ID A0A395SD99_9HYPO Unreviewed; 669 AA.
AC A0A395SD99;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative mbp1-transcription subunit of the mbf factor {ECO:0000313|EMBL:RGP70396.1};
GN ORFNames=FLONG3_7467 {ECO:0000313|EMBL:RGP70396.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP70396.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP70396.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP70396.1,
RC ECO:0000313|Proteomes:UP000266234};
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:RGP70396.1}.
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DR EMBL; PXOG01000171; RGP70396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SD99; -.
DR STRING; 694270.A0A395SD99; -.
DR Proteomes; UP000266234; 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:SF15; TRANSCRIPTION FACTOR MBP1; 1.
DR Pfam; PF00023; Ank; 2.
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:UP000266234};
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 8..119
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 250..282
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 372..404
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 110..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 74665 MW; 7974C4DD69900298 CRC64;
MVKANANAAP AATAPGVYSA VYSGFGADLK EHVMRRRSDN WINATHILKA AGFDKPARTR
ILERDVQKDV HEKIQGGYGK YQGTWIPLES GQALAERHSV IDRLRPIFEY TQGAESPPPA
PRHASKPKGP KSRPPLPKWN NPPPPAPVPA PIIQEDGDTL MGDEDTPDNL TVASASYMAE
DERFELPQAP GTGRKRRRDD SSNLQDLTEQ QHALYGDELL DYFLLSKTDQ PAVKPDPPAN
FQPNWPIDAE DHTALHWASA MGDLDVVKQL KRFNASSTVK NIRGETPFMH SVNFTNCYEK
QSFPMVMKEL FETFDARDNM GCTVIHHAAV MKNGRVFNSS CSRYYLDNIL NKLQETLEPS
AFQQLLDIQD NDGNTALHLA AQRNARKCIR ALLGRNASSD LANHEGIRAE DLIMDLNATK
KDRGPQRSSS PFAPESQRHA SFKDALIEKA NRQSTVVFQS AAANTVQSRI SPLIMEKFQD
LAKSYEDEFR EKDIAESEAK RLLSNTQQEL TSVRQSITDV EGQLEPEEAA SKQATEANLA
KHQVLSLITH QNRLHVQRAV DSELSRINGE GGGQEESYDK RLRLARELSS LLAEQRKAEA
EYVEALSMVG TGDKIEKYKK LLNRCLDPKE AESLDTNLDS LIEMMEEERD ENGMVGAMDP
EPMELSVGI
//
