ID A0A069I2F8_9BURK Unreviewed; 862 AA.
AC A0A069I2F8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=CF70_023935 {ECO:0000313|EMBL:KDP83687.1};
OS Cupriavidus sp. SK-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP83687.1, ECO:0000313|Proteomes:UP000023560};
RN [1] {ECO:0000313|EMBL:KDP83687.1, ECO:0000313|Proteomes:UP000023560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-3 {ECO:0000313|EMBL:KDP83687.1,
RC ECO:0000313|Proteomes:UP000023560};
RA Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT "Cupriavidus sp. strain SK-3.";
RL Submitted (MAY-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:KDP83687.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JFJV02000282; KDP83687.1; -; Genomic_DNA.
DR RefSeq; WP_035874897.1; NZ_JFJV02000282.1.
DR AlphaFoldDB; A0A069I2F8; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000023560; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 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; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 2.
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 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 663..744
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 755..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 95987 MW; 58652470306A6570 CRC64;
MNQNNYPIPS REEILGVLRT SGSPLSAGDI AKALAVTRKE HDGFQKRLAA MERDGQIELN
RKGRYELAHQ PNFVVGRVQG HRDGFGFLIR DDGDDDIFLP ERELQKAMHN DRAQVRVIGY
DRRGRPEGQI VEILERANRY VIGRLLSEGG VLVVAPEDKR ISQDILIPPK AQGKAQVGQV
VSVEIIDYPD RYVQPVGRVV EVLGDFDDPG MEIEIAVRKY GVPHAFSDAC AKEALALPDE
VREADLEHRI DLRDVPLVTI DGEDARDFDD AVYCEPVKIG RAKGWRLVVA IADVSHYVRP
GTPLDADALD RATSVYFPRR VIPMLPEKIS NGLCSLNPLV DRLCMVCDAV ITAKGELKGY
QFYPAVMHSA ARLTYNEVWS VLSNTKGPEA HKRADLVPHL QNLYELFQVL LKARRERGAI
DFDTTETYIV CNAQGKIEQI LPRTRNDAHR LIEECMLTAN VCAADFLERF KHPALYRIHA
GPSEEKLKNL REFLRSAGLS LAGGDKPQAA DYAEVMDKIK SRPDAPMLQT MLLRSMQQAV
YSPDNIGHFG LAYEAYAHFT SPIRRYPDLL VHRAIKAVLA HTKYVPAFAP GTALNTAIAP
KARRLQAKDA AAKAEQTAAR AKRNEAIWDE LGLHCSANER RADEASRDVE AWLKCYFMRD
KLGSEYSGTV SSVTSFGIFV QLDELYVEGL VHVTELGSDY FQYDEARNEL RGERTGIRYR
LTDRVRVQVS RVDLDARKID FRLVQEPSAK NLRARVPTNE AAPRVPAAHA VPARKKGRQL
AALLGGSSKP EESFDETLDR VIEEQSVFEA VMTPVKPHVG QGAKAGGKPA KRAAKPKPQH
LGSTHKAGAK PAGKSSRASR KR
//
