L_LYCVA
ID L_LYCVA Reviewed; 2210 AA.
AC P14240; Q27V69; Q49K84;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=RNA-directed RNA polymerase L {ECO:0000255|HAMAP-Rule:MF_04086};
DE Short=Protein L {ECO:0000255|HAMAP-Rule:MF_04086};
DE EC=2.7.7.48 {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Large structural protein {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Replicase {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Transcriptase {ECO:0000255|HAMAP-Rule:MF_04086};
DE Includes:
DE RecName: Full=cap-snatching endonuclease {ECO:0000255|HAMAP-Rule:MF_04086};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04086, ECO:0000269|PubMed:29765612};
GN Name=L {ECO:0000255|HAMAP-Rule:MF_04086}; OrderedLocusNames=Segment L;
OS Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11624;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10036; Mesocricetus auratus (Golden hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2705303; DOI=10.1016/0042-6822(89)90163-3;
RA Salvato M.S., Shimomaye E.M., Oldstone M.B.A.;
RT "The primary structure of the lymphocytic choriomeningitis virus L gene
RT encodes a putative RNA polymerase.";
RL Virology 169:377-384(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Armstrong 53b;
RX PubMed=16051837; DOI=10.1128/jvi.79.16.10451-10459.2005;
RA Grande-Perez A., Gomez-Mariano G., Lowenstein P.R., Domingo E.;
RT "Mutagenesis-induced, large fitness variations with an invariant arenavirus
RT consensus genomic nucleotide sequence.";
RL J. Virol. 79:10451-10459(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Armstrong-derived variant Cl13;
RX PubMed=16537369; DOI=10.1073/pnas.0600652103;
RA Flatz L., Bergthaler A., de la Torre J.C., Pinschewer D.D.;
RT "Recovery of an arenavirus entirely from RNA polymerase I/II-driven cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4663-4668(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 161-387; 424-619 AND 1646-1906.
RX PubMed=3318094; DOI=10.1016/0042-6822(87)90138-3;
RA Singh M.K., Fuller-Pace F.V., Buchmeier M.J., Southern P.J.;
RT "Analysis of the genomic L RNA segment from lymphocytic choriomeningitis
RT virus.";
RL Virology 161:448-456(1987).
RN [5]
RP FUNCTION.
RX PubMed=7682625; DOI=10.1128/jvi.67.5.2621-2627.1993;
RA Meyer B.J., Southern P.J.;
RT "Concurrent sequence analysis of 5' and 3' RNA termini by intramolecular
RT circularization reveals 5' nontemplated bases and 3' terminal heterogeneity
RT for lymphocytic choriomeningitis virus mRNAs.";
RL J. Virol. 67:2621-2627(1993).
RN [6]
RP SUBUNIT, AND MUTAGENESIS OF ASP-1182; SER-1320 AND ASP-1321.
RX PubMed=15890965; DOI=10.1128/jvi.79.11.7262-7268.2005;
RA Sanchez A.B., de la Torre J.C.;
RT "Genetic and biochemical evidence for an oligomeric structure of the
RT functional L polymerase of the prototypic arenavirus lymphocytic
RT choriomeningitis virus.";
RL J. Virol. 79:7262-7268(2005).
RN [7]
RP REVIEW.
RX PubMed=28418734; DOI=10.1080/1040841x.2017.1307805;
RA Amroun A., Priet S., de Lamballerie X., Querat G.;
RT "Bunyaviridae RdRps: structure, motifs, and RNA synthesis machinery.";
RL Crit. Rev. Microbiol. 43:753-778(2017).
RN [8]
RP REVIEW.
RX PubMed=31948728; DOI=10.1016/j.tim.2019.12.006;
RA Olschewski S., Cusack S., Rosenthal M.;
RT "The Cap-Snatching Mechanism of Bunyaviruses.";
RL Trends Microbiol. 28:293-303(2020).
RN [9] {ECO:0007744|PDB:3JSB}
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 2-197, FUNCTION, DOMAIN,
RP MUTAGENESIS OF GLU-51; ASP-89; GLU-102; LYS-115; ASP-119 AND LYS-122, AND
RP COFACTOR.
RX PubMed=20862324; DOI=10.1371/journal.ppat.1001038;
RA Morin B., Coutard B., Lelke M., Ferron F., Kerber R., Jamal S.,
RA Frangeul A., Baronti C., Charrel R., de Lamballerie X., Vonrhein C.,
RA Lescar J., Bricogne G., Guenther S., Canard B.;
RT "The N-terminal domain of the arenavirus L protein is an RNA endonuclease
RT essential in mRNA transcription.";
RL PLoS Pathog. 6:E1001038-E1001038(2010).
RN [10] {ECO:0007744|PDB:5LTF, ECO:0007744|PDB:5LTN, ECO:0007744|PDB:5LTS, ECO:0007744|PDB:5T2T}
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 2-197, COFACTOR, CATALYTIC
RP ACTIVITY, AND DOMAIN.
RX PubMed=29765612; DOI=10.1107/s2052252518001021;
RA Saez-Ayala M., Yekwa E.L., Carcelli M., Canard B., Alvarez K., Ferron F.;
RT "Crystal structures of Lymphocytic choriomeningitis virus endonuclease
RT domain complexed with diketo-acid ligands.";
RL IUCrJ 5:223-235(2018).
CC -!- FUNCTION: RNA-dependent RNA polymerase, which is responsible for the
CC replication and transcription of the viral RNA genome using antigenomic
CC RNA as an intermediate. During transcription, synthesizes subgenomic
CC RNAs and assures their capping by a cap-snatching mechanism, which
CC involves the endonuclease activity cleaving the host capped pre-mRNAs.
CC These short capped RNAs are then used as primers for viral
CC transcription. The 3'-end of subgenomic mRNAs molecules are
CC heterogeneous and not polyadenylated. The replicase function is to
CC direct synthesis of antigenomic and genomic RNA which are encapsidated
CC and non capped. As a consequence of the use of the same enzyme for both
CC transcription and replication, these mechanisms need to be well
CC coordinated. These processes may be regulated by proteins N and Z in a
CC dose-dependent manner. {ECO:0000255|HAMAP-Rule:MF_04086,
CC ECO:0000269|PubMed:7682625}.
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|HAMAP-Rule:MF_04086};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site.
CC The divalent metal ions are crucial for catalytic activity.
CC {ECO:0000255|HAMAP-Rule:MF_04086};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC Note=For polymerase activity. {ECO:0000255|HAMAP-Rule:MF_04086};
CC -!- SUBUNIT: Homomultimer; the oligomeric structure is essential for the
CC polymerase activity. Interacts with nucleoprotein N. Interacts with
CC protein Z; this interaction inhibits viral transcription and
CC replication. {ECO:0000255|HAMAP-Rule:MF_04086}.
CC -!- INTERACTION:
CC P14240; P09992: N; NbExp=2; IntAct=EBI-26968662, EBI-6149284;
CC P14240; O00571: DDX3X; Xeno; NbExp=2; IntAct=EBI-26968662, EBI-353779;
CC P14240; P11940: PABPC1; Xeno; NbExp=2; IntAct=EBI-26968662, EBI-81531;
CC P14240; P19474: TRIM21; Xeno; NbExp=2; IntAct=EBI-26968662, EBI-81290;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04086}. Host
CC cytoplasm {ECO:0000255|HAMAP-Rule:MF_04086}.
CC -!- DOMAIN: The N-terminus contains the endonuclease activity (endoN). The
CC central region contains the RdRp activity. {ECO:0000255|HAMAP-
CC Rule:MF_04086, ECO:0000269|PubMed:20862324}.
CC -!- MISCELLANEOUS: Classified as His(-) endonuclease since it does not have
CC a histidine upstream of the active site that coordinates the first
CC cation. His(-) endonucleases display very low activity in vitro,
CC although they are clearly active in vivo. {ECO:0000255|HAMAP-
CC Rule:MF_04086}.
CC -!- SIMILARITY: Belongs to the Bunyavirales RNA polymerase family.
CC {ECO:0000255|HAMAP-Rule:MF_04086}.
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DR EMBL; J04331; AAA66591.1; -; Genomic_RNA.
DR EMBL; AY847351; AAX49344.1; -; Genomic_RNA.
DR EMBL; DQ361066; ABC96004.1; -; Genomic_RNA.
DR EMBL; M18381; AAA46258.1; ALT_SEQ; Genomic_RNA.
DR EMBL; M18382; AAA46259.1; -; Genomic_RNA.
DR EMBL; M18383; AAA46260.1; ALT_SEQ; Genomic_RNA.
DR PIR; A30181; RRXPLC.
DR RefSeq; NP_694845.1; NC_004291.1.
DR PDB; 3JSB; X-ray; 2.13 A; A/B=2-197.
DR PDB; 5LTF; X-ray; 2.43 A; A/B=2-197.
DR PDB; 5LTN; X-ray; 1.88 A; A/B=2-197.
DR PDB; 5LTS; X-ray; 2.51 A; A/B=2-197.
DR PDB; 5T2T; X-ray; 1.97 A; A/B=2-197.
DR PDBsum; 3JSB; -.
DR PDBsum; 5LTF; -.
DR PDBsum; 5LTN; -.
DR PDBsum; 5LTS; -.
DR PDBsum; 5T2T; -.
DR SMR; P14240; -.
DR IntAct; P14240; 228.
DR MINT; P14240; -.
DR PRIDE; P14240; -.
DR GeneID; 956589; -.
DR KEGG; vg:956589; -.
DR EvolutionaryTrace; P14240; -.
DR Proteomes; UP000002474; Genome.
DR Proteomes; UP000121528; Genome.
DR Proteomes; UP000204492; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-UniRule.
DR GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB.
DR GO; GO:0039696; P:RNA-templated viral transcription; IDA:UniProtKB.
DR HAMAP; MF_04086; ARENA_L; 1.
DR InterPro; IPR026382; CapSnatchArena.
DR InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR InterPro; IPR010453; RNA_pol_arenavir.
DR Pfam; PF06317; Arena_RNA_pol; 1.
DR Pfam; PF17296; ArenaCapSnatch; 1.
DR PIRSF; PIRSF000836; L_ArenaV; 1.
DR PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cap snatching; Host cytoplasm; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..2210
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000079198"
FT DOMAIN 1166..1360
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT REGION 26..287
FT /note="Endonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT ACT_SITE 115
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 1322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT VARIANT 108
FT /note="S -> T (in strain: Isolate Armstrong 53b and Isolate
FT Armstrong-derived variant Cl13)"
FT VARIANT 1079
FT /note="K -> Q (in strain: Isolate Armstrong-derived variant
FT Cl13)"
FT VARIANT 1513
FT /note="T -> K (in strain: Isolate Armstrong 53b and Isolate
FT Armstrong-derived variant Cl13)"
FT VARIANT 2185
FT /note="I -> T (in strain: Isolate Armstrong 53b and Isolate
FT Armstrong-derived variant Cl13)"
FT MUTAGEN 51
FT /note="E->A: About 70% loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:20862324"
FT MUTAGEN 89
FT /note="D->A: About 50% loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:20862324"
FT MUTAGEN 102
FT /note="E->A: About 90% loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:20862324"
FT MUTAGEN 115
FT /note="K->A: About 80% loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:20862324"
FT MUTAGEN 119
FT /note="D->A: Complete loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:20862324"
FT MUTAGEN 122
FT /note="K->A: About 70% loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:20862324"
FT MUTAGEN 1182
FT /note="D->A: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:15890965"
FT MUTAGEN 1182
FT /note="D->E: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:15890965"
FT MUTAGEN 1182
FT /note="D->N: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:15890965"
FT MUTAGEN 1320
FT /note="S->G: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:15890965"
FT MUTAGEN 1321
FT /note="D->A: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:15890965"
FT MUTAGEN 1321
FT /note="D->N: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:15890965"
FT CONFLICT 164
FT /note="L -> Y (in Ref. 4; AAA46258)"
FT CONFLICT 354
FT /note="Q -> R (in Ref. 4; AAA46258)"
FT CONFLICT 361
FT /note="K -> E (in Ref. 4; AAA46258)"
FT CONFLICT 382
FT /note="H -> D (in Ref. 4; AAA46258)"
FT CONFLICT 552
FT /note="C -> S (in Ref. 4; AAA46259)"
FT CONFLICT 1727
FT /note="R -> L (in Ref. 4; AAA46260)"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 35..58
FT /evidence="ECO:0007829|PDB:5LTN"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:5LTN"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5LTN"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:5LTN"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 154..179
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:5LTN"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5LTN"
SQ SEQUENCE 2210 AA; 254532 MW; 470C8E623176AFD3 CRC64;
MDEIISELRE LCLNYIEQDE RLSRQKLNFL GQREPRMVLI EGLKLLSRCI EIDSADKSGC
THNHDDKSVE TILVESGIVC PGLPLIIPDG YKLIDNSLIL LECFVRSSPA SFEKKFIEDT
NKLACIREDL AVAGVTLVPI VDGRCDYDNS FMPEWANFKF RDLLFKLLEY SNQNEKVFEE
SEYFRLCESL KTTIDKRSGM DSMKILKDAR STHNDEIMRM CHEGINPNMS CDDVVFGINS
LFSRFRRDLE SGKLKRNFQK VNPEGLIKEF SELYENLADS DDILTLSREA VESCPLMRFI
TAETHGHERG SETSTEYERL LSMLNKVKSL KLLNTRRRQL LNLDVLCLSS LIKQSKFKGL
KNDKHWVGCC YSSVNDRLVS FHSTKEEFIR LLRNRKKSKV FRKVSFEELF RASISEFIAK
IQKCLLVVGL SFEHYGLSEH LEQECHIPFT EFENFMKIGA HPIMYYTKFE DYNFQPSTEQ
LKNIQSLRRL SSVCLALTNS MKTSSVARLR QNQIGSVRYQ VVECKEVFCQ VIKLDSEEYH
LLYQKTGESS RCYSIQGPDG HLISFYADPK RFFLPIFSDE VLYNMIDIMI SWIRSCPDLK
DCLTDIEVAL RTLLLLMLTN PTKRNQKQVQ SVRYLVMAIV SDFSSTSLMD KLREDLITPA
EKVVYKLLRF LIKTIFGTGE KVLLSAKFKF MLNVSYLCHL ITKETPDRLT DQIKCFEKFF
EPKSQFGFFV NPKEAITPEE ECVFYEQMKR FTSKEIDCQH TTPGVNLEAF SLMVSSFNNG
TLIFKGEKKL NSLDPMTNSG CATALDLASN KSVVVNKHLN GERLLEYDFN KLLVSAVSQI
TESFVRKQKY KLSHSDYEYK VSKLVSRLVI GSKGEETGRS EDNLAEICFD GEEETSFFKS
LEEKVNTTIA RYRRGRRAND KGDGEKLTNT KGLHHLQLIL TGKMAHLRKV ILSEISFHLV
EDFDPSCLTN DDMKFICEAV EGSTELSPLY FTSVIKDQCG LDEMAKNLCR KFFSENDWFS
CMKMILLQMN ANAYSGKYRH MQRQGLNFKF DWDKLEEDVR ISERESNSES LSKALSLTKC
MSAALKNLCF YSEESPTSYT SVGPDSGRLK FALSYKEQVG GNRELYIGDL RTKMFTRLIE
DYFESFSSFF SGSCLNNDKE FENAILSMTI NVREGFLNYS MDHSKWGPMM CPFLFLMFLQ
NLKLGDDQYV RSGKDHVSTL LTWHMHKLVE VPFPVVNAMM KSYVKSKLKL LRGSETTVTE
RIFRQYFEMG IVPSHISSLI DMGQGILHNA SDFYGLLSER FINYCIGVIF GERPEAYTSS
DDQITLFDRR LSDLVVSDPE EVLVLLEFQS HLSGLLNKFI SPKSVAGRFA AEFKSRFYVW
GEEVPLLTKF VSAALHNVKC KEPHQLCETI DTIADQAIAN GVPVSLVNSI QRRTLDLLKY
ANFPLDPFLL NTNTDVKDWL DGSRGYRIQR LIEELCPNET KVVRKLVRKL HHKLKNGEFN
EEFFLDLFNR DKTEAILQLG DLLGLEEDLN QLADVNWLNL NEMFPLRMVL RQKVVYPSVM
TFQEERIPSL IKTLQNKLCS KFTRGAQKLL SEAINKSAFQ SCISSGFIGL CKTLGSRCVR
NKNRENLYIK KLLEDLTTDD HVTRVCNRDG ITLYICDKQS HPEAHRDHIC LLRPLLWDYI
CISLSNSFEL GVWVLAEPTK GKNNSENLTL KHLNPCDYVA RKPESSRLLE DKVNLNQVIQ
SVRRLYPKIF EDQLLPFMSD MSSKNMRWSP RIKFLDLCVL IDINSESLSL ISHVVKWKRD
EHYTVLFSDL ANSHQRSDSS LVDEFVVSTR DVCKNFLKQV YFESFVREFV ATTRTLGNFS
WFPHKEMMPS EDGAEALGPF QSFVSKVVNK NVERPMFRND LQFGFGWFSY RMGDVVCNAA
MLIRQGLTNP KAFKSLKDLW DYMLNYTKGV LEFSISVDFT HNQNNTDCLR KFSLIFLVRC
QLQNPGVAEL LSCSHLFKGE IDRRMLDECL HLLRTDSVFK VNDGVFDIRS EEFEDYMEDP
LILGDSLELE LLGSKRILDG IRSIDFERVG PEWEPVPLTV KMGALFEGRN LVQNIIVKLE
TKDMKVFLAG LEGYEKISDV LGNLFLHRFR TGEHLLGSEI SVILQELCID RSILLIPLSL
LPDWFAFKDC RLCFSKSRST LMYEIVGGRF RLKGRSCDDW LGGSVAEDID
