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Database: UniProt
Entry: A0A1Q2HYK3_9CORY
LinkDB: A0A1Q2HYK3_9CORY
Original site: A0A1Q2HYK3_9CORY 
ID   A0A1Q2HYK3_9CORY        Unreviewed;      1048 AA.
AC   A0A1Q2HYK3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Ribonuclease E {ECO:0000313|EMBL:AQQ15899.1};
DE            EC=3.1.26.12 {ECO:0000313|EMBL:AQQ15899.1};
GN   Name=rne {ECO:0000313|EMBL:AQQ15899.1};
GN   ORFNames=CGLAU_09740 {ECO:0000313|EMBL:AQQ15899.1};
OS   Corynebacterium glaucum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=187491 {ECO:0000313|EMBL:AQQ15899.1, ECO:0000313|Proteomes:UP000217209};
RN   [1] {ECO:0000313|EMBL:AQQ15899.1, ECO:0000313|Proteomes:UP000217209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 30827 {ECO:0000313|EMBL:AQQ15899.1,
RC   ECO:0000313|Proteomes:UP000217209};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP019688; AQQ15899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2HYK3; -.
DR   KEGG; cgv:CGLAU_09740; -.
DR   Proteomes; UP000217209; Chromosome.
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, ECO:0000313|EMBL:AQQ15899.1};
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:UP000217209};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          416..499
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          796..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          917..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..44
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..198
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..840
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..1005
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  114814 MW;  F8372338696787AE CRC64;
     MAHTQDSTEQ QQSDATKAPR KASRKAAKKT AKKTAKKASK KSVKKATKSS ALNESAATEN
     TAPNPYADFD RTQLSDKMRV FQFAKALDLT SKDLILALAD LGVVKVAQSS LTRAEMEQLL
     DALAAKGDSP EPEAAPAEEK IRERIRKDVA NEITQIERKV EAELTDREED RDEDDVTDAE
     DDALTDPEDV DDAFDLLTDI EPEVTPAPVE ENPAYAPIFK APTRSKRRRA SRPSDAEAAD
     AANASDGAAD ATDTADTADS AEVAGTANTV EAEAAAPAET RSRKRRRGSR KSSETKVDTS
     DENANILDVE DTDDFVGARD VADVEELEEP KAIKGSSRLE AQRRRRTEKR EEQRKRSRIV
     SQAEFLARRE SVTRTMVVRE RDRHDGPGRI TQVGVLEDGL LVEHFVTSDQ QASMIGNIYL
     GRVQNVLPSM EAAFIDIGQG RNGVLYAGEV DWKAAGLGGR SRRIEHALKS GDQVVVQVTK
     DPVGHKGARL TTQISLAGRF LVYVPGGRSA GISRKLPAPE RKRLKEVLNN VVPGKGGAII
     RTAAEGVPED AIAADVNRLH TQWEAIQEHA EREKNSKGAK PVTLYEEPNL LIKVVRDLFN
     EDFAALIVDG KKPWNTVKAY VESVAPDLAD RLEQFDRNDH GGKDAFEVYR VDEQIQKALS
     RSVWLPSGGS LIIDRTEAMT VIDVNTGKFT GSGGSLEETV TSNNLEAAEE IVRQIRLRDI
     GGIIIIDFID MILPENQDLV LRRLKEALGR DRTRHQVSEV TSLGLVQMTR KRLGTGLLET
     FSEPCETCGG RGIVLAEDPV DHDAHDDHPR RGKDRDRRRP VGEHPAAKAM RTHSEEELDE
     IAGSVIADQG DDAGNGAGGD GEERETKRSR RRGRRGGSRG RGKQREADST NVEATDAAED
     EVSSDAAYAV EAAVAAAQVD STEPVKAAES AAQTYEEAVE EFESSPRRKR RTRGNSKSDY
     RPKPEDFVQP AEVEVEESEA VEEGVDKQKP ATTRSGRDRR RASRRSTSTA SQPKKQEARE
     GRVKAASKDS ATQSRAGRGR RRASRKSS
//
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