ID A0A2C5Z5C7_9HYPO Unreviewed; 618 AA.
AC A0A2C5Z5C7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=FHA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDD80_983 {ECO:0000313|EMBL:PHH77045.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH77045.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH77045.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH77045.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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:PHH77045.1}.
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DR EMBL; NJES01000136; PHH77045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5Z5C7; -.
DR STRING; 2004952.A0A2C5Z5C7; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000226431; 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}; Reference proteome {ECO:0000313|Proteomes:UP000226431};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 119..183
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 299..395
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 299..395
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 66912 MW; 6B2BABD2235B796B CRC64;
MPLSAKRSQR VRRDLRNKDR AVDADAEPDQ SSPSRPTKRR KKAPSPDGGA STAAVDPDET
RGTDDDQVVS QVTQHLKSQP VQAAKDHANA IYEANKDGVK AYAKVAAQDW TFYITKLSVN
IGRASELPQT EDDHCDQLQV NIDLGPSKMV SRDHAAIIFD PKDQKWLLEV KGRNGAKIDG
QLLKPHGSRS LTSGQVIEIA NVEMMFVLPS EISPLHVHSS FLKRCGLAPE LSSQPTALHK
HTPGTSADSG YVRPGTPPSV QRQTGPSTGK SPFAAASTPA VVMGPHGVDL SHDDCQHIKP
QYSYAQMITQ AIDNAPDGKL NLNGIYTFIT KNYSYYRHQQ AAGWQNSIRH NLSLNKAFDK
VARSTDEPGK GMKWQIVADA KEDMIRNAYK LGRGGHRGSS APSSPNQLNY VTHGPRDMAL
REPLSIRKHQ GSPLASPPPR PLTQSTPERV GGRRATLIAD GSPLPRQRKA GAAPNSSLSA
FSLQSPTLTS SFLQDDGPSL VTPAPPRIHP KLAPPSTAQR PSQHMPTSSP APFWKYAEIG
STPLRPTQYE ASPSKVAGRI PSNSSSPPCV GKSPPSSPLR PQKSAITHDH VEAAETTEEQ
GFDLTKLAPV QYTLRNIG
//