RNJ_MYCPN
ID RNJ_MYCPN Reviewed; 569 AA.
AC P75497;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ribonuclease J {ECO:0000255|HAMAP-Rule:MF_01491};
DE Short=RNase J {ECO:0000255|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491};
GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=MPN_280;
GN ORFNames=A65_orf569, MP555;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly
CC endoonuclease activity. Involved in maturation of rRNA and in some
CC organisms also mRNA maturation and/or decay (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01491};
CC Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+)
CC or Mg(2+) is physiologically important. {ECO:0000255|HAMAP-
CC Rule:MF_01491};
CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01491}.
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DR EMBL; U00089; AAB96203.1; -; Genomic_DNA.
DR PIR; S73881; S73881.
DR RefSeq; NP_109968.1; NC_000912.1.
DR RefSeq; WP_010874637.1; NC_000912.1.
DR AlphaFoldDB; P75497; -.
DR SMR; P75497; -.
DR IntAct; P75497; 6.
DR STRING; 272634.MPN_280; -.
DR EnsemblBacteria; AAB96203; AAB96203; MPN_280.
DR GeneID; 66609071; -.
DR KEGG; mpn:MPN_280; -.
DR PATRIC; fig|272634.6.peg.300; -.
DR HOGENOM; CLU_008727_3_3_14; -.
DR OMA; KNTCVFE; -.
DR BioCyc; MPNE272634:G1GJ3-440-MON; -.
DR Proteomes; UP000000808; 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:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10710; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01491; RNase_J_bact; 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; IPR030854; RNase_J_bac.
DR InterPro; IPR041636; RNase_J_C.
DR InterPro; IPR001587; RNase_J_CS.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR PIRSF; PIRSF004803; RnjA; 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; Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; rRNA processing; Zinc.
FT CHAIN 1..569
FT /note="Ribonuclease J"
FT /id="PRO_0000215272"
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_01491"
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_01491"
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_01491"
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_01491"
FT BINDING 150
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_01491"
FT BINDING 172
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_01491"
FT BINDING 172
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_01491"
FT BINDING 373..377
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 399
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_01491"
SQ SEQUENCE 569 AA; 64086 MW; FB6A5470369B00DD CRC64;
MIKDFDPSEF VGKTPTKIFA FGGIQEVGKN MYGIEYDDEI IIIDCGIKFA SDDLLGIDGI
IPSFEYLIEN QAKVKALFIT HGHEDHIGGV PYLLKQVDVP VIYAPRIAAS LILKKVNEHK
DAKLNKVVVY DDFSNFETKH FKIDFYRVNH SIPDAFGVCV QTPNGNIVES GDFRFDFAAG
GEMLDVHKVV KIAERNVHVF MCETTNAEIP GFSQSEKLIY RNINKIIKEA RGRVILTTFA
SNITRINEII EIAVNNKRKV CLLGKSMDVN VNISRKIGLM DIDSNDIVEV RDIKNYPDRS
ILILCTGSQG EDSAALNTMA RGKHNWVSLK STDTIIMSSN PIPGNYAAVE NLLNELSKYG
VTIFENSPNM KLHASGHATQ QELQLMLNLV FPRYLIPIHG EYKMMRTIKN IAQECGINGD
DVGLLANGQV MYLIDGKLYY SGEVINADPI YIESRNSSPD LARVIKQRQI LSREGMFAVI
VVFDKNNNIL GMPTLITRGC FFALDSSPLM TKITHSIKRG LENVIQNKRF NTREQMIKEL
KRVCKETVSY FIWKNKSRNP LISTVLSWV
