ID A0A1Q5TGD7_9EURO Unreviewed; 719 AA.
AC A0A1Q5TGD7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Fork-head transcriptional regulator 2 {ECO:0000313|EMBL:OKO99307.1};
GN ORFNames=PENSUB_8694 {ECO:0000313|EMBL:OKO99307.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO99307.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO99307.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO99307.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC 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:OKO99307.1}.
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DR EMBL; MNBE01000664; OKO99307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5TGD7; -.
DR STRING; 1316194.A0A1Q5TGD7; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000186955; 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; cd20024; FH_FOXJ2-like; 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 SMART; SM00240; FHA; 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}; Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW 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 336..412
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 336..412
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..700
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 43..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 78742 MW; F334237673A47055 CRC64;
MPLSNRRRAR RKEIQLQETS DAEAPDSSPS RPSAKKRKVD RRASPTRTAV KNESADEAED
SAGEHDQSAH QDIVDLVISY LNTPREELRV SRDHSNTKTE NKQSIQAYAK IAGRNWTYYV
KTLHVNIGRE PDREQRSTEQ SSPVTIAARA LPDVHVDLGP SKFVSRLHAE IFYDGEETPA
WHIRVNGRNG VRLNNVILKR GADAILHCGD IIEVANCQMM FVTPGDDANI QPSFIERAQR
IASGQEPDPA SQAWDASQHA HPSASQATEP IRPSSSGGPS LAPAPQFLKR QVTPPPRSPD
TAGQRTAKQS PLYNRGMMME STEEIDYSKD SAKDLKPPYS YANLIAQAIF SSEEEKLTLN
SIYNWIMDRY AFYRHSQSGW QNSIRHNLSL NKAFQKVPRR TDEPGKGMKW QIAVEHREEY
RKKQMRKGTQ SSAPSSPATK EPPSSARGTH VVALDTSFSA TAKKSPPVSS PGFSSFPVAP
VEAYTPERGS RGGRGVGSDH PLRHMNPRDY EEPSPLPARS HNGNTNASSS RVQNSSNSLS
RAYGLSDNVA GSPPVLSSSY YDEGPSSMIT PAPQRQQPRL PPPSTAQIPS KFMPMSSPAQ
FWKFADIGST PARPVPDMSP LKGEPDERII GGFPSSSPPP PNLVSPSKPG TSNGLGSSRT
LPPLQSDGPS DLGGHGPIKE ERMHEEDEDD GGGFDLARGF QPIGSYHRQL SNAARATAT
//
