ID A0A3Q3NKZ4_9TELE Unreviewed; 879 AA.
AC A0A3Q3NKZ4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000034084.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000034084.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3NKZ4; -.
DR Ensembl; ENSMAMT00000034952.2; ENSMAMP00000034084.2; ENSMAMG00000022916.2.
DR GeneTree; ENSGT00940000154675; -.
DR Proteomes; UP000261640; 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 Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 527..650
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 704..876
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 474..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 99969 MW; E66249E351ECC881 CRC64;
MKVEGKHDSL VSYEVMKEAC SVLRYSITPD VCVSFCFCSA SSGGGGGRGA PQHYPKTVGN
SEFLGKTPGQ SVQRWVPSRS TRRDVNSSNE KERHDAIFRK VRGILNKLTP EKFDKLCLEL
LNVGVDSKLV LKGIILLIVD KALEEPKYSS LYAQLCLRLA EDAPNFDGPS SEIQTSQKQS
TTFRRLLISK LQDEFENRTR NVEIYDKHDN PLTSEEEEQR AIAKIKMLGN IKFIGELGKL
DLIHESILHK CIKTLLEKKK RVQLKDMGED LECLCQIMRT VGPRLDHEKA KSLMDQYFGR
MRSLMNNKEL PARIRFLLQD TVELRENNWV PRKAFIDNGP KTINQIRQDA VKDLGVFIPA
PMSQGMRMDF FLESPFMPNR MKLDRETLGG LADMFGQMPG SGIGTGPGVI QDRYSPTMGR
HRTNPLFNGH SGHIAPQPQS QFDMGPKSFV KSNQISLRPA QSFLLNKNQV PKLQPQIPTM
MPPSTQPPRT QTPPLGQPPQ LGLKTNPPPI QEKPQKTNKK PPPAKEELLK MTETVVTEYL
NSKNLTEAVN GVREMRAPKH FLPEMLSKII VCSLDRPDED KEHASTLIHT LRTEGLITGE
NFMQAFLSVL DQCPKIEVDV PLVKSYLAQF AARAIIAELV SVAELAHPLE NGTHFPLFLL
CLQQSAKLKD REWLTDLFQQ SKVNMQKMLP EIDQNKDRML EILEGKGLSF LFPLLKLEKE
LLKQIKADPS PQSIYKWIKD NISPKLHTDK GFVNILMTSF LQYISQELCV TEQLEQEKQL
LLAFKPVMQK FLHDHTELQV SALYALQVHC NASGFPKGML LRYFVNFYDM EIIEEEAFLA
WKEDITQEFP GKGRALFQVN QWLTWLETAE EEESEDEAD
//
