GenomeNet

Database: UniProt
Entry: M0CT69_9EURY
LinkDB: M0CT69_9EURY
Original site: M0CT69_9EURY 
ID   M0CT69_9EURY            Unreviewed;       448 AA.
AC   M0CT69;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01492};
DE            Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01492};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01492};
GN   Name=rnj {ECO:0000256|HAMAP-Rule:MF_01492};
GN   ORFNames=C475_10328 {ECO:0000313|EMBL:ELZ25592.1};
OS   Halosimplex carlsbadense 2-9-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halosimplex.
OX   NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ25592.1, ECO:0000313|Proteomes:UP000011626};
RN   [1] {ECO:0000313|EMBL:ELZ25592.1, ECO:0000313|Proteomes:UP000011626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ25592.1,
RC   ECO:0000313|Proteomes:UP000011626};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: An RNase that has 5'-3' exonuclease activity. May be involved
CC       in RNA degradation. {ECO:0000256|HAMAP-Rule:MF_01492}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01492};
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|HAMAP-Rule:MF_01492};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01492}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01492}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. Archaeal RNase J
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01492}.
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:ELZ25592.1}.
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; AOIU01000024; ELZ25592.1; -; Genomic_DNA.
DR   RefSeq; WP_006883740.1; NZ_AOIU01000024.1.
DR   AlphaFoldDB; M0CT69; -.
DR   STRING; 797114.C475_10328; -.
DR   PATRIC; fig|797114.5.peg.2100; -.
DR   eggNOG; arCOG00546; Archaea.
DR   OrthoDB; 63419at2157; -.
DR   Proteomes; UP000011626; 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-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07714; RNaseJ_MBL-fold; 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_01492; RNase_J_arch; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR004613; RNase_J.
DR   InterPro; IPR042173; RNase_J_2.
DR   InterPro; IPR030879; RNase_J_arc.
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   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_01492};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01492}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01492};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01492};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011626};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01492}; Zinc {ECO:0000256|HAMAP-Rule:MF_01492}.
FT   DOMAIN          15..226
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT   BINDING         385..389
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT   BINDING         411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
SQ   SEQUENCE   448 AA;  50053 MW;  193E55E0645761A0 CRC64;
     MEIEIATIGG YEEVGRQMTA VRAGDDVVVF DMGLNLSKVL IHDNVETERM HSLDLIDMGA
     IPDDRVMSDL EGDVKAIVPT HGHLDHIGAI SKLAHRYDAP IVATPFTIEL VKQQIKSEEK
     FGVQNDLKKM EAGETMSIGD KNELEFVNVT HSIIDAINPV LHTPEGAIVY GLDKRMDHTP
     VIGDPIDMER FREIGREGEG VLCYIEDCTN AGKKGRTPSE SVARRHLKDV MYSLEDYDGG
     IVATTFSSHI ARVTSLVEFA EDIGRQPVLL GRSMEKYSGT AERLDFVDFP DDLGMYGHRK
     SVDRTFKRIM NEGKENFLPI VTGHQGEPRA MLTRMGRGET PYEIDDGDKV IFSARVIPEP
     TNEGQRYQSE KLLGMQGARI YDDIHVSGHL NKEGHYEMLD ALQPQNIIPA HQDLSGFSDY
     VNLCESEGYK MGRDLHVTRN GNLIQLVE
//
DBGET integrated database retrieval system