ID C0MCS9_STRS7 Unreviewed; 364 AA.
AC C0MCS9;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Putative RNA helicase {ECO:0000313|EMBL:CAW99874.1};
GN OrderedLocusNames=SZO_13270 {ECO:0000313|EMBL:CAW99874.1};
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:CAW99874.1, ECO:0000313|Proteomes:UP000001368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70 {ECO:0000313|EMBL:CAW99874.1,
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; CAW99874.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MCS9; -.
DR KEGG; seq:SZO_13270; -.
DR PATRIC; fig|40041.11.peg.1407; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_1_3_9; -.
DR Proteomes; UP000001368; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:CAW99874.1};
KW Hydrolase {ECO:0000313|EMBL:CAW99874.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 29..198
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 218..363
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 364 AA; 41153 MW; 15FC7DC7A3E36339 CRC64;
MITNLPTQWQ EKLAKLGFTN LTPIQEQVFQ PIVDGKSLLG ISPTGTGKTL AYLWPSLLRL
SPKKAQQLLI LAPNTELAGQ LFEVTKEWAE PLGLTAQLFI SGSSQKRQIE RLKKGPEIII
GTPGRIFELV KLKKIKMMAI NTIILDEYDD LLSDSQYQFV QKLSHHAPRD HQMIYMSATN
KVDQDSLADH TLVIDLSKQA LPCIEHCYML VNKRHRTDIL RKLANIPDFR GLVFFNSLSD
LGATEERLQY SGASVASLAS DVNVKQRKAI LEAFKEQSIS LLLATDIVAR GIDIDQLEYV
INAEVPRNKE QYTHRAGRTG RMGRSGIVIT LVSHPEDIKR LKKFAKVTEI YLKHQQLYQK
EIRG
//
