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Database: UniProt/TrEMBL
Entry: B7HDS1_BACC4
LinkDB: B7HDS1_BACC4
Original site: B7HDS1_BACC4 
ID   B7HDS1_BACC4            Unreviewed;       556 AA.
AC   B7HDS1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   29-APR-2015, entry version 40.
DE   RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803};
DE            Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803};
GN   Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN   OrderedLocusNames=BCB4264_A3896 {ECO:0000313|EMBL:ACK62190.1};
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532 {ECO:0000313|EMBL:ACK62190.1, ECO:0000313|Proteomes:UP000007096};
RN   [1] {ECO:0000313|EMBL:ACK62190.1, ECO:0000313|Proteomes:UP000007096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264 {ECO:0000313|EMBL:ACK62190.1,
RC   ECO:0000313|Proteomes:UP000007096};
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly
CC       endonuclease activity. Involved in maturation of rRNA and in some
CC       organisms also mRNA maturation and/or decay. {ECO:0000256|HAMAP-
CC       Rule:MF_01491}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR004803};
CC       Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or
CC       Mg(2+) is physiologically important.
CC       {ECO:0000256|PIRNR:PIRNR004803};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01491};
CC       Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if
CC       Zn(2+) or Mg(2+) is physiologically important. {ECO:0000256|HAMAP-
CC       Rule:MF_01491};
CC   -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC       {ECO:0000256|HAMAP-Rule:MF_01491}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491,
CC       ECO:0000256|PIRNR:PIRNR004803}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       RNA-metabolizing metallo-beta-lactamase-like family. Bacterial
CC       RNase J subfamily. {ECO:0000256|HAMAP-Rule:MF_01491,
CC       ECO:0000256|PIRNR:PIRNR004803}.
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DR   EMBL; CP001176; ACK62190.1; -; Genomic_DNA.
DR   RefSeq; YP_002368599.1; NC_011725.1.
DR   STRING; 405532.BCB4264_A3896; -.
DR   EnsemblBacteria; ACK62190; ACK62190; BCB4264_A3896.
DR   KEGG; bcb:BCB4264_A3896; -.
DR   PATRIC; 18879693; VBIBacCer117876_3753.
DR   eggNOG; COG0595; -.
DR   HOGENOM; HOG000280201; -.
DR   KO; K12574; -.
DR   OMA; INGLIRW; -.
DR   OrthoDB; EOG6P5ZDC; -.
DR   BioCyc; BCER405532:GI1K-3866-MONOMER; -.
DR   Proteomes; UP000007096; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01491; RNase_J_bact; 1.
DR   InterPro; IPR001279; Beta-lactamas-like.
DR   InterPro; IPR011108; RMMBL.
DR   InterPro; IPR004613; RNase_J.
DR   InterPro; IPR030854; RNase_J_bac.
DR   InterPro; IPR001587; RNase_J_CS.
DR   PANTHER; PTHR11203:SF22; PTHR11203:SF22; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   PIRSF; PIRSF004803; RnjA; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR00649; MG423; 1.
DR   PROSITE; PS01292; UPF0036; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007096};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491,
KW   ECO:0000256|PIRNR:PIRNR004803};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_01491,
KW   ECO:0000256|PIRNR:PIRNR004803};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01491,
KW   ECO:0000256|PIRNR:PIRNR004803};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01491,
KW   ECO:0000256|PIRNR:PIRNR004803};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01491,
KW   ECO:0000256|PIRNR:PIRNR004803};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01491,
KW   ECO:0000256|PIRNR:PIRNR004803};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01491}.
FT   REGION      365    369       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
FT   METAL        74     74       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
FT   METAL        76     76       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
FT   METAL        78     78       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
FT   METAL        79     79       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
FT   METAL       142    142       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
FT   METAL       164    164       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
FT   METAL       164    164       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
FT   METAL       391    391       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491}.
SQ   SEQUENCE   556 AA;  60962 MW;  E97BF95BC7CAF762 CRC64;
     MKRKENESVK VFALGGVGEI GKNMYCVEID SEIFIVDAGL MFPGDEMFGI DIVIPDITYL
     VENQERVKGL FITHGHEDHI GGIVYVLRKL SIPVYATKLT VGLIQEKLGE AGMLGRVDLK
     TIDSNSTVEF NTTTVSFFGT THSIPDSVGV CFHTSKGAVV YTGDFKFDQT PIGNSGADLG
     KMAQIGNEGV LCLLSDSTNA ERPGYTGSEK EVGVEISKVF YGAEGRIIVA SFASNVHRIQ
     QVFDAAAETG RKVAVVGRSM VKVVDIARRL GYLNVPEGMV ISLQEVDNFP EKKVAILTTG
     SQGEPMAALS RMAKQAHKQI SIRKGDTVII AASPIPGNEI SVSKIIDLLF RAGAEVVYYG
     ERKVHVSGHG SQEELKLMLN LMKPKYFVPV HGEFRMQKAH AYLAEDVGIT RENIFIVEKG
     DVIAFGDDEA NLVGKVQAGN VLIDGLGVGD VGNIVLRDRK MLSQDGILVV VVTLGKDEKK
     IISGPEIISR GFVYVRESEA LIERSTEIVR MIVEQSIKEY SIEWSMLKQN IRELLGQFLY
     EETKRKPMIL PIIMEV
//
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