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Database: UniProt
Entry: R7D0Y4_9BACE
LinkDB: R7D0Y4_9BACE
Original site: R7D0Y4_9BACE 
ID   R7D0Y4_9BACE            Unreviewed;       719 AA.
AC   R7D0Y4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=BN666_02647 {ECO:0000313|EMBL:CDD83363.1};
OS   Bacteroides sp. CAG:462.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262740 {ECO:0000313|EMBL:CDD83363.1, ECO:0000313|Proteomes:UP000018063};
RN   [1] {ECO:0000313|EMBL:CDD83363.1, ECO:0000313|Proteomes:UP000018063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:462 {ECO:0000313|Proteomes:UP000018063};
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:CDD83363.1}.
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DR   EMBL; CBHU010000173; CDD83363.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7D0Y4; -.
DR   STRING; 1262740.BN666_02647; -.
DR   Proteomes; UP000018063; 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   Reference proteome {ECO:0000313|Proteomes:UP000018063};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          638..719
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   719 AA;  82666 MW;  C58D6C4E50C4267E CRC64;
     MGKKDKKVKK EKKGGKRMTK KQLVEKLTDL IQLNAPESVS LKRIYAELKL NTHPLKMLCL
     DILQDMLTDD FICEPEKGRY KLKNPDQIVT GTFQRKSNGK NSLLPEDGST PIFVAERNSA
     HAMNNDKVRV ALFARRKNRE REGEVIEILE RANDTFVGRL KVDRHYAFLL TESRTLANDI
     FIPKERLKGA KDGDKVVVRV AEWPDDAKNP IGQVIDVLGR AGDNTTEMHA ILAEYGLPYS
     YPENVEHAAE QIPAEISAED LAEREDFRDV LTFTIDPKDA KDFDDALSIR RVNDGLWEVG
     VHIADVSHYV KEGSIIDKEA FKRATSVYLV DRTVPMLPER LCNFICSLRP DEEKLAYSVI
     FRIDDKGNVR DSHIAHTVIR SNRRFTYEEV QDILEARQGE YAAELMQLNT FAKILRERRM
     AAGAINFDRM EVRFEIDEAT GRPLSVYFKV QKDAHKLIEE FMLLANRTVA ERIGKVRGGA
     KPKVFPYRIH DLPDPEKLED LKNFIVKFGY KLKTAGSKTD VSRSLNHLLD EIQGKKEENL
     IETVSLRAMQ KARYSTFNIG HYGLAFDYYT HFTSPIRRYP DLMVHRLLTR YLAGGRSVQQ
     QKYEDKCEHC SDMEQVAASA ERASIKYKQV EFMSEHIGEV YDGTISGITE WGIYVEINEN
     KCEGMVPMRD LGEDYYDFDE KNYCLIGRKR HKRFSLGDPV RIKVARANLE KKQLDFTIA
//
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