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Database: UniProt
Entry: A0A1J5LAM3_9BACT
LinkDB: A0A1J5LAM3_9BACT
Original site: A0A1J5LAM3_9BACT 
ID   A0A1J5LAM3_9BACT        Unreviewed;       730 AA.
AC   A0A1J5LAM3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-MAY-2019, entry version 12.
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=BM564_02395 {ECO:0000313|EMBL:OIQ31082.1};
OS   Bacteroidetes bacterium MedPE-SWsnd-G2.
OC   Bacteria; Bacteroidetes.
OX   NCBI_TaxID=1860095 {ECO:0000313|EMBL:OIQ31082.1, ECO:0000313|Proteomes:UP000183188};
RN   [1] {ECO:0000313|EMBL:OIQ31082.1, ECO:0000313|Proteomes:UP000183188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MedPE-SWsnd-G2 {ECO:0000313|EMBL:OIQ31082.1};
RX   PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA   Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT   "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT   Associated Bacteria from the Mediterranean Sea.";
RL   Front. Microbiol. 7:996-996(2016).
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:OIQ31082.1}.
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DR   EMBL; MPDE01000001; OIQ31082.1; -; Genomic_DNA.
DR   Proteomes; UP000183188; 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; 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; SM00357; CSP; 2.
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:UP000183188};
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   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      645    726       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED       49     69       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   730 AA;  83753 MW;  D9B56C7EA16C6437 CRC64;
     MTRKKKRKSS KSISNLSNTI LSILKKDRNK TFNYKQIAAI IGTTDASSRN QIIKKLQQLK
     ANKEIEEVDR GKFKALITTD YHTGILDLSG KGSGFIISDE FEDDVYIASN NINKALNGDE
     VEFYVYKRKK RGRMEGEITF IIRRDRSEYV GVIQIHEKKN FAFVVADSNK MYKDIFVPIN
     KINKAEDGDK VLVRLEDWPE KADSPYGKVL KVLGKPGEHN TEIHSILAEY GLPYEFPYDV
     ENFANEIDTS ITPEEISKRR DMRDVLTFTI DPKDAKDFDD ALSFQVLDNG NYEIGIHIAD
     VSHYLQEGTV LDDEAYERAT SVYLVDRVVP MLPEILSNGA CSLRPHEEKY TFSAVFEMND
     KTEIKNQWFG RTVTYSDARF AYEEAQSIIE TKSAVIPEEV SLTGKSYEAD SKIKEAVLKM
     DDLAKLMRSK RMSTGAISFD KVEVKFNLDE TNNPVGVFFK TSKDANKLIE EFMLLANKKV
     AEFIGKQEPK KTFIYRVHDE PDDSKLAALQ GIVAKFGYKL NFQDRKTVSQ SLNNLLKEVN
     GKKEQNLVDT LAIRSMSKAE YTTNNIGHYG LAFDYYSHFT SPIRRYPDVM AHRLLQHYLD
     GGKSVNEEIF EERCKHSSNM EYLATKAERD SIKYMQIKFM QDHRDEAFVG VISGVTDWGI
     YVEIISNKCE GMVRIRDIKD DYYEFDETQY ALVGRETKNI YQLGEQVVVK VKETDLAKKH
     LDFSLLGKPE
//
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