ID X0PBD5_9LACO Unreviewed; 775 AA.
AC X0PBD5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=FD41_GL000318 {ECO:0000313|EMBL:KRM07841.1}, JCM14108_2122
GN {ECO:0000313|EMBL:GAF37113.1};
OS Lentilactobacillus farraginis DSM 18382 = JCM 14108.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF37113.1, ECO:0000313|Proteomes:UP000019488};
RN [1] {ECO:0000313|EMBL:GAF37113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF37113.1};
RA Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis JCM
RT 14108T and L. composti JCM 14202T, Isolated from Compost of Distilled
RT Shochu Residue.";
RL Genome Announc. 2:e00257-14(2014).
RN [2] {ECO:0000313|EMBL:KRM07841.1, ECO:0000313|Proteomes:UP000051966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18382 {ECO:0000313|EMBL:KRM07841.1,
RC ECO:0000313|Proteomes:UP000051966};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAF37113.1}.
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DR EMBL; BAKI01000024; GAF37113.1; -; Genomic_DNA.
DR EMBL; AZFY01000092; KRM07841.1; -; Genomic_DNA.
DR RefSeq; WP_035180233.1; NZ_BAKI01000024.1.
DR AlphaFoldDB; X0PBD5; -.
DR STRING; 1423743.FD41_GL000318; -.
DR PATRIC; fig|1423743.5.peg.329; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000019488; Unassembled WGS sequence.
DR Proteomes; UP000051966; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 634..714
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 716..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..775
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 88209 MW; CF231CAC3B3E33F7 CRC64;
MQDNDLKKEI ENVLRTYPDN EFSVEKIADV LRYHGSAAFK LIVQELAALE RDQLVIVTAD
GKFQLNPDKQ KLSGIFHAND KGFGFVAYDE TAPDAFIAPD NTMNALNGDT VDMEIVKPAD
PGSDRGPEGK VTAITDRKYK RVVGPFSRSE NRKYFGEVKL TDKKIAKYKF YITDVGLKPT
PGEVITAQIV EYPNEAHPDY MVGIADEVIG SVDDPGIDIL QIVYAHDIPA EFPEDVLQAA
DAIPDHVTDE EKVGREDITD QDLVTIDGES SKDLDDAVTA WKLPNGHYHL GVHIADVSHY
VKPGGLIDKE AYRRGTSVYL TDRVIPMLPR RLSNGICSLN EGELRLCMSC EMEIDQAGNV
VKHRIHPSLM RSKARMTYTA VNKILESHDQ KTMDQYHELV PMFETMGELH RILYKHRHAR
GAIDFDDNEA EIIVDEKGHP IDIKLRIRGL AEKMIESFML AANETVAKHY YEAHVPFIYR
VHEQPDADRI KTFFETLTAF GINVKGDPKH ITPKMLQNVL KRVAGKPEEM MVSVMLLRSL
KQARYADQSL GHFGLAAPFY THFTSPIRRY PDTMVHRMIH YYEDNGINDE TKKKYVNVLD
EIATTTSEYE RRAVDAERDT DAMKKAEYMN DHIGEEFDGV VSSVMKFGLF IELPNTVEGL
VHISRMDDDY YQYVEQFMAL VGRRTHRTYK MGQPIRVKVI NVDVSQSAVD FDIVNPQETP
TSNYLPKESY HRHNNDRRNN NHGGGANIHF SSKQHQSNKN SKNSKSKKQF GRKRR
//
