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Database: UniProt
Entry: A0A0H1B7I1_9EURO
LinkDB: A0A0H1B7I1_9EURO
Original site: A0A0H1B7I1_9EURO 
ID   A0A0H1B7I1_9EURO        Unreviewed;      1711 AA.
AC   A0A0H1B7I1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN   ORFNames=EMPG_17555 {ECO:0000313|EMBL:KLJ06947.1};
OS   Blastomyces silverae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ06947.1, ECO:0000313|Proteomes:UP000053573};
RN   [1] {ECO:0000313|Proteomes:UP000053573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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:KLJ06947.1}.
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DR   EMBL; LDEV01002943; KLJ06947.1; -; Genomic_DNA.
DR   STRING; 2060906.A0A0H1B7I1; -.
DR   OrthoDB; 2783776at2759; -.
DR   Proteomes; UP000053573; 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:UP000053573}.
FT   DOMAIN          1237..1279
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1125..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1366..1604
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..48
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..80
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..122
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..392
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..488
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1128..1142
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1370..1515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1554..1587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1711 AA;  189438 MW;  3607CA5B3883D41A CRC64;
     MPRTSKRTLE EIVLKSDSDD ADYSDSKPRP ARKSTTSKPK PKKRPTKRQR RNSMDDDDDE
     SNILTSEDDM EIESEFDEDD PTLERNARGS IKRRAAKKPN YQLSSTSDEG EDELEEEDEE
     EEDKREVKGK SRNTDKGRTT KRLLVKFPIA AQSNTTRPTR STRGRSASKE NPTPTEYQGT
     RRNTRRTYNE TEDMVALTGS GRHVQTVRKA TRSPEALSRT RRGAAAPAHV PSKSTIDEEE
     EISRQELQDE GDTVPADPVA SQIEIMESDQ HGDFEEDAPA VAASDNINPP PEAEEAEENS
     QDKDVEMGGE GFVPESDQGG ENEEEEDEDE APRSIRNTRT SRKQNMPAET VEEANPPTRR
     STRRSAARSS RQPEEDGSDF EPNDDEANDE DLSGSEPPQA SPRKDSQQNI DEAYESSNDR
     RSRLRKRQSQ SQGHVESEAG ELAEELAELR PERRRRRAQN EIVYEDKPRR TRKSVDYRII
     RPEITLPIED ENDVPSGSPS RRGRGGGSGW QRTLFSTYGP FGGAGGLPPL LGAPGTGAAG
     GADSDSSDDD SGQRPMVGGM SGMTPTAGFA PGFNVAPGHA FAPDTAPGLS GTPANFGKVK
     DKQALADSDP LGIDPNVNFD SVGGLQGHID QLKEMVALPL LYPEIFQRFH IVPPRGVLFH
     GPPGTGKTLL ARALASSVSS EGRKVTFYMR KGADALSKWV GEAERQLRLL FDEARKTQPS
     IIFFDEIDGL APVRSSKQEQ IHASIVSTLL ALMDGMDGRG QVIVIGATNR PDSIDPALRR
     PGRFDREFYF PLPNIEARRA ILDIHTRGWD PPLPDEIKDE LAELTKGYGG ADLRALCTEA
     ALTAVQRKYP QIYRSNEKLL IDPKKIEVSP KDFMMSIKKL VPSSERSASS GASPLPSIVE
     PLLKAPLRDI KQILAGILPQ KKRLTALEEA QFEEPEDSAG FKKERMQQEF ETSRVFRPRL
     LIRGNPGMGQ QYLAAALLHH FEGLHVQAFD LPTLISDSTR SPEASVVQLF TEVKRHKPSV
     IYIPNVQTWY ETVGQTVIST FLGLLRSLPP TDPVLLLGVL EDDGDNIDTT MMRDLFGFSK
     KNRFDLHAPE SLWRYEFFSN LIKYIKSAPP EFPDPENRKR RKLETLERAP PPPPPPPVPP
     TRQEIKAQKK RDRYTLNALK IRIQPIMDEI KKYKKFRAGV IDEAQIGYLY EEEDPNIVTT
     DIPLVHRTTF RPFEKDVDKH GVPGLRETVS GKFYYNLDIV TIEKRLSNGY YKRPKDFLAD
     IKRIAKDARQ LGDQDRQLKA NELLSNVEVD IGNIEHTDPL LVAECEQVYL REVERERVAL
     EKAKRAAGAD GVMAPPPIMN VPHGNTETSH QSSGPVVLGE PFASRHLSAH GEPTTPTRPS
     HASTVTNGHG PGKTAGETGS RPPTSNGFVG ADGDVQMSNS DDVQPSERDN TQNSSFGQSA
     QPRPPHSYTA PSQQLRQQSG LSNLSQKGTM TPMAPGSQPG DYTNDASTTQ TTSDKKHSGP
     SYAHQINTQS SIGGSARHEY PDLNLYPDRL SGDEPLPDTQ QGESGAWGTP LTGIVDFANS
     QPSLVNGSQS QSNFNNSNAS KLSQLDTQPP IPPFDGAGPR TTTTPRQARM QELLPGEGTQ
     QQPHHPLPPF PPAAGKLIVD DRRLEALHQT FTQRTNGLSV EQLEQVNTSL MDCVWKMRGE
     WNRVEVAEAV EQAFEEVLSD IQSMQDFAVI S
//
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