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Database: UniProt
Entry: A0A075LN58_9BACI
LinkDB: A0A075LN58_9BACI
Original site: A0A075LN58_9BACI 
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
//
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