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 27-MAR-2024, entry version 166. 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 Autographiviridae; Studiervirinae; Teseptimavirus; Teseptimavirus T7. 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 ACTIVITY REGULATION. RX PubMed=32937646; DOI=10.1038/s41586-020-2762-2; RA Bernheim A., Millman A., Ofir G., Meitav G., Avraham C., Shomar H., RA Rosenberg M.M., Tal N., Melamed S., Amitai G., Sorek R.; RT "Prokaryotic viperins produce diverse antiviral molecules."; RL Nature 589:120-124(2021). RN [17] 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 [18] 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 -!- ACTIVITY REGULATION: Inhibited by the product of prokaryotic viperins CC (as well as the human ortholog RSAD2), which make various 3'-deoxy- CC 3',4'-didehydro-NTPs, suggesting these modifed nucleotides act as CC specific chain terminators for this RNA polymerase. CC {ECO:0000269|PubMed:32937646}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8DH0; X-ray; 2.90 A; B/F/J/N=1-883. DR PDB; 8DH1; X-ray; 2.65 A; B/E/I/L=1-883. DR PDB; 8DH2; X-ray; 2.90 A; B/E/I/L=1-883. DR PDB; 8DH3; X-ray; 3.00 A; B/E/I/M=1-883. DR PDB; 8DH4; X-ray; 2.80 A; B/E/I/M=1-883. DR PDB; 8DH5; X-ray; 2.85 A; B/E/I/M=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 PDBsum; 8DH0; -. DR PDBsum; 8DH1; -. DR PDBsum; 8DH2; -. DR PDBsum; 8DH3; -. DR PDBsum; 8DH4; -. DR PDBsum; 8DH5; -. 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 OrthoDB; 309at10239; -. 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:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB. DR Gene3D; 1.10.287.260; -; 1. DR Gene3D; 1.10.287.280; -; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 1.10.1320.10; DNA-directed RNA polymerase, N-terminal domain; 1. DR InterPro; IPR024075; DNA-dir_RNA_pol_helix_hairp_sf. DR InterPro; IPR046950; DNA-dir_Rpol_C_phage-type. 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; DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR10102:SF0; DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL; 1. DR Pfam; PF00940; RNA_pol; 1. DR Pfam; PF14700; RPOL_N; 1. DR SMART; SM01311; RPOL_N; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 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 TURN 157..159 FT /evidence="ECO:0007829|PDB:8DH5" 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 224..226 FT /evidence="ECO:0007829|PDB:8DH2" 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 TURN 348..350 FT /evidence="ECO:0007829|PDB:8DH4" 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 593..595 FT /evidence="ECO:0007829|PDB:8DH0" FT STRAND 597..602 FT /evidence="ECO:0007829|PDB:1MSW" FT STRAND 605..610 FT /evidence="ECO:0007829|PDB:8DH1" 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 808..810 FT /evidence="ECO:0007829|PDB:8DH1" 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..857 FT /evidence="ECO:0007829|PDB:8DH1" FT STRAND 858..861 FT /evidence="ECO:0007829|PDB:1H38" 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 //