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Database: UniProt
Entry: A0PU18_MYCUA
LinkDB: A0PU18_MYCUA
Original site: A0PU18_MYCUA 
ID   A0PU18_MYCUA            Unreviewed;       988 AA.
AC   A0PU18;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Ribonuclease E Rne {ECO:0000313|EMBL:ABL05837.1};
GN   Name=rne {ECO:0000313|EMBL:ABL05837.1};
GN   OrderedLocusNames=MUL_3715 {ECO:0000313|EMBL:ABL05837.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL05837.1, ECO:0000313|Proteomes:UP000000765};
RN   [1] {ECO:0000313|EMBL:ABL05837.1, ECO:0000313|Proteomes:UP000000765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99 {ECO:0000313|EMBL:ABL05837.1,
RC   ECO:0000313|Proteomes:UP000000765};
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA   Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP000325; ABL05837.1; -; Genomic_DNA.
DR   RefSeq; WP_011741442.1; NC_008611.1.
DR   AlphaFoldDB; A0PU18; -.
DR   KEGG; mul:MUL_3715; -.
DR   eggNOG; COG1530; Bacteria.
DR   HOGENOM; CLU_003468_2_0_11; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd04453; S1_RNase_E; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR004659; RNase_E/G.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00757; RNaseEG; 1.
DR   PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR   PANTHER; PTHR30001:SF0; RIBONUCLEASE G; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          384..461
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..160
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..231
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..950
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   988 AA;  106966 MW;  86E6AC7E1C23861D CRC64;
     MVDGAPSSDP ENEPTQREDL PDRLRVHSLA RTLGTSSRRV LDALSALDGR IRSAHSSVDR
     VDAVRVRDLL AEQPAEEGQA EEDQQAPDAV AAEVPDAPGE PAEPESRLML ETQETVQVVE
     TWVERPHYMP LFVAPQPISE PVAGDDADDE SGDEGDDDEE QADRPGNRRR RRGRRGRGRG
     RGEQGANDGQ DQPGDDGDEA PQKAGGNSTS SDDSEAQDGA DSEESDNGDD DNGSADGASR
     RRRRRRRRKS GAGDDGDEGP APDDPPNTVV HERAPRSGDK SGNSDSGDDS GGNEIKGIDG
     STRLEAKRQR RRDGRDAGRR RPPVLSEAEF LARREAVERV MVVRDRVRTE PPHPGSRYTQ
     IAVLEDGIVV EHFVTSAASA SLVGNIYLGI VQNVLPSMEA AFVDIGRGRN GVLYAGEVNW
     DAAGLGGADR KIEQALKPGD YIVVQVSKDP VGHKGARLTT QVSLAGRYLV YVAGASSTGI
     SRKLPDTERQ RLKEILREVV PSDAGVIIRT ASEGVKEDDI RADVTRLQER WNQIEAKAVE
     IKQKAAGAAV ALYEEPDVLV KVIRDLFNED FAGLVVSGDD AWDTINEYVS SVAPDLVSKL
     SKYEPAVGSE GQVGPDVFAV HRIDEHLAKA MDRKVWLPSG GTLVIDRTEA MTVVDVNTGK
     FTGSGGNLEQ TVTKNNLEAA EEIVRQLRLR DIGGIVVIDF IDMVLESNRD LVLRRLTEAL
     ARDRTRHQVS EVTSLGLVQL TRKRLGTGLI EAFSTSCPHC SGRGILLHAD PVDSAPTTGR
     KADSGGRRNR RSKKNRAEEP SEKEAVAKVP TYAPGEHPMF KAMAASSSSE AEHGDGEVEE
     SGEELTAAVD DQTAVQVALD LGETEESEET DGTDETDDFD DDSDDSDDSD EDDDTDETND
     TDVDADEDED TDDDSDEDED TEDDDELDDD LDDELDDDDS DSDDEDSESE LTEPAAGRPA
     ALEVTTIAER PRRRRAAGRP AGPPIHLG
//
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