ID A0A1I0RW26_9RHOB Unreviewed; 746 AA.
AC A0A1I0RW26;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04488515_3352 {ECO:0000313|EMBL:SEW45559.1};
OS Cognatiyoonia koreensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatiyoonia.
OX NCBI_TaxID=364200 {ECO:0000313|EMBL:SEW45559.1, ECO:0000313|Proteomes:UP000199167};
RN [1] {ECO:0000313|EMBL:SEW45559.1, ECO:0000313|Proteomes:UP000199167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17925 {ECO:0000313|EMBL:SEW45559.1,
RC ECO:0000313|Proteomes:UP000199167};
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|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; FOIZ01000002; SEW45559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0RW26; -.
DR STRING; 364200.SAMN04488515_3352; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000199167; 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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
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:UP000199167};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 623..709
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 710..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..746
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 82192 MW; EBCF136CD23D8A15 CRC64;
MAQIPSKQDI LDFIADNPAR TAKRDIARAF GIKGAQRIDL KRILKEMEAD GQLQKRRSSY
RDPETLPPVG VLEIVGPDAD GDLIAKPMEW NGEGVEPTVL LSLRNGDPAL GPGDRVLGRL
TQTPKDDHPY HARMIRRIGA NPLRIIGIFR AGSEGGRILP IDKGSDKEWI VPAGATGGAK
DGELVEVEQA GPKGRMGLPK ARIVNRLGDP SQPKAVSLIA IHQHGIPDHF PDDVVAEADA
AKPATLGKRT DLRDLPLVTI DPWDARDRDD ACYVQAHDDG FTIWVAIADV AHYVRPNSPL
DHEARKRGNS TYFPDRVVPM LPDTLSGDLC SLHENVDRAC LAVSMRIDGN GNKVSHEFHR
ALMRSSASFN YEEVQAAIVG QPNEKTEPLL EDVLRPLYAA YEALKKARAV RQPLELDLPE
RQIVLGDDGT VTSVNFKERL DAHRLIEEFM VLANVAAAET LIAKKSPLLF RVHEEPTPEK
LDALRDVADA SGLQLAKGQV LKTSHLNRLL AQAKDTDQAE LINLNTLRSM TQAYYHHENF
GHFGLALRAY AHFTSPIRRY SDLIVHRALI SAHGWGKDGL SPWDVEHLED TGKLISDTER
RSMMAERDTT DRYLSAFLAD RVGTEMTGRI SGIAKFGVFV KLDETGADAM IPIRTLGAEY
FHYDADTQTL MGADTGTVIG LGQRVTVKLA EVTPVTGGLT AELIRLDERL MPKGPAKGRG
KPPRRKVGAA KKKSAKIARK VKRRRK
//
