ID A0A3Q1BTB1_AMPOC Unreviewed; 432 AA.
AC A0A3Q1BTB1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Eukaryotic translation initiation factor 5 {ECO:0000256|ARBA:ARBA00018059};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000017957.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000017957.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC {ECO:0000256|ARBA:ARBA00010397}.
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DR AlphaFoldDB; A0A3Q1BTB1; -.
DR STRING; 80972.ENSAOCP00000017957; -.
DR Ensembl; ENSAOCT00000027387.1; ENSAOCP00000017957.1; ENSAOCG00000023121.1.
DR GeneTree; ENSGT00390000016478; -.
DR OMA; YRYKMEK; -.
DR OrthoDB; 5475947at2759; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd11561; W2_eIF5; 1.
DR Gene3D; 1.25.40.180; -; 1.
DR Gene3D; 2.20.25.350; -; 1.
DR Gene3D; 3.30.30.170; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; EUKARYOTIC TRANSLATION INITIATION FACTOR; 1.
DR PANTHER; PTHR23001:SF7; EUKARYOTIC TRANSLATION INITIATION FACTOR 5; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF100966; Translation initiation factor 2 beta, aIF2beta, N-terminal domain; 1.
DR SUPFAM; SSF75689; Zinc-binding domain of translation initiation factor 2 beta; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160}.
FT DOMAIN 229..388
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 142..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 49216 MW; 96A20A9907CAD3BA CRC64;
MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKFFGCE
LGAQTQFDTK NDRYIVNGSH EANKLQDMLD GFIRKFVLCT ECDNPETDLH VNPKKQTIGT
SCKACGNRGM LDTRHKLCTF ILKNPPESND SGSASVKKEK EKKNRKKDKE NGSGSGEAGN
HDNFDAPQAV DGDDDDEDWA EETTEEAQRR RMEEISDHAK NLTLSEDLEK PLEERVNLFY
NFVKQKKESG TIDGADKEIL AEAERLDVKA MGPLILSELL FNENIRDQIK KYKRHFLRFC
HNNKKAQKYL MGGFECVVKL HQVQLLPRVP IILKDLYDAD LLEEDVIFAW AEKVSKKYVS
KELAKEIHAK AAPFVKWLKE AEEESEGSEE EEEEDDENVE VVYSSSAREL KVETVKPDTP
EKEEDDIDID AI
//
