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Database: UniProt
Entry: R6CZ37_9BACE
LinkDB: R6CZ37_9BACE
Original site: R6CZ37_9BACE 
ID   R6CZ37_9BACE            Unreviewed;       722 AA.
AC   R6CZ37;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=BN697_00385 {ECO:0000313|EMBL:CDA76871.1};
OS   Bacteroides sp. CAG:530.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262741 {ECO:0000313|EMBL:CDA76871.1, ECO:0000313|Proteomes:UP000018392};
RN   [1] {ECO:0000313|EMBL:CDA76871.1, ECO:0000313|Proteomes:UP000018392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:530 {ECO:0000313|Proteomes:UP000018392};
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|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   -!- 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:CDA76871.1}.
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DR   EMBL; CBCL010000128; CDA76871.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6CZ37; -.
DR   Proteomes; UP000018392; 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; IPR013223; RNase_B_OB_dom.
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; PF08206; OB_RNB; 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:UP000018392};
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   722 AA;  82424 MW;  8852536F6191122C CRC64;
     MAKKKKEKKG GKRMKKRELA ELLVTFFRTR PETSFGLKQI FGSLNLTTHP LKMLCVDIID
     EMLEENFLVE TEKGHFQLNG RGQIMTGVFQ RKSNGKNTFI PDDGGDPIAI SDSNSAHAMN
     GDKVKIALSA RRRRHDPEGQ VLEILEHSDT PFVGTLKVSK NYAFLLTETN TLANDIFIPK
     DKLKGGKDGD KAVVRITEWP EDAKNPFGEV IDILGKAGEN TTEMHAILAE YGLPYHYPQN
     VEAAAEKISA EITPEDYAER EDCRDVTTFT IDPKDAKDFD DALSIRQLKP GLWEVGVHIA
     DVSHYVKEGS VIDKEAVKRA TSVYLVDRTI PMLPERLCNF ICSLRPDEEK LAYSVIFTMN
     EKAEVKDYRI RHTVIKSNRR FTYEEAQEII ETGKGEYKEE ILELNKLAQI LREKRMANGS
     INFDRCEVKF EIDESGKPLS VYFKESKEAN KLIEEFMLLA NRTVAEHIGK VPKNKKPKVF
     PYRIHDLPDP DKLENLSQFI ARFGYKIRTG GTKTEVSKSI NRLLNDIDGK KEQNLIETVS
     LRAMQKARYS IHNIGHYGLA FDYYTHFTSP IRRYPDLMVH RLLTRYLAGG RTAQADKYEE
     LCEHSSAMEQ TAAAAERASV KYKQVEFMGE RIGNVYDGVI SGVTEWGLYV EINENKCEGM
     VPMRDLGDDY YEFDEKNYCL IGRKRHQKFS LGDPVQIKVA RANLEKKQLD FVLADDKLPI
     KK
//
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