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Database: UniProt
Entry: A0A0Q9M1N4_9MICO
LinkDB: A0A0Q9M1N4_9MICO
Original site: A0A0Q9M1N4_9MICO 
ID   A0A0Q9M1N4_9MICO        Unreviewed;      1000 AA.
AC   A0A0Q9M1N4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Ribonuclease {ECO:0000313|EMBL:KRE55711.1};
GN   ORFNames=ASG70_07775 {ECO:0000313|EMBL:KRE55711.1};
OS   Phycicoccus sp. Soil748.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE55711.1, ECO:0000313|Proteomes:UP000051855};
RN   [1] {ECO:0000313|Proteomes:UP000051855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE55711.1, ECO:0000313|Proteomes:UP000051855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil748 {ECO:0000313|EMBL:KRE55711.1,
RC   ECO:0000313|Proteomes:UP000051855};
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:KRE55711.1}.
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DR   EMBL; LMSC01000007; KRE55711.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9M1N4; -.
DR   STRING; 1736397.ASG70_07775; -.
DR   Proteomes; UP000051855; 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   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          414..498
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..287
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1000 AA;  104664 MW;  6C71EC3FE926772F CRC64;
     MTDATADHEA TDLPAVAADA APAKKTARKA AAKKTAKKAP AKRATKKADP KADGEPLVEG
     APVVEGAAVI DEGALVDPAP LDVPVPAGVA ADADPETDAD ADDEAEEEAR AAAEAAAQEA
     TATVPSFGLL FQPPDPAKAA PRRRRASAAA GAPAPAPAPA EVPAVEAPAA DGAPADGRGA
     SADEETQAER PSRGRARGRG RGRGAKNAED KGSEETTSDE AVAAPSGDDG QTDGQDSTSD
     DESTSEGGRR RRRRGGKGRG RGRGQGDAES ADSTAEGDED EQHGPEGEDE QSGEAEGSST
     RRRRRRRRSG SSGEGDDPPG TVTKVREARR ERDEPQSVKG STRLEAKKQR RREGREAGRR
     RTIITEAEFL ARRESVERVM VVREREGRTQ IGVLEDDVLV EHYVSRETNA SMAGNIYLGR
     VQNVLPSMEA AFVDIGKGRN AVLYAGEVNW DAAGLDNNQP KRIENALKSG DSVLVQVTKD
     PIGHKGARLT SQISLPGRYL VYVPEGSMTG ISRKLPDTER ARLKGILKEV VPDRAGVIVR
     TAAEGASEEE LRADVERLTR TWEKIQAKAD SKSGGKGKGG APVLVHGEPD LTVRVIRDVF
     NEDFTSLVVA GDQAYGEVSD YLGDVAPDLA ERLHKWTSEE DLFTHYRVDE QIAKAMDRKV
     WLPSGGSLVI DRTEAMTVVD VNTGKFVGSG GNLEETVTKN NIEAAEEIVR QLRLRDIGGI
     IVIDFIDMVL ESNRDLVVRR LLECLGRDRT KHQVAEVTSL GLVQMTRKRV GSGLIEIFSE
     NCEHCGGRGI IVHADPVDKP SGGDSGSGGG QSQRGGGNDG GNTGGTGGGS TRGRRGGRSG
     GAQEQAPAQP AAQAAPVHGG PTPAQIAAAA HAAALKSAGE HHDEDALLAV PGQDEPVVEV
     REAAGQDAPV ALPAVEPLEL PEGPAAEVRP VADEPAAEVH PVGDEPAAPA EPEQPVAAAA
     AEAPAAPKRR KRGRVVAPAG PPRPVGEDAA EPSVVAVPTS
//
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