ID C0MCK7_STRS7 Unreviewed; 427 AA.
AC C0MCK7;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Putative DNA-binding protein {ECO:0000313|EMBL:CAW99836.1};
GN OrderedLocusNames=SZO_13050 {ECO:0000313|EMBL:CAW99836.1};
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368};
RN [1] {ECO:0000313|EMBL:CAW99836.1, ECO:0000313|Proteomes:UP000001368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70 {ECO:0000313|EMBL:CAW99836.1,
RC ECO:0000313|Proteomes:UP000001368};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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DR EMBL; FM204884; CAW99836.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MCK7; -.
DR KEGG; seq:SZO_13050; -.
DR PATRIC; fig|40041.11.peg.1381; -.
DR eggNOG; COG4109; Bacteria.
DR HOGENOM; CLU_054913_0_0_9; -.
DR Proteomes; UP000001368; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd04596; CBS_pair_DRTGG_assoc; 1.
DR CDD; cd03440; hot_dog; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR010766; DRTGG.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; NF038279; TF_CBS_SpxR; 1.
DR PANTHER; PTHR43080:SF31; CBS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43080; CBS DOMAIN-CONTAINING PROTEIN CBSX3, MITOCHONDRIAL; 1.
DR Pfam; PF03061; 4HBT; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF07085; DRTGG; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51371; CBS; 2.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW DNA-binding {ECO:0000313|EMBL:CAW99836.1}.
FT DOMAIN 194..252
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 255..313
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 427 AA; 48002 MW; 2A9C86F3BF13ADB9 CRC64;
MSKHQEILDY LERLAIGKRV SVRSISNHLK VSDGTAYRAI KEAENRGIVE TKPRSGTVRI
EKKGRVRIDR LTYAEIARIS DSEVLAGHAG LGHEFSKFSI GAMTQQNIHR YLIKGGLLIV
GDRENIQLLA LKNHNAILVT GGFPVSKQVI ETADSQGIPV MVTHYDTFTV ATMINHALSN
IRIKTDLKTV AQVLIPVEEY GCLYETDTVE EFNALIKKTG QVRFPIVDAL DQVVGVVSMR
DVVDQPAETR LEQVMSPNPI TAKPNASLAN ISQKMIFEDL NMLPVVDDHH FLLGIITRRQ
AMENLPNHQP GNLYTYSQQM LSSLEETLDY YQVMIEPTMI DSAGNLSNGV VAEFLKEISV
RVLTKKHQKN IIIEQMMIYF LHAVQIDDQL RIYPKIITEN RRSSTLDMEV MVDDQVIAKA
IITTKLN
//
