ID U5QBL3_9BACT Unreviewed; 723 AA.
AC U5QBL3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:AGY54835.1};
GN ORFNames=BRDCF_p2208 {ECO:0000313|EMBL:AGY54835.1};
OS Bacteroidales bacterium CF.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY54835.1, ECO:0000313|Proteomes:UP000017642};
RN [1] {ECO:0000313|EMBL:AGY54835.1, ECO:0000313|Proteomes:UP000017642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AGY54835.1};
RX PubMed=24356833;
RA Tang S., Edwards E.A.;
RT "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT Dechlorinating Enrichment Culture.";
RL Genome Announc. 1:e01066-13(2013).
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}.
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DR EMBL; CP006772; AGY54835.1; -; Genomic_DNA.
DR AlphaFoldDB; U5QBL3; -.
DR STRING; 1400053.BRDCF_p2208; -.
DR KEGG; bacc:BRDCF_p2208; -.
DR HOGENOM; CLU_002333_7_3_10; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000017642; Chromosome.
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; IPR011129; CSD.
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; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 2.
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:UP000017642};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 575..656
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 82816 MW; 3FAD9471A0A57A8F CRC64;
MHNNRNEKNS GKFNKRGKSV SKTPKEETIG RVSMTREGYG FIIREGFEDD IFVSARKMRH
ALHGDTVKVV MTSKKTNTKR IEGEVIDIVE RSKKPIIGIL QIAGSQAWVI TESKNMPYDI
RIPLESIDVK QNGLKVAALV DDWPRRSDEP LGHIIDILGA PGDNNTEMHA ILAEFGLPYK
FEANVEKEAD KISEIISLDE IKSRRDFRMV PTLTIDPADA KDFDDALSLQ KLDNGNWEIG
VHIADVTHYV RPGSLIEKEA LDRATSVYLV DRTVPMLPEK LSNKLCSLRP NEEKLCFSAV
FEMNDKGKLI NKWFGRTVIN SDMRFNYDQA QEIIEGGNGP MKKEILKLHE LATILRNERF
RSGAISFERP EMKVEVDENG KPLGVYSKIT KESNWLIEEF MLLANREVAY FIGGKGKDSK
TFVYRIHEEP NIDKIIAFRT FIKHFGYEMK PTKNAREISS EINKLLETAK GRPEEGAIEI
MALRSMARAR YSTENLGHYG LAFDYYTHFT SPIRRYPDMM VHRLLAMYLD KAKSQDKKYY
EERCKYSSER EQLATEAERA SIKYKMVEFM QDKVGMEFEG NVSGVTEWGM FVELAETKIE
GLVALRDIKE DYLEYNEDSM SLTGKRSGKR FTLGDKVRVK VDRANLEQKQ LDFILIWDKT
EESEPVSESN SSKKPTGRYP RKSSGPSKRT NSPSKKTSST SKKSTKEKES KKPSRRERKG
DSK
//
