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Database: UniProt
Entry: A0A1A0EW41_9GAMM
LinkDB: A0A1A0EW41_9GAMM
Original site: A0A1A0EW41_9GAMM 
ID   A0A1A0EW41_9GAMM        Unreviewed;       810 AA.
AC   A0A1A0EW41;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-JUL-2019, entry version 21.
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=ADS46_07165 {ECO:0000313|EMBL:OAZ91608.1};
OS   Halomonas sp. G11.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1684425 {ECO:0000313|EMBL:OAZ91608.1, ECO:0000313|Proteomes:UP000092250};
RN   [1] {ECO:0000313|EMBL:OAZ91608.1, ECO:0000313|Proteomes:UP000092250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G11 {ECO:0000313|EMBL:OAZ91608.1,
RC   ECO:0000313|Proteomes:UP000092250};
RA   Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M.,
RA   Ghedira K., Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA   Eddine Masmoudi A.S., Cherif A.;
RT   "Genomic basis for crude oil degradation, heavy metal resistance and
RT   high salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated
RT   from Tunisian Chott El-Djerid salt lake.";
RL   Submitted (FEB-2016) 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
CC         yield nucleoside 5'-phosphates.; EC=3.1.13.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01895,
CC         ECO:0000256|SAAS:SAAS01124678};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
CC       ECO:0000256|SAAS:SAAS00089931}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAZ91608.1}.
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DR   EMBL; LYXG01000041; OAZ91608.1; -; Genomic_DNA.
DR   RefSeq; WP_066321713.1; NZ_LYXG01000041.1.
DR   EnsemblBacteria; OAZ91608; OAZ91608; ADS46_07165.
DR   Proteomes; UP000092250; 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   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; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
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; 2.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02063; RNase_R; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000092250};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462075};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00089915};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00446781};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092250};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      663    744       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      741    810       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1A0EW41}.
FT   COMPBIAS    741    794       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1A0EW41}.
FT   COMPBIAS    795    810       Basic. {ECO:0000256|MobiDB-lite:
FT                                A0A1A0EW41}.
SQ   SEQUENCE   810 AA;  91863 MW;  0BCE1F3B7E2AB65D CRC64;
     MKYWTLNDDP HAEREAHKYD NPAPSREYLL AALEQHGKPV THEDMSQLLG LEDEDHHEAV
     RRRLAAMERD GQVLRDRRGA YALINKLDLI KGKVLGHRDG FGFLLRDDGK KPDLVLPPRQ
     MRRVFHGDHV LVRISGRDRR GRDEATIADV ISRNTQTIVG VYRSNTPEFG ILIPENPRIT
     QEVIIPHSAC NGAKDGQVIS AKIVKQPETR VQPVGEVIEV LGERMDPGME IDIAIRSYEI
     PAEFPPEVLD QTSGISAEVL EDDKQHRVDL RDTPLVTIDD ESAKDFDDAV CAWKTKSGSW
     KLLVAIADVS HYVRPGTPLD DEARKRGNSV YFPGQVVPML PELLSNGLCS LNPHVDRLVM
     VCEMNISKTG AISRYRFYEA VMNSHARLTY NKVAAMLEED NEEGKALREE HAGLVKPLEN
     LHELYTLLRQ AREERGAIDF DTTETAIIFN DERKIEKIVP RSRNDAHKMI EECMLAANVA
     TARFLDKHDL PALYRIHERP TPERLDKLRL FLNELGLSLG GGDMPTPQDY QALRETITDR
     SDFDIIQTVM LRSMNQAVYS PQNEGHFGLA YQAYAHFTSP IRRYPDLLVH RAIRSVIRGP
     RQTNTVLRVE GAPVEPPSKW CPYTFEQMLE LGEHCSMTER RADDATRDVE SWLKCEFMSD
     KLGETFDGTI ASVTQFGLFV RLDAFYVEGL VHVTSLPSDY YHYEAEKHRL KGERTGTTYR
     LGDGLSVQVA RVDMDDRKID FALADEKPRP RRQPRKKPST EGAKTSGKGD KERSGKDKPG
     QDKSGKDKPD TRRGPRRTRK GPRKPSPNKG
//
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