ID R9SKZ3_9EURY Unreviewed; 451 AA.
AC R9SKZ3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=Abm4_1227 {ECO:0000313|EMBL:AGN17110.1};
OS Methanobrevibacter sp. AbM4.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=224719 {ECO:0000313|EMBL:AGN17110.1, ECO:0000313|Proteomes:UP000014066};
RN [1] {ECO:0000313|EMBL:AGN17110.1, ECO:0000313|Proteomes:UP000014066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AbM4 {ECO:0000313|EMBL:AGN17110.1};
RA Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA Attwood G.T.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGN17110.1, ECO:0000313|Proteomes:UP000014066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abm4 {ECO:0000313|Proteomes:UP000014066};
RG Pastoral Greenhouse Gas Research Consortium;
RA Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA Attwood G.T.;
RT "The comlpete genome sequence of Methanobrevibacter sp. AbM4.";
RL Submitted (JUN-2013) 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; CP004050; AGN17110.1; -; Genomic_DNA.
DR RefSeq; WP_016358809.1; NC_021355.1.
DR AlphaFoldDB; R9SKZ3; -.
DR STRING; 224719.Abm4_1227; -.
DR GeneID; 15798719; -.
DR KEGG; meb:Abm4_1227; -.
DR eggNOG; arCOG00546; Archaea.
DR HOGENOM; CLU_008727_4_1_2; -.
DR OrthoDB; 63419at2157; -.
DR Proteomes; UP000014066; 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:UP000014066};
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 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 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 451 AA; 50139 MW; 869C0F95A8C3D256 CRC64;
MTVEIIAIGG YEEVGKNMTA VKVNDDVIIF DMGIHLDRIN IHEDTDIDRM HSLDLIERGV
IPDDTLMKDV DGKVKAIVFS HGHLDHIGAV AKLAHRYDAP LIGTPYTAAL IKKQIKGERK
FKVNNPIRVL NPGSKLKLSK DVTLEFVHTT HSIPQAVFPV LHTPEGIIIY ALDFKFDNHQ
KVSPPPDYER LKQLGKQGVL ALIVETTNAA NTQQVKTYSE RVPRIILEDL MREPLKEKTG
MIVTTFSSHI ERIQTIADIA KKSDREILFL GRSMERFLGI AQNLGILKLP KNSSIHGSPK
AVNRALAKAE ENRSKYLLVT TGHQGEPDAL LPRIASGKTP FNIKKGDNVI ISAPIIPNPT
NAANRHIMEA RLKASGARIY ANAHVSGHAG REDHREFLRM VKPAHIIPAH GDLHMLTAYG
ELAEEEGYRI GSNVHILRNA QAQVFNDTDE E
//
