ID A0A3Q1J6Y7_ANATE Unreviewed; 161 AA.
AC A0A3Q1J6Y7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000030567.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000030567.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the 43S pre-initiation complex (43S PIC), which
CC binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated
CC region, and locates the initiation codon. This protein enhances
CC formation of the cap-proximal complex. Together with EIF1, facilitates
CC scanning, start codon recognition, promotion of the assembly of 48S
CC complex at the initiation codon (43S PIC becomes 48S PIC after the
CC start codon is reached), and dissociation of aberrant complexes. After
CC start codon location, together with EIF5B orients the initiator
CC methionine-tRNA in a conformation that allows 60S ribosomal subunit
CC joining to form the 80S initiation complex. Is released after 80S
CC initiation complex formation, just after GTP hydrolysis by EIF5B, and
CC before release of EIF5B. Its globular part is located in the A site of
CC the 40S ribosomal subunit. Its interaction with EIF5 during scanning
CC contribute to the maintenance of EIF1 within the open 43S PIC. In
CC contrast to yeast orthologs, does not bind EIF1.
CC {ECO:0000256|RuleBase:RU004365}.
CC -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|RuleBase:RU004364}.
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DR AlphaFoldDB; A0A3Q1J6Y7; -.
DR Ensembl; ENSATET00000031028.2; ENSATEP00000030567.2; ENSATEG00000021109.2.
DR GeneTree; ENSGT00390000008256; -.
DR InParanoid; A0A3Q1J6Y7; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd05793; S1_IF1A; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00216; aIF_1A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR001253; TIF_eIF-1A.
DR InterPro; IPR018104; TIF_eIF-1A_CS.
DR NCBIfam; TIGR00523; eIF-1A; 1.
DR PANTHER; PTHR21668; EIF-1A; 1.
DR PANTHER; PTHR21668:SF31; EUKARYOTIC TRANSLATION INITIATION FACTOR 1A, X-LINKED; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS01262; IF1A; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|PROSITE-ProRule:PRU00181,
KW ECO:0000256|RuleBase:RU004365};
KW Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181,
KW ECO:0000256|RuleBase:RU004365};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040}.
FT DOMAIN 22..96
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 161 AA; 18631 MW; C92B6EF13F885F9C CRC64;
MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGTKRLCH
IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT
FGPGDDDEIQ FDDIGDDDED IDDVSYFNFI WACKYSLTFF Y
//
