ID A0A2G8RWY8_9APHY Unreviewed; 1089 AA.
AC A0A2G8RWY8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Transcription factor {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSI_11789 {ECO:0000313|EMBL:PIL26035.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL26035.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL26035.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL26035.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIL26035.1}.
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DR EMBL; AYKW01000045; PIL26035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8RWY8; -.
DR STRING; 1077348.A0A2G8RWY8; -.
DR OrthoDB; 5399336at2759; -.
DR Proteomes; UP000230002; 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 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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 PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002}.
FT DOMAIN 383..525
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 706..860
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..59
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 123256 MW; CC71DEE29F0A2288 CRC64;
MTTAPKKVSG YTKRNDQSSA VPLDLDSDSD FNPGSFVPTP KKKRGRQSRH SRKSGEPPRK
RRRKESLEDE GSRERLIDGV KTGDAVPLQR NLLTQYFGNL GAADGSESEK EVADDEEEEE
EEEEEERDSD GDTDHPPHST PNILLVPSTK MATPQSSQPD GDEDSVTEYE SDEIEENDPV
HAELKPPDTV ASSNSKPSTA KTPSPEDDDS VTEPEPDEED WLNEDFSSTT PASVPGPLSA
SQVPPAKKKI PSPKKVKPED SGSDTEPEYD ADPYFTQPKP AFQLKPGQQI LGPLVLDREH
KVPERINTFL REYQRDGIRF FWERYKGGRG GLLGDDMGLG EYRYLWRRKT IQVISFLSAI
MGKRGDTLDE DRRRKHVSKL QDLPDWRKHR RLPPANATWP TCLIIAPSSV VGNWEREFQT
WGYFEVGMYI GTPSARADVL NEFKLGRLDV LVTSFDVARG DIDLIDELPW SCIFIDEVHR
VKNPKSKLAE AFSRFTCACR FGLSGTVIQN GYDELWTVVN WTNPGAVGTR KQWETYVEKP
LRVGQSKSAS DEEHVKAALV AKVLTDRLLP QVFLRRTKQI IQDQLPHKTD QVVFCPLTPT
QIDIYKRILS LDAVKSLVYK DLLCTCGSRQ PRKKCCHPVH QGDLFKYMST LIKISNHLAL
ILPSPSDTIE QTARNRELAR LAFPSGFVPK YGPAMLRPEY CGKWQVLETL LRAWKKDASK
VLIFTKSVKL LDMLEFHLNA QGHGFVKLDG STKQSDRMPM IDRFQEDPDI FVFLVSTMAG
GTGLNLTAAN KVVIFDPNWN PAHDLQAMDR AYRFGQTRDV AVYRLLGAGS IEELIYARQV
YKQQQMQVGY NASLQTRYFE GVQGDKSKQG ELFGIKNIFK LHETTLATKM AIERANVSDL
DWAFAYMGGS GSGTKRPKTK PDGVKWVYEE EAKTGKEYDD LRGLGALLFD DAAPEVNQEP
NDIEKTLTAI GIQYTHRNDD LIAENVIEGQ RMQKLIQEKK KAAKKAKKQR ESDKDKPPEP
EWPPRRRHHK PPPSPHTKLQ IRQRALIEQG ILQSPQDLPK FAHEFGQKSL QEQNDFLAQL
DEYAKTHFN
//