ID A0A178EP59_TRIRU Unreviewed; 643 AA.
AC A0A178EP59;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=BZIP transcription factor AP-1/Yap1 {ECO:0000313|EMBL:OAL61840.1};
GN ORFNames=A7C99_6410 {ECO:0000313|EMBL:OAL61840.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL61840.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL61840.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OAL61840.1}.
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DR EMBL; LHPM01000019; OAL61840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EP59; -.
DR VEuPathDB; FungiDB:TERG_02940; -.
DR Proteomes; UP000243015; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd14688; bZIP_YAP; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.10.238.100; YAP1 redox domain. Chain B; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013910; TF_PAP1.
DR InterPro; IPR023167; Yap1_redox_dom_sf.
DR PANTHER; PTHR40621:SF6; AP-1-LIKE TRANSCRIPTION FACTOR YAP1-RELATED; 1.
DR PANTHER; PTHR40621; TRANSCRIPTION FACTOR KAPC-RELATED; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF08601; PAP1; 2.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR SUPFAM; SSF111430; YAP1 redox domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000243015}.
FT DOMAIN 145..208
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 25..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 68854 MW; 9B987077E9C20144 CRC64;
MAEFDPSFQR SLYLSPDQQD LLLAALSSNN QPTKPGPQPN LGSANGSSGN DIFDSSPQDI
PDSGQLSFNP DDSPFLGLDL DAEFDVSDQA LIGDLPGIEG EQQITAEPRE KRKSLDGGEG
ADTGKKRKEN EEKVAKKPGR KPLTSEPTTK RKAQNRAAQR AFRDRKEKHL KDLETKVADL
ERASQTANQE NTLLRAHIQR LQVELKEYRK RLSWISSGNS FSPTTSLLNQ ARSLHAQSRL
NNDFSFDFPK FGDLPGAHMN NMGSLAKGSP NARSQTHPAL GIKATSHIGA TPQFTPSNGS
AFRQNGQSSS ANKGHEAPGN TYNSHHFETS PATFSESPSA SSESQHISSI CTSPESSLTS
PTIAQKGDAS NSTQANGNGN AKKNSPSQCE LKFYQQLGEA CGCVDNPIPA ALAKKSSQGS
TNPKSPENAV STLSPANSTP NMSTSTASEN TNNTQTASDP SGNGSATASS NALSDQSIPS
FDWLAQQNGG HFDPVLFGDY RDPQDAVLSQ DFSGFFDDAF PLPDLGAFDA ATPGSTAKTP
GKTDAPVTTV DIDDDEEVVP GEDRSQMLSC TKIWSVPTVK SVDSNDSSSN PASRDRLQRL
EKFRNGEIDV DNLCTQLRTK ARCSEGGVVI DQKDVDDIVT RAI
//
