EIF2A_CHICK
ID EIF2A_CHICK Reviewed; 586 AA.
AC Q5ZKC1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Eukaryotic translation initiation factor 2A;
DE Short=eIF-2A;
GN Name=EIF2A; ORFNames=RCJMB04_11n11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC number of specific mRNAs. Acts by directing the binding of methionyl-
CC tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC GTP-dependent manner. {ECO:0000250|UniProtKB:Q9BY44}.
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family. {ECO:0000305}.
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DR EMBL; AJ720163; CAG31822.1; -; mRNA.
DR RefSeq; NP_001026494.1; NM_001031323.2.
DR AlphaFoldDB; Q5ZKC1; -.
DR SMR; Q5ZKC1; -.
DR BioGRID; 685344; 1.
DR STRING; 9031.ENSGALP00000016918; -.
DR PaxDb; Q5ZKC1; -.
DR PRIDE; Q5ZKC1; -.
DR GeneID; 425042; -.
DR KEGG; gga:425042; -.
DR CTD; 83939; -.
DR VEuPathDB; HostDB:geneid_425042; -.
DR eggNOG; KOG2315; Eukaryota.
DR InParanoid; Q5ZKC1; -.
DR OrthoDB; 464990at2759; -.
DR PhylomeDB; Q5ZKC1; -.
DR PRO; PR:Q5ZKC1; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0042255; P:ribosome assembly; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13227; PTHR13227; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF017222; eIF2A; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Initiation factor; Protein biosynthesis; Reference proteome;
KW Repeat; Translation regulation; WD repeat.
FT CHAIN 1..586
FT /note="Eukaryotic translation initiation factor 2A"
FT /id="PRO_0000286078"
FT REPEAT 23..63
FT /note="WD 1"
FT REPEAT 125..163
FT /note="WD 2"
FT REPEAT 356..401
FT /note="WD 3"
FT REGION 434..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 532..583
FT /evidence="ECO:0000255"
FT COMPBIAS 469..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 64504 MW; A4A1DD61FA8A2E4D CRC64;
MAPPAPLLAV RGSEGLFMVN GPPSFTESAV FQRDSGRNCK AVAFSKDGSL FAWCNGEKVN
IVNVTSAGLL RSFDLPKVVC LEFSPKNNIL ATWQAYSAAK DGTAGAPNLQ LYDVKTGKCL
KSFIQKKMQN WCPCWADDES ICARNVNNEV HFFENNNFNT IANKLHLQKV NDFVLSPGAQ
PTKVAVYVPG SKGAPSFVRL YQYPNFGGPQ SALANKSFFK ADKVTMLWNK KATAVLVIAS
TDVDKTGASY YGEQTLHYIA TNGESAIVQL PKNGPIYDVV WNPNSVEFCA VYGFMPAKAT
VFNLKCDPVF DFGTGPRNAA YYSPHGHILV LAGFGNLRGQ MEVWDVKNYK LISKPVASDS
TYFAWCPDGE HIVTATCAPR LRVSNGYKIW HYTGSVLHNY EVPSNEEMWQ VSWQPFLDGV
FPVKAVKYQA VPSELPSAEP KPAQAYRPPA LRNKPVTSSK LHEDEPPQNM KPQSGSSEKP
LSKTALKNQK KHEPKKAAKQ EAKADCSQES TQSSASQNTP RSAVPVVTSG DPEIDKKIKN
LKKKLKAIEQ LKEQAAAGKQ LEKNQLEKIQ KESALLQELE DLELGL