ID A0A138ZXL0_GONPJ Unreviewed; 453 AA.
AC A0A138ZXL0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Transcription factor {ECO:0000256|PIRNR:PIRNR002595};
GN ORFNames=M427DRAFT_117548 {ECO:0000313|EMBL:KXS09238.1};
OS Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC Gonapodyaceae; Gonapodya.
OX NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS09238.1, ECO:0000313|Proteomes:UP000070544};
RN [1] {ECO:0000313|EMBL:KXS09238.1, ECO:0000313|Proteomes:UP000070544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL478 {ECO:0000313|EMBL:KXS09238.1,
RC ECO:0000313|Proteomes:UP000070544};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR002595}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ965875; KXS09238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A138ZXL0; -.
DR STRING; 1344416.A0A138ZXL0; -.
DR OMA; DSVCIQL; -.
DR OrthoDB; 1117127at2759; -.
DR Proteomes; UP000070544; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProtKB-UniRule.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR014402; Sig_transdc_resp-reg_Skn7.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; HEAT SHOCK TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR10015:SF457; HSF_DOMAIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF002595; RR_SKN7; 2.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR002595};
KW Nucleus {ECO:0000256|PIRNR:PIRNR002595};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000070544};
KW Transcription {ECO:0000256|PIRNR:PIRNR002595};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR002595}.
FT DOMAIN 340..453
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 390
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 453 AA; 50667 MW; 3A221C4AFB9484E9 CRC64;
MPDDQSRRVE DDSTSRNTRS AKRRSADDAA ENQNRGNAAK GTKKAKKASK DDGEASEEGD
EFAEGVSDFV KKLYRMLEDP TSTSVAMWSP PGTSFVVTDS SDFNVKVLPK HFKHNNFSSF
VRQLNKYDFH KVKGDDGWSK VYGSQAWEFQ HPNFRRDRQD LLEQIRRKVP PHRSRAKPVN
TPTNNGSGTR NSNDVSPSSQ QPLPSATAMA SKHGELDRQH IETRRMLAEL RNENEELRRF
VIMRSDKSNH EEVARKAAEQ MDNNAIRQEV DLIMSQANAV NPTLPNTSPQ TMSESGLLSP
VLSSFPGNAI TFSANTTQSM PPKTSPNIAS GAGYLHPDGH VLLVDDDPVC RMLSARFLQL
FGCIYDLASD GSEALEYIDM GRKYDIVLMD IVMPNIDGIM ATTHIRQFDQ ITPIISMTSS
TTERDCIHYF SSGMTDILAK PFNRDSLLKV LET
//
