ID A0A318ZUN6_ASPLB Unreviewed; 696 AA.
AC A0A318ZUN6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Forkhead transcription factor Fkh1/2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO96DRAFT_196902 {ECO:0000313|EMBL:PYH51266.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH51266.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH51266.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH51266.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR EMBL; KZ821382; PYH51266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZUN6; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR CDD; cd00059; FH_FOX; 1.
DR CDD; cd22701; FHA_FKH1-like; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45881; CHECKPOINT SUPPRESSOR 1-LIKE, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR45881:SF1; FORK HEAD PROTEIN HOMOLOG 2; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 125..198
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 335..425
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 335..425
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 76299 MW; A375426E28B01A03 CRC64;
MPLSNRRRAR RKEIQLQETS DAEAPDSSPT RPSNKKRKID HRASPQPRPV KQESADEADD
SSPDQELSEN QDLVDMVISY LDAAREEVRV LRDHSNAKTE NKQSIRAYAK IAGRNWTYYV
KTLHVNIGRE PDREQKLDEQ SSPVTIAARA LPEVNVDLGP SKFVSRLHAE IFYDGEETAS
WHIRVNGRNG VRLNSAILKR GTDAILSCGD IIEIANTQMM FVTPGDKANI HPSFVERAQR
LANGEEDVAT WDASQHAHPQ PPSTTATADA APVTTGAPSL APAPQFLKRQ VTPPPRSPDT
VGARTAKQSP LYNRGMMMES TEEIDYSKDA AKDLKPPYSY ATLIAQAIFS SEEEKLTLNS
IYNWIMDKYA FYRHSQSGWQ NSIRHNLSLN KAFQKVPRRT DEPGKGMKWQ IAPEYREEYW
KKQLRKGTQS SAPSSPATRD PAARGANGME AVFSATKKSP PVSSPGFSSF PVAPIEAYTP
ERGSRAARNG TGAPLRPSNT RDYEEPSPLP TRSATKNTSN GTSLSRTYGL SDNIAGSPPV
LSSSYYDDGP SSMITPAPQR QQPRLPPPST AQIPSKFMPM SSPAQFWKFA DIGSTPARPV
PDMSPLKGDP GDGLGSIPSS SPPPPNLASP SKPGTANGMA TGRMPPRREP ETKNERPDEE
DDEEEGSGFD LARGFQTIGS YHRQLSNAAR ASAATS
//
