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}.
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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
//