RNR_HELPJ
ID RNR_HELPJ Reviewed; 644 AA.
AC Q9ZJX9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Ribonuclease R {ECO:0000255|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000255|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895};
DE AltName: Full=VacB protein homolog;
GN Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; Synonyms=vacB;
GN OrderedLocusNames=jhp_1169;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000255|HAMAP-Rule:MF_01895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01895}.
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DR EMBL; AE001439; AAD06743.1; -; Genomic_DNA.
DR PIR; H71840; H71840.
DR RefSeq; WP_001161370.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZJX9; -.
DR SMR; Q9ZJX9; -.
DR STRING; 85963.jhp_1169; -.
DR EnsemblBacteria; AAD06743; AAD06743; jhp_1169.
DR KEGG; hpj:jhp_1169; -.
DR PATRIC; fig|85963.30.peg.1403; -.
DR eggNOG; COG0557; Bacteria.
DR OMA; YRTHKEP; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR011805; RNase_R.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; RNA-binding.
FT CHAIN 1..644
FT /note="Ribonuclease R"
FT /id="PRO_0000166405"
FT DOMAIN 573..644
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
SQ SEQUENCE 644 AA; 74160 MW; 72A66008C20425F9 CRC64;
MQGFLRSLFF GVKKIPKRFA PLVEKGVLKE ALQSNKDRYL LKEGFDIGKI ERVKNKAFFI
SLAKNYPKDP LIKNLPPSFK TDALILCQIE CSKKRPIAFF KAALLNADHA MIAYLAKEKN
QIVAIPFKEP FKKPISLKHS QRSLLELPRH CVVKIDLKKR EISEILGALE DPLIDENLSL
SLFDRIKDFS KDCLDLAQYY AQLKASDFKD RINYSHIPFI TIDPKDAKDF DDAIFYDKEK
NTLFVAVADV SEFVPKHSSL DKEARIRGFS VYFPNSVYPM LPLSLSQGAC SLKAFEKRLA
LVYEIPLDNL KNARLSQGVI EVRANCAYEE INHFLNTQQS SLGKDLQQSL LGFLEVALKL
KKERLKKGFN FNSFENKLYL NEEGRIEKIE TEKESGAHTL IEEAMLLANQ SSARLLDGHF
HNRGIYRTHK EPSLEQQKRL YDKLFDYEIV RPKNMGFFPF LEHALKISQE KSIEREVSRL
IIKSQNLALY SPMQESHFGL GFASYTHFTS PIRRYSDLAL HRLLKELLFH QAKGCSYLLE
ETPELCAELN ALQKKAALIE RDFIKRKFAR LALEFLEKEF LGVVLEAKDW VVVGLKEFIG
LKVLIKTNKV FKPLEKVRIK ITHADLILGQ VRGEITERIK EHVS
