ID U7LI23_9CORY Unreviewed; 709 AA.
AC U7LI23;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=HMPREF1264_00288 {ECO:0000313|EMBL:ERS57374.1};
OS Corynebacterium sp. KPL1821.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1203560 {ECO:0000313|EMBL:ERS57374.1, ECO:0000313|Proteomes:UP000017152};
RN [1] {ECO:0000313|EMBL:ERS57374.1, ECO:0000313|Proteomes:UP000017152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPL1821 {ECO:0000313|EMBL:ERS57374.1,
RC ECO:0000313|Proteomes:UP000017152};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium sp. KPL1821.";
RL Submitted (OCT-2013) 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:ERS57374.1}.
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DR EMBL; AXLZ01000001; ERS57374.1; -; Genomic_DNA.
DR RefSeq; WP_023021349.1; NZ_KI515751.1.
DR AlphaFoldDB; U7LI23; -.
DR GeneID; 81705953; -.
DR PATRIC; fig|1203560.3.peg.279; -.
DR HOGENOM; CLU_008727_3_2_11; -.
DR Proteomes; UP000017152; 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; PF12706; Lactamase_B_2; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 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|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:UP000017152};
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 158..352
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 501..505
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491"
SQ SEQUENCE 709 AA; 76683 MW; B77854E831062D30 CRC64;
MNEPRNRSRK VTRKAGPPAE NETASNEAAS PVFQAPATDA GNSAQDKPAK GDKDNSGKKN
SSDNHHDGGG NNRRSRSRGS RGRGRGGNGN GNNHGGNNNH GGNNKNGNGK GRGRNNRGRR
NVPKSMQGAD LTKRLPEPPK QPKDALRIYA LGGISEIGRN MTVFEYGDDL LIIDCGVLFP
SSGEPGVDLI LPDFGPIEKK IHKVKALVVT HAHEDHIGAI PWLLKLRPDI PIVASRFTIA
LIAAKCKEHR QKPKFVEVNE KSDVTYGPFR VRFWAVNHSV PDALGIMLGT PAGNIIHTGD
IKLDQTPLDN RPTDLPALSR YGDEGVDLML CDSTNATVPG VSASEGDIPA NFKRLVAGAK
QRVILASFAS NVYRVQAAID AAVANGRKVA FNGRSMMRNM EIAEKMGFLK VPRGTIIPID
EAAKMAPHKT MLITTGTQGE PMAALSRMAR REHRQITVRD GDTIIFSSSL IPGNEEAVYG
VINMLSQIGA NVITNQDVKV HASGHGYAGE LLFLYNAARP RNAMPVHGEW RHLRANKELA
ISTGVDRDRT VLAQNGVVVD LRKGRAEVVG QMQVGNLYVD GVSMGDVDAD TLADRTNLGT
GGVVSITCVI DNRTSRLLEH PTVSTTGFSD DDRGIVPEVA EMVENTMNDL AAEGENDTYR
MVQKLRRKVS KLMDSKYKRE PVILPTIVPT NSGPLVTDDE DVDASRESL
//
