RPOC_MYCTU
ID RPOC_MYCTU Reviewed; 1316 AA.
AC P9WGY7; L0T4I2; O06771; P0A674; P47769;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=Rv0668;
GN ORFNames=MTCI376.07c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-148.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8031050; DOI=10.1128/aac.38.4.805;
RA Miller L.P., Crawford J.T., Shinnick T.M.;
RT "The rpoB gene of Mycobacterium tuberculosis.";
RL Antimicrob. Agents Chemother. 38:805-811(1994).
RN [3]
RP INDUCTION FOLLOWING STARVATION.
RC STRAIN=ATCC 25618 / H37Rv / NCTC 7416;
RX PubMed=11929527; DOI=10.1046/j.1365-2958.2002.02779.x;
RA Betts J.C., Lukey P.T., Robb L.C., McAdam R.A., Duncan K.;
RT "Evaluation of a nutrient starvation model of Mycobacterium tuberculosis
RT persistence by gene and protein expression profiling.";
RL Mol. Microbiol. 43:717-731(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22570422; DOI=10.1093/nar/gks346;
RA Hu Y., Morichaud Z., Chen S., Leonetti J.P., Brodolin K.;
RT "Mycobacterium tuberculosis RbpA protein is a new type of transcriptional
RT activator that stabilizes the sigma A-containing RNA polymerase
RT holoenzyme.";
RL Nucleic Acids Res. 40:6547-6557(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000269|PubMed:22570422}.
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|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000269|PubMed:22570422}.
CC -!- INDUCTION: 6-fold repressed by starvation.
CC {ECO:0000269|PubMed:11929527}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; AL123456; CCP43411.1; -; Genomic_DNA.
DR EMBL; L27989; AAA21417.1; -; Genomic_DNA.
DR PIR; G70535; G70535.
DR RefSeq; NP_215182.1; NC_000962.3.
DR RefSeq; WP_003403413.1; NZ_NVQJ01000007.1.
DR PDB; 5UH5; X-ray; 3.75 A; D=1-1316.
DR PDB; 5UH6; X-ray; 3.84 A; D=1-1316.
DR PDB; 5UH7; X-ray; 2.20 A; A/B=124-271.
DR PDB; 5UH8; X-ray; 4.18 A; D=1-1316.
DR PDB; 5UH9; X-ray; 4.40 A; D=1-1316.
DR PDB; 5UHA; X-ray; 3.91 A; D=1-1316.
DR PDB; 5UHB; X-ray; 4.29 A; D=1-1316.
DR PDB; 5UHC; X-ray; 3.80 A; D=1-1316.
DR PDB; 5UHD; X-ray; 4.01 A; D=1-1316.
DR PDB; 5UHE; X-ray; 4.04 A; D=1-1316.
DR PDB; 5UHF; X-ray; 4.34 A; D=1-1316.
DR PDB; 5UHG; X-ray; 3.97 A; D=1-1316.
DR PDB; 5ZX2; X-ray; 2.80 A; D=2-1316.
DR PDB; 5ZX3; X-ray; 2.75 A; D=2-1316.
DR PDB; 6BZO; EM; 3.38 A; D=1-1316.
DR PDB; 6C04; EM; 3.27 A; D=1-1316.
DR PDB; 6C05; EM; 5.15 A; D=1-1316.
DR PDB; 6C06; EM; 5.15 A; D=1-1316.
DR PDB; 6DV9; X-ray; 3.80 A; D=1-1316.
DR PDB; 6DVB; X-ray; 3.80 A; D=1-1316.
DR PDB; 6DVC; X-ray; 3.30 A; D=1-1316.
DR PDB; 6DVD; X-ray; 3.90 A; D=1-1316.
DR PDB; 6DVE; X-ray; 3.81 A; D=1-1316.
DR PDB; 6EDT; EM; -; D=1-1316.
DR PDB; 6EE8; EM; 3.92 A; D=1-1316.
DR PDB; 6EEC; EM; 3.55 A; D=1-1316.
DR PDB; 6FBV; EM; 3.50 A; D=1-1316.
DR PDB; 6JCX; X-ray; 2.90 A; D=2-1316.
DR PDB; 6JCY; X-ray; 3.11 A; D=2-1316.
DR PDB; 6KON; X-ray; 3.00 A; D=2-1316.
DR PDB; 6KOO; X-ray; 2.80 A; D=2-1316.
DR PDB; 6KOP; X-ray; 3.30 A; D=2-1316.
DR PDB; 6KOQ; X-ray; 3.35 A; D=2-1316.
DR PDB; 6M7J; EM; 4.40 A; D=1-1316.
DR PDB; 6TYE; X-ray; 3.79 A; D=1-1316.
DR PDB; 6TYF; X-ray; 3.80 A; D=1-1316.
DR PDB; 6TYG; X-ray; 3.50 A; D=1-1316.
DR PDB; 6VVX; EM; 3.39 A; D=1-1316.
DR PDB; 6VVY; EM; 3.42 A; D=1-1316.
DR PDB; 6VVZ; EM; 3.72 A; D=1-1316.
DR PDB; 6VW0; EM; 3.59 A; D=1-1316.
DR PDB; 7KIF; EM; 2.94 A; D=1-1316.
DR PDB; 7KIM; EM; 3.38 A; D=1-1316.
DR PDB; 7KIN; EM; 2.74 A; D=1-1316.
DR PDBsum; 5UH5; -.
DR PDBsum; 5UH6; -.
DR PDBsum; 5UH7; -.
DR PDBsum; 5UH8; -.
DR PDBsum; 5UH9; -.
DR PDBsum; 5UHA; -.
DR PDBsum; 5UHB; -.
DR PDBsum; 5UHC; -.
DR PDBsum; 5UHD; -.
DR PDBsum; 5UHE; -.
DR PDBsum; 5UHF; -.
DR PDBsum; 5UHG; -.
DR PDBsum; 5ZX2; -.
DR PDBsum; 5ZX3; -.
DR PDBsum; 6BZO; -.
DR PDBsum; 6C04; -.
DR PDBsum; 6C05; -.
DR PDBsum; 6C06; -.
DR PDBsum; 6DV9; -.
DR PDBsum; 6DVB; -.
DR PDBsum; 6DVC; -.
DR PDBsum; 6DVD; -.
DR PDBsum; 6DVE; -.
DR PDBsum; 6EDT; -.
DR PDBsum; 6EE8; -.
DR PDBsum; 6EEC; -.
DR PDBsum; 6FBV; -.
DR PDBsum; 6JCX; -.
DR PDBsum; 6JCY; -.
DR PDBsum; 6KON; -.
DR PDBsum; 6KOO; -.
DR PDBsum; 6KOP; -.
DR PDBsum; 6KOQ; -.
DR PDBsum; 6M7J; -.
DR PDBsum; 6TYE; -.
DR PDBsum; 6TYF; -.
DR PDBsum; 6TYG; -.
DR PDBsum; 6VVX; -.
DR PDBsum; 6VVY; -.
DR PDBsum; 6VVZ; -.
DR PDBsum; 6VW0; -.
DR PDBsum; 7KIF; -.
DR PDBsum; 7KIM; -.
DR PDBsum; 7KIN; -.
DR AlphaFoldDB; P9WGY7; -.
DR SASBDB; P9WGY7; -.
DR SMR; P9WGY7; -.
DR IntAct; P9WGY7; 3.
DR STRING; 83332.Rv0668; -.
DR DrugBank; DB01201; Rifapentine.
DR PaxDb; P9WGY7; -.
DR GeneID; 888177; -.
DR KEGG; mtu:Rv0668; -.
DR TubercuList; Rv0668; -.
DR eggNOG; COG0086; Bacteria.
DR OMA; YRNIRVE; -.
DR PhylomeDB; P9WGY7; -.
DR BRENDA; 2.7.7.6; 3445.
DR Reactome; R-HSA-9639775; Antimicrobial action and antimicrobial resistance in Mtb.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1316
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067765"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 968
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 975
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6BZO"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5UH7"
FT HELIX 141..186
FT /evidence="ECO:0007829|PDB:5UH7"
FT HELIX 191..227
FT /evidence="ECO:0007829|PDB:5UH7"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:7KIM"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:5UH7"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:5UH7"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5UH7"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 287..304
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6JCY"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 340..360
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 364..382
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:5ZX3"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:5ZX3"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 418..432
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 469..478
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 482..491
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 509..524
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:5ZX2"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:6FBV"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 580..589
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:5ZX3"
FT HELIX 615..623
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 631..641
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 644..650
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:7KIF"
FT TURN 657..659
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 662..667
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 668..674
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:6BZO"
FT HELIX 690..703
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 706..725
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 726..728
FT /evidence="ECO:0007829|PDB:6JCY"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:5ZX3"
FT HELIX 742..761
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 763..765
FT /evidence="ECO:0007829|PDB:6FBV"
FT HELIX 767..792
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:6DVC"
FT HELIX 798..804
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:6BZO"
FT HELIX 811..817
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 822..824
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 832..836
FT /evidence="ECO:0007829|PDB:7KIF"
FT TURN 840..842
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 846..880
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 886..889
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 902..904
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 906..908
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 910..912
FT /evidence="ECO:0007829|PDB:5ZX3"
FT TURN 917..920
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 924..927
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 929..931
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:6KOO"
FT STRAND 935..938
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 946..955
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 960..962
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 965..967
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 971..975
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 976..979
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 983..985
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 986..988
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 995..1004
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1005..1009
FT /evidence="ECO:0007829|PDB:5ZX3"
FT HELIX 1028..1034
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 1035..1037
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1041..1044
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 1048..1057
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1059..1068
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1069..1072
FT /evidence="ECO:0007829|PDB:7KIM"
FT STRAND 1075..1077
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1082..1084
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1088..1090
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 1092..1094
FT /evidence="ECO:0007829|PDB:6JCX"
FT STRAND 1096..1098
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 1101..1105
FT /evidence="ECO:0007829|PDB:6JCY"
FT STRAND 1112..1115
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1118..1124
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1127..1143
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 1144..1146
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1151..1153
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1155..1159
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1162..1169
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1171..1174
FT /evidence="ECO:0007829|PDB:6JCX"
FT STRAND 1180..1182
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1183..1186
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 1187..1193
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1194..1198
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1202..1205
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1212..1215
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1216..1218
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1220..1223
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 1224..1226
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1229..1236
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 1237..1240
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1242..1244
FT /evidence="ECO:0007829|PDB:6DVC"
FT STRAND 1247..1249
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1250..1254
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1261..1263
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1265..1268
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1271..1274
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1276..1280
FT /evidence="ECO:0007829|PDB:7KIN"
SQ SEQUENCE 1316 AA; 146769 MW; 45BF24839AF53E8B CRC64;
MLDVNFFDEL RIGLATAEDI RQWSYGEVKK PETINYRTLK PEKDGLFCEK IFGPTRDWEC
YCGKYKRVRF KGIICERCGV EVTRAKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
APKDLEKIIY FAAYVITSVD EEMRHNELST LEAEMAVERK AVEDQRDGEL EARAQKLEAD
LAELEAEGAK ADARRKVRDG GEREMRQIRD RAQRELDRLE DIWSTFTKLA PKQLIVDENL
YRELVDRYGE YFTGAMGAES IQKLIENFDI DAEAESLRDV IRNGKGQKKL RALKRLKVVA
AFQQSGNSPM GMVLDAVPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRLIDL
GAPEIIVNNE KRMLQESVDA LFDNGRRGRP VTGPGNRPLK SLSDLLKGKQ GRFRQNLLGK
RVDYSGRSVI VVGPQLKLHQ CGLPKLMALE LFKPFVMKRL VDLNHAQNIK SAKRMVERQR
PQVWDVLEEV IAEHPVLLNR APTLHRLGIQ AFEPMLVEGK AIQLHPLVCE AFNADFDGDQ
MAVHLPLSAE AQAEARILML SSNNILSPAS GRPLAMPRLD MVTGLYYLTT EVPGDTGEYQ
PASGDHPETG VYSSPAEAIM AADRGVLSVR AKIKVRLTQL RPPVEIEAEL FGHSGWQPGD
AWMAETTLGR VMFNELLPLG YPFVNKQMHK KVQAAIINDL AERYPMIVVA QTVDKLKDAG
FYWATRSGVT VSMADVLVPP RKKEILDHYE ERADKVEKQF QRGALNHDER NEALVEIWKE
ATDEVGQALR EHYPDDNPII TIVDSGATGN FTQTRTLAGM KGLVTNPKGE FIPRPVKSSF
REGLTVLEYF INTHGARKGL ADTALRTADS GYLTRRLVDV SQDVIVREHD CQTERGIVVE
LAERAPDGTL IRDPYIETSA YARTLGTDAV DEAGNVIVER GQDLGDPEID ALLAAGITQV
KVRSVLTCAT STGVCATCYG RSMATGKLVD IGEAVGIVAA QSIGEPGTQL TMRTFHQGGV
GEDITGGLPR VQELFEARVP RGKAPIADVT GRVRLEDGER FYKITIVPDD GGEEVVYDKI
SKRQRLRVFK HEDGSERVLS DGDHVEVGQQ LMEGSADPHE VLRVQGPREV QIHLVREVQE
VYRAQGVSIH DKHIEVIVRQ MLRRVTIIDS GSTEFLPGSL IDRAEFEAEN RRVVAEGGEP
AAGRPVLMGI TKASLATDSW LSAASFQETT RVLTDAAINC RSDKLNGLKE NVIIGKLIPA
GTGINRYRNI AVQPTEEARA AAYTIPSYED QYYSPDFGAA TGAAVPLDDY GYSDYR
