ID A0A3M7TVV7_9BACI Unreviewed; 554 AA.
AC A0A3M7TVV7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803};
DE Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803};
GN Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN ORFNames=EBO34_07710 {ECO:0000313|EMBL:RNA69810.1};
OS Alteribacter keqinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacter.
OX NCBI_TaxID=2483800 {ECO:0000313|EMBL:RNA69810.1, ECO:0000313|Proteomes:UP000278746};
RN [1] {ECO:0000313|EMBL:RNA69810.1, ECO:0000313|Proteomes:UP000278746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KQ-3 {ECO:0000313|EMBL:RNA69810.1,
RC ECO:0000313|Proteomes:UP000278746};
RA Wang H.;
RT "Bacillus Keqinensis sp. nov., a moderately halophilic bacterium isolated
RT from a saline-alkaline lake.";
RL Submitted (OCT-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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR004803};
CC Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or
CC Mg(2+) is physiologically important. {ECO:0000256|PIRNR:PIRNR004803};
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 ECO:0000256|PIRNR:PIRNR004803}.
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 ECO:0000256|PIRNR:PIRNR004803}.
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:RNA69810.1}.
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DR EMBL; RHIB01000001; RNA69810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7TVV7; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000278746; 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 ECO:0000256|PIRNR:PIRNR004803};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491};
KW Reference proteome {ECO:0000313|Proteomes:UP000278746};
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 20..214
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 363..367
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 554 AA; 61112 MW; 0BC61D13F0771A2D CRC64;
MKAKNHQAAV FALGGLGEIG KNTYAVQFQD EIILIDAGIK FPEDELLGID YVIPDYTYLV
KNEDKIKGLF ITHGHEDHIG GVPYLLRQVN IPIYGGKLAL GLLRNKLEEH GLLRNAKLIE
IQEDDVIKFQ KTSVSFYRTT HSIPDSFGVV VKTPAGNIVH TGDFKFDFTP VGEPANLTKM
AKIGEEGVLC LLSDSTNSEV PGFTMSERKV GESIDNIFRS VEGRIIFATF ASNIYRLQQA
VEAAVKFRRK VAVFGRSMEN AINIGLDLGY INAPKNTFID ASQLNKIPAE QVVILCTGSQ
GEPMAALSRI AFGTHRQIQV IPGDTVVFSS SPIPGNTLSV SKTINQLYRA GANVIHGSLN
DIHTSGHGGQ EEQKLMLRLM KPKYFMPIHG EFRMQKMHAT LAEGCGIPEE NCFLMDNGDV
LALDKEEARL AGKVPSGSIY VDGSGIGDIG NIVLRDRRIL SEEGLVVVVV SLNMKEFKVT
AGPDLISRGF VYMRESSDLI NEAQKMLASH LDGMMERKTT QWSEIKNEIS DVLGPFLYEK
TKRKPMILPI IMEV
//