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Database: UniProt
Entry: A0A1E5Q0C1_9ACTN
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ID   A0A1E5Q0C1_9ACTN        Unreviewed;       561 AA.
AC   A0A1E5Q0C1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   ORFNames=BGK67_31615 {ECO:0000313|EMBL:OEJ35247.1};
OS   Streptomyces subrutilus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ35247.1, ECO:0000313|Proteomes:UP000095705};
RN   [1] {ECO:0000313|EMBL:OEJ35247.1, ECO:0000313|Proteomes:UP000095705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ35247.1,
RC   ECO:0000313|Proteomes:UP000095705};
RA   Chen X.;
RT   "The complete genome of Streptomyces subrutilus 10-1-1.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease
CC       activity. Involved in maturation of rRNA and in some organisms also
CC       mRNA maturation and/or decay. {ECO:0000256|HAMAP-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. RNA-
CC       metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEJ35247.1}.
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DR   EMBL; MEHK01000001; OEJ35247.1; -; Genomic_DNA.
DR   RefSeq; WP_069923433.1; NZ_MEHK01000001.1.
DR   AlphaFoldDB; A0A1E5Q0C1; -.
DR   STRING; 36818.BGK67_31615; -.
DR   OrthoDB; 9770211at2; -.
DR   Proteomes; UP000095705; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd07714; RNaseJ_MBL-fold; 1.
DR   Gene3D; 3.10.20.580; -; 1.
DR   Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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   NCBIfam; TIGR00649; MG423; 1.
DR   PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR   PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
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; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01491};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095705};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01491}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          31..225
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   BINDING         373..377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT                   ECO:0000256|PIRSR:PIRSR004803-2"
SQ   SEQUENCE   561 AA;  60699 MW;  E6CE3F5E55E82E16 CRC64;
     MSHPHPELQA APPLPAGGLR VTALGGLGEI GRNMTVFEHA GKLLIVDCGV LFPEEHQPGV
     DVILPDFTSI RDRLDDIVAV VLTHGHEDHI GGVPYLLRER ADIPVVGSKL TLAFLEAKLK
     EHGIKPRTAR VREGDRRRFG PFDCEFVAVN HSIPDGLAVA IRTGAGMVLH TGDFKMDQFP
     LDERITDLRA FARLGEEGVD LFLTDSTNAE VPGFTTSERE LNPAIEQVLR TAPRRVIVSS
     FASHVHRIQQ VLDAAHQHGR KVAFVGRSMV RNMGIARELG YLKVPAGLVV SMKELEQLPD
     NKITLVCTGS QGEPMAALSR MANRDHQIRI GKGDTVLLAS SLIPGNENAI YRIINGLTRW
     GANVVHKGNA KVHVSGHASA GELVYCYNIV KPRNVMPVHG EWRHLRANAD LAIRTGVDPD
     RVVIAEDGVV VDLVDGHAKI TGKVPAGYVY VDGMTVGGAT EASLKDRVTL AQEGVVTVVA
     IVDANTGMLA EAPDFLARGF EHDDTTFAAV IPVIEKTLAT AAKEGVGDAV QLEQLIARAV
     ANWAFRTHRR KPLIIPVIID A
//
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