ID A0A1H9F9K5_9FIRM Unreviewed; 890 AA.
AC A0A1H9F9K5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN02910382_02717 {ECO:0000313|EMBL:SEQ34577.1};
OS Butyrivibrio sp. TB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520809 {ECO:0000313|EMBL:SEQ34577.1, ECO:0000313|Proteomes:UP000198682};
RN [1] {ECO:0000313|EMBL:SEQ34577.1, ECO:0000313|Proteomes:UP000198682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TB {ECO:0000313|EMBL:SEQ34577.1,
RC ECO:0000313|Proteomes:UP000198682};
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; FOER01000020; SEQ34577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9F9K5; -.
DR Proteomes; UP000198682; 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; 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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 638..718
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 748..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..890
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 101546 MW; CF5D128C1815D2F4 CRC64;
MAKRKKKNEQ ETFMIAQDRK AMVNAFIHDD RYSPMKEKEL AVFLQVEKED RNELAQILED
LIKEGQIIRN SRGRYLKSDA GIIGVFTSNS RGFGFVTVEG RDEDIYIPEG DTGNAFLGDT
VAVELKPSQA GRREEGRIIR IVMRGMTEVV GTYESSKTFG FVRADNNKIP NDIFVPKERS
KGAVSGDKVV VEITDYGDSV SGKNPEGKVK EIIGNINDPG VDILAIVKGY EIPSEFPERV
MNQAMRTADE VSEADMLGRR DLRDVQMVTI DGEESKDLDD AVSVSVDEEG FYHLGVHIAD
VANYVQEGSA LDREALKRGT SVYLVDRVIP MLPHKLSNGI CSLNHGEDRL AMSCLMKINS
KGEIVDHEIV ESVINVDERM TYTSVGKIIV DNDEEEKEKY AALVPMFEQM YELAKILKKR
RSDRGAIEFD SVEAKIKLDS EGNPVSIEKE ERGPANELIE DFMLAANETV AQHFYWMSVP
FVYRTHEQPS EAKIDTLTNF IRGFGYHLNI RQDEIRPMEI QKLLTKIEGS REESIISRVA
LRSMMQAKYT TECVGHFGLA LQYYCHFTSP IRRYPDLQIH RIIKDSIRGR LDEKKLAHYA
EILPDVAKHC SDTERRADDA ERDTDKLKKA QYMEQHIGEV YEGVVSGVTA WGMFVELDNT
CEGMIRLAEL TDDYYVFDEQ NFTLTGTDFG KEYRLGQKVK IKVVGADRLE KTVDFRIVDE
DTDPDDIELK PAKKHYVLKL MEEEAARKSE QDALKDKEHS KAEASKDGSN IKSTRKKKKR
NLDEISDEFE EIEDHYRSRK HTDLDDIDLE DGEDDNLMTA LELREHLRKK RMIEGLEPDG
RTGSPREKKR KGVKNKENGP KEKGHKKYKV HKYKKSATSK AARSNQKKKR
//
