ID A0A0F7ZNK4_9HYPO Unreviewed; 525 AA.
AC A0A0F7ZNK4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN ORFNames=HIM_06798 {ECO:0000313|EMBL:KJZ73905.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ73905.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ73905.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ73905.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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DR EMBL; KQ030531; KJZ73905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZNK4; -.
DR OrthoDB; 1361169at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
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 CDD; cd14687; bZIP_ATF2; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR021755; TF_Aft1_HRA.
DR InterPro; IPR021756; TF_Aft1_HRR.
DR InterPro; IPR020956; TF_Aft1_OSM.
DR PANTHER; PTHR19304; CYCLIC-AMP RESPONSE ELEMENT BINDING PROTEIN; 1.
DR PANTHER; PTHR19304:SF43; TRANSCRIPTION FACTOR ATF1-RELATED; 1.
DR Pfam; PF11786; Aft1_HRA; 1.
DR Pfam; PF11787; Aft1_HRR; 1.
DR Pfam; PF11785; Aft1_OSA; 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.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054481}.
FT DOMAIN 410..473
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..469
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 54850 MW; B2878E14EF6966FD CRC64;
MGTSPNTASA RGPSKSPKQS NNTPPRQDRK PDAKTDTASK LESSTNAEAA KPLAPPPRPG
QQQQPQGTNT PDFFAPQAGG SLSLEPNPFE QSFGGGGAET PGGTKLPSVA ALTSPSSLLP
GSTATPFNWG GGSLRTGPLS PAMLSGPAND YFGDTHHLRG GFPTPNESSL RTGLTPGGSG
SMFPAPSPNS QALFAQLASG GATPSTIDFH RTALSAAAKR EQSNGTQQPA QTQPAVTSQP
QDMANGTAPI KSEPKPATGP FDPHDNDAAN GLFMLAQGAQ NRNGAQNGAQ FPPANTTVHA
RTAPASPPNP ETSPQMSSTH AASIDSGRGA SEGSRASDDG EQIKSYARGK GKRGSTSTNG
RRKADDPPAK NPPGKKAKSN SGAAMPSDEG SDDDMGPPDE NGNKTKMTDE EKRKNFLERN
RVAALKCRQR KKQWLANLQT KVEMFSSEND ALTAQITQLR EEVVNLKTLL LAHKDCPVTQ
QQGLHGAFMS QVVEPYNAQM NPYGMAGPMS NQQVMAGQGV QRRFS
//