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Database: UniProt
Entry: R5B798_9BACE
LinkDB: R5B798_9BACE
Original site: R5B798_9BACE 
ID   R5B798_9BACE            Unreviewed;       751 AA.
AC   R5B798;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-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=BN813_01916 {ECO:0000313|EMBL:CCX48772.1};
OS   Bacteroides sp. CAG:927.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262753 {ECO:0000313|EMBL:CCX48772.1, ECO:0000313|Proteomes:UP000017907};
RN   [1] {ECO:0000313|EMBL:CCX48772.1, ECO:0000313|Proteomes:UP000017907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:927 {ECO:0000313|Proteomes:UP000017907};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCX48772.1}.
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DR   EMBL; CAWM010000076; CCX48772.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5B798; -.
DR   STRING; 1262753.BN813_01916; -.
DR   Proteomes; UP000017907; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000017907};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          630..711
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          714..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  84491 MW;  21DDF0FA9EC6C00B CRC64;
     MAPKKSNSKK LTASDMRQAV MKYISEHSSG TFNYKQVAYA IDADTPAAHR SVAMLLAGMA
     FDGDLIETSP GKYKAPARSN VTTGVFVRRS NGKNSVITDE DGESIFVAER NSMHALNGDK
     VRVIVAARRR GVEPEAEVME IIEPKEQTFI GTLKVEKQYA FLQTDSKFLA TDILIPKNRL
     KGGVTGDKAI VRITSWPDDA KNPIGDIIDI LGKTGENTTE MHAILAEFGL PYRYPKAVED
     AAAKIDAGIT DDVVASRVDM RDVTTFTIDP TDAKDFDDAL SFRELPNGHY EVGVHIADVT
     YYVQPDTILD KEARSRATSV YLVDRVVPML PEHLSNGICS LRPDEDKLTF SCIFEMDAAA
     KVYSSRIART VTRSNRRFTY DEAQNIIETG KGDYAKEVLT LDAMAKILRR ERFENGSVEF
     DRAEVRFEID ETGHPIRTYF KESKDANKLI EEFMLLANKT VAAFIGKPQG HKKAKAFVYR
     VHDMPDPGKL TDLSKIARAF GYKVKESGSA REVNRSINRM LAEVKGKGEE NFLSTLAIRS
     MAKAIYTTQN IGHYGLGFDF YTHFTSPIRR YPDMMVHRLL DRYMADGRSV NVAKLEDQCK
     HSSEMEQLAS NAERASIKYK QVEYMADHLG ETFDGVISGV TEWGLYVELN ENLCEGLVPV
     RDLADDYYDF DEKNYCLIGR RNNVRYRLGD DVKVRVARTS LERKQLDFVL VDDRGRRPGE
     DEMGKTVSAR QALSKGGKQK RSKEKTRSHR K
//
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