(data stored in ACNUC7421 zone)

SWISSPROT: RNJ1_STAAS

ID   RNJ1_STAAS              Reviewed;         565 AA.
AC   Q6GAC5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=Ribonuclease J 1 {ECO:0000255|HAMAP-Rule:MF_01491};
DE            Short=RNase J1 {ECO:0000255|HAMAP-Rule:MF_01491};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491};
GN   Name=rnj1 {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=SAS1024;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
DR   EMBL; BX571857; CAG42798.1; -; Genomic_DNA.
DR   RefSeq; WP_000811375.1; NC_002953.3.
DR   SMR; Q6GAC5; -.
DR   KEGG; sas:SAS1024; -.
DR   HOGENOM; HOG000280201; -.
DR   KO; K12574; -.
DR   OMA; KNTCVFE; -.
DR   BioCyc; SAUR282459:G1G3P-1128-MONOMER; -.
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;
DR   PRODOM; Q6GAC5.
DR   SWISS-2DPAGE; Q6GAC5.
KW   Cytoplasm; Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW   RNA-binding; rRNA processing; Zinc.
FT   CHAIN           1..565
FT                   /note="Ribonuclease J 1"
FT                   /id="PRO_0000286848"
FT   REGION          364..368
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT   METAL           74
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT   METAL           76
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT   METAL           78
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT   METAL           79
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT   METAL           142
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT   METAL           164
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT   METAL           164
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT   METAL           390
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
SQ   SEQUENCE   565 AA;  62669 MW;  B1C619591C2E42B9 CRC64;
     MKQLHPNEVG VYALGGLGEI GKNTYAVEYK DEIVIIDAGI KFPDDNLLGI DYVIPDYTYL
     VQNQDKIVGL FITHGHEDHI GGVPFLLKQL NIPIYGGPLA LGLIRNKLEE HHLLRTAKLN
     EINEDSVIKS KHFTISFYLT THSIPETYGV IVDTPEGKVV HTGDFKFDFT PVGKPANIAK
     MAQLGEEGVL CLLSDSTNSL VPDFTLSERE VGQNVDKIFR NCKGRIIFAT FASNIYRVQQ
     AVEAAIKNNR KIVTFGRSME NNIKIGMELG YIKAPPETFI EPNKINTVPK HELLILCTGS
     QGEPMAALSR IANGTHKQIK IIPEDTVVFS SSPIPGNTKS INRTINSLYK AGADVIHSKI
     SNIHTSGHGS QGDQQLMLRL IKPKYFLPIH GEYRMLKAHG ETGVECGVEE DNVFIFDIGD
     VLALTHDSAR KAGRIPSGNV LVDGSGIGDI GNVVIRDRKL LSEEGLVIVV VSIDFNTNKL
     LSGPDIISRG FVYMRESGQL IYDAQRKIKT DVISKLNQNK DIQWHQIKSS IIETLQPYLF
     EKTARKPMIL PVIMKVNEQK ESNNK
//

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