ID S6GY96_9PSED Unreviewed; 884 AA.
AC S6GY96;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=CFII64_25349 {ECO:0000313|EMBL:EPJ77476.1};
OS Pseudomonas sp. CFII64.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=911242 {ECO:0000313|EMBL:EPJ77476.1, ECO:0000313|Proteomes:UP000014850};
RN [1] {ECO:0000313|EMBL:EPJ77476.1, ECO:0000313|Proteomes:UP000014850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFII64 {ECO:0000313|EMBL:EPJ77476.1,
RC ECO:0000313|Proteomes:UP000014850};
RA Feris K.P., Lalor S.J.;
RL Submitted (NOV-2010) 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:EPJ77476.1}.
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DR EMBL; ATLO01000049; EPJ77476.1; -; Genomic_DNA.
DR RefSeq; WP_020293661.1; NZ_ATLO01000049.1.
DR AlphaFoldDB; S6GY96; -.
DR PATRIC; fig|911242.4.peg.5050; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000014850; 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; 2.
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 667..748
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 754..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 98466 MW; A2788AEB73F0D9EF CRC64;
MADWQSLDPE AAREAEKYEN PIPSRELILK HLSDRGSPAS REQLVEEFGL TTEDQFEALR
RRLRAMERDA QLIYTRRGTY APVDKLDLIL GRISGHRDGF GFLIPDDGTD DLFMSPAQMR
LVFDGDRALA RVSGLDRRGR REGVIVEVIS RAHETVVGRY FEESGIGFVI PDNPKIQQEV
LVTPGRNNNA QIGQFVEVKI THWPTPRFQP QGDIVEVVGN YMAPGMEIDV ALRTYDIPHV
WPEAVLKEAA KLKPEVEEKD KENRVDLRHL PFVTIDGEDA RDFDDAVFCE AKPGKLRLFS
GGWKLYVAIA DVSSYVKIGS ALDAESQVRG NSVYFPERVV PMLPEQLSNG LCSLNPHVDR
LAMVCEMTIS KTGEMTDYVF YEAVIHSHAR LTYNKVSSML EQPKTTEARQ LRGEYPDVLP
HLKQLYALYK VLLAARHVRG AIDFETQETR IIFGTERKIA EIRPTTRNDA HKLIEECMLA
ANVATAEFLK KHEIPALYRV HDGPPPERLE KLRAFLGELG LSLHKGKDGP SPKDYQALLE
TVRGRPDYHL IQTVMLRSLS QAVYSSDNHG HFGLNYEAYT HFTSPIRRYP DLLTHRAIRS
VIRSKQDTPH VRRAGAMTIP KARIYPYDEA ALEQLGEQCS MSERRADEAT RDVVNWLKCE
FMKDRVGESF PGVITAVTGF GLFVELTDIY VEGLVHVTAL PGDYYHFDPV HHRLAGERTG
RSFRLGDTVE VRVMRVDLDE RKIDFEMAEK TIAAPIGRKR RGGHETTPAP VEKQSAAPSK
APSKRPAKAK AKAEPEAYRP SDAAAKNAEV RKSRELKQAL LAEAKGGSKA PSGKSSNSGS
ASSGSAPGGS GKPAKSGKHR KGPPKAGSAP AAKSGGVRKP KAKS
//
