ID A0A081BKD1_9LACO Unreviewed; 786 AA.
AC A0A081BKD1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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 ORFNames=LOSG293_340020 {ECO:0000313|EMBL:GAK48499.1};
OS Secundilactobacillus oryzae JCM 18671.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1291743 {ECO:0000313|EMBL:GAK48499.1, ECO:0000313|Proteomes:UP000028700};
RN [1] {ECO:0000313|EMBL:GAK48499.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG293 {ECO:0000313|EMBL:GAK48499.1};
RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Nakamura Y., Tohno M.;
RT "Draft Genome Sequence of Lactobacillus oryzae Strain SG293T.";
RL Genome Announc. 2:e00861-14(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}.
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:GAK48499.1}.
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DR EMBL; BBJM01000034; GAK48499.1; -; Genomic_DNA.
DR RefSeq; WP_034529161.1; NZ_BBJM01000034.1.
DR AlphaFoldDB; A0A081BKD1; -.
DR STRING; 1291743.LOSG293_340020; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000028700; 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 635..715
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 714..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 88597 MW; 8B18A8ABDE9619A9 CRC64;
MQDNNLKNQI IDLLQKNPDK SYSVEDISDA LKYHGAAAFK LIVQEMAALE RDKQSIVTDT
GRFQLNPATR VLTGIFHGND KGFGFIAYSD EEPDAYIAPD NTLSALNGDE VEMEIVRRAT
PGSDKGPEGK VLKITAHHYD HVVGEFQKTD DDNGYYGQIR LTDKKLKRFK FYVSDNGLKP
TPGEVVTADI TEYPNAQHPL AMVGIAKQVI GSVDDPGIDI LQIVYAHDIP AEFPEDVLQE
ADAIPDHVTE EELVGREDIT DQNLVTIDGE SSKDLDDAVT VWKLDNGNYH LGVHIADVSH
YVKEGSQLDQ EAFKRGTSVY LTDRVIPMLP RRLSNGICSL NEGVLRLCMS CEMEIDPEGN
VISHRIHPSV MKSKARMTYT AVNQILESHD EKTRNEYEEL VPMFETMGEL HKILYKHRKR
RGAIDFDDHE AEIIVDENGH AIDIKLRTRG LAERMIESFM LAANETVAEH YDHAKAPFIY
RVHETPDGER IKSFFEFLTA FGINVKGDPA HLSPKTMQGI LKQVAGKPEE AVVSVMMLRS
LKQARYADQS LGHFGLGAEF YTHFTSPIRR YPDTMVHRMI HYYEDNGVNK ESKKKFAGIL
DEIATQTSEN ERRAIDAERD TDAMKKAEYM ADHVGEEFEA TISSVMKFGM FIELENTVEG
LVHISRMQDD YYEYVEQYLA LVGRNTKRTY RIGQTVKVKV INVDKEQSAV DFDIVNPEET
PTSDLLPKRA SRPRGPRRDG NGGSHRPNQS RSNGQQRSGQ RGNGSGRPNN VGRSNNRNNS
NQGHRK
//
