ID A0A1L8WC93_9ENTE Unreviewed; 763 AA.
AC A0A1L8WC93;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=RV14_GL001126 {ECO:0000313|EMBL:OJG78664.1};
OS Enterococcus ratti.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=150033 {ECO:0000313|EMBL:OJG78664.1, ECO:0000313|Proteomes:UP000182152};
RN [1] {ECO:0000313|EMBL:OJG78664.1, ECO:0000313|Proteomes:UP000182152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15687 {ECO:0000313|EMBL:OJG78664.1,
RC ECO:0000313|Proteomes:UP000182152};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG78664.1}.
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DR EMBL; JXLB01000023; OJG78664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8WC93; -.
DR STRING; 150033.RV14_GL001126; -.
DR Proteomes; UP000182152; 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 Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 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 Reference proteome {ECO:0000313|Proteomes:UP000182152};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 615..695
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 705..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..763
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 87297 MW; 6A7B338336DF4671 CRC64;
MEEIAQGLGL QKSKDFKLLV QTIAQMEREQ RVIFTKKGKV KLPLKPILIE GIFRANERGF
GFVTIDSEED DVYVPKEATG YAMDGDTVAI DIVKTADAAM DRGAEGKVVE IRKRAITQLV
GEFVAYTKEE INETDLYGVV LPKEKKLNQF KVYAAAEGIR PVDGSIVMIE LTHYPEKNYT
NSLEGIIKQV IGHKNDPGMD ILSIIVSNGI PTKFSDDVLL EADDIPDAIS EKDLVDRKDL
REQLIVTIDG EDAKDLDDAV TVKKLANGNY FLGVHIADVS YYVTQGSQLD KEAYERGTSV
YLTDRVIPMI PQRLSNGICS LNPQVPRLTM SCEMEIDANG RVVTHDIFSS VIQTTERMTY
TAVNQILEEQ DEIVMERYEQ LVPMLQEMQE LHYILETMRI RRGAVSFEDR EAKILVEPDG
RPMDIQLRDR GIGERLIESF MLVANETVAQ HFNQQHFPFI YRIHEQPKEE KMQRFFDFAS
ALGIVVRGTK GTITPKDLQK VIETVENRPE SAVINTMLLR SMQQARYSED NFGHYGLAAD
YYTHFTSPIR RYPDLIVHRL IRSYRQDASE ENQTYWEKKL PEIADHSSKM ERRAVEAERE
VDAMKKAEYM LDKVGEEFEG IISSVVKFGL FVELSNTIEG LVHINDLKQD YFHFIENHLA
LVGERTGVTF KIGQKVRVKV IKADPIERAI DFELVEAEEV LPFERPKASK KGKHSNRQQK
RQAKNRLQMN NKKNQLFNER KKGKKAANKK GKKPFYKGIK KKK
//
