ID A0A3B3QLM6_9TELE Unreviewed; 909 AA.
AC A0A3B3QLM6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
GN Name=EIF4G2 {ECO:0000313|Ensembl:ENSPKIP00000006475.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000006475.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000006475.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B3QLM6; -.
DR STRING; 1676925.ENSPKIP00000006475; -.
DR Ensembl; ENSPKIT00000030502.1; ENSPKIP00000006475.1; ENSPKIG00000022719.1.
DR GeneTree; ENSGT00940000154675; -.
DR Proteomes; UP000261540; Unplaced.
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; PF02847; MA3; 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 Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 547..670
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 724..906
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 25..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..537
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 102919 MW; 2B82D32E2225D673 CRC64;
MLPRPKHSAI WNDCSHECFV RSASSGGGGG RGAPQHYPKT VGNSEFLGTA PGPSVQRWVP
SRSTRRDVNS SNEKERHDAI FRKVRGILNK LTPEKFDKLC LELLNVGVDS KLILKGIILL
IVDKALEEPK YSSLYAQLCL RLAEDAPNFD GPSPEIQTSQ KQSTTFRRLL ISKLQDEFEN
RTRNVEIYDK HDNPLTTEEE EQRAIAKIKM LGNIKFIGEL GKLDLIHESI LHKCIKTLLE
KKKRIQLKDM GEDLECLCQI MRTVGPRLDH EKAKSLMDQY FGRMRSLMSN KDLPARIRFL
LQDTVELREN SWVPRKAFID NGPKTINQIR QEAVKDLGVF IPQMVPGMRT DFFLEGPFMP
TRVKLDRESL GGLADMFGQM PGSGIGTGPG VIQDRFSPTM GRHRSNPLFN GHGGHITPVP
QSQFDIGAKS FMKSSQGQNQ HFHNQNQSHL VQQPAQSKDM PPRFIKKGQL NADEISLRPA
QSFLLSKNQV PKLQPQIPTM IPPSAQPPRT QTPPLGQPPQ LGLKTNPPPI QEKPPKSSKK
PPPAKEELIK MTETIMTEYL NSGNVGGAAS SVREMKAPKH FLPDMLSKML LCSLERSDED
KEHTSTLVYA LRAEGLISGD NFLQAFLNVL DQCPKIEVDV PLVKSYLAQF AARAIIAELI
SLAELAHPLE NGTHFPLFLL CLQQMAKLND REWLTDLFQQ SKVNMQKMLP EIDQNKDRML
EILEGKGLSF LFPLLKLEKE LLKQIKADPS PQAIYKWIKD NISPKLHTDK GFVNILMTSF
LQYISHEMCF SGDDQLSAPT KDQLDQEKQL LLAFKPVMQK FLHDHVDLQV SALYALQVHC
NATAFPKGML LRYFVNFYDM EIIEEEAFLA WKEDITQEFP GKGKALFQVN QWLTWLETAE
EEESEEEAD
//