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Database: UniProt
Entry: A0A109LSJ3_9SPHN
LinkDB: A0A109LSJ3_9SPHN
Original site: A0A109LSJ3_9SPHN 
ID   A0A109LSJ3_9SPHN        Unreviewed;       770 AA.
AC   A0A109LSJ3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-JUN-2019, entry version 20.
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=AUC45_02225 {ECO:0000313|EMBL:KWV92980.1};
OS   Erythrobacter sp. YT30.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=1735012 {ECO:0000313|EMBL:KWV92980.1, ECO:0000313|Proteomes:UP000055668};
RN   [1] {ECO:0000313|EMBL:KWV92980.1, ECO:0000313|Proteomes:UP000055668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YT30 {ECO:0000313|EMBL:KWV92980.1,
RC   ECO:0000313|Proteomes:UP000055668};
RA   Lin W., Zheng Q.;
RT   "Draft genome sequence of Erythrobacter sp. YT30.";
RL   Submitted (OCT-2015) 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:KWV92980.1}.
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DR   EMBL; LMAF01000001; KWV92980.1; -; Genomic_DNA.
DR   RefSeq; WP_067597533.1; NZ_LMAF01000001.1.
DR   EnsemblBacteria; KWV92980; KWV92980; AUC45_02225.
DR   Proteomes; UP000055668; 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; 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; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 2.
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:UP000055668};
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:UP000055668};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      634    715       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      721    770       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A109LSJ3}.
FT   COILED      599    619       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    721    735       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A109LSJ3}.
FT   COMPBIAS    749    770       Basic. {ECO:0000256|MobiDB-lite:
FT                                A0A109LSJ3}.
SQ   SEQUENCE   770 AA;  84806 MW;  ECE19D3DC04EB3D5 CRC64;
     MKKKKHIQGL PTRQQVLEFI QTSDSAAGKR EIAKAFGLKG QEKIALKRLL KDMAEEGLID
     GRKSAYHRMG GIPKVTVLRV VEIEDGEPVA QPDNWDPEAP GKPPRLTIKE AKDRGAKRTP
     ALKVGDRVLA RTEETDGNWS AYPIKKLPAR TEGLLGVVEI DASNKAWLAP VDKRVRQSAR
     ISDLGEAEEG QLVLAERAGR SERSGVNVIE VIGDPLAPKS FSLIAIAKHG IPHVFPEKVI
     EEAGQAAELT LSEEKREDLR HLPIVAIDPA DARDHDDAIW AEPDGEGGFN ALVAIADVSF
     YVRPGSALDK EARKRGNSVY FPDRVVPMLP ELLSADMCSL REDETRAAMA CHLKISGEGK
     VTHFRFTRAL VRIHHNIAYE DAQAAIDKGD APVHLQHLWE AWAALAHARA KREPLDLDLP
     ERRVQLDDEG RIAEIAVRER LDAHRVVEDF MIAANVAAAK ALEAKSSPVV YRVHETPARE
     KLIALRDYLA TMDKKLALGQ VVTPSLFNRM LKDVTDESEK AQVMEAVLRS QMQAYYGPAN
     SGHFGLALGS YAHFTSPIRR YADLLVHRAL VDAYKLEQPE PSNGMPPKTG LSDKDRASLQ
     EISDAISQTE RRAMEAERDT TDRYVAAWLS NRVGEVFDTR ITGVQGFGFF ATIDGLGGDG
     LVPISTLGRE YFRHDEAAQA LIGEDTGTRY AAGDRLKLKL AEANALTGAL KFVLEDADAQ
     TIEPRGKRPE RASRGGSKPN GRGGPRKAGK YAIGKRGRPK NIRHQGRKRK
//
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