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Database: UniProt
Entry: A6QTW8_AJECN
LinkDB: A6QTW8_AJECN
Original site: A6QTW8_AJECN 
ID   A6QTW8_AJECN            Unreviewed;      1703 AA.
AC   A6QTW8;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN   ORFNames=HCAG_00824 {ECO:0000313|EMBL:EDN02960.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN02960.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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DR   EMBL; CH476655; EDN02960.1; -; Genomic_DNA.
DR   STRING; 339724.A6QTW8; -.
DR   VEuPathDB; FungiDB:HCAG_00824; -.
DR   HOGENOM; CLU_000536_3_2_1; -.
DR   OMA; VTPKDFM; -.
DR   OrthoDB; 2783776at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd05491; Bromo_TBP7_like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR045199; ATAD2-like.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23069:SF0; TAT-BINDING HOMOLOG 7; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
PE   3: Inferred from homology;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT   DOMAIN          1204..1278
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1323..1600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..49
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..82
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..130
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..330
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..393
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..488
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1403..1475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1483..1519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1556..1584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1703 AA;  189332 MW;  697A4EC3DBDEE95C CRC64;
     MPRVSKRTLE EIVLKSDSDD GDYSDTRPRP ARKSATAKSK SKKRPTKRRR RNSMIDDDDD
     DESDILTSED DISGESEFDE DDPTLERNAR GSIKRRAAKK ANYQLSSTSD DDEEDLEEEE
     QEDEDEEEAD ERDMKGKSRN NDKGRTTKRL LVKFPIAAQS SNTRTTRNTR GRSASKEHPT
     LTEYQGNRRI TRRTYDETED IVALTGSGRH VETVRKATRS PDALPRTRRG TAVPARAPSK
     SIIDEEDYGD KVPVEPVASQ IEIMESDQHG DFEEDAPAVA ASDNIQPSAE AEENVQDKDV
     EMGEEGIIPE SDQGGENEDE EEEEEEEEED APRSSRNSRA SRKQNMALET VEGASQATRR
     SARKSTARNS RQPQDDGSDF EPNDDEANDE DLSESEASAA SPRKGSQQNI EEVYESSNDR
     RSRLRKRQSH SQGRVESEAG ELAEELAELR PERRRRRVQN EIIYEDKPRR TRKSVDYRII
     RPEITLPIEE EDAPSGSPSR RGRGGGSGWQ RTLFSTYGPF GGAGGRPPLL GGPAGTGAAG
     GADSDSSDDD SGQRPMVGGM AGMTPTSGPA SGFNVAGHAF APDNAPGLSG TPANFGKVKD
     RQALADADPL GIDPNVNFDS VGGLQGHIDQ LKEMVALPML YPEIFQRFHI VPPRGVLFHG
     PPGTGKTLLA RALASSVSSE GRKVTFYMRK GADALSKWVG EAERQLRLLF DEARKTQPSI
     IFFDEIDGLA PVRSSKQEQI HASIVSTLLA LMDGMDGRGQ VIVIGATNRP DSIDPALRRP
     GRFDREFYFP LPNTEARRAI LDIHTRGWDP PLPNEIKDEL AELTKGYGGA DLRALCTEAA
     LTAVQRRYPQ IYRSNEKLLI DPKKIEVSPK DFMISLKKLV PSSERSASSG ASPLPSIVEP
     LLRVPLRDIK QILAEILPQK KRLTALEEAQ FEEPEDSVGF KRERMQQEFE TSRIFRPRLL
     IRGNPGMGQH YIAGALLHHF EGLHVQAFDL PTLISDSTRS PEASVVQLFT EVKRHKPSVI
     YIPNVQTWYE TVGQTVIATF LGLLRSLHPT DPVLLLGVLE DDGDNIDTTM MRDFFSFSKK
     NRFDLHAPES LWRHEFFNTL IKYIKSAPPE FPDSENRKRR KLETLERAPL APPPPPAPPT
     RQEIKAQKKK DRQTLNILKI RIQPIMDEIK KYKKFRAGVI DEAQIMYLYE EEDPNVVTTD
     VPLEHRTTFR PFEKDVDKHG VPGLRETVSG KFYYNMDIVT IEKRLSNGYY KRPKDFLADI
     KRIAKDARQL GDQDRQLKAN ELLSNVEVDI GNLEQSDPPL VAECEQVYLR EVERERVALE
     KAKRVAGSDG AMAPPPIMNV PHGNTENSNQ SSGPVVLGEP FSNGRLPLRR EPATPPRPSH
     PSTITNGYGP NKSSKDADED VTRPLTSNGS IGADGDVQMS NSDDVQPSER ENTQNSSFGP
     SAQPRPPHSY TGPSQQLRQQ SGLSNLSQKG TLTPMAPGSQ PGDYANDAST TQTTTDKKQS
     GPSDSNQLNT QSSIDGSTKH EYPDLNLYPD RLSGDEPLPD TQQGESGAWG TPLAGNLDFV
     NSQHSLVNGS QSQSNNSKFS QLGTQPHIPP FDGSGPRTTT TPRQVRVQEL LHAEGAQQHQ
     RHTFDTGKLI VDDRRLEALH HTLTQRTNGL SVEQLEQVNK SLMDCVWKMR GEWNRVEVAE
     AVKQAFEEVL GDIQSMQDFA AIP
//
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