ID D7IDW6_9BACE Unreviewed; 718 AA.
AC D7IDW6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=HMPREF9007_02523 {ECO:0000313|EMBL:EFI03910.1};
OS Bacteroides sp. 1_1_14.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469585 {ECO:0000313|EMBL:EFI03910.1, ECO:0000313|Proteomes:UP000003951};
RN [1] {ECO:0000313|EMBL:EFI03910.1, ECO:0000313|Proteomes:UP000003951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_14 {ECO:0000313|EMBL:EFI03910.1,
RC ECO:0000313|Proteomes:UP000003951};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 1_1_14.";
RL Submitted (MAR-2010) 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; GG774706; EFI03910.1; -; Genomic_DNA.
DR RefSeq; WP_008761713.1; NZ_GG774706.1.
DR AlphaFoldDB; D7IDW6; -.
DR GeneID; 60924259; -.
DR HOGENOM; CLU_002333_7_3_10; -.
DR Proteomes; UP000003951; 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; 3.
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; 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 635..716
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 718 AA; 82045 MW; B3D9C1334D9B7FD0 CRC64;
MAKKKEKKEK KAGKRMSKKE LAALLIDFFH AKPSETLSMK YIFSELHLTT HPQKMLCADL
LHDLSDDDYI SEIEKGKFRL NNHGTEMIGT FQRKSNGKNS FIPEGGGDPI FVAERNSAHA
MNNDKVKITF YAKRKNKDAE GEVIEILERA NDTFVGTLEV AKSYAFLVTE NRTLANDIFI
PKEKLKGGKT GDKAIVKVTE WPDKAKNPIG QVIDILGVAG DNTTEMHAIL AEFGLPYVYP
KAVETAADKI PAEITPEEIA RREDFRKVTT FTIDPKDAKD FDDALSIRPI KDGLWEVGVH
IADVTHYVKE GGIIDKEAEK RATSVYLVDR TIPMLPERLC NFICSLRPNE EKLAFSVIFD
ITEKGEVRDS RIVHTVINSD RRFTYEEAQQ IIETKTGDFK EEVLMLDTIA KALREKRFAA
GAINFDRYEV KFEIDEKGKP ISVYFKESKD ANKLVEEFML LANRTVAEKV GRVPKNKKPK
VLPYRIHDLP DPEKLENLSQ FIARFGYKVR TSGTKTDISK SINHLLDDIH GKKEENLIET
VSIRAMQKAR YSTHNIGHYG LAFDYYTHFT SPIRRFPDMM VHRLVTKYMD GGRSVSESKY
EDLCDHSSNM EQIAANAERA SIKYKQVEFM SERLGQIYDG VISGVTEWGL YVELNENKCE
GMVPIRDLDD DYYEFDEKNY CLRGRRKNKI YSLGDAITIR VARANLEKKQ LDFALIEK
//
