ID A0A1E5XFD5_9PSED Unreviewed; 849 AA.
AC A0A1E5XFD5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AX279_03365 {ECO:0000313|EMBL:OEO27330.1};
OS Pseudomonas sp. J237.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1904754 {ECO:0000313|EMBL:OEO27330.1, ECO:0000313|Proteomes:UP000095383};
RN [1] {ECO:0000313|EMBL:OEO27330.1, ECO:0000313|Proteomes:UP000095383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J237 {ECO:0000313|EMBL:OEO27330.1,
RC ECO:0000313|Proteomes:UP000095383};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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}.
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:OEO27330.1}.
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; MKEP01000004; OEO27330.1; -; Genomic_DNA.
DR RefSeq; WP_069898274.1; NZ_MKEP01000004.1.
DR AlphaFoldDB; A0A1E5XFD5; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000095383; 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; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 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; 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 669..750
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 756..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 95123 MW; E4BF33EB86D1102F CRC64;
MADWQSLDPE AAREAEKYEN PIPSRELILS HLAERGSPAN REQLLEEFGL TTDEQVEALR
RRLRAMERDG QLIYTRRGTY APVDKLDLVL GRISGHRDGF GFLVPDDGSD DLFLSPAQMR
LVFDGDRALA RVAGLDRRGR REGAVVEVIS RGHETIVGRY YEESGIGFVI PDNPKIQQEV
LVTQGRNGGA KQGQFVQVTI THWPTQRFQP QGDVTEVVGN YMAPGMEIDV ALRTYDIPHV
WPDAVIKEAH KLKPEVEEKD KEKRVDLRHL PFVTIDGEDA RDFDDAVYCE KSGGSWRLFS
GGWKLYVAIA DVSHYVKVGS ALDAEAQVRG NSVYFPERVI PMLPEELSNG LCSLNPHVDR
LAMVCEMTIS KTGQMTDYQF YEAVIHSHAR LTYNKVSAML EQPKSTEGKQ LRSEYKEVLP
DLKQLYSLYQ VLLSARHERG AIDFETQETR IIFGSGRKIA EILPTQRNDA HKLIEECMLA
ANVATAAFMQ KHEIPALYRV HDGPPPERLE KLKAFLGELG LSLQRGKSKD GPSPKDYQAL
LETIKDRPDY HLIQTVMLRS LSQAVYSADN QGHFGLNYDA YAHFTSPIRR YPDLLIHRAI
RSVIRSRIDT PHVKRAGATS MPKARIYPYD EAMLEELGEQ CSMSERRADE ATRDVVNWLK
CEFMKDRVGE VFPGVITAVT GFGLFVELTD IFVEGLVHVT ALPGDYYHFD PVHHRLAGER
SGRNFRLGDT VEVRVMRVDL DERKIDFEMS EGAANAAVGR KRGDDGRAPR SSRGDRAKPG
NTDVQKSRDV KKALLAESKS KSGKSRSGSK AAPAKSDSKA AKPSKHRKGP PKAGAEGKSG
APRKRKAKS
//
