ID A0A1H5BC79_9ACTN Unreviewed; 1351 AA.
AC A0A1H5BC79;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Ribonuclease E {ECO:0000313|EMBL:SED52025.1};
GN ORFNames=SAMN05216489_03666 {ECO:0000313|EMBL:SED52025.1};
OS Streptomyces sp. 3213.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855348 {ECO:0000313|EMBL:SED52025.1, ECO:0000313|Proteomes:UP000198754};
RN [1] {ECO:0000313|EMBL:SED52025.1, ECO:0000313|Proteomes:UP000198754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3213 {ECO:0000313|EMBL:SED52025.1,
RC ECO:0000313|Proteomes:UP000198754};
RA de Groot N.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; FNTK01000001; SED52025.1; -; Genomic_DNA.
DR STRING; 1855348.SAMN05216489_03666; -.
DR Proteomes; UP000198754; 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:UP000198754};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 645..722
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..508
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1351 AA; 143795 MW; BB45F81B8555D743 CRC64;
MLEPTEPIEG SEPNTPSDTL PPRRRRRAAS RPAGPPTAPE GAVESGTPAI PAEVSDEKKE
TDESVVEVTE VTPEAPVVVE AVEEAAPAGR TRRRATRRVS APAGAPEASA VPEAAEIVVP
AVAAAAPEET TVAEEAAPVV SDEDAAPRRT RRRATRKVTA PEAVVPETVV EQAEEPAAPA
AVEEAVAAEA PVEEAAPAGR TRRRATRRAS APAGTPQAAG AVENTEVAEA AEETEASAAP
AAAAATEVTE GAAPAASEED AAPRRSRRRA TRRVSAPAGT PVGEEAPVND ETAADAAEQN
TTADAPAEDS GPRRRRRVVR TAAGGFSAPA PKNGNAAEED EGPRRPARPA VAVFRAPVFT
EPMFQTPERA AAAAAEAVED DEEEVVVAEP VAVEVVEEET GGRRRRRRRG AAFEAEPVAA
AVVETAAVEE EPEEADEAAE DSADGDETEE TGSRRRRRRG GRRRRRGESA TGEDESEDGE
EYAAEQAAED AEDTAEQVEE DAEEADEDQG GSGSSSSRRR RRRRRRAGDS GGESESASSS
DDPERTVVKV REPRAKKDDH PSDEVQSIKG STRLEAKKQR RREGREQGRR RVPIITEAEF
LARREAVERV MVVRQTGERT QIGVLEDGVL VEHYVNKEQS TSYVGNVYLG KVQNVLPSME
AAFIDIGKGR NAVLYAGEVN FEALGMANGP RRIESALKSG QSVLVQVTKD PIGHKGARLT
SQVSLPGRYL VYVPEGSMTG ISRKLPDTER ARLKTILKKI VPEDAGVIVR TAAEGASEDE
LSRDVERLQA QWEDIQKKAK GGGGSNAPSL LYGEPDMTVR VVRDIFNEDF TKVIVSGDEA
WDTIHGYVSH VAPDLADRLS KWTSEVDVFA TYRIDEQLMK ALDRKVWLPS GGSLVIDKTE
AMIVIDVNTG KFTGQGGNLE ETVTRNNLEA AEEIVRQLRL RDLGGIVVID FIDMVLESNR
DLVLRRLLEC LGRDRTKHQV AEVTSLGLVQ MTRKRVGQGL LESFSETCVH CNGRGVIVHM
EQPTSVGGGG KRKRRGRGGD GQDAHDTHDG HETHEHDHDA DEVETEAEVA AEVAMPVPFA
ETEFRPDEDL YSSAAEAEAA ATRGRSRRRT SRRASAPAGA PRAESRESRQ PREVHEPREV
REEAEPVAVA QAEPVAVEDP VVEAPAVEAP AAVDDAAPKG RTRRRATRKA TAPAGSPAGS
EEAAVVTVTE AAAPVVVETP APAVQAEQPE APAESAAPAR PRRRAVRKAT APTASEEAAV
VVVPSTVGEA AATQAEADVE VPAKKTAARK AAKKAPAKKA VAKKAAATKT AAKKTAAKKT
TAKKAAKTTS KKTAAAEQTS PSSVTASTDE G
//
