ID A0A069CW52_WEIOS Unreviewed; 783 AA.
AC A0A069CW52;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=WOSG25_100190 {ECO:0000313|EMBL:GAK31453.1};
OS Weissella oryzae (strain DSM 25784 / JCM 18191 / LMG 30913 / SG25).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; Weissella.
OX NCBI_TaxID=1329250 {ECO:0000313|EMBL:GAK31453.1, ECO:0000313|Proteomes:UP000030643};
RN [1] {ECO:0000313|Proteomes:UP000030643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25784 / JCM 18191 / LMG 30913 / SG25
RC {ECO:0000313|Proteomes:UP000030643};
RX PubMed=25013139; DOI=10.1128/genomea.00667-14;
RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Suzuki Y.,
RA Nakamura Y., Tohno M.;
RT "Draft genome sequence of Weissella oryzae SG25T, isolated from fermented
RT rice grains.";
RL Genome Announc. 2:0-0(2014).
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; DF820493; GAK31453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A069CW52; -.
DR STRING; 1329250.WOSG25_100190; -.
DR eggNOG; COG0557; Bacteria.
DR Proteomes; UP000030643; Unassembled WGS sequence.
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; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000030643};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 638..718
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 727..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 87868 MW; D18DF69BE52A852E CRC64;
MEEKMEENTL QDQLFGFLKA NSTQAFSAQN LTDGLHLADS QAFTKVVQAL AALERARKVR
VTQAGDFQYN ADSEGVIGIF KANDKGFGFV HYDEQAEDIF INPDNTLLAQ QGDEVRVKLI
TKPDSANGRG PEGRVMEIIT RHFTQLVGAF KLGSEYAGYI GSVRLTDKKL AAHQLLIKDG
GLKPNDGEVV VVSIDEYPSL AAPKRFTGVV TETIGYKDEP GVDILQVVYQ HEVPHVFPAD
VLEQAEKIPA EVQAAEREGR EDITDQPLVT IDSIESKDLD DAVVVWRLAN GNFHLGVHIA
DVSHYVVEGT PLDREAYKRG TSVYLTDRVI PMLPRNISNG IASLNPGVDR LAMSAEMEFT
PDGRLVNHRL HTSVMRSHAR MTYKAVNAIL AGDAETRDEY RELVPMFEEM ALLHEALANR
RTERGAIEFD APEAKIIVDE NGKPTDIQLR ERGLSERIIE SFMLAANEAV AMHFDQAKVP
FLYRIHESPD LDRVTKFFEF VKALGAPVYA DPNKVQSSDL QTIHNYFADR PEEQMVSTMM
LRTMKQAKYS DEPLGHFGIG AQYYTHFTSP IRRYPDLTVH RLIKWYASAG LDEQAQAKYR
DQLAQIGADT STRERRAIDT ERDTDAMKKA EFMEDRLGEE FDAVVNGVLK FGMFVSLENT
VEGLIHTSNL TDDNYYFDEG HLALIGRRSH HIYQIGQTVK VRLIRVDKEQ SALDFVLVDP
EAAPVTDIKV PEERHGRGNF ASRNRNERRH NDKDAKKNNQ GYKAGGAKSP KQSTNGGSHR
QHN
//
