ID A0A1H1KQI0_9ACTO Unreviewed; 957 AA.
AC A0A1H1KQI0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Ribonuclease E {ECO:0000313|EMBL:SDR64563.1};
GN ORFNames=SAMN04489715_0195 {ECO:0000313|EMBL:SDR64563.1};
OS Schaalia meyeri.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=52773 {ECO:0000313|EMBL:SDR64563.1, ECO:0000313|Proteomes:UP000181914};
RN [1] {ECO:0000313|Proteomes:UP000181914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20733 {ECO:0000313|Proteomes:UP000181914};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; FNLK01000005; SDR64563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1KQI0; -.
DR STRING; 52773.ADJ76_02285; -.
DR Proteomes; UP000181914; 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 293..376
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 85..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 103765 MW; 5D590E062A155921 CRC64;
MDVAGVPPWR ESGDDVFNCR RPLRICAPLG FRPSRAMMTG ASGHVARAHH WRIVTTESAN
PVAPAASLLF QAPVFQAVPE VSTSAAAEEI EPKRRRHSSA SAEANAPREE TAPKRRRRSK
KSADDADSPD SAAPSSADAG GDEATEQKSR RRRRSKKADE ASAPAADSSD QSDTSSSGSD
SSDGEESSTR RRRRRARSSA ASASADEGAA ADQVQALKGS TRLEAKKMRR REGRREGRRR
HSISESEFLA RRESVERTMV IRDQDGLDQI AILEDGLLVE HYVARRTQSS MVGNIYLGRV
QNVLPSMEAA FVDVGRGRNA VLYAGEVNWD AVGMEGKPRR IESALKSGDP VLVQVTKDPI
GHKGARLTSQ ITLAGRYLVL IPGGSMMGIS RKLPDKERAR LKKILKAVVP SGSGVIVRTA
AEGATEGQIR DDVARLTRQW EEIDKKRSAT KAAPVLLRGE PELAVRVVRD IFNEDFTKLV
IEGRDTYATV KDYVDELSPE LSDRVEQWVG THDVFRAHRI DEQLAKGMDR KVWLPSGGTL
IIDRTEAMTV IDVNTGKFIG AGGTLEETVT RNNLEAAEEI VRQLRLRDIG GIVIIDFVDM
VLESNRDLVL RRLVECLGRD RTRHQVTEIT SLGLVQMTRK RVGEGLVEAF SSPCEACEGR
GFIVHRHPVE TTGGESSSKA SKSSKKQQKK AEPRRVDDSV EHERAKEALS AIAAASSRKE
EGASDAESTP TKKRRPKGSA AKTQESAAAP AKEPSTTPRG ATETPAAATD EEASTKRPRR
RRRAAETTPV PELPVHIELP NPVEHAGDPA VPTKDTADIR LPDHQEKAAT TRRRVARKAV
AASSAEPASA SAPQASRARV ADAEPNIPED GAKAGAFATP DVQPRRTHKR RAAVSTGVVE
PEASPAPVVV DLPARAEESA PVTPTRSTED ITLPEASGQP RTKRRRRAVS TGIVDAG
//