ID A0A1X9NBG9_9GAMM Unreviewed; 796 AA.
AC A0A1X9NBG9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BST96_09770 {ECO:0000313|EMBL:ARN74384.1};
OS Oceanicoccus sagamiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Oceanicoccus.
OX NCBI_TaxID=716816 {ECO:0000313|EMBL:ARN74384.1, ECO:0000313|Proteomes:UP000193450};
RN [1] {ECO:0000313|EMBL:ARN74384.1, ECO:0000313|Proteomes:UP000193450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107125 {ECO:0000313|EMBL:ARN74384.1,
RC ECO:0000313|Proteomes:UP000193450};
RA Kumagai Y.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (NOV-2016) 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|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}.
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DR EMBL; CP019343; ARN74384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9NBG9; -.
DR STRING; 716816.BST96_09770; -.
DR KEGG; osg:BST96_09770; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000193450; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 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; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
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:UP000193450};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 661..742
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 89948 MW; 166619F0490975C0 CRC64;
MAKRLTDKDP HADREAQNYE QPIPSREFIM EFLEQAEGPL NRNQLTKALE LKDYQDVEAL
RRRLKAMERD GQLMRNRKGA YGLVDKMDLV RGRVSAHRDG YGFLMPQEGG DDLYLNSRQM
STVFDGDEVI CRSAGYDHRG KLEGVIVEVI NRNTQQLVGR LFDENGVVYV SPDNAKINHD
IIIPREAVGD AEVEQYVMVE ITSQPGWRKP PTGRVVEVLG EHMAPGMEID VAIRTHNIPH
VWPEEAEREA LALSAEPLEE DKLNRVDLRK LPFVTIDGED ARDFDDAVYC ESKLLGGWRL
WVAIADVSHY VQVGSALDQE ATLRGNSVYF PEQVVPMLPE ALSNGLCSLK PKVDRLCMVC
EMTISKAGKI SGYKFYEGVM HSHARLTYNK VGAILDKKNP DSKPLRIEYK KVVPHLENLH
DLYKTLRIAR SKRGAIDFET TETRMVFGDD RKISEIIPVV RNDAHKLIEE CMLAANVAAA
KFLEKHNVPA LFRVHEGPTE EKLEALRKFL GELAMDLPGG NKPGPDDYQV LLSQLGDRPD
AHIIQTMMLR SLRQAVYQPE NLGHFGLNYD AYGHFTSPIR RYPDLLVHRA IRHVVRSNME
SKKVKRVDGA TVLPKKTIYP YEMPDLLVLG EQCSMTERRA DDATREVVAW LKCEYLQDRV
GDTFEGVISA VTGFGLFVDL VDVYVEGLVH VSALASDYYH FDPVKQRLVG ERTGTSFQLG
DSVKVQVARV SLDDKKIDLE LVEGSSRAKR RAEKSGKPLK KGDRRPVIKK KKDDKKGGKK
TTSKSTAGKG VRKRKR
//
