ID I4ETY8_9ACTN Unreviewed; 240 AA.
AC I4ETY8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Ribonuclease PH {ECO:0000256|HAMAP-Rule:MF_00564};
DE Short=RNase PH {ECO:0000256|HAMAP-Rule:MF_00564};
DE EC=2.7.7.56 {ECO:0000256|HAMAP-Rule:MF_00564};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564};
GN Name=rph {ECO:0000256|HAMAP-Rule:MF_00564,
GN ECO:0000313|EMBL:CCH86851.1};
GN OrderedLocusNames=MODMU_1402 {ECO:0000313|EMBL:CCH86851.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH86851.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH86851.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH86851.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_00564};
CC -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC {ECO:0000256|HAMAP-Rule:MF_00564}.
CC -!- SIMILARITY: Belongs to the RNase PH family.
CC {ECO:0000256|ARBA:ARBA00006678, ECO:0000256|HAMAP-Rule:MF_00564}.
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DR EMBL; FO203431; CCH86851.1; -; Genomic_DNA.
DR RefSeq; WP_014739455.1; NC_017955.1.
DR AlphaFoldDB; I4ETY8; -.
DR STRING; 477641.MODMU_1402; -.
DR KEGG; mmar:MODMU_1402; -.
DR PATRIC; fig|477641.3.peg.1327; -.
DR eggNOG; COG0689; Bacteria.
DR HOGENOM; CLU_050858_0_0_11; -.
DR OMA; RVICTAT; -.
DR OrthoDB; 9802265at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease 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; GHMP Kinase, N-terminal domain; 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_Su5_D2-typ_SF.
DR InterPro; IPR002381; RNase_PH_bac-type.
DR InterPro; IPR018336; RNase_PH_CS.
DR NCBIfam; TIGR01966; RNasePH; 1.
DR PANTHER; PTHR11953; EXOSOME COMPLEX COMPONENT; 1.
DR PANTHER; PTHR11953:SF2; EXOSOME COMPLEX COMPONENT MTR3; 1.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS01277; RIBONUCLEASE_PH; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564,
KW ECO:0000313|EMBL:CCH86851.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00564};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00564};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000313|EMBL:CCH86851.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00564};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00564}.
FT DOMAIN 11..141
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT DOMAIN 161..225
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF03725"
FT BINDING 87
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564"
FT BINDING 125..127
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564"
SQ SEQUENCE 240 AA; 25330 MW; A2CAFCDBE8387837 CRC64;
MTRPDGRAAD QLRPVTITRN WLDHAEGSVL VEFGRTRVLC AASVTEGVPR WRRGSGLGWV
TAEYSMLPRA THTRSDRESV KGKIGGRTHE ISRLIGRSLR ASIDLAALGE NSIALDCDVL
QADGGTRTAA ITGAYVALAD AVGWLDARGK LARPTAIAQS VAAVSVGVVD GEPRLDLAYE
EDVKAGTDMN VVCTGAGDFV EVQGTAEGAV FDRATLDQLL DLAVTGCTAL TRLQQQALSA
//
