ID Q0W8D5_METAR Unreviewed; 445 AA.
AC Q0W8D5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=LRC396 {ECO:0000313|EMBL:CAJ35358.1};
OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=351160 {ECO:0000313|EMBL:CAJ35358.1, ECO:0000313|Proteomes:UP000000663};
RN [1] {ECO:0000313|EMBL:CAJ35358.1, ECO:0000313|Proteomes:UP000000663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22066 / NBRC 105507 / MRE50
RC {ECO:0000313|Proteomes:UP000000663};
RX PubMed=16857943; DOI=10.1126/science.1127062;
RA Erkel C., Kube M., Reinhardt R., Liesack W.;
RT "Genome of rice cluster I archaea -- the key methane producers in the rice
RT rhizosphere.";
RL Science 313:370-372(2006).
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; AM114193; CAJ35358.1; -; Genomic_DNA.
DR RefSeq; WP_012037134.1; NC_009464.1.
DR AlphaFoldDB; Q0W8D5; -.
DR STRING; 351160.LRC396; -.
DR GeneID; 5143185; -.
DR KEGG; rci:LRC396; -.
DR PATRIC; fig|351160.9.peg.2889; -.
DR eggNOG; arCOG00546; Archaea.
DR OrthoDB; 63419at2157; -.
DR Proteomes; UP000000663; 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; IPR011108; RMMBL.
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; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01492};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01492};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01492};
KW Reference proteome {ECO:0000313|Proteomes:UP000000663};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01492};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01492}.
FT DOMAIN 16..230
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 82
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 84
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 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 87
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 152
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 174
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 174
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 384..388
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT BINDING 410
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 445 AA; 49669 MW; 6A6EF31C4603CD03 CRC64;
MKDVGIIAVG GYEEVGRNMT AIRVGKDIVV MDMGVRLDRI QIHEETEIEK MHSLDLIQMG
AIPDDKIMNN VDGNVIGIVC SHGHLDHIGA VPKLAHRYKC PIIGTPFTAE LIRQEIESER
KFDVANKVND LPCGQIMELS KNISIELIRV QHSIIDCAFV AVHTPSGVIL YACDFKIDRT
PVIGEAPDFK RLKQIGKEGV LAMITESTNV NRSGKTPSEK VARDLVWDAL LGTEETESGV
LVTTFSSHIA RLKSIIEAAE KMNRIPVLLG NSMERYYGTA LKMGYVKKPD NLRIFGYRKS
IVKEVKRMMD DGKEKYLPII TGHQGEPGAI LGRIASGELD YKLESGDKII FSANVIPNQL
NMANRYSLET KLKMKGARIY DNVHVSGHAY KEDHWELLRM VKPEHVIPAH GTLEMHSAYA
EMAEDTGYEF GQTVHILRNG QELSL
//
