ID A0A137QDM9_9AGAR Unreviewed; 1097 AA.
AC A0A137QDM9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative SWI/SNF-like matrix-associated actin-dependent regulator {ECO:0000313|EMBL:KXN85344.1};
GN ORFNames=AN958_11444 {ECO:0000313|EMBL:KXN85344.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN85344.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN85344.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN85344.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KQ962483; KXN85344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QDM9; -.
DR STRING; 1714833.A0A137QDM9; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 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 Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
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; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF00645; zf-PARP; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM01336; zf-PARP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50064; ZF_PARP_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 23..114
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 455..639
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 804..842
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 901..1069
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 117..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 122206 MW; 079CBE0D9748DB3B CRC64;
MASRHAFGVS FSGFTCSCSR NDILLQYSKS IRAKCHGPPP CKARRGTGLP VGTLRYGLTI
SNQYGENVEW RHWGCVTPNI LQWLATVNLN DVSGFIELSP ADQKKVRLAV QMRRIDPADV
PESAKSKHKP SVSGVQTSQK RKATEDLPSS STPRVTSAQP PVASQVVEVI DDESPEDEVV
DELYTMYHTN VVGIQYYTGL VGPGEEVVLV REPRNRFDAN AIQVKNIGQD QVGHIPRAVA
AKLAPLLDRN SITVEGVIND GNLGRSNAYT LSLTLRIYVV ADTLDVLEPQ LVWATPSQRG
GAALYRAPTP AYAYGSPAVQ QTPSISTAQQ EAMRKHQEAI LKQQALRKAA ELKQMIDGLE
KVNDEGRRGS LLDTLCSTED ILNLPLHPDP PGTQKGNLQV DLLKHQSQAL QWCIEREHPV
LPTKESDKPV QFWQYKTANG KQPYYFNLAT NTPQTQPPVL GRGALCADVM GLGKTLTMLS
LIIATKGDES PTTSKTTLIV SPLSILSNWE KQVEGHCAPG AISACVYYGS NRNMSVEELK
SYDVVITTYQ TITSEYGSLD AGGGNGFGTK KKRKSEQVLF SMDWKRVILD EGHNIRNPKT
KMAKSVCALK GERRWVLSGT PIINSPRDLG SLLTFLRICK PLDNEDFFKR LLLRPLKDAL
PSGIGLLSAL MSQICIRRTK EMQDSQGNPL IPLPPVEMIK VPVTLDDETR QLYDQVEQAS
RQRFRDYMNN RAVTTFAQSN VLGMLTRMRQ LVLHPGLIHS SYLEELRKGD SDSHAEDLIT
SLKPEEKLHL QDILAQAIED CEECPICFGL LNNPRITYCA HKFCLACISE VISRDPKCPM
VRRLVLVLGH CLLILVPIKD RRPISMNDML EPPPLTELTQ KPIRDNKPEQ ATGVRAGSSA
KIDQLVRLLQ LTPGSEKSLV FSQFTSFLDK IEEALDAAGI PFVRFDGQMS ARRRQEAITR
FSVPVKKSEN SQDDEVSDQM NPRVMLISLK AGAFGLNLTV ANNVYLMDPW WQEGIESQAI
DRVNRIGQKK PVHVYQLIAE DTIESKVLEI QERKKKLVQQ AFSGITRRET QREQREARFQ
GIVEIFGARN QNEAGEE
//
