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Database: UniProt
Entry: A0A0C9ZSI3_9AGAM
LinkDB: A0A0C9ZSI3_9AGAM
Original site: A0A0C9ZSI3_9AGAM 
ID   A0A0C9ZSI3_9AGAM        Unreviewed;      1542 AA.
AC   A0A0C9ZSI3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=MI domain-containing protein {ECO:0000259|PROSITE:PS51366};
GN   ORFNames=PISMIDRAFT_11424 {ECO:0000313|EMBL:KIK22713.1};
OS   Pisolithus microcarpus 441.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK22713.1, ECO:0000313|Proteomes:UP000054018};
RN   [1] {ECO:0000313|EMBL:KIK22713.1, ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|EMBL:KIK22713.1,
RC   ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000256|ARBA:ARBA00005775}.
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DR   EMBL; KN833736; KIK22713.1; -; Genomic_DNA.
DR   STRING; 765257.A0A0C9ZSI3; -.
DR   HOGENOM; CLU_002459_2_0_1; -.
DR   OrthoDB; 92033at2759; -.
DR   Proteomes; UP000054018; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.180; -; 2.
DR   Gene3D; 1.20.970.30; eIF4G, eIF4E-binding domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR022745; eIF4G1_eIF4E-bd.
DR   InterPro; IPR036211; eIF4G_eIF4E-bd_sf.
DR   InterPro; IPR045208; IF4G.
DR   InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR   PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1.
DR   Pfam; PF12152; eIF_4G1; 1.
DR   Pfam; PF02847; MA3; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   SMART; SM00544; MA3; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   SUPFAM; SSF101489; Eukaryotic initiation factor 4f subunit eIF4g, eIF4e-binding domain; 1.
DR   PROSITE; PS51366; MI; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054018}.
FT   DOMAIN          1409..1530
FT                   /note="MI"
FT                   /evidence="ECO:0000259|PROSITE:PS51366"
FT   REGION          1..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1238..1400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..325
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..438
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1327..1341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1355..1371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1542 AA;  167417 MW;  58BBC0B0F5E0A80E CRC64;
     MSKGSTASGK TPTQLPSQSA WARGPPQNNS SAPSTRSQSP APSHVQSITA SHSRRPSALG
     QGVPVKEGVS VPRNNVGSVR QGSSLNFGSI DDASAPVSSS PTATPVVRHE SVKTFGSLPV
     TTAPTSNIVN GKTPASGPTP GSLKSSSRHT AAPSISSSIS AAASSSSVST TMTSSMAPAS
     VANITPSTSS SGTSSTSTPS TSAKPAFNVA KLFQGNPSAS QPSSDATSPS SRPSNLPHQS
     SSAGQHAQQP PVQAPSLSAH PYTPFTQGMR PPRGTSGPGS PAFSRAAPNG TGPQSRPISG
     PGGPGGPPMP ASPRLGPPAH PHAPSSAGVP PQQLPMQHMP WPYYYMDYQT TPWYYPMQPP
     HGMGHTPHAP GPTPQGPPHP GIPLSPRNQP PPLPPGTPSM AHAVPHSPHT PQPPPPHVHQ
     PSASVSSMSP PPPTPSTATA PGGRSLNTNA TTFVPTSTRS HKITIKSEDG KEVKLESLKK
     PSPQPSTTPI PPPSPVAANR RTASVRIESE EAKRKREEQA RLEQEKQEAE DRAKREEEER
     KRKEEEAAKR REEEEEEKKR KEKEEEEERA RKAEEEKLRQ EEERKRREEE ERLEEERRIE
     ERVREEKERV ERERREREQA ELEEKERAER EAERQRQEAE AETQKDGDIV ESPTQEPLEV
     EEGEVIENGE VLEPQINGAS NLSKSQKESL RIDTSELARR RPGPLDINAA KKDSSAPPLS
     ALLTARNIDR LEEVEYPEGI RSPKTELNQN VKDGKFRYDR DFLLQFMAVC KEKPPNLPPL
     DILGIEPVEQ SAFGLSRGGS GRHRQPSAPM SATGARSASI GLGIGPFKPG PPPGPFAMGQ
     FGTPGTKLTS EERFLMSQGV RSASVGTGPA AASLLSRPAL TRTPSQGGPG GHPMGGHRVR
     SKRGEKRADP GKVGSVQQGQ GFGPGAFPSG PALEPVAPLE ASANRWVPAS TQRRGAAEGD
     TPDVVDRKVK SLLNKLTMEK FESISDQIIA WANKSENEKD GRTLIQVIRL VFEKATDEAN
     WSEMYARLCR KMMETISPKV QDDGIKNAEG KPITGGQLFR KYLLNRCQED FERGWVAKEA
     TARAAAAKAS DDEAIKAANE KTGNESELYS DEYYAAQKAK RQGLGLIKFI GELFKLQMLT
     ERIMHECVKK LLGNVENPEE EEIESLCQLL RTVGQLLDVP KARAHMDVYF QRMRELCKSQ
     NVSPRMQFML QDVIELRDRK WQPRNVVNAP TTLAAVHEAA AKEKAAQESQ ASQRQFSMSR
     GGSRRGAERN VEPAPDGWAV AGGSQPRPPT KAGDLSHFGK ISKASPMVMG PSSVFAGKKD
     NKRESLTRTN SSSNMFSMLS QNPELVIEPK PSRAPSRRPS TDMDKPEPVP QRRKLQLLPR
     TIPAPGETPP PTSEEEPEGA LAAQMSEEDA KKKIDEDVKE FFAVRNLEEA DAYLTALTEE
     HRFRLVDKLV SSALESKEAD ARLVADFFSR SASQQECSPD VFEAGFTPMV ELLDDIAIDA
     PKAPEYMAIM LKGAGLDKDE ERLKRMAEKM MDSDMLLQLV SS
//
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