NQO3_THET8
ID NQO3_THET8 Reviewed; 783 AA.
AC Q56223; Q5SM53;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=NADH-quinone oxidoreductase subunit 3;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I chain 3;
DE AltName: Full=NDH-1 subunit 3;
GN Name=nqo3; OrderedLocusNames=TTHA0090;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=9020134; DOI=10.1074/jbc.272.7.4201;
RA Yano T., Chu S.S., Sled' V.D., Ohnishi T., Yagi T.;
RT "The proton-translocating NADH-quinone oxidoreductase (NDH-1) of
RT thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of
RT the gene cluster and thermostable properties of the expressed NQO2
RT subunit.";
RL J. Biol. Chem. 272:4201-4211(1997).
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.
RN [3]
RP EXPRESSION OF 240-324 FOR CHARACTERIZATION OF A FOURTH [4FE-4S] CENTER, AND
RP MUTAGENESIS OF CYS-256; CYS-259; CYS-263 AND CYS-291.
RX PubMed=11704668; DOI=10.1074/jbc.m108796200;
RA Nakamaru-Ogiso E., Yano T., Ohnishi T., Yagi T.;
RT "Characterization of the iron-sulfur cluster coordinated by a cysteine
RT cluster motif (CXXCXXXCX27C) in the Nqo3 subunit in the proton-
RT translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus
RT HB-8.";
RL J. Biol. Chem. 277:1680-1688(2002).
RN [4]
RP PROTEIN SEQUENCE OF 1-8, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, EPR
RP SPECTROSCOPY, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=16584177; DOI=10.1021/bi0600998;
RA Hinchliffe P., Carroll J., Sazanov L.A.;
RT "Identification of a novel subunit of respiratory complex I from Thermus
RT thermophilus.";
RL Biochemistry 45:4413-4420(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF ENZYME HYDROPHILIC DOMAIN IN
RP COMPLEX WITH 2FE-2S AND 4FE-4S CLUSTER; MAG, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, DOMAIN, AND ELECTRON TRANSFER MECHANISM.
RX PubMed=16469879; DOI=10.1126/science.1123809;
RA Sazanov L.A., Hinchliffe P.;
RT "Structure of the hydrophilic domain of respiratory complex I from Thermus
RT thermophilus.";
RL Science 311:1430-1436(2006).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is menaquinone.
CC Couples the redox reaction to proton translocation (for every two
CC electrons transferred, four hydrogen ions are translocated across the
CC cytoplasmic membrane), and thus conserves the redox energy in a proton
CC gradient required for the synthesis of ATP.
CC {ECO:0000269|PubMed:16469879, ECO:0000269|PubMed:16584177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:16469879};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster 1 is
CC referred to as N1b. {ECO:0000269|PubMed:16469879};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:16469879};
CC Note=Binds 3 [4Fe-4S] clusters per subunit. The [4Fe-4S] clusters 2, 3,
CC and 4 are referred to as N5, N4, and N7, respectively. The [4Fe-4S]
CC cluster 4 is too far away from the main redox chain to participate in
CC electron transfer but probably confers structural stability.
CC {ECO:0000269|PubMed:16469879};
CC -!- SUBUNIT: NDH-1 is composed of 15 different subunits, Nqo1 to Nqo15. The
CC complex has a L-shaped structure, with the hydrophobic arm (subunits
CC Nqo7, Nqo8 and Nqo10 to Nqo14) embedded in the membrane and the
CC hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9 and Nqo15)
CC protruding into the bacterial cytoplasm. The hydrophilic domain
CC contains all the redox centers. {ECO:0000269|PubMed:16469879,
CC ECO:0000269|PubMed:16584177}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16469879};
CC Peripheral membrane protein {ECO:0000305|PubMed:16469879}; Cytoplasmic
CC side {ECO:0000305|PubMed:16469879}.
CC -!- DOMAIN: The subunit comprises two main parts, an N-terminal [FeFe]-
CC hydrogenase-like domain (residues 1 to 240) that coordinates clusters
CC 1, 2 and 3, and a domain similar to molybdopterin-containing enzymes
CC (residues 241 to 767) whose first subdomain coordinates cluster 4.
CC {ECO:0000269|PubMed:16469879}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U52917; AAA97944.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69913.1; -; Genomic_DNA.
DR PIR; T11904; T11904.
DR RefSeq; WP_011227701.1; NC_006461.1.
DR RefSeq; YP_143356.1; NC_006461.1.
DR PDB; 2FUG; X-ray; 3.30 A; 3/C/L/U=1-783.
DR PDB; 2YBB; EM; 19.00 A; 3=1-783.
DR PDB; 3I9V; X-ray; 3.10 A; 3/C=1-783.
DR PDB; 3IAM; X-ray; 3.10 A; 3/C=1-783.
DR PDB; 3IAS; X-ray; 3.15 A; 3/C/L/U=1-783.
DR PDB; 3M9S; X-ray; 4.50 A; 3/C=1-783.
DR PDB; 4HEA; X-ray; 3.30 A; 3/D=1-783.
DR PDB; 6I0D; X-ray; 3.60 A; 3/D=1-783.
DR PDB; 6I1P; X-ray; 3.21 A; 3/D=1-783.
DR PDB; 6Q8O; X-ray; 3.60 A; 3/D=1-783.
DR PDB; 6Q8W; X-ray; 3.40 A; 3/D=1-783.
DR PDB; 6Q8X; X-ray; 3.51 A; 3/D=1-783.
DR PDB; 6Y11; X-ray; 3.11 A; 3/D=1-783.
DR PDB; 6ZIY; EM; 4.25 A; 3=1-783.
DR PDB; 6ZJL; EM; 4.30 A; 3=1-783.
DR PDB; 6ZJN; EM; 6.10 A; 3=1-783.
DR PDB; 6ZJY; EM; 5.50 A; 3=1-783.
DR PDBsum; 2FUG; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 3I9V; -.
DR PDBsum; 3IAM; -.
DR PDBsum; 3IAS; -.
DR PDBsum; 3M9S; -.
DR PDBsum; 4HEA; -.
DR PDBsum; 6I0D; -.
DR PDBsum; 6I1P; -.
DR PDBsum; 6Q8O; -.
DR PDBsum; 6Q8W; -.
DR PDBsum; 6Q8X; -.
DR PDBsum; 6Y11; -.
DR PDBsum; 6ZIY; -.
DR PDBsum; 6ZJL; -.
DR PDBsum; 6ZJN; -.
DR PDBsum; 6ZJY; -.
DR AlphaFoldDB; Q56223; -.
DR SMR; Q56223; -.
DR DIP; DIP-59261N; -.
DR IntAct; Q56223; 1.
DR STRING; 300852.55771472; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69913; BAD69913; BAD69913.
DR GeneID; 3168388; -.
DR KEGG; ttj:TTHA0090; -.
DR PATRIC; fig|300852.9.peg.88; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_11_6_0; -.
DR OMA; HKNVGPL; -.
DR PhylomeDB; Q56223; -.
DR EvolutionaryTrace; Q56223; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR01973; NuoG; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; 4Fe-4S; Cell membrane; Direct protein sequencing;
KW Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Quinone;
KW Reference proteome; Translocase.
FT CHAIN 1..783
FT /note="NADH-quinone oxidoreductase subunit 3"
FT /id="PRO_0000118541"
FT DOMAIN 1..99
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 99..138
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 249..305
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 34
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184,
FT ECO:0000269|PubMed:16469879"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 181
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 230
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 256
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 259
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 291
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:16469879"
FT MUTAGEN 256
FT /note="C->A: Decreases amount and stability of iron-sulfur
FT center 4."
FT /evidence="ECO:0000269|PubMed:11704668"
FT MUTAGEN 259
FT /note="C->A: Decreases amount and stability of iron-sulfur
FT center 4."
FT /evidence="ECO:0000269|PubMed:11704668"
FT MUTAGEN 263
FT /note="C->A: Decreases amount and stability of iron-sulfur
FT center 4."
FT /evidence="ECO:0000269|PubMed:11704668"
FT MUTAGEN 291
FT /note="C->A: Decreases amount and stability of iron-sulfur
FT center 4."
FT /evidence="ECO:0000269|PubMed:11704668"
FT CONFLICT 332
FT /note="G -> S (in Ref. 1; AAA97944)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 98..112
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3IAM"
FT TURN 221..225
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2FUG"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6I1P"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:6I1P"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 297..303
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2FUG"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 387..392
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 408..417
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:3IAM"
FT HELIX 473..481
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 488..499
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 515..527
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 541..544
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:2FUG"
FT STRAND 564..570
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 581..585
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 592..597
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 619..624
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 637..646
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 657..667
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 691..696
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 708..711
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 715..718
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 720..725
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 733..738
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 741..749
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:6Q8W"
FT STRAND 758..762
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 765..768
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 783 AA; 86529 MW; 19A56201A20F9B82 CRC64;
MVRVKVNDRI VEVPPGTSVM DAVFHAGYDV PLFCSEKHLS PIGACRMCLV RIGLPKKGPD
GKPLLNEKGE PEIQWQPKLA ASCVTAVADG MVVDTLSDVV REAQAGMVEF TLLNHPLDCP
TCDKGGACEL QDRTVEYGLY EKYYQKGPLE LPVYTRFEFT RRHVDKHHPL SPFVILDRER
CIHCKRCVRY FEEVPGDEVL DFIERGVHTF IGTMDFGLPS GFSGNITDIC PVGALLDLTA
RFRARNWEME ETPTTCALCP VGCGITADTR SGELLRIRAR EVPEVNEIWI CDAGRFGHEW
ADQNRLKTPL VRKEGRLVEA TWEEAFLALK EGLKEARGEE VGLYLAHDAT LEEGLLASEL
AKALKTPHLD FQGRTAAPAS LFPPASLEDL LQADFALVLG DPTEEAPILH LRLSEFVRDL
KPPHRYNHGT PFADLQIKER MPRRTDKMAL FAPYRAPLMK WAAIHEVHRP GEEREILLAL
LGDKEGSEMV AKAKEAWEKA KNPVLILGAG VLQDTVAAER ARLLAERKGA KVLAMTPAAN
ARGLEAMGVL PGAKGASWDE PGALYAYYGF VPPEEALKGK RFVVMHLSHL HPLAERYAHV
VLPAPTFYEK RGHLVNLEGR VLPLSPAPIE NGEAEGALQV LALLAEALGV RPPFRLHLEA
QKALKARKVP EAMGRLSFRL KELRPKERKG AFYLRPTMWK AHQAVGKAQE AARAELWAHP
ETARAEALPE GAQVAVETPF GRVEARVVHR EDVPKGHLYL SALGPAAGLR VEGRVLVPAG
GEA
