLGSKTSES TSILQPWERE SKVPLIKRAT RLRDAISWFV EPDSKLAMTI
LSNIHSLTGE EWTKRQHGFK RTGSALHRFS TSRMSHGGFA SQSTAALTRL MATTDTMRDL
GDQNFDFLFQ ATLLYAQITT TVARDGWITS CTDHYHIACK SCLRPIEEIT LDSSMDYTPP
DVSHVLKTWR NGEGSWGQEI KQIYPLEGNW KNLAPAEQSY QVGRCIGFLY GDLAYRKSTH
AEDSSLFPLS IQGRIRGRGF LKGLLDGLMR ASCCQVIHRR SLAHLKRPAN AVYGGLIYLI
DKLSVSPPFL SLTRSGPIRD ELETIPHKIP TSYPTSNRDM GVIVRNYFKY QCRLIEKGKY
RSHYSQLWLF SDVLSIDFIG PFSISTTLLQ ILYKPFLSGK DKNELRELAN LSSLLRSGEG
WEDIHVKFFT KDILLCPEEI RHACKFGIAK DNNKDMSYPP WGRESRGTIT TIPVYYTTTP
YPKMLEMPPR IQNPLLSGIR LGQLPTGAHY KIRSILHGMG IHYRDFLSCG DGSGGMTAAL
LRENVHSRGI FNSLLELSGS VMRGASPEPP SALETLGGDK SRCVNGETCW EYPSDLCDPR
TWDYFLRLKA GLGLQIDLIV MDMEVRDSST SLKIETNVRN YVHRILDEQG VLIYKTYGTY
ICESEKNAVT ILGPMFKTVD LVQTEFSSSQ TSEVYMVCKG LKKLIDEPNP DWSSINESWK
NLYAFQSSEQ EFARAKKVST YFTLTGIPSQ FIPDPFVNIE TMLQIFGVPT GVSHAAALKS
SDRPADLLTI SLFYMAIISY YNINHIRVGP IPPNPPSDGI AQNVGIAITG ISFWLSLMEK
DIPLYQQCLA VIQQSFPIRW EAVSVKGGYK QKWSTRGDGL PKDTRISDSL APIGNWIRSL
ELVRNQVRLN PFNEILFNQL CRTVDNHLKW SNLRRNTGMI EWINRRISKE DRSILMLKSD
LHEENSWRD
