ID R5GFA7_9BACT Unreviewed; 766 AA.
AC R5GFA7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=BN773_01803 {ECO:0000313|EMBL:CCY15863.1};
OS Prevotella sp. CAG:755.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262935 {ECO:0000313|EMBL:CCY15863.1, ECO:0000313|Proteomes:UP000018353};
RN [1] {ECO:0000313|EMBL:CCY15863.1, ECO:0000313|Proteomes:UP000018353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:755 {ECO:0000313|Proteomes:UP000018353};
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:CCY15863.1}.
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DR EMBL; CAXR010000106; CCY15863.1; -; Genomic_DNA.
DR AlphaFoldDB; R5GFA7; -.
DR STRING; 1262935.BN773_01803; -.
DR Proteomes; UP000018353; 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; 1.
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:UP000018353};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 657..738
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 394..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..766
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 87256 MW; 2EE61A422ABB81F6 CRC64;
MGKGKTKGAR RLTKKEIRKR ILDLMERHAS TEFDVKDIFK TIQADTHPAK MLTMDVLREL
VLDDYLSTDE RGHYRYAVRS QVMEGTFMRK RNGRNSFIPD DGGKSILVCE RNSGHALDGD
RVRVTMLARR SGHTREAEVI EVLKRARETF VGKLKVSHDY GFLITEGRAL ANDIFIPKDL
LGGGQTGDKA VVKIVEWPDE AKNPIGKVID ILGKEGENNA EMHAILAEFG LPYTYPKKVE
EAAERIPADI TPEDLKERED FRSVTTFTID PRDAKDFDDA LSIRRLDDGL WEIGVHIADV
SHYVKEGDII DREAQQRATS VYLVDRTIPM LPERLCNYIC SLRPDEDKLA FSAIFTMNDK
GDVLTWHPAH TVIRSNRRFV YEEVQNILEQ NGEASEEDLH QPGEHPARVE PGPNGKPVGE
YATELITLNR LAKLLRKRRF AHGSIGFDRA EVRFEIDEQG KPVSTYFKVA KDANKLVEEF
MLLANRSVAE KIGKPGKGKK PKTFPYRIHD VPDPEKLEKL SAFIGKFGYR LRTEGSKTDI
SKSLNKLLED VKGQKEEDLV ETIALRAMMK ARYSVHNIGH YGLMFDYYTH FTSPIRRYPD
TMVHRLLTRY MAGGRSVNAD KCEELCEHAS AMEQLAAKAE RASIKYKQVE FMAERVGQEF
DGKVSGVTEF GLYVEIDENK CEGMVPLRDL EGDYYEFDER NYCLRGRKRG RVYAIGDPVR
IRVARANIDR KQLDFALVAT EEPTPAAPKT KGRGRRKPQA KRSPKK
//
