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Database: UniProt
Entry: A0A1I0IXP0_9BACT
LinkDB: A0A1I0IXP0_9BACT
Original site: A0A1I0IXP0_9BACT 
ID   A0A1I0IXP0_9BACT        Unreviewed;       883 AA.
AC   A0A1I0IXP0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 16.
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=SAMN04487998_3522 {ECO:0000313|EMBL:SEU02181.1};
OS   Hymenobacter actinosclerus.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=82805 {ECO:0000313|EMBL:SEU02181.1, ECO:0000313|Proteomes:UP000198697};
RN   [1] {ECO:0000313|EMBL:SEU02181.1, ECO:0000313|Proteomes:UP000198697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15310 {ECO:0000313|EMBL:SEU02181.1,
RC   ECO:0000313|Proteomes:UP000198697};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOHS01000006; SEU02181.1; -; Genomic_DNA.
DR   Proteomes; UP000198697; 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; 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; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF17876; CSD2; 1.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198697};
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:SAAS00089892};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198697};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      732    813       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION        1     28       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I0IXP0}.
FT   REGION      102    152       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I0IXP0}.
FT   REGION      162    181       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I0IXP0}.
FT   REGION      817    883       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I0IXP0}.
FT   COILED       72     92       {ECO:0000256|SAM:Coils}.
FT   COILED      483    503       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    817    834       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1I0IXP0}.
FT   COMPBIAS    854    870       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1I0IXP0}.
SQ   SEQUENCE   883 AA;  99233 MW;  8BCAB69859335086 CRC64;
     MKQPSTKAPR APRAKAAPAE PTAPAAPTAA ISQDQIMRIF RDNPGKVLTY RQLSRRLGVT
     TKDQREVVFA HLRELRQQNQ LLLIQNDEYR LTDEAQAALA AAPKGRRKAG VSVKQDEESE
     AAEPTTEPGE LPAGKRLPRG GRVAESEFGQ NPVVHRRREA GFDFADADEP QSPRRRRESG
     GDTIVGTVAL ATEKYAFVIS EETEKDVRVF TDRLRFAMQG DTVRVRLRDS RDGRPVGDVV
     EVLDRKRPEV VGRLQIRDHV AFVKADNRKL YFDVYVSHDD LNGAQNGDKV LVHVTEFPED
     GSDRSPAGVI VRSFGQAGGN EAEINAIMAE FGLPFEFPAE VEADAEGMPD TIPAEEIARR
     RDFRDVTTFT IDPADAKDFD DALSIQQLEN GRWEIGVHIA DVTHYVRLDT ALENEARTRA
     TSVYLVDRVI PMLPEHLSNG LCSLRPNEDK LTFSAVFELD ENGKLYSTWL GKTVIHSDRR
     FAYEDAQERI EGLESDYTQE VQLMNRIAKK LCAARFKQGA ISFETQEVKF RLDENGKPLG
     VYVKERKDAH KMIEEFMLLA NRKVAEFVFK LKKTKPRLTM VYRVHDSPDP ERLQNFALFA
     KKFGYQLDLK SPQNLSTELN DLSQEVVGRP EQNVLQTLAI RTMAKATYTT DPRGHFGLAF
     EHYSHFTSPI RRYPDMMAHR LLEHYLEGGK NVEVEPIEEE CKHSSEREKL AASAERASIK
     FKQVEFLQDH IGEQFTGVVS GLTEWGMYVE IAENKCEGMI RISDIPGDYF ELDKDNYRLV
     GQRTKRIIQF GDELEVEVKA VNLLDRTIDF ALVDDRPDAV KQREQQERRE NGGSSRPPRG
     SSRGGKSGGN GGGRADGKNS SNSAGGRSDG KSSKGGSGGK RRR
//
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