ID I2JPT9_9GAMM Unreviewed; 911 AA.
AC I2JPT9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=DOK_00477 {ECO:0000313|EMBL:EIF44991.1};
OS gamma proteobacterium BDW918.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae.
OX NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF44991.1, ECO:0000313|Proteomes:UP000003473};
RN [1] {ECO:0000313|EMBL:EIF44991.1, ECO:0000313|Proteomes:UP000003473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDW918 {ECO:0000313|EMBL:EIF44991.1,
RC ECO:0000313|Proteomes:UP000003473};
RX PubMed=22740675; DOI=10.1128/JB.00678-12;
RA Kim S.M., Cho S.J., Lee S.B.;
RT "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL J. Bacteriol. 194:3753-3754(2012).
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}.
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:EIF44991.1}.
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DR EMBL; AJMK01000002; EIF44991.1; -; Genomic_DNA.
DR AlphaFoldDB; I2JPT9; -.
DR PATRIC; fig|1168065.3.peg.103; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_1_6; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000003473; 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; 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; 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; 2.
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:UP000003473};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 663..744
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 101009 MW; A09686DB41266C51 CRC64;
MAKRRNIPDP HAEREASNYE NPVPSREYIL EQLKESEKGI SQAQLRRQLE IEGEEQEEGL
RRRIKAMLRD GQIIEGRRGQ LRAISGGDSM VGKVIGHRDG FGFVSIDGES EDVYLANRQM
QQVFDGDTVK VEVTGVDQRG RREGVIVEVV EHNTQQLVGK LMMHRGLPQV VPENTRIQNW
LALEDNDVAT AKEGDYVMVE LTQQPGQRQQ ARGRITEVLG DRRTVGVATE LAIRSHDIPF
EWPEAVEEEA RRFGSEPAEA DKAHRVDLRQ LPLVTIDGED ARDFDDAVYC EPKKTGGYRL
WVAIADVSHY VQVGSALDQE AHKRATSVYF PDRVVPMLPE ALSNGLCSLK PDVDRLTMVC
EMTISASGKL SGYVFYEGLI RSHARLTYNE VGALLELEGV DPKHNTGRNA HLLPQLRYLH
DLYKVLRKAR SERGAIDFET VETRIVFDDE KRIEAIVPIR RHDAHKLIEE CMLCANVATA
RALDRSGLEA LYRVHSGPSE QKLTNLREFL GEIGLSLQGG EEPSPKDYQM LLSNLGERPD
AAVIQTMMLR SLSQAVYHPE NEGHFGLHYA GYTHFTSPIR RYPDLLVHRA LRYLVRSGGG
EAPACFHKVG DAPNIDRKKI YPYDLEALIA QGGNSSVAER RADEASRDVM AFLKCEFLQD
HVGSEHEGII TAVTGFGMFV ELQDLYIEGL VHITALPQDF YQFDQAHQRL IGERTRRVFQ
LGDALKVQVL AVNLDQRKID LGVLAGDDIG KKAAFDTAKP ASDGPKRQRR KPGQSRGRNT
EPKAAADSPR RRKPDASAPA AKSAPRKKRQ VVAPVVADVP VAVPKKTSVR EALAKGLKGL
MPTKAKASAK PKAAFKSVGA KAAEAKAAAE AKPKAQPRRS RSGAKSAAPS DTPKKSGGKP
KSGAPRTRRS R
//
