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Database: UniProt
Entry: A0A3B4AZC5_9GOBI
LinkDB: A0A3B4AZC5_9GOBI
Original site: A0A3B4AZC5_9GOBI 
ID   A0A3B4AZC5_9GOBI        Unreviewed;       750 AA.
AC   A0A3B4AZC5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Forkhead box protein P2 {ECO:0000256|ARBA:ARBA00040052};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000022632.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000022632.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   AlphaFoldDB; A0A3B4AZC5; -.
DR   STRING; 409849.ENSPMGP00000022632; -.
DR   Ensembl; ENSPMGT00000024104.1; ENSPMGP00000022632.1; ENSPMGG00000018268.1.
DR   Proteomes; UP000261520; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd20065; FH_FOXP2; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR047412; FH_FOXP1_P2.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR032354; FOXP-CC.
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; PTHR45796; FORKHEAD BOX P, ISOFORM C; 1.
DR   PANTHER; PTHR45796:SF1; FORKHEAD BOX PROTEIN P2; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   Pfam; PF16159; FOXP-CC; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          490..563
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        490..563
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   750 AA;  81326 MW;  BD1998C9CF99E990 CRC64;
     MMQESATETI SNSSMSQNGL SSLCSNQLEA GSRDARSSGC DTSSEVSTVE LLHLQQQQAL
     QAARQLLLQQ PGSGLKSPKS QDKQRPLQVP VSVAMMSPQV ITPQQMQQIL QQQVLSPQQL
     QALLQQQQAV MLQQVQTLTH KYTRTEGSNS GQQQQQQQLA AQQLVFQQQL LQMQQLQQQQ
     HLLNMQRQGL LSLPGPAPGQ AALPGQALPP PGGLSPAELQ QLWKDVTGGG GHGLEDNGIK
     HSNSTGPGAA GGLDLSTNNT NTTTSSNPAK ASPPITHHTL ANGQSPVLNH RRERERERDR
     ERESSLHEEN GGTHPLYGHG VCKWPGCESI CEDFGQFLKH LNNEHALDDR STAQCRVQMQ
     VVQQLEIQLS KERERLQAMM AHLHMRPSEP KSSPKPLNLV SSVTMSKNLP SASPPNLPQT
     PTTPTAPITP MAAMPQVPSV LGGANVPSMG AMRRRHADKY SMPLSSGGDT VFIFPEIAPN
     YEFYKNADVR PPFTYATLIR QAIMDSADMQ LTLNEIYSWF TRTFAYFRRN AATWKNAVRH
     NLSLHKCFVR VENVKGAVWT VDEMEYQKRR SQKITGSPSL VKNLPSSLGY GTALNASLQA
     ALAETSLPLL GNPALMNSGS TGPMGCHGLL GGDPSGLAGS PPGLLGGSPP GLLGGSPPGT
     LRGSPPSLLQ STHEELNGTL DHLDTNGHSS PGYSPPVHMP PVHVKEEPLN MDDEDCPMSL
     VTTANHSPEL EEERDLEEGN LSEEGRTWSD
//
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