ID RPOB_THET8 Reviewed; 1119 AA. AC Q8RQE9; Q5SHB7; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321}; DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; GN OrderedLocusNames=TTHA1813; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12198314; DOI=10.1107/s0907444902011770; RA Vassylyeva M.N., Lee J., Sekine S.I., Laptenko O., Kuramitsu S., RA Shibata T., Inoue Y., Borukhov S., Vassylyev D.G., Yokoyama S.; RT "Purification, crystallization and initial crystallographic analysis of RNA RT polymerase holoenzyme from Thermus thermophilus."; RL Acta Crystallogr. D 58:1497-1500(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. 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_01321}; 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 -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000255|HAMAP-Rule:MF_01321}. 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; AB083789; BAB89400.1; -; Genomic_DNA. DR EMBL; AP008226; BAD71636.1; -; Genomic_DNA. DR RefSeq; WP_011228935.1; NC_006461.1. DR RefSeq; YP_145079.1; NC_006461.1. DR PDB; 1IW7; X-ray; 2.60 A; C/M=1-1119. DR PDB; 1SMY; X-ray; 2.70 A; C/M=1-1119. DR PDB; 1ZYR; X-ray; 3.00 A; C/M=1-1119. DR PDB; 2A68; X-ray; 2.50 A; C/M=1-1119. DR PDB; 2A69; X-ray; 2.50 A; C/M=1-1119. DR PDB; 2A6E; X-ray; 2.80 A; C/M=1-1119. DR PDB; 2A6H; X-ray; 2.40 A; C/M=1-1119. DR PDB; 2BE5; X-ray; 2.40 A; C/M=1-1119. DR PDB; 2CW0; X-ray; 3.30 A; C/M=1-1119. DR PDB; 2O5I; X-ray; 2.50 A; C/M=1-1119. DR PDB; 2O5J; X-ray; 3.00 A; C/M=1-1119. DR PDB; 2PPB; X-ray; 3.00 A; C/M=1-1119. DR PDB; 3AOH; X-ray; 4.10 A; C/H/M=1-1119. DR PDB; 3AOI; X-ray; 4.30 A; C/H/M=1-1119. DR PDB; 3DXJ; X-ray; 3.00 A; C/M=1-1119. DR PDB; 3EQL; X-ray; 2.70 A; C/M=1-1119. DR PDB; 3WOD; X-ray; 3.60 A; C=1-1119. DR PDB; 3WOE; X-ray; 2.35 A; A/C=703-830. DR PDB; 3WOF; X-ray; 3.30 A; A/C/E/G/I/K/M/O/Q/S/U/W=703-830. DR PDB; 4G7H; X-ray; 2.90 A; C/M=1-1119. DR PDB; 4G7O; X-ray; 2.99 A; C/M=1-1119. DR PDB; 4G7Z; X-ray; 3.82 A; C/M=1-1119. DR PDB; 4GZY; X-ray; 3.51 A; C=1-1119. DR PDB; 4GZZ; X-ray; 4.29 A; C=1-1119. DR PDB; 4MQ9; X-ray; 3.35 A; C=1-1119. DR PDB; 4OIN; X-ray; 2.80 A; C=1-1119. DR PDB; 4OIO; X-ray; 3.10 A; C=1-1119. DR PDB; 4OIP; X-ray; 3.40 A; C=1-1119. DR PDB; 4OIQ; X-ray; 3.62 A; C=1-1119. DR PDB; 4OIR; X-ray; 3.10 A; C=1-1119. DR PDB; 4Q4Z; X-ray; 2.90 A; C=1-1119. DR PDB; 4Q5S; X-ray; 3.00 A; C=1-1119. DR PDB; 4WQS; X-ray; 4.31 A; C/M=1-1119. DR PDB; 4WQT; X-ray; 4.40 A; C/H/M=1-1119. DR PDB; 5D4C; X-ray; 3.28 A; C/M=1-1119. DR PDB; 5D4D; X-ray; 3.00 A; C/M=1-1119. DR PDB; 5D4E; X-ray; 3.08 A; C/M=1-1119. DR PDB; 5E17; X-ray; 3.20 A; C=1-1119. DR PDB; 5E18; X-ray; 3.30 A; C=1-1119. DR PDB; 5I2D; X-ray; 4.41 A; C/N=1-1119. DR PDB; 5TMC; X-ray; 2.71 A; C=1-1119. DR PDB; 5TMF; X-ray; 3.00 A; C=1-1119. DR PDB; 5VO8; X-ray; 3.30 A; C=1-1119. DR PDB; 5VOI; X-ray; 2.80 A; C=1-1119. DR PDB; 5X21; X-ray; 3.32 A; C=1-1119. DR PDB; 5X22; X-ray; 3.35 A; C/M=1-1119. DR PDB; 5XJ0; X-ray; 4.00 A; C=1-1119. DR PDB; 6ASG; X-ray; 3.80 A; C=1-1119. DR PDB; 6CUU; X-ray; 2.99 A; C=1-1119. DR PDB; 6KQD; X-ray; 3.30 A; C/M=1-1119. DR PDB; 6KQE; X-ray; 3.30 A; C=1-1119. DR PDB; 6KQF; X-ray; 2.45 A; C=1-1119. DR PDB; 6KQG; X-ray; 2.78 A; C=1-1119. DR PDB; 6KQH; X-ray; 3.18 A; C=1-1119. DR PDB; 6KQL; X-ray; 2.89 A; C=1-1119. DR PDB; 6KQM; X-ray; 3.20 A; C=1-1119. DR PDB; 6KQN; X-ray; 3.49 A; C=1-1119. DR PDB; 6L74; X-ray; 3.12 A; C=1-1119. DR PDB; 6LTS; X-ray; 3.45 A; C=1-1119. DR PDB; 6M6A; EM; 5.00 A; C=1-1119. DR PDB; 6M6B; EM; 4.10 A; C=1-1119. DR PDB; 6M6C; EM; 3.10 A; C=1-1119. DR PDB; 6OVR; X-ray; 2.84 A; C=1-1119. DR PDB; 6OVY; X-ray; 3.00 A; C=1-1119. DR PDB; 6OW3; X-ray; 2.77 A; C=1-1119. DR PDB; 6OY5; X-ray; 3.10 A; C=1-1119. DR PDB; 6OY6; X-ray; 3.10 A; C=1-1119. DR PDB; 6OY7; X-ray; 3.04 A; C=1-1119. DR PDB; 6P70; X-ray; 3.05 A; C=1-1119. DR PDB; 6P71; X-ray; 2.92 A; C=1-1119. DR PDB; 6WOX; X-ray; 3.14 A; C=1-1119. DR PDB; 6WOY; X-ray; 3.00 A; C=1-1119. DR PDB; 7EH0; X-ray; 2.81 A; C=1-1119. DR PDB; 7EH1; X-ray; 2.90 A; C=1-1119. DR PDB; 7EH2; X-ray; 3.34 A; C/M=1-1119. DR PDB; 7MLB; X-ray; 3.60 A; C=1-1119. DR PDB; 7MLI; X-ray; 3.60 A; C=1-1119. DR PDB; 7MLJ; X-ray; 3.75 A; C=1-1119. DR PDB; 7RDQ; EM; 3.00 A; C=1-1119. DR PDB; 8HSG; EM; 3.20 A; I=1-1119. DR PDB; 8HSH; EM; 3.40 A; I=1-1119. DR PDB; 8HSL; EM; 5.80 A; I=1-1119. DR PDB; 8HSR; EM; 4.00 A; I=1-1119. DR PDBsum; 1IW7; -. DR PDBsum; 1SMY; -. DR PDBsum; 1ZYR; -. DR PDBsum; 2A68; -. DR PDBsum; 2A69; -. DR PDBsum; 2A6E; -. DR PDBsum; 2A6H; -. DR PDBsum; 2BE5; -. DR PDBsum; 2CW0; -. DR PDBsum; 2O5I; -. DR PDBsum; 2O5J; -. DR PDBsum; 2PPB; -. DR PDBsum; 3AOH; -. DR PDBsum; 3AOI; -. DR PDBsum; 3DXJ; -. DR PDBsum; 3EQL; -. DR PDBsum; 3WOD; -. DR PDBsum; 3WOE; -. DR PDBsum; 3WOF; -. DR PDBsum; 4G7H; -. DR PDBsum; 4G7O; -. DR PDBsum; 4G7Z; -. DR PDBsum; 4GZY; -. DR PDBsum; 4GZZ; -. DR PDBsum; 4MQ9; -. DR PDBsum; 4OIN; -. DR PDBsum; 4OIO; -. DR PDBsum; 4OIP; -. DR PDBsum; 4OIQ; -. DR PDBsum; 4OIR; -. DR PDBsum; 4Q4Z; -. DR PDBsum; 4Q5S; -. DR PDBsum; 4WQS; -. DR PDBsum; 4WQT; -. DR PDBsum; 5D4C; -. DR PDBsum; 5D4D; -. DR PDBsum; 5D4E; -. DR PDBsum; 5E17; -. DR PDBsum; 5E18; -. DR PDBsum; 5I2D; -. DR PDBsum; 5TMC; -. DR PDBsum; 5TMF; -. DR PDBsum; 5VO8; -. DR PDBsum; 5VOI; -. DR PDBsum; 5X21; -. DR PDBsum; 5X22; -. DR PDBsum; 5XJ0; -. DR PDBsum; 6ASG; -. DR PDBsum; 6CUU; -. DR PDBsum; 6KQD; -. DR PDBsum; 6KQE; -. DR PDBsum; 6KQF; -. DR PDBsum; 6KQG; -. DR PDBsum; 6KQH; -. DR PDBsum; 6KQL; -. DR PDBsum; 6KQM; -. DR PDBsum; 6KQN; -. DR PDBsum; 6L74; -. DR PDBsum; 6LTS; -. DR PDBsum; 6M6A; -. DR PDBsum; 6M6B; -. DR PDBsum; 6M6C; -. DR PDBsum; 6OVR; -. DR PDBsum; 6OVY; -. DR PDBsum; 6OW3; -. DR PDBsum; 6OY5; -. DR PDBsum; 6OY6; -. DR PDBsum; 6OY7; -. DR PDBsum; 6P70; -. DR PDBsum; 6P71; -. DR PDBsum; 6WOX; -. DR PDBsum; 6WOY; -. DR PDBsum; 7EH0; -. DR PDBsum; 7EH1; -. DR PDBsum; 7EH2; -. DR PDBsum; 7MLB; -. DR PDBsum; 7MLI; -. DR PDBsum; 7MLJ; -. DR PDBsum; 7RDQ; -. DR PDBsum; 8HSG; -. DR PDBsum; 8HSH; -. DR PDBsum; 8HSL; -. DR PDBsum; 8HSR; -. DR AlphaFoldDB; Q8RQE9; -. DR EMDB; EMD-34996; -. DR EMDB; EMD-34997; -. DR EMDB; EMD-35000; -. DR EMDB; EMD-35004; -. DR SMR; Q8RQE9; -. DR DIP; DIP-47011N; -. DR IntAct; Q8RQE9; 7. DR DrugBank; DB08266; Methyl [(1E,5R)-5-{3-[(2E,4E)-2,5-dimethyl-2,4-octadienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hexylidene]carbamate. DR DrugBank; DB08226; Myxopyronin B. DR DrugBank; DB04788; Tagetitoxin. DR EnsemblBacteria; BAD71636; BAD71636; BAD71636. DR GeneID; 3169736; -. DR KEGG; ttj:TTHA1813; -. DR PATRIC; fig|300852.9.peg.1784; -. DR eggNOG; COG0085; Bacteria. DR HOGENOM; CLU_000524_4_1_0; -. DR PhylomeDB; Q8RQE9; -. DR BRENDA; 2.7.7.6; 2305. DR EvolutionaryTrace; Q8RQE9; -. DR PRO; PR:Q8RQE9; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW. 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:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.100; -; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1100.10; -; 1. DR Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 1. DR HAMAP; MF_01321; RNApol_bact_RpoB; 1. DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf. DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom. DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf. DR InterPro; IPR010243; RNA_pol_bsu_bac. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR NCBIfam; TIGR02013; rpoB; 1. DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF20; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF10385; RNA_pol_Rpb2_45; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transcription; Transferase. FT CHAIN 1..1119 FT /note="DNA-directed RNA polymerase subunit beta" FT /id="PRO_0000047985" FT STRAND 2..5 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 20..29 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 31..33 FT /evidence="ECO:0007829|PDB:2O5I" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:6KQF" FT HELIX 43..51 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 53..56 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 80..85 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:2O5I" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:6KQF" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 166..169 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 172..177 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 181..191 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 193..200 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 204..212 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:6KQF" FT HELIX 218..221 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 231..241 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 250..252 FT /evidence="ECO:0007829|PDB:6OVY" FT HELIX 253..257 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 269..271 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 280..284 FT /evidence="ECO:0007829|PDB:5TMC" FT TURN 287..290 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 297..302 FT /evidence="ECO:0007829|PDB:6KQF" FT HELIX 303..314 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:4G7O" FT TURN 328..330 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 336..361 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 364..366 FT /evidence="ECO:0007829|PDB:6KQF" FT TURN 370..372 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 376..387 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 390..394 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 401..408 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 409..418 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:5TMC" FT HELIX 425..428 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 435..437 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 440..443 FT /evidence="ECO:0007829|PDB:2O5I" FT STRAND 445..448 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 450..455 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 456..458 FT /evidence="ECO:0007829|PDB:2O5J" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:3DXJ" FT STRAND 463..465 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 467..475 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 478..486 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 488..493 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 494..497 FT /evidence="ECO:0007829|PDB:6KQF" FT STRAND 499..501 FT /evidence="ECO:0007829|PDB:2CW0" FT STRAND 503..508 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 511..524 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 526..528 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 531..533 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 536..539 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 542..545 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 555..565 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 571..573 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 578..580 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 584..590 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 594..596 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 598..606 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 608..615 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 616..618 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 619..621 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 622..624 FT /evidence="ECO:0007829|PDB:6OY6" FT STRAND 628..630 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 634..637 FT /evidence="ECO:0007829|PDB:6KQF" FT STRAND 654..657 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 661..666 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 669..675 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 680..683 FT /evidence="ECO:0007829|PDB:6KQF" FT STRAND 684..691 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 693..696 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 697..700 FT /evidence="ECO:0007829|PDB:6KQF" FT STRAND 703..713 FT /evidence="ECO:0007829|PDB:3WOE" FT STRAND 727..729 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 731..734 FT /evidence="ECO:0007829|PDB:3WOE" FT HELIX 735..737 FT /evidence="ECO:0007829|PDB:1IW7" FT TURN 738..740 FT /evidence="ECO:0007829|PDB:1IW7" FT STRAND 741..743 FT /evidence="ECO:0007829|PDB:3WOE" FT STRAND 754..756 FT /evidence="ECO:0007829|PDB:3WOE" FT STRAND 758..761 FT /evidence="ECO:0007829|PDB:3WOE" FT STRAND 762..766 FT /evidence="ECO:0007829|PDB:1IW7" FT HELIX 769..778 FT /evidence="ECO:0007829|PDB:3WOE" FT STRAND 785..787 FT /evidence="ECO:0007829|PDB:3WOE" FT STRAND 798..807 FT /evidence="ECO:0007829|PDB:3WOE" FT TURN 808..812 FT /evidence="ECO:0007829|PDB:5TMC" FT STRAND 819..829 FT /evidence="ECO:0007829|PDB:3WOE" FT STRAND 838..840 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 842..844 FT /evidence="ECO:0007829|PDB:3EQL" FT STRAND 846..853 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 855..857 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 862..864 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 868..870 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 874..880 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 883..896 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 899..902 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 905..907 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 911..932 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 938..948 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 949..951 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 955..957 FT /evidence="ECO:0007829|PDB:5TMC" FT HELIX 959..968 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 977..979 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 980..982 FT /evidence="ECO:0007829|PDB:5D4D" FT STRAND 987..997 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 1001..1003 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 1006..1010 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 1015..1017 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 1024..1026 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 1030..1032 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 1034..1042 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 1047..1053 FT /evidence="ECO:0007829|PDB:2A6H" FT TURN 1054..1058 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 1060..1071 FT /evidence="ECO:0007829|PDB:2A6H" FT HELIX 1083..1094 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 1098..1102 FT /evidence="ECO:0007829|PDB:2BE5" FT STRAND 1104..1106 FT /evidence="ECO:0007829|PDB:2A6H" FT STRAND 1114..1117 FT /evidence="ECO:0007829|PDB:2A6H" SQ SEQUENCE 1119 AA; 125264 MW; C1260F31CEC6B40D CRC64; MEIKRFGRIR EVIPLPPLTE IQVESYRRAL QADVPPEKRE NVGIQAAFRE TFPIEEEDKG KGGLVLDFLE YRLGEPPFPQ DECREKDLTY QAPLYARLQL IHKDTGLIKE DEVFLGHIPL MTEDGSFIIN GADRVIVSQI HRSPGVYFTP DPARPGRYIA SIIPLPKRGP WIDLEVEPNG VVSMKVNKRK FPLVLLLRVL GYDQETLARE LGAYGELVQG LMDESVFAMR PEEALIRLFT LLRPGDPPKR DKAVAYVYGL IADPRRYDLG EAGRYKAEEK LGIRLSGRTL ARFEDGEFKD EVFLPTLRYL FALTAGVPGH EVDDIDHLGN RRIRTVGELM TDQFRVGLAR LARGVRERML MGSEDSLTPA KLVNSRPLEA AIREFFSRSQ LSQFKDETNP LSSLRHKRRI SALGPGGLTR ERAGFDVRDV HRTHYGRICP VETPEGANIG LITSLAAYAR VDELGFIRTP YRRVVGGVVT DEVVYMTATE EDRYTIAQAN TPLEGNRIAA ERVVARRKGE PVIVSPEEVE FMDVSPKQVF SVNTNLIPFL EHDDANRALM GSNMQTQAVP LIRAQAPVVM TGLEERVVRD SLAALYAEED GEVAKVDGNR IVVRYEDGRL VEYPLRRFYR SNQGTALDQR PRVVVGQRVR KGDLLADGPA SENGFLALGQ NVLVAIMPFD GYNFEDAIVI SEELLKRDFY TSIHIERYEI EARDTKLGPE RITRDIPHLS EAALRDLDEE GVVRIGAEVK PGDILVGRTS FKGESEPTPE ERLLRSIFGE KARDVKDTSL RVPPGEGGIV VRTVRLRRGD PGVELKPGVR EVVRVYVAQK RKLQVGDKLA NRHGNKGVVA KILPVEDMPH LPDGTPVDVI LNPLGVPSRM NLGQILETHL GLAGYFLGQR YISPIFDGAK EPEIKELLAQ AFEVYFGKRK GEGFGVDKRE VEVLRRAEKL GLVTPGKTPE EQLKELFLQG KVVLYDGRTG EPIEGPIVVG QMFIMKLYHM VEDKMHARST GPYSLITQQP LGGKAQFGGQ RFGEMEVWAL EAYGAAHTLQ EMLTLKSDDI EGRNAAYEAI IKGEDVPEPS VPESFRVLVK ELQALALDVQ TLDEKDNPVD IFEGLASKR //