ID A0A166DYX4_9AGAM Unreviewed; 944 AA.
AC A0A166DYX4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZP15216.1};
GN ORFNames=FIBSPDRAFT_795829 {ECO:0000313|EMBL:KZP15216.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP15216.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP15216.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP15216.1,
RC ECO:0000313|Proteomes:UP000076532};
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).
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DR EMBL; KV417607; KZP15216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166DYX4; -.
DR STRING; 436010.A0A166DYX4; -.
DR OrthoDB; 1614794at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532}.
FT DOMAIN 439..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 835..905
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 266..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 106571 MW; 0A2C347C10E5EC80 CRC64;
MWARIGWQGS TVSTLDSKLR KSHSSFAACL LALGRAAWPE LKRGREQETL NELAKCYVQL
EQESTSLRHI KVDAVIVQDH LGRSLPVPMI FCTSSHDFHI VITGFCRGVA GDVLIQRGNY
RILNSKDDQV INPEEFAIVL RPGMAVGMSI ALHEQVEERQ GSEGHRCPRC KHINARCTGW
VTCAKCNGSF KISPEEAIIS PETEQRAGAD SIPNERFLFR KISIFQRKRN NVVYKDGLDD
KQFAMASEDG EDFQDVGRKR GDRAAQLVED TSNRGTSMSD SESRGRNGRK GTSKTNDHEP
ASVERKRGAK AMSVTSPLDK DDDDDRDTKR RKTKAGDLPA DQMTQDVEKD LPDKVEKIIK
VRMSALQSQL YKQMKKHKMI ADDQDSKGKA AGLKGRSNEL MQLRKICQHP FLFESVEDRM
NPSGMIDDKL VRSSGKLELL SRILPKFFAT GHRVLISFQM TRVMDIMEDF MKMMGYRYLR
LDGGTKTEER ASYVRLFNEK DSEIKVFILS TRAGGLGLNL PAADTIIIFD SDWNPHTDLQ
AQYLAHRIGQ TKAVRILRFV TEKSVEEAMF ARARFKLGID DKVIKAGRFD NKSTQEEQED
FLRSILEADQ EEENEEAGDM NDDELNEMLA RDENEAEVFR DFDVARDRQQ LEAWRAAGNR
GKPPTGLMQF DELPKCYQVD EPFKVETIVE GTENRGQRKR EDAVYNNALN DKQSAMAPED
GEDLEDDGRK RGGRAAPLVE DHSNRGTSNS DSESRGRKSK KGKSKTNDYE PAVVKRKRGA
KAMSVTPSLD EDDDDDRDAK RLKTKVGDLP AAVRDRMKKA FLECHTAVMR CEDDTGRKRC
ELFKELPAKR DYPDYHKLIK KPIALSHIRK RISSNTYKNA AAYKDDLRLM FDNARTYNQE
GSLVYVDAEE MEKAFEGAWD RYVVGSGLPG APDGTPAVAA GPVG
//
