ID A0A1Z2TKP5_9EURY Unreviewed; 440 AA.
AC A0A1Z2TKP5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=CDI07_01400 {ECO:0000313|EMBL:ASA77004.1};
OS Thermococcus sp. 5-4.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=2008440 {ECO:0000313|EMBL:ASA77004.1, ECO:0000313|Proteomes:UP000196843};
RN [1] {ECO:0000313|EMBL:ASA77004.1, ECO:0000313|Proteomes:UP000196843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-4 {ECO:0000313|EMBL:ASA77004.1,
RC ECO:0000313|Proteomes:UP000196843};
RX PubMed=28628615; DOI=10.1371/journal.pgen.1006847;
RA Cossu M., Badel C., Catchpole R., Daniele G., Marguet E., Barbe V.,
RA Forterre P., Oberto J.;
RT "Flipping chromosomes in deep-sea archaea.";
RL PLoS Genet. 13:e1006847-e1006847(2017).
RN [2] {ECO:0000313|Proteomes:UP000196843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-4 {ECO:0000313|Proteomes:UP000196843};
RA Cossu M., Badel C., Catchpole R., Daniele G., Marguet E., Barbe V.,
RA Forterre P., Oberto J.;
RT "Flipping Chromosomes in Deep-Sea Archaea.";
RL PLoS Genet. 0:0-0(2017).
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; CP021848; ASA77004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2TKP5; -.
DR KEGG; thh:CDI07_01400; -.
DR OrthoDB; 63419at2157; -.
DR Proteomes; UP000196843; 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 InterPro; IPR001587; RNase_J_CS.
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.
DR PROSITE; PS01292; UPF0036; 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 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 14..221
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 78
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 80
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 82
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 83
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 149
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 171
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 171
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 378..382
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01492"
FT BINDING 404
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 440 AA; 49306 MW; DAFED864064C00C4 CRC64;
MIKIHTVSGY EEVGKNMTAV EYNGEVVIID MGIRLDRVLI HEDVNIQQFP TKELQKLGAI
PDDSSIRNKK VVAITFTHGH LDHIGAVAKL APHYPDVPIY GTPYTIKLAK GEVKSEQYFE
VKNPMYETEY GEIVQVSENL AIEFVRITHS IPQSSMVVVH TPEGAVVHTG DFKFDNNNPL
GERPDYKRLR ELGKEGVKVL IPESTRIEQP TKTPSEAVAQ MLLEDFFLYE GMEADGLIAT
TFASHIARLQ ELIWIANKMG RQAVLVGRSL AKYTGIAKQL GLIKMKGAKA VRSPNAVRKV
LKEVSGAREN YLLIVTGHQG EPGAVLTRMA NGELYDIGKR DTVVFSAGTI PNPLNRAQRY
VLETKLKMKG VRMIKDLHVS GHASREDHRY LLRMLNPENI VPAHGDFRML THYAELAEEE
GYLIGRDVFV SRNGYLVEIR
//
