ID A0A369GUD1_9HYPO Unreviewed; 1542 AA.
AC A0A369GUD1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=MIF4G domain-containing protein {ECO:0000259|SMART:SM00543};
GN ORFNames=CP532_1632 {ECO:0000313|EMBL:RDA87486.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA87486.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA87486.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA87486.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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:RDA87486.1}.
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DR EMBL; PDHP01000022; RDA87486.1; -; Genomic_DNA.
DR STRING; 2039875.A0A369GUD1; -.
DR Proteomes; UP000252748; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR Gene3D; 1.25.40.180; -; 1.
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; 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; PF02854; MIF4G; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101489; Eukaryotic initiation factor 4f subunit eIF4g, eIF4e-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000252748}.
FT DOMAIN 1121..1365
FT /note="MIF4G"
FT /evidence="ECO:0000259|SMART:SM00543"
FT REGION 1..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1542 AA; 165088 MW; EBDB2B93F55012AD CRC64;
MTSPANRQNP IPATNTSATT AASYASAAGA PKKPAQAPVV ATSSQLPAAA GGVSAPFAQN
AKAASPSPVN GKTAASAAAA VSHGSSAANG STSDHTRKSS VTMAASGPNS YAANGGPVGG
SKSGIQFGYD SPAMAHSTPH VGTSAPISIP GGNPRVTSPA HSPSPIPQPS ASGGRPPSGL
QQPQGQMTFG SLSSDGERHM RQASVPPNPN PMVSQPGAHF RRESGHSVQS ENHGAPGRGN
YPPQGGRGRG GFNPHGNSYS NQMGYPPNNQ FRNGPGQGRG IPPSFQPQPR NMPYPNSPQP
SRSPALVPSM PNTPNMGSAN MQQNMPMPTP PQYHYPQPMA HQHQVHPPFP VAFSSQMHRP
RSKSSAHREH DAAASHSGRA VWELGGHDVR QHPRRHVQRA DPGRYENEMG TPSAPSDDVL
RPGLMPAPSS LTASKRIPES FDLSPENGEF ERWLTLKNQN YYPTQPMEQY GRPMPITYGY
GGMPFMAPQA NNQGYGQQYQ PPPYHPQGHA MSRSPSQPER PTSANHQNQP VIVSSAAQPP
SVQPNPAAKN FVKPRKSAAI QIKNAAGEVV DTSSFKQPAS PAPHVQQAKT PPVVSSTPTP
PPPKSSTPAA HGRTESQATP KTAKEIQEEL KEKIKQATQA SAENKPKEDK ATPKEQPTPV
EMAPTVVKSS PHVEPAAPTT ADVPRDEASA PVEKAPAVED KAADSKPSKP VEASKAADPE
EDEVERMIRE MEEADAKREK EEEEHRKRKE AEKLAAKKKA EEERNSNAAD ADRKLREQER
EMERLEEERE KKQKQAESSG KTLSVADAFA QLRSGKEPGE TAVNVDAVAE KLADTKIDGE
KQASPVEGSG QKPTPTEKRG FKPAALNLAP LITKPVEPAQ PSAALQSLKS ARFLQVMDQD
IYPAGINSPN PSLNAAVTKK GKTFKYDAKF LLQFQKVFTE QPSHEFHQQV KSLIGDGDGG
RSARAQTPGS ARQGSRGGGT TFSMGSFNAP PVRTLPPGTT SSERMAMASG TMPRPSINSI
GSFQRPGAPF PTSTPMSRTS SQSNMRNMPN SPRQSSRSTR GSRRNEFNAK DAQSAKTMPL
TAGMDIKPIT VSAGGWKPSS IGRSAQPGVT GVAYLEPEMV QRKVKAALNK MTPEKFDRIA
DQVLEIASQS KDESDGRTLR QVIQLTFEKA TDEAHWASMY AKFCKRMLDT MSPEVRDERI
KDKAGNVVSG GNLFRKYLLN RCQEDFERGW TTNLPEPKEA EGAEKKTGDA AMLSDEYYIA
AAAKRRGLGL VQFIGELYKL GMLTERIMHE CVHKLVSYKG VPDEAEIESL CKLLRTIGAN
LDQTEKGRPA MDAYFQRIQA VAELPELQSR MKFMLMDVVD LRRANWHSKE ANKGPKTLDE
VRADAEAANA AKAQEAARNS QRGGGGGGGG GRPMVGRGDG RNFSAGYVQQ TSNQVGMDDL
RRLKAASRTP SQNVMLGPTS MFASRSNSGR RMGPGGSLGR PGEDSGASSR TGTPPTRDST
TNTNAFSLLA NMETEHPASP PSAGPSPSMS KAVPVNDKKE SE
//
