RPOL_BPT7
ID RPOL_BPT7 Reviewed; 883 AA.
AC P00573; Q38543;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=T7 RNA polymerase;
DE AltName: Full=DNA-directed RNA polymerase;
DE EC=2.7.7.6 {ECO:0000269|PubMed:8133519};
GN OrderedLocusNames=1;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=6708104; DOI=10.1016/0022-2836(84)90194-3;
RA Moffatt B.A., Dunn J.J., Studier F.W.;
RT "Nucleotide sequence of the gene for bacteriophage T7 RNA polymerase.";
RL J. Mol. Biol. 173:265-269(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7310873; DOI=10.1016/0022-2836(81)90187-x;
RA Stahl S.J., Zinn K.;
RT "Nucleotide sequence of the cloned gene for bacteriophage T7 RNA
RT polymerase.";
RL J. Mol. Biol. 148:481-485(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6093820;
RA Grachev M.A., Pletnev A.G.;
RT "Phage T7 RNA-polymerase: gene cloning and its structure.";
RL Bioorg. Khim. 10:824-843(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59 AND 829-883.
RX PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
RA Dunn J.J., Studier F.W.;
RT "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to
RT the beginning of gene 4.";
RL J. Mol. Biol. 148:303-330(1981).
RN [6]
RP FUNCTION IN DNA REPLICATION.
RX PubMed=7373707; DOI=10.1128/jvi.34.1.136-141.1980;
RA Hinkle D.C.;
RT "Evidence for direct involvement of T7 RNA polymerase bacteriophage DNA
RT replication.";
RL J. Virol. 34:136-141(1980).
RN [7]
RP FUNCTION IN DNA REPLICATION.
RX PubMed=6945573; DOI=10.1073/pnas.78.7.4107;
RA Romano L.J., Tamanoi F., Richardson C.C.;
RT "Initiation of DNA replication at the primary origin of bacteriophage T7 by
RT purified proteins: requirement for T7 RNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4107-4111(1981).
RN [8]
RP FUNCTION.
RX PubMed=3415967; DOI=10.1021/bi00411a012;
RA Martin C.T., Muller D.K., Coleman J.E.;
RT "Processivity in early stages of transcription by T7 RNA polymerase.";
RL Biochemistry 27:3966-3974(1988).
RN [9]
RP ACTIVE SITE LYS-631, AND MUTAGENESIS OF LYS-631.
RX PubMed=1847871; DOI=10.1111/j.1432-1033.1991.tb15773.x;
RA Maksimova T.G., Mustayev A.A., Zaychikov E.F., Lyakhov D.L.,
RA Tunitskaya V.L., Akbarov A.K., Luchin S.V., Rechinsky V.O., Chernov B.K.,
RA Kochetkov S.N.;
RT "Lys631 residue in the active site of the bacteriophage T7 RNA polymerase.
RT Affinity labeling and site-directed mutagenesis.";
RL Eur. J. Biochem. 195:841-847(1991).
RN [10]
RP MUTAGENESIS OF LYS-172.
RX PubMed=1470170;
RA Lyakhov D.L., Ilgenfrits H., Chernov B.K., Dragan S.M., Rechinsky V.O.,
RA Pokholok D.K., Tunitskaya V.L., Kochetkov S.N.;
RT "Site-specific mutagenesis of residue Lys-172 of phage T7 RNA polymerase:
RT characterization of transcription properties of mutant proteins.";
RL Mol. Biol. (Mosk.) 26:1022-1035(1992).
RN [11]
RP ACTIVE SITE ASP-537; LYS-631; ASP-812, AND MUTAGENESIS.
RX PubMed=8492813; DOI=10.1007/bf00292005;
RA Rechinsky V.O., Kostyuk D.A., Lyakhov D.L., Chernov B.K., Kochetkov S.N.;
RT "Random mutagenesis of the gene for bacteriophage T7 RNA polymerase.";
RL Mol. Gen. Genet. 238:455-458(1993).
RN [12]
RP MUTAGENESIS.
RX PubMed=8462683; DOI=10.1016/0014-5793(93)81646-h;
RA Rechinsky V.O., Tunitskaya V.L., Dragan S.M., Kostyuk D.A., Kochetkov S.N.;
RT "Tyr-571 is involved in the T7 RNA polymerase binding to its promoter.";
RL FEBS Lett. 320:9-12(1993).
RN [13]
RP MUTAGENESIS.
RX PubMed=8133519; DOI=10.1006/jmbi.1994.1205;
RA Osumi-Davis P., Sreerama N., Volkin D.B., Middaugh C.R., Woody R.W.,
RA Woody A.-Y.M.;
RT "Bacteriophage T7 RNA polymerase and its active-site mutants. Kinetic,
RT spectroscopic and calorimetric characterization.";
RL J. Mol. Biol. 237:5-19(1994).
RN [14]
RP FUNCTION.
RX PubMed=9192997; DOI=10.1006/jmbi.1997.1016;
RA Zhang X., Studier F.W.;
RT "Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7
RT lysozyme.";
RL J. Mol. Biol. 269:10-27(1997).
RN [15]
RP FUNCTION.
RX PubMed=15223315; DOI=10.1016/j.jmb.2004.05.006;
RA Zhang X., Studier F.W.;
RT "Multiple roles of T7 RNA polymerase and T7 lysozyme during bacteriophage
RT T7 infection.";
RL J. Mol. Biol. 340:707-730(2004).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX PubMed=7688864; DOI=10.1038/364593a0;
RA Sousa R., Chung Y.J., Rose J.P., Wang B.-C.;
RT "Crystal structure of bacteriophage T7 RNA polymerase at 3.3-A
RT resolution.";
RL Nature 364:593-599(1993).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH LYSOZYME.
RX PubMed=9670025; DOI=10.1093/emboj/17.14.4101;
RA Jeruzalmi D., Steitz T.A.;
RT "Structure of T7 RNA polymerase complexed to the transcriptional inhibitor
RT T7 lysozyme.";
RL EMBO J. 17:4101-4113(1998).
CC -!- FUNCTION: Highly processive DNA-dependent RNA polymerase that catalyzes
CC the transcription of class II and class III viral genes. Recognizes a
CC specific promoter sequence and enters first into an 'abortive phase'
CC where very short transcripts are synthesized and released before
CC proceeding to the processive transcription of long RNA chains. Unwinds
CC the double-stranded DNA to expose the coding strand for templating.
CC Participates in the initiation of viral DNA replication presumably by
CC making primers accessible to the DNA polymerase, thus facilitating the
CC DNA opening. Also plays a role in viral DNA packaging, probably by
CC pausing the transcription at the right end of concatemer junction to
CC allow packaging complex recruitment and beginning of the packaging
CC process. {ECO:0000269|PubMed:15223315, ECO:0000269|PubMed:3415967,
CC ECO:0000269|PubMed:6945573, ECO:0000269|PubMed:7373707,
CC ECO:0000269|PubMed:9192997}.
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=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031,
CC ECO:0000255|PROSITE-ProRule:PRU10032, ECO:0000269|PubMed:8133519};
CC -!- SUBUNIT: Monomer. Interacts with T7 lysozyme; this interaction inhibits
CC transcriptional function of T7 RNA polymerase.
CC -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC family. {ECO:0000305}.
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DR EMBL; V01146; CAA24390.1; -; Genomic_DNA.
DR EMBL; V01127; CAA24333.1; -; Genomic_DNA.
DR EMBL; M38308; AAA32569.1; -; Genomic_DNA.
DR PIR; A94615; RNBP17.
DR RefSeq; NP_041960.1; NC_001604.1.
DR PDB; 1ARO; X-ray; 2.80 A; P=1-883.
DR PDB; 1CEZ; X-ray; 2.40 A; A=1-883.
DR PDB; 1H38; X-ray; 2.90 A; A/B/C/D=1-883.
DR PDB; 1MSW; X-ray; 2.10 A; D=1-883.
DR PDB; 1QLN; X-ray; 2.40 A; A=1-883.
DR PDB; 1S0V; X-ray; 3.20 A; A/B/C/D=1-883.
DR PDB; 1S76; X-ray; 2.88 A; D=1-883.
DR PDB; 1S77; X-ray; 2.69 A; D=1-883.
DR PDB; 2PI4; X-ray; 2.50 A; A=6-883.
DR PDB; 2PI5; X-ray; 2.90 A; A=6-883.
DR PDB; 3E2E; X-ray; 3.00 A; A=1-883.
DR PDB; 3E3J; X-ray; 6.70 A; B/C=1-883.
DR PDB; 4RNP; X-ray; 3.00 A; A/B/C=1-883.
DR PDBsum; 1ARO; -.
DR PDBsum; 1CEZ; -.
DR PDBsum; 1H38; -.
DR PDBsum; 1MSW; -.
DR PDBsum; 1QLN; -.
DR PDBsum; 1S0V; -.
DR PDBsum; 1S76; -.
DR PDBsum; 1S77; -.
DR PDBsum; 2PI4; -.
DR PDBsum; 2PI5; -.
DR PDBsum; 3E2E; -.
DR PDBsum; 3E3J; -.
DR PDBsum; 4RNP; -.
DR SMR; P00573; -.
DR DIP; DIP-6091N; -.
DR IntAct; P00573; 1.
DR MINT; P00573; -.
DR BindingDB; P00573; -.
DR ChEMBL; CHEMBL1075072; -.
DR GeneID; 1261050; -.
DR KEGG; vg:1261050; -.
DR BRENDA; 2.7.7.6; 736.
DR EvolutionaryTrace; P00573; -.
DR PRO; PR:P00573; -.
DR Proteomes; UP000000840; Genome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.1320.10; -; 1.
DR Gene3D; 1.10.287.260; -; 1.
DR InterPro; IPR024075; DNA-dir_RNA_pol_helix_hairp_sf.
DR InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR037159; RNA_POL_N_sf.
DR InterPro; IPR029262; RPOL_N.
DR PANTHER; PTHR10102; PTHR10102; 1.
DR Pfam; PF00940; RNA_pol; 1.
DR Pfam; PF14700; RPOL_N; 1.
DR SMART; SM01311; RPOL_N; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase; Viral transcription.
FT CHAIN 1..883
FT /note="T7 RNA polymerase"
FT /id="PRO_0000087749"
FT ACT_SITE 537
FT /evidence="ECO:0000269|PubMed:8133519"
FT ACT_SITE 631
FT /evidence="ECO:0000269|PubMed:1847871,
FT ECO:0000269|PubMed:8133519"
FT ACT_SITE 812
FT /evidence="ECO:0000269|PubMed:8133519"
FT MUTAGEN 172
FT /note="K->L,G: No change in activity."
FT /evidence="ECO:0000269|PubMed:1470170"
FT MUTAGEN 563
FT /note="P->A,T: Inactivated."
FT MUTAGEN 571
FT /note="Y->S: Inactivated."
FT MUTAGEN 631
FT /note="K->G: Partially inactivated."
FT /evidence="ECO:0000269|PubMed:1847871"
FT MUTAGEN 631
FT /note="K->L: Partially inactivated."
FT /evidence="ECO:0000269|PubMed:1847871"
FT MUTAGEN 631
FT /note="K->R: Partially inactivated."
FT /evidence="ECO:0000269|PubMed:1847871"
FT MUTAGEN 636
FT /note="T->P: Inactivated."
FT MUTAGEN 639
FT /note="Y->D: Inactivated."
FT MUTAGEN 646
FT /note="F->C: Inactivated."
FT CONFLICT 388..424
FT /note="DKARKSRRISLEFMLEQANKFANHKAIWFPYNMDWRG -> TRLASLAVSAL
FT SSCLSKPISLLTIRPSGSLTTWTGAV (in Ref. 3; CAA24333)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="K -> R (in Ref. 4; AAA32569)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="L -> R (in Ref. 3; CAA24333)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="P -> S (in Ref. 3; CAA24333)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="Y -> H (in Ref. 4; AAA32569)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="L -> P (in Ref. 4; AAA32569)"
FT /evidence="ECO:0000305"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1CEZ"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 30..59
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 71..94
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 101..107
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3E2E"
FT HELIX 134..156
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 191..198
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1S77"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1H38"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1CEZ"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1CEZ"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 332..341
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:1CEZ"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:3E2E"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:2PI4"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1QLN"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:2PI4"
FT HELIX 379..402
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:1ARO"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2PI4"
FT HELIX 438..443
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 453..467
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 475..484
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 496..499
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 508..524
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:1CEZ"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:1ARO"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 541..550
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 559..564
FT /evidence="ECO:0007829|PDB:1ARO"
FT HELIX 570..586
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:1S0V"
FT STRAND 597..602
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:1H38"
FT HELIX 613..621
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 627..635
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 643..653
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 655..660
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 662..666
FT /evidence="ECO:0007829|PDB:1S77"
FT HELIX 670..688
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 690..707
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 713..715
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 718..720
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:2PI5"
FT STRAND 734..737
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 740..746
FT /evidence="ECO:0007829|PDB:1CEZ"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:1S77"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:1CEZ"
FT STRAND 760..769
FT /evidence="ECO:0007829|PDB:1CEZ"
FT HELIX 771..801
FT /evidence="ECO:0007829|PDB:1MSW"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:1S0V"
FT STRAND 811..816
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 818..820
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 821..838
FT /evidence="ECO:0007829|PDB:1MSW"
FT HELIX 841..849
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 852..854
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 855..858
FT /evidence="ECO:0007829|PDB:1ARO"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:2PI5"
FT HELIX 872..876
FT /evidence="ECO:0007829|PDB:1MSW"
FT TURN 879..881
FT /evidence="ECO:0007829|PDB:1S76"
SQ SEQUENCE 883 AA; 98855 MW; 7FBDEAC457842549 CRC64;
MNTINIAKND FSDIELAAIP FNTLADHYGE RLAREQLALE HESYEMGEAR FRKMFERQLK
AGEVADNAAA KPLITTLLPK MIARINDWFE EVKAKRGKRP TAFQFLQEIK PEAVAYITIK
TTLACLTSAD NTTVQAVASA IGRAIEDEAR FGRIRDLEAK HFKKNVEEQL NKRVGHVYKK
AFMQVVEADM LSKGLLGGEA WSSWHKEDSI HVGVRCIEML IESTGMVSLH RQNAGVVGQD
SETIELAPEY AEAIATRAGA LAGISPMFQP CVVPPKPWTG ITGGGYWANG RRPLALVRTH
SKKALMRYED VYMPEVYKAI NIAQNTAWKI NKKVLAVANV ITKWKHCPVE DIPAIEREEL
PMKPEDIDMN PEALTAWKRA AAAVYRKDKA RKSRRISLEF MLEQANKFAN HKAIWFPYNM
DWRGRVYAVS MFNPQGNDMT KGLLTLAKGK PIGKEGYYWL KIHGANCAGV DKVPFPERIK
FIEENHENIM ACAKSPLENT WWAEQDSPFC FLAFCFEYAG VQHHGLSYNC SLPLAFDGSC
SGIQHFSAML RDEVGGRAVN LLPSETVQDI YGIVAKKVNE ILQADAINGT DNEVVTVTDE
NTGEISEKVK LGTKALAGQW LAYGVTRSVT KRSVMTLAYG SKEFGFRQQV LEDTIQPAID
SGKGLMFTQP NQAAGYMAKL IWESVSVTVV AAVEAMNWLK SAAKLLAAEV KDKKTGEILR
KRCAVHWVTP DGFPVWQEYK KPIQTRLNLM FLGQFRLQPT INTNKDSEID AHKQESGIAP
NFVHSQDGSH LRKTVVWAHE KYGIESFALI HDSFGTIPAD AANLFKAVRE TMVDTYESCD
VLADFYDQFA DQLHESQLDK MPALPAKGNL NLRDILESDF AFA
