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Database: UniProt
Entry: A0A0T2KUC3_9MICO
LinkDB: A0A0T2KUC3_9MICO
Original site: A0A0T2KUC3_9MICO 
ID   A0A0T2KUC3_9MICO        Unreviewed;       793 AA.
AC   A0A0T2KUC3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Ribonuclease G {ECO:0000313|EMBL:KRA23287.1};
GN   ORFNames=ASD65_01780 {ECO:0000313|EMBL:KRA23287.1};
OS   Microbacterium sp. Root61.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA23287.1, ECO:0000313|Proteomes:UP000051216};
RN   [1] {ECO:0000313|EMBL:KRA23287.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA23287.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA23287.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA23287.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRA23287.1}.
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DR   EMBL; LMGU01000001; KRA23287.1; -; Genomic_DNA.
DR   RefSeq; WP_056217603.1; NZ_LMGU01000001.1.
DR   AlphaFoldDB; A0A0T2KUC3; -.
DR   STRING; 1736570.ASD65_01780; -.
DR   Proteomes; UP000051216; Unassembled WGS sequence.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000051216};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          283..366
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   793 AA;  85999 MW;  B786312258D34551 CRC64;
     MADDTNHQSE FENTPEAPAD EAVTLDVPDS VADAVIEGGD AVVAEPEVAE IVAEAEAEVV
     AEVEVVAEIE ATAEVAAEAV AEVEAEVATE ADAEAVTETE VAPAVEEPVV EEKPLTAATL
     GLLPENFVSA VSTQLMFYAP EPPPVTERSG PLEIPSDEPA ASSTARRRNR RRGGAEDRDA
     ASDAPPVQQQ QPPRQRAVEL ITEPQRIKGS TRLEAKKQRR RDGREAGRRR TVVTEAEFLA
     RREAVDRVMI VRSKNGRIQI AVLEDKVLVE HYVARNQDAS LIGNVYVGRV QNVLPSMEAA
     FVDIGRGRNA VLYSGEVDWD AVETGNQPRR IELALKSGDR VLVQVTKDPV GHKGARLTSQ
     ISLPGRYLVY VPGGAMNGIS RKLPDTERAR LKRILKEVLP ESSGVIVRTA AEGATEDQLT
     RDVQRLTAQW EHISRQIESI QAPALLHSEP DLLVKIVRDV FNEDFTKMLI QGEDAQHTIA
     NYLASVAPDL LERVEKYEGE NDPFDEFRVT EQIEKALDRK VWLPSGGSLV IDRTEAMTVV
     DVNTGKFVGS GGNLEETVTK NNLEAAEEIV RQLRLRDIGG IIVVDFIDMV LESNRDLVLR
     RLVECLSRDR TKHQVAEVTS LGLVQMTRKK LGLGLLETFS EPCDVCAGRG VVVHHDPVVK
     HRSAAGGAPN GRRPRAGAPV ANGASTGTHV ITEGVKSALA QIAASTIHHE EHAVADAAPV
     ELVLEAPVER PKKARKKRAA PSQSAPKSEK EQLLDTVLNA LPEPKAPGQG RGRRRVSTAA
     LTGTPIAHTP AED
//
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