RPO1N_SACSH
ID RPO1N_SACSH Reviewed; 880 AA.
AC B8YB53;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1N {ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000303|PubMed:19419240};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000305|PubMed:19419240};
DE AltName: Full=DNA-directed RNA polymerase subunit A' {ECO:0000255|HAMAP-Rule:MF_00863};
GN Name=rpo1N {ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000303|PubMed:19419240};
GN Synonyms=rpoA1 {ECO:0000255|HAMAP-Rule:MF_00863};
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1] {ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS)
RP OF THE RNA POLYMERASE COMPLEX IN COMPLEX WITH MAGNESIUM AND ZINC, FUNCTION,
RP COFACTOR, SUBUNIT, AND NOMENCLATURE.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=19419240; DOI=10.1371/journal.pbio.1000102;
RA Korkhin Y., Unligil U.M., Littlefield O., Nelson P.J., Stuart D.I.,
RA Sigler P.B., Bell S.D., Abrescia N.G.;
RT "Evolution of complex RNA polymerases: the complete archaeal RNA polymerase
RT structure.";
RL PLoS Biol. 7:e1000102-e1000102(2009).
RN [2] {ECO:0007744|PDB:2Y0S}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN
RP COMPLEX WITH MAGNESIUM AND ZINC, FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=21265742; DOI=10.1042/bst0390025;
RA Wojtas M., Peralta B., Ondiviela M., Mogni M., Bell S.D., Abrescia N.G.;
RT "Archaeal RNA polymerase: the influence of the protruding stalk in crystal
RT packing and preliminary biophysical analysis of the Rpo13 subunit.";
RL Biochem. Soc. Trans. 39:25-30(2011).
RN [3] {ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN
RP COMPLEX WITH MAGNESIUM AND ZINC WITH AND WITHOUT DNA, FUNCTION, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, AND DNA-BINDING.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=22848102; DOI=10.1093/nar/gks692;
RA Wojtas M.N., Mogni M., Millet O., Bell S.D., Abrescia N.G.;
RT "Structural and functional analyses of the interaction of archaeal RNA
RT polymerase with DNA.";
RL Nucleic Acids Res. 40:9941-9952(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. Forms the clamp head domain.
CC {ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000269|PubMed:19419240,
CC ECO:0000269|PubMed:21265742, ECO:0000269|PubMed:22848102}.
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_00863,
CC ECO:0000305|PubMed:19419240, ECO:0000305|PubMed:21265742,
CC ECO:0000305|PubMed:22848102};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00863,
CC ECO:0000269|PubMed:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102, ECO:0007744|PDB:2WAQ,
CC ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
CC ECO:0007744|PDB:4V8S};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00863,
CC ECO:0000269|PubMed:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102, ECO:0007744|PDB:2WAQ,
CC ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
CC ECO:0007744|PDB:4V8S};
CC Note=Binds at least 2 Zn(2+) per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00863, ECO:0000269|PubMed:19419240,
CC ECO:0000269|PubMed:21265742, ECO:0000269|PubMed:22848102};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex
CC (PubMed:19419240, PubMed:21265742, PubMed:22848102). Rpo1N and Rpo5
CC form a cleft which docks Rpo13. Interacts with Rpo8 on the periphery of
CC the clamp head (PubMed:19419240, PubMed:21265742, PubMed:22848102).
CC {ECO:0000269|PubMed:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00863,
CC ECO:0000269|PubMed:22848102}.
CC -!- MISCELLANEOUS: Corresponds to about the first two-thirds of the
CC bacterial beta' subunit. {ECO:0000305|PubMed:19419240}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000305|PubMed:19419240}.
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DR EMBL; FJ515665; ACL36488.1; -; Genomic_DNA.
DR PDB; 2WAQ; X-ray; 3.35 A; A=1-880.
DR PDB; 2WB1; X-ray; 3.52 A; A/W=1-880.
DR PDB; 2Y0S; X-ray; 3.80 A; A/W=1-880.
DR PDB; 4AYB; X-ray; 3.20 A; A=1-880.
DR PDB; 4V8S; X-ray; 4.32 A; AW/BA=1-880.
DR PDBsum; 2WAQ; -.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB53; -.
DR BRENDA; 2.7.7.6; 6162.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd02582; RNAP_archeal_A; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR HAMAP; MF_00863; RNApol_arch_Rpo1N; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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; 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 InterPro; IPR012758; RPO1N.
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; TIGR02390; RNA_pol_rpoA1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..880
FT /note="DNA-directed RNA polymerase subunit Rpo1N"
FT /id="PRO_0000453785"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 88
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 92..95
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 138
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S"
FT BINDING 303
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 305..310
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 323
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 422
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S,
FT ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S,
FT ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S,
FT ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S"
FT BINDING 812..822
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 815
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2WAQ"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 236..253
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 259..277
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 319..328
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:2WAQ"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 470..479
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 501..509
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 538..547
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 548..553
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:2WAQ"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 592..595
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 603..606
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 611..617
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 621..642
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 648..651
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 655..680
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 692..717
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 724..731
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 740..744
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 751..757
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 760..763
FT /evidence="ECO:0007829|PDB:2WAQ"
FT STRAND 764..766
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 776..779
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 786..788
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 792..811
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 813..827
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 830..832
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 841..843
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 844..849
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 850..853
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 857..859
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 860..865
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 868..875
FT /evidence="ECO:0007829|PDB:4AYB"
SQ SEQUENCE 880 AA; 99625 MW; 90F176C758C6F7A9 CRC64;
MSEKNIKGIK FGILSPDEIR KMSVTAIITP DVYDEDGTPI EGSVMDPRLG VIEPGQKCPT
CGNTLGNCPG HFGHIELVRP VIHVGFVKHV YEFLKATCRR CGRVKISEDE IEKYSRIYNA
IKKRWPSAAR RLTEYVKKTA MKAQVCPHCG EKQFKIKLEK PYNFYEERKE GVAKLTPSDI
RERLEKVPES DVEILGYDPT TSRPEWMILT VLPVPPITIR PSIMIESGIR AEDDLTHKLV
DIVRINERLK ESIDAGAPQL IIEDLWDLLQ YHVATYFDNE IPGLPPSKHR SGRPLRTLAQ
RLKGKEGRFR GNLSGKRVDF SSRTVISPDP NISIDEVGVP EIIARTLTVP ERITPWNIEK
LRQFVINGPD KWPGANYVIR PDGRRIDLRY VKDRKELAST LAPGYVVERH LTDGDVVLFN
RQPSLHRISM MAHRVRVLKG LTFRLNLLVC PPYNADFDGD EMNLHVPQSE EAIAEAKEIM
LVHKNIITPR YGGPIIGAAQ DYISGAYLLT VKTTLLTKEE AQQILGVADV KIDLGEPAIL
APREYYTGKQ VVSAFLPKDF NFHGQANVSS GPRLCKNEDC PHDSYVVIKN GILLEGVFDK
KAIGNQQPES ILHWLIKEYS DEYGKWLMDN LFRVFIRFVE LQGFTMRLED VSLGDDVKKE
IYNEIDRAKV EVDNLIQKYK NGELEPIPGR TLEESLENYI LDTLDKLRST AGDIASKYLD
PFNFAYVMAR TGARGSVLNI TQMAAMLGQQ SVRGERIKRG YMTRTLPHFK PYDISPEARG
FIYSSFRTGL KPTELFFHAA GGREGLVDTA VRTSQSGYMQ RRLINALSDL RAEYDGTVRS
LYGEVIQVAY GDDGVFPMYS AHGKTVDVNR IFERVVGWKT
