ID A0A0G3UI92_9ACTN Unreviewed; 1334 AA.
AC A0A0G3UI92;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Ribonuclease E {ECO:0000313|EMBL:AKL66127.1};
GN ORFNames=M444_12715 {ECO:0000313|EMBL:AKL66127.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL66127.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL66127.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL66127.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP011664; AKL66127.1; -; Genomic_DNA.
DR RefSeq; WP_037797589.1; NZ_CP011664.1.
DR KEGG; strm:M444_12715; -.
DR PATRIC; fig|465541.12.peg.2772; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000035653; 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; 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:UP000035653};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 627..704
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..493
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1314
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1334 AA; 139380 MW; 3713EE638187D71C CRC64;
MLNNENTTPA AGNADGDSPS DNLPPRRRRR AASRPAGPPG ATAAAATASD EAAPAAAAAA
APVVEEPAAA PAPRARRRAT RAVAAPETAA ADVVVEAAPA AAAAAAPVVE EPAAAPAPRA
RRRATRAVAA PEAPAADVVE AAPAAEEPAA AAPAPRARRR ATRAVAAPET AAADVVGQAA
PAAAAAAPVV EEPAAAPAPR ARRRATRAVA APETAAADVV VEAAPAAAAA PVVEEPAAAP
APRARRRATR AVAAPAAEAA AETPAVVEEP AAAKATVTVA DAVDSPKRGG RRRATRSAAP
AAPVQQAPAP AAEAEAPSGP ARGRRAARPA VAVFQAPVFA EPMFQTPETA AMAAAAAAAA
TRAEEAEEEE EEAEVEAEAV QAPAAQPAGR RRRRGRGAAA EPAAPAAESG PLTVADVEQA
EIEEPEAEAA DLDEDETDGE RPSRRRRRGG RRRRRGESAD LDDSAEEEGE TEAAEQEADG
DEDSAEDDDE DNGASGSSSS RRRRRRRRRS GDSAADAEAG EEDGVRTVVK VREPRPAREK
AEPSDEVQSI KGSTRLEAKK QRRREGREQG RRRVPIITEA EFLARREAVE RVMVVRQAGE
RTQIGVLEDN VLVEHYVNKE EATSYVGNVY LGKVQNVLPS MEAAFIDIGK GRNAVLYAGE
VNFEALGMAN GPRRIESALK SGQSVLVQVT KDPIGHKGAR LTSQVSLPGR YLVYVPEGSM
TGISRKLPDT ERARLKTILK KIVPEDAGVI VRTAAEGASE DELRRDVERL QAQWEDIQKK
SKQISTSSPS LLYGEPDMTV RVVRDIFNED FSKVIVSGDG AWETIHGYVN HVAPDLADRL
SRWTSEVDVF ATYRIDEQLA KALDRKVWLP SGGSLVIDKT EAMIVIDVNT GKFTGQGGNL
EETVTRNNLE AAEEIVRQLR LRDLGGIVVI DFIDMVLESN RDLVLRRMLE CLGRDRTKHQ
VAEVTSLGLV QMTRKRVGQG LLESFSETCV HCNGRGVIVH METPTVVGGG GNGKRAKRRG
GKSESDQHEH EHVTGTVEAD SFEAETEAEV AAEAAAPVAL PEPEFVADEE LYSNPAEAEA
AVSGRRNRRR ATRKATAAAG APRTAAAPAP AVEAEPVTAP ADTVLEPAAE AVTEAAPAPE
AVAEAVADEA APKGRTRRRA TRKATAPAPV AEAEPVVVAE PEPEPVVEPE PEPVVVETPA
EPVADAAPAR PRRRATRKAT APAGSPAGAA EAAVVVVEAA PVAEPEPVAA EPAAEAEAEP
EAAPVKKAAR KAPAKKATTT AKKAPAKKAA AAKTTAKKTV AKKTTVKKTA AKRTTKKTAA
AEQTAPSVSA PTED
//