NARG_ECOLI
ID NARG_ECOLI Reviewed; 1247 AA.
AC P09152; P78294;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Respiratory nitrate reductase 1 alpha chain;
DE EC=1.7.5.1;
DE AltName: Full=Nitrate reductase A subunit alpha;
DE AltName: Full=Quinol-nitrate oxidoreductase subunit alpha;
GN Name=narG; Synonyms=bisD, narC; OrderedLocusNames=b1224, JW1215;
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 / TG1;
RX PubMed=2674654; DOI=10.1007/bf00331275;
RA Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.;
RT "Nitrate reductase of Escherichia coli: completion of the nucleotide
RT sequence of the nar operon and reassessment of the role of the alpha and
RT beta subunits in iron binding and electron transfer.";
RL Mol. Gen. Genet. 218:249-256(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / TG1;
RX PubMed=2233673; DOI=10.1007/bf00283030;
RA Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.;
RT "Nitrate reductases of Escherichia coli: sequence of the second nitrate
RT reductase and comparison with that encoded by the narGHJI operon.";
RL Mol. Gen. Genet. 222:104-111(1990).
RN [3]
RP SEQUENCE REVISION.
RC STRAIN=K12 / TG1;
RA Blasco F.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
RC STRAIN=K12;
RX PubMed=6094247; DOI=10.1016/0014-5793(84)81295-8;
RA McPherson M.J., Baron A.J., Pappin D.J.C., Wootton J.C.;
RT "Respiratory nitrate reductase of Escherichia coli. Sequence identification
RT of the large subunit gene.";
RL FEBS Lett. 177:260-264(1984).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RC STRAIN=PK27;
RX PubMed=2995309; DOI=10.1128/jb.164.1.25-32.1985;
RA Li S.F., Rabi T., Demoss J.A.;
RT "Delineation of two distinct regulatory domains in the 5' region of the nar
RT operon of Escherichia coli.";
RL J. Bacteriol. 164:25-32(1985).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=K12;
RX PubMed=2668029; DOI=10.1016/0014-5793(89)80906-8;
RA Noji S., Nohno T., Saito T., Taniguchi S.;
RT "The narK gene product participates in nitrate transport induced in
RT Escherichia coli nitrate-respiring cells.";
RL FEBS Lett. 252:139-143(1989).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=3308846; DOI=10.1128/jb.169.10.4614-4620.1987;
RA Li S.F., Demoss J.A.;
RT "Promoter region of the nar operon of Escherichia coli: nucleotide sequence
RT and transcription initiation signals.";
RL J. Bacteriol. 169:4614-4620(1987).
RN [11]
RP PROTEIN SEQUENCE OF 2-11.
RX PubMed=3053688; DOI=10.1016/s0021-9258(18)37572-0;
RA Sodergren E.J., Hsu P.Y., Demoss J.A.;
RT "Roles of the narJ and narI gene products in the expression of nitrate
RT reductase in Escherichia coli.";
RL J. Biol. Chem. 263:16156-16162(1988).
RN [12]
RP MUTAGENESIS OF HIS-50, AND EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
RX PubMed=9585550; DOI=10.1021/bi972858f;
RA Magalon A., Asso M., Guigliarelli B., Rothery R.A., Bertrand P.,
RA Giordano G., Blasco F.;
RT "Molybdenum cofactor properties and [Fe-S] cluster coordination in
RT Escherichia coli nitrate reductase A: investigation by site-directed
RT mutagenesis of the conserved his-50 residue in the NarG subunit.";
RL Biochemistry 37:7363-7370(1998).
RN [13]
RP INTERACTION WITH NARJ.
RX PubMed=9632249; DOI=10.1046/j.1365-2958.1998.00795.x;
RA Blasco F., Dos Santos J.P., Magalon A., Frixon C., Guigliarelli B.,
RA Santini C.L., Giordano G.;
RT "NarJ is a specific chaperone required for molybdenum cofactor assembly in
RT nitrate reductase A of Escherichia coli.";
RL Mol. Microbiol. 28:435-447(1998).
RN [14]
RP INTERACTION WITH NARJ, AND DOMAIN.
RX PubMed=16540088; DOI=10.1016/j.bbrc.2006.02.133;
RA Chan C.S., Howell J.M., Workentine M.L., Turner R.J.;
RT "Twin-arginine translocase may have a role in the chaperone function of
RT NarJ from Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 343:244-251(2006).
RN [15]
RP INTERACTION WITH NARJ, AND DOMAIN.
RC STRAIN=K12 / MC4100 / JA176;
RX PubMed=16286471; DOI=10.1074/jbc.m505902200;
RA Vergnes A., Pommier J., Toci R., Blasco F., Giordano G., Magalon A.;
RT "NarJ chaperone binds on two distinct sites of the aponitrate reductase of
RT Escherichia coli to coordinate molybdenum cofactor insertion and
RT assembly.";
RL J. Biol. Chem. 281:2170-2176(2006).
RN [16]
RP INTERACTION WITH NARJ.
RX PubMed=20236317; DOI=10.1111/j.1742-4658.2010.07611.x;
RA Zakian S., Lafitte D., Vergnes A., Pimentel C., Sebban-Kreuzer C., Toci R.,
RA Claude J.B., Guerlesquin F., Magalon A.;
RT "Basis of recognition between the NarJ chaperone and the N-terminus of the
RT NarG subunit from Escherichia coli nitrate reductase.";
RL FEBS J. 277:1886-1895(2010).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=12910261; DOI=10.1038/nsb969;
RA Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F.,
RA Weiner J.H., Strynadka N.C.J.;
RT "Insights into the respiratory electron transfer pathway from the structure
RT of nitrate reductase A.";
RL Nat. Struct. Biol. 10:681-687(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-1247.
RX PubMed=14725769; DOI=10.1016/j.str.2003.11.020;
RA Jormakka M., Richardson D., Byrne B., Iwata S.;
RT "Architecture of NarGH reveals a structural classification of Mo-bisMGD
RT enzymes.";
RL Structure 12:95-104(2004).
CC -!- FUNCTION: The nitrate reductase enzyme complex allows E.coli to use
CC nitrate as an electron acceptor during anaerobic growth. The alpha
CC chain is the actual site of nitrate reduction.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit.;
CC -!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta and a
CC gamma chain. Alpha and beta are catalytic chains; gamma chains are
CC involved in binding the enzyme complex to the cytoplasmic membrane.
CC Interacts with the NarJ chaperone. {ECO:0000269|PubMed:16286471,
CC ECO:0000269|PubMed:16540088, ECO:0000269|PubMed:20236317,
CC ECO:0000269|PubMed:9632249}.
CC -!- INTERACTION:
CC P09152; P11349: narH; NbExp=13; IntAct=EBI-547248, EBI-555067;
CC P09152; P0AF26: narJ; NbExp=18; IntAct=EBI-547248, EBI-555043;
CC P09152; P19317: narW; NbExp=9; IntAct=EBI-547248, EBI-555088;
CC P09152; P19318: narY; NbExp=5; IntAct=EBI-547248, EBI-555059;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- INDUCTION: By nitrate.
CC -!- DOMAIN: Apoenzyme contains at least 2 NarJ-binding sites, one
CC interfering with membrane anchoring and another being involved in
CC molybdenum insertion. The first binding-site is a short peptide
CC sequence near the N-terminus that contains a twin-arginine homologous
CC motif. {ECO:0000269|PubMed:16286471, ECO:0000269|PubMed:16540088}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/NAR/";
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; X16181; CAA34303.1; -; Genomic_DNA.
DR EMBL; X01164; CAA25611.1; -; Genomic_DNA.
DR EMBL; M11586; AAA24201.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74308.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36094.1; -; Genomic_DNA.
DR EMBL; X15996; CAA34127.1; -; Genomic_DNA.
DR EMBL; L36649; AAA64296.1; -; Genomic_DNA.
DR PIR; E64869; RDECNA.
DR RefSeq; NP_415742.1; NC_000913.3.
DR RefSeq; WP_000032939.1; NZ_LN832404.1.
DR PDB; 1Q16; X-ray; 1.90 A; A=1-1247.
DR PDB; 1R27; X-ray; 2.00 A; A/C=2-1247.
DR PDB; 1SIW; X-ray; 2.20 A; A=2-1247.
DR PDB; 1Y4Z; X-ray; 2.00 A; A=2-1247.
DR PDB; 1Y5I; X-ray; 1.90 A; A=2-1247.
DR PDB; 1Y5L; X-ray; 2.50 A; A=2-1247.
DR PDB; 1Y5N; X-ray; 2.50 A; A=2-1247.
DR PDB; 3EGW; X-ray; 1.90 A; A=2-1245.
DR PDB; 3IR5; X-ray; 2.30 A; A=1-1247.
DR PDB; 3IR6; X-ray; 2.80 A; A=1-1247.
DR PDB; 3IR7; X-ray; 2.50 A; A=1-1247.
DR PDBsum; 1Q16; -.
DR PDBsum; 1R27; -.
DR PDBsum; 1SIW; -.
DR PDBsum; 1Y4Z; -.
DR PDBsum; 1Y5I; -.
DR PDBsum; 1Y5L; -.
DR PDBsum; 1Y5N; -.
DR PDBsum; 3EGW; -.
DR PDBsum; 3IR5; -.
DR PDBsum; 3IR6; -.
DR PDBsum; 3IR7; -.
DR AlphaFoldDB; P09152; -.
DR SMR; P09152; -.
DR BioGRID; 4263271; 68.
DR BioGRID; 850149; 5.
DR ComplexPortal; CPX-1974; Nitrate reductase A complex.
DR DIP; DIP-10311N; -.
DR IntAct; P09152; 23.
DR MINT; P09152; -.
DR STRING; 511145.b1224; -.
DR DrugBank; DB07349; (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE.
DR DrugBank; DB04464; N-Formylmethionine.
DR TCDB; 5.A.3.1.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P09152; -.
DR PaxDb; P09152; -.
DR PRIDE; P09152; -.
DR EnsemblBacteria; AAC74308; AAC74308; b1224.
DR EnsemblBacteria; BAA36094; BAA36094; BAA36094.
DR GeneID; 945782; -.
DR KEGG; ecj:JW1215; -.
DR KEGG; eco:b1224; -.
DR PATRIC; fig|1411691.4.peg.1057; -.
DR EchoBASE; EB0632; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_6; -.
DR InParanoid; P09152; -.
DR OMA; DKPSQYF; -.
DR PhylomeDB; P09152; -.
DR BioCyc; EcoCyc:NARG-MON; -.
DR BioCyc; MetaCyc:NARG-MON; -.
DR BRENDA; 1.7.5.1; 2026.
DR EvolutionaryTrace; P09152; -.
DR PRO; PR:P09152; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:EcoCyc.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0044799; C:NarGHI complex; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:EcoCyc.
DR GO; GO:0008940; F:nitrate reductase activity; IDA:EcoCyc.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0042126; P:nitrate metabolic process; IDA:ComplexPortal.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR Gene3D; 4.10.1200.10; -; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF14710; Nitr_red_alph_N; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01580; narG; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell membrane; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Molybdenum;
KW Nitrate assimilation; Oxidoreductase; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3053688"
FT CHAIN 2..1247
FT /note="Respiratory nitrate reductase 1 alpha chain"
FT /id="PRO_0000063233"
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 223
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT MUTAGEN 50
FT /note="H->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9585550"
FT CONFLICT 10
FT /note="Y -> K (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 163..180
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 218..222
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:1Y5N"
FT HELIX 303..318
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:1Y5N"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1SIW"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 450..462
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 505..512
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 516..533
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 543..546
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 551..564
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 587..594
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 595..599
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 608..615
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 618..621
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 643..652
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:3EGW"
FT HELIX 669..675
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 680..690
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 691..693
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 702..706
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 709..714
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 717..721
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:1R27"
FT HELIX 725..731
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 744..748
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 767..775
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 778..781
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 784..789
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 805..810
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:1Y5L"
FT HELIX 823..837
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 838..841
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 844..851
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 858..860
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 864..866
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 870..872
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 879..881
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 885..892
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 893..895
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 896..900
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 906..909
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 912..914
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 917..919
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 922..932
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 936..938
FT /evidence="ECO:0007829|PDB:1Y5L"
FT TURN 939..942
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 943..945
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 949..959
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 961..963
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 965..979
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 984..986
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 988..990
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 997..1002
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1013..1015
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1019..1021
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 1027..1032
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 1050..1054
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 1072..1078
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1085..1090
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1095..1098
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 1102..1104
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 1106..1111
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1117..1121
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 1122..1128
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1135..1140
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1143..1152
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1159..1161
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1168..1171
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 1176..1178
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1179..1181
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 1185..1187
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 1195..1197
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1205..1207
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 1209..1211
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1222..1227
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1229..1231
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 1234..1238
FT /evidence="ECO:0007829|PDB:1Q16"
SQ SEQUENCE 1247 AA; 140489 MW; 640ABAD5FF01DF25 CRC64;
MSKFLDRFRY FKQKGETFAD GHGQLLNTNR DWEDGYRQRW QHDKIVRSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPMMRKRLMK
MWREAKALHS DPVEAWASII EDADKAKSFK QARGRGGFVR SSWQEVNELI AASNVYTIKN
YGPDRVAGFS PIPAMSMVSY ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE
SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ
GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY AAGRMLRAAD
LVDALGQENN PEWKTVAFNT NGEMVAPNGS IGFRWGEKGK WNLEQRDGKT GEETELQLSL
LGSQDEIAEV GFPYFGGDGT EHFNKVELEN VLLHKLPVKR LQLADGSTAL VTTVYDLTLA
NYGLERGLND VNCATSYDDV KAYTPAWAEQ ITGVSRSQII RIAREFADNA DKTHGRSMII
VGAGLNHWYH LDMNYRGLIN MLIFCGCVGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ
RPARHMNSTS YFYNHSSQWR YETVTAEELL SPMADKSRYT GHLIDFNVRA ERMGWLPSAP
QLGTNPLTIA GEAEKAGMNP VDYTVKSLKE GSIRFAAEQP ENGKNHPRNL FIWRSNLLGS
SGKGHEFMLK YLLGTEHGIQ GKDLGQQGGV KPEEVDWQDN GLEGKLDLVV TLDFRLSSTC
LYSDIILPTA TWYEKDDMNT SDMHPFIHPL SAAVDPAWEA KSDWEIYKAI AKKFSEVCVG
HLGKETDIVT LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIMVVE RDYPATYERF
TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI DAAEMILTLA
PETNGQVAVK AWAALSEFTG RDHTHLALNK EDEKIRFRDI QAQPRKIISS PTWSGLEDEH
VSYNAGYTNV HELIPWRTLS GRQQLYQDHQ WMRDFGESLL VYRPPIDTRS VKEVIGQKSN
GNQEKALNFL TPHQKWGIHS TYSDNLLMLT LGRGGPVVWL SEADAKDLGI ADNDWIEVFN
SNGALTARAV VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG
GYAHLAYGFN YYGTVGSNRD EFVVVRKMKN IDWLDGEGND QVQESVK
