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Database: UniProt
Entry: A0A0A2HY05_PENEN
LinkDB: A0A0A2HY05_PENEN
Original site: A0A0A2HY05_PENEN 
ID   A0A0A2HY05_PENEN        Unreviewed;       848 AA.
AC   A0A0A2HY05;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   RecName: Full=HTH myb-type domain-containing protein {ECO:0000259|PROSITE:PS51294};
GN   ORFNames=PEX2_087850 {ECO:0000313|EMBL:KGO60603.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO60603.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO60603.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO60603.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO60603.1}.
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DR   EMBL; JQFZ01000070; KGO60603.1; -; Genomic_DNA.
DR   RefSeq; XP_016601660.1; XM_016746055.1.
DR   AlphaFoldDB; A0A0A2HY05; -.
DR   STRING; 27334.A0A0A2HY05; -.
DR   GeneID; 27681475; -.
DR   HOGENOM; CLU_008791_1_0_1; -.
DR   OrthoDB; 2690250at2759; -.
DR   PhylomeDB; A0A0A2HY05; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0042162; F:telomeric DNA binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   CDD; cd11660; SANT_TRF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR   PANTHER; PTHR47807; PROTEIN TBF1; 1.
DR   PANTHER; PTHR47807:SF1; PROTEIN TBF1; 1.
DR   Pfam; PF08558; TRF; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS51294; HTH_MYB; 1.
PE   4: Predicted;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   DOMAIN          663..716
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51294"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..543
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..767
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   848 AA;  93852 MW;  6E0C3DD6F2A21D6B CRC64;
     MRPTPKPSFL LSEVDTPTSG RRFVQMVETR GVRPSFDGQE TSDFPPFPSD GGDIDQKVPH
     SLDDEEHGSP PAAKKRRTGD GPDGDISLPD DVILMADQHG PGHKIEEELA SALGEGVIDT
     VEQTDHNINQ SLQHGTLDTH DTSTGIATTQ DGTSDLNPDV ATIISEIMDH TERQEQTVAM
     GPQELPPSND FPGARGFAFL KANSHLKIQS LPILDNLSTQ ILSFLSKNTY QDLTAMVSEP
     DSENGQAYAT MRSLFDHTKR VYTVKHSFLQ PTDLEITDPS QIDVIRKANL ASFVSSIFGS
     QEIGFADLND HFLDVFVPEG GRLLKVQGAL YLELKTQAFI AAMHNKSLTR TQLLYNLFPD
     DMEQRLLARR PGTRQLAPSE TDFVNRLTSR RDILLNEINN EEALNALPDK YHWEDFLRDL
     SSYISKNFDA INTQQGKKAV KGRQPSSSNG DAHESPNTTH QGQFSLNQQV EVPVDRNMHG
     DLVARAARAA QIALQGHGLR RSQQQSQQQH QQQPQQTQSQ ASPSPLPQQP QHQQPPPQQQ
     QPQQQPSQPE NQYLHGYTAA QQPQPAHQQY HHSPTPPGGY QTQQASPLTF QQSPLQATFQ
     QYNPNAAQAM QARANGMSSN HGYMPGIPHY SQSQPTQVLY ERARMAASAK SSPTSRKSGL
     PSQRRPWTTE EENALMAGLD RVKGPHWSQI LAMFGPGGTI SEALKDRNQV QLKDKARNLK
     LFFLKSGIEV PYYLKFVTGE LKTRAPAQAA KREARERQKK QGEEDKAHVE GIKGMMALAG
     AHGAPVSGHD MSASPSLPPD ANSQSVFDQT AEQNLMQTLS QEVHGSQYPQ QHAQPTPDHI
     DPHMQLGQ
//
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