ID A0A178E4G7_9PLEO Unreviewed; 991 AA.
AC A0A178E4G7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=Bromodomain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ07DRAFT_612007 {ECO:0000313|EMBL:OAL50261.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL50261.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL50261.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL50261.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441645; OAL50261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178E4G7; -.
DR STRING; 765867.A0A178E4G7; -.
DR InParanoid; A0A178E4G7; -.
DR OrthoDB; 152619at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR CDD; cd05500; Bromo_BDF1_2_I; 1.
DR CDD; cd05499; Bromo_BDF1_2_II; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR PANTHER; PTHR22880:SF225; BROMODOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR22880; FALZ-RELATED BROMODOMAIN-CONTAINING PROTEINS; 1.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT DOMAIN 439..511
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 642..714
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 834..916
FT /note="NET"
FT /evidence="ECO:0000259|PROSITE:PS51525"
FT REGION 74..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..766
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 991 AA; 107366 MW; 5212DE9DE039046B CRC64;
MTTLSAADNG SGLADTVFPR LPGSIYLGGG LFCRGAIDEC FEAGRSGGRG RLGELRLLCG
RGAVAGPRFG IAGPRGDDCR HGAGQRRRGG QETGEGRDVA SGSATPLNPA TSSATVRKPA
FLFHGPMAVM ATPAFEKSPV DLKASAFAPA DTMAVDSETN GISGVLFNNS DSNPNPATDP
AQPKPTLNGT RGPTDTSAPA MEPTTNVSSG IDGVAQFLPD SQQDTSSLFG DSDVMATAVT
AVEAPTSDVR DEPATAEELL TATQATSEST QQVPETQFEP SEDLAPDAMD ITADASQALK
IEEPAGPPTK PMNDLSIQTD LASTTQPELT QSPALVDREM EDAPSTGKVR PREDDEDDVP
DAKRTKTNDE LATQSDFKIP DVPAPTEQSN GTGAEAPIAS DPAQEASGIL KAVDYEPWPT
TPITEAQSKF LLERIRNTKK IKVSLAFKDP VNPVALGIPT YPDIVKNPMD LSTMENKLKD
KQYQYVREFM GDLDQMIENS ELFNNKQHPV TQAGYNLRAY FLKGMGKMPR AGAEEPKQTK
AKKPTVNTAP KPRRESRVVP PTVKSPAAPT PTATSPQAAW PLQQDGTPLI RRDSSTADGR
PKREIHRPTK DLPYSNAKPR RKKYQQELKF CESVLAEIMK PKYSGFTFPF TTAVDPVALN
IPSYLKIIKK PMDFGTIEKN MKNGVYQSAK DFYNDAQLVF LNCYKFNPET DAVNKMGHQL
EELFESLWKE KADWLAQHAP APEQSPSELY SDDEDEEEEE EEEEVDPKQA QFLAIQQQIA
ALNATAQQLL QQQTGGGKRA SPKAPGKKKK AAAVPAKRKS LPLAVPPPAK PNKPAKRAKA
PAPLTFAQKQ EISEGISTLG DSDMRRAVQI IRNGCPHLAN VHDDEMELDM DEINDETLRE
LFKFIKSLRG PKAGHVADDD FEPPRQVAKQ AVNRPKKNKP MGKTEQEDNM RKIQEKLNAF
QGGVSGSSQS PPAHDASSDD DESSGSESEE E
//