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Database: UniProt
Entry: D4ASM8_ARTBC
LinkDB: D4ASM8_ARTBC
Original site: D4ASM8_ARTBC 
ID   D4ASM8_ARTBC            Unreviewed;       702 AA.
AC   D4ASM8;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   03-MAY-2023, entry version 52.
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=ARB_07243 {ECO:0000313|EMBL:EFE33778.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE33778.1, ECO:0000313|Proteomes:UP000008866};
RN   [1] {ECO:0000313|Proteomes:UP000008866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFE33778.1}.
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DR   EMBL; ABSU01000008; EFE33778.1; -; Genomic_DNA.
DR   RefSeq; XP_003014681.1; XM_003014635.1.
DR   AlphaFoldDB; D4ASM8; -.
DR   STRING; 663331.D4ASM8; -.
DR   GeneID; 9527044; -.
DR   KEGG; abe:ARB_07243; -.
DR   eggNOG; KOG2315; Eukaryota.
DR   HOGENOM; CLU_013809_0_1_1; -.
DR   OMA; WNPNSKE; -.
DR   OrthoDB; 22264at2759; -.
DR   Proteomes; UP000008866; 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; 1.
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; 2.
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:UP000008866};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW   ECO:0000256|PIRNR:PIRNR017222}.
FT   DOMAIN          181..375
FT                   /note="Translation initiation factor beta propellor-like"
FT                   /evidence="ECO:0000259|Pfam:PF08662"
FT   REGION          379..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  75812 MW;  1586E57AD7E1195E CRC64;
     MAAPTQLAYL KGTSGVPHTL PVADISPGLP QKVNQIPAEN VYEIDFSPLG TYVITWQRPS
     KDENGDAVRN LKVWKVATES ETQDQQTPIG SFVQKSQTGW NLQYASDEQY CARVVTNEVQ
     FYESGNLGSV WKKLRVEGVA DFALSPGKGH AVATFIPERK GQPASVRIFD MPNFNAPVSQ
     KSFYKGDKVQ LKWNNTGTTL IVLAQTDVDK SGKSYYGETT LYLLSVSGTF DSRIDLDKEG
     PIHDVTWSPT SKEFGVVYGY MPAKTTIFNT RAVATHSFQL GPRNTILFSP HGRFVLVAGF
     GNLAGQMDIY DVEKDYKKIV TIEASNASVC EWSPDGRHIL TATTSPRLRV DNGVRIWHVT
     GALMYNEDMN ELYSVSWRPQ SPNSHPLTSN PLNPVPTPHP SATAYLSTKK APTKPAGAYR
     PPGARGQSTP LAFRREDEGG AAFVREDSSS FASNGGSAPS PFGKPRRRAV PGAEPVEEFL
     PPGAAPGGGV ALPPGAEASA PGPEKLSKSA AKNKKKREAK KAKEASAGGQ GDGGENSMAA
     TPNSGRRDRS RSRHRQQASG GANGANGANL DPNYPRGGRD RSRSAHRRQR SDGRNSTPNR
     NGNGNQPHDR RSPAVNTTGR QQAAPPDLTV TSPDGGNTAN AAPDAAAIAR DKKMRSLLKK
     VRAIDELKMR VASGEKLEET QMKKIHTEDS VRSELEALGW TG
//
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