ID A0A101JQS8_9ACTN Unreviewed; 1383 AA.
AC A0A101JQS8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Ribonuclease E {ECO:0000313|EMBL:KUL31349.1};
GN ORFNames=ADL12_25385 {ECO:0000313|EMBL:KUL31349.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL31349.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-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:KUL31349.1}.
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DR EMBL; LLZG01000265; KUL31349.1; -; Genomic_DNA.
DR RefSeq; WP_062705493.1; NZ_LLZG01000265.1.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000053923; 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:UP000053923};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 677..754
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..481
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1359
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1383 AA; 145842 MW; F937BB5A4966E05A CRC64;
MLEPTEPTEG SELTTPSDTL PPRRRRRAAS RPAGPPSAAA EAQPAEAVEP AIPVAETADV
AALGDEAEKA EESIEAEAEV TPEAAAAEET EVSEEIEETV QAAPAGRTRR RAVRRASAPA
GAPAAVEAAE TVVPVAAAAS VAEESPAVAE APAAESAEVT EEAAPAARTR RRAVRRVSAP
AGAPEKAEDA ETVAETVVSA AESPAAAEVP AGAEAPAAET AEVSEETAPR RTRRRATRRV
SAPAGAPAAE AAVSADVSAE AEEPVEAAAP VAAADSDEAA EAAAPRRARR RATRRGSAPA
EASEAVVAEA PAETPVTAET PVTPGIEAET AAVTGVGAPA EAPEAEADEE VTPRRRRRAV
RRAAAGFAAP AQAPAAEAPE APRPARPAVA VFQAPVFTEP QFQTPQRAAA EAAAEAETED
VEEFPEEQAP ASRRRRRRRG GAFGEEVEAQ GVEAAAEDET EETEEAAEDV VESEEAEEAE
EFEETGSRRR RRRGGRRRRR GEAAEAEGGD GEELAAAQAA QDAEDTAEQE EEDAEDEGAE
EGAGSSASSR RRRRRRRRAG DSGVDAEPGE GDPERTVVKV REPRPLREKG AEPSDEVQSI
KGSTRLEAKK QRRREGREQG RRRVPIITEA EFLARREAVE RVMVVRQHGD RTQIGVLEDN
VLVEHYVNKE QSTSYVGNVY LGKVQNVLPS MEAAFIDIGK GRNAVLYAGE VNFEALGMAN
GPRRIESALK SGQSVLVQVT KDPIGHKGAR LTSQVSLPGR YLVYVPEGSM TGISRKLPDT
ERARLKTILK KIVPEDAGVI VRTAAEGASE DELRRDVERL QAQWEEIQKK AKNGNAPTLL
YGEPDMTVRV VRDIFNEDFS KVVVSGDEGW ETIHGYVSHV APDLADRLQK WTSEVDVFAT
YRIDEQLAKA LDRKVWLPSG GSLVIDRTEA MVVVDVNTGK FTGQGGNLEE TVTRNNLEAA
EEIVRQLRLR DLGGIIVIDF IDMVLESNRD LVLRRLLECL GRDRTKHQVA EVTSLGLVQM
TRKRVGQGLL ESFSETCVHC NGRGVIVHME QPTAVGGGGK RKKRARAGAG PEHVHEAAVA
LEPVETAEEE AETEIEVAAE IAEPAALPEP AFAPDEELYS SIAEAEAAAG RGGRSRRRGG
RRVSAPAGTP RKPEAVPTAQ DVTVAEEVAR PVQPEPAAEA KAEPVAVEDV VVEAPAAEAP
ATAPVAEEAA PKGRTRRRAT RKVSAPAGSP AGAEAAVVTV SEAASPAPEP EAEAPAAAPA
EQAEKAPAEA AAPTAAPARP RRRAVRKATA PTAPEETAVV VVPAAEAAEA PAAVEGVEET
APAKKTARKT AKKATAKKAA TKKTAAKKTV AKKTTAKKAA KTAKTAAAKS TAKKTTVSAA
TDE
//
