ID G0HEJ7_CORVD Unreviewed; 711 AA.
AC G0HEJ7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 OrderedLocusNames=CVAR_1629 {ECO:0000313|EMBL:AEK36983.1};
OS Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS NCIMB 30131) (Corynebacterium mooreparkense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK36983.1, ECO:0000313|Proteomes:UP000006659};
RN [1] {ECO:0000313|EMBL:AEK36983.1, ECO:0000313|Proteomes:UP000006659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC {ECO:0000313|Proteomes:UP000006659};
RX PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA Schroeder J., Maus I., Trost E., Tauch A.;
RT "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT from the surface of smear-ripened cheeses and insights into cheese ripening
RT and flavor generation.";
RL BMC Genomics 12:545-545(2011).
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; CP002917; AEK36983.1; -; Genomic_DNA.
DR RefSeq; WP_014010148.1; NC_015859.1.
DR AlphaFoldDB; G0HEJ7; -.
DR STRING; 858619.CVAR_1629; -.
DR KEGG; cva:CVAR_1629; -.
DR eggNOG; COG0595; Bacteria.
DR HOGENOM; CLU_008727_3_2_11; -.
DR Proteomes; UP000006659; 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 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 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 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 162..356
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505..509
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491"
SQ SEQUENCE 711 AA; 76537 MW; B2688BD6F3FB4A33 CRC64;
MTDNRSRARK VTRKAAPPSA ETAASAASTP AFNDGGVADA AQSGQASAPA TESGESTDSR
KNESGNEGRN SQGGNRNRSR RSRGNRSERN DNSRNDNKGG NRNRGGQNRN DNGGGNRGGG
DRRRNAVQTM QGADLTQRLP KPPKAPKDGL RLVALGGISE IGRNMTVFEY HDRLLIIDCG
VLFPSSGEPG VDLILPDFSY LEGKWDKVEA LVVTHGHEDH IGAIPWLLKQ RSDIPIIASR
FTCALIAAKC QEHRQRPKLI QVDDTSHEKR GPFDIRFFNV GHSIPECLGI ALKTPAGLLI
HTGDVKMDQT PADGRPTDLP ALSRFGDEGV DLMLCDSTNA TTPGVSPSEA GIAPTLERLI
SNAKQRVLVA SFASNVSRVQ MAVDAAVKAG RKVAFSGRSM IRNMEIAERL GLLTAPRGTI
VSMDEASRLA PHKVVLITTG TQGEPMAALS RMARREHRQI TIRPGDLIIL SSSLVPGNEE
AVFGVINMLS QIGATVITGK DAMVHTSGHG YSGELLFLYN AARPKNAMPV HGEWRHLRAN
RELAISTGVN PDNTVLAQNG GVVDLVNGHA KVVGQIPVGN LYVDGVTMGD VGAEEIEDRT
QMSEGGLISV TVVIDNRSGR PLEDPQVVAK GFSEGSKEMM KQVAEVVDNA MLDLSGQGEN
DPYRMAQTLR RKVAKFVKDK WKREPMIIPT IVPMTSEVVE ELDPEDHAPS L
//
