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Database: UniProt
Entry: F2NHR4_DESAR
LinkDB: F2NHR4_DESAR
Original site: F2NHR4_DESAR 
ID   F2NHR4_DESAR            Unreviewed;       255 AA.
AC   F2NHR4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
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   OrderedLocusNames=Desac_1544 {ECO:0000313|EMBL:AEB09399.1};
OS   Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobaccia; Desulfobaccales;
OC   Desulfobaccaceae; Desulfobacca.
OX   NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB09399.1, ECO:0000313|Proteomes:UP000000483};
RN   [1] {ECO:0000313|EMBL:AEB09399.1, ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RX   PubMed=21886866;
RA   Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA   Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of the acetate-degrading sulfate reducer
RT   Desulfobacca acetoxidans type strain (ASRB2).";
RL   Stand. Genomic Sci. 4:393-401(2011).
RN   [2] {ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL   Submitted (MAR-2011) 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: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; CP002629; AEB09399.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2NHR4; -.
DR   STRING; 880072.Desac_1544; -.
DR   KEGG; dao:Desac_1544; -.
DR   eggNOG; COG0689; Bacteria.
DR   HOGENOM; CLU_050858_0_0_7; -.
DR   OMA; RYNMAPF; -.
DR   Proteomes; UP000000483; 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   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:SF0; EXOSOME COMPLEX COMPONENT RRP41; 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:AEB09399.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000483};
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:AEB09399.1};
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          21..151
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF01138"
FT   DOMAIN          168..233
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF03725"
FT   BINDING         97
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00564"
FT   BINDING         135..137
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00564"
SQ   SEQUENCE   255 AA;  28227 MW;  8EFB17ED499C9A33 CRC64;
     MVERCRNTHP MIRSEGRRLD ELRQVKITPR YLSQAEGAVL ISLGRTWVIC TATVEERVPA
     FLQDSGQGWV TAEYDMLPRA THSRHPRSAN LGKPSSRSQE IQRLIGRSLR AVVDLDALGE
     RTIVLDCDVI QADGGTRTAA ITGAFVALCE ALAGLQRQEI IATLPVLDQV AAVSVGLAND
     QILVDLDYQE DSRAEVDANF VVTGRGQLVE VQATGERGPF RPALLLEMLE RAQPALQRLR
     QAQEKALRPW MSLPW
//
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