ID Q3IPL0_NATPD Unreviewed; 446 AA.
AC Q3IPL0;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
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 ECO:0000313|EMBL:CAI49940.1};
GN OrderedLocusNames=NP_3698A {ECO:0000313|EMBL:CAI49940.1};
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780 {ECO:0000313|EMBL:CAI49940.1, ECO:0000313|Proteomes:UP000002698};
RN [1] {ECO:0000313|EMBL:CAI49940.1, ECO:0000313|Proteomes:UP000002698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 /
RC NCIMB 2260 / Gabara {ECO:0000313|Proteomes:UP000002698};
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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}.
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DR EMBL; CR936257; CAI49940.1; -; Genomic_DNA.
DR RefSeq; WP_011323558.1; NC_007426.1.
DR AlphaFoldDB; Q3IPL0; -.
DR STRING; 348780.NP_3698A; -.
DR EnsemblBacteria; CAI49940; CAI49940; NP_3698A.
DR GeneID; 3701841; -.
DR KEGG; nph:NP_3698A; -.
DR eggNOG; arCOG00546; Archaea.
DR HOGENOM; CLU_008727_4_1_2; -.
DR OrthoDB; 63419at2157; -.
DR Proteomes; UP000002698; Chromosome.
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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01492, ECO:0000313|EMBL:CAI49940.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01492};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01492};
KW Reference proteome {ECO:0000313|Proteomes:UP000002698};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01492}; Zinc {ECO:0000256|HAMAP-Rule:MF_01492}.
FT DOMAIN 15..225
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 383..387
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT BINDING 409
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 446 AA; 49498 MW; F58928BCE6E0C767 CRC64;
MEVEIATIGG YEEVGRQMTA VRAGDNVVIF DMGLNLSKVL IHDNVETERM HSLDLIDMGA
IPDDRVMSDI EGDVQAIVPT HGHLDHIGAI SKLAHRYDAP IVATPFTIEL VKQQIEGEEK
FGVQNDLVKM DAGGTMPIGE KCELEFVNVT HSIIDAINPV LHTPEGAVVY GLDKRMDHNP
VLGDPIDMDR FREIGREGVL CYIEDCTNAG KKGKTPSESV ARSQLKDVMY SLEDYDGGIV
ATTFSSHIAR VKSLVEFAED IGRQPVLLGR SMEKYSGTAE RLDFVDFPSD LGMYGHRKSV
DRTFKRIMDE GKEDYLPVVT GHQGEPRAML TRMARGETPY ELDEGDKVIF SARVIPEPTN
EGQRYQAEKL LGMQGARIYD DIHVSGHLNS EGHYQMLQAL NPTNVIPAHQ DMKGFSPYVE
LASNEGYELG RDLHVTKNGN TIQLTE
//
