ID E5V6Y3_9BACE Unreviewed; 714 AA.
AC E5V6Y3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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 ECO:0000313|EMBL:RGJ32415.1};
GN ORFNames=DXD65_13775 {ECO:0000313|EMBL:RGJ32415.1}, HMPREF1007_00516
GN {ECO:0000313|EMBL:EFV27415.1};
OS Bacteroides sp. 4_1_36.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=457393 {ECO:0000313|EMBL:EFV27415.1, ECO:0000313|Proteomes:UP000004735};
RN [1] {ECO:0000313|EMBL:EFV27415.1, ECO:0000313|Proteomes:UP000004735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4_1_36 {ECO:0000313|EMBL:EFV27415.1,
RC ECO:0000313|Proteomes:UP000004735};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Sibley C., Strauss J., Daigneault M., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 4_1_36.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RGJ32415.1, ECO:0000313|Proteomes:UP000263804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM07-1 {ECO:0000313|EMBL:RGJ32415.1,
RC ECO:0000313|Proteomes:UP000263804};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:EFV27415.1}.
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DR EMBL; ACTC01000030; EFV27415.1; -; Genomic_DNA.
DR EMBL; QSOX01000014; RGJ32415.1; -; Genomic_DNA.
DR RefSeq; WP_005830959.1; NZ_QSOX01000014.1.
DR AlphaFoldDB; E5V6Y3; -.
DR HOGENOM; CLU_002333_7_3_10; -.
DR Proteomes; UP000004735; Unassembled WGS sequence.
DR Proteomes; UP000263804; 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; 2.
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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 633..714
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 714 AA; 81704 MW; 12C5C43E55C25EB8 CRC64;
MAKKKEKKAG KRMKKKELVK VLLEFFHTKQ DEVLSLKYIF EQLHLTTHPL KMLCMDILSE
LSMDDYITEV DKHKYKLNNH GVEMTGTFQR KSNGKNSFIP EGGGEPIFVA ERNSAHAMNN
DKVRIAFYAK RRGREAEGEV IEILERANDT FVGTLEVAKS YAFLVTENRT LANDIFIPKE
KLKGGKTGDK AIVKVVEWPD KAKNPIGQVI DILGRAGDNT TEMHAILAEF GLPYVYPAAV
EKAADKIPAE ISAEEIARRE DFRGVTTFTI DPKDAKDFDD ALSIRKLKGG LWEVGVHIAD
VTHYVKEGGI IDKEAEKRAT SVYLVDRTIP MLPERLCNFI CSLRPDEEKL AYSVIFEMTE
KGEVKNSRVV HTVIKSDRRF TYEEAQEIIE TGKGDFQEEV LQLDKLAKIL RENRFKAGAI
NFDRYEVKFE IDEKGKPVSV YFKESKDANK LIEEFMLLAN RTVAEKIGRV PKGKKAKVLP
YRIHDLPDPE KLDNLAQFIA RFGYKLRTSG TKTDISKSIN HLLDDIQGKK EENLIETVSI
RAMQKARYSV HNVGHYGLAF DYYTHFTSPI RRYPDMMVHR LLTKYLDQGG RTVSEQKYEA
LCEHSSSMEQ IASNAERASI KYKQVEFMTE RLGQTFDGVI SGVTEWGLYV ELNENKCEGM
IPIRDLDDDY YEFDEKNYCL RGRRKNKIYS LGDAITIKVA RANLEKKQLD FALV
//
