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Database: UniProt
Entry: F2SI95_TRIRC
LinkDB: F2SI95_TRIRC
Original site: F2SI95_TRIRC 
ID   F2SI95_TRIRC            Unreviewed;       975 AA.
AC   F2SI95;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN   ORFNames=TERG_01817 {ECO:0000313|EMBL:EGD85546.2};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD85546.2, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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DR   EMBL; GG700649; EGD85546.2; -; Genomic_DNA.
DR   AlphaFoldDB; F2SI95; -.
DR   STRING; 559305.F2SI95; -.
DR   VEuPathDB; FungiDB:TERG_01817; -.
DR   eggNOG; KOG0732; Eukaryota.
DR   HOGENOM; CLU_000536_6_1_1; -.
DR   InParanoid; F2SI95; -.
DR   OMA; CIPSIRS; -.
DR   OrthoDB; 2783776at2759; -.
DR   Proteomes; UP000008864; 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; 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; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF00439; Bromodomain; 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:UP000008864}.
FT   DOMAIN          486..528
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          377..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   975 AA;  108104 MW;  7F83611D3984FF0F CRC64;
     MDGMDGRGQV IVIGATNRPD SVDPALRRPG RFDREFYFPL PNVEARRAII DINTRGWEPA
     LSDEFKDKLA ASTKGYGGAD LRALCTEAAL NAVQRVYPQI YQSKDKLLID PKKIKVSFKD
     FMISLNKIVP SSERSASSGA SPLHSTIEPL LREPLREIQE RIAKLVPRRK ALTALEEAQF
     EQPNDDVGFK REKLQEEFDR SRVFRPRLLI RGEYGMGQQY ITSALLNHFE GIHVQSFDLP
     TLLSDSTRSP EAVVVQLFAE VKRNKPSVIC IPSIRSWYET LGNAVISTFM GLLRSIPPTD
     PVLLLGILEG EADYEANSDI VRNLFGFSKK NQYFLSYPEL SQRREFFQPI IDFIRTPPAD
     FPEPDNRKKR VIEQLELAPP APPKPPPAPT KEELKAQKRK DRQTLNLMKI RIQPIMDQIR
     KYKRFRTGVV DESQIRYLYD DDDPNVVTSD LPPQQRSTFR PYEKDTDKAG VPGLREVASG
     KFYYNLDIVT IEKRLSNGYY KRPKDFLADI KRLAKDAKQL GDPDRQLKAN ELLANVEVDI
     GAIDNTDPAL VAECEVVYTR ELEREKAALE KIKQPVADAD GTMKPPAGPP PQMNIAHGSI
     ELSNVSSAGP VVLGELFNSP CPAPGSKSGP GHPSLTNGHT PGFHLHGGVD GVRPPTSNGP
     LHKPEGDGDV EMSNSDHTSG AHQNNTQNSS FGPSAQPRPL HSYTAPSQFM RHQSGLSTLS
     QKGNITPMAP GSQPGDYVND ASTTQTTSDK KNSGPTDIMH TNPHASLIGS AMHDAPDLTL
     YPDRASGDEH LPETQQGDSS WISSQMTPLR GVAEFIHSQS TSNANGSQSQ PRHSQASQPH
     PVGPPPLFDA ASSRSSGGNT HGNPVTPPSR NGETTRISNL INSEPKQPEP PLPNLIVDED
     LNRELHDELS TKTGGFSVEQ LEQINTELMD CLWVNRNEWN RQEVAMILRS TFLETLDDIK
     SSQNYVDTTQ KLGRQ
//
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