ID A0A165N1K7_9AGAM Unreviewed; 1163 AA.
AC A0A165N1K7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=SNF2 family DNA-dependent ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEOLEDRAFT_1142558 {ECO:0000313|EMBL:KZT19055.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT19055.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT19055.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT19055.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KV425651; KZT19055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165N1K7; -.
DR STRING; 1314782.A0A165N1K7; -.
DR InParanoid; A0A165N1K7; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000076761; 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; 2.
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; 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:UP000076761};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 4..92
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 458..639
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 805..843
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 95..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1011
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 128902 MW; 4DFFC2C82F54C395 CRC64;
MVGHLIEYSK SSRAKCHGRP PCKGSNIEAG ALRYGKVLKS DYGDTVEWRH WGCVTPDILT
ELAVLPVDDV SGLKSLKIED QHKIRRAVAI RQIDPADIPA SAKPSPATQA KSSGGAPSQK
KRRAAFEASQ TATSSKSFVP STSAVRTVGI DLTQNEELED DAPDEESRDE LYCTMGTSIV
GVQYYKGLVG HGEEVRLVRE PQNRYDRNAI QVKNISGIQV GHIPRQTAAS LAPLLDEGLV
TVEGVMRDGN LSGFSYSLSM TLKIYGAADK RAQLEPRLIW ATPARRGFAK RNNAPTASTS
YQTPARGSSS IAGASVAPPP SMSTASQQRG MTAAQIQAQQ EAARKQQEAW QKAQELQQML
NTLEKVDDEG RRSSLLDTLC SQEDILSFPE HPSPPGINTG DLKVNLLKHQ SQALKWCLEK
EYPVLPKKES DKPVQFWQLR KAGARSFYFN VATKTPQEAP PVLGRGALVA DSMGLGKTLT
MLALILDTRQ DIPPEHSKST LIVVPLSVLS NWEKQIQDHV VEGALRYYVY YGASRSITPD
QLKQFDVVIT TYQVVTKEHA ESGSPGATGQ KRKRSEKGLF DVPWKRIILD EGHSIRNPRT
KMAKAVCGLD AHRRWVLSGT PIINSPRDLG SILTFLRICR PMDNEDFFKR LLLRPLKDGS
PSGAELLRAL MSQICIRRTK EMRDSEGNYL VPLPPVEMIM VPVTLHEDAK TLYDAVDEVS
RQRVERFMDR EGGLHGVAIH SNVLSMLTRL RQLALHPGLV PADYLEQLRS ADAEDEAPPA
VVLTSQDRLR LQSRLFQAIE DNEECPICFG VLSDPRITSC GHSFCLTCIS EVISRDPKCP
MDRRPITMGD LVEPPPPTDL TQAPVSRDED DDDSELRKGS SAKIDQLVHL LKLTPSTEKS
LVFSQFTTFL DKIGDRLAEE GISFVRFDGK MSAKRRQETL ERFSVPIDED SPEETVASTT
SQAAPQSTHR RRQTRRKSTA PIVLDSDPLT GQDDDFVPDN NDDDVSFAED DSDEEVARNS
RKKGKGKGKA RASTRKAGSS LVNFDGPNPK VMLISLKAGA LGLNLTVANN VYLMDPWWQE
GIESQAIDRV NRIGQKKPVH VYQLIAENTV ESKVIDIQER KKKLIKEAFA GIKSNETQRQ
KKEAKLQELV ELFGLRQQTA KKS
//
