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Ribonuclease J1 (RNase J1) (EC 3.1.-.-)

 RNJ1_BACSU              Reviewed;         555 AA.
Q45493;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 114.
RecName: Full=Ribonuclease J1 {ECO:0000255|HAMAP-Rule:MF_01491};
Short=RNase J1 {ECO:0000255|HAMAP-Rule:MF_01491};
EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491};
Name=rnjA {ECO:0000255|HAMAP-Rule:MF_01491}; Synonyms=ykqC;
OrderedLocusNames=BSU14530;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
Winters P., Caldwell R.M., Enfield L., Ferrari E.;
"The ampS-nprE (124 degrees-127 degrees) region of the Bacillus
subtilis 168 chromosome: sequencing of a 27 kb segment and
identification of several genes in the area.";
Microbiology 142:3033-3037(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Caldwell R.M., Ferrari E.;
"Sequence analysis of the mobA-ampS region of the Bacillus subtilis
chromosome.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
FUNCTION AS AN ENDONUCLEASE, COFACTOR, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=168;
PubMed=15831787; DOI=10.1093/nar/gki505;
Even S., Pellegrini O., Zig L., Labas V., Vinh J.,
Brechemmier-Baey D., Putzer H.;
"Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis
with functional homology to E.coli RNase E.";
Nucleic Acids Res. 33:2141-2152(2005).
[5]
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=168;
PubMed=17005971; DOI=10.1099/mic.0.29152-0;
Hunt A., Rawlins J.P., Thomaides H.B., Errington J.;
"Functional analysis of 11 putative essential genes in Bacillus
subtilis.";
Microbiology 152:2895-2907(2006).
[6]
FUNCTION AS AN EXONUCLEASE, ENZYME REGULATION, DISRUPTION PHENOTYPE,
AND MUTAGENESIS OF HIS-76.
PubMed=17512403; DOI=10.1016/j.cell.2007.02.051;
Mathy N., Benard L., Pellegrini O., Daou R., Wen T., Condon C.;
"5'-to-3' exoribonuclease activity in bacteria: role of RNase J1 in
rRNA maturation and 5' stability of mRNA.";
Cell 129:681-692(2007).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-76.
STRAIN=168;
PubMed=17229210; DOI=10.1111/j.1365-2958.2006.05499.x;
Britton R.A., Wen T., Schaefer L., Pellegrini O., Uicker W.C.,
Mathy N., Tobin C., Daou R., Szyk J., Condon C.;
"Maturation of the 5' end of Bacillus subtilis 16S rRNA by the
essential ribonuclease YkqC/RNase J1.";
Mol. Microbiol. 63:127-138(2007).
[8]
FUNCTION IN PRE-SCRNA PROCESSING, AND DISRUPTION PHENOTYPE.
PubMed=17576666; DOI=10.1093/nar/gkm460;
Yao S., Blaustein J.B., Bechhofer D.H.;
"Processing of Bacillus subtilis small cytoplasmic RNA: evidence for
an additional endonuclease cleavage site.";
Nucleic Acids Res. 35:4464-4473(2007).
[9]
FUNCTION IN MRNA DECAY, AND DISRUPTION PHENOTYPE.
PubMed=18445592; DOI=10.1074/jbc.M801461200;
Deikus G., Condon C., Bechhofer D.H.;
"Role of Bacillus subtilis RNase J1 endonuclease and 5'-exonuclease
activities in trp leader RNA turnover.";
J. Biol. Chem. 283:17158-17167(2008).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18713320; DOI=10.1111/j.1365-2958.2008.06400.x;
Mader U., Zig L., Kretschmer J., Homuth G., Putzer H.;
"mRNA processing by RNases J1 and J2 affects Bacillus subtilis gene
expression on a global scale.";
Mol. Microbiol. 70:183-196(2008).
[11]
FUNCTION AS AN ENDONUCLEASE, DOMAIN, AND MUTAGENESIS OF ASP-45;
78-ASP-HIS-79; ASN-337 AND SER-366.
PubMed=18204464; DOI=10.1038/nsmb.1376;
Li de la Sierra-Gallay I., Zig L., Jamalli A., Putzer H.;
"Structural insights into the dual activity of RNase J.";
Nat. Struct. Mol. Biol. 15:206-212(2008).
[12]
SUBUNIT.
STRAIN=168;
PubMed=19193632; DOI=10.1074/mcp.M800546-MCP200;
Commichau F.M., Rothe F.M., Herzberg C., Wagner E., Hellwig D.,
Lehnik-Habrink M., Hammer E., Volker U., Stulke J.;
"Novel activities of glycolytic enzymes in Bacillus subtilis:
interactions with essential proteins involved in mRNA processing.";
Mol. Cell. Proteomics 8:1350-1360(2009).
[13]
FUNCTION IN 23S RRNA PROCESSING, RNASE ACTIVITY, AND DISRUPTION
PHENOTYPE.
PubMed=19880604; DOI=10.1128/JB.01096-09;
Redko Y., Condon C.;
"Maturation of 23S rRNA in Bacillus subtilis in the absence of Mini-
III.";
J. Bacteriol. 192:356-359(2010).
[14]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH RNASE J2,
AND SUBUNIT.
STRAIN=168;
PubMed=20025672; DOI=10.1111/j.1365-2958.2009.07004.x;
Mathy N., Hebert A., Mervelet P., Benard L., Dorleans A.,
Li de la Sierra-Gallay I., Noirot P., Putzer H., Condon C.;
"Bacillus subtilis ribonucleases J1 and J2 form a complex with altered
enzyme behaviour.";
Mol. Microbiol. 75:489-498(2010).
[15]
INTERACTION WITH RNY, AND SUBUNIT.
STRAIN=168;
PubMed=21803996; DOI=10.1128/JB.05500-11;
Lehnik-Habrink M., Newman J., Rothe F.M., Solovyova A.S.,
Rodrigues C., Herzberg C., Commichau F.M., Lewis R.J., Stulke J.;
"RNase Y in Bacillus subtilis: a natively disordered protein that is
the functional equivalent of RNase E from Escherichia coli.";
J. Bacteriol. 193:5431-5441(2011).
[16]
FUNCTION.
PubMed=22014150; DOI=10.1111/j.1365-2958.2011.07888.x;
Taverniti V., Forti F., Ghisotti D., Putzer H.;
"Mycobacterium smegmatis RNase J is a 5'-3' exo-/endoribonuclease and
both RNase J and RNase E are involved in ribosomal RNA maturation.";
Mol. Microbiol. 82:1260-1276(2011).
[17]
FUNCTION, INTERACTION WITH RNASE J2, AND SUBUNIT.
PubMed=21893286; DOI=10.1016/j.str.2011.06.018;
Dorleans A., Li de la Sierra-Gallay I., Piton J., Zig L., Gilet L.,
Putzer H., Condon C.;
"Molecular basis for the recognition and cleavage of RNA by the
bifunctional 5'-3' exo/endoribonuclease RNase J.";
Structure 19:1252-1261(2011).
[18]
INTERACTION WITH PNP, AND SUBUNIT.
STRAIN=168;
PubMed=22198292; DOI=10.1016/j.jmb.2011.12.024;
Newman J.A., Hewitt L., Rodrigues C., Solovyova A.S., Harwood C.R.,
Lewis R.J.;
"Dissection of the network of interactions that links RNA processing
with glycolysis in the Bacillus subtilis degradosome.";
J. Mol. Biol. 416:121-136(2012).
[19]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=168;
PubMed=22412379; DOI=10.1371/journal.pgen.1002520;
Durand S., Gilet L., Bessieres P., Nicolas P., Condon C.;
"Three essential ribonucleases-RNase Y, J1, and III-control the
abundance of a majority of Bacillus subtilis mRNAs.";
PLoS Genet. 8:E1002520-E1002520(2012).
[20]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=168 / JH642, 168 / PY79, 168 / W168, and 168 trpC2;
PubMed=23504012; DOI=10.1128/JB.00164-13;
Figaro S., Durand S., Gilet L., Cayet N., Sachse M., Condon C.;
"Bacillus subtilis mutants with knockouts of the genes encoding
ribonucleases RNase Y and RNase J1 are viable, with major defects in
cell morphology, sporulation, and competence.";
J. Bacteriol. 195:2340-2348(2013).
[21]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN OPEN CONFORMATION, ACTIVE
SITE, DISCUSSION OF MECHANISM, AND SUBUNIT.
STRAIN=168;
PubMed=21893285; DOI=10.1016/j.str.2011.06.017;
Newman J.A., Hewitt L., Rodrigues C., Solovyova A., Harwood C.R.,
Lewis R.J.;
"Unusual, dual endo- and exonuclease activity in the degradosome
explained by crystal structure analysis of RNase J1.";
Structure 19:1241-1251(2011).
-!- FUNCTION: An RNase that has endonuclease and 5'-3' exonuclease
activity, playing a role in both rRNA and mRNA stability and
degradation. Endonuclease activity can cleave within 4 nucleotides
of the 5'-end of a triphosphorylated RNA. Endonuclease digestion
by the RNase J1/J2 complex occurs at a different site and in some
cases more efficiently than J1 or J2 alone. The exonuclease
activity of the J1/J2 complex is highly processive on substrates
longer than 5 nucleotides, on shorter substrates is distributive.
Preferentially cleaves ssRNA, possibly in AU-rich regions. The 5'-
exonuclease activity acts on 5'-hydroxyl and 5'-monophosphate but
not 5'-triphosphate ends; it can digest through stem-loop
structures if they are not too stable. Required for maturation of
16S rRNA. Acts preferentially on 16S rRNA precursors after
association of the 30S and 50S ribosomal subunits. Plays a role in
the secondary pathway of 23S rRNA 5' end maturation. Probably also
participates in processing of pre-scRNA (the precursor of the
signal recognition particle RNA). {ECO:0000269|PubMed:15831787,
ECO:0000269|PubMed:17229210, ECO:0000269|PubMed:17512403,
ECO:0000269|PubMed:17576666, ECO:0000269|PubMed:18204464,
ECO:0000269|PubMed:18445592, ECO:0000269|PubMed:18713320,
ECO:0000269|PubMed:19880604, ECO:0000269|PubMed:20025672,
ECO:0000269|PubMed:21893286, ECO:0000269|PubMed:22014150,
ECO:0000269|PubMed:22412379, ECO:0000269|PubMed:23504012}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:15831787};
Note=Binds 1 Ca(2+) cation per subunit. Seen in 1 crystal
structure, it is not clear if it is physiologically important.
{ECO:0000269|PubMed:15831787};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:15831787};
Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or
Mg(2+) is physiologically important.
{ECO:0000269|PubMed:15831787};
-!- ENZYME REGULATION: 30S ribosomal subunit binding to Shine-Dalgarno
sequences blocks exonuclease activity.
{ECO:0000269|PubMed:17512403}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.47 uM for exonuclease on 30 nt RNA hybridized to 17 nt
quenching DNA, J1 alone {ECO:0000269|PubMed:20025672};
KM=0.22 uM for exonuclease on 30 nt RNA hybridized to 17 nt
quenching DNA, J1/J2 complex {ECO:0000269|PubMed:20025672};
Note=kcat is 0.58 sec (-1) for J1, 0.13 sec (-1) for J1/J2 and
<0.005 sec (-1) for J2.;
-!- SUBUNIT: Unclear whether it forms homodimers or belongs to a
larger complex. According to (PubMed:20025672) probably does not
form homodimers, while (PubMed:21893285) shows homodimer
formation. Both reports show RNase J1 and J2 interaction, probably
as a heterotetramer (PubMed:19193632) shows it is a component of a
possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp,
pfkA and eno, while (PubMed:20025672) finds no evidence of an RNA
degradosome complex. {ECO:0000269|PubMed:19193632,
ECO:0000269|PubMed:20025672, ECO:0000269|PubMed:21803996,
ECO:0000269|PubMed:21893285, ECO:0000269|PubMed:21893286,
ECO:0000269|PubMed:22198292}.
-!- INTERACTION:
O31774:rny; NbExp=2; IntAct=EBI-6415229, EBI-6415578;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491,
ECO:0000269|PubMed:15831787, ECO:0000269|PubMed:17005971}.
Note=Colocalizes with ribosomes.
-!- DOMAIN: The C-terminal domain (residues 450-555) are required for
nuclease activity and dimerization. {ECO:0000269|PubMed:18204464}.
-!- DISRUPTION PHENOTYPE: Essential. In depletion experiments there is
decreased 5'-exonuclease processing of 16S rRNA (PubMed:17512403),
decreased accumulation of correctly-sized scRNA (PubMed:17576666),
decreased decay of trp mRNA leader (PubMed:18445592), while
correct processing of the 5' end of 23S rRNA no longer occurs in
the absence of mrnC (PubMed:19880604). While depletion/deletion of
RNase J1 or J2 has no large impact on global gene expression, a
double mutant alters the expression of hundreds of genes
(PubMed:18713320). In a more severe depletion experiment
alteration of about 30% of transcripts was seen (PubMed:22412379).
Later shown not to be essential in 4 strains, with a tripled
doubling time. 168 trpC2 cells able to grow on minimal medium.
Loss of competence for plasmid transformation, nearly complete
loss of sporulation, poor growth at 30 degrees Celsius and no
growth under 25 degrees Celsius. Increased sensitivity to a wide
range of antibiotics. Irregularly shaped cells form clumps of
spiral cells connected by long chains, with few visible septa,
cell walls are altered with looser, less dense peptidoglycan.
Double pnp-rnjA or rnjA-rny mutants could not be isolated
(PubMed:23504012). {ECO:0000269|PubMed:17005971,
ECO:0000269|PubMed:17229210, ECO:0000269|PubMed:17512403,
ECO:0000269|PubMed:17576666, ECO:0000269|PubMed:18445592,
ECO:0000269|PubMed:18713320, ECO:0000269|PubMed:19880604,
ECO:0000269|PubMed:22412379, ECO:0000269|PubMed:23504012}.
-!- MISCELLANEOUS: Present in about 2500 monomers per cell in mid-log
phase.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
RNA-metabolizing metallo-beta-lactamase-like family. Bacterial
RNase J subfamily. {ECO:0000255|HAMAP-Rule:MF_01491}.
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EMBL; AF012285; AAC24928.1; -; Genomic_DNA.
EMBL; AL009126; CAB13326.1; -; Genomic_DNA.
PIR; B69862; B69862.
RefSeq; NP_389336.1; NC_000964.3.
RefSeq; WP_003245660.1; NZ_JNCM01000035.1.
PDB; 3ZQ4; X-ray; 3.00 A; A/C/D/E=1-555.
PDBsum; 3ZQ4; -.
ProteinModelPortal; Q45493; -.
SMR; Q45493; -.
DIP; DIP-46392N; -.
IntAct; Q45493; 3.
MINT; MINT-8365355; -.
STRING; 224308.Bsubs1_010100008056; -.
PaxDb; Q45493; -.
PRIDE; Q45493; -.
EnsemblBacteria; CAB13326; CAB13326; BSU14530.
GeneID; 939483; -.
KEGG; bsu:BSU14530; -.
PATRIC; fig|224308.179.peg.1583; -.
eggNOG; ENOG4105CN5; Bacteria.
eggNOG; COG0595; LUCA.
HOGENOM; HOG000280201; -.
InParanoid; Q45493; -.
KO; K12574; -.
OMA; KNTCVFE; -.
PhylomeDB; Q45493; -.
BioCyc; BSUB:BSU14530-MONOMER; -.
EvolutionaryTrace; Q45493; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:UniProtKB.
GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006397; P:mRNA processing; IDA:UniProtKB.
GO; GO:0006364; P:rRNA processing; IDA:UniProtKB.
Gene3D; 3.60.15.10; -; 1.
HAMAP; MF_01491; RNase_J_bact; 1.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR011108; RMMBL.
InterPro; IPR004613; RNase_J.
InterPro; IPR030854; RNase_J_bac.
InterPro; IPR001587; RNase_J_CS.
Pfam; PF00753; Lactamase_B; 1.
Pfam; PF07521; RMMBL; 1.
PIRSF; PIRSF004803; RnjA; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
TIGRFAMs; TIGR00649; MG423; 1.
PROSITE; PS01292; UPF0036; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Cytoplasm; Endonuclease;
Exonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease;
Reference proteome; RNA-binding; rRNA processing; Zinc.
CHAIN 1 555 Ribonuclease J1.
/FTId=PRO_0000215268.
REGION 364 368 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01491}.
REGION 450 555 Required for endo- and 5'-exonuclease
activity and dimerization.
ACT_SITE 195 195 Proton donor.
{ECO:0000305|PubMed:21893285}.
ACT_SITE 368 368 Proton acceptor.
{ECO:0000305|PubMed:21893285}.
METAL 49 49 Calcium; via carbonyl oxygen.
METAL 51 51 Calcium.
METAL 74 74 Zinc 1; via pros nitrogen; catalytic.
METAL 76 76 Zinc 1; via pros nitrogen; catalytic.
METAL 78 78 Zinc 2; catalytic.
METAL 79 79 Zinc 2; via tele nitrogen; catalytic.
METAL 142 142 Zinc 1; via tele nitrogen; catalytic.
METAL 164 164 Zinc 1; catalytic.
METAL 164 164 Zinc 2; catalytic.
METAL 390 390 Zinc 2; via tele nitrogen; catalytic.
METAL 443 443 Calcium.
MUTAGEN 45 45 D->A: Slight decrease in endonuclease and
10-fold decrease in 5'-exonuclease
activity; when associated with A-337.
{ECO:0000269|PubMed:18204464}.
MUTAGEN 76 76 H->A: Loss of endo- and 5'-exonuclease
activity. {ECO:0000269|PubMed:17229210,
ECO:0000269|PubMed:17512403}.
MUTAGEN 78 79 DH->KA: Severe loss of endo- and 5'-
exonuclease activity.
{ECO:0000269|PubMed:18204464}.
MUTAGEN 337 337 N->A: Slight decrease in endonuclease and
10-fold decrease in 5'-exonuclease
activity; when associated with A-45.
{ECO:0000269|PubMed:18204464}.
MUTAGEN 366 366 S->L: 30% endonuclease and 10% 5'-
exonuclease activity.
{ECO:0000269|PubMed:18204464}.
STRAND 8 21 {ECO:0000244|PDB:3ZQ4}.
STRAND 24 29 {ECO:0000244|PDB:3ZQ4}.
STRAND 32 38 {ECO:0000244|PDB:3ZQ4}.
STRAND 51 55 {ECO:0000244|PDB:3ZQ4}.
HELIX 58 61 {ECO:0000244|PDB:3ZQ4}.
TURN 62 66 {ECO:0000244|PDB:3ZQ4}.
STRAND 67 73 {ECO:0000244|PDB:3ZQ4}.
HELIX 77 80 {ECO:0000244|PDB:3ZQ4}.
HELIX 83 87 {ECO:0000244|PDB:3ZQ4}.
STRAND 94 96 {ECO:0000244|PDB:3ZQ4}.
HELIX 98 111 {ECO:0000244|PDB:3ZQ4}.
TURN 113 116 {ECO:0000244|PDB:3ZQ4}.
STRAND 119 121 {ECO:0000244|PDB:3ZQ4}.
STRAND 128 130 {ECO:0000244|PDB:3ZQ4}.
STRAND 133 141 {ECO:0000244|PDB:3ZQ4}.
STRAND 143 154 {ECO:0000244|PDB:3ZQ4}.
STRAND 157 161 {ECO:0000244|PDB:3ZQ4}.
STRAND 172 174 {ECO:0000244|PDB:3ZQ4}.
HELIX 178 186 {ECO:0000244|PDB:3ZQ4}.
STRAND 189 195 {ECO:0000244|PDB:3ZQ4}.
TURN 197 200 {ECO:0000244|PDB:3ZQ4}.
HELIX 208 221 {ECO:0000244|PDB:3ZQ4}.
STRAND 226 229 {ECO:0000244|PDB:3ZQ4}.
HELIX 235 246 {ECO:0000244|PDB:3ZQ4}.
TURN 247 249 {ECO:0000244|PDB:3ZQ4}.
STRAND 251 256 {ECO:0000244|PDB:3ZQ4}.
HELIX 257 267 {ECO:0000244|PDB:3ZQ4}.
HELIX 268 270 {ECO:0000244|PDB:3ZQ4}.
HELIX 276 278 {ECO:0000244|PDB:3ZQ4}.
HELIX 282 284 {ECO:0000244|PDB:3ZQ4}.
TURN 285 287 {ECO:0000244|PDB:3ZQ4}.
HELIX 290 292 {ECO:0000244|PDB:3ZQ4}.
STRAND 293 297 {ECO:0000244|PDB:3ZQ4}.
HELIX 307 312 {ECO:0000244|PDB:3ZQ4}.
STRAND 326 329 {ECO:0000244|PDB:3ZQ4}.
HELIX 338 350 {ECO:0000244|PDB:3ZQ4}.
STRAND 354 356 {ECO:0000244|PDB:3ZQ4}.
STRAND 358 361 {ECO:0000244|PDB:3ZQ4}.
HELIX 371 380 {ECO:0000244|PDB:3ZQ4}.
STRAND 383 391 {ECO:0000244|PDB:3ZQ4}.
HELIX 393 405 {ECO:0000244|PDB:3ZQ4}.
HELIX 410 412 {ECO:0000244|PDB:3ZQ4}.
STRAND 421 425 {ECO:0000244|PDB:3ZQ4}.
STRAND 428 431 {ECO:0000244|PDB:3ZQ4}.
STRAND 439 443 {ECO:0000244|PDB:3ZQ4}.
HELIX 452 464 {ECO:0000244|PDB:3ZQ4}.
STRAND 466 473 {ECO:0000244|PDB:3ZQ4}.
STRAND 475 477 {ECO:0000244|PDB:3ZQ4}.
STRAND 480 492 {ECO:0000244|PDB:3ZQ4}.
HELIX 494 497 {ECO:0000244|PDB:3ZQ4}.
HELIX 500 516 {ECO:0000244|PDB:3ZQ4}.
HELIX 523 542 {ECO:0000244|PDB:3ZQ4}.
STRAND 547 554 {ECO:0000244|PDB:3ZQ4}.
SEQUENCE 555 AA; 61517 MW; 48091B448B8431C9 CRC64;
MKFVKNDQTA VFALGGLGEI GKNTYAVQFQ DEIVLIDAGI KFPEDELLGI DYVIPDYTYL
VKNEDKIKGL FITHGHEDHI GGIPYLLRQV NIPVYGGKLA IGLLRNKLEE HGLLRQTKLN
IIGEDDIVKF RKTAVSFFRT THSIPDSYGI VVKTPPGNIV HTGDFKFDFT PVGEPANLTK
MAEIGKEGVL CLLSDSTNSE NPEFTMSERR VGESIHDIFR KVDGRIIFAT FASNIHRLQQ
VIEAAVQNGR KVAVFGRSME SAIEIGQTLG YINCPKNTFI EHNEINRMPA NKVTILCTGS
QGEPMAALSR IANGTHRQIS INPGDTVVFS SSPIPGNTIS VSRTINQLYR AGAEVIHGPL
NDIHTSGHGG QEEQKLMLRL IKPKFFMPIH GEYRMQKMHV KLATDCGIPE ENCFIMDNGE
VLALKGDEAS VAGKIPSGSV YIDGSGIGDI GNIVLRDRRI LSEEGLVIVV VSIDMDDFKI
SAGPDLISRG FVYMRESGDL INDAQELISN HLQKVMERKT TQWSEIKNEI TDTLAPFLYE
KTKRRPMILP IIMEV


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