ID A0A1E5TGP8_9STAP Unreviewed; 618 AA. AC A0A1E5TGP8; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 07-OCT-2020, entry version 18. DE RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803}; DE Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491}; DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803}; GN Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491}; GN ORFNames=ASS94_11730 {ECO:0000313|EMBL:OEK52317.1}; OS Staphylococcus equorum. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=246432 {ECO:0000313|EMBL:OEK52317.1, ECO:0000313|Proteomes:UP000095464}; RN [1] {ECO:0000313|Proteomes:UP000095464} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=738_7 {ECO:0000313|Proteomes:UP000095464}; RA Wolfe B.E.; RT "Genomic diversity of Staphylococcus saprophyticus strains from urinary RT tract infections, animal surfaces, and fermented foods."; RL Submitted (NOV-2015) 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR004803}; CC Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or CC Mg(2+) is physiologically important. {ECO:0000256|PIRNR:PIRNR004803}; 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 ECO:0000256|PIRNR:PIRNR004803}. 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 ECO:0000256|PIRNR:PIRNR004803}. 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:OEK52317.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LNPX01000050; OEK52317.1; -; Genomic_DNA. DR RefSeq; WP_021338648.1; NZ_UHDI01000001.1. DR EnsemblBacteria; OEK52317; OEK52317; ASS94_11730. DR Proteomes; UP000095464; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01491, KW ECO:0000256|PIRNR:PIRNR004803}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803}; 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 ECO:0000256|PIRNR:PIRNR004803}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR004803}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491, KW ECO:0000256|PIRNR:PIRNR004803}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_01491}; Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 21..215 FT /note="Lactamase_B" FT /evidence="ECO:0000259|SMART:SM00849" FT REGION 364..368 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491, FT ECO:0000256|PIRSR:PIRSR004803-2" FT REGION 562..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 575..600 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 603..618 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 618 AA; 68582 MW; 2CE060BEC237D491 CRC64; MKQIHKNEVA VYALGGLGEI GKNTYAVEYQ DEIVIIDAGI KFPDDNLLGI DYVIPDITYL EQNQDKIVGL FITHGHEDHI GGVPYLLKQI NVPIYGGPLA LGLIRNKLEE HHLLRTAKLI EIDESSVIKS KHFEVSFYLT THSIPEAYGV IVNTPEGNIV HTGDFKFDFT PVGEPANIAK MAKLGEEGVL CLLSDSTNSL VPDFTLSERE VGQNVEKIFH DCNGRIIFAT FASNIYRVQQ AVEAAIKHNR KIVTFGRSME NNIKIGMELG YIKAPPETFV EPNKINTVPK HELLILCTGS QGEPMAALSR IANGTHKQIK IIPEDTVVFS SSPIPGNTKS INRTINSLYR AGAEVIHNKV SNIHTSGHGS KGDQQLMLRL LRPKFFLPIH GEYRMLKAHG QSGVECGVEP DNVFIFDIGD VLALTHDSAR KAGRIPSGNV LVDGSGIGDI GNVVIRDRKL LSEEGLVIVV VSIDFKTNKL LSGPDIISRG FVYMRESGQL IYDAQRRIKT DVISKLNQNP EIQWHQIKSS IIETLQPYLF EKTARKPMIL PVIMKVNEDN NQSFAKKPSP KNDKPKNNNT KAPAKNPKPN NQNKKKNNNN NNPKPKPKKD ETNQSSES //