GenomeNet

Database: UniProt
Entry: A0A2N7QM66_9GAMM
LinkDB: A0A2N7QM66_9GAMM
Original site: A0A2N7QM66_9GAMM 
ID   A0A2N7QM66_9GAMM        Unreviewed;       880 AA.
AC   A0A2N7QM66;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 36.
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   ECO:0000313|EMBL:PMQ02715.1};
GN   ORFNames=DyAD56_22830 {ECO:0000313|EMBL:PMQ02715.1};
OS   Dyella sp. AD56.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1528744 {ECO:0000313|EMBL:PMQ02715.1, ECO:0000313|Proteomes:UP000235676};
RN   [1] {ECO:0000313|EMBL:PMQ02715.1, ECO:0000313|Proteomes:UP000235676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD56 {ECO:0000313|EMBL:PMQ02715.1,
RC   ECO:0000313|Proteomes:UP000235676};
RA   Schulz-Bohm K., Janssens T.K., De Jager V., Gawehns F., De Boer W.,
RA   Garbeva P.;
RT   "Bacterial performance in fungal presence.";
RL   Submitted (AUG-2017) 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|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:PMQ02715.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NRDP01000039; PMQ02715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N7QM66; -.
DR   Proteomes; UP000235676; 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   Reference proteome {ECO:0000313|Proteomes:UP000235676};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          680..761
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..871
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   880 AA;  97729 MW;  0BB368C7F3147E77 CRC64;
     MTKKKEPRSS KQDAKRGPKP PKSGGARPKR SALDPSRQRA DVGVVDDPHA EREAQRYDRP
     IPSREAILAL LEQRGELLTE ARIAEAMSLH DEYDLNALRK RLGAMVRDGQ LLLGRRAGYA
     PANKLDLIQG VVLANAEGYG FLRPDGGGDD LYLSPQQMRT VLHGDRVLAS VVGIDRRGRK
     QGAIVEVLQR RSPRLVGRVV IENGVTLVAP DDRRVHQDVM IVPGQDMGAR SGQIVVAEIT
     DPPTPHRGPM GAIRAVLGER LQPSLLVEMA IASHDLPHDW PAEVTRDAAQ VEPQVTAAER
     EGRVDLRSLP LVTIDGADAR DFDDAVYAEP KRGGGYRLVV AIADVSHYVK LGSALDKEAY
     ERSTSTYFPG FVVPMLPETL SNGICSLNPK VERLCMVCDM VVNAEGEVTK SKFYNAVMRS
     HARLTYDRVW QAIGLNDADA RHELADVLPQ VEHLHGLYKL MAEQRKRRGA IDFETPEVKF
     RLDQRGEVET MGATERNDAH KLIEECMIAA NVQAALFLEK KKIPALFRAH EPPPAEKYED
     LQQFLREFKL RMPPVEDMTP ADYADILRLV RDRPERELIQ SVLLRSQSMA AYQPDNRGHF
     GLALEAYAHF TSPIRRYPDL LVHRAIRYAV ADGKPAAYQY SASEMAAMAV HCSQRERRAE
     EAERDVDERF KCAWMSKHVG SEFDGTVTGV TSFGLFVELD DSKVSGLVHI SQLSNDYYHF
     DPVRHLLKGE RSGVQFRLGD HVRIQVLRAS LEDRKIDFRL VSPRKEGFTP PHSERRYDYA
     ATGERYSLPK GKGNKGSGKG AERPATRDNA GPAISLPPLP PVGRKATTHD KPMVASPFSK
     AKAAAKGALA KVKSVASGKK KAPDKADAHV KKVKKNKGKR
//
DBGET integrated database retrieval system