ID N9UNR2_9SPHN Unreviewed; 769 AA.
AC N9UNR2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=EBMC1_16009 {ECO:0000313|EMBL:ENY79989.1};
OS Sphingopyxis sp. MC1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY79989.1, ECO:0000313|Proteomes:UP000013072};
RN [1] {ECO:0000313|EMBL:ENY79989.1, ECO:0000313|Proteomes:UP000013072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|EMBL:ENY79989.1,
RC ECO:0000313|Proteomes:UP000013072};
RA Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., Nielsen J.L.;
RT "Differential expression analysis of membrane associated proteins from
RT triclosan-degrading sphingopyxis.";
RL Submitted (FEB-2013) 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}.
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:ENY79989.1}.
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DR EMBL; AOUN01000022; ENY79989.1; -; Genomic_DNA.
DR RefSeq; WP_003051258.1; NZ_AOUN01000022.1.
DR AlphaFoldDB; N9UNR2; -.
DR PATRIC; fig|1174684.3.peg.3234; -.
DR eggNOG; COG0557; Bacteria.
DR Proteomes; UP000013072; 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 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:UP000013072};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 647..728
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 729..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..769
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 84014 MW; DC3681F5FEE0A428 CRC64;
MAKAPKRPQP AGLPSREQIL RFIEDSPGAV GKREIAKHFA LRGADKIALK ALLKDMTDEG
VVDMAPGRAF HKHGGLPKVT VLRVAAVEGD TVWAVPDRWE GGGQAPRLRV MEKGRKSALG
VGDRILARTE ERGSGHVAHP MKKLQSGGES VIGVLVADTG PGGKPMTWLR PADKRARFDF
AVADMGDAAI GDLVRAELSG RGPATKARVI DRIGDPFAPR SLSMIAIAKH NIPHVFGDEM
LAEAERAATL PLTPEGREDL RDLPIVAIDP ADARDHDDAV WAIPDEDPGN KGGWKAIVAI
ADVSYYVRPD GALDREARRR GNSVYFPDRV VPMLPETLSA GVCSLKAGQD RAAMACHLTV
DKHGKVTSWR FTRALVRLRA NIAYERAQAA YDADAPDEGW DADVLPALRH LWGCWTLLTK
ARAARSPLDL DLPERQVILD AQGNIAEIRV RERLDAHRLI EDYMIAANVA AAKALEAKKS
PVMYRIHEPP SREKLVSLKE YLESFEQSFA LGQVITPAVF NRLIDGFSGD DRLPEIMEAI
LRSQTQAYYG PANAGHFGLA LGSYAHFTSP IRRYADLLVH RALVDSYRLE VPGKPKGLPE
RSGLGEADQK GFSRIGEAIS GLERRAMEAE RETVDRYVAA YLAGKVGEIV PARITGVQPF
GFFATVDGLG GDGLVPVSML GSERFFYDEA ARTLDSEHGR VSYSVGQRLD LRLMEANPVS
GALRFELPDA PEGGFRNRPP RRDGVKKAGK HMVGKRGRPG NIRHEGKRR
//
