ID L1NYU9_9NEIS Unreviewed; 242 AA.
AC L1NYU9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ORFNames=HMPREF9120_00714 {ECO:0000313|EMBL:EKY08593.1};
OS Neisseria sp. oral taxon 020 str. F0370.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1127694 {ECO:0000313|EMBL:EKY08593.1, ECO:0000313|Proteomes:UP000010457};
RN [1] {ECO:0000313|EMBL:EKY08593.1, ECO:0000313|Proteomes:UP000010457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0370 {ECO:0000313|EMBL:EKY08593.1,
RC ECO:0000313|Proteomes:UP000010457};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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}.
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:EKY08593.1}.
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DR EMBL; AMER01000052; EKY08593.1; -; Genomic_DNA.
DR RefSeq; WP_009425085.1; NZ_KB291059.1.
DR AlphaFoldDB; L1NYU9; -.
DR STRING; 1127694.HMPREF9120_00714; -.
DR PATRIC; fig|1127694.3.peg.664; -.
DR HOGENOM; CLU_050858_0_0_4; -.
DR OrthoDB; 9802265at2; -.
DR Proteomes; UP000010457; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000010457};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
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:EKY08593.1};
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 13..143
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT DOMAIN 162..227
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF03725"
FT BINDING 89
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564"
FT BINDING 127..129
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564"
SQ SEQUENCE 242 AA; 25528 MW; 5D0C6F702B8D1FD3 CRC64;
MQTYARTGRA ADQLRPLRIT PHFLPHADGS ALIECGSTRV ICTASIDENV PPFLRGKGQG
WVTAEYGMLP ASTASRMRRE AAAGKQSGRT QEIQRLIGRS LRAAVNMEKL GERQILIDCD
VIQADGGTRT ASITGAYVAL ALAVRKLLSD GRIAENPLVS QIAAVSAGIV GGVPLLDLDY
PEDSGCDSDV NIVMNADGGI IEIQGTAEGA AFSFDELAEL VRLAQKGIVT LAAEQNRALA
AV
//
