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Database: UniProt
Entry: A0A077Z5K5_TRITR
LinkDB: A0A077Z5K5_TRITR
Original site: A0A077Z5K5_TRITR 
ID   A0A077Z5K5_TRITR        Unreviewed;       445 AA.
AC   A0A077Z5K5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Transcription factor kayak {ECO:0000313|EMBL:CDW55099.1};
GN   ORFNames=TTRE_0000337001 {ECO:0000313|EMBL:CDW55099.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW55099.1};
RN   [1] {ECO:0000313|EMBL:CDW55099.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW55099.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
CC       {ECO:0000256|ARBA:ARBA00007619}.
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DR   EMBL; HG805935; CDW55099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077Z5K5; -.
DR   STRING; 36087.A0A077Z5K5; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1.
DR   PANTHER; PTHR23351:SF24; TRANSCRIPTION FACTOR KAYAK, ISOFORMS A_B_F; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125}.
FT   DOMAIN          240..303
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          196..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  48714 MW;  2912B9F8CE1F558A CRC64;
     MAANEESSFT GFKFYRELYS GLRCTMQVRT GDTSTSLLLL PLQLLRCSSL PDSEGSVSIN
     FPIMYWPSGG GGGPLDSMTT SPSVSSYSIS DVTGGGEQTR IALPSPMSLW SSSSAGSSYD
     TSDLLLKSSI PFSPFHHHQQ QATMEQSCCL HSSAGDPEPP VTYGIGEYAN RSLGVDIPWP
     VVSMVPAVGR RATKGRCRES GIDSADTDGS LVMDLSKPQR KRTGGRRPKE ESMELTPEEE
     EKRRLRRLRN KEAAARCRRR RLEHMCRLEN EVEDLLAQRD QLQEEIDALH QEKTELEVAL
     ENHLPRCHLP CGGESPSDDG LLNVGVATTS YNSDDTAVLS MQAVRHESNK SPGSDSPTES
     FLVRPKSLGI IRLGTTPDMP METPSKIFLF DPLRIPTGMT PVTHKEVDPI LNAASGYMHC
     RMDDEDDRPS SSSSSASKSK ALVTL
//
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