ID   MIG1_MAGOR              Reviewed;         702 AA.
AC   A9YDN6;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=MADS-box MEF2 type transcription factor MIG1 {ECO:0000303|PubMed:18344407};
GN   Name=MIG1 {ECO:0000303|PubMed:18344407};
OS   Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=318829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH MPS1, AND INDUCTION.
RC   STRAIN=Guyane 11;
RX   PubMed=18344407; DOI=10.1128/ec.00009-08;
RA   Mehrabi R., Ding S., Xu J.R.;
RT   "MADS-box transcription factor mig1 is required for infectious growth in
RT   Magnaporthe grisea.";
RL   Eukaryot. Cell 7:791-799(2008).
CC   -!- FUNCTION: Transcription factor acting downstream of the MPS1 MAP kinase
CC       (MAPK) cascade during conidiation and plant infection
CC       (PubMed:18344407). Required for overcoming plant defense responses and
CC       the differentiation of secondary infectious hyphae in live plant cells
CC       (PubMed:18344407). {ECO:0000269|PubMed:18344407}.
CC   -!- SUBUNIT: Interacts with MAPK MPS1. {ECO:0000269|PubMed:18344407}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18344407}.
CC   -!- INDUCTION: Expressed in conidia but not in aerial hyphae or
CC       conidiophores. {ECO:0000269|PubMed:18344407}.
CC   -!- DOMAIN: The MADS-box domain is essential for the function but
CC       dispensable for nuclear localization. {ECO:0000269|PubMed:18344407}.
CC   -!- DISRUPTION PHENOTYPE: Leads to reduced aerial hyphal growth and
CC       conidiation (PubMed:18344407). Does not affect appressorium formation
CC       but impairs infectious growth (PubMed:18344407).
CC       {ECO:0000269|PubMed:18344407}.
CC   -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
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DR   EMBL; EU164776; ABX79379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9YDN6; -.
DR   SMR; A9YDN6; -.
DR   PHI-base; PHI:1070; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd00265; MADS_MEF2_like; 1.
DR   Gene3D; 3.40.1810.10; -; 1.
DR   InterPro; IPR033896; MADS_MEF2-like.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SSF55455; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation; Virulence.
FT   CHAIN           1..702
FT                   /note="MADS-box MEF2 type transcription factor MIG1"
FT                   /id="PRO_0000453103"
FT   DOMAIN          1..61
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   REGION          73..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..150
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..242
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..306
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..397
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..603
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  76310 MW;  73C1A60327CAC2D9 CRC64;
     MGRRKIEIKA IKDDRNRSVT FLKRKGGLFK KAHELSVLCS VDVAVFIFGT NKKLYEYSSG
     DMRELITRYT YHGGATEHKG PSDFNGGDDD DEEEGDGTPP LDQPMDAHMM PPHFQGQGPF
     PPHVMRHYTP SASPPIPNGV PFPPHGHGVP RGHTPQPQML SRPGSRNDAR RMGQPMGPQG
     SPQVNGFGFG QQQSMYGPPN TTMPPHMPPQ MAPGPPFPYP QHPQHPPHPP HPPHPPHPQQ
     PHQPQMQQQF IEDGRRATMP ANFAPHPPPP HGPMGMQRHS VSPPQQHPHH VPQLPPQQPQ
     QHPHSSPPQP QHHQMQSPPQ PMVKFESPQQ IEPPQHQHQQ QPEPQEPRPE QQQQQQQSQQ
     SQQPQEPQSE PARSLPPPPP PLEVKTELAP PAQPGRIPQP SLLDTAVKKL PRQKQHSIFT
     PIDENRSILS QHLAAFHAEP SKNKSSPPAH HRSSSVDEST SNASEASRGK DKDIASSPPL
     LKRADPRASI SSVSSAPESA PAPPSRSNSL RAGPPRPRLK VQIPDEQSED GSGSATAESA
     SSAQGGASTD ATSQSTRQND SHSSTNMVLP PPSPSASALL SAGATGPPNP FAPKRPPQHP
     APGLNIDTPV SALPSRFLNN EFLPSPSSFY PDWNFRGGDN NTLPSPLNFA TPVVGTGPSF
     LRDENPGASL KRKSPDNLSI HGPISDNPLE AGNEPKRVKV DS