ID Q135H9_RHOPS Unreviewed; 781 AA.
AC Q135H9;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
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=RPD_3034 {ECO:0000313|EMBL:ABE40260.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE40260.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE40260.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE40260.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) 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|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; CP000283; ABE40260.1; -; Genomic_DNA.
DR AlphaFoldDB; Q135H9; -.
DR STRING; 316057.RPD_3034; -.
DR KEGG; rpd:RPD_3034; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_1_5; -.
DR BioCyc; RPAL316057:RPD_RS15235-MONOMER; -.
DR Proteomes; UP000001818; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 642..723
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 728..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..781
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 85540 MW; 8FD30324949640F2 CRC64;
MSKTRDATFP DKATLVAFIR AHPGKVGTRE IAREFGLKNA DRAELKRMIR ELSDDGTIRK
SGRRKIAEPA ALPPTLLADI TARDSDGELI ATPAEWDEQD GDPPRIRIHV PRRAKPGTAA
GLGDRALLHV EPAEASDNGP AYVGRVIRVL DRGKPRILGI FRVQPQGGGR LVPVDKKQAG
RELNIAAHDA GGAQDGDLVS VELIRARGYG LSSGRVKERL GSLATEKAVS LIAIHSHDIP
QEFAPAALRE SEAAEPATLK GREDWRSLPL VTIDPPDAKD HDDAVHAEPD PDPANKGGVI
LHVAIADVAY YVRPESALDH DALRRGNSVY FPDRVVPMLP ERISNDLCSL KPGEPRGALA
VRMVMDADGR KRSHSFHRVL MRSAAKLNYA QAQAAIDGHP DDVTGPLLET ILKPLYDAYA
IVKRGRDERD PLDLDLPERK ILLKPDGTVD RVIVPERLDA HRLIEEFMIL ANVAAAEMLE
KKALPLIYRV HDEPTVEKVH NLVDFLKTLD LSFAKGGAMR PAQFNRILAM VKGHDAELLV
NEVVLRSQAQ AEYASENYGH FGLNLRRYAH FTSPIRRYAD LVVHRALIRA LDLGDGALPQ
TETVETLAEV AAQISVTERR AMKAERETVD RLIAHHLADR IGATFQGRIS GVTKAGLFVK
LSDTGADGLI PIRTLGDEYY NYDETRHALI GSRSGAMHRL GDVVDVRLVE AAPVAGALRF
ELLSESRSVV RGQRKGPHKT KGKEQATSKA AIGRSSRGKA RKAKVAKPPK RKPNKPGKGK
R
//