ID A0A9P0LBT8_ACAOB Unreviewed; 495 AA.
AC A0A9P0LBT8;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Forkhead box protein K1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACAOBT_LOCUS18316 {ECO:0000313|EMBL:CAH1988160.1};
OS Acanthoscelides obtectus (Bean weevil) (Bruchus obtectus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Bruchinae; Bruchini; Acanthoscelides.
OX NCBI_TaxID=200917 {ECO:0000313|EMBL:CAH1988160.1, ECO:0000313|Proteomes:UP001152888};
RN [1] {ECO:0000313|EMBL:CAH1988160.1}
RP NUCLEOTIDE SEQUENCE.
RA Sayadi A.;
RL Submitted (MAR-2022) 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:CAH1988160.1}.
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DR EMBL; CAKOFQ010007038; CAH1988160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P0LBT8; -.
DR OrthoDB; 691130at2759; -.
DR Proteomes; UP001152888; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:TreeGrafter.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:UniProtKB-ARBA.
DR CDD; cd20054; FH_FOXK1; 1.
DR FunFam; 1.10.10.10:FF:000030; Forkhead box protein K2; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR047394; FH_FOXK1.
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:SF7; CHECKPOINT SUPPRESSOR 1-LIKE, ISOFORM A-RELATED; 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:UP001152888};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..38
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 210..305
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 210..305
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 75..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..373
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 53608 MW; E1E9C3DC2AF8FF8C CRC64;
MGHSSFISRR HLEVFYEHPY FYMLCNGKNG VFVDGVFQRK GAPSIRLPKT CTFRFPSTNI
RLSFQSLIDD NNCEPPPKVR DISPVRMRDR SGGGAQATLH PLRINIPDAE YGSPFPSPTG
TISAANSCPA SPRAHGGHSA NHGKRNVQAD LQMVAQYAAQ VAHRDDSHHV PPSNSPDYRQ
STSNGNAISQ VISSEGSYLS SSGGGKDDSK PPFSYAQLIV QAIASAPDKQ LTLSGIYSYI
TKNYPYYRTA DKGWQNSIRH NLSLNRYFIK VPRSQEEPGK GSFWRIDPQS ETKLIEQAFR
RRRQRGVSCF RAPFGLSSRS APASPSHVSM SDIMTPECLS REGSPSGMET SGGEASQSAP
GSPGGTMGGG GTGASYAGSG AMIGHQQMSA LVGSTKARLM LSHQGEDANG QEYREEKYVE
ERSVSPSTFS PQPVIVQAAN YSPYSGGSYG NIGLDLKRHI DDQSVGSPSS TGESLDNLQE
PDAKRPRSVG KYEVE
//