ID A0A1I4TH93_9PSED Unreviewed; 876 AA.
AC A0A1I4TH93;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=SAMN04487858_106113 {ECO:0000313|EMBL:SFM76158.1};
OS Pseudomonas sp. ok602.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1761898 {ECO:0000313|EMBL:SFM76158.1, ECO:0000313|Proteomes:UP000199362};
RN [1] {ECO:0000313|Proteomes:UP000199362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK602 {ECO:0000313|Proteomes:UP000199362};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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}.
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DR EMBL; FOUL01000006; SFM76158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4TH93; -.
DR STRING; 1761898.SAMN04487858_106113; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000199362; 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 667..748
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 754..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 97474 MW; 3EE8986C1CFD4E53 CRC64;
MADWQSLDPE AAREAEKYEN PIPSRELILQ HLADRGSPAA REQLVEEFGL TTEDQVEALR
RRLRAMERDA QLIYTRRGTY APVDKLDLIL GRISGHRDGF GFLVPDDGSA DLFMSPAQMR
LVFDGDRALA RVSGLDRRGR REGVIVEVVS RAHETIVGRY FEEGGIGFVV ADNPKIQQEV
LVTPGRNANA KIGQFVEVKI THWPTPRFQP QGDVVEVVGN YMAPGMEIDI ALRTYDIPHV
WPEAVLKEAA KLKPEVEDKD KEKRIDLRHL PFVTIDGEDA RDFDDAVYCE SKPGKLRLFS
GGWKLYVAIA DVSSYVKIGS ALDDESQVRG NSVYFPERVI PMLPEQLSNG LCSLNPHVDR
LAMVCEMTIS KSGEMTDYCF YEAVIHSHAR LTYNKVSAML ETPKLTEGRQ LRGEYSEVLP
HLKQLYSLYK VLLAARHVRG AIDFETQETR IIFGSERKIA EIRPTVRNDA HKLIEECMLA
ANVATAEFLK KHEIPALYRV HDGPPPERLE KLRAFLGELG LSLHKGKDGP SPKDYQALLA
GIKDRPDFHL IQTVMLRSLS QAVYSADNQG HFGLNYEAYT HFTSPIRRYP DLLTHRAIRS
VIHSKRETPH VKRAGAMAIP KARIYPYDEA ALEQLGEQCS MSERRADEAT RDVVNWLKCE
FMKDRVGESF PGVITAVTGF GLFVELTDIY VEGLVHVTAL PGDYYHFDPV HHRLAGERTG
RSFRLGDTVE VRVMRVDLDE RKIDFEMAEK TISAPIGRKK RDTQTSAPAA KTAAEPASAK
SGRRGPAKEK AVEAYRPSDA AAKNAEVRKS RELKQALLAE AKSGGKAASG GKTGRSAPET
ASGGKPAKPS KHRKGPPKAG SAPARSGGAR KPKAKS
//
