ID Q12RX3_SHEDO Unreviewed; 817 AA.
AC Q12RX3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=Sden_0511 {ECO:0000313|EMBL:ABE53803.1};
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE53803.1, ECO:0000313|Proteomes:UP000001982};
RN [1] {ECO:0000313|EMBL:ABE53803.1, ECO:0000313|Proteomes:UP000001982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC {ECO:0000313|Proteomes:UP000001982};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) 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}.
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DR EMBL; CP000302; ABE53803.1; -; Genomic_DNA.
DR RefSeq; WP_011494969.1; NC_007954.1.
DR AlphaFoldDB; Q12RX3; -.
DR STRING; 318161.Sden_0511; -.
DR KEGG; sdn:Sden_0511; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000001982; Chromosome.
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; 3.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000001982};
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 730..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 91826 MW; A5AD81BFD3F6F3BF CRC64;
MINDPHFERE QDKYDNPIPS REFILEYLRA QKSPITRDNI AKALNIHDEE PLEALRRRLR
AMERDGQLVF TRGQSYGLPE RMDLLSGTVL GHRDGFGFFK PDEGGDDLFI NNRDMLMYFH
GDKVLAQKAG TDRRGRREAR IVRLVQPRTA ALVGRYHVDA GMGFVIADDR RITQEILIAS
EDTHGARAGD VVVVELTRRP GRFVKAAAKV TEVLGKTLAP GMEIEIALRN YDLPHTWSAV
IEKKLKRIPD EVTEEDKLDR VDLRHLPLVT IDGEDARDFD DAVYAEKKPS GGWRLWVAIA
DVSHYVRTDS ALDEEARARG NSVYFPSQVI PMLPEKISNG LCSLMPHVDR LCMVAEMTIA
ASGKLSGTKF YPAVMHSHAR FTYTQVADML EGGAIAPEHA ALFPHLQCLQ SLYLTLDERR
AERGAIAFET LETQFIFNEQ RKIEKIVPRG RNQAHKIIEE CMILANVASA NFVKKHKGEV
LYRVHEAPSE QKLANFKEFL AERGISMDGG LEPTPSDYQN LMLKIADRPD AELIQVMLLR
SMRQAVYSPD NEGHFGLALE AYSHFTSPIR RYPDLVLHRV IKYLLAKEAG ETKDKWTQNG
GYHYLTEELD ALGEECSTTE RRADEATRDV SDWLKCEYMQ DHVGDSFEAV IASVTNFGLF
VRLNELFIDG LVHISSLASD YYQFDGTRQR LIGENTRKIY QVGDAVSVKV AAVNLDDRQI
DLVMIGDNVK GRAKSGASGS RKPLTARERT NLEGAKTDKK SSTKAAAKSD AKPRRKRKPA
KSAAESGSKS TQKKPATKKP AANKSAPKKT VKKKPKQ
//
