ID A0A0G3XFU8_9SPHN Unreviewed; 765 AA.
AC A0A0G3XFU8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=AB433_08600 {ECO:0000313|EMBL:AKM10022.1}, GGR19_002530
GN {ECO:0000313|EMBL:MBB3991095.1};
OS Croceicoccus naphthovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM10022.1, ECO:0000313|Proteomes:UP000035287};
RN [1] {ECO:0000313|EMBL:AKM10022.1, ECO:0000313|Proteomes:UP000035287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PQ-2 {ECO:0000313|EMBL:AKM10022.1,
RC ECO:0000313|Proteomes:UP000035287};
RA Zeng Y., Huang Y.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3991095.1, ECO:0000313|Proteomes:UP000536420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102796 {ECO:0000313|EMBL:MBB3991095.1,
RC ECO:0000313|Proteomes:UP000536420};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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}.
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DR EMBL; CP011770; AKM10022.1; -; Genomic_DNA.
DR EMBL; JACIEL010000015; MBB3991095.1; -; Genomic_DNA.
DR RefSeq; WP_047820702.1; NZ_JACIEL010000015.1.
DR AlphaFoldDB; A0A0G3XFU8; -.
DR STRING; 1348774.AB433_08600; -.
DR KEGG; cna:AB433_08600; -.
DR PATRIC; fig|1348774.3.peg.1802; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000035287; Chromosome.
DR Proteomes; UP000536420; 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 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:UP000035287};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 641..722
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 718..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 84153 MW; 1F7921FE3C2B7FAF CRC64;
MARTPKRPTG LPNKEQVMEF IRSSDTPAGK REIAKAFGLK GQEKIALKAL LKDMADEGLI
DGDRRAFHRM GGVPKVTVLR VVAIEEGDAI AIPDNWQPDD AMPPPRIRLI ESKGRGKSRQ
MPALRKGDRV LARTEETGTG YLAHPMKKLP QVHDSLMGVV EIDGSGKGWL APIDKSVRSS
VPIADLGGAE KGNLVLAEPA GKSPRAGVRV VELLGDPLAP KSYSLIAIHK HDIPYVFPAE
ALSEADIAAK LPLSEDKRED LRALPIVGID PADARDHDDA IWAMPDDDPA NAGGWKALVA
IADVSFYVRP GSAVDREARK RGNSVYFPDR VVPMLPEVLS AEVCSLGEGE ARAAMACHMT
IDRDGRVRDW RFTRAIVQIA EVIAYEDAQA RIDDGSAADH LKHLWACWKV LHGAREARDP
LDLDLPERRV VLDEKGRIAE IAVRERLDAH KVVEEFMIAA NVAAAKALEA KAAPVVYRVH
EPPSREKLVA LKDYLATMDR NLALGQVITP SLFNRLIKDV SDEAEKALVM EQVLRSQTQA
YYGPKNAGHF GLALGSYAHF TSPIRRYSDL LVHRALVEAY GLEQPKPKDA TIPAHSGLSD
RDRASLERVT DAISKTERRA MEAERDTIDR YVAAWLSGKV GETFDTRVTG VQKFGLFATI
LGFGGDGLVP VSVLGDERFH YDDRAQVLRG ERTGTEYRSG DRMKLRLAEA NPLTGALKFE
PPEFEGRIEP RGGRPQGKPK RQNKTGYMQG KRGRPGNIRH SGKRK
//
