RNJ_METJA
ID RNJ_METJA Reviewed; 448 AA.
AC Q58271;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ribonuclease J {ECO:0000255|HAMAP-Rule:MF_01492};
DE Short=RNase J {ECO:0000255|HAMAP-Rule:MF_01492};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01492};
GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01492}; OrderedLocusNames=MJ0861;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease activity. May be involved
CC in RNA degradation. {ECO:0000255|HAMAP-Rule:MF_01492}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01492};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01492}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01492}.
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DR EMBL; L77117; AAB98866.1; -; Genomic_DNA.
DR PIR; E64407; E64407.
DR RefSeq; WP_010870376.1; NC_000909.1.
DR AlphaFoldDB; Q58271; -.
DR SMR; Q58271; -.
DR STRING; 243232.MJ_0861; -.
DR EnsemblBacteria; AAB98866; AAB98866; MJ_0861.
DR GeneID; 1451750; -.
DR KEGG; mja:MJ_0861; -.
DR eggNOG; arCOG00546; Archaea.
DR HOGENOM; CLU_008727_4_1_2; -.
DR InParanoid; Q58271; -.
DR OMA; KNTCVFE; -.
DR OrthoDB; 12384at2157; -.
DR PhylomeDB; Q58271; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease 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 Gene3D; 3.40.50.10710; -; 1.
DR Gene3D; 3.60.15.10; -; 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 Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR00649; MG423; 1.
DR PROSITE; PS01292; UPF0036; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; Zinc.
FT CHAIN 1..448
FT /note="Ribonuclease J"
FT /id="PRO_0000215275"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01492"
FT BINDING 383..387
FT /ligand="substrate"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01492"
SQ SEQUENCE 448 AA; 50062 MW; FEF70CFCEF78770D CRC64;
MKLEIIAIGG YEEVGRNMTA VNVDGEIIIL DMGIRLDRVL IHEDTDISKL HSLELIEKGI
IPNDTVMKNI EGEVKAIVLS HGHLDHIGAV PKLAHRYNAP IIGTPYTIEL VKREILSEKK
FDVRNPLIVL NAGESIDLTP NITLEFIRIT HSIPDSVLPV LHTPYGSIVY GNDFKFDNFP
VVGERPDYRA IKKVGKNGVL CFISETTRIN HEGKTPPEII ASGLLKNDLL AADNDKHGII
VTTFSSHIAR IKSITDIAEK MGRTPVLLGR SMMRFCGIAQ DIGLVKFPED LRIYGDPSSI
EMALKNIVKE GKEKYLIIAT GHQGEEGAVL SRMATNKTPY KFEKYDCVVF SADPIPNPMN
AAQRYMLESR LKLLGVRIFK GAHVSGHAAK EDHRDMLRWL NPEHIIPSHG DFNLTAEYTK
LAEEEGYRLG EDVHLLRNGQ CLSFERII
