ID A0A137QJR0_9AGAR Unreviewed; 1340 AA.
AC A0A137QJR0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Eukaryotic translation initiation factor 4 gamma {ECO:0000313|EMBL:KXN87473.1};
GN ORFNames=AN958_08778 {ECO:0000313|EMBL:KXN87473.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN87473.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN87473.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN87473.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) 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; KQ962246; KXN87473.1; -; Genomic_DNA.
DR STRING; 1714833.A0A137QJR0; -.
DR OrthoDB; 92033at2759; -.
DR Proteomes; UP000070249; 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; 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 Initiation factor {ECO:0000313|EMBL:KXN87473.1};
KW Protein biosynthesis {ECO:0000313|EMBL:KXN87473.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT DOMAIN 1211..1332
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1340 AA; 144099 MW; A38B473184C23FBE CRC64;
MNRPSTAQIS KNPTIPRNSA WYKGPPQSSA PSRSQSPAPS TPIVQTHSRR PSALSGVSIK
DGVSVNRNNV GAAKQGSAVT FGSIDDISAP ISSSPAAAPS IKSESVKSFG TIDAETHVNG
KSALSSRPSV AVPTSTTSSS TPSPAVSVAP AAKLAKTDIA KLFQNPSSAP SPQPSSDASS
PSLRSAGLPS SQSTPSSQTP QSSAPTQPSH FTPYRHPQPG TNTGASRSPA YSTRQVANGT
GPRSQGGPNG APSQMNTGMP SPRLAPMSHN GQPPAMPPPP QMQPSMGQQM PVAWGGYYYP
GVPDQHYYPQ PQWYHPPPHP PPPGGPHGPP HAGMPISSPR NPPIGLQGGP GTPTLSHATA
TPVHQPHPPP PITHPSTSMG NITSPPPTPS STTSRLNANS SAFAPRPRVV IKKADGTEVN
IENLKPPTSS SPANNVSTNG QASTFRQGSP GTLNRRSVRL ETPEQQEKAV KAKEAEEAAK
TQQAKEDGEI DEPQQAESTP TPKEKSQAKE PLRINTSEPL KKRPERLDLS NTGSVPAPLP
SALATARIID DLSRVQYPEG ISSPNPELNA NAKDGKFRYD RDFLLQFMAI CKEKPDSLPP
LDAIGLEPID QASLAMHRTS SGRHRQASGP SAPSRQGSIG LGIGAPSGFG KPSGLNPFAG
GGMGNFQTAP KLTSEERFQL STSRSASVGG PAGMPFGRPV AMQRTPSQGG PGGMSSNRTR
SQRGKQRDGG KMAAQQAASA QATAPANFEP IVPLKVSENR WNRKAIQVDN DSPEAVDRKV
RGLLNKLTME RFDSISDQII EWANKSEKEK DGRTLIQVIR LVFEKATDEA TWSEMYARLC
RKMMEQISNK VQDDGIKNQE GKPIAGGQLF RKYLLNRCQE DFERGWVAKE ATAAAAATKA
MEDEAVKAAN DKKEGEDGEV ALYSDEYYAA QKAKRQGLGL IKFIGELFKL QMLTERIMHE
CVKKLLGNVN NPEEEEIESL CKLLTTVGSI LDTPKAHAHM DVYFRRMREL TESPHVSPRM
QFMLQDVIEL RERKWVARNA VAAPATIAQI HEAAAKEKAA QEKEYSQRQI SMSRGGSRRG
HDRNEQSQVN PEGWAVAGNA TRPPSKGVDL SNFGKISKAI PVTFGPSSVF AGKKDKRESL
SRTSSSSNMF SMLQNAESGA DKTPEAQPQR RKLALLPRTK PIEAETQQQQ ESSEDEEVSI
PAPAAEMSEE VAEKKIKEDL KEFFAVRNLD EAEVYFTALP TMHHSKLVDK LVSSAVESKE
ADAKLVADLF TRAVSKNLCS QETFEQGFVP CAEIIDDVAI DAPKAFQLFA IMVKGAELDE
ERRSRLASKS MDDKLLALLS
//
