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Database: UniProt
Entry: A0A3B3QLM6_9TELE
LinkDB: A0A3B3QLM6_9TELE
Original site: A0A3B3QLM6_9TELE 
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
//
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