ID   RNPH_BREBN              Reviewed;         253 AA.
AC   C0ZAF8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Ribonuclease PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            Short=RNase PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            EC=2.7.7.56 {ECO:0000255|HAMAP-Rule:MF_00564};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_00564};
GN   Name=rph {ECO:0000255|HAMAP-Rule:MF_00564}; OrderedLocusNames=BBR47_17900;
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599;
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorolytic 3'-5' exoribonuclease that plays an important
CC       role in tRNA 3'-end maturation. Removes nucleotide residues following
CC       the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of
CC       RNA molecules by using nucleoside diphosphates as substrates, but this
CC       may not be physiologically important. Probably plays a role in
CC       initiation of 16S rRNA degradation (leading to ribosome degradation)
CC       during starvation. {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         tRNA(n); Xref=Rhea:RHEA:10628, Rhea:RHEA-COMP:17343, Rhea:RHEA-
CC         COMP:17344, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:173114;
CC         EC=2.7.7.56; Evidence={ECO:0000255|HAMAP-Rule:MF_00564};
CC   -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC       {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00564}.
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; AP008955; BAH42767.1; -; Genomic_DNA.
DR   RefSeq; WP_012685510.1; NC_012491.1.
DR   AlphaFoldDB; C0ZAF8; -.
DR   SMR; C0ZAF8; -.
DR   STRING; 358681.BBR47_17900; -.
DR   EnsemblBacteria; BAH42767; BAH42767; BBR47_17900.
DR   KEGG; bbe:BBR47_17900; -.
DR   eggNOG; COG0689; Bacteria.
DR   HOGENOM; CLU_050858_0_0_9; -.
DR   OMA; KGKGQGW; -.
DR   OrthoDB; 1824064at2; -.
DR   Proteomes; UP000001877; Chromosome.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd11362; RNase_PH_bact; 1.
DR   Gene3D; 3.30.230.70; -; 1.
DR   HAMAP; MF_00564; RNase_PH; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR002381; RNase_PH_bac-type.
DR   InterPro; IPR018336; RNase_PH_CS.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55666; SSF55666; 1.
DR   TIGRFAMs; TIGR01966; RNasePH; 1.
DR   PROSITE; PS01277; RIBONUCLEASE_PH; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..253
FT                   /note="Ribonuclease PH"
FT                   /id="PRO_1000194468"
FT   BINDING         86
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
FT   BINDING         124..126
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
SQ   SEQUENCE   253 AA;  27383 MW;  9C111065C5D18338 CRC64;
     MRVDGRAHDQ LRPVTITRNY IKHAEGSCLI EVGDTKVICT ATLEERVPPF MRGGGKGWIT
     AEYSMLPRAT ATRNARESSK GKVGGRTMEI QRLIGRALRS VVNLEAMGER TIWLDCDVIQ
     ADGGTRTASI TGAFVAMVDA MQKLVDSGTW KQLPLNDFLA ATSVGVVGEE AVLDLNYKED
     STAIVDMNVV MTGKGKFVEL QGTGEDAPFS PEQLQEMISL AKVGIDNLIH SQKEALADVT
     LSFAQSVAEE SHA