NUOG_ECOLI
ID NUOG_ECOLI Reviewed; 908 AA.
AC P33602; P76489; P78184; P78185;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=NADH-quinone oxidoreductase subunit G;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit G;
DE AltName: Full=NDH-1 subunit G;
DE AltName: Full=NUO7;
GN Name=nuoG; OrderedLocusNames=b2283, JW2278;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX PubMed=7690854; DOI=10.1006/jmbi.1993.1488;
RA Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
RT "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase
RT in Escherichia coli. Organization of the 14 genes and relationship between
RT the derived proteins and subunits of mitochondrial complex I.";
RL J. Mol. Biol. 233:109-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-170.
RX PubMed=8157582; DOI=10.1128/jb.176.8.2143-2150.1994;
RA Pruss B.M., Nelms J.M., Park C., Wolfe A.J.;
RT "Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect
RT growth on mixed amino acids.";
RL J. Bacteriol. 176:2143-2150(1994).
RN [6]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
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 believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient.
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; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 3 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC -!- INTERACTION:
CC P33602; P33599: nuoC; NbExp=2; IntAct=EBI-559737, EBI-552399;
CC P33602; P0AFD1: nuoE; NbExp=4; IntAct=EBI-559737, EBI-1117136;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell
CC inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16079137}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA16111.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA48366.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X68301; CAA48366.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75343.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16111.2; ALT_INIT; Genomic_DNA.
DR EMBL; L25055; AAA03538.1; -; Unassigned_DNA.
DR PIR; A65000; A65000.
DR RefSeq; NP_416786.4; NC_000913.3.
DR RefSeq; WP_000190939.1; NZ_LN832404.1.
DR PDB; 7NYR; EM; 3.30 A; G=1-908.
DR PDB; 7NYU; EM; 3.80 A; G=1-908.
DR PDB; 7NYV; EM; 3.70 A; G=1-908.
DR PDB; 7NZ1; EM; 2.10 A; G=1-908.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR PDBsum; 7NZ1; -.
DR AlphaFoldDB; P33602; -.
DR SMR; P33602; -.
DR BioGRID; 4260512; 49.
DR BioGRID; 851103; 6.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-10383N; -.
DR IntAct; P33602; 32.
DR STRING; 511145.b2283; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P33602; -.
DR PaxDb; P33602; -.
DR PRIDE; P33602; -.
DR EnsemblBacteria; AAC75343; AAC75343; b2283.
DR EnsemblBacteria; BAA16111; BAA16111; BAA16111.
DR GeneID; 946762; -.
DR KEGG; ecj:JW2278; -.
DR KEGG; eco:b2283; -.
DR PATRIC; fig|511145.12.peg.2376; -.
DR EchoBASE; EB2011; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_11_4_6; -.
DR InParanoid; P33602; -.
DR OMA; NVYFGRV; -.
DR PhylomeDB; P33602; -.
DR BioCyc; EcoCyc:NUOG-MON; -.
DR BioCyc; MetaCyc:NUOG-MON; -.
DR PRO; PR:P33602; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc.
DR GO; GO:0045271; C:respiratory chain complex I; IC:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
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:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
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; 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; 1.
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 inner membrane; Cell membrane;
KW Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Quinone; Reference proteome; Translocase; Ubiquinone.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..908
FT /note="NADH-quinone oxidoreductase subunit G"
FT /id="PRO_0000118546"
FT DOMAIN 2..83
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 83..122
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 221..277
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:0000250"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 188
FT /note="T -> Q (in Ref. 1; CAA48366)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="T -> K (in Ref. 1; CAA48366)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="Missing (in Ref. 1; CAA48366)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="S -> T (in Ref. 1; CAA48366)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 255..260
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 343..358
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 415..422
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 438..442
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 451..465
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 477..491
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 494..501
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 507..522
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 538..544
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 577..583
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 626..630
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 636..639
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 648..661
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 669..679
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 681..688
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 712..719
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 730..741
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 762..768
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 769..771
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 810..815
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 818..820
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 825..827
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 831..834
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 844..850
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 857..862
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 865..873
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 881..885
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 893..895
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 903..905
FT /evidence="ECO:0007829|PDB:7NZ1"
SQ SEQUENCE 908 AA; 100299 MW; 7B8626E19709D540 CRC64;
MATIHVDGKE YEVNGADNLL EACLSLGLDI PYFCWHPALG SVGACRQCAV KQYQNAEDTR
GRLVMSCMTP ASDGTFISID DEEAKQFRES VVEWLMTNHP HDCPVCEEGG NCHLQDMTVM
TGHSFRRYRF TKRTHRNQDL GPFISHEMNR CIACYRCVRY YKDYADGTDL GVYGAHDNVY
FGRPEDGTLE SEFSGNLVEI CPTGVFTDKT HSERYNRKWD MQFAPSICQQ CSIGCNISPG
ERYGELRRIE NRYNGTVNHY FLCDRGRFGY GYVNLKDRPR QPVQRRGDDF ITLNAEQAMQ
GAADILRQSK KVIGIGSPRA SVESNFALRE LVGEENFYTG IAHGEQERLQ LALKVLREGG
IYTPALREIE SYDAVLVLGE DVTQTGARVA LAVRQAVKGK AREMAAAQKV ADWQIAAILN
IGQRAKHPLF VTNVDDTRLD DIAAWTYRAP VEDQARLGFA IAHALDNSAP AVDGIEPELQ
SKIDVIVQAL AGAKKPLIIS GTNAGSLEVI QAAANVAKAL KGRGADVGIT MIARSVNSMG
LGIMGGGSLE EALTELETGR ADAVVVLEND LHRHASAIRV NAALAKAPLV MVVDHQRTAI
MENAHLVLSA ASFAESDGTV INNEGRAQRF FQVYDPAYYD SKTVMLESWR WLHSLHSTLL
SREVDWTQLD HVIDAVVAKI PELAGIKDAA PDATFRIRGQ KLAREPHRYS GRTAMRANIS
VHEPRQPQDI DTMFTFSMEG NNQPTAHRSQ VPFAWAPGWN SPQAWNKFQD EVGGKLRFGD
PGVRLFETSE NGLDYFTSVP ARFQPQDGKW RIAPYYHLFG SDELSQRAPV FQSRMPQPYI
KLNPADAAKL GVNAGTRVSF SYDGNTVTLP VEIAEGLTAG QVGLPMGMSG IAPVLAGAHL
EDLKEAQQ
