ID A0A0A2WRH9_THEFI Unreviewed; 734 AA.
AC A0A0A2WRH9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, 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=THFILI_06890 {ECO:0000313|EMBL:KGQ22746.1};
OS Thermus filiformis.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=276 {ECO:0000313|EMBL:KGQ22746.1, ECO:0000313|Proteomes:UP000030364};
RN [1] {ECO:0000313|EMBL:KGQ22746.1, ECO:0000313|Proteomes:UP000030364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43280 {ECO:0000313|EMBL:KGQ22746.1,
RC ECO:0000313|Proteomes:UP000030364};
RA Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I.,
RA Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.;
RT "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280
RT producer of carotenoid-(di)glucoside-branched fatty acids (di)esters.";
RL Submitted (FEB-2015) 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:KGQ22746.1}.
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DR EMBL; JPSL02000039; KGQ22746.1; -; Genomic_DNA.
DR RefSeq; WP_038061426.1; NZ_JPSL02000039.1.
DR AlphaFoldDB; A0A0A2WRH9; -.
DR STRING; 276.THFILI_06890; -.
DR PATRIC; fig|276.5.peg.413; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000030364; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
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 InterPro; IPR005471; Tscrpt_reg_IclR_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
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; PF09339; HTH_IclR; 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; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 599..676
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 676..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 564..591
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 676..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 82550 MW; A546D836BC2194C4 CRC64;
MQEVLYEFFK SNPKPHGLNE IIRRFGLEKR EAKRLLRSMV EEGLLDKVGS AYRLSERVVG
PISLHRDGYG FVRVEGGKDL FIPPGYTLDA WPGDLVEARP MPPGRDGRPW GVVERVLKRA
REQVVGTLDL RRGYALLLPD EAGIPPLKLH PKGLEGLMPG ARLLVRVEYG PRLHGVVERY
LGQGEAPETE TEAVIAKYGL RAEFPPEVLQ AAEAIPLEIP EGEAARRQDF RSLRVFTIDG
VDAKDFDDAI HVEKTRTGYR VGVHIADVSH YVAEGSPLDQ EAYLRGTSVY LPGRVLPMLP
ERLSNGVCSL RPGEDRLVLS VLFDLTPEGE VRRYQIREGI IRSVARLTYT EVEAFAEGFG
LPEEHAFLAE DLRLLLDLTA RLKARRLEAG ALDFAFPEVK VELDEEGNLH LLPQEEPRAR
SLIEELMLLA NRTVAEHLVA KGVPALFRVH EDPLADAYEK LRQALARLGY VLPRVPSSKA
LQEVLLASRG RPEAQVVANL LLRSLRLARY APENLGHFGL ALEHYLHFTS PIRRYPDLVV
HRVVKALLAR RLTPRRKAAW AEAFKGVAEH ASEMERKAEA AERELTKYYM ARWAELHVGE
RFSGTVSGVT SFGAFVTLKN GVEGLVRLEH LGPYTYSEEA LALLGPKGAR IRLGDPMEVV
ILGANPRARQ IDLAPYREEK KTKEEKKMAR KVVGPPEGKE RQDRPEKVTV QRIYFGEWTG
KEPSGPPKKR RKRR
//
