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 02-SEP-2026, entry version 228. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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=nitrate + a quinol = a quinone + nitrite + H2O; 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 --------------------------------------------------------------------------- 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_CP009789.1. 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 PDB; 8JZD; X-ray; 2.45 A; B/D=1-15. DR AlphaFoldDB; P09152; -. DR SMR; P09152; -. DR BioGRID; 4263271; 74. DR BioGRID; 850149; 5. DR ComplexPortal; CPX-1974; Nitrate reductase A complex. DR DIP; DIP-10311N; -. DR FunCoup; P09152; 374. 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; 511145-b1224; -. DR EnsemblBacteria; AAC74308; AAC74308; b1224. DR GeneID; 945782; -. DR KEGG; ecj:JW1215; -. DR KEGG; eco:b1224; -. DR KEGG; ecoc:C3026_07200; -. 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; VWMSEAD; -. DR OrthoDB; 9759518at2; -. DR PhylomeDB; P09152; -. DR BioCyc; EcoCyc:NARG-MONOMER; -. DR BioCyc; MetaCyc:NARG-MONOMER; -. DR BRENDA; 1.7.5.1; 2026. DR EvolutionaryTrace; P09152; -. DR PHI-base; PHI:10512; -. DR PRO; PR:P09152; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P09152; -. 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:0043546; F:molybdopterin cofactor binding; IDA:EcoCyc. DR GO; GO:0160182; F:nitrate reductase (quinone) activity; IEA:UniProtKB-EC. 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:0042126; P:nitrate metabolic process; IDA:ComplexPortal. DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1. DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1. DR FunFam; 3.40.50.12440:FF:000001; Nitrate reductase subunit alpha; 1. DR FunFam; 4.10.1200.10:FF:000001; Respiratory nitrate reductase subunit alpha; 1. DR Gene3D; 3.40.50.12440; -; 1. DR Gene3D; 4.10.1200.10; nitrate reductase tail; 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 NCBIfam; TIGR01580; narG; 1. DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1. DR PANTHER; PTHR43105:SF8; RESPIRATORY NITRATE REDUCTASE 1 ALPHA CHAIN; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR Pfam; PF28599; NarG_dom_V; 1. DR Pfam; PF14710; Nitr_red_alph_N; 1. DR SMART; SM00926; Molybdop_Fe4S4; 1. DR SUPFAM; SSF50692; ADC-like; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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. 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 PDBsum; 8JZD; -. 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:1Y5I" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 94..97 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 99..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..315 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 316..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 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 728..733 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 744..748 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 750..752 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 880..882 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 HELIX 1007..1009 FT /evidence="ECO:0007829|PDB:1Y5L" 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 HELIX 1034..1036 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 HELIX 1064..1066 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 //