ID A0A395S5W3_FUSSP Unreviewed; 794 AA.
AC A0A395S5W3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=HTH APSES-type domain-containing protein {ECO:0000259|PROSITE:PS51299};
GN ORFNames=FSPOR_5999 {ECO:0000313|EMBL:RGP67439.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP67439.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP67439.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP67439.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RGP67439.1}.
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DR EMBL; PXOF01000081; RGP67439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395S5W3; -.
DR STRING; 5514.A0A395S5W3; -.
DR Proteomes; UP000266152; Unassembled WGS sequence.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:UniProt.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR43828; ASPARAGINASE; 1.
DR PANTHER; PTHR43828:SF3; REGULATORY PROTEIN SWI6; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 26..134
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 366..398
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 513..545
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 188..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 86302 MW; 97C2E737FD9682BB CRC64;
MSQQSQSGMG NSFRGGYNGD PDNSGIYSAS YSGVDVYEME VNSIAVMRRR NDSWLNATQI
LKVAGVDKGK RTKILEKEIQ TGEHEKVQGG YGKYQGTWIK FDRGLQVCRQ YGVEELLRPL
LTYDMGQDGG VAGRGDFNTP TKEQAMAAQR KRLYNQSADG RANGVSGTFF KNISTTASHA
VAAISKARFD SPGPRSSRNG ASRTASFSRQ ASMQNGDDFP SNSQQSFASD YGQQVDSAYS
TQQANNSVQM TEPDPPRKRQ RVTMTPAESF NGYGQNMDMY AAAYPGSPTE PNESFMYTQS
AIHDRSPMEE GNGPLPPLPY EMSPDVENKR NVLMGLFLET SGTDPTKNDT LRGFTPLELD
MPIDLQSHTA LHWAATLARM PLLRALIAAG ASPARVNASG ETALMRACLV TNSQDHNSFP
DLLEVLGGTI EARDHKGRTV LHHIAVTSAV KGRNAASRYY LESLLEWVVR QGSAPNSQNA
QTNGNGPSNS QAASPKMGIA RFMSEIVNAQ DSVGDTALNI AARIGNRSII SQLLEVGADP
NIANRVGLRP LDFGIGSENA ENKTNGETNV ENGAVGTNQR SRESSDEIVA SISHLLSETG
STFQAEMKAK QASLDTLHST LRTTSTQLGE ARRSLEHLSA TLKKQQLAKQ KVANLSHARE
AEQVRLMQEQ SRASQPNPSS SWETELSAML EAADDTSDGE FGNEGLLPSA AVLEARVRAV
KKRCESTRKM VSALKGRSRD TEVKYRRVVA LCTGVQEDEV DAVIDGLLKA VESEQEELEI
NRVRRFLGGV EGVH
//
