ID A0A369WAW9_9GAMM Unreviewed; 831 AA.
AC A0A369WAW9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DV711_17490 {ECO:0000313|EMBL:RDE18441.1};
OS Motiliproteus coralliicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Motiliproteus.
OX NCBI_TaxID=2283196 {ECO:0000313|EMBL:RDE18441.1, ECO:0000313|Proteomes:UP000253769};
RN [1] {ECO:0000313|EMBL:RDE18441.1, ECO:0000313|Proteomes:UP000253769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C34 {ECO:0000313|EMBL:RDE18441.1,
RC ECO:0000313|Proteomes:UP000253769};
RA Wang G.;
RT "Motiliproteus coralliicola sp. nov., a bacterium isolated from Coral.";
RL Submitted (JUL-2018) 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}.
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:RDE18441.1}.
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DR EMBL; QQOH01000005; RDE18441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369WAW9; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000253769; Unassembled WGS sequence.
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; IPR022966; RNase_II/R_CS.
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; 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:UP000253769};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 673..754
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 760..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 92948 MW; 655EA41B9A524F8E CRC64;
MSTDMSRDPY ADREAKKYDN PIPSREYILE LLKKARRPMS HPQLSTELGL VSDQQTEALR
RRLRAMERDG QLVHTRRGGY GLADKMDLLA GRVIGHRDGY GFLSPDDGSD DVFLHNRQMR
KLFHGDRAMV RVSGVDQRGR REGSVVEVLE HCTQQLVGRY VDDFGIGYLV PENNKISQDV
VIADEDRLGA ETGQYVLVEL LVQPSKGRPR ARVVEVLGEQ MAPGMEIEVA IRNYDIPHLW
PDAATDEANR YGAEVREQDK QHRVDLRELP LVTIDGEDAR DFDDAVYCEA KKGGGWRLYV
AIADVSHYVR PGSALDQEAR NRGTSVYFPQ QVVPMLPEAL SNGLCSLNPN VDRLAMVCEM
TISAKGKLSG YQFYEAVIRS QARLTYTRVG ALLDEPESAV AQQLTAEHPD IVPHLYELFW
LYQALRGARD ERGAIDFETT ETRIVFGPDR KIDQIVPVVR NDAHKLIEEC MLCANVATAR
FLEKLKIPAL YRVHQGPKTQ KLENLRAYLG ELGLNLPGGE KPTPDDYQQL LQQAEGRPDA
ALIQTMMLRS LSQAVYTPDN EGHFGLAYSA YAHFTSPIRR YPDLLVHRAI RSVILDKGGL
MGRVKSLLSK SAKPPVRRVE GAPRADAGKV YPYDLAAMME LGEHCSLTER RADEATWDVQ
AWLKCEYMRD HIGDEFDGVV SAVTGFGLFV ELQGIHTEGL IHVTALQGDY YHFDAAKQRL
TGERTRVTYR LGDELRVRVV RVDLDERKID FELVETFSKK KGRKQDRRAP RSFGADAKSG
SKPGFRGGSR SASGGSRSAN SGSRNTKGGS KRGSKSVGNG GPSSAAKKRR R
//