ID A0A075LN58_9BACI Unreviewed; 763 AA.
AC A0A075LN58;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=GZ22_16935 {ECO:0000313|EMBL:AIF68150.1};
OS Terribacillus goriensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Terribacillus.
OX NCBI_TaxID=386490 {ECO:0000313|EMBL:AIF68150.1, ECO:0000313|Proteomes:UP000027980};
RN [1] {ECO:0000313|EMBL:AIF68150.1, ECO:0000313|Proteomes:UP000027980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP602 {ECO:0000313|EMBL:AIF68150.1,
RC ECO:0000313|Proteomes:UP000027980};
RA Wang Y., Lu P., Zhang L.;
RT "Complete genome sequence of a moderately halophilic bacterium
RT Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in
RT Tianmu mountain in China.";
RL Submitted (JUL-2014) 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|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; CP008876; AIF68150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075LN58; -.
DR KEGG; tap:GZ22_16935; -.
DR HOGENOM; CLU_002333_4_1_9; -.
DR Proteomes; UP000027980; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000027980};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 628..708
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 713..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..763
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 87224 MW; 9952CFCB353374BC CRC64;
MMEEIKQKIL AYFKENAAKP LTVEEIEEQL TLDEASEFTV LVKGLNELET EGQLVRTRSN
RFGLPEKLNL VRGKIQMHAK GFAFLIPDEE GVADVYIHYS DLQSAMNNDI VLVRIENQAE
GGQRREGQVV RILERAIAEV VGTYEDNGRF GFLIADDKRI PNDIFIPRGA SGGATDGHKV
IARITKYPEG RMSAEGEVIR ILGHKNDPGI DILSIIYKHG ISTEFPPEVL EQAANTPDTI
DPAEIENRRD IRDMMTVTID GADAKDLDDA VSVSRLENGN YRLVVSIADV SYYVEEGSPI
DEEALERATS VYLVDRVIPM IPHRLSNGIC SLNPQVDRLT LTCDMQITPQ GEVVEHEIYQ
SVIKTNERMT YGDVNRILLE DDQELKDRYS DLVPMFQQME DLAAALRKKR MDRGAIDFDF
PEARVAVDEE GKAIDVILRE RSVAEKLIEE FMLAANETVA EHFHWMDVPA IHRIHTDPDP
DKLQNFFEFI TSLGYTVRGS SSDIHPQTLQ KIVERVRGTQ EEMIINRLML RSMQQAKYDP
QGLGHFGLAT KFYTHFTSPI RRYPDLIVHR LIRTYIVNNQ LDKKTQDHWK ERMPEIARQS
SERERAAVDA ERETDDLKKA EFMQDKVGEE FDGVISSVTG FGLFVELPNT IEGLVHVSYL
TDDFYHFDDK RYAMIGERTG NQFRIGDEIT IRVVKVNIEE RIIDFEVVGM KPRKPRENRD
RPTIIKAEKK NKPGDHRPPK NKGKKKPPAR GKKSKKRNTR KRP
//