ID B1JAH3_PSEPW Unreviewed; 859 AA.
AC B1JAH3;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
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 OrderedLocusNames=PputW619_4670 {ECO:0000313|EMBL:ACA75150.1};
OS Pseudomonas putida (strain W619).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA75150.1};
RN [1] {ECO:0000313|EMBL:ACA75150.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W619 {ECO:0000313|EMBL:ACA75150.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Psuedomonas putida W619.";
RL Submitted (FEB-2008) 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; CP000949; ACA75150.1; -; Genomic_DNA.
DR AlphaFoldDB; B1JAH3; -.
DR STRING; 390235.PputW619_4670; -.
DR KEGG; ppw:PputW619_4670; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
DR OrthoDB; 9764149at2; -.
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 665..746
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 754..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..859
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 96655 MW; B7E7A0F834583B0D CRC64;
MADWQSLDPE AAREAEKYDN PIPSRELILQ RLADRGEPAA REELAAEFGL YEEDQIEALR
RRLRAMERDG QLIYTRRGTY APVDKLDLIC GRISGHRDGF GFLIPDDGSD DLFLSPSQMR
LVFDGDRALA RVSGLDRRGR REGVLVEVIS RGHESVVGRY FEEGGIGYVT PDNPKIQQEV
LVTAGRNGGA KIGQFVEIKI THWPTPRFQP QGDVVEVIGN YMAPGMEIDV ALRSYDIPHV
WPQDVIKEAR KFRSDVEEKD KEKRIDLRHL PFVTIDGEDA RDFDDAVYCE PLGKLRLFSG
GWRLYVAIAD VSSYVRLGSA LDVEAQQRGN SVYFPERVVP MLPEELSNGL CSLNPHVDRL
AMVCEMTMNK AGQMVDYQFY EGVIHSHARL TYNKVSSMLE HARTREGKAL REEYKEVLPD
LKNLYNLYKV LLDARHARGA IDFETQETRI IFGEERKIAE IRPTVRNDAH KLIEECMLAA
NVATAEFLNK HGVPALYRVH DGPPPERLEK LRAFLGELGL SLHKGKDPSP KDYQALLASI
AGRPDFHLIQ TVMLRSLSQA VYSTDNNGHF GLNYEAYTHF TSPIRRYPDL LVHRAIRSII
RSKVDTPHVK RAGAMSIPKA RIYPYDVNTL DQLGEQCSMT ERRADEATRD VVNWLKCEFM
KDRVGETFPG VITAVTGFGL FVELTDIYVE GLVHVSALPG DYYHFDPVHH RLAGERTGRS
FRLGDTIEVK VMRVDLDERK IDFEVSEQQL AAPIGRKGRG AAPAAEKAEQ QPAVEAKATP
KPRSRKSETA EAYFPKDAVQ RNAEVRKSRE MKKALMTDAR TGGNAGSKSD KGGKPSGKPT
KHRKGPSKSG APRKSKNKS
//
