ID Q8XJX8_CLOPE Unreviewed; 1084 AA.
AC Q8XJX8;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=SWI/SNF family helicase {ECO:0000313|EMBL:BAB81331.1};
GN OrderedLocusNames=CPE1625 {ECO:0000313|EMBL:BAB81331.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81331.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB81331.1, ECO:0000313|Proteomes:UP000000818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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DR EMBL; BA000016; BAB81331.1; -; Genomic_DNA.
DR RefSeq; WP_011010546.1; NC_003366.1.
DR AlphaFoldDB; Q8XJX8; -.
DR STRING; 195102.gene:10490889; -.
DR KEGG; cpe:CPE1625; -.
DR HOGENOM; CLU_000315_21_1_9; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18012; DEXQc_arch_SWI2_SNF2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR013663; Helicase_SWF/SNF/SWI_bac.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR10799:SF1020; BTAF (TBP-ASSOCIATED FACTOR) HOMOLOG; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF08455; SNF2_assoc; 1.
DR Pfam; PF04434; SWIM; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:BAB81331.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 59..105
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 632..789
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 909..1074
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1084 AA; 126647 MW; 20039B8C47709B89 CRC64;
MLVEDLLLQR FKEETTGRNY AKGQRIINND LVESVEIEDE EDLVAVNGIV ISEQLFSKYS
TKLEIDIRSR GILSTYCTCT DYEKHEFSKE NYCCKHLVAT FYKALGDLAK KKEFEEDKNL
FSKKKENKIL DLILQEETDK EELKIEVYIN KNEWSNSILA EFKIGTKSMS SNKLYILKDI
EQFLVAYYNR IPIKYSKVFT FDIREQKLST KDRELIEFIE SLKEIEKPIK SFLRNRDTFI
EGKSIKIPNY LVRDFFRVIK NHRIYLNEGF FYRAVESEVL FEDVPIDFSL KDSKNNFELS
SLNGMPKVLG DRADVFLYGT NIYIPKKDFC YKIKNYLDIF SEGKVIKIDK CEEERVFRKL
IPSLRDLTEN VVLSKNIMNK TVLEPVKFNF YFDKEGKEVT LTLKVKYGSY EFNIFDDCKE
KIIYRDIKKE KEVIALIERF SLEEINKKFY FYLGDEYIFR FFKYDVCKLQ EYGEVYYSEN
FKGIKSLGSK GIKGDIKPGR YNYFEFDFKI GDIPSEETRE ILRAFRENLK FFKLKSGEFL
DLEELELKQF LKLLDSVDNG DLEKNCLEIN NSRALYIANY IEEKGIRYIK GKKKLNELKS
KFKNINKLSF EVPKDLKANL REYQKFGYNW LKTLEHLGLG GILGDEMGLG KTLQAITFIL
SNKGKKTLVV APTSLIYNWK EEFNKFAPNL VVEVLNEGKD KREEALRDIE SKDVIITTYN
LLKRDLEEYK KINFDYCFID EAQAIKNPDS QNSEAVKEVN SEYKFALTGT PMENSLMELW
SIFDFVMPGY LYDRKRFTVR YYKKLNESEE VLSEIHSLIK PFILRRKKKD VIKELPDKIE
KMHLVDLGEE QKKVYSIYAN NALSIMEKKQ DAEEFNKSKI EILSYITKLR QLALDPSVTI
NDYMGESAKI EALVEILNQG VEEGHKILVF SQFTSVLKNI SSRLKEEKIS FSYLDGSVSS
KKRINMVNEF NEGENSVFLI SLKAGGTGLN LTSADIVIHF DPWWNPAVEN QATDRAHRMG
QKNVVEVIKL IAKGTIEEKV VALQEEKKEL ISKIIEEGEL GAGSTFNTLS EEELMDLFKV
DYLG
//
