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Database: UniProt
Entry: A0A139NT88_9STRE
LinkDB: A0A139NT88_9STRE
Original site: A0A139NT88_9STRE 
ID   A0A139NT88_9STRE        Unreviewed;       553 AA.
AC   A0A139NT88;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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=STRDD13_00240 {ECO:0000313|EMBL:KXT79051.1};
OS   Streptococcus sp. DD13.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777881 {ECO:0000313|EMBL:KXT79051.1, ECO:0000313|Proteomes:UP000070387};
RN   [1] {ECO:0000313|EMBL:KXT79051.1, ECO:0000313|Proteomes:UP000070387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD13 {ECO:0000313|EMBL:KXT79051.1,
RC   ECO:0000313|Proteomes:UP000070387};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:KXT79051.1}.
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DR   EMBL; LQRH01000010; KXT79051.1; -; Genomic_DNA.
DR   RefSeq; WP_067100771.1; NZ_KQ969506.1.
DR   AlphaFoldDB; A0A139NT88; -.
DR   STRING; 1777881.STRDD13_00240; -.
DR   PATRIC; fig|1777881.3.peg.250; -.
DR   OrthoDB; 9758375at2; -.
DR   Proteomes; UP000070387; 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:SF4; RIBONUCLEASE J2; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   Pfam; PF17770; RNase_J_C; 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|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   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:UP000070387};
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          16..206
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   553 AA;  61993 MW;  AA8D856078FB371C CRC64;
     MSTIKIMALG GVRENGKNLY IAEVNDQIFV LDAGLKYPEN EQLGVDIIVP NFDYLEENKH
     RVAGVFLTHG HADAIGALPY LLEKVRVPVF GSHLTIELAK LVVKSYNATK KFNEFHVINA
     ETEIEFDETT ISFFKTTHSI PESLGIVVKT DQGNIVYTGD FKFDQAANKY YRTDFSRLAE
     IGQEGVLALL SDSANADSAV QVASMHEEAE EILQTIEDWE GRVIVAAVAS NIARIQQIID
     AAEETGRRIV LTGHDVENIV RTAIKLKKLR LASERLLVKP KDMNKYEDHE LIVLETGRMG
     EPLNGLRKMS IGRHRYVQIQ DGDLVYIVTT PTISKEAVVA RVENQIYQAG GVVKSVTDSL
     RVSGHGNARD LQLMLNLLRP KYLFPIQGEY RQLDAHAKAA LAIGFYPENI FIVKRGDVMS
     YENGDFVHAG AVPSGDVMID GNAIGDVGNI VLRDRKILSE DGIFIVAITV NRREKRIISK
     AKVHTRGFVY VKKSRDILRE ASEIVNQSVE KYFTKDSFDW GELKSTVRDD LSKYLYDQTK
     RRPSILPVIM EVK
//
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