ID S9X0H8_SCHCR Unreviewed; 575 AA.
AC S9X0H8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=SPOG_01224 {ECO:0000313|EMBL:EPY50467.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY50467.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY50467.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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|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 EMBL; KE546993; EPY50467.1; -; Genomic_DNA.
DR RefSeq; XP_013024950.1; XM_013169496.1.
DR AlphaFoldDB; S9X0H8; -.
DR STRING; 653667.S9X0H8; -.
DR EnsemblFungi; EPY50467; EPY50467; SPOG_01224.
DR GeneID; 25035555; -.
DR eggNOG; KOG2315; Eukaryota.
DR HOGENOM; CLU_013809_0_1_1; -.
DR OMA; WNPNSKE; -.
DR OrthoDB; 22264at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
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; SSF82171; DPP6 N-terminal domain-like; 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:UP000015464};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW ECO:0000256|PIRNR:PIRNR017222}.
FT DOMAIN 210..404
FT /note="Translation initiation factor beta propellor-like"
FT /evidence="ECO:0000259|Pfam:PF08662"
FT REGION 423..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 64018 MW; 9BE507B8FF1480CB CRC64;
MSQKNQFAYR SSKTIGLVNT NENYTKPAEF EEANEPARVS CYSPNGKFFA YASGSVVVIV
DAESGKTLRV LPAGNIYELG FSPLGNFLGT WERPGKEADG NPKQNMKVWN TNTGDLIFSF
VQRNQTGWNL QYTVDEKLAA RLVTNEIHFY ETANLGKPPV FKLRVEGLSD FALSPGRNHV
VAVFVPERKG APASVRTYSI PNFTRPLSQK TFFKADKVQF KWNALGTSLL VLTQTDVDKS
NKNYYGETNL YLLGITGQFD CRVDLDREGP IHDVAWNSNS KEFGIVYGYM PAKTSIFDSR
ANVIHNFPLA PRNTLLFSPN SRYIMLAGFG NLQGSIDVFD RLNHMKKIAT VEASNCTFCE
FSPDSQFLLT AVTSPRLRVD NSIKIWHITG APMFYEESVE LYQAFWRPSL LNVALMEEDS
QSFSSLPSAP KAHESASKLA AKPTVKPTGA YRPPGARGQA STFSYRREEL DVLSSNSTSK
SQATPRQRVV PGAAPVVDKN NKKNKTNGQK VAPEPPTEVS DEKKIRSLCK KLRAIDDLKA
RLEKNEKLEA TQVKKVESEG KVLEELKALG WNSNA
//
