ID F2TPS6_AJEDA Unreviewed; 1487 AA.
AC F2TPS6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=RSC complex subunit {ECO:0000313|EMBL:EGE85239.1};
GN ORFNames=BDDG_08184 {ECO:0000313|EMBL:EGE85239.1};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE85239.1};
RN [1] {ECO:0000313|EMBL:EGE85239.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE85239.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GG749487; EGE85239.1; -; Genomic_DNA.
DR HOGENOM; CLU_000315_15_3_1; -.
DR Proteomes; UP000007802; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; 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}.
FT DOMAIN 193..228
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 417..490
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 602..767
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 913..1064
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1316..1386
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1431..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 169416 MW; C97817DA8012294E CRC64;
MTSIQGVPNM ATANLSLPPN LTQQHVQEVY QKFRKMQEQG VRPDDPEYVK AHGLLSAVQR
QQAFQKQRQL AQQQQQLQNQ RLQLAQQQQQ QQQHQHQHQH QQQQQQQQQQ QQQQQQQQQQ
QQQSQSQSQQ PNGIPNDNLA NGVDGRNGSV APMSSGASLD PTAAVAAGQQ SNSVAQQQGN
TAPSKPASST GGTFSPEQLT TLRNQILAFK MLSKNLAIPP RVQQQLFAKK VHTVTTDGVA
LPDNVDNVAQ ARGSQPVEPN ENANKSKTMY ETFESPYKAL AETINYADHS FRRNRRRIPS
LMPIGIDIEK LREDQETALY NLITLRKAEL GKLPANLGVW NTDESDTPNG DDSLKLKALI
EYKMLNLLPK QRLFRKQIQT EMFHFDNLAM SANRAGHRRM KKQSLREARV TEKLEKQQRD
ARELRERTKQ SEQLQAILNH GREVQLAAGQ QRARVQKLGR LMLKHHQDME RDEQKRVERT
AKQRLQALKA NDEETYMKLL GQAKDSRISH LLKQTDGFLR QLAASVKEQQ KSTAQKYGEE
DRFDDDESDI DDDDDEEVEE GGRKVDYYAV AHRIKEEVTE QPNILVGGTL KEYQIKGLQW
MISLYNNNLN GILADEMGLG KTIQTISLIT YLIEKKKQNG PFLVIVPLST LTNWNIEFEK
WAPSVSRIVY KGPPTTRKQQ QQAIRWGNFQ VLLTTYEYII KDRPVLSKVK WVHMIVDEGH
RMKNAGSKLS CTLTQYYTTR YRLILTGTPL QNNLPELWNL LNFVLPNIFK SVKSFDEWFN
TPFANTGGQD RMDLTEEEQL LVIRRLHKVL RPFLLRRLKK DVEKDLPEKT ERVIKCRFSA
LQAKLYKQLA THNKLVVSDG KGGKTGVRGL SNMLMQLRKL CNHPFVFESV EDEMNPGRAT
NDLIWRTAGK FELLDRILPK FKASGHRVLM FFQMTQIMNI MEDFLRLRGM KYLRLDGSTK
SDDRSDLLKE FNAPGSDYFC FLLSTRAGGL GLNLQTADTV IIYDSDWNPH QDLQAQDRAH
RIGQKNEVRI LRLITSNSVE ERILEAAQFK LDMDGKVIQA GKFDNKSTNE ERDALLRTLL
ESAETADQIG DQDEMDDDDL NDIMARSEDE ILLFQKLDQE RAKNDLYGPG RKYPRLMVEE
ELPDIYLAED NPVPEEVEEY AGRGARERKV MKYDDGLTEE QWLMAVDADD DTIEDAIARN
EAKMDRRRQN KEKRARKAQG LDSSPEPSRE NSEAPQQPKK RRKGPVPKRK AEEAIDETPV
KRKKGRLSKA AMAAADTLAP SERAILQKIL NKVYQSLMEL EQELPADSSD SEDGPVTRSI
IDPFMKPPPK SHYPDYYMII QTPIAMDMIR KKINREEYRS VKEFREDIRL LCSNARTYNE
DGSVLFQDAN DIEALCVSEL KKETEAHPEF ADFEDLPSSS AAVSSVGTPL ASVVSTSTPG
GQQQQQHQKL RLTFGGSKDG NNNNNNGGGG GGLLTNGTNS GVVSDNE
//
