GenomeNet

Database: UniProt
Entry: A0A3M7TVV7_9BACI
LinkDB: A0A3M7TVV7_9BACI
Original site: A0A3M7TVV7_9BACI 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system