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Database: UniProt
Entry: A0A397GQE6_9EURO
LinkDB: A0A397GQE6_9EURO
Original site: A0A397GQE6_9EURO 
ID   A0A397GQE6_9EURO        Unreviewed;       724 AA.
AC   A0A397GQE6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Fork-head domain-containing protein {ECO:0000259|PROSITE:PS50039};
GN   ORFNames=CDV56_105068 {ECO:0000313|EMBL:RHZ50250.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ50250.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ50250.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ50250.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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:RHZ50250.1}.
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DR   EMBL; NKHU02000164; RHZ50250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397GQE6; -.
DR   STRING; 41047.A0A397GQE6; -.
DR   VEuPathDB; FungiDB:CDV56_105068; -.
DR   OrthoDB; 5385885at2759; -.
DR   Proteomes; UP000215305; 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   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001766; Fork_head_dom.
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; PTHR11829:SF343; FORK HEAD DOMAIN TRANSCRIPTION FACTOR SLP1-RELATED; 1.
DR   PANTHER; PTHR11829; FORKHEAD BOX PROTEIN; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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}; Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215305}.
FT   DOMAIN          211..306
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        211..306
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..404
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  79498 MW;  812CF5D4A76B553B CRC64;
     MNPTRSAPFV PPLSEPAAEY DKKVSQSHSQ RLGLSCPSSL PLQPPENVPS GQECILDPPL
     SSAHRPSPMK TPRGLKTSLS GRRELGFIPI TAPAPPKFTT DSPAKRTPST TYPYATSSSS
     AMPQSALFTT FPSVNHEKQS SKEKRQLAES CNDNLADFPE PSFTSKPLKR TLMDAAPLKE
     RTIKKQKRED VDLARLPNPQ EMTPIEDDGT KPPYSYATLI GMSILRAPNR RLTLAQIYKW
     ISDTFSYYKH SDPGWQNSIR HNLSLNKAFI KQERPKDDPG KGNYWAIEPG MEAQFLKDKP
     LRRATMSSLP LPVTSQREPA HTQSSSTTTW AVPPPNHSLV PKSSKNVDLS SDATIPASDP
     ALQDDTSDEG ANATTSQAPL RSSPPQPMRS SPPIAPPRFI RQGTPPTPAH PISSAIVPRS
     RKRESTTMND SGYFSSLESS AMRPKKTGHI LTSDLDIDPP RIKRGRAEEE IARIRSSSHD
     ISPRRPGMLK DAGVVIGSSP VRGEYVSMLP PPLTPVIKFK KPTKPPPSVS PNTNLRNHRK
     KIQQMVNSPL KHLGLTDEDL PWSPAFRIQD ETYTPSDHLH ATFDVFAESA EEGISTPAYG
     SPEKRSAKRA RMDPENHTGT VLADITSVSV NSKPGIQSLS SAKSKGPLFP ESPSKISEHG
     RFGDATHDDF FSFHLFDESP VEVDGVDLLQ GFQKIGSSSK DESARSKSHT SRPQLNIRSN
     TALF
//
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