ID A0A0M3QVG6_DROBS Unreviewed; 1489 AA.
AC A0A0M3QVG6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
DE Flags: Fragment;
GN ORFNames=Dbus_chr2Rg1922 {ECO:0000313|EMBL:ALC42343.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC42343.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC42343.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC42343.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Appears to play a role in the switch from cap-dependent to
CC IRES-mediated translation during mitosis, apoptosis and viral
CC infection. Cleaved by some caspases and viral proteases.
CC {ECO:0000256|ARBA:ARBA00037759}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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DR EMBL; CP012524; ALC42343.1; -; Genomic_DNA.
DR SMR; A0A0M3QVG6; -.
DR STRING; 30019.A0A0M3QVG6; -.
DR OMA; KIRQHDS; -.
DR Proteomes; UP000494163; Chromosome 2r sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd11559; W2_eIF4G1_like; 1.
DR Gene3D; 1.25.40.180; -; 3.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR PANTHER; PTHR23253:SF82; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 2; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 1125..1251
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 1307..1489
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 21..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ALC42343.1"
SQ SEQUENCE 1489 AA; 164159 MW; 87730989191680AB CRC64;
RYRKVITIPL TTFDAAPHLH SYDDSPIRWT NGTSNSSRSS KSRNSFDHLR GAKTFTIEGG
TSTLDTTSIG GGVNDLRLVI TAQPSDTIER NYDQLTNRGG GGGGGGAVIG SASPQSPTTP
AANPTTPTLV PGKTLLNTSP NLLPIITATD TFNNLKNLVK IDSSSNSGNG KGNGTPNSSN
YRGGGGANSN KSGIGAPRGA VTAVGSGPVS GGTVGGPSGH YSSGYNKNSA KIRQHDSELS
PRPRRTYPND SSSSSSRYYN KNSDLLGAAG NNNLNNHIGG IDSSTSSYNG GLQRGRNSYH
NSSDGATGGY QRGLSSNSSS AGSGNYRSQQ QRYELVNGNG HGHRHYNNSN GSSSSSNNNN
HQSNAGKPNY GLSGGRYRDD YNQRDNYRDR DSYADDNNSS PVHQRYNQST GGGGAATAGG
SLERNGYGGG GVGSGGRYQQ PNTGRQTDYE RRSQVGSAPP QAVAVKSVTP PPATATPGGG
SSAPVPTATI TGRWIPPSLR PQHGLTQSEK NDAVFRRVRG ILNKLTPEKF QELSDELLKL
DLNSIVILNG VILLIFDKAL DEPKYSSMYA QLCKRLSEEA PSFEQDPNNS CTFLRLLIAV
CRDKFNNRLK RDEAHDNRPP PENEADEEER RHLAKQRMLG NVKFIGELNK LDMLSKNVLH
ACIMELLDKK KKRTAGAQEM CEDMECLAQL LKTCGKNLDS EQGKELMNQY FETLERRSKS
TEYPPRIRFM LKDVIELRQN TWIPRKVGGT SEGPVPIKQI RSDDDSIIRT PFANRQRDMR
NNDRDGDNWM SRLGSHLGYN DVFSGLSVTG ASPIVSPFAT SANNRDRDRD NRSYNQRDRQ
RDQGSGNTVG NGGNVGNYNN RYNKHNNQNG GSGSHREDSR GGSHRNNDRN AMDDTRGGGG
GGQYGSGNNG GSSNTLLLGS KELAPRFKRN LMSTNQDAVE NLQMRPAANS LLFRAASQNQ
KMPTQLPIST PPNGNNSMGQ AVSTAAQLSN SHYPLLGTPT SHLMQQTTRP ASTPSAEYDT
RSLQGNQQQP QYTEKSLKST SSSPNFGTVM AAEEKKSTES GGNKEQQKID GGERPTTPIG
GKQEKKKDKG PNKEELSKKA SAYFKDKFYF DEEQSKNEEQ EFPKQNEEQS VSSDAELESK
LEDAFTTLVN GFLELKLPEK SLKDVCLQLL MEVLDRMNDV YLERVVRFLQ TLRKQSSIKP
NVIVEIFKQL VNKMNEREAL NNRITTLVAS VLSKAVVCEP PLIKLNDIAN YTDNGQHYPL
FLLVLQQLHK SIGKALLEEK FRASKVELMN SLPEVDRNKE RLAAILEDRQ LSFLYPLLKV
QAEMLKQLQS DPNPNNFYKW IKANVDNKYY KDPGFIQALM TVVVKYITKE TTLASNMDTK
EHPEKSITQR EQAMLETYSQ MLQTFLGQNE LQLMALYALQ LFCYSENFPK GMLCRWFKYL
YDSEIIEEEA FVLWKEEISD KYPGKGSALF QVNAWLTWLQ EAESEDDED
//
