ID A0A1Y4U8H3_9BACT Unreviewed; 760 AA.
AC A0A1Y4U8H3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=B5E60_07635 {ECO:0000313|EMBL:OUQ53254.1};
OS Alistipes sp. An116.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1965546 {ECO:0000313|EMBL:OUQ53254.1, ECO:0000313|Proteomes:UP000195395};
RN [1] {ECO:0000313|Proteomes:UP000195395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An116 {ECO:0000313|Proteomes:UP000195395};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUQ53254.1}.
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DR EMBL; NFLR01000009; OUQ53254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4U8H3; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000195395; 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; 2.
DR HAMAP; MF_01895; RNase_R; 1.
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 SMART; SM00955; RNB; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 637..718
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 720..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 86812 MW; 9230241C7131B0D7 CRC64;
MNKRQQRTPK EGAKNKRSAR EEIILHMFRD FPNTQFTLKY LASVSGGASK EGRRETFEIL
SRLFDEGIVE ECSREKYRLS QQHRPLYEGV ASMTQSGAVY VEVEGQEEDI FVNPRNTANA
LDGDRVEVAV IHRGRNGKFE GEVTRILERC HKPYVGVAEV GAHQIFVRAD SRRMPMDIYL
SKRAYPDVRD GEKVVVRIVD WQPGSKSPVG ELVERLGIAG NNDTEMHAIL AEYELPYRFE
PEIEEAAKAI DGSITAREIA SRRDFRQVVT FTVDPADAKD FDDALSVRKV RDGVWEIGVH
IADVTHYVKP HSVLDDEAVE RGTSVYLVDR TVPMLPERLS NELCSLRPNE TSLCFSAVFT
MNENLEILDE WFGRTVIHSD RRFTYAEAQE VIETGRGDYA EEILTLNRLA QAMRAQRFKN
GAIAFEREEV KFKLDESGKP LGVYFKEQKE SNQMIEEFML LANRRVAEFC AHRRNDKGRA
VPRTMVFRVH DSPSEEKLDR FRQFILRFGH IFKASKGRAV AREMNKLLKQ VKGSTEENAV
TTMAVRSMAK AYYSTDNIGH YGLAFPYYTH FTSPIRRYPD MMVHRLLAHY LEGGKSVPKD
PVEELCVRAS EREVIAAEAE RASIKYKMVE FMKEHIGEEF DGHVSGLTEW GIYVELDETH
IEGMSFLRDI PGDFFLFDEQ QYEVIGRSTG IKLTLGSPVR IRVKRADLQK RQLDFELLLP
GLPNRRSGSS DDRSRGKGKG KASDKGSGPK VSHSSRRRGR
//
