ID V9X3U0_9PSED Unreviewed; 858 AA.
AC V9X3U0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=C163_23805 {ECO:0000313|EMBL:AHD16660.1};
OS Pseudomonas sp. FGI182.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1259844 {ECO:0000313|EMBL:AHD16660.1, ECO:0000313|Proteomes:UP000018783};
RN [1] {ECO:0000313|EMBL:AHD16660.1, ECO:0000313|Proteomes:UP000018783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI182 {ECO:0000313|EMBL:AHD16660.1,
RC ECO:0000313|Proteomes:UP000018783};
RG DOE Joint Genome Institute;
RA Currie C., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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 ---------------------------------------------------------------------------
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; CP007012; AHD16660.1; -; Genomic_DNA.
DR RefSeq; WP_025340822.1; NZ_CP007012.1.
DR AlphaFoldDB; V9X3U0; -.
DR PATRIC; fig|1259844.3.peg.4685; -.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000018783; Chromosome.
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..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..858
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 96561 MW; 547680585BE2CF06 CRC64;
MADWQSLDPE AAREAEKYDN PIPSRELILQ RLADRGEPAA REELAAEFGL YDEDQIEALR
RRLRAMERDG QLIYTRRGTY APVDKLDLIC GRVSGHRDGF GFLIPDDGSE DLFLSPSQMR
LVFDGDRGLA RVSGVDRRGR REGVLVEIIS RAHESVVGRY FEEGGIGYVT PDNPKIQQEV
LVTAGRNGGA KIGQFVEIKI THWPTPRFQP QGDVVEVIGN YMAPGMEIDV ALRSYDIPHV
WPKDVIKEAR KFRSEVEEKD KEKRVDLRHL PFVTIDGEDA RDFDDAVYCE PLGKLRLFSG
GWRLYVAIAD VSSYVRLGSA LDVEAQQRGN SVYFPERVVP MLPEELSNGL CSLNPHVDRL
AMVCEMTMNK AGQMVDYQFY EGVIHSHARL TYNKVSSMLE HSRTREGKAL REEYKAVVPD
LKNLYNLYKV LVEARHTRGA IDFETQETRI IFGDERKIAE IRPTVRNDAH KLIEECMLAA
NVATAEFLQK HGVPALYRVH DGPPPERLEK LRAFLGELGL TLHKGKDPSP KDYQALLASI
AGRPDFHLIQ TVMLRSLSQA VYSTDNNGHF GLNYEAYTHF TSPIRRYPDL LVHRAIRSII
RSRVETPHVK RAGAMSIPKA RIYPYDENTL EQLGEQCSMT ERRADEATRD VVNWLKCEFM
KDRVGETFPG VITAVTGFGL FVELTDIYVE GLVHVSALPG DYYHFDPVHH RLSGERTGRS
FRLGDTIEVK VMRVDLDERK IDFEVSEKTL AAPIGRKQRG AAPAAGQAEQ APVEAKATPK
PRSRKSETAE AYFPKDAVQR NAEVRKSREM KKALMSEARS GGHASSKSDK GGKASGKPTK
HRKGPSKSGA PRKSKSKS
//
