ID A0A1Y1YR21_9FUNG Unreviewed; 2057 AA.
AC A0A1Y1YR21;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN ORFNames=K493DRAFT_405875 {ECO:0000313|EMBL:ORY00488.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORY00488.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORY00488.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORY00488.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY00488.1}.
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DR EMBL; MCFE01000082; ORY00488.1; -; Genomic_DNA.
DR STRING; 1314790.A0A1Y1YR21; -.
DR InParanoid; A0A1Y1YR21; -.
DR OrthoDB; 1342632at2759; -.
DR Proteomes; UP000193498; Unassembled WGS sequence.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR Gene3D; 1.20.920.10; Bromodomain-like; 6.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR037813; TAF2.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR15137; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR PANTHER; PTHR15137:SF9; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 2; 1.
DR Pfam; PF00439; Bromodomain; 6.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00297; BROMO; 6.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47370; Bromodomain; 6.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 3.
DR PROSITE; PS50014; BROMODOMAIN_2; 6.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS51420; RHO; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Reference proteome {ECO:0000313|Proteomes:UP000193498}.
FT DOMAIN 933..1005
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1087..1159
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1326..1398
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1437..1509
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1573..1645
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1725..1797
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 771..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1822..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1862
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1863..1880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2057 AA; 233873 MW; 43708D9B167884D3 CRC64;
MYSATMTIAS THLLHGDDII DQTYETRRHL SLALAKQWFG IHVVPKYGAD LWLTVGLANY
ATSLLIKHLH GNNEYRFRLK KDIDKVCELD VDRPPLYNVN LSYPVDPDDY NFMQLKAPLV
LFVLGKRMMK GGPSLGIHRA IPKVLVAAMS GELGSGNALS TNWFLKVCRK VSGVDNKPFA
EQWIFGSGCP IFHFTYSFNR KKMVVEINME QRSTNSNGLA NKHDDRAMYP STTMFTGHMT
ALIREADGTP YEHVLDIQDL SKKYEVQFNT KYKRIRRLTK RFQQRQAAAA AAEASVGAEE
MPEAVMEDLE DVFGYGMDEK EKEEWRVVEW GEIDEESTAS GTFEWIRLDS DLEWICVMQF
EQPDYMWACQ LLNDRDVVAQ IEAIEALSNC PSPATSTSLM RTMMDPKCFY RIRMEGAFAL
AKCAIPQLDW IGLHHLFKIF QKRYCYASTT ADGDGEIAIV PKPNNFSGFT EYFVQKAIVA
AFSTVKNSKG HTPIKIKQFL LELLRYNDNT GNHFSDNYYI SALINALGNA LVPNERSNQS
EQEGEKELFA DAVQEIERYR TLDYLVPSYH NTVTISVMQV MMKLMMASLL APNLKLFLGY
TRYGNFLRVR LVAFEALLLL DGLRNRPIGF YIFQVIAHDP SHYVRYYLAK CLSEMLGVHI
ARASLSDHDT SEEMVFEEVG QPKAISEKAS EDGFIHTPGL EAIHKEFSGR EDIQDQVWAI
LTSDPVQDYR VFRYIFLFCE LLYKPIDTVP KLKIKMPAAV STEARNDVSL RIPGKASESS
KPSDKAESIG PIRKESANYD IPTVSAFDDE DIEIEAGTVL SPVKSAPTSK EDKKVKATSI
PKPRKESKIS DVRREPRTKD TGKSSKPDQA ALDVQVKIEP VEVSPATTTT TTIPVEAPKQ
PPKQTPQQET VLTVSMLRPD EMKICKRIIR KMMAHKSAFY FLQPVDPIRD GCPTYFDLIK
HPMDLGTVKA KLDEGGYHNL KEFEDDIRLM LNNCFIFNPI GSYVYNEGQE LESVFEKEWS
ELNAQELVGR EPEFNMTIVE SPVTKSKALP SEKSDPELEQ PKNEAEKSSK GLIPELQKCR
SILKRIAQHE SAFEFLRPVD PIKQGIPTYF EMIKNPMDLG TINKKLKSRQ YQTKDNFRED
IELMLNNCFT FNTPGTFVYN QAKSLSEVFQ REWVNQFGKP TKSAVTESTN ITVKSEPAPE
PINSREPSEK PVAELPHTSE TATPGPSVEY GSKETKTSNF AKPTPSSPKP KSPMVRAGTS
DTVKDNGGKL TPKAASKDSR KSLTPMPLQS PVRHSSSPAT KAAAKPANTM NSTAYKRCQK
ILKKLWSNPS SEPFQLPVDP VMLKIPTYTD IVKDPMDLKT VTEKLEREEY TSVRSFEKDI
RQIFFNCFLF NQPGTWVFEE GKKMEAYFYE LFDRDKPRRP ILPEDKQSLL KLVQKMIKNK
HSSLFREPVD WVALQIPDYP RIIQNPMDLG TIKDKLENDQ YRTWVDFERD VRLIFNNCFT
FNPSGTYAHE ESQQLENYFF ERYEELKNAL KAIPEVSRTP SREPSIKREP EPEPVTMSPE
QMKLCEKIHK KLSGNKNAIA FLEPVDPIAM GIPHYFDVIH NPMDFSTVHK KLKAGEYSTP
TEFETDIRQI FKNCVTFNGP EHYYSQQAMA LEKTLDKEMI AFQTLKSSTK SSGGIGSRKS
DKQPKKETIP VVASSPSRSV KVSTKPKTLD RSALKICENV LARIKTHPSF EPFGTPVDVK
ALGIPHYNKI VKHPMDFGTI EGKLRGGKYS SVEQFLSDAQ LVFDNCYIFN IPGDAVYVMG
QELQRAFEKA CKKYNLLDIL ENPNPERSTT KRPHPEESDQ LERHGSHERK RKKDKKEKKK
HKHSHREDMD KYDVEDNVTD SENSRTSVPQ ASPQRQVYVP TVFENYVADV EVDGKRVELA
LWDTAGQEDY DRLRPLSYPD SHVILICFSV DSPDSLENVQ EKWISEVLHF CAGLPIILVG
CKKDLRNDPR TIEELRKQGQ SPVTPDQANG VASKIGAYKY LECSAKENDG VRQVFEHATR
AALLTKTKQK KKGCLVL
//
