ID A0A517N2I0_9BACT Unreviewed; 739 AA.
AC A0A517N2I0;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 02-APR-2025, entry version 20.
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 ECO:0000313|EMBL:QDT01208.1};
GN ORFNames=HG15A2_45500 {ECO:0000313|EMBL:QDT01208.1};
OS Adhaeretor mobilis.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Pirellulales;
OC Lacipirellulaceae; Adhaeretor.
OX NCBI_TaxID=1930276 {ECO:0000313|EMBL:QDT01208.1, ECO:0000313|Proteomes:UP000319852};
RN [1] {ECO:0000313|EMBL:QDT01208.1, ECO:0000313|Proteomes:UP000319852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HG15A2 {ECO:0000313|EMBL:QDT01208.1,
RC ECO:0000313|Proteomes:UP000319852};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) 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; CP036263; QDT01208.1; -; Genomic_DNA.
DR RefSeq; WP_145063240.1; NZ_CP036263.1.
DR AlphaFoldDB; A0A517N2I0; -.
DR KEGG; amob:HG15A2_45500; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000319852; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:TreeGrafter.
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; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR050180; RNR_Ribonuclease.
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; PF08206; OB_RNB; 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; 4.
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:UP000319852};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 639..720
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 96..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 83002 MW; 596A076874209351 CRC64;
MPELSDAILR HVNDERYRPV KPKTIAKKLG LEEADVSRVK KEVKRLVREK KLAYGPSHLV
CPVKADHPAA KVGEQPAKNK RPKQITGMFR RNASGYGFVR PEGTTKSEGR DSDVFIPANG
AGDAASGDTV RIKLDGKMGR KGKPEGRITE VIERANNRFV GTYFEEADQA LVQVDGGVFM
KPIYVGDPGA KGARTDDKVV MEMVRFPSNV RDGEGVIVEI LGQRGQPGVD TLSVIHEFNL
PGPFPEDVLE EAREQAVQFD ESIPKKRTDF TGETVITIDP DTARDFDDAI SLEQLDNGHW
VLGVHIADVS HFVQPKTPLD REARDRATSV YLPDRVIPML PEIISNNLAS LQPDRVRYAV
TAKIEFNAEG VRIGTDVYKA AIKSCRRFTY EEVDEYLADP KDWKSKLTPQ VHQLLGNMHT
LAMILRKRRF DKGALELHMP ELKIDLDKDG KVSGAHLQEN TESHQIIEEF MLAANIAVAE
RLADEGLIFL RRVHGAPDPR RLKALTEFVK ALGLKTDDLQ SRFALQKLLD EVKNDPRQHA
VNFATLRSMQ RAIYSPEDEG HFALASDCYC HFTSPIRRYP DLTIHRLIES LTEGRKPVQE
YQQILSLGDH CSEREQRATA AEREITKVKL LDYFEDKVGK KMDGIVTGVE SFGLFVTATD
IPAEGLVHIS SLTDDHYKFD RAGHVLTGFR SGGTFRLGDK VRIEVASVDL DKRELDFRVV
KSAKKAKQKG KDKHKKKRR
//
