ID D6E6Q5_9ACTN Unreviewed; 633 AA.
AC D6E6Q5;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=GPA_03490 {ECO:0000313|EMBL:CBL03402.1};
OS Gordonibacter pamelaeae 7-10-1-b.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL03402.1, ECO:0000313|Proteomes:UP000008805};
RN [1] {ECO:0000313|EMBL:CBL03402.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL03402.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA Pajon A.;
RL Submitted (MAR-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}.
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DR EMBL; FP929047; CBL03402.1; -; Genomic_DNA.
DR RefSeq; WP_015538752.1; NC_021021.1.
DR AlphaFoldDB; D6E6Q5; -.
DR KEGG; gpa:GPA_03490; -.
DR PATRIC; fig|657308.3.peg.3035; -.
DR HOGENOM; CLU_008727_3_2_11; -.
DR BioCyc; GPAM657308:GPA_RS01615-MONOMER; -.
DR Proteomes; UP000008805; Chromosome.
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 NCBIfam; TIGR00649; MG423; 1.
DR PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
DR Pfam; PF12706; Lactamase_B_2; 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01491};
KW Endonuclease {ECO:0000256|HAMAP-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:UP000008805};
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 99..303
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 444..448
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 633 AA; 68555 MW; B9CA7B33522C2C2B CRC64;
MEQQNNQRSE RRSQEQSRNG RGGGNGNGAK GAARGDEKKT RSYKHVQLEH RRPQLSKAGQ
GQQRQGGQQN ARRANFSSPK KDPNATLKII PLGGLDAIGK NMTVFECKGD MILDDAGLMF
PDDDHPGIDL ILPDYTYVLE NADKLRGIII THGHEDHTGT LPYLMKDLDR QIPIYGTKMT
LGLIEGKFAE HKIKNAKLIE IKPGDQVKLG CFTAEFFAVN HSIPGAVGVF FQSPAGNVLH
TGDFKLDQTP IDGVTTDFGA LAKFSKTGVD LMMSDSTNAQ NPNFTPSEAE VGKELRKIIS
QARGRVIIAS FASHIHRMQQ ICDAARDNGR KVVVTGRSMI QNTDIARRLG YLNIPDEDIV
DAYDLKGIPP EQVVIMCTGS QGEPLSALAR IANGEHKTID LEQGDTVIIS ATPVPGNEKA
VTRVINSLAK IGADVYDKKR AMVHVSGHAG AEELKLVLSI VQPNAFMPVH GEATHLRAHA
KLAEATGVPA ENVFICENGE GLELSSRGVK RGETVQSGIV FVDGLSVGDT SQDVLDERNA
LGSQGFASVA AAISSKRKDV VGEVQVEMHG ITGGDDDYLV REARSTVKNA LKRQLGKGGG
QKELKKAARD ALLSLLWERT KQRPMAIVNL LEV
//
