RHO_ECOLI
ID RHO_ECOLI Reviewed; 419 AA.
AC P0AG30; P03002; Q2M891; Q48357;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transcription termination factor Rho;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase Rho;
GN Name=rho; Synonyms=nitA, psuA, rnsC, sbaA, tsu;
GN OrderedLocusNames=b3783, JW3756;
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;
RX PubMed=6304634; DOI=10.1093/nar/11.11.3531;
RA Pinkham J.L., Platt T.;
RT "The nucleotide sequence of the rho gene of E. coli K-12.";
RL Nucleic Acids Res. 11:3531-3545(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
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 1-196.
RX PubMed=2423505; DOI=10.1128/jb.166.3.945-958.1986;
RA Matsumoto Y., Shigesada K., Hirano M., Imai M.;
RT "Autogenous regulation of the gene for transcription termination factor rho
RT in Escherichia coli: localization and function of its attenuators.";
RL J. Bacteriol. 166:945-958(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 397-419.
RX PubMed=1722555; DOI=10.1111/j.1365-2958.1991.tb00809.x;
RA Ohta M., Ina K., Kusuzaki K., Kido N., Arakawa Y., Kato N.;
RT "Cloning and expression of the rfe-rff gene cluster of Escherichia coli.";
RL Mol. Microbiol. 5:1853-1862(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 405-419.
RX PubMed=7828920; DOI=10.1016/0378-1119(94)00664-e;
RA Opperman T., Martinez A., Richardson J.P.;
RT "The ts15 mutation of Escherichia coli alters the sequence of the C-
RT terminal nine residues of Rho protein.";
RL Gene 152:133-134(1995).
RN [8]
RP PROTEIN SEQUENCE OF 1-13.
RC STRAIN=K12;
RX PubMed=6219230; DOI=10.1016/0022-2836(82)90527-7;
RA Brown S., Albrechtsen B., Pedersen S., Klemm P.;
RT "Localization and regulation of the structural gene for transcription-
RT termination factor rho of Escherichia coli.";
RL J. Mol. Biol. 162:283-298(1982).
RN [9]
RP PROTEIN SEQUENCE OF 1-12.
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 [10]
RP FUNCTION, AND RNA-BINDING DOMAIN.
RX PubMed=1716628; DOI=10.1016/s0021-9258(19)47373-0;
RA Brennan C.A., Platt T.;
RT "Mutations in an RNP1 consensus sequence of Rho protein reduce RNA binding
RT affinity but facilitate helicase turnover.";
RL J. Biol. Chem. 266:17296-17305(1991).
RN [11]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=2461932; DOI=10.1016/s0021-9258(18)37353-8;
RA Dombroski A.J., Brennan C.A., Spear P., Platt T.;
RT "Site-directed alterations in the ATP-binding domain of rho protein affect
RT its activities as a termination factor.";
RL J. Biol. Chem. 263:18802-18809(1988).
RN [12]
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP CYS-202.
RX PubMed=7487110; DOI=10.1006/abbi.1995.0066;
RA Park H.G., Zhang X., Moon H.S., Zwiefka A., Cox K., Gaskell S.J.,
RA Widger W.R., Kohn H.;
RT "Bicyclomycin and dihydrobicyclomycin inhibition kinetics of Escherichia
RT coli rho-dependent transcription termination factor ATPase activity.";
RL Arch. Biochem. Biophys. 323:447-454(1995).
RN [13]
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 [14]
RP STRUCTURE BY NMR OF 1-130.
RX PubMed=9008362; DOI=10.1007/bf00228145;
RA Briercheck D.M., Allison T.J., Richardson J.P., Ellena J.F., Wood T.C.,
RA Rule S.G.;
RT "1H, 15N and 13C resonance assignments and secondary structure
RT determination of the RNA-binding domain of E.coli rho protein.";
RL J. Biomol. NMR 8:429-444(1996).
RN [15]
RP STRUCTURE BY NMR OF 1-130.
RX PubMed=9587002; DOI=10.1038/nsb0598-393;
RA Briercheck D.M., Allison T.J., Wood T.C., Richardson J.P., Rule G.S.;
RT "The NMR structure of the RNA binding domain of E. coli rho factor suggests
RT possible RNA-protein interactions.";
RL Nat. Struct. Biol. 5:393-399(1998).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-130, AND SUBUNIT.
RX PubMed=9586995; DOI=10.1038/nsb0598-352;
RA Allison T.J., Wood T.C., Briercheck D.M., Rastinejad F., Richardson J.P.,
RA Rule G.S.;
RT "Crystal structure of the RNA-binding domain from transcription termination
RT factor rho.";
RL Nat. Struct. Biol. 5:352-356(1998).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-118 IN COMPLEX WITH POLY-C
RP OLIGONUCLEOTIDE, INTERACTION WITH TARGET RNA, AND SUBUNIT.
RX PubMed=10230401; DOI=10.1016/s1097-2765(00)80476-1;
RA Bogden C.E., Fass D., Bergman N., Nichols M.D., Berger J.M.;
RT "The structural basis for terminator recognition by the Rho transcription
RT termination factor.";
RL Mol. Cell 3:487-493(1999).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH AMPPNP AND
RP OLIGONUCLEOTIDE, AND SUBUNIT.
RX PubMed=12859904; DOI=10.1016/s0092-8674(03)00512-9;
RA Skordalakes E., Berger J.M.;
RT "Structure of the Rho transcription terminator: mechanism of mRNA
RT recognition and helicase loading.";
RL Cell 114:135-146(2003).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP BICYCLOMYCIN; MAGNESIUM-ATP ANALOG AND OLIGO-U OLIGONUCLEOTIDE, AND
RP SUBUNIT.
RX PubMed=15642265; DOI=10.1016/j.str.2004.10.013;
RA Skordalakes E., Brogan A.P., Park B.S., Kohn H., Berger J.M.;
RT "Structural mechanism of inhibition of the Rho transcription termination
RT factor by the antibiotic bicyclomycin.";
RL Structure 13:99-109(2005).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH POLY-U
RP OLIGONUCLEOTIDE; ADP; MAGNESIUM AND BERYLLIUM IONS, AND SUBUNIT.
RX PubMed=19879839; DOI=10.1016/j.cell.2009.08.043;
RA Thomsen N.D., Berger J.M.;
RT "Running in reverse: the structural basis for translocation polarity in
RT hexameric helicases.";
RL Cell 139:523-534(2009).
CC -!- FUNCTION: Facilitates transcription termination by a mechanism that
CC involves Rho binding to the nascent RNA, activation of Rho's RNA-
CC dependent ATPase activity, and release of the mRNA from the DNA
CC template. RNA-dependent NTPase which utilizes all four ribonucleoside
CC triphosphates as substrates. {ECO:0000269|PubMed:1716628,
CC ECO:0000269|PubMed:2461932}.
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by bicyclomycin and
CC dihydrobicyclomycin. {ECO:0000269|PubMed:7487110}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for ATP {ECO:0000269|PubMed:7487110};
CC -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC structure. {ECO:0000269|PubMed:10230401, ECO:0000269|PubMed:12859904,
CC ECO:0000269|PubMed:15642265, ECO:0000269|PubMed:19879839,
CC ECO:0000269|PubMed:9586995}.
CC -!- INTERACTION:
CC P0AG30; P0AES0: gss; NbExp=5; IntAct=EBI-545468, EBI-557080;
CC P0AG30; P0A6X3: hfq; NbExp=5; IntAct=EBI-545468, EBI-547637;
CC P0AG30; P0AFG0: nusG; NbExp=8; IntAct=EBI-545468, EBI-369628;
CC P0AG30; P0AG30: rho; NbExp=4; IntAct=EBI-545468, EBI-545468;
CC P0AG30; P0AFW8: rof; NbExp=2; IntAct=EBI-545468, EBI-1114609;
CC P0AG30; P0CE47: tufA; NbExp=2; IntAct=EBI-545468, EBI-301077;
CC P0AG30; P0AGK4: yhbY; NbExp=3; IntAct=EBI-545468, EBI-543346;
CC -!- DOMAIN: Each subunit has two RNA-binding sites, one at the surface of
CC the hexameric ring, and one at the center of the open ring structure,
CC where RNA helicase activity is thought to take place.
CC -!- SIMILARITY: Belongs to the Rho 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; J01673; AAA24532.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67583.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76788.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77515.1; -; Genomic_DNA.
DR EMBL; M12779; AAA24695.1; -; Genomic_DNA.
DR EMBL; S75640; AAB20841.1; -; Genomic_DNA.
DR EMBL; L34404; AAA68985.1; -; Genomic_DNA.
DR PIR; A03530; TWECR.
DR RefSeq; NP_418230.1; NC_000913.3.
DR RefSeq; WP_001054527.1; NZ_STEB01000021.1.
DR PDB; 1A62; X-ray; 1.55 A; A=1-130.
DR PDB; 1A63; NMR; -; A=1-130.
DR PDB; 1A8V; X-ray; 2.00 A; A/B=1-118.
DR PDB; 1PV4; X-ray; 3.00 A; A/B/C/D/E/F=1-419.
DR PDB; 1PVO; X-ray; 3.00 A; A/B/C/D/E/F=1-419.
DR PDB; 1XPO; X-ray; 3.15 A; A/B/C/D/E/F=1-419.
DR PDB; 1XPR; X-ray; 3.15 A; A/B/C/D/E/F=1-419.
DR PDB; 1XPU; X-ray; 3.05 A; A/B/C/D/E/F=1-419.
DR PDB; 2A8V; X-ray; 2.40 A; A/B/C=1-118.
DR PDB; 2HT1; X-ray; 3.51 A; A/B=1-411.
DR PDB; 3ICE; X-ray; 2.80 A; A/B/C/D/E/F=1-419.
DR PDB; 5JJI; X-ray; 2.60 A; A/B/C/D/E/F=2-417.
DR PDB; 5JJK; X-ray; 3.15 A; A/B/C/D/E/F=2-417.
DR PDB; 5JJL; X-ray; 3.20 A; A/B/C/D/E/F=2-417.
DR PDB; 6DUQ; X-ray; 3.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-419.
DR PDB; 6WA8; X-ray; 3.30 A; A/B/C/D/E/F=1-419.
DR PDB; 6XAS; EM; 3.80 A; A/B/C/D/E/F=1-419.
DR PDB; 6XAV; EM; 7.70 A; A/B/C/D/E/F=1-419.
DR PDB; 6Z9P; EM; 3.90 A; a/b/c/d/e/f=1-419.
DR PDB; 6Z9Q; EM; 5.70 A; a/b/c/d/e/f=1-419.
DR PDB; 6Z9R; EM; 4.10 A; a/b/c/d/e/f=1-419.
DR PDB; 6Z9S; EM; 4.40 A; a/b/c/d/e/f=1-419.
DR PDB; 6Z9T; EM; 4.10 A; a/b/c/d/e/f=1-419.
DR PDB; 7ADB; EM; 4.40 A; a/b/c/d/e/f=1-419.
DR PDB; 7ADC; EM; 4.00 A; a/b/c/d/e/f=1-419.
DR PDB; 7ADD; EM; 4.30 A; a/b/c/d/e/f=1-419.
DR PDB; 7ADE; EM; 4.20 A; a/b/c/d/e/f=1-419.
DR PDBsum; 1A62; -.
DR PDBsum; 1A63; -.
DR PDBsum; 1A8V; -.
DR PDBsum; 1PV4; -.
DR PDBsum; 1PVO; -.
DR PDBsum; 1XPO; -.
DR PDBsum; 1XPR; -.
DR PDBsum; 1XPU; -.
DR PDBsum; 2A8V; -.
DR PDBsum; 2HT1; -.
DR PDBsum; 3ICE; -.
DR PDBsum; 5JJI; -.
DR PDBsum; 5JJK; -.
DR PDBsum; 5JJL; -.
DR PDBsum; 6DUQ; -.
DR PDBsum; 6WA8; -.
DR PDBsum; 6XAS; -.
DR PDBsum; 6XAV; -.
DR PDBsum; 6Z9P; -.
DR PDBsum; 6Z9Q; -.
DR PDBsum; 6Z9R; -.
DR PDBsum; 6Z9S; -.
DR PDBsum; 6Z9T; -.
DR PDBsum; 7ADB; -.
DR PDBsum; 7ADC; -.
DR PDBsum; 7ADD; -.
DR PDBsum; 7ADE; -.
DR AlphaFoldDB; P0AG30; -.
DR SMR; P0AG30; -.
DR BioGRID; 852595; 4.
DR DIP; DIP-35363N; -.
DR IntAct; P0AG30; 67.
DR MINT; P0AG30; -.
DR STRING; 511145.b3783; -.
DR jPOST; P0AG30; -.
DR PaxDb; P0AG30; -.
DR PRIDE; P0AG30; -.
DR EnsemblBacteria; AAC76788; AAC76788; b3783.
DR EnsemblBacteria; BAE77515; BAE77515; BAE77515.
DR GeneID; 67414430; -.
DR GeneID; 948297; -.
DR KEGG; ecj:JW3756; -.
DR KEGG; eco:b3783; -.
DR PATRIC; fig|511145.12.peg.3898; -.
DR EchoBASE; EB0838; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_6; -.
DR InParanoid; P0AG30; -.
DR OMA; TRLCRAH; -.
DR PhylomeDB; P0AG30; -.
DR BioCyc; EcoCyc:EG10845-MON; -.
DR BRENDA; 3.6.1.3; 2026.
DR SABIO-RK; P0AG30; -.
DR EvolutionaryTrace; P0AG30; -.
DR PRO; PR:P0AG30; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IDA:EcoCyc.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IDA:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd04459; Rho_CSD; 1.
DR CDD; cd01128; rho_factor; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01884; Rho; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041703; Rho_factor_ATP-bd.
DR InterPro; IPR011112; Rho_N.
DR InterPro; IPR036269; Rho_N_sf.
DR InterPro; IPR011113; Rho_RNA-bd.
DR InterPro; IPR004665; Term_rho.
DR PANTHER; PTHR46425; PTHR46425; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF07498; Rho_N; 1.
DR Pfam; PF07497; Rho_RNA_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00959; Rho_N; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF68912; SSF68912; 1.
DR TIGRFAMs; TIGR00767; rho; 1.
DR PROSITE; PS51856; RHO_RNA_BD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation; Transcription termination.
FT CHAIN 1..419
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188962"
FT DOMAIN 48..123
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 61..66
FT /note="RNA-binding 1"
FT REGION 78..80
FT /note="RNA-binding 1"
FT REGION 108..110
FT /note="RNA-binding 1"
FT REGION 284..288
FT /note="RNA-binding 2"
FT BINDING 169..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 181..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT SITE 326
FT /note="RNA-binding 2"
FT MUTAGEN 62
FT /note="F->L,A: Defective for RNA-binding."
FT /evidence="ECO:0000269|PubMed:2461932"
FT MUTAGEN 64
FT /note="F->L,A: Defective for RNA-binding."
FT /evidence="ECO:0000269|PubMed:2461932"
FT MUTAGEN 181
FT /note="K->Q: Partial loss of ATPase, helicase and
FT termination activity."
FT /evidence="ECO:0000269|PubMed:2461932"
FT MUTAGEN 184
FT /note="K->Q: Improves ATPase and helicase activity but
FT reduced termination activity."
FT /evidence="ECO:0000269|PubMed:2461932"
FT MUTAGEN 202
FT /note="C->G,S: Does not affect the kinetics of ATP
FT hydrolysis and inhibition by bicyclomycin."
FT /evidence="ECO:0000269|PubMed:7487110"
FT MUTAGEN 265
FT /note="D->N: Loss of ATPase activity, helicase and
FT termination activity."
FT /evidence="ECO:0000269|PubMed:2461932"
FT CONFLICT 411..419
FT /note="DFFEMMKRS -> EVMTPTY (in Ref. 7; AAA68985)"
FT /evidence="ECO:0000305"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:1A62"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:1A62"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1A62"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1A8V"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:1A62"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6WA8"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:1A62"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1XPU"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1A62"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1A62"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1A8V"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1A62"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1A62"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1A62"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1A63"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:1A62"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:3ICE"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3ICE"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5JJI"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1XPO"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3ICE"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:5JJI"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:5JJI"
FT HELIX 236..255
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:5JJI"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3ICE"
FT TURN 291..295
FT /evidence="ECO:0007829|PDB:5JJI"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3ICE"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:5JJI"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:5JJI"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:5JJI"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:3ICE"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:5JJI"
FT HELIX 374..387
FT /evidence="ECO:0007829|PDB:5JJI"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:6WA8"
FT HELIX 392..404
FT /evidence="ECO:0007829|PDB:5JJI"
FT HELIX 409..415
FT /evidence="ECO:0007829|PDB:5JJI"
SQ SEQUENCE 419 AA; 47004 MW; 5970A85334C43467 CRC64;
MNLTELKNTP VSELITLGEN MGLENLARMR KQDIIFAILK QHAKSGEDIF GDGVLEILQD
GFGFLRSADS SYLAGPDDIY VSPSQIRRFN LRTGDTISGK IRPPKEGERY FALLKVNEVN
FDKPENARNK ILFENLTPLH ANSRLRMERG NGSTEDLTAR VLDLASPIGR GQRGLIVAPP
KAGKTMLLQN IAQSIAYNHP DCVLMVLLID ERPEEVTEMQ RLVKGEVVAS TFDEPASRHV
QVAEMVIEKA KRLVEHKKDV IILLDSITRL ARAYNTVVPA SGKVLTGGVD ANALHRPKRF
FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELHLSRKIA EKRVFPAIDY
NRSGTRKEEL LTTQEELQKM WILRKIIHPM GEIDAMEFLI NKLAMTKTND DFFEMMKRS
