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Database: UniProt
Entry: A0A3Q1EIR4_9TELE
LinkDB: A0A3Q1EIR4_9TELE
Original site: A0A3Q1EIR4_9TELE 
ID   A0A3Q1EIR4_9TELE        Unreviewed;       433 AA.
AC   A0A3Q1EIR4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Eukaryotic translation initiation factor 5 {ECO:0000256|ARBA:ARBA00018059};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000003047.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000003047.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3Q1EIR4; -.
DR   STRING; 80966.ENSAPOP00000003047; -.
DR   Ensembl; ENSAPOT00000012419.1; ENSAPOP00000003047.1; ENSAPOG00000004515.1.
DR   GeneTree; ENSGT00390000016478; -.
DR   InParanoid; A0A3Q1EIR4; -.
DR   OrthoDB; 5475947at2759; -.
DR   Proteomes; UP000257200; 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:ARBA00023134};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
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          380..433
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..401
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  49345 MW;  1DF17BE16E9D9B1C 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 EEEEEDDENV EVVYSSSARE LKVETVKPDT
     PEKEEDDIDI DAI
//
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