ID A0A0E4CU32_9BACL Unreviewed; 952 AA.
AC A0A0E4CU32;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:CQR51416.1};
GN ORFNames=PRIO_0191 {ECO:0000313|EMBL:CQR51416.1};
OS Paenibacillus riograndensis SBR5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC Paenibacillus sonchi group.
OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR51416.1, ECO:0000313|Proteomes:UP000033163};
RN [1] {ECO:0000313|Proteomes:UP000033163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (MAR-2015) 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; LN831776; CQR51416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E4CU32; -.
DR STRING; 483937.AMQ84_08390; -.
DR KEGG; pri:PRIO_0191; -.
DR PATRIC; fig|1073571.4.peg.175; -.
DR HOGENOM; CLU_002333_4_0_9; -.
DR Proteomes; UP000033163; Chromosome I.
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; 3.
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; 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; SM00357; CSP; 2.
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 632..712
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 720..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 104505 MW; 86D33E88644F4028 CRC64;
MTKLITQEQL LDFMRETAYK PLTYDELVSH FALEDSESFK AFEELLLALE QDGRMILTRN
ARYGVPERMD LVRGRVQAHA KGFAFLIPDD RDHPDIYMNA NDLKGAMNGD IVLVRITSRS
PSGGRMEGEV VRIVKRGVLQ TVGVFQSLEN YGFVLPDDKR INRDIFIPKQ SFKGAVDGEK
VVVRIVNYPE GRAAAEGEII EILGHKDDPG VDILSVIRKH QLPEAFPAEV MREAEQAPDS
ITEEEIIQQG RRDLRGLNIV TIDGADAKDL DDAVNVSRLE NGHYKLGVHI ADVGYYVREG
SELDKEAFDR GCSVYLVDRV IPMLPHRLSN GICSLNPKVD RLTMSCEMEF DEHMKVVKHD
VFTSVIRTKE RMTYSDVRKI VEDEDPELLE RYSPLIEDFR LMKELAMKLR GARMRRGAVD
FDFEESKIIV DENGKAIDIV KRERSVAEQI IEEFMLAANE TVAEHFHWLK VPFLYRIHED
PDPEKLQNFM AFAANFGYHV KGRGNSVHPR ALQDLLEQIQ GTKEQTVIST MMLRSMKQAK
YDAESTGHFG LAAEFYSHFT SPIRRYPDLV IHRVMREVIE NGGALTEKRH EYLASRMPEI
AQQSSERERV AVEAERDTEQ LKKAEFMQDK VGEEFDAMVS SVTSFGMFIE LENTVEGLIR
LSALSDDYYH FDEAHMALIG ERTSKVFRIG DEVKIRVAKV NMDDHTIDFE LVDMKPRAAG
EHRSFGGRGG KGGRAGGGFA KPFGSKAGGK GRAGGKGKPG SAAGRGKAGG AAHAGKGKSG
AAARAGEAPR AAEEASGGAP AGGRGKRGGG GPAEAARRAF AAVNRGEAGG AGTPRERDRS
GGRGRGGEAG GSAGGRGISF GFGSGKGGYG APAGEQISEL RGVDASTRFR SREDLGSGAA
ANGGGGKSRR KKNKKGGVFI SPSVTPGNVE RSDKSGNPEG SGRRKKKKKT QE
//
