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Database: UniProt
Entry: T0HRD3_9SPHN
LinkDB: T0HRD3_9SPHN
Original site: T0HRD3_9SPHN 
ID   T0HRD3_9SPHN            Unreviewed;       754 AA.
AC   T0HRD3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=L284_03335 {ECO:0000313|EMBL:EQB18906.1};
OS   Novosphingobium lindaniclasticum LE124.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB18906.1, ECO:0000313|Proteomes:UP000015527};
RN   [1] {ECO:0000313|EMBL:EQB18906.1, ECO:0000313|Proteomes:UP000015527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LE124 {ECO:0000313|EMBL:EQB18906.1,
RC   ECO:0000313|Proteomes:UP000015527};
RX   PubMed=24029761;
RA   Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT   "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT   a Hexachlorocyclohexane Dumpsite.";
RL   Genome Announc. 1:e00715-13(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|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:EQB18906.1}.
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DR   EMBL; ATHL01000028; EQB18906.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0HRD3; -.
DR   PATRIC; fig|1096930.3.peg.660; -.
DR   eggNOG; COG0557; Bacteria.
DR   Proteomes; UP000015527; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000015527};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          633..714
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          716..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  83768 MW;  4818933BA694F51B CRC64;
     MAETMPSKNR PAHGLPSRKQ ILDLIQNSAE PIGKREIARE FGLKGHEKIE LKALLKDMAE
     EGLIDGKRTA FHRMGGLPKV TVLRVVEVDE GEPVAIPDTW TPDDATPPPR IRLIEKGRSA
     LRKGDRVLAR TEETVTGWRA YPMKKLMLRS EQMLGVVEID GAGKPWLAPV DKRIRNSSPI
     SDLGGAEKGE LVLAEPIGRS ARPSVKVTEV LGEPLAPKAF SLIAIHKHGI PNHFDDETIS
     EAERAAKMPL SHDKREDLRH LPIVAIDPSD ARDHDDAIWA KPNEEGGFDA LVAIADVSFY
     VRPGGHIDRE ARRRGNSVYF PDRVVPMLPE VLSADVCSLR SGEDRAAMAC HLKIDGQGKV
     TEWRFTRALV RIDEVIAYEE AQARIDEGRA QQHLQDLWAC WKLLAKARAD RDPLELELPE
     RRVKLDEQGR ITEIAIRERL DAHRVVEDFM ISANVAAAKA LEAKVAPVVY RVHETPSREK
     LTSLKDYLAT FGRKLSLGQV ITPGLFNRML KDIADESEKA LIMEAVLRSQ TQAYYGPRNE
     GHFGLALGSY AHFTSPIRRY ADLLVHRALV DAYGLEQPKP ESDIPAASGL SDRDRDDLGR
     VSEAISNYER RAMEAERETI DRYVAAWLSG RVGQVFDTRI TGVQKFGFFA TIIGLGGDGL
     VPVSTLGDER FAYDEKAQVL EGESTGTTFG MGQILRLRLA EANPLTGALK FELEEGGGRI
     EQRGKPAPLK KKGKHFVSPR GRPGNIRHQG RKKK
//
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