ID A0A1M6IZJ6_9BURK Unreviewed; 833 AA.
AC A0A1M6IZJ6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN05192548_1001299 {ECO:0000313|EMBL:SHJ39881.1};
OS Paraburkholderia terricola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=169427 {ECO:0000313|EMBL:SHJ39881.1, ECO:0000313|Proteomes:UP000184395};
RN [1] {ECO:0000313|EMBL:SHJ39881.1, ECO:0000313|Proteomes:UP000184395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20594 {ECO:0000313|EMBL:SHJ39881.1,
RC ECO:0000313|Proteomes:UP000184395};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
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; FRAB01000001; SHJ39881.1; -; Genomic_DNA.
DR RefSeq; WP_073426878.1; NZ_JAVDRI010000002.1.
DR AlphaFoldDB; A0A1M6IZJ6; -.
DR STRING; 169427.SAMN05192548_1001299; -.
DR KEGG; pts:CUJ90_07215; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000184395; 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; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 668..749
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 755..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 93019 MW; 829F782DBA23B3DA CRC64;
MQREKTIDKP LSKFPYPIPS REEILGVLRT SEAPLAANEI AEALSIKRQE REGFFKRLGA
MERDGQIRLD QRNLYQLTHP SNFVAGRVQG HRDGYGFLIR DDGQDDLFLP TGEMQKVMHN
DRVLARIVGY DRRGRPEGHI VEVTDRANKR VIGRLLNENG ALIVAPEDKR IGHDILITQN
TKKAKVGQVV VVELTDFPSR HSQPLGRVAE VLGDIDDPGM EIEIAVRKYG VPHEFSQAAL
DEASKLPDEV RPVDARHRID LRDVPLVTID GEDARDFDDA VYCEPVQVGR GEGFRLIVAI
ADVSHYVHPK SGLDADAIER STSVYFPRRV IPMLPEKLSN GLCSLNPNVD RCVLVCDMIV
TARGEVKAYQ FYPGVMHSAA RLTYTEVAAV LKNTKGPEAA RRAALLPQLQ NLYGVYKSLF
AARQKRGAID FDTTETYIVC NAQGKIEQIV PRTRNEAHKL IEECMLAANV CAADFLKRNK
HPGLFRVHAG PTAEKLENLR TFLRGMGLTL AGGETPHASD YAALMAQIRE RPDAPMLQTM
LLRSMQQAVY SPENIGHFGL AYEAYAHFTS PIRRYPDLLT HRAIYAILQG RKYQPEPAQG
IELNTALSPR ARAMQKADDE KRGRVRGNNV AIWEELGLHC SANERRADEA SRDVEAWLKC
YFMRDKLGEE YGGMVNGVTS FGIFVQLDSL FIEGLVHVTE LGSDYFQYDE IKNELRGERT
GIRYRLSDRV RVQVSRVDLD ARKIDFRLVR DTPIKPPVNR TPLADKSSGE NGGARVRVLP
PIEGAVPAPV GRRKKAAPAQ SAAVQEARAA RGAAKKHGAT AKPASKPQTR KKR
//
