ID A0A084QFT9_STAC4 Unreviewed; 1168 AA.
AC A0A084QFT9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Fork-head domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=S40285_03802 {ECO:0000313|EMBL:KFA62824.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA62824.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA62824.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA62824.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR EMBL; KL660776; KFA62824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QFT9; -.
DR STRING; 1283841.A0A084QFT9; -.
DR HOGENOM; CLU_002508_1_0_1; -.
DR InParanoid; A0A084QFT9; -.
DR OMA; HYKSDKV; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000028524; 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:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IEA:InterPro.
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; IPR045178; Fhl1/FHA1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR21712:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR PANTHER; PTHR21712; UNCHARACTERIZED; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR PRINTS; PR01217; PRICHEXTENSN.
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; 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:UP000028524}.
FT DOMAIN 420..471
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 720..793
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 720..793
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..584
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..908
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..975
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 125411 MW; 0F2D4D8483E86CD3 CRC64;
MASPSSTSIP SPLPSFCGAS APDATAEQVP SVHSGLKVEA SDLSSPATAI GTATTPTPSA
TTATATATAS ASDLAPAAST SGSQPALSSI LTASRPSTPS SNAVAATSSA IVESVNGNKP
AAPSTSHNPS DQDQPMPDAP ETIAQNLHDS ALPNLPEIDQ TQPTQEHQPQ PDDAILQTPR
RESTHSQTQF PMAATSNTML AEHDAPSTPF NPGSMLFNPE RQAYMMMALM TDQSLMPPAP
TVVTPAQVTL PHPDFHNNTL APAHTLREAA VDNGLQSFAR IEFADSIFQM TTHEVMIGRD
QRALNQARQD QKRSEQYERQ VKKNQSMGLP PPPPPVTQDR SKFSKSYVSA EGGMLGPESS
DDEDNVRVAK RRKTSTAGSS QHDDHHLEDN VISDRQYVGH TPGAAAVDLA ALKPSPSYVP
FIGIHSPGPD IASKTKAISR KHLSIRYNKE TGVFEAIPKH KNGFFCEDVH YNTEKVVLKS
GDRLQIKDVD FRFFINGVER GHTGAEDHTE RKLKSAENPS RSGKQMSFDF EQSHGSGQVQ
DTSDELSDVE VSPPELSDFG DDYGDDPEAM EDPGAYEAGE DEDPAVKDEM GPTAEPMLPQ
LPRKRGPGRP PKNGIMSKRE QRLLKKQEQE MAKKTLPQAP PVEPPIKRKV GRPRKHPLPE
DAGDRPEKRK YKPRKPKTED GAEGSEAERR AKEKKEKKAR PKSPPLELKI GDYTQEQLQK
PNKNYGVLID ETLTAAPDGL TLKQIYKRIC LRYPWFYFHT ETKGWESSVR HNLIGNEAFK
KDETTNLWSR VPGVELDAGK KRKASSPDRA LAAQGYGPYS FPYNAQPMGQ NAPGYHPNQV
PQGYQVPPYN GQPPAHVPRP PQQYGEQAAL APQPGAPTTV TAPQPQPQPQ PAPLPGYGPP
PAPARPQQVG PQPSSYSSPY TPRPPPQATA AVKSEEPHVP APSPVAGPST QPPPSLPANA
IPRTVPGPAP ATQGPSPAPV NASTATPPVN AAPKQLIEPR LLHAIVQLKN GLIGNLAKAK
NPQAEAIVMS AINRCIGLKK DSVENEKLEA ICMKGVSQVI SGAMKNRSPT PGSSSAQPGP
AHIFEPSILT HLNGFRDATV EAIGGKVGEA RAEALALSVI DRVLGLAQAS IIQPRTDGEA
AAASERLEQS MMVRLRQILN PAQPSTSS
//
