ID A0A1W0BL09_9NOCA Unreviewed; 1148 AA.
AC A0A1W0BL09;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ribonuclease E {ECO:0000313|EMBL:ONM46543.1};
GN ORFNames=B0T46_22440 {ECO:0000313|EMBL:ONM46543.1};
OS Nocardia donostiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM46543.1, ECO:0000313|Proteomes:UP000188836};
RN [1] {ECO:0000313|EMBL:ONM46543.1, ECO:0000313|Proteomes:UP000188836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1655 {ECO:0000313|EMBL:ONM46543.1,
RC ECO:0000313|Proteomes:UP000188836};
RX PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA Potter G., Perez-Trallero E.;
RT "Nocardia donostiensis sp. nov., isolated from human respiratory
RT specimens.";
RL Antonie Van Leeuwenhoek 109:653-660(2016).
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:ONM46543.1}.
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DR EMBL; MUMY01000023; ONM46543.1; -; Genomic_DNA.
DR RefSeq; WP_077120654.1; NZ_MUMY01000023.1.
DR AlphaFoldDB; A0A1W0BL09; -.
DR STRING; 1538463.B0T36_03360; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000188836; 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; 1.10.10.2480; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR006847; IF2_N.
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; PF04760; IF2_N; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000188836};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 450..533
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 50..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 122097 MW; EE827E9F149518F8 CRC64;
MADQEPLDTT SQDADQLPER IRVHALAKRL GVTSKRILAK LAELGFQVRS PQSNVERAVA
ESVRDSLTTS DEAASPAAAA EPATTVPGVA ESAGEVAGAA AAADSVPQTP AEEPATGSGQ
TSGSRADTAA EHVPAFTGGL FASPIPEEPA AAEPVVFESA VVAAPLFLSP DAAAAEELRR
QRRAEREAAR VREAEAAEAE ADTESRGNGE TETDEQTIVE QQAESDDQPR RRRRGRRGRG
RGRGEQPTEA ETDSDTERSE VAESDQDEQA TEERGADKTD STTAAAAAVS SETEEPSGAT
ESAESGEDTE TPEGSSRRRR RRRRRKVVGE SGADNEPADD DPPNTVVHER EPRNKSRGRA
TVDEVQGISG STRLEAKRQR RRDGREAGRR RPPILTESEF LARREAVDRV MVVREKSFPG
HPTATQVAVL EDNILVEHFV TNTGSPSMVG NVYLGKVQNV LPSMEAAFVD IGRGRNGVLY
AGEVNWEAAG LGGKERKIEQ ALKPGDQVLV QVSKDPVGHK GARLTTQISL AGRFLVYVPG
GTSTGISRKL PDTERKRLKE ILREIVPADA GVIIRTASEG VSEAELTRDV ERLQTTWRTI
EEASTRDSGA PKTLYEEPDL LVKVIRDLFN EDFSKLVIEG ERSWSTVENY IRTVAPDLLS
RVSRHESGTG SHPGADVFET YRIDEQLAKA LDRKVWLPSG GTLVIDRTEA MTVIDVNTGK
FTGSGGGNLE ETVTRNNLEA AEEIVRQMRL RDIGGMIVVD FIDMVLESNR DLVLRRLTEA
LGRDRTRHQV SEVTSLGLVQ MTRKKLGTGL VEAFSTTCEH CHGRGILVHN YPVEPSAGED
GSGRGRETGS RRRRGRDKAA APVTPAAQPG ETPDEDAAVK RAHPVALAMA AHQAEETGAV
EQRPDSVEAA EPERVATEAI AVELSPEAAQ AVAEDTGRVA SSAVDSADAR PAETAAESTE
SGESGEFAEP AEQRPARARR RARSKPSTIG ATAARNGMAA EAASGGTATD TGAETPAAAK
ANGRAVVPEP APAPGRVTDE AVAATGQTEA AEPATTEQAQ SAAEESRSGM TEPVARQPRR
RRVARSAAAP AADSAGAVFV VGAEQPAAPA VDYTDYSTAA SAAAQLPARK TRRRAAGRPA
GPPVDADE
//
