ID A0A2H3CDS7_9AGAR Unreviewed; 1267 AA.
AC A0A2H3CDS7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=SNF2 family DNA-dependent ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARMSODRAFT_949298 {ECO:0000313|EMBL:PBK77382.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK77382.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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DR EMBL; KZ293416; PBK77382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3CDS7; -.
DR STRING; 1076256.A0A2H3CDS7; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000218334; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 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; 3.
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; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000218334};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 444..778
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1100..1248
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 139428 MW; E10364FC7FCB502E CRC64;
MSLRSTPSLS NLTISNKSNP IDLTADDADE TYDYPRQLKR MRLENITHPN NSILPTSHSM
PSTPSPTPSM SSFTSYNQKP AMAMPIARHN SFMVPSIFAP NPNPSNNGPY RPPFAGPSSS
FHAPPPVPPS SIPQKRPSAH SLDRAIIDLT DSPSPPPQIQ KSFPPPNLID LSPKTPVCIG
QLTVTALVLY PIDYMMATNP ASPHVEWGSV KLQYEHAPKP DGTTDNLNIK TPTGDPFGIV
EHKVASSLGH MVGKGLIRLE AKVQKCRSNA PILPLTMLVY TPKGNVPVVG DYFFQCGLLL
DHPTPPFSYN EIVSSKTPYL NPHNPPPGGH NRVQYAPNRT VYPPGGNGRW TTATPAGKSV
EVQRSQVDEL FKNMKNGVEL AEMEAAPEVA TQLYPHQKKA LTFLMERERE VKTAEGVYSS
MWLMRKTMSG HGTWTHLVTE KEVYEEPQES KGAILADDMG LGKTITCVSL IAATLNSALT
FASAPLETPS LPWGSSSDDS SPAPSQFAGS VWGMPDVSEN GPSSVKAKAK AQRAQEKIEA
EHVRANRIKA KSRATLIICP LSTVSNWEDQ FREHWNGEVQ VFGGGGGAAA TALCSQPPSQ
GSLVDVKSET KPTRIRNGKP LKVYIYHGNA RRPDPAFLAD FDAVITTYAT LASEFSKQNR
SLVTAEVEEE EEGAGSSDGG GVEIDERGNQ ILRLPKTKKG GVKRKKPGLW ASEASSALQS
IHWFRVVLDE AHCIKETGTV GSRASCDLMA DRRLCLTGTP VQNKLDDVFA LIKFLRLHPL
DDKAVWTEYI GTPVKFGQSM GIARLQTLMK TITLRRTKES KTLDGKRILS LPPRRDELRL
LKFDAQEQEI YDQFFTASKA EFNEMSDKNE VMKNYVGILQ KILRLRQICD HFELVEGKDL
LEQDGTLSYE DIVAAIAKEG FTTSRAVAIF AILKESATTQ CVECGSELCT SSGEAPDDAM
DEMGPKKKKG KASSKAPTRA SSPSVPRPIL TRCQHLFCLQ CYRQCIHPSW PNVAPDIYRS
CSACQTGLCP ADAIEIKSEY LDGSPAKKKP ARKEKRQRGT GSETCHPSTK IKALLGDLVQ
FSRTNPYSSN YDPDSIEVHM VDEKGVEVDE GVVKTVVFSQ WTTMLDKIEE ALESAAIRFD
RLDGTMKRDE RIRAMDALKH DPGCEVLLVS LKAGGVGLNL TAAQRVYLMD PYWNPAVENQ
AVDRIHRLGQ TRPVTTVKLI IENSIEARLL EVQRKKTELA NMTLGSNFSK AELMTRRMEE
LNQLFGS
//
