ID A0A0B4S0X7_9FIRM Unreviewed; 697 AA.
AC A0A0B4S0X7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=NW74_03720 {ECO:0000313|EMBL:AIZ36507.1};
OS Parvimonas micra.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Parvimonas.
OX NCBI_TaxID=33033 {ECO:0000313|EMBL:AIZ36507.1, ECO:0000313|Proteomes:UP000031386};
RN [1] {ECO:0000313|EMBL:AIZ36507.1, ECO:0000313|Proteomes:UP000031386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCOM 1535 / ChDC B708 {ECO:0000313|Proteomes:UP000031386};
RA Kook J.-K., Park S.-N., Lim Y.K., Roh H.;
RT "Complete genome sequence of Parvimonas micra KCOM 1535 (= ChDC B708).";
RL Submitted (OCT-2014) 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; CP009761; AIZ36507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4S0X7; -.
DR STRING; 33033.NW74_03720; -.
DR KEGG; pmic:NW74_03720; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000031386; Chromosome.
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; 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; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
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:UP000031386};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 616..696
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 697 AA; 80662 MW; 29814DA683606E4E CRC64;
MNLEKQLLNF MKKKDYIPLT KEELAVALNI SFNSLKQFFK LLDSLVNSKK VSFDDYKYSI
YQKKETLKGK ISFTTKGNAF FISEEDIDDI FIPKKELNHA NHNDDVEIEI IKEKRMNSKA
EGRVLKVLNR NSNLIVGTFT ENKNFGFVVP DDIKCNYDIF IKKGDKNGAK TDDKVVCKLV
EFPDKKKNPE GVVIEVIGNK KDKNAQIISL LKDMEIPYKF SNKINKELEE LTQTDIKKEI
KNRVDFRNLF TVTIDGADAK DFDDAISIDK KDNDYVLYVH IADVSHYVKK DSKLDREAYK
RGNSVYLIDY VVPMLPEVLS NNLCSLNPNT DKLSITVKMI IGKNGNVKEY KFYESVINSN
YRLVYDDVTN FLEGKKHFYD DETLKENLLV MKELDEILTN KRINRGTIDF NFPEIAITFG
KDGKVENIAK KENGLANRII ESFMICANEV VGKHFGELDI PIIYRIHSKP PEDKLEILKN
NLSRLNIKMK PIDMISSKYL SEIIDQFKDT NKSDFINYSI LRSMTKAKYS PNIDIHFGLA
TFLYCHFTSP IRRYADLTVH RTLKNYLHSN IEIPKNYISY LDITSNHIND TEVLAIDAER
KLEDIKKVEF MKNKIGQVFR GIIVSVTSFG LFVQLENTVE GLVKYEDIMD DYYEFDEQTL
TAIGRRTKNV FDIGMGVEVI VAKVNEITNE INFYLNR
//
