RNR_UREPA
ID RNR_UREPA Reviewed; 721 AA.
AC Q9PR88;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=UU057;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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; AF222894; AAF30462.1; -; Genomic_DNA.
DR RefSeq; WP_006688547.1; NC_002162.1.
DR AlphaFoldDB; Q9PR88; -.
DR SMR; Q9PR88; -.
DR STRING; 273119.UU057; -.
DR EnsemblBacteria; AAF30462; AAF30462; UU057.
DR GeneID; 29672268; -.
DR KEGG; uur:UU057; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_3_14; -.
DR OMA; DWYEYRS; -.
DR Proteomes; UP000000423; 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 Gene3D; 2.40.50.140; -; 2.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR TIGRFAMs; TIGR02063; RNase_R; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding.
FT CHAIN 1..721
FT /note="Ribonuclease R"
FT /id="PRO_0000166414"
FT DOMAIN 639..719
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
SQ SEQUENCE 721 AA; 83174 MW; 67EEFA9A4E4FD4AA CRC64;
MSDFTKQTIT EVISKEERPI PAAILAKKVL EKIPTLNKTD VYKLIDLLIQ ENTIKKLENN
RLVIGYLDYE FDHEIKQGII TINSKGDGFI KEDNTEIEYY VNKKYLNGAL KKDSVKFVKL
KKEPKNNLQD AAVIEIVGHA KDHYVGQFIT LPNGGYYIFV DDPLFYLNIN LKDTTGLVNG
HKILFKIISQ TTKDAIAELV HIIGHKNDVG SDVLSIVYDN GIDPTFDPQV VDLASKLEFY
VDEHQNKIRR SIIDREIISI DPVGSKDIDD AVYVKKLNDQ RYFLGISIAD VSFYVQPNTI
LDADAFKRGT STYLVDRVIP MLPHNISNNI CSLNEGEFRM CITCDMVIDK DGKICWKDVY
PAIMKNYRQM SYDEVNDFYE GKSRFESATL TMKEMLLEAK ELHHILRNKK IKDGYVDFDI
KEPKIILDET GVPIDIKIYE RKTAQMMVED FMIAANEAVT MFAEEHMDKT LKEFNLEMPF
IYRVHDKPSI INLQKFEIEA KKLSFNISHD FENIQPNTIS NWLKMNDNHV NLPLISKLLL
RSMAKASYEI INTGHFGLAS DNYTHFTSPI RRYPDLIVHR LLWMFIFDSQ SYTDKQRVEL
VNKLKLITEE SNKNEIIAVK TERDVNAAKF AEYMNLHIGK EFIGVVTTVS SFGVFVELEN
TIEGLIRIKN LKDDFYDFIP ENMTLVGQKR KKIITVGNKV RVRVIEANKL TRKIDFELVA
Q