ID D5U636_BRAM5 Unreviewed; 665 AA.
AC D5U636;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Bmur_0424 {ECO:0000313|EMBL:ADG70527.1};
OS Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS murdochii).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG70527.1, ECO:0000313|Proteomes:UP000001915};
RN [1] {ECO:0000313|EMBL:ADG70527.1, ECO:0000313|Proteomes:UP000001915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC {ECO:0000313|Proteomes:UP000001915};
RX PubMed=21304710; DOI=10.4056/sigs.831993;
RA Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL Stand. Genomic Sci. 2:260-269(2010).
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}.
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DR EMBL; CP001959; ADG70527.1; -; Genomic_DNA.
DR RefSeq; WP_013112954.1; NC_014150.1.
DR AlphaFoldDB; D5U636; -.
DR STRING; 526224.Bmur_0424; -.
DR KEGG; brm:Bmur_0424; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_4_1_12; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000001915; 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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
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 PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 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; 2.
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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 525..603
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 73..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 665 AA; 77350 MW; 3D4AF037E197EE4F CRC64;
MKVIKLLKRI NKEKELDISV YKNKYVETKK DKLRFEKMLQ KSVSMGLVMK KSNILKLTNE
GKVYLEKELR RSSEKANNIS ENKRDRRNSK NKKSDTGNKK TSIPKPEIKV DINNAKKDAE
IIAKAYNVPT DFPKKCLEEA KLLPDSMENV ELEFDRIDLR NIRTVTIDGA DSKDFDDAIS
IEKLNDGYKL GIHIADVSHF VVMGSALDRE ARKRGNSVYL IDTVYPMFPH ELSNGICSLN
EGVSRFTMTV FVTIDNNGNV KESTFHKSVI KSDRRLTYDY AQDVLDGIEQ DEDWLIELLK
NADDVKKILL QKRIENGSIE FNLNETQIIL DKGGNPKDFF IGERKETHKI IEELMLIANC
EVAKRLKNIK GSIYRVHDSP DIEKLDTFTR IAFNRGYRLT KDADGNLDFH SFIESIMGKP
DEKLLLTLLL RSMKQAIYDV NNIGHFGLGF EYYTHFTSPI RRYTDLLTHR LLKLSLEGIN
NLKPTMQQFY TNSAEWCSKT ERVAVECERS LAKVKAARFM KDKVGNEYNG IISGITNFGI
FVEIEDRGIE GLIRYAVLKS RYRYDENEQA AYSEEDAKWY TLGDRIRIVV YKVDIRELFI
DFIPASEFDN SFDDRDIIDS RDFIKNKKNK KEIYSRKYNK SSKDRKRGAK DRRDRKERKK
SKKRR
//
