ID A0A7X0V9V7_9ACTN Unreviewed; 1150 AA.
AC A0A7X0V9V7;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Ribonuclease E {ECO:0000256|ARBA:ARBA00072999};
DE EC=3.1.26.12 {ECO:0000256|ARBA:ARBA00066879};
GN ORFNames=H5V45_05120 {ECO:0000313|EMBL:MBB6626700.1};
OS Nocardioides luti.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2761101 {ECO:0000313|EMBL:MBB6626700.1, ECO:0000313|Proteomes:UP000523955};
RN [1] {ECO:0000313|EMBL:MBB6626700.1, ECO:0000313|Proteomes:UP000523955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIGAM211 {ECO:0000313|EMBL:MBB6626700.1,
RC ECO:0000313|Proteomes:UP000523955};
RA Seo M.-J.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U-
CC rich regions.; EC=3.1.26.12;
CC Evidence={ECO:0000256|ARBA:ARBA00050524};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the RNase E/G family.
CC {ECO:0000256|ARBA:ARBA00005522}.
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:MBB6626700.1}.
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DR EMBL; JACKXE010000001; MBB6626700.1; -; Genomic_DNA.
DR RefSeq; WP_185251944.1; NZ_JACKXE010000001.1.
DR AlphaFoldDB; A0A7X0V9V7; -.
DR Proteomes; UP000523955; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008995; F:ribonuclease E activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:TreeGrafter.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd04453; S1_RNase_E; 1.
DR FunFam; 2.40.50.140:FF:000066; Ribonuclease 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Reference proteome {ECO:0000313|Proteomes:UP000523955};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 470..554
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..59
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..89
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..101
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..114
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..189
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..243
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..291
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..349
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1019
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1041
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1070
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1114
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1150
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 121008 MW; 2CF20112070579EB CRC64;
MLDDNPVDES TPTTDSPDTA PVTSEAPPAK KAAAKKTAAK KAPAKKAAAK KAPAKKAAAK
KAAVADEPLP EVDAPAAEAP AADAAPVTKA VKRAPAKRTT TRKTAAAKAE APAEQTDTTG
QPTSVEVAPD AVAAQVPAAA TGEAAGAPSV LFQAPEVTTR PARRTRKKAA APVEAPADAT
ADETAAAEAA SDETPAEAPA EETKAPARKR SQPRKRAAAK PVEDEEETPA EAAATDDAPQ
ADAASDDTDD ADGTADDSAD DAEGDNDNES DDNEGGTGRR RRRRGGRRRR KSGDGDTNDD
DNRQDGRQGN GGGRQDAKQS GQDGKQDAKQ GGNRGAEDKD ADGDSDEPGG EGSSRRRRRR
RRTGDDDGGS DDPENTTTRV RRPRNAEDEI TAISGSTRLE AKKQRRRDGR EAGRRRAPIV
SEAEFLARRE AVERVMVIRQ REDLTQIAVL EDKVLVEHYV ARESQTSIIG NVYLGRVQNV
LPSMEAAFID IGKGRNAVLY AGEVNWSALG HKDGAPRKIE SVLTSGQPIL VQVTKDPIGH
KGARLTSQVS LAGRFLVYVP DGTTSGISRK LPDTERQRLK TLLKEIVPDT AGVIVRTAAE
GASEDELTRD VERLKARWED IEGKVKGSAP QLLYGEPDLT LKVVRDLFTE DFAKLVIEGE
DAWDTVQSYV QHVAPDLEER LERYDRGANN GKDSFGAFRI DEQIAKGLDR KVWLPSGGSL
IIDRTEAMTV VDVNTGKFTG SGGNLEETVT KNNLEAAEEM VRQLRLRDIG GIIVIDFIDM
VLESNRDLVL RRLVECLGRD RTRHQVAEVT SLGLVQMTRK RIGTGLVESF SENCSHCQGR
GVVIQDTPVD PGRSGDDDGG RRSGGGRRSR GGRGGDDQGN QGGQQDQGSS DKGDHRSDSG
RGDNGNRGGR DGGRDGGRDG GRGRGRGGDQ ERGSQERADS PADKGAVPSP SYVASVAKPE
NADKARPVDE APADSTPVAP PSEAPETLTE APAAAAPVRQ EAAPAAEPSP EAGSASEPPK
VVTRSRRRSA SRPTTTTTSP AEPMTVSVPV AEPAPVAPEP VAPATAPEPP KVITRTRGRS
ASRPAGPPAS TPEASASTGA ATSAATTGTV GAPPVSGTVE PGTAVHEPGD NGEGHPVGHV
PIKKKGSRKR
//
