ID A0A1I5DBA5_9PROT Unreviewed; 731 AA.
AC A0A1I5DBA5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=SAMN05216386_2264 {ECO:0000313|EMBL:SFN96397.1};
OS Nitrosospira briensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=35799 {ECO:0000313|EMBL:SFN96397.1, ECO:0000313|Proteomes:UP000183107};
RN [1] {ECO:0000313|Proteomes:UP000183107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nsp8 {ECO:0000313|Proteomes:UP000183107};
RA Varghese 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOVJ01000005; SFN96397.1; -; Genomic_DNA.
DR RefSeq; WP_074797450.1; NZ_FOVJ01000005.1.
DR AlphaFoldDB; A0A1I5DBA5; -.
DR STRING; 1266925.GCA_000619905_02632; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000183107; 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; 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; 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:UP000183107};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 639..720
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 731 AA; 83181 MW; 2E26219EBDC1554B CRC64;
MSIKKKRKLR DLDPQLEREK ARYGHALPSR EFILQALEDQ GVPVNENVLQ NLLEITEEET
EIFGRRVSAM LREGQIMRNR KGDICVVEKL DLIRGRVQGH PDGFGFLIPD DSSPDLFLSA
KEMHKALHGD RVMVRETGVD RRGRREGTIV EVLERAVTQL VGRLHADHGI LFVEAENRRI
SQDILIPGEE SMGARAGQVV MVEIIQQPSK HAQPIGRIVE ILGNYTSPGM EIEIALRKHE
LPHQFPPEVD KRSAKFPDKV LKADLKERED IRHLPMVTID GETARDFDDA VYCERDGKDY
KLYVAIADVS HYVSSGDALD REAFNRGNSV YFPRRVIPML PEVLSNGLCS LNPQVERLCM
VCEMNLDTKG GFREYRFYPA VMFSHARLTY TKVAAMLENP KGEDAQQYKN LLPHIKLLYK
LFKVLLKARG KRGAIDFETI ETQMIFNDQG KIERILPVKR NDAHRLIEEC MLAANVCASD
FLQKHKQQTL YRIHEGPTPE KLLALRDFLK EFGVQLSGGD EPGAKDYAKT LTRIKDRPDA
QLLQTVMLRS LRQAVYSPDN VGHFGLAYES YTHFTSPIRR YPDLLVHRAI KAVLSDTVYS
PGNWHELGEH CSQTERRADD ATRDVETWLK CYYMQDRIGE CFDGVISGVT GFGLFVALDG
IYVEGLVHIS ELPSDYFHFD AAKHMLLGER SGKRYRLGDR LRVKLVRVDL ETSKIDFVLD
GNGAASRTAE S
//
