ID S0DUK8_GIBF5 Unreviewed; 1421 AA.
AC S0DUK8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Probable component of SWI/SNF global transcription activator complex {ECO:0000313|EMBL:CCT66151.1};
GN ORFNames=FFUJ_03151 {ECO:0000313|EMBL:CCT66151.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT66151.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; HF679025; CCT66151.1; -; Genomic_DNA.
DR STRING; 1279085.S0DUK8; -.
DR EnsemblFungi; CCT66151; CCT66151; FFUJ_03151.
DR VEuPathDB; FungiDB:FFUJ_03151; -.
DR HOGENOM; CLU_000315_15_0_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000016800; Chromosome 3.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:EnsemblFungi.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IEA:EnsemblFungi.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000182; F:rDNA binding; IEA:EnsemblFungi.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:EnsemblFungi.
DR GO; GO:0035973; P:aggrephagy; IEA:EnsemblFungi.
DR GO; GO:0042148; P:DNA strand invasion; IEA:EnsemblFungi.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IEA:EnsemblFungi.
DR GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0031496; P:positive regulation of mating type switching; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
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; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT DOMAIN 141..176
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 378..450
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 558..723
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 869..1020
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1277..1347
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 162491 MW; 8E48DC09FC9F219F CRC64;
MASVHAPHAV QHPGAPMPAG ATKQQAEEVF RKLRQMKEQG VPPSDPEYIK ASQFLMSFQQ
QHTMRRNQQQ FLQQQQKQQM QNATNGTPAN GVMPGRSMQQ GSPQSTQPPS NPLGASAMPN
QTTPTPASTG TSPSTAPSSN HFTQQQLGLL RQQIHAFKLL GKNAGVSLQL QQAIFNQRHR
RQAAIADAAQ VIQATKSNQA DPESTKDGQN GPGAVTEDEG SDIPKAHTFK TVKSPYGTSM
IRPEIKYFDH SQRKNRWFIP GVFPTGIDFD HLRYEREVVV SNRMRQRYAE LKNLPGDLAH
WDSSKETLEA DDSLKRKAII EMKSIALYAK QRALRDKIGR QMIHYDNLAM TTNRSGFRRM
KKQNVREARI TEKLEKQQRD ARENREKKKH TDFLRAIYTH RQEIQDSASS QRNKSHKLSR
LMYQQHFNIE KEEQKRIERT AKQRLQALKA NDEEAYLKLL DQAKDTRITH LLKQTDGFLH
QLASSVKAQQ RQAAERYGDG DDPQMDDASD YDEDDESSKK IDYYAVAHRI REEVTEQANM
LVGGKLKEYQ VKGLQWMISL YNNNLNGILA DEMGLGKTIQ TISLITYLIE RKQQAGPYLV
IVPLSTLTNW NLEFERWAPS VSRIVYKGPP NARKQQQDKI RQGGFQVLLT TYEYIIKDRP
ILSKIKWFHM IIDEGHRMKN SNSKLSFTIQ QYYHTRFRLI LTGTPLQNNL SELWAMLNFV
LPNIFKSATT FDEWFNTPFA NTGGQDKMEL TEEEQILVIR RLHKVLRPFL LRRLKKDVEK
DLPDKTEKVI KCKFSALQSK LYKQMVTHNR LVVSDGKGGK TGARGLSNMI MQLRKLCNHP
FVFDVVENVM NPMNVSNDLL WRTAGKFELL DRILPKYQAT GHRVLMFFQM TAIMDIMEDY
LRYKRFEYLR LDGTTKSDER SDLLREFNAP DSKYFMFLLS TRAGGLGLNL QTADTVIIYD
SDWNPHQDLQ AQDRAHRIGQ KNEVRILRLI SSNSVEEKIL ERARFKLDMD GKVIQAGRFD
NKSSETDRDA MLRTLLETAD MAESGEQDEM EDEELNMLLA RSDDEITVFQ KIDEERQRTS
PYGNGPGSKP RLMGEDELPD IYLNEGNPIS DETEDVVLGR GARERTKVKY DDGLTEEQWL
MAVDDDDDSP EAAAARKQAR KDRRENNRLK KSGVSNSVDE SPSGSRASTE EIETPKKRGR
KPGSKNEKRK AEDGNDEPPP KKRRGPQGRP SKVSLESRLP PHQREVLQRS LRNLYDALMT
LEVDDIEPPE DDESDPGKRL IIGPFVKLPP KRDYADYYLI IQNPICMNQI QTRIKKEEYT
SLSGLRKDIE LMIRNCQTYN EDGSILYQDA KVMNEFFNSK YQEELVAHPE LQELEEGVKD
SSVAPSGGGG TPQPSGTRIK LISSGSKEAN GGSTAAQSDE E
//
