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Database: UniProt
Entry: A0A167E1M1_9PEZI
LinkDB: A0A167E1M1_9PEZI
Original site: A0A167E1M1_9PEZI 
ID   A0A167E1M1_9PEZI        Unreviewed;       982 AA.
AC   A0A167E1M1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Transcription factor {ECO:0000313|EMBL:KZL84597.1};
DE   Flags: Fragment;
GN   ORFNames=CI238_07187 {ECO:0000313|EMBL:KZL84597.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL84597.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL84597.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL84597.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TEC1 family.
CC       {ECO:0000256|ARBA:ARBA00008421}.
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:KZL84597.1}.
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DR   EMBL; LFIW01000856; KZL84597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167E1M1; -.
DR   STRING; 1573173.A0A167E1M1; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   Gene3D; 6.10.20.40; TEA/ATTS domain; 1.
DR   InterPro; IPR000818; TEA/ATTS_dom.
DR   InterPro; IPR038096; TEA/ATTS_sf.
DR   PANTHER; PTHR11834:SF0; PROTEIN SCALLOPED; 1.
DR   PANTHER; PTHR11834; TRANSCRIPTIONAL ENHANCER FACTOR TEF RELATED; 1.
DR   Pfam; PF01285; TEA; 1.
DR   SMART; SM00426; TEA; 1.
DR   PROSITE; PS51088; TEA_2; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          182..265
FT                   /note="TEA"
FT                   /evidence="ECO:0000259|PROSITE:PS51088"
FT   DNA_BIND        182..265
FT                   /note="TEA"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00505"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZL84597.1"
SQ   SEQUENCE   982 AA;  110330 MW;  5E62ECDDC0367EA9 CRC64;
     LSRNPFTIQS KPLPGEKEED EERSKFYAST NPHTITSWKE SPATQDIAAI YSRNAQMEHP
     RPMLPSQRYS PSPVYSYDSR RCTPTGRQPL KESTGNAQSA GSHLGSLASS CRNSPLGLFS
     PSLTNIPTPP IVPSQAGTGY RSSSSLRRPD AFHMARQARL DINPIYLAPE FRPYREKQDQ
     KDPNEKQIWP RVLEDAFLDS LLIIPHMGRK KYSMQGKQFG RNMLISEYLW IAYRCSLQPG
     QKPEERKRKQ VSSHIQVVKK MFEKHRCYHF FFVKDPDKSE ARLKDNMEVA SFKDNPVLIA
     LAEGRLPDVR PNYEYFRQIL GMDSLVAMRP KTAWIFVASN NVRMDEDGEA YDHHGKLLDK
     NYYPHLEKNM HKEDGTSRGL NGSILLHEYN KELSQKESAA VTELAQEWEA KFPPLHKSLE
     HAIHDNKWLD ILEMTVTLEI HPRSNFPTGS ELNGFVELNI SRPELQNHRW KCVTKLARPE
     ELRRADNDAF VVEQTSEVGV QYTHRPGCQE NKFECDCRSR PRQDVRVPFP AAEWASILST
     CAGYLEPVEN KSKIEDDDER AKVAEDAALE AERTTAELIQ QVGMFQELWS APPDNSDRRV
     WTRRGIILWK FRTIHAFDDK WNPIFEKPVP QKGRKPTDED GEEQGTSSRR GGRSKRVFNP
     AGTTWRFLTA LDPVSSAHQQ NVCINPAAAS GRDMLMAPTP PYSHQLAAVM NDNLSSAWES
     VSMPGQLPSL ASTGTLGMMD NFSHGLATPP PTASIHSSYA SSYDGSHELA GGPHHHHHQL
     DFLAAACTSS MDNQSTLVTD MGSAPADPFL SATAGIQVSN GVGVGVYDEG EVDGISDWDT
     ATSSFQSLNH WNGWNESSDA KTQQWQNENQ RSVTANANLW AESKDHQTWN QQPWAQAVSA
     VAAVAGTDGR SGWSPVDQQR GLPSLDQISP LKSMAGRKRA RSSSLDMENR ENYPATAIQK
     LVHHRAPAAV MDEGGHGYRS WE
//
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