RNR_MYCPU
ID RNR_MYCPU Reviewed; 725 AA.
AC Q98QL0;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-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=MYPU_3510;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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; AL445564; CAC13524.1; -; Genomic_DNA.
DR PIR; G90555; G90555.
DR RefSeq; WP_010925155.1; NC_002771.1.
DR AlphaFoldDB; Q98QL0; -.
DR SMR; Q98QL0; -.
DR STRING; 272635.MYPU_3510; -.
DR EnsemblBacteria; CAC13524; CAC13524; CAC13524.
DR KEGG; mpu:MYPU_3510; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_3_14; -.
DR OMA; DWYEYRS; -.
DR OrthoDB; 1602988at2; -.
DR BioCyc; MPUL272635:G1GT6-351-MON; -.
DR Proteomes; UP000000528; 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; 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; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
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..725
FT /note="Ribonuclease R"
FT /id="PRO_0000166410"
FT DOMAIN 611..689
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
SQ SEQUENCE 725 AA; 83720 MW; FF734E9E7D27A5CD CRC64;
MKNLVLQNLK SNKAYSFLEI ARINKINPNF NSQLSKALFS LLDQGLIVKN NDGNFIKVNE
IKKIQGIFKQ SNRNFAFIET ADEQSYFVAK AHFNGAINSF EVEAIVYESP FEKDKKYAVV
KKILKNTHPE IIGFIKISNG IKYFNAFEES FRSYKFFVDQ NIDVEEDDVI LVVVEKIVDQ
KIYVNFVKKV STLKSNFYQI DIVLEKSKTI IDFPEDVLDE SALIEDHVIE KDYQNRKDLR
DKLIITIDGE DTKDFDDAIY VEKNKDHFLL SVHIADVAHY VKENSAIDKE ALRRATSIYL
PHMVIPMLPE KLSNGICSLN PGVDRLVMSI DIFIDFQGNT IKTELYEGII NSKHRLTYNQ
VNDFYNNKIK LDPNLEKMLN DSLELSKILE NYKKDEGYIN LEIEESKVIL DKEGKTVGIK
VIQRGLSEVL IENFMVRANE AVAWKMNKLK LPSIYRVHDN PSIESLVLFE KTLKTLGIDF
DTPKITSPKA FSDSFEKIKQ NYQIDNFVKL MVLRTMEKAI YSDKNIGHFG LASSYYSHFT
SPIRRYPDLQ LHRLIKQMVF DKSNLKEKKN HFSLILSDVS VQSSKKEVEA VSIERQINDI
KKAEYYESKI GKSLKAQIVS ILSFGMFVEF EDKVSGLIHI SNLLGEDFQV SEDGLLISSN
KTKYKLGQEI DVVVVKVDKN LGKVDVVLEK DYQEYLKKEQ AFQAFKKNKF TQDKEKQNGK
INYKK