ID A0A1L7CNF8_CORFL Unreviewed; 1291 AA.
AC A0A1L7CNF8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN ORFNames=CFLV_09265 {ECO:0000313|EMBL:APT87358.1};
OS Corynebacterium flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=28028 {ECO:0000313|EMBL:APT87358.1, ECO:0000313|Proteomes:UP000185479};
RN [1] {ECO:0000313|EMBL:APT87358.1, ECO:0000313|Proteomes:UP000185479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OJ8 {ECO:0000313|EMBL:APT87358.1,
RC ECO:0000313|Proteomes:UP000185479};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium flavescens OJ8(T)(=DSM
RT 20296(T)), isolated from cheese.";
RL Submitted (AUG-2014) 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; CP009246; APT87358.1; -; Genomic_DNA.
DR STRING; 28028.CFLV_09265; -.
DR KEGG; cfc:CFLV_09265; -.
DR Proteomes; UP000185479; 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};
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:UP000185479};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 499..582
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 80..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 141131 MW; 690CFB87F7703E9C CRC64;
MQNASENTGS HAAAVAFAQH IDREALPAKT RLYTLAKQLG IASREIVTEF GKLGVKKAAQ
SSVSKQEVVL LLDSLVASAP AEDKQAQQER PEKKSKKPAT KPRRKATTKA ATKAAEKPKK
ATKKSKAVDP ELAPSVEETP AAVQDNADEA ADVAGAAGGE AGKPAKKTTR KAGRKATRKA
VRKSSSPKKD KEAVAEVKPG EDEKAEHSEN LAPLAANADV SAKSAGEEDE QEAKLRTRVR
KNVENEIAQI EEKVDSQLAD TVENPEHSGA NSEGSAESSQ DAAQSAETVA DAQAAEDVVA
QLQEALEEAG EQSHDFDDLG EDYRPIITPK PGADSQTYEL APVFMPPHVQ PASASVPEFT
GEDDSEEEEA KGSRRRGRRG TSRGRGSQEH AAKATSDAAA EGDEVEEDLI EEPKAIKGST
RIEAQRRRRA ELREKGRERQ HIVSQAEFLA RRESVERTMV VRDKQRKDGA GVVTQVGVLE
DDLLVEHFVT SESQTSLIGN IYLGRVQNVL PSMEAAFVDI GQGRNGVLYA GEVDWRSTKL
GGRARRIENA LKSGDQVLVQ VAKDPIGHKG ARLTTQISLA GRYLVYVPGG RSAGISRKLP
APERKRLKSI LENVIPGRGG AIIRTAAENV PEDAIAADVR RLNNTWQDIT ERANEEKSSK
GAKPVTLYEE PDVLVKVVRD LFNEDFHQLV VDGTRSYNVV RAYVDSMAPD LADRVVQYRA
AEHGGMDAFE TYRIDEQLHK ALSRKVWLPS GGTLIIDRTE AMTVIDVNTG KFTGSGGNLE
ETVTRNNLEA AEEIVRQMRL RDIGGMIVVD FIDMVLPENQ DLVLRRLKET LERDRTRHQV
SEVTSLGLVQ MTRKRLGTGL IETFATECEH CHGRGLIIHE YPVDEIAEEE HNDHASRHPK
KAHQHKSEKK LEGEDTQQRN SRQRHSIEDL VANVIVDDEE DSDASHAEGD KNAGDGQRSK
RRAQRSRRGR RGHDELHHDE PRHHESRHEG SEHTSAAEDI ASIGYAAAES AAAQDEVAEF
NSYVADEPPV ESVVERTVEH SGESKEDSKE LNSARRSRRT SRRGVRSAQR AASTQEPAKA
TELEVETRAE AQGTSRMTFA QAQAEFEASP RRKRATRGNS RSDHAPRPED YVDSAVGSTS
AVSGETASED PAVSAQAAQA AQPAQAEPAA AQPARTRGHR RAVRNTSKRA SHKQAAAATV
KAQPKKKHAS PVETSPEQAP SAEPGVETKV IRRGRKRAVR KVTAVRQAPR RAEKKEQATV
KESAAESWEE SAAPNRGNGR GRRRLARRRS K
//
