ID A0A1H9BMC1_9FIRM Unreviewed; 722 AA.
AC A0A1H9BMC1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN02910369_00795 {ECO:0000313|EMBL:SEP89558.1};
OS Lachnospiraceae bacterium NE2001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520823 {ECO:0000313|EMBL:SEP89558.1, ECO:0000313|Proteomes:UP000199680};
RN [1] {ECO:0000313|EMBL:SEP89558.1, ECO:0000313|Proteomes:UP000199680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE2001 {ECO:0000313|EMBL:SEP89558.1,
RC ECO:0000313|Proteomes:UP000199680};
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; FOEK01000005; SEP89558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9BMC1; -.
DR STRING; 1520823.SAMN02910369_00795; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000199680; 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 Reference proteome {ECO:0000313|Proteomes:UP000199680};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 642..722
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 722 AA; 82976 MW; B6FC1B9AD4705DA8 CRC64;
MEYTDRENEI YESFQELMSK NDYRPLRFKE LCYMYEVDDE EKKEEFLGFL NKLCDDVKLI
KTKNNRYMLP PKDMLTGIYN STRRGFGFVT VEGFDEDFFV SAKDSANAFH GDKVLISTIK
GARGPRKEAR VVRVLSRNTT ELIGVYQQCD GYGFVIPNNK KIADDIYIPQ HNASNAVTGS
VVIVNLEDFG DEKKSPTGRV SEVLGHVDDP RTDILQVVRA YGIPVEFPDD VENQLNQIPD
EVAEEEKAGR RDFRDLDTIT IDGEDAKDLD DAISLSYKNG IYHLGVHIAD VSNYVREGSP
LDKEALKRGT SNYLVDSVIP MLPHKLSNGI CSLNHDVDRL TLSCVMDIDE NGKVVNHEIV
EGLINVNERM NYTDVATILT GEAIHPELVE EDPSRGYEAL MKRYDYLVPM FRLMLQLSEI
IRAAREKRGS IDFDVAETKI IVNEEGVPVD IHPYDRNCAT KIIEDFMLMA NETVAEEYFW
ADIPFEYRIH ENPLPEKVDI LRETMRSFKK YFKVSRDNIH PKEYQKLLDS IKGEPYEALL
TKMTLRSMQQ ARYSTECAGH FGLACKYYCH FTSPIRRYPD LQIHRIIKEN LHGELTGGRV
SHYAKLLPRV AEDNSMKERR AVDAERDVVK LKQIEYMSEH IGEFFEGIIS GFTNQTIFVE
LPNTVEGAVR VADMTDDYYT YYEDKFEMVG RTTGKVLKLG DPCHVRLVRC DKVDRVIDFE
FA
//
