ID Q4WTW4_ASPFU Unreviewed; 1406 AA.
AC Q4WTW4;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=RSC complex subunit (Sth1), putative {ECO:0000313|EMBL:EAL91962.1};
GN ORFNames=AFUA_5G06330 {ECO:0000313|EMBL:EAL91962.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL91962.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL91962.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EAL91962.1}.
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DR EMBL; AAHF01000003; EAL91962.1; -; Genomic_DNA.
DR RefSeq; XP_754000.1; XM_748907.1.
DR STRING; 330879.Q4WTW4; -.
DR EnsemblFungi; EAL91962; EAL91962; AFUA_5G06330.
DR GeneID; 3511328; -.
DR KEGG; afm:AFUA_5G06330; -.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000315_15_3_1; -.
DR InParanoid; Q4WTW4; -.
DR OMA; VNYISHT; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
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; SM00573; HSA; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT DOMAIN 131..166
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 356..429
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 541..706
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 852..1003
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1253..1323
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 65..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..373
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 65..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1406 AA; 160916 MW; 84ECE67F1D51AEEE CRC64;
MAAGNMSLPP NLTQQHIQEV LQKFKQMQEQ GVRHDDPEYL KAHNLLAAVQ RQQVYQKQRQ
FAQQQLQAQH RQQQLNGATP ESAAANGING RNGPIPSSGP TQDASTPAAA QPQPANPAAA
AQKGAPVASG SFSAEQLTTL RNQILAFKLL SKNLTIPPRV QQQLFASKKS QTPSPSDDIA
SAESVLENVT QSKSEQPTPD VAPQSKDFYE NFQSPYELFP KSVSFTDHAS RANRLRIPAL
MPPGIDLEQL REDREMILYN KINARKAELA ELPANLGVWD TSKSDTPSGD DSLKLKALIE
YKMLHLLPKQ RLFRKQIQNE MFHFDNLGMT ANRSSHRRMK KQSLREARIT EKLEKQQRDA
RETREKKKQY DQLQAILNHG AELQNAANQQ RTRMQKLGRM MLQHHQHMER EEQKRVERTA
KQRLQALKAN DEETYMKLLG QAKDSRISHL LKQTDGFLKQ LAASVKEQQR SQAERYGEDE
HLFEDDDEED VGSDDDEEGG RRKIDYYAVA HRIKEEVTEQ PKILVGGTLK EYQMKGLQWM
ISLYNNNLNG ILADEMGLGK TIQTISLITY IIEKKKNNGP FLVIVPLSTL TNWNLEFEKW
APSVSRVVYK GPPNARKQQQ QQIRWGNFQV LLTTYEYIIK DRPILSKIKW THMIVDEGHR
MKNTQSKLSS TLSQYYTSRY RLILTGTPLQ NNLPELWALL NFVLPNIFKS VKSFDEWFNT
PFANTGGQDR MELSEEEQLL VIRRLHKVLR PFLLRRLKKD VEKDLPDKQE RVIKCRFSAL
QARLYKQLVT HNKMVVSDGK GGKTGMRGLS NMLMQLRKLC NHPFVFEPVE DQMNPGRGTN
DLIWRTAGKF ELLDRILPKF RATGHRVLMF FQMTQIMNIM EDFLRLRGMK YLRLDGSTKS
DDRSDLLKLF NAPGSEYFCF LLSTRAGGLG LNLQTADTVI IFDSDWNPHQ DLQAQDRAHR
IGQKNEVRIL RLISSNSVEE KILERAQFKL DMDGKVIQAG KFDNKSTNEE RDALLRTLLE
SAEAADQLGE QDEMDDDDLN DIMARSDEEL LTFQRIDKER QKNDQYGPGH RYPRLMGEDE
LPDIYLADEN PVQEEIDIEV TGRGARERKV TRYDDGLTEE QWLMAVDADD DTIENAIARK
EARVERRRLN KEKRQKRAMG IESSPEPSRE SSETPQPKKR GRRGPAPKRK AEEPVEETPQ
PKRKRGRQPK PVETLSSEDR ATLQRILNTA YQALMDMEQE LPADSSDSED GPVTRSIIEP
FMKPPPKSQY PDYYLIIQNP IAMEMIRKKI NREEYQNLKD FRNDIHLLCQ NARTYNEDGS
ILFQDANDIE AKCVEVLRKE TEDYPQFADF DDSLSSAGNA ASVAPALSTG TPVAATPTQP
KLKLTFNNSN RDSVGTSNGG PDSEDA
//
