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Database: UniProt
Entry: A0A1M6LN59_9CLOT
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Original site: A0A1M6LN59_9CLOT 
ID   A0A1M6LN59_9CLOT        Unreviewed;      1077 AA.
AC   A0A1M6LN59;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Superfamily II DNA or RNA helicase, SNF2 family {ECO:0000313|EMBL:SHJ72552.1};
GN   ORFNames=SAMN02745163_02435 {ECO:0000313|EMBL:SHJ72552.1};
OS   Clostridium cavendishii DSM 21758.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121302 {ECO:0000313|EMBL:SHJ72552.1, ECO:0000313|Proteomes:UP000184310};
RN   [1] {ECO:0000313|EMBL:SHJ72552.1, ECO:0000313|Proteomes:UP000184310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21758 {ECO:0000313|EMBL:SHJ72552.1,
RC   ECO:0000313|Proteomes:UP000184310};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQZB01000010; SHJ72552.1; -; Genomic_DNA.
DR   RefSeq; WP_072987812.1; NZ_FQZB01000010.1.
DR   AlphaFoldDB; A0A1M6LN59; -.
DR   STRING; 1121302.SAMN02745163_02435; -.
DR   OrthoDB; 9760715at2; -.
DR   Proteomes; UP000184310; Unassembled WGS sequence.
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:SHJ72552.1};
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:UP000184310};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          58..104
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          631..788
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          911..1058
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1077 AA;  124760 MW;  2749049A4CA0A46C CRC64;
     MSGKDVVNLV EQQGRLSVLR EGEKVLASDL ITHMDYEIED KCLVTDAWVL SEDLFSEYEV
     SLVVDLGVKR IKLSSCTCDE YEKHSIKNNT YCCKHIMATA LKVAKQLGNF KNTNEKPSLS
     KNIEPIEEKG ESLLKDILFE KKQRENLKYE IIVKRNKQGY LGEIKIGIDK LYIVKDIREF
     IHCYTYGEDL NLGKGFCYNS WKYKMPVRLK EIITFINSLK ETEDIGERIF ELNKQGLING
     KNFVIVQSRL KDFFSILEGD KVSLELEFGK YKDVKIEKEN MNLLFGIDEK KNNVVLTYKG
     SVPKPLNTKG DVYLFSNKLY LLDYKRAIDY KKLLKALDKD KKIYFSKDNL NVVLNYLVPI
     IRNINSEVEI TSKIKKKLIK EDLKVELYFD IDKQKNISLD IKLVYGDYKI GLNETTVNKP
     ILRDMTKEDN LMNYVYSLGF EESYDKLYFT GSDEKVYDFL TQDIITLKEY GEVFYSQSFK
     NIKLNRNISP KFKIKSKGRN YFEFSYDLDG IDKIEVNDIL EAFKNEKKFY KLKDGDLLNL
     QDKNIYNFLD ALDNVTYGND VNKESLNITA EKAVYLSSIA EEENLNIEGD LQDINKIKEK
     LKNLNYEEIV SPKNLKADLR EYQKLGFKWF KTLSHLGFGG ILGDEMGLGK TLQAISFISN
     EKDKNTLIVA PTSLIYNWEA EFKKFSPNTN ILVVNGNKQF RNEVIKNYKN YDVIITSYNL
     LRIDFDLYKD LNFHNFFIDE AQNIKNPTSN ISKLVKEINA ESKFALTGTP IENSILELWS
     IFDFILPGYL YSEKNFMNRF GNNIRKDKNM IVELNKMIKP FILRRLKTEV IKELPPKIEK
     KLIIDMSEEQ KKVYAVYVNE AKAVIEQSIK EEGLAKSKFK ILSHLTKLRQ LCLDPSLVME
     DYKGESAKFE ALRELLTQSL QAGHKILVFS QFTSVLSKLK IILNEEKIKY SYLDGTTKAE
     DRIRLVNEFN EGENAVFLIS LKAGGTGLNL TSADVVIHFD PWWNPAVEDQ ATDRAHRFGQ
     KNVVEVIKLI AKGSVEEKII ELQEEKKEII NLVLNESIQG TEGFKNFSEK DILDIFN
//
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