ID A0A179EUK6_ENTTH Unreviewed; 452 AA.
AC A0A179EUK6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|HAMAP-Rule:MF_01405};
DE Includes:
DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405};
DE Includes:
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=rphA {ECO:0000313|EMBL:GEK36067.1};
GN Synonyms=rph {ECO:0000256|HAMAP-Rule:MF_00564};
GN ORFNames=A6E74_03930 {ECO:0000313|EMBL:OAQ56569.1}, CK496_07345
GN {ECO:0000313|EMBL:ASZ07731.1}, ETH01_03540
GN {ECO:0000313|EMBL:GEK36067.1};
OS Enterococcus thailandicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=417368 {ECO:0000313|EMBL:OAQ56569.1, ECO:0000313|Proteomes:UP000078516};
RN [1] {ECO:0000313|EMBL:OAQ56569.1, ECO:0000313|Proteomes:UP000078516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0711D 46 {ECO:0000313|EMBL:OAQ56569.1,
RC ECO:0000313|Proteomes:UP000078516};
RA Beukers A.G., Zaheer R., Goji N., Cook S.R., Amoako K., Chaves A.V.,
RA Ward M.P., Mcallister T.A.;
RT "Draft genome of an Enterococcus thailandicus strain isolated from bovine
RT feces.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ASZ07731.1, ECO:0000313|Proteomes:UP000217197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a523 {ECO:0000313|Proteomes:UP000217197}, and A523
RC {ECO:0000313|EMBL:ASZ07731.1};
RA Ybazeta G., Douglas L., Graham J., Fraleigh N., Murad Y., Perez J.,
RA Diaz-Mitoma F., Nokhbeh R.;
RT "Whole genome sequencing and hybrid de novo assembly of Enterococcus
RT thailandicus a523.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEK36067.1, ECO:0000313|Proteomes:UP000321361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101867 {ECO:0000313|EMBL:GEK36067.1,
RC ECO:0000313|Proteomes:UP000321361};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Enterococcus thailandicus NBRC 101867.";
RL Submitted (JUL-2019) 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 -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside
CC triphosphates to their monophosphate derivatives, with a high
CC preference for the non-canonical purine nucleotides XTP (xanthosine
CC triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to
CC function as a house-cleaning enzyme that removes non-canonical purine
CC nucleotides from the nucleotide pool, thus preventing their
CC incorporation into DNA/RNA and avoiding chromosomal lesions.
CC {ECO:0000256|HAMAP-Rule:MF_01405}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.66;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.66;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.66;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405}.
CC -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC {ECO:0000256|HAMAP-Rule:MF_00564}.
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family.
CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_01405,
CC ECO:0000256|RuleBase:RU003781}.
CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000256|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; CP023074; ASZ07731.1; -; Genomic_DNA.
DR EMBL; BJUG01000002; GEK36067.1; -; Genomic_DNA.
DR EMBL; LWMN01000010; OAQ56569.1; -; Genomic_DNA.
DR RefSeq; WP_067482370.1; NZ_LWMN01000010.1.
DR AlphaFoldDB; A0A179EUK6; -.
DR GeneID; 77487452; -.
DR KEGG; eth:CK496_07345; -.
DR PATRIC; fig|417368.6.peg.394; -.
DR OrthoDB; 9807456at2; -.
DR Proteomes; UP000078516; Unassembled WGS sequence.
DR Proteomes; UP000217197; Chromosome.
DR Proteomes; UP000321361; Unassembled WGS sequence.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; 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; cd00515; HAM1; 1.
DR CDD; cd11362; RNase_PH_bact; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1.
DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR HAMAP; MF_00564; RNase_PH; 1.
DR InterPro; IPR020922; dITP/XTP_pyrophosphatase.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR002637; RdgB/HAM1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR002381; RNase_PH_bac-type.
DR InterPro; IPR018336; RNase_PH_CS.
DR NCBIfam; TIGR00042; RdgB/HAM1 family non-canonical purine NTP pyrophosphatase; 1.
DR NCBIfam; TIGR01966; RNasePH; 1.
DR PANTHER; PTHR11067:SF9; INOSINE TRIPHOSPHATE PYROPHOSPHATASE; 1.
DR PANTHER; PTHR11067; INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN; 1.
DR Pfam; PF01725; Ham1p_like; 1.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF52972; ITPase-like; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01405};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01405}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01405}; Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564};
KW Reference proteome {ECO:0000313|Proteomes:UP000078516};
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:GEK36067.1};
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 10..140
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT DOMAIN 160..224
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF03725"
FT REGION 416..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 86
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564"
FT BINDING 124..126
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564"
FT BINDING 259..264
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 404..407
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 432..433
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
SQ SEQUENCE 452 AA; 49446 MW; 1EA4B94AA6A6338D CRC64;
MRHDGRKAQE LRKIDIRTNV FKHPEGSVVI SFGDTEVICS ATIEASVPPF LRGTGTGWVT
AEYSMLPRAT NTRNRRESSK GKLTGRTMEI QRLIGRSLRA VVDLEKLGER SIIVDCDVVQ
ADGGTRTASI TGAFVALTLA VEKLVREKEV TEDPLKEHLA AISVGILPDG QCVADLDYEE
DSAALVDMNL VMTESGKFVE IQGTGEEATF DGEQLNDMLF YGKSAIEQLI AEQKHALLTE
LSTEASQAPE VAKTIVIATK NPGKAEEFRQ MFGKEGYAVK TLFDYPEIPD VEETGKTFEE
NARLKAETIA QILKQPVLAD DSGLKVDALG GMPGVYSARF AGEPKSDAGN NAKLLHELTD
VPNEQRTAQF HCTLVFAAPD KDSLVVEAEW PGKIARIPEG ENGFGYDPLF IPDGSTQTAA
EMSSEEKNQV SHRGQAMKKL SQKWQQWLEG AK
//
