ID A0A2K6LZK5_RHIBE Unreviewed; 560 AA.
AC A0A2K6LZK5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|ARBA:ARBA00013819, ECO:0000256|PIRNR:PIRNR017222};
DE Short=eIF-2A {ECO:0000256|PIRNR:PIRNR017222};
GN Name=EIF2A {ECO:0000313|Ensembl:ENSRBIP00000028950.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000028950.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000028950.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000028950.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003993,
CC ECO:0000256|PIRNR:PIRNR017222}.
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC {ECO:0000256|ARBA:ARBA00009573, ECO:0000256|PIRNR:PIRNR017222}.
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DR AlphaFoldDB; A0A2K6LZK5; -.
DR Ensembl; ENSRBIT00000052897.1; ENSRBIP00000028950.1; ENSRBIG00000038363.1.
DR GeneTree; ENSGT00730000111053; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13227; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR PANTHER; PTHR13227:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF017222; eIF2A; 1.
DR SUPFAM; SSF50960; TolB, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|PIRNR:PIRNR017222};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|PIRNR:PIRNR017222};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW ECO:0000256|PIRNR:PIRNR017222}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 191..386
FT /note="Translation initiation factor beta propellor-like"
FT /evidence="ECO:0000259|Pfam:PF08662"
FT REGION 409..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 62233 MW; 7E39F267AA363BC6 CRC64;
MAPSTPLLTV RGSEGLYMVN GPPHFTESTV FPRVNIISVT NKGLLHSFDL PKAVCLEFSP
KNTVLATWQP YTTSKDGTAG IPNLQLYDVK TGTCLKSFIQ KKTQNWCPSW SEDETLCARS
VNNEVHFFEN NNFNTIANKL HLQKINDFVL SPGPQPYKVA VYVPGSKGAP SFVRLYQYPN
FAGPHAALAN KSFFKADKVT MLWNKKATAV LVIASTDVDK TGASYYGEQT LHYIATNGES
AVVQLPKNGP IYDVVWNSSS TEFCAVYGFM PAKATIFNLK CDPVFDFGTG PRNAAYYSPH
GHILVLAGFG NLRGQMEVWD VKNYKLISKP VASDSTYFAW CPDGEHILTA TCAPRLRVNN
GYRIWHYTGS ILHKYDVPSN AELWQVSWQP FLDGIFPAKT ITYQAVPSEV PNEEPKVATA
YRPPALRNKP ITNSKLHEEE PPQNMKSQSG NDKPLSKTAL KNQRKHEAKK AAKQEARSDK
SPDLAPTPGP QSTPRNTISQ SISGDPEIDK KIKNLKKKLK AIEQLKEQAA TGKQLEKNQL
EKIQKETALL QELKDLELGI
//