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Database: UniProt
Entry: E6LHH5_ENTI1
LinkDB: E6LHH5_ENTI1
Original site: E6LHH5_ENTI1 
ID   E6LHH5_ENTI1            Unreviewed;       567 AA.
AC   E6LHH5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491};
DE            Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491};
GN   Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN   ORFNames=HMPREF9088_1815 {ECO:0000313|EMBL:EFU73374.1};
OS   Enterococcus italicus (strain DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=888064 {ECO:0000313|EMBL:EFU73374.1, ECO:0000313|Proteomes:UP000010296};
RN   [1] {ECO:0000313|EMBL:EFU73374.1, ECO:0000313|Proteomes:UP000010296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5
RC   {ECO:0000313|Proteomes:UP000010296};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease
CC       activity. Involved in maturation of rRNA and in some organisms also
CC       mRNA maturation and/or decay. {ECO:0000256|HAMAP-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   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFU73374.1}.
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DR   EMBL; AEPV01000069; EFU73374.1; -; Genomic_DNA.
DR   RefSeq; WP_007208828.1; NZ_JXKT01000027.1.
DR   AlphaFoldDB; E6LHH5; -.
DR   STRING; 888064.HMPREF9088_1815; -.
DR   PATRIC; fig|888064.11.peg.1115; -.
DR   eggNOG; COG0595; Bacteria.
DR   HOGENOM; CLU_008727_3_1_9; -.
DR   OMA; KNTCVFE; -.
DR   OrthoDB; 9758375at2; -.
DR   Proteomes; UP000010296; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd07714; RNaseJ_MBL-fold; 1.
DR   Gene3D; 3.10.20.580; -; 1.
DR   Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   HAMAP; MF_01491; RNase_J_bact; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR011108; RMMBL.
DR   InterPro; IPR004613; RNase_J.
DR   InterPro; IPR042173; RNase_J_2.
DR   InterPro; IPR030854; RNase_J_bac.
DR   InterPro; IPR041636; RNase_J_C.
DR   InterPro; IPR001587; RNase_J_CS.
DR   NCBIfam; TIGR00649; MG423; 1.
DR   PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR   PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   Pfam; PF17770; RNase_J_C; 1.
DR   PIRSF; PIRSF004803; RnjA; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS01292; UPF0036; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_01491};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01491};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010296};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01491}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          22..216
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   BINDING         365..369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT                   ECO:0000256|PIRSR:PIRSR004803-2"
SQ   SEQUENCE   567 AA;  61998 MW;  41BA7DD4B51992D1 CRC64;
     MKVSLKNNET GVFGIGGLGE IGKNCYGVQF QDEIILIDAG IKFPEDELLG IDYVISDYSY
     IIQNLHKVKG LFITHGHEDH IGGIPFLLRQ ANMPIYAGPL AMALITNKLE EHGLLRDAEL
     HEIHEDTIVR FRKTAVSFFR TTHSIPDTLG VVVKTPSGNI VATGDFKFDF TPVGEPADLH
     KMARIGEEGV LCLLSDSTNA EIPTFTKSEK TIGSSIVHIF EKIEGRIIFA SFASNIFRLQ
     QAADAAVATG RKIAVFGRSM ENAIVNGQRL GYINVPKGTF VDASELNKLP ANETLILCTG
     SQGEPMAALS RIANGTHRQI QIHPDDTVIF SSSPIPGNTT SVNHLINLLL QAGANVIHGK
     LNNIHTSGHG GQEEQKLMLR LMKPKFFMPV HGEFRMLKIH TKLAQATGVP RENCYILENG
     DMLALTADTA RVAGHFNAND VYVDGNGVGD IGNVVLRDRR ILSEEGLVLA VATVDIAKKE
     ILSGPEILSR GFVYMRESGE MINEGQGILF RALREALKQP DCNEHKLKEA MAGALQPFLF
     DQTERHPMIL GMIMTPDPLN TEASPAQ
//
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