ID A0A1G5F1J2_9FIRM Unreviewed; 818 AA.
AC A0A1G5F1J2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN02910370_02131 {ECO:0000313|EMBL:SCY32770.1};
OS Lachnospiraceae bacterium XPB1003.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520825 {ECO:0000313|EMBL:SCY32770.1, ECO:0000313|Proteomes:UP000199543};
RN [1] {ECO:0000313|EMBL:SCY32770.1, ECO:0000313|Proteomes:UP000199543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XPB1003 {ECO:0000313|EMBL:SCY32770.1,
RC ECO:0000313|Proteomes:UP000199543};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FMVK01000011; SCY32770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5F1J2; -.
DR STRING; 1520825.SAMN02910370_02131; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000199543; Unassembled WGS sequence.
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; 2.
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:UP000199543};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 563..643
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 659..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..800
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 92240 MW; A48F6EEDAD919084 CRC64;
MSEKKKSVYT GRLITNRKGF GFVEVEELED DIFIPHSGLH GAFHHDTVEV KIKESFGGRH
RMEGNIINIL ERGYTKVIGT YRQGRGFGYV VPDDSKIADD IHVFDSDAGK AKDGDKVVVK
ITFYGGDHKR PEGKVVEVLG SMDDPGVDIL SVIRAHDIPE TFPDDVKKQI RGIRLKVPKK
DMVGRKDLRD LMMVTIDGED SKDLDDAVSL EMDGEDYILG VHIADVSNYV KEGTALDKEA
VSRGTSVYLI DRVIPMLPEK LSNGICSLNE GEDRLAMSCI MRIDKKGNIT DYEIAESLIC
VNRRMTYTAV KKILADHDKK TIKEYKELVP MFERMEKLAA ILKAMRVKRG SIDFDLPESK
IILDKKGRPI DIVPYEHNVA TGMIEQFMLS ANETVAAHMY EQGLPFLYRV HETPDADRIG
DLIELMRGLG LNVDGDPSDI KPVWLQKMLG EVAGRPEEVL IRSLSLRSMK RARYSTECLG
HFGLAVLEYT HFTSPIRRYP DLQIHRILKD EIHGRLDHKQ IAHYVSILDG IAKRSSDREC
AATDAEREAD KIKMAEFMEY HIGEEFDGVI SGVTGWGMYV QLKNTVEGMV PVAKIAGDDY
DYSEREYALV GRYTGRRFTL GQPVSIRVVA VDLDLKSIEF ELAGADALYD DDLEKRKAKG
KYSKKKSEKR SDKKFGRKSD KKSDKKSGKR SDKKSDKKFD KKFDKKKPDK YSDEKRSDKK
SGKKSGKKNS GNKSSDKEIF SDLSFDWKNY DKKDSDKKKS GKKSNGKKNP GKISSGKKNS
GKKSATKKGS AKKNSAKKNS DKKKKERSNT GKRYGVID
//
