ID A0A0R1Q6I1_9LACO Unreviewed; 803 AA.
AC A0A0R1Q6I1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=FD01_GL002336 {ECO:0000313|EMBL:KRL40176.1};
OS Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL40176.1, ECO:0000313|Proteomes:UP000051790};
RN [1] {ECO:0000313|EMBL:KRL40176.1, ECO:0000313|Proteomes:UP000051790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL40176.1,
RC ECO:0000313|Proteomes:UP000051790};
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:KRL40176.1}.
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DR EMBL; AZEU01000273; KRL40176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1Q6I1; -.
DR PATRIC; fig|1423769.4.peg.2523; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000051790; 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; 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; 3.
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:UP000051790};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 642..722
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 721..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 89844 MW; 378517D30CDB14B3 CRC64;
MTTVGHMRNE LLAAFRRNPQ IAFSTASLNR ALKLTDAEDF KVLVQALTGL ENDDLIHSTG
EALFQLGGKP AGHLEGIFHG NEKGFGFVAV EDEENDFFIA PPATKFALDG DTVEINITRK
ARPGDSRGSE AEVVKVLERK ITRLVGEYSP LSDGEKERTG FIGVVVSHEK KLKNYPIFVK
DTGMIPELGD MLMVEVTAYP DRDHPKAMQG IVSENLGNKN APGVDVLSLV LANDIHTEYP
EDAMAQANAI PDHVTDEDRI GRRDITDQPV VTIDGDDSKD FDDAVVAWKL PNGNYHLGVH
IADVSYYVTE GSPLDKETYD RGTSTYLTDR VIPMLPFRLS NGICSLNPDV DRLAMSCDME
ITPEGKVVNH DIYQSVIRSH GRLTYNNVNK MITDQDPELR AQYADLVPML DLMGDLHKIL
YKMRHDRGAI DFEEHEAKII VDENGHPTDI VLRDRGLSER MIESFMLEAN ETVAEHYNKL
HLPFLYRVHE TPDDDRIKDF IDFLATFGIT VPIKPGAKLT PKMLQEVNTS VQGTPEEMMV
NVKMLRSLKQ AHYSEDPLGH FGIAAEYYCH FTSPIRRYPD LIVHRLIRSY ATQGAGEDNQ
AKWSSKLPDI AVQTSVRERH SIDAERAVDD LKKAEFMADK VGEDFDAVVS GVAGFGMFVA
LPNTVEGLVH ISRMKDDYYA FVENQMALVG ERFHKIYRIG QPVKVHLDNV DVEQRQVDFS
LIPSDDTPKT DIVVKRETRG RGQNHSDGPR NGNRNGGNRN NSNNRGGNNN RGRNHNNNRG
GSRPFNKLGD QLRQGGQRGG NKH
//
