ID A0A1U9KAJ9_9BACL Unreviewed; 760 AA.
AC A0A1U9KAJ9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=B0W44_16055 {ECO:0000313|EMBL:AQS57036.1};
OS Novibacillus thermophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Novibacillus.
OX NCBI_TaxID=1471761 {ECO:0000313|EMBL:AQS57036.1, ECO:0000313|Proteomes:UP000188603};
RN [1] {ECO:0000313|EMBL:AQS57036.1, ECO:0000313|Proteomes:UP000188603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-1 {ECO:0000313|EMBL:AQS57036.1,
RC ECO:0000313|Proteomes:UP000188603};
RX PubMed=25951858; DOI=10.1099/ijs.0.000306;
RA Yang G., Chen J., Zhou S.;
RT "Novibacillus thermophilus gen. nov., sp. nov., a Gram-staining-negative
RT and moderately thermophilic member of the family Thermoactinomycetaceae.";
RL Int. J. Syst. Evol. Microbiol. 65:2591-2597(2015).
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
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DR EMBL; CP019699; AQS57036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9KAJ9; -.
DR STRING; 1471761.B0W44_16055; -.
DR KEGG; ntr:B0W44_16055; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000188603; 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 GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
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; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 2.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW Reference proteome {ECO:0000313|Proteomes:UP000188603};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 626..706
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 719..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 87148 MW; C2B07713FE1586B5 CRC64;
MVQAEDIVAF MREKAYRPLT VKELEQVFGV EGSDGFRQLV KTLNQLEESG QIVRTRTNRY
GIPERLNLIR GKLQVHPKGF GFVLPSETDH PDIFIHPNDM KGAMDGDTVI ARINKQHTGE
KRMEGEIVRI IGRGQTKIVG TFSASHNFGF VIPDDKRLTA DVFIPPDGLN GAVDGQKVVV
EIKDYPDDRK SAAGEVVEIL GHKNDPGVDI VSIIRKYDLP EKFPEEVMEE ARQVPDEIAP
EEISGRRDLR ERTTVTIDGD DAKDLDDAVS VEPLDNGHIR LGVHIADVSY YVREGSALDR
EAYRRGCSVY LVDRVIPMLP PRLSNGICSL NPHVDRLTMS CEMEIDRQGT VVRYDIFPSV
IRSNARMTYR DVWKILEEED PEVTARYAEL VPHFQLMKQL ALTLRQKRLQ RGAIDFDFAE
AKIIVDEAGK PTDIVERPRT IAEQIIEEFM LVANETVAEH FHWLNVPFIY RIHEHPDSEK
LMSFFSFVTH FGYSVRGKAD DLHPRALQQL LETVRGEPEE TVISRVMLRS MQQARYAAKN
DGHYGLAAKH YTHFTSPIRR YPDLVVHRII REVLTDHTLS DERTAHWSET LPSIAEQSSE
RERVAVDAER ETDDLKKAEF MLDKVGEEFT GIISSVTSFG IFVELENTVE GMVHVSYMVD
DYYHFLDDQF MLVGERTGKQ YRIGDEVKIR VTNVNVDERS VDFELVDIKP RKKRKNRQAA
VIAGEEFHQN NGRKGKKRRR QKAVTPFYEK TAKKRRTRER
//
