ID A0A1I5WR34_9BACT Unreviewed; 779 AA.
AC A0A1I5WR34;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04515674_112115 {ECO:0000313|EMBL:SFQ22027.1};
OS Pseudarcicella hirudinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Pseudarcicella.
OX NCBI_TaxID=1079859 {ECO:0000313|EMBL:SFQ22027.1, ECO:0000313|Proteomes:UP000199306};
RN [1] {ECO:0000313|EMBL:SFQ22027.1, ECO:0000313|Proteomes:UP000199306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E92,LMG 26720,CCM 7988 {ECO:0000313|Proteomes:UP000199306};
RA de Groot N.N.;
RL Submitted (OCT-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; FOXH01000012; SFQ22027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5WR34; -.
DR STRING; 1079859.SAMN04515674_112115; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000199306; 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; 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:UP000199306};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 659..740
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 742..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 89251 MW; 3C05EE47B691C19A CRC64;
MSKKIKSTKE ERFLLNLKEE IIAFFDINED RALSVNQVHK GFAVRDRKTK ELFSELVEEL
HAEGRLIRNS DGNYIIDNQT LFVTGKVDHV NARFAFVVVG NEVPDIWVNT KDLNGAIDGD
TVKVLARSTA RKKKSERPEG EVVEIIERRS DEIVGTIEVL PNFAFVNPDS KKIFQDIFIA
KDYIKDAKNG DKVIVKVTQW AENERKAEGR IIEVLGKAGE NNTEMHAILA EFGLPIHFPE
VVEKEAERIS EKITKEEIDK RRDFRKVTTF TIDPIDAKDF DDAISFQYLE NGNYEIGVHI
ADVSHYVTEN TLLEQEAYKR ATSVYLVDRV VPMLPEKLSN GLCSLRPHED KLTFSAVFEV
SPEAKVVKEW FGRTVIHSDK RFSYEEAQEV MDGTYQLPVE ESVIEEEPVK KGKKKKKDVV
SGNIFKGELL ILNSLAHKLR DERFRKGAVN FETVEVRFVL DENGKPLSVY PKIRKDAHKL
IEEFMLLANK KVAEFVHNLR KKEPVNVMVY RIHEAPDPEK LKTFSSFAKK FGYNVDIDKE
GVSSSLNHLM DDVEGKPEQN ILQSLAVRTM SKARYSTDPI GHFGLSFPFY SHFTSPIRRY
PDVMAHRLLQ HYLDGGEPVE KGPWEIRCKH SSEMEKLASE AERASIKYKQ VEFMSLMEEK
VFDGIITGVT EFGFFVEITE TACEGLVRMV DLKDDFYDLD KDNFRIVGQR NGRVFTFGDP
VQVKVKECNL ARRSMDLELI GMTGKKGRGS SGERSRSKSK VIPRGKRREN SMRGKNKRK
//
