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
//