(data stored in ACNUC29543 zone)

SWISSPROT: A5GQ14_SYNR3

ID   A5GQ14_SYNR3            Unreviewed;       619 AA.
AC   A5GQ14;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491};
DE            Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491};
GN   Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN   OrderedLocusNames=SynRCC307_0070 {ECO:0000313|EMBL:CAK26973.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK26973.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly
CC       endonuclease activity. Involved in maturation of rRNA and in some
CC       organisms also mRNA maturation and/or decay. {ECO:0000256|HAMAP-
CC       Rule:MF_01491}.
CC   -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC       {ECO:0000256|HAMAP-Rule:MF_01491}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       RNA-metabolizing metallo-beta-lactamase-like family. Bacterial
CC       RNase J subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
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DR   EMBL; CT978603; CAK26973.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0070; -.
DR   EnsemblBacteria; CAK26973; CAK26973; SynRCC307_0070.
DR   KEGG; syr:SynRCC307_0070; -.
DR   eggNOG; ENOG4105CN5; Bacteria.
DR   eggNOG; COG0595; LUCA.
DR   HOGENOM; HOG000280201; -.
DR   KO; K12574; -.
DR   OMA; KNTCVFE; -.
DR   BioCyc; SSP316278:G1GJL-70-MONOMER; -.
DR   Proteomes; UP000001115; 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; 3.60.15.10; -; 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; IPR030854; RNase_J_bac.
DR   InterPro; IPR001587; RNase_J_CS.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF07521; RMMBL; 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; A5GQ14.
DR   SWISS-2DPAGE; A5GQ14.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01491,
KW   ECO:0000313|EMBL:CAK26973.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01491};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01491}.
FT   DOMAIN       25    222       Lactamase_B. {ECO:0000259|SMART:SM00849}.
FT   REGION      371    375       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01491, ECO:0000256|PIRSR:
FT                                PIRSR004803-2}.
SQ   SEQUENCE   619 AA;  68438 MW;  EDBF6B5C3E998D36 CRC64;
     MSSNGSKTQQ PTLRVIPLGG LHEIGKNTCV FEFGDDLVLI DAGLAFPSDG MHGVNVVMPD
     TSFLRENQKR IRGMIVTHGH EDHIGGISHH LKHFNIPIIY GPRLALSLLE GKMSEAGVAD
     RTVLQTVTPR EVVKLGQHFK IEFIRNTHSM ADSYSLAVTT PVGTVIFTGD FKFDHTPVDG
     EHFDMARLAH HGDQGVLCLF SDSTNSEVPG FCPPERSVFP CLDRRIAEAE GRVIITTFAS
     SIHRVAMVLE LAMKNGRKVS LLGRSMLNVI AKARELGYMR CPDDLFVPIK QIRDLPDRET
     LLLMTGSQGE PLAALSRISR GEHPQVQVKS TDTIIFSASP IPGNTISVVN TIDRLMMLGA
     KVVYGKGEGI HVSGHGFQED QKLMLALTKP KFMVPVHGEH RMLVQHARTA HSMGVPENNT
     LIIDNGDVVE LTADSIRKGD PVKAGIELLD NSRTGIVDAR VLKERQQLAE DGVITLLAAV
     SVDGKMVAPP RVNLRGVVTT AEPRKLSMWA EREVNWVLDN RWKQLCRNTG GKAPEVDWIG
     VQREIEVGLQ RRLRRELQIE PLIICLVQPA PAGTPPYKSK AMEEKDDRPA PRHQRNNDRG
     GDRNNDNRQR RRRSTAVAG
//

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