ID Q2RPE7_RHORT Unreviewed; 842 AA.
AC Q2RPE7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=Rru_A3203 {ECO:0000313|EMBL:ABC23998.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC23998.1, ECO:0000313|Proteomes:UP000001929};
RN [1] {ECO:0000313|EMBL:ABC23998.1, ECO:0000313|Proteomes:UP000001929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC {ECO:0000313|Proteomes:UP000001929};
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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|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; CP000230; ABC23998.1; -; Genomic_DNA.
DR RefSeq; YP_428285.1; NC_007643.1.
DR AlphaFoldDB; Q2RPE7; -.
DR STRING; 269796.Rru_A3203; -.
DR EnsemblBacteria; ABC23998; ABC23998; Rru_A3203.
DR KEGG; rru:Rru_A3203; -.
DR PATRIC; fig|269796.9.peg.3316; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_1_5; -.
DR PhylomeDB; Q2RPE7; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; 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; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000001929};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 685..766
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 32..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 92042 MW; E665AE89757A4946 CRC64;
MPSLAPLWHD GADPGNGIRA RRVFPQDSLW LSRPNRRFPD PKDSPLTPKA PKHVPFPSRE
QVLEFIRAAN GEVDRREIAR AFHITGPERA DLRTLLKELE SEGALQRGRG RRIAPPGSLP
EVAVLIVARA DAEGDLFCKP EHWPEDEEPP RILLWPEPHH ARRPGVGAEI GVGDRILARL
TRIGDARYDA RTIRRLAAAP SRLLGVLALA RDGLRLRPTN RRDRDEYLVA PEDAGGAEPG
ELVEAELLPS RRLGLRRAKV IERLGGREGP RSISLVVVHS HDIPVDFPPE ALAEAEAAVG
VDLRGREDLR AVPLVTIDGE DARDFDDAVF AEPDDDPANP GGWRALVAIA DVAHYVRIGA
ALDKAARERG NSVYFPDRVV PMLPEALSNG WCSLRPNEDR GCLAVWMIFD AEGNKLRHRF
LRGLMRSAAR LTYTQVQAAR DGHADDLTAP LQERVIAPLY GVFQALLGAR SRRGTLELDL
PERKVVLDDG GEVARIEPRL RFDSHKLIEE LMIAANVSAA ETLEEKRRPC MYRVHDQPAP
DKLVALGEFL ESLDIPFHKG SINRSGQFNG VLKAARGTPH EHMVNEVVLR SQAQAEYSPD
NIGHFGLALR RYAHFTSPIR RYADLLVHRA LIAGLGLGDD GLRPGAEEDF VETAAHITAT
ERRAAQAERD AVNRYTVSFL AAKVGATFAG RINGVTRAGL FVTLEDTGAD GLIPIGSLPN
DYYVHDDAHH CLRGQRDGLE FHLGAPVEVL LREANPVSGG LVFGLLQGGV AGAAKGRGFS
GKTKGRDGLG KTRLKERGAA AKLKKGARGK PKAAGRDALA GEPVGSGPKK RPPTTTSRRK
TR
//
