ID A0A2A3H5Z6_9ACTN Unreviewed; 1349 AA.
AC A0A2A3H5Z6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Ribonuclease E/G {ECO:0000313|EMBL:PBC63854.1};
GN ORFNames=BKI49_12000 {ECO:0000313|EMBL:PBC63854.1};
OS Streptomyces sp. Tue6028.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2036037 {ECO:0000313|EMBL:PBC63854.1, ECO:0000313|Proteomes:UP000217789};
RN [1] {ECO:0000313|EMBL:PBC63854.1, ECO:0000313|Proteomes:UP000217789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tue6028 {ECO:0000313|EMBL:PBC63854.1,
RC ECO:0000313|Proteomes:UP000217789};
RA Greule A., Flemming S., Bechthold A.;
RT "The Draft Genome Sequence of Streptomyces sp. Tue6028 - Producer of
RT Polyketomycin and Foxicin.";
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};
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:PBC63854.1}.
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DR EMBL; MLCE01000013; PBC63854.1; -; Genomic_DNA.
DR Proteomes; UP000217789; 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:UP000217789};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 616..693
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..480
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1319
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1349 AA; 142900 MW; 313E483F59651F06 CRC64;
MLEPTEPAEP STGSENNDTP SDTLPPRRRR RAASRPAGPP AAATEAAAET TAPAIPAVAS
ADELAEEETA EAVETEQAVA EEIPAATEAA ETETPSAEDT APRRTRRRAT RRASAPAGAP
ASVETAEAAE AAETVVPAAE AVTAEAEPVA EAPAPAAEEA APAGRTRRRA TRRASAPTGA
PKETEAVVIA EAEETPEAVE PAETAAAQVT APAEPVAETE EAAPRRTTRR RATRRVSAPA
ATPEGGAVEE RAETPEPVAE TAPATAAEVT DGEAAQAEDG GPRRTRRRAT RKAAGGFSAP
AAKEEETDEG GRRPARPAVA VFQAPVFTEP MFQTPERAAA AAAAEAAEAA EEAAEEEAAG
TEVAEVAEAA EESTGGRRRR RRRAVEDEPV TVPAAVDEAE EEPEEGAESA EDVVEGDEGE
EESAGSRRRR RRGGRRRRRG ESAEADGESA DDEFAAEQAA QDAEDTAEQV EEDAEEADER
EEAGGSGSSS SRRRRRRRRR AGDSGGEAEA GENDPERTVV KVREPRKKDE HPVDEVQSIK
GSTRLEAKKQ RRREGREQGR RRVPIITEAE FLARREAVER VMVVRQSGER TQIGVLEDNV
LVEHYVNKEQ STSYVGNVYL GKVQNVLPSM EAAFIDIGKG RNAVLYAGEV NFEALGLANG
PRRIETALKS GQSVLVQVTK DPIGHKGARL TSQVSLPGRY LVYVPEGSMT GISRKLPDTE
RARLKTILKK IVPEDAGVIV RTAAEGASED ELRRDVERLQ AQWEDIQKKA KSGNAPTLLY
GEPDMTVRVV RDIFNEDFSK VIVSGDEAWE TIHGYVSHVA PDLADRLSKW TSEVDVFATY
RIDEQLMKAL DRKVWLPSGG SLVIDKTEAM VVVDVNTGKF TGQGGNLEET VTRNNLEAAE
EIVRQLRLRD LGGIVVIDFI DMVLESNRDL VLRRLLECLG RDRTKHQVAE VTSLGLVQMT
RKRVGQGLLE SFSETCVHCN GRGVIVHMEQ PSSAGGGGKR KKRGRGGAEQ PHEHEHEAVA
AETTEAAETV EAETEAEVAA EAAVPAALLA PEFAPDEELY SSAAEAEAAA GRGRSRRRAT
RRASAPAGAP RAEGRPSKRA ERAERAAKSR EAAESEPVAV EDPVVEAPQE LVAEAPAVTE
APVVTEAAVV ESVEDEAAPK GRTRRRATRK VSAPAGSPKA SEEAVVTVTE PVAAPVAEPE
AAAEPQPEPV AETAAEAPAE SAAPARPRRR AVRKATAPTA SQEAAVVVVP SAAAPAEETA
DAAEAVVAET EADEAEAPAA AKKAAARKTA KKATAKKAAT KKTAAKKTAA KKATAKKATA
KKAATKATSK KTAAAEQTLS AVTASTDEG
//
