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Database: UniProt
Entry: A0A1B9G2Y5_9TREE
LinkDB: A0A1B9G2Y5_9TREE
Original site: A0A1B9G2Y5_9TREE 
ID   A0A1B9G2Y5_9TREE        Unreviewed;      1578 AA.
AC   A0A1B9G2Y5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Translation initiation factor 4G {ECO:0000313|EMBL:OCF25387.1};
GN   ORFNames=I302_05206 {ECO:0000313|EMBL:OCF25387.1};
OS   Kwoniella bestiolae CBS 10118.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF25387.1, ECO:0000313|Proteomes:UP000092730};
RN   [1] {ECO:0000313|EMBL:OCF25387.1, ECO:0000313|Proteomes:UP000092730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF25387.1,
RC   ECO:0000313|Proteomes:UP000092730};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) 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; KI894021; OCF25387.1; -; Genomic_DNA.
DR   RefSeq; XP_019046457.1; XM_019191827.1.
DR   STRING; 1296100.A0A1B9G2Y5; -.
DR   GeneID; 30209605; -.
DR   VEuPathDB; FungiDB:I302_05206; -.
DR   OrthoDB; 92033at2759; -.
DR   Proteomes; UP000092730; 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; 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   Initiation factor {ECO:0000313|EMBL:OCF25387.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:OCF25387.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092730}.
FT   DOMAIN          958..1219
FT                   /note="MIF4G"
FT                   /evidence="ECO:0000259|SMART:SM00543"
FT   REGION          1..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1074..1103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1244..1314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1346..1422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..419
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..617
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..825
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1074..1102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1293..1308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1387..1412
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1578 AA;  166832 MW;  1C1B17E8726807E5 CRC64;
     MSKTTTPNVN QASGKASAPT STSSAWSRGP PTASATSTPI PSNPASGSNT PAQSNPSLPN
     GVNSQSSASN GPNPVPIAGG GHSRKSSMLV GGGMDIKRGS IAFGTVDHPN PMLSSSPAAP
     STTGSHLSDA VKSFGSIDAD ASNDSNAVKT KRMSSLGASS ATSPVPGPGA VPPKKNLDLH
     SLFAGKPHPQ SPAPSTMSPQ PQQAVPPTHD RRQSMGQSGF QPGPNGLPGS PYTGAPHLRP
     PVSGLPNQQR SPVLNQAIPP NQFNPSAPTH VQQGFRPPQQ GGMPPQQAPV RPNGVGPQGV
     PRPGMMMGPG GMGAYGMHPG PQGPGYPMMQ YPQQNYYPGY NPYEQQQYNQ QWAPQQHPQN
     QQYNSGYNSG QQQAGPMSPR AAQGQLPSTQ SPMPPSATLP SSGGASPVPT PPTRPPSLMS
     GHQPTPSNAS NASIPVTPQR PMPPTFTPQQ AQSPSTPGFP PHLSGAAVAF TPRRSTAAIK
     ISRPDGSALD LKAEAAAKAK TSPVPSSGAG TPELGSEAAA PQPAEAPKKK LALPIVVRIE
     SEEQKKIRLA EEADKEKLRL TEEREEKERQ ERKEKKAKEE EERKAKEAAE KAEKEKSEKE
     NKEKADAEAE KKKLEQAFAA EQAAAEKAAA EKEANAKALR EHTEKSEQEK AAAHAAAQEA
     REKADDQRRA LMTPVASTPP SPLASPALGA GLPAKPVAAI NGARRPPPSA LDLKPSSPSL
     ADESPSASQS ALNTAKPIED LTSIVYPAST KSPQPQLNVG AEPGKFRYDR DFLMQFMGVC
     REKPDSLPPL EEIGLEADAS SGFGNRGSRG GRNSMGPSSR SVSGAPTGLG IGGINRPAFP
     GQGMGSFGMG QFGSGSGSLR GTTSEQRYQA TLRAGSMGRS PSQGGPGMPG MAGLPSMGPS
     TSRSGASRGS QRGTKRAPQE PRASLSQEPA PPPLQVSGNA WTRTRLGGDD EGSPAFIERK
     VKSLLNKLTE EKFDGISKQI LEWANKSQNE TDGMTLKLVI KLIFDKATDE AHWSAMYAKL
     CRMLMVEVDP NVTEVLEGKP TSGGVLFRKY LLGRCQMDFE SGWKAREDTA VAAAAKSEED
     KERLAKQQKD KEAAEKEGGA EGESEAVMMS DEYYAAQKAK RRGLGLVQLI GELYKLEMVS
     KGVIRQCLIR LLGNVTDPDE EDIESTCKLL STIGEAYDRA APDNMNTVFE RLQQVVNSES
     ISSRIKFMIM DIMDLRKAKW KSRNKQAGVM TIAEIHQQAA QEKAAAAAQA AQGSISRGGS
     RAGRARDGPQ PGEWQSVSAN PRAGLGRPAD FSNIGRNISS TGMPSAPTFG PSSVFARKGK
     AGAAGTVTPP LSRQPSSANM FSALNDASEA APAEGRRGSA DASEPAPQRK KLQLAPRTKP
     LPGDGEEGEG EGEGEEEEGE EEEEEEEETP AEEASAPKEL TEAGAKLKIT SDMKELWGEK
     DQGGSRDPED IAEYFRTLPE IRRHLLAERL LEDVFRIAKE KDAKVVAKGW KAALEADVVT
     SDVLRTAIEA RMPSLDDDSL DFPAAYKAIG FLIRPLSLSP EEVSALGDKI DVYGEPKITP
     KQKLEKAIGQ VAEEEASA
//
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