SYQ_ECOLI
ID SYQ_ECOLI Reviewed; 554 AA.
AC P00962; Q59403;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126};
DE EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:15845536, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563};
DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126};
DE Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126};
GN Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126};
GN OrderedLocusNames=b0680, JW0666;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2464170;
RA Uemura H., Conley J., Yamao F., Rogers J., Soell D.G.;
RT "Escherichia coli glutaminyl-tRNA synthetase: a single amino acid
RT replacement relaxes rRNA specificity.";
RL Protein Seq. Data Anal. 1:479-485(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6288695; DOI=10.1016/s0021-9258(18)33810-9;
RA Yamao F., Inokuchi H., Cheung A., Ozeki H., Soell D.G.;
RT "Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence
RT of the glnS gene.";
RL J. Biol. Chem. 257:11639-11643(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6389180;
RA Hoben P., Uemura H., Yamao F., Cheung A., Swanson R., Sumner-Smith M.,
RA Soell D.;
RT "Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in
RT wild-type and mutant enzymes.";
RL Fed. Proc. 43:2972-2976(1984).
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 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 [8]
RP PROTEIN SEQUENCE OF 2-6, AND CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=6749844; DOI=10.1016/s0021-9258(18)33811-0;
RA Hoben P., Royal N., Cheung A., Yamao F., Biemann K., Soell D.;
RT "Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the
RT glnS gene product.";
RL J. Biol. Chem. 257:11644-11650(1982).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=2479982; DOI=10.1126/science.2479982;
RA Rould M.A., Perona J.J., Soell D., Steitz T.A.;
RT "Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln)
RT and ATP at 2.8-A resolution.";
RL Science 246:1135-1142(1989).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1857417; DOI=10.1038/352213a0;
RA Rould M.A., Perona J.J., Steitz T.A.;
RT "Structural basis of anticodon loop recognition by glutaminyl-tRNA
RT synthetase.";
RL Nature 352:213-218(1991).
RN [12] {ECO:0007744|PDB:1QTQ}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH GLUTAMINYL-ADENYLATE
RP ANALOG AND RNA, AND CATALYTIC ACTIVITY.
RX PubMed=9562563; DOI=10.1016/s0969-2126(98)00046-x;
RA Rath V.L., Silvian L.F., Beijer B., Sproat B.S., Steitz T.A.;
RT "How glutaminyl-tRNA synthetase selects glutamine.";
RL Structure 6:439-449(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=10860750; DOI=10.1006/jmbi.2000.3749;
RA Sherlin L.D., Bullock T.L., Newberry K.J., Lipman R.S., Hou Y.M.,
RA Beijer B., Sproat B.S., Perona J.J.;
RT "Influence of transfer RNA tertiary structure on aminoacylation efficiency
RT by glutaminyl and cysteinyl-tRNA synthetases.";
RL J. Mol. Biol. 299:431-446(2000).
RN [14] {ECO:0007744|PDB:1O0B, ECO:0007744|PDB:1O0C}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 2-554 IN COMPLEX WITH AMP AND
RP L-GLUTAMINE, AND CATALYTIC ACTIVITY.
RX PubMed=12691748; DOI=10.1016/s0022-2836(03)00305-x;
RA Bullock T.L., Uter N., Nissan T.A., Perona J.J.;
RT "Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified
RT by negative determinants.";
RL J. Mol. Biol. 328:395-408(2003).
RN [15] {ECO:0007744|PDB:1ZJW}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-554 IN COMPLEX WITH AMP AND
RP L-GLUTAMINE, AND CATALYTIC ACTIVITY.
RX PubMed=15845536; DOI=10.1074/jbc.m414260200;
RA Gruic-Sovulj I., Uter N., Bullock T., Perona J.J.;
RT "tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I
RT aminoacyl-tRNA synthetase.";
RL J. Biol. Chem. 280:23978-23986(2005).
RN [16] {ECO:0007744|PDB:2RD2, ECO:0007744|PDB:2RE8}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-548 IN COMPLEX WITH
RP GLUTAMINYL-ADENYLATE ANALOG, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-31;
RP CYS-230 AND GLN-256.
RX PubMed=18477696; DOI=10.1073/pnas.0711812105;
RA Bullock T.L., Rodriguez-Hernandez A., Corigliano E.M., Perona J.J.;
RT "A rationally engineered misacylating aminoacyl-tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7428-7433(2008).
RN [17] {ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-554 IN COMPLEX WITH ATP AND
RP RNA, AND CATALYTIC ACTIVITY.
RX PubMed=23727144; DOI=10.1016/j.jmb.2013.05.018;
RA Rodriguez-Hernandez A., Spears J.L., Gaston K.W., Limbach P.A., Gamper H.,
RA Hou Y.M., Kaiser R., Agris P.F., Perona J.J.;
RT "Structural and mechanistic basis for enhanced translational efficiency by
RT 2-thiouridine at the tRNA anticodon wobble position.";
RL J. Mol. Biol. 425:3888-3906(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00126, ECO:0000269|PubMed:12691748,
CC ECO:0000269|PubMed:15845536, ECO:0000269|PubMed:18477696,
CC ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000305}.
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DR EMBL; V01575; CAA24894.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73774.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35328.1; -; Genomic_DNA.
DR EMBL; M16470; AAA69006.1; -; Genomic_DNA.
DR EMBL; M16368; AAA69006.1; JOINED; Genomic_DNA.
DR PIR; G64802; SYECQT.
DR PIR; I41235; I41235.
DR RefSeq; NP_415206.1; NC_000913.3.
DR RefSeq; WP_001287154.1; NZ_STEB01000044.1.
DR PDB; 1EUQ; X-ray; 3.10 A; A=1-548.
DR PDB; 1EUY; X-ray; 2.60 A; A=1-548.
DR PDB; 1EXD; X-ray; 2.70 A; A=1-548.
DR PDB; 1GSG; X-ray; 2.80 A; P=2-554.
DR PDB; 1GTR; X-ray; 2.50 A; A=2-554.
DR PDB; 1GTS; X-ray; 2.80 A; A=2-554.
DR PDB; 1NYL; X-ray; 2.60 A; A=9-547.
DR PDB; 1O0B; X-ray; 2.70 A; A=2-554.
DR PDB; 1O0C; X-ray; 2.70 A; A=2-554.
DR PDB; 1QRS; X-ray; 2.60 A; A=2-554.
DR PDB; 1QRT; X-ray; 2.70 A; A=2-554.
DR PDB; 1QRU; X-ray; 3.00 A; A=2-554.
DR PDB; 1QTQ; X-ray; 2.25 A; A=2-554.
DR PDB; 1ZJW; X-ray; 2.50 A; A=2-554.
DR PDB; 2RD2; X-ray; 2.60 A; A=1-548.
DR PDB; 2RE8; X-ray; 2.60 A; A=1-548.
DR PDB; 4JXX; X-ray; 2.30 A; A=2-554.
DR PDB; 4JXZ; X-ray; 2.40 A; A=2-554.
DR PDB; 4JYZ; X-ray; 2.50 A; A=2-554.
DR PDBsum; 1EUQ; -.
DR PDBsum; 1EUY; -.
DR PDBsum; 1EXD; -.
DR PDBsum; 1GSG; -.
DR PDBsum; 1GTR; -.
DR PDBsum; 1GTS; -.
DR PDBsum; 1NYL; -.
DR PDBsum; 1O0B; -.
DR PDBsum; 1O0C; -.
DR PDBsum; 1QRS; -.
DR PDBsum; 1QRT; -.
DR PDBsum; 1QRU; -.
DR PDBsum; 1QTQ; -.
DR PDBsum; 1ZJW; -.
DR PDBsum; 2RD2; -.
DR PDBsum; 2RE8; -.
DR PDBsum; 4JXX; -.
DR PDBsum; 4JXZ; -.
DR PDBsum; 4JYZ; -.
DR AlphaFoldDB; P00962; -.
DR SMR; P00962; -.
DR BioGRID; 4261207; 52.
DR DIP; DIP-9787N; -.
DR IntAct; P00962; 5.
DR STRING; 511145.b0680; -.
DR BindingDB; P00962; -.
DR SWISS-2DPAGE; P00962; -.
DR jPOST; P00962; -.
DR PaxDb; P00962; -.
DR PRIDE; P00962; -.
DR EnsemblBacteria; AAC73774; AAC73774; b0680.
DR EnsemblBacteria; BAA35328; BAA35328; BAA35328.
DR GeneID; 66671050; -.
DR GeneID; 945310; -.
DR KEGG; ecj:JW0666; -.
DR KEGG; eco:b0680; -.
DR PATRIC; fig|1411691.4.peg.1596; -.
DR EchoBASE; EB0385; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_001882_2_3_6; -.
DR InParanoid; P00962; -.
DR OMA; INNFCAQ; -.
DR PhylomeDB; P00962; -.
DR BioCyc; EcoCyc:GLNS-MON; -.
DR BioCyc; MetaCyc:GLNS-MON; -.
DR BRENDA; 6.1.1.18; 2026.
DR BRENDA; 6.1.1.24; 2026.
DR SABIO-RK; P00962; -.
DR EvolutionaryTrace; P00962; -.
DR PRO; PR:P00962; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IDA:EcoCyc.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IDA:EcoCyc.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1160.10; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00126; Gln_tRNA_synth; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR022861; Gln_tRNA_ligase_bac.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6749844,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..554
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_0000195833"
FT REGION 317..324
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126,
FT ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563"
FT MOTIF 34..44
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT MOTIF 268..272
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 35..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126,
FT ECO:0000269|PubMed:23727144, ECO:0007744|PDB:4JXX,
FT ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ"
FT BINDING 41..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126,
FT ECO:0000269|PubMed:23727144, ECO:0007744|PDB:4JXX,
FT ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ"
FT BINDING 67
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126,
FT ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:18477696,
FT ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B"
FT BINDING 212
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126,
FT ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:15845536,
FT ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563,
FT ECO:0007744|PDB:1O0B, ECO:0007744|PDB:1ZJW"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126,
FT ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144,
FT ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX,
FT ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ"
FT BINDING 261..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126,
FT ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144,
FT ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX,
FT ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ"
FT BINDING 269..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126,
FT ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144,
FT ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX,
FT ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ"
FT MUTAGEN 31
FT /note="R->A,K: Decreased affinity for glutamine and
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:18477696"
FT MUTAGEN 230
FT /note="C->R: Decreases catalytic activity 1000-fold, but
FT has no effect on affinity for glutamine. Loss of catalytic
FT activity; when associated with I-256."
FT /evidence="ECO:0000269|PubMed:18477696"
FT MUTAGEN 256
FT /note="Q->I: Loss of catalytic activity; when associated
FT with R-230."
FT /evidence="ECO:0000269|PubMed:18477696"
FT CONFLICT 549..554
FT /note="WAKVGE -> GRK (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4JXX"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1QTQ"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1QTQ"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1QTQ"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1NYL"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4JXX"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 345..354
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:1QTQ"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 466..473
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:4JXX"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 496..504
FT /evidence="ECO:0007829|PDB:1QTQ"
FT HELIX 506..510
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:1QTQ"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:1QTQ"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:1QTQ"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:1QTQ"
SQ SEQUENCE 554 AA; 63478 MW; E720164EF990F335 CRC64;
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG
QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA
YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA
SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL
YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE
GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA
ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP
NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN
RTVGLRDTWA KVGE
