ID A0A1H4RNV7_9MICC Unreviewed; 563 AA.
AC A0A1H4RNV7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=C6401_00290 {ECO:0000313|EMBL:PSS45695.1}, SAMN04489745_2610
GN {ECO:0000313|EMBL:SEC33498.1};
OS Arthrobacter woluwensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=156980 {ECO:0000313|EMBL:SEC33498.1, ECO:0000313|Proteomes:UP000182652};
RN [1] {ECO:0000313|EMBL:SEC33498.1, ECO:0000313|Proteomes:UP000182652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10495 {ECO:0000313|EMBL:SEC33498.1,
RC ECO:0000313|Proteomes:UP000182652};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSS45695.1, ECO:0000313|Proteomes:UP000240525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM-35 {ECO:0000313|EMBL:PSS45695.1,
RC ECO:0000313|Proteomes:UP000240525};
RA Nazipi S., Marshall I.P.G., Schramm A., Suvanto M.T., Hansen J.H.;
RT "Draft genome sequence of Arthrobacter woluwensis NM-35, an antimicrobial
RT bacteria found in nests of social spider Stegodyphus dumicola.";
RL Submitted (MAR-2018) 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; PVZO01000001; PSS45695.1; -; Genomic_DNA.
DR EMBL; FNSN01000003; SEC33498.1; -; Genomic_DNA.
DR RefSeq; WP_066215319.1; NZ_VEMO01000003.1.
DR AlphaFoldDB; A0A1H4RNV7; -.
DR SMR; A0A1H4RNV7; -.
DR STRING; 156980.SAMN04489745_2610; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000182652; Unassembled WGS sequence.
DR Proteomes; UP000240525; 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 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.
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:UP000182652};
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 32..226
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 374..378
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 563 AA; 61057 MW; 5A6A8E20C495CCB4 CRC64;
MTQLAFSHLT TPPKLAKDTL RIVPLGGLGE VGRNMAVFEI AGKLLIVDCG VLFPEETQPG
VDLILPDFSY IEDRVDDILA VILTHGHEDH IGAVPYLLRL RRDIPLVGSQ LTLALVEAKL
VEHRIRPKTM VVEEGQVEQF GPFNCEFVAV NHSIPDALAV FIRTAGGTVL HTGDFKMDQL
PLDGRITDLR HFARLGEEGV DLFMSDSTNA DVPGFTTAEK EIGPTLDRLF GQAKKRIIVA
SFSSHVHRVQ QVLDAAAKHG RKVAFVGRSM VRNMQIAAKL GYLEVPDGIL VDLKNVDKLP
DEKVVLMSTG SQGEPMAALS RMANGDHRVQ VGTGDTVILA SSLIPGNENA VFRIINGLLK
LGADVIHKGN AKVHVSGHAA AGELLYCYNI LEPLNAMPVH GETRHLIANG KIAEESGVPG
ENIILADNGT VVDLHDGLAN IVGQVEVGFV YVDGSSVGEI TDADLKDRRI LGDEGFISIV
TVINRSTGKV VSGPEIHARG VAEEDAVFDE IIPKINAALE EAVAERKDHT THQLQQVVRR
VIGTWVNRRL RRKPMIIPVV LEA
//
