ID   L7U8H2_MYXSD            Unreviewed;      1189 AA.
AC   L7U8H2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=SNF2/helicase domain-containing protein {ECO:0000313|EMBL:AGC45226.1};
GN   OrderedLocusNames=MYSTI_03920 {ECO:0000313|EMBL:AGC45226.1};
OS   Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC45226.1, ECO:0000313|Proteomes:UP000011131};
RN   [1] {ECO:0000313|EMBL:AGC45226.1, ECO:0000313|Proteomes:UP000011131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC   {ECO:0000313|Proteomes:UP000011131};
RX   PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA   Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT   "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT   fruiting myxobacterium.";
RL   Genome Announc. 1:E0010013-E0010013(2013).
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DR   EMBL; CP004025; AGC45226.1; -; Genomic_DNA.
DR   RefSeq; WP_015349486.1; NC_020126.1.
DR   AlphaFoldDB; L7U8H2; -.
DR   STRING; 1278073.MYSTI_03920; -.
DR   KEGG; msd:MYSTI_03920; -.
DR   PATRIC; fig|1278073.3.peg.3994; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_000315_21_7_7; -.
DR   OrthoDB; 9814088at2; -.
DR   Proteomes; UP000011131; 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; 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; 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   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:AGC45226.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          184..217
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          724..881
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1008..1169
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1189 AA;  132395 MW;  2F34A8737715AEEE CRC64;
     MSVERPQPDL SSVPHFATEG ALRSWLREKG VEHLSRLSLT VLVPWVDAAL LPQARPATAR
     RRLVEMLSEE ARTRWAQESL PSPKMKELLP RLAWRFVEEE RRGAERTRAE LAARLSPPDD
     PRTHRVHGLL LDLRSRAPDT VAPRPTQALF LEPLQHDPEL PGFRFRETRC SELPYGAQMG
     FILPEATLTF TPNSVQADCT CGAPPCVHVL AAIDTVLLWL HQPWTPSFGE TLEELVRPGW
     DRTLRAMERA LDDGTGSGAG VEISWRVDVI EGYGVEVFPY VHKRNKKGLR STGAKVSRRK
     LLQEHGSQLS ALDARLASLL PDGDAPVSRG LLIELVDHPR LYQEGTQDLL VQVERAKVGI
     VAVERGGTVI VTAGVDGATL HATMVDRVRK SKPEEALFLW DEGARRLTVL DVGPEVRALV
     TVLQRHGNVF PPESHEVLLE KLSKLAVRMP VALPRGVMGE RVPSLQLPVL RFELEPGGAV
     RVELRMRALP DSISFVPGEG PRDVYVRRNL EPVHTVRDFM KELALAQSLQ ARLPFAQGEA
     QVIPFTFSFE GVQGALALLS ACQELESPPE LEWVGSPLKL AGSRGASALR ITVERKRDWF
     GVLGGLAVQG ERVELGRLLD AARRKERFIQ VKDQTYVEVE EALRHHLERL ADHAHLSRHG
     LEVSPAAAES LSALGTAGAT LDADETWKRL VERIFAAKEL KPKVPATLKT ELRDYQADGF
     RWLTRLASWG AGGVLADDMG LGKTVQALTV LLERSKLGPA LVLAPTSVAF NWMDEAKRFA
     PSLRMRLFSE AADRGGLLER LGPRDVLVLS YGLLTRDIGR LSELRFATIV FDEAQALKNA
     GTHRFRAARA LQGDFKFALS GTPLENHLGE LWSVFALVFP GLLGSHDAFR TRFAIPIERR
     VDPTAAPALA RVLEPFLLRR TKAQVEAQLP PRTDVRVPVV LSTAEWTMYE DARLAALSAL
     ESRPEVKQER RAREHEQRFE VLAALTRLRL LASHPRLYDA TSRVESSKLE RFLELVEELR
     AEGHRALVFS QFTSHLALVR EVLDARGIRY EYLDGQSTPK AREQSVRAFQ EGTAPLFLIS
     LKAGGFGLNL TAANSVIHLD PWWNPAVEDQ ASDRAHRIGQ DRPVTVYRLV ARGTIEEQML
     SLHEHKRALV ADVLEGKDGA GRLSTQEMLG LLSQRLSRPD EEEPPQTRH
//