MFD_ECOLI
ID MFD_ECOLI Reviewed; 1148 AA.
AC P30958; P77592;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000255|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000255|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000255|HAMAP-Rule:MF_00969};
GN OrderedLocusNames=b1114, JW1100;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND DNA-BINDING.
RX PubMed=8465200; DOI=10.1126/science.8465200;
RA Selby C.P., Sancar A.;
RT "Molecular mechanism of transcription-repair-coupling.";
RL Science 260:53-58(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, DNA-BINDING, INTERACTION WITH UVRA AND RNAP, AND DOMAIN.
RX PubMed=7876261; DOI=10.1074/jbc.270.9.4882;
RA Selby C.P., Sancar A.;
RT "Structure and function of transcription-repair coupling factor. I.
RT Structural domains and binding properties.";
RL J. Biol. Chem. 270:4882-4889(1995).
RN [6]
RP FUNCTION, AND LACK OF HELICASE ACTIVITY.
RX PubMed=7876262; DOI=10.1074/jbc.270.9.4890;
RA Selby C.P., Sancar A.;
RT "Structure and function of transcription-repair coupling factor. II.
RT Catalytic properties.";
RL J. Biol. Chem. 270:4890-4895(1995).
RN [7]
RP FUNCTION, AND INTERACTION WITH RNAP.
RX PubMed=12086674; DOI=10.1016/s0092-8674(02)00769-9;
RA Park J.S., Marr M.T., Roberts J.W.;
RT "E. coli transcription repair coupling factor (Mfd protein) rescues
RT arrested complexes by promoting forward translocation.";
RL Cell 109:757-767(2002).
RN [8]
RP CRYSTALLIZATION.
RX PubMed=16511235; DOI=10.1107/s1744309105035876;
RA Deaconescu A.M., Darst S.A.;
RT "Crystallization and preliminary structure determination of Escherichia
RT coli Mfd, the transcription-repair coupling factor.";
RL Acta Crystallogr. F 61:1062-1064(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), AND DOMAIN.
RX PubMed=16469698; DOI=10.1016/j.cell.2005.11.045;
RA Deaconescu A.M., Chambers A.L., Smith A.J., Nickels B.E., Hochschild A.,
RA Savery N.J., Darst S.A.;
RT "Structural basis for bacterial transcription-coupled DNA repair.";
RL Cell 124:507-520(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-333, AND DOMAIN.
RX PubMed=16309703; DOI=10.1016/j.jmb.2005.10.033;
RA Assenmacher N., Wenig K., Lammens A., Hopfner K.P.;
RT "Structural basis for transcription-coupled repair: the N terminus of Mfd
RT resembles UvrB with degenerate ATPase motifs.";
RL J. Mol. Biol. 355:675-683(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-470, FUNCTION, AND DOMAIN.
RX PubMed=19700770; DOI=10.1093/nar/gkp680;
RA Murphy M.N., Gong P., Ralto K., Manelyte L., Savery N.J., Theis K.;
RT "An N-terminal clamp restrains the motor domains of the bacterial
RT transcription-repair coupling factor Mfd.";
RL Nucleic Acids Res. 37:6042-6053(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 127-213 IN COMPLEX WITH UVRA, AND
RP DOMAIN.
RX PubMed=22331906; DOI=10.1073/pnas.1115105109;
RA Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N.;
RT "Nucleotide excision repair (NER) machinery recruitment by the
RT transcription-repair coupling factor involves unmasking of a conserved
RT intramolecular interface.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3353-3358(2012).
CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC release of RNAP and its truncated transcript from the DNA, and
CC recruitment of nucleotide excision repair machinery to the damaged
CC site. Can also dissociate RNAP that is blocked by low concentration of
CC nucleoside triphosphates or by physical obstruction, such as bound
CC proteins. In addition, can rescue arrested complexes by promoting
CC forward translocation. Has ATPase activity, which is required for
CC removal of stalled RNAP, but seems to lack helicase activity. May act
CC through a translocase activity that rewinds upstream DNA, leading
CC either to translocation or to release of RNAP when the enzyme active
CC site cannot continue elongation. {ECO:0000255|HAMAP-Rule:MF_00969,
CC ECO:0000269|PubMed:12086674, ECO:0000269|PubMed:19700770,
CC ECO:0000269|PubMed:7876261, ECO:0000269|PubMed:7876262,
CC ECO:0000269|PubMed:8465200}.
CC -!- SUBUNIT: Monomer. Interacts with UvrA and RNAP.
CC {ECO:0000269|PubMed:12086674, ECO:0000269|PubMed:22331906,
CC ECO:0000269|PubMed:7876261, ECO:0000269|PubMed:8465200}.
CC -!- INTERACTION:
CC P30958; P0A698: uvrA; NbExp=2; IntAct=EBI-554211, EBI-552091;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}.
CC -!- DOMAIN: Consists of a compact arrangement of structured domains linked
CC by long, flexible linkers. The N-terminal region interacts with UvrA,
CC the central region interacts with RNAP, and the C-terminal DNA
CC translocase region possesses ATPase activity. Activity is regulated by
CC a conformational switch from a dormant closed state to an active open
CC state upon substrate binding. {ECO:0000269|PubMed:16309703,
CC ECO:0000269|PubMed:16469698, ECO:0000269|PubMed:19700770,
CC ECO:0000269|PubMed:22331906, ECO:0000269|PubMed:7876261}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000255|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000255|HAMAP-Rule:MF_00969}.
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DR EMBL; U00096; AAC74198.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35929.1; -; Genomic_DNA.
DR PIR; G64855; G64855.
DR RefSeq; NP_415632.1; NC_000913.3.
DR RefSeq; WP_001115094.1; NZ_SSZK01000019.1.
DR PDB; 2B2N; X-ray; 2.10 A; A/B=1-333.
DR PDB; 2EYQ; X-ray; 3.20 A; A/B=1-1148.
DR PDB; 3HJH; X-ray; 1.95 A; A=1-470.
DR PDB; 4DFC; X-ray; 2.80 A; A/C=127-213.
DR PDB; 6X26; EM; 4.10 A; A=1-1148.
DR PDB; 6X2F; EM; 4.00 A; A=1-1148.
DR PDB; 6X2N; EM; 3.90 A; A=1-1148.
DR PDB; 6X43; EM; 3.60 A; A=1-1148.
DR PDB; 6X4W; EM; 3.80 A; A=1-1148.
DR PDB; 6X4Y; EM; 3.60 A; A=1-1148.
DR PDB; 6X50; EM; 3.30 A; A=1-1148.
DR PDB; 6XEO; EM; 5.50 A; A=1-1148.
DR PDB; 6YHZ; NMR; -; A=472-547.
DR PDBsum; 2B2N; -.
DR PDBsum; 2EYQ; -.
DR PDBsum; 3HJH; -.
DR PDBsum; 4DFC; -.
DR PDBsum; 6X26; -.
DR PDBsum; 6X2F; -.
DR PDBsum; 6X2N; -.
DR PDBsum; 6X43; -.
DR PDBsum; 6X4W; -.
DR PDBsum; 6X4Y; -.
DR PDBsum; 6X50; -.
DR PDBsum; 6XEO; -.
DR PDBsum; 6YHZ; -.
DR AlphaFoldDB; P30958; -.
DR SMR; P30958; -.
DR BioGRID; 4260086; 165.
DR ComplexPortal; CPX-2155; TRCF-UvrA complex.
DR DIP; DIP-10199N; -.
DR IntAct; P30958; 17.
DR STRING; 511145.b1114; -.
DR jPOST; P30958; -.
DR PaxDb; P30958; -.
DR PRIDE; P30958; -.
DR EnsemblBacteria; AAC74198; AAC74198; b1114.
DR EnsemblBacteria; BAA35929; BAA35929; BAA35929.
DR GeneID; 945681; -.
DR KEGG; ecj:JW1100; -.
DR KEGG; eco:b1114; -.
DR PATRIC; fig|511145.12.peg.1158; -.
DR EchoBASE; EB1576; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_2_6; -.
DR InParanoid; P30958; -.
DR OMA; WAPPCRE; -.
DR PhylomeDB; P30958; -.
DR BioCyc; EcoCyc:EG11619-MON; -.
DR EvolutionaryTrace; P30958; -.
DR PRO; PR:P30958; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0015616; F:DNA translocase activity; IDA:EcoCyc.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:EcoliWiki.
DR GO; GO:0006281; P:DNA repair; IMP:EcoliWiki.
DR GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoliWiki.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IDA:EcoCyc.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IDA:EcoliWiki.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.1150.50; -; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR036101; CarD-like/TRCF_dom_sf.
DR InterPro; IPR003711; CarD-like/TRCF_domain.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004576; Mfd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR Pfam; PF02559; CarD_CdnL_TRCF; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF03461; TRCF; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM01058; CarD_TRCF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00982; TRCF; 1.
DR SUPFAM; SSF141259; SSF141259; 1.
DR SUPFAM; SSF143517; SSF143517; 1.
DR SUPFAM; SSF52540; SSF52540; 4.
DR TIGRFAMs; TIGR00580; mfd; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1148
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000102166"
FT DOMAIN 615..776
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 798..951
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT MOTIF 729..732
FT /note="DEEH box"
FT BINDING 628..635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT CONFLICT 365
FT /note="A -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6X50"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:4DFC"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:6X50"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:3HJH"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 201..212
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2B2N"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 288..306
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6X50"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 372..380
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:3HJH"
FT TURN 394..398
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:3HJH"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:3HJH"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:3HJH"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 467..472
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 489..503
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 518..522
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 523..528
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 549..576
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 587..595
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 603..617
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 632..635
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 636..646
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 659..672
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 674..677
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 689..700
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 705..709
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 712..715
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 721..730
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 736..746
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 749..757
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 761..767
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 768..770
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 771..775
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 786..792
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 795..806
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 807..809
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 811..815
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 822..832
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 847..858
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 864..869
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 872..874
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 880..885
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 886..889
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 893..900
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:6X50"
FT STRAND 910..916
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 924..933
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 941..959
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 961..970
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 972..988
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 995..997
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 1014..1016
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 1020..1032
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 1036..1050
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 1055..1073
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 1078..1080
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 1082..1088
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 1097..1106
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 1108..1110
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 1111..1114
FT /evidence="ECO:0007829|PDB:2EYQ"
FT TURN 1115..1117
FT /evidence="ECO:0007829|PDB:2EYQ"
FT STRAND 1118..1122
FT /evidence="ECO:0007829|PDB:2EYQ"
FT HELIX 1128..1143
FT /evidence="ECO:0007829|PDB:2EYQ"
SQ SEQUENCE 1148 AA; 129983 MW; 8E0D149306C8C31C CRC64;
MPEQYRYTLP VKAGEQRLLG ELTGAACATL VAEIAERHAG PVVLIAPDMQ NALRLHDEIS
QFTDQMVMNL ADWETLPYDS FSPHQDIISS RLSTLYQLPT MQRGVLIVPV NTLMQRVCPH
SFLHGHALVM KKGQRLSRDA LRTQLDSAGY RHVDQVMEHG EYATRGALLD LFPMGSELPY
RLDFFDDEID SLRVFDVDSQ RTLEEVEAIN LLPAHEFPTD KAAIELFRSQ WRDTFEVKRD
PEHIYQQVSK GTLPAGIEYW QPLFFSEPLP PLFSYFPANT LLVNTGDLET SAERFQADTL
ARFENRGVDP MRPLLPPQSL WLRVDELFSE LKNWPRVQLK TEHLPTKAAN ANLGFQKLPD
LAVQAQQKAP LDALRKFLET FDGPVVFSVE SEGRREALGE LLARIKIAPQ RIMRLDEASD
RGRYLMIGAA EHGFVDTVRN LALICESDLL GERVARRRQD SRRTINPDTL IRNLAELHIG
QPVVHLEHGV GRYAGMTTLE AGGITGEYLM LTYANDAKLY VPVSSLHLIS RYAGGAEENA
PLHKLGGDAW SRARQKAAEK VRDVAAELLD IYAQRAAKEG FAFKHDREQY QLFCDSFPFE
TTPDQAQAIN AVLSDMCQPL AMDRLVCGDV GFGKTEVAMR AAFLAVDNHK QVAVLVPTTL
LAQQHYDNFR DRFANWPVRI EMISRFRSAK EQTQILAEVA EGKIDILIGT HKLLQSDVKF
KDLGLLIVDE EHRFGVRHKE RIKAMRANVD ILTLTATPIP RTLNMAMSGM RDLSIIATPP
ARRLAVKTFV REYDSMVVRE AILREILRGG QVYYLYNDVE NIQKAAERLA ELVPEARIAI
GHGQMREREL ERVMNDFHHQ RFNVLVCTTI IETGIDIPTA NTIIIERADH FGLAQLHQLR
GRVGRSHHQA YAWLLTPHPK AMTTDAQKRL EAIASLEDLG AGFALATHDL EIRGAGELLG
EEQSGSMETI GFSLYMELLE NAVDALKAGR EPSLEDLTSQ QTEVELRMPS LLPDDFIPDV
NTRLSFYKRI ASAKTENELE EIKVELIDRF GLLPDPARTL LDIARLRQQA QKLGIRKLEG
NEKGGVIEFA EKNHVNPAWL IGLLQKQPQH YRLDGPTRLK FIQDLSERKT RIEWVRQFMR
ELEENAIA
