ID A0A270PH99_9PSED Unreviewed; 878 AA.
AC A0A270PH99;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ECO:0000313|EMBL:PAM83744.1};
GN ORFNames=CES87_12520 {ECO:0000313|EMBL:PAM83744.1};
OS Pseudomonas sp. ERMR1:02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1805930 {ECO:0000313|EMBL:PAM83744.1, ECO:0000313|Proteomes:UP000215719};
RN [1] {ECO:0000313|EMBL:PAM83744.1, ECO:0000313|Proteomes:UP000215719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:02 {ECO:0000313|EMBL:PAM83744.1,
RC ECO:0000313|Proteomes:UP000215719};
RA Kumar R., Acharya V., Singh D., Kumar S.;
RT "Pseudomonas sp. ERMR1:02, Genome sequencing and assembly.";
RL Submitted (JUN-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:PAM83744.1}.
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DR EMBL; NKJI01000005; PAM83744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A270PH99; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000215719; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 756..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..76
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 784..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 97686 MW; 8E63B80FA7548436 CRC64;
MADWQSLDPE AAREAEKYEN PIPSRELILQ HLADRGSPAN REQLVEEFGL TTEDQIEALR
RRLRAMERDA QLIYTRRGTY APVDKLDLIL GRVSGHRDGF GFLVPDDGSD DLFMSPAQMR
LVFDGDRALA RVSGLDRRGR REGMIVEVVS RAHESIVGRY FEEGGIGFVV ADNPKIQQEV
LVTPGRNANA QVGQFVEVKI THWPTPRFQP QGDVVEVVGN YMAPGMEIDV ALRTYDIPHV
WPDAVLKEAA KLKPEVEEKD KEKRIDLRHL PFVTIDGEDA RDFDDAVYCE ARPGKLRLFS
GGWKLYVAIA DVSSYVKLGS ALDAEAQVRG NSVYFPERVI PMLPEQLSNG LCSLNPQVDR
LAMVCEMTIS KSGEMTDYCF YEAVIHSHAR LTYNKVSAML ETPKVAEARK LRGEYTDVVP
HLKQLYALYK VLLAARHVRG AIDFETQETR IIFGSERKIA EIRPTIRNDA HKLIEECMLA
ANVATAEFLK KHEIPALYRV HDGPPPERLE KLRAFLGELG LSLHKGKDGP SPKDYQALLA
GIKDRPDFHL IQTVMLRSLS QAVYSADNQG HFGLNYEAYT HFTSPIRRYP DLLTHRAIRS
VIHSKQDTPH VRRAGAMTIP KARIYPYDEA ALEQLGEQCS MSERRADEAT RDVVNWLKCE
FMKDRVGESF PGVITAVTGF GLFVELTDIY VEGLVHVTAL PGDYYHFDPV HHRLAGERTG
RSFRLGDTVE VRVMRVDLDE RKIDFEMAET TISAPIGRKK RGTETAAPAA SATKTAAEPA
PAKTGRRPVK EKAVEAYRPS DAAAKNAEVR KSREMKKALL SDAKNGGKAA SAGKTGRSAP
DKAVGGKPAK PSKHRKGPPK AGSAPAKSGG ARKPKAKP
//
