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Database: UniProt
Entry: D7E6M9_METEZ
LinkDB: D7E6M9_METEZ
Original site: D7E6M9_METEZ 
ID   D7E6M9_METEZ            Unreviewed;       447 AA.
AC   D7E6M9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   OrderedLocusNames=Metev_0324 {ECO:0000313|EMBL:ADI73251.1};
OS   Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC 107634
OS   / OCM 161 / Z-7303).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalobium.
OX   NCBI_TaxID=644295 {ECO:0000313|EMBL:ADI73251.1, ECO:0000313|Proteomes:UP000000391};
RN   [1] {ECO:0000313|EMBL:ADI73251.1, ECO:0000313|Proteomes:UP000000391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303
RC   {ECO:0000313|Proteomes:UP000000391};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence chromosome of Methanohalobium evestigatum Z-7303.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002069; ADI73251.1; -; Genomic_DNA.
DR   RefSeq; WP_013193819.1; NC_014253.1.
DR   AlphaFoldDB; D7E6M9; -.
DR   STRING; 644295.Metev_0324; -.
DR   GeneID; 9345939; -.
DR   KEGG; mev:Metev_0324; -.
DR   HOGENOM; CLU_008727_4_1_2; -.
DR   OrthoDB; 63419at2157; -.
DR   Proteomes; UP000000391; 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; PF12706; Lactamase_B_2; 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:UP000000391};
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..215
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   447 AA;  49369 MW;  E7571DDB4AC7CE66 CRC64;
     MTDIGIIAVG GYNEMGRNMT AIRVGEDIII LDMGLRLDRV QIHEDVEINK MHSLELIEMG
     AIPDDTIMKE INGTVRAIVC THGHLDHIGA IPKLAHRYAA PIISTPYTTS LIKQQIESEV
     KFGVKNKIVT LNAGGIYQVT EDISIEFIRA QHSIIDCVFA VIHTPDGAIL YACDYKLDRM
     PTMGEQPDFD RLKSLGEEGV LAMITESTNS GVPGKTPSER IAHDLVRDVL LGTEESDVGM
     IVTTFASHIA RINSIIKFAA EMGRTPVLIG RAMDNYVLTA KKLGYIELPD NIEVYGARKD
     VDKALKKIVN KGKDKYLPIV TGHQGEPGAI LPRIANGETP YTIESGDKVI FSANVIPSPM
     TEGNRYSLET KLKMRGARLF TDVHVSGHAC KEDHWELLRI INPEHVIPAH GTINMHSSYI
     EMAEDAGYVL GNTLHLLRNG EELYIEE
//
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