ID A0A075KMR7_9FIRM Unreviewed; 774 AA.
AC A0A075KMR7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=UFO1_4005 {ECO:0000313|EMBL:AIF53548.1};
OS Pelosinus sp. UFO1.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF53548.1, ECO:0000313|Proteomes:UP000027983};
RN [1] {ECO:0000313|EMBL:AIF53548.1, ECO:0000313|Proteomes:UP000027983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFO1 {ECO:0000313|EMBL:AIF53548.1};
RX PubMed=25189589;
RA Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT Single-Molecule Real-Time DNA Sequencing Technology.";
RL Genome Announc. 2:e00881-14(2014).
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; CP008852; AIF53548.1; -; Genomic_DNA.
DR RefSeq; WP_038673664.1; NZ_CP008852.1.
DR AlphaFoldDB; A0A075KMR7; -.
DR STRING; 484770.UFO1_4005; -.
DR KEGG; puf:UFO1_4005; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_4_1_9; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000027983; 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; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000027983};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 628..708
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 718..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..410
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 734..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..774
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 87846 MW; 7976CC318DD5A045 CRC64;
MMILKNRILE FMKTEAYKPL TAEELAEHME LKGTELGELW KVIEELENNA DIIKTRYDKY
GVPERMNLVV GKLSASNKGY GFVIPEKVKS PDETDVFIPP DGMMSAMHHD RVVARVHCQS
GHGKSRDGEI IRIVQRANPR IVGTYEASRN FGFVTPDDLR LGQDIFVPKD GKTIVKSGTK
VVVEITKWPE KKRSAEGKII EVLGNTGDTG IEILSIIKRH NLPIDFPPEV EQAAEKAPDT
ISEDEIAGRR DLRHLPIMTI DGEDAKDLDD GVYVERLKNG NYLLGVYIAD VSHYVRENTV
LDKEARERGT SVYLVDRVLP MLPRRLSNGI CSLNAGEDRL AMSAHMEVNH QGQVVKYELF
PSVIRVKKRF SYTVVRKILV EHDEELISEN QELLSQLENM ERLCRILRDR RMRRGAIDFD
FPELKVKLDE TGKPIEIVKR VRSLAESIIE EFMLVANETV AEHMHKLKVP FVFRVHEEPD
SEKMVKLNNL LHNFGQSLAK VDEVQPSALQ KILSRISGRP EERIISTVML RSLKQARYES
QNLGHFGLAA TYYTHFTSPI RRYPDLIVHR VIRETFSTGD ISAKRKEKLT AMLPQIALHS
SERERAAAEA ERETVSLKTV EYMAQFVGEH FDGIINGVTA FGIFVELDNG VEGLVRVSSM
EDDYYQYIEE QYSLIGERSH KIYRLGDAVK VILVRVSPEE RNIDFVLEAN SAWIERAANR
RPSGARPQGQ GSRGPKKDSF SPSKKTVSTT KSKGNKPKGG VARAKPKRNK SKKK
//
