ID B1VGM2_CORU7 Unreviewed; 1190 AA.
AC B1VGM2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=Ribonuclease E {ECO:0000313|EMBL:CAQ05329.1};
GN OrderedLocusNames=cu1369 {ECO:0000313|EMBL:CAQ05329.1};
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ05329.1, ECO:0000313|Proteomes:UP000001727};
RN [1] {ECO:0000313|EMBL:CAQ05329.1, ECO:0000313|Proteomes:UP000001727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its complete
RT genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AM942444; CAQ05329.1; -; Genomic_DNA.
DR RefSeq; WP_012360617.1; NC_010545.1.
DR AlphaFoldDB; B1VGM2; -.
DR STRING; 504474.cu1369; -.
DR GeneID; 60604149; -.
DR KEGG; cur:cu1369; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_2_1_11; -.
DR OMA; NWHSPHL; -.
DR Proteomes; UP000001727; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001727};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 421..498
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 72..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..129
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 131900 MW; FDD688883ED05A22 CRC64;
MAFTPEPALI ESAGKINTES FGRRVRVHSV AKELGITSKE FIAVLGEFGI AGKVPSSTLS
NEEATDVVSR LAAGGGVTQS EQPAAKREAD AAEPAADKVE AKKRTAKKAG AKKSAAKKAT
PKKTTAKKST KKTAAKEAAP TQETPEQDTS PEAAEQQEEQ KKAEPKKGAR KSTQKSAEKS
AQQAEKKGAA KKSSTKRAAT KKAEAKKAEV DNAQPRQAAA EQPAQAESPA GTTPESQTST
DEATPQPTRR RVRRIVRRVG SRAIQQDSAA AKTELSDEGS KKQEPSKNSE AKKAEPKKKE
QKAQQPNPEP QGATEEAITA DQLHPGEREE ADIVDEPVRL KGSTRLESKR RWREENRERG
RHKAISRSEF LARRESVHRQ MMVRDAERHD HTGLTTQVGV VEDGQLVEHF VTSDTQQSMV
GNIYLGRVQN VLASMEAAFI DIGTGRNAVL YASEVNWHSP HLHSKSRRID QALRSGDQVM
VQVIKDPVGH KGARLTNRIS FAGRYLVYFP GGTTAGISRK LPEAERKRLK EILQRVVPGQ
GGAIIRTAAE NVAEELIEED VNRLHKQWLN IEKTEAKERK SKGAKPVTLY EEPNMLITVI
RDLFNEDFSE LLVEGDKSWR MVRDYMGRMA PELMDRVHKW HPEQHADEDV FAAHRLDDQL
AKALCRKVWL PSGGHLVIDH TEAMTVIDVN TGSFVGSGGN LEETVTENNL EAAEEIVRQM
RLRDIGGMIV VDFIDMVLEE NQDLVLRRLI EYLGRDRTHH KVSEVTSLGL VQITRKRLGA
GLLETFSTTC ECCDGRGVIV HPDPVEQDFS EEPERRRRSS RGNGRGRDER GSKEQRNGQG
TEQRQGGRGD QGSKNHGRDE QRDQRGKNAT RHEDKGSKSK VANGKGREDA QDHRNSEGQE
RRSGKQRQDS QAGSESAADL GGEQKQETRT SRRGGRRSVQ RRTSSSVKDA TARTEQGSAE
KKQSADRSDE ASQSGQERAP RRVVRRIVRR TAPSQQRGGA AQRRSAANAD APELKISSRE
DRGSDQRGEQ QKSESGSRGA RRRGRRVVRS RPAVRQSDTR QAGGDTLRGE ESSGQQRSGQ
KQGSAGDRRS SATRRSGTRG AGKYGATTYE EAVKEFENSP RRRRRTRGNS VSDRRPQPED
FGAQPEANQA KEEPKRESRN AGKTEQPAQS ESRGRTRDRR RRVVRSNPRR
//