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

 E0PCZ7_STREI            Unreviewed;       553 AA.
E0PCZ7;
02-NOV-2010, integrated into UniProtKB/TrEMBL.
02-NOV-2010, sequence version 1.
05-JUN-2019, entry version 36.
RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491};
Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491};
Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
ORFNames=HMPREF9319_0720 {ECO:0000313|EMBL:EFM27750.1};
Streptococcus equinus ATCC 700338.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=864569 {ECO:0000313|EMBL:EFM27750.1, ECO:0000313|Proteomes:UP000004290};
[1] {ECO:0000313|EMBL:EFM27750.1, ECO:0000313|Proteomes:UP000004290}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700338 {ECO:0000313|EMBL:EFM27750.1,
ECO:0000313|Proteomes:UP000004290};
Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
Petrosino J., Highlander S., Gibbs R.;
Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly
endonuclease activity. Involved in maturation of rRNA and in some
organisms also mRNA maturation and/or decay. {ECO:0000256|HAMAP-
Rule:MF_01491}.
-!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
{ECO:0000256|HAMAP-Rule:MF_01491}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
RNA-metabolizing metallo-beta-lactamase-like family. Bacterial
RNase J subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01491}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EFM27750.1}.
-----------------------------------------------------------------------
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EMBL; AEEL01000012; EFM27750.1; -; Genomic_DNA.
RefSeq; WP_003064302.1; NZ_GL397128.1.
EnsemblBacteria; EFM27750; EFM27750; HMPREF9319_0720.
BioCyc; GCF_000146405-HMP:HMPREF9319_RS03490-MONOMER; -.
Proteomes; UP000004290; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
Gene3D; 3.40.50.10710; -; 1.
Gene3D; 3.60.15.10; -; 1.
HAMAP; MF_01491; RNase_J_bact; 1.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
InterPro; IPR011108; RMMBL.
InterPro; IPR004613; RNase_J.
InterPro; IPR042173; RNase_J_2.
InterPro; IPR030854; RNase_J_bac.
InterPro; IPR041636; RNase_J_C.
Pfam; PF00753; Lactamase_B; 1.
Pfam; PF07521; RMMBL; 1.
Pfam; PF17770; RNase_J_C; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
TIGRFAMs; TIGR00649; MG423; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000004290};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491};
Endonuclease {ECO:0000256|HAMAP-Rule:MF_01491};
Exonuclease {ECO:0000256|HAMAP-Rule:MF_01491};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01491};
Nuclease {ECO:0000256|HAMAP-Rule:MF_01491};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_01491};
rRNA processing {ECO:0000256|HAMAP-Rule:MF_01491}.
DOMAIN 16 212 Lactamase_B. {ECO:0000259|SMART:SM00849}.
SEQUENCE 553 AA; 61531 MW; 3A5FCBE00E4B1398 CRC64;
MSDIKIIALG GVRENAKNLY VVEVNDSIFI LDAGLKYPEN EQLGVDEVIP NIDYLVENKK
RVQGIFLTHG HADAIGALPY ILSEFKAPVF GSPLTIELAK LFVKKNNNVK KFNNFHVIDA
ETEIEFADAT ISFFKSTHSV PESLGIVVGT DEGNIVYTGD FKFDQAARKY YRTDLSRLTE
IGREGVLALL SDSANATSNV LTASESEVAA EMDSIIADAE GRVIIAAVAS NLIRIQQVFD
SAADYGRRVV LTGFDAENIV RTAIRMKRLR LVDEKLIVKP KDMHKFEDHE LIILETGRMG
EPINGLQKMA LGRHRYVQIK EGDLVYIVTT PSLSKEAAVA RVENLIYKAG GVVKLITQTM
NVSGHANARD LQLMINLLHP KYLFPVQGEY RNLATHAELA QEVGMYPENI YIVKRGDVMV
LDKDGFNHEG SVPAGDVMID GNAIGDVGNI VLRDRKVLSE DGIFIVALTV NKREKKIVSK
AKIHTRGFVY VKKSRDILRE SAELVNQTVE NYLAQDSFDW GELKGAVRDE VAKFLFDQTK
RRPAILPVVM EVR


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[rnj Rv2752c] Ribonuclease J (RNase J) (EC 3.1.-.-) (Beta-lactamase) (EC 3.5.2.6) (Penicillinase)
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[Dicer1 Dicer Mdcr] Endoribonuclease Dicer (EC 3.1.26.3) (Double-strand-specific ribonuclease mDCR-1)
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[hchA A8M42_01610 AM465_15370 AWF23_018680 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C1I57_21890 C7B02_06890 C7H11_13425 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D3C88_02905 D6X47_12880 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 EPS76_06485 ERS085406_02591 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150 WM48_10115] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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