ID R8X7C0_9ENTR Unreviewed; 820 AA.
AC R8X7C0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=WC7_00197 {ECO:0000313|EMBL:EOQ51232.1};
OS Citrobacter sp. KTE151.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=1169322 {ECO:0000313|EMBL:EOQ51232.1, ECO:0000313|Proteomes:UP000014006};
RN [1] {ECO:0000313|EMBL:EOQ51232.1, ECO:0000313|Proteomes:UP000014006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTE151 {ECO:0000313|EMBL:EOQ51232.1,
RC ECO:0000313|Proteomes:UP000014006};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Escherichia coli KTE151.";
RL Submitted (FEB-2013) 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 -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-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:EOQ51232.1}.
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DR EMBL; ASQK01000001; EOQ51232.1; -; Genomic_DNA.
DR RefSeq; WP_016151418.1; NZ_KB976059.1.
DR AlphaFoldDB; R8X7C0; -.
DR GeneID; 66271715; -.
DR PATRIC; fig|1169322.3.peg.200; -.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000014006; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 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 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 644..725
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 726..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 93014 MW; 76DB9D595058A7EA CRC64;
MSQDPFQERE AEKYANPIPS REFILEHLTK REKPANRDEL AAELNIEGEE QQEALRRRLR
AMERDGQLVF TRRQCYALPE RLDLLKGTVI GHRDGYGFLR VEGRKDDLYL SSEQMKTCIH
GDQVLAQPLG ADRKGRREAR IVRVLVPKTS QIVGRYFTDA GVGFVVPDDS RLSFDILIPP
EEVMGARMGF VVVVELTQRP TRRTKAVGKI VEVLGDNMGT SMAVDMALRT HEIPYIWPQA
VEKQVAGLKE EVPEEAKAGR VDLRSLPLVT IDGEDARDFD DAVYCEKKRG GGWRLWVAIA
DVSYYVRPPT PLDQEARSRG TSVYFPSQVV PMLPEVLSNG LCSLNPQVDR LCMVCEMTIS
SKGRLTGFKF YEAVMSSHAR LTYTKVWHML QGDQELREQY APLVKHIEEL HNLYKVLDKA
REERGGISFE SEEAKFIFNA ERRIERIEQT QRNDAHKLIE ECMIMANISA ARFVEKAKEP
ALFRIHDKPT TEAINSFRSV LAELGLELPG GNKPEPRDYA ELLESIADRP DAEMLQTMLL
RSMKQAIYDP ENRGHFGLAL QSYAHFTSPI RRYPDLSLHR AIKYLLAQEQ GHKGNTTETG
GYHYSMEEML QLGQHCSMAE RRADEATRDV SDWLKCDFML DQVGNVFKGV IASVTGFGFF
VRLDELFIDG LVHVSSLDND YYRFDQVGQR LTGESSGQMY RLGDRVEVRV EAVNMDERKI
DFSLISSERA PRNEGKTARE KAKKGDAGKN TGKRRQMGKK VNFEPDSAFR GEKKGRAKPQ
ADKKTAEKKG DKKAKKPSAK TLKIAAATKA KRATKKKVAQ
//
