RNJ_HALSA
ID RNJ_HALSA Reviewed; 448 AA.
AC Q9HQI4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=VNG_1149C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG19531.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG19531.1; ALT_INIT; Genomic_DNA.
DR PIR; G84270; G84270.
DR RefSeq; WP_010902826.1; NC_002607.1.
DR AlphaFoldDB; Q9HQI4; -.
DR SMR; Q9HQI4; -.
DR STRING; 64091.VNG_1149C; -.
DR PaxDb; Q9HQI4; -.
DR EnsemblBacteria; AAG19531; AAG19531; VNG_1149C.
DR GeneID; 5952844; -.
DR GeneID; 62886666; -.
DR KEGG; hal:VNG_1149C; -.
DR PATRIC; fig|64091.14.peg.878; -.
DR HOGENOM; CLU_008727_4_1_2; -.
DR InParanoid; Q9HQI4; -.
DR OrthoDB; 12384at2157; -.
DR PhylomeDB; Q9HQI4; -.
DR Proteomes; UP000000554; 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; IPR004613; RNase_J.
DR InterPro; IPR042173; RNase_J_2.
DR InterPro; IPR030879; RNase_J_arc.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR00649; MG423; 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_0000429575"
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 385..389
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01492"
FT BINDING 411
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; 49826 MW; 580687AF8FA63942 CRC64;
MEIEIATIGG YEEVGRQMTA VRAGDDIVIF DMGLNLSKVL VHDNVETEKM HSLDLIDMGA
IPDDRVMSDL EGDVKAIVPT HGHLDHIGAI SKLAHRYDAP IVGSPFTIEL VKGEIESEQK
FGVENDLVKM EAGGTMEIGD RCELEFVHVT HSIIDAINPV LHTPEGAVVY GLDKRMDHDP
VLEDPIDMER FREIGREGEG VLCYIEDCTN AGKKGRTPSE STARRHLKDV LTSVADYDGG
IVATTFSSHI SRVSSLVEFA KEIGREPILL GRSMERYSGT AERMGRVNFP DDLGMFGHRK
SVDRAFKRVM NEGKENFLPI VTGHQGEPQA MLTRMGRGET PYDIEDGDKI IFSASVIPEP
TNKGQRYQSE QLLRMQGARI YDDIHVSGHL REEGHYQMLD ALQPQHLIPA HQDMKGMAPY
AKLAKSQGYK IGRDLHMTEN GNTIQLVE
