ID A0A841DTK1_9ACTN Unreviewed; 1270 AA.
AC A0A841DTK1;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Ribonuclease E {ECO:0000256|ARBA:ARBA00072999};
DE EC=3.1.26.12 {ECO:0000256|ARBA:ARBA00066879};
GN ORFNames=HDA44_002978 {ECO:0000313|EMBL:MBB5979637.1};
OS Kribbella solani.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=236067 {ECO:0000313|EMBL:MBB5979637.1, ECO:0000313|Proteomes:UP000558997};
RN [1] {ECO:0000313|EMBL:MBB5979637.1, ECO:0000313|Proteomes:UP000558997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17294 {ECO:0000313|EMBL:MBB5979637.1,
RC ECO:0000313|Proteomes:UP000558997};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
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:MBB5979637.1}.
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DR EMBL; JACHNF010000001; MBB5979637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A841DTK1; -.
DR Proteomes; UP000558997; 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, ECO:0000313|EMBL:MBB5979637.1};
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:UP000558997};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 728..811
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..103
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..114
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..188
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..228
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..248
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..315
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..450
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..526
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..550
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..617
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1125
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1177
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1247
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 132440 MW; AE83AD292F813458 CRC64;
MLDNEPTTDA AETTATDQPA PSARRGAKKA PAAKKTTTTR KRTVKKTAEP GPAAEATQAA
EAVPTQADDR SADPAPVKKA AAKTAAKAAA KKAPAAKKTA AKAPAKKATK RVAKKVAAQD
TLPDVTAEAA STVDAGPVVE TPAKKTTRKR TTKKAASTAD AASADPASAD AASAGSSSAA
GRSTGSASAD RDLVTTDSPV TDGPGASADT SGTREVTAPR KRTTRRRTTP TDTPAAETTA
DSGVAADGAA GGSGSSSGGA SVEETGARRT RRRAAAPAAV LFQAPTQDNP AQQAPAQAAT
PLEAAAAAEP GADEQPTTRR RTRRGASADA EDTGSTTSTR RARRGSGADG AQSVAGQDAA
TDGSHGSSTN RSRGSSTDGS HASATDGSHG ASTDGSHGAS AGDSRTGDSG SGEVDGDGGT
RTRTRRTRRG APSADAAQAA DGSQAGVADG TQAASGDAEE SGSTRTRTRR SRRGAETSVV
DAEADAPAEA DAQVDGPADG HGDDGEEGGE GTRRRRRRRG GRRRRKGGDA DGADDSTDEH
SDDDQDDDTD RDGAGRGAKQ DGGRDGRDGA KDGARDGGKD GAKQDGSDSD SADDEHDSDD
DEGGSGSSRR RRRRRRRKGE DSGSSPDDPD ETVVRVREPR SKNTANEITA VEGSTRLEAK
KQRRREGRAA GRRRAPIVTE AEFLARRESV ERTMVIRSRE DLTQIAVSED NVLVEHYVTT
AEQTSLIGNV YLGRVQNVLP SMEAAFIDIG KGRNAVLYAG EVDWATLGGA NGPRKIEQVL
KSGQSVLVQV TKDPIGHKGA RLTNQISLPG RYVVYVPRGG NGGISRKLPD TERNRLKTIL
KDIVPDEAGV IVRTAAEGAS EEELTADVSR LQAAWEDIEK KSKNGQAPQL LYGEPDLLIR
VVRDLFTEDF AKLVISGDQA YDQVREYVAG VAPHLVDRVE KAHNDVFANY RIDEQIKKAL
DRKVWLPSGG SLIIDRTEAM TVVDVNTGKF TGSGGNLEET VTKNNLEAAE EIVRQLRLRD
IGGIIVIDFI DMVLESNRDL VLRRLVECLG RDRTKHQVAE VTSLGLVQMT RKRIGTGLLE
AFSENCDHCG GRGLILHDEP KESRRRDSRN NGAAANGGNG NGNGQEHGKA AQPEESGRKS
SRRRRGKNRG EDEPAAEAEA PQHNGDAAQR LAQIAAASVK KDDEPGTPSS ADADTPEPTG
YPIAGTEAHV SPEATGFPAA DSTESADAAQ NGAGKSTRRR RSSRSRSKAT TDGDGAGGST
DAAELVSTHG
//
