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Database: UniProt
Entry: R1GYH8_BOTPV
LinkDB: R1GYH8_BOTPV
Original site: R1GYH8_BOTPV 
ID   R1GYH8_BOTPV            Unreviewed;       707 AA.
AC   R1GYH8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-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=UCRNP2_2090 {ECO:0000313|EMBL:EOD51129.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD51129.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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; KB915893; EOD51129.1; -; Genomic_DNA.
DR   RefSeq; XP_007581397.1; XM_007581335.1.
DR   AlphaFoldDB; R1GYH8; -.
DR   STRING; 1287680.R1GYH8; -.
DR   KEGG; npa:UCRNP2_2090; -.
DR   eggNOG; KOG2315; Eukaryota.
DR   HOGENOM; CLU_013809_0_1_1; -.
DR   OMA; WNPNSKE; -.
DR   OrthoDB; 22264at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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:UP000013521};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW   ECO:0000256|PIRNR:PIRNR017222}.
FT   DOMAIN          217..411
FT                   /note="Translation initiation factor beta propellor-like"
FT                   /evidence="ECO:0000259|Pfam:PF08662"
FT   REGION          448..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  76934 MW;  D5BB248019E2D019 CRC64;
     MAAPTQLAFR TLKGIGVFNA APVYENLPGF QHPEGNLRCC VYSPDGKYFA WASPEQVTVI
     DASTGNVATV LPAENVFELG FSPLGTYIIT WQRPTKDETG NATKNLKVWR TVDDNAGAEG
     QRNVVGQFVQ KNQYGWNLQY TSDESYCARC VTNEVQFYQS NDLSTVWNKL RVEGVADLAV
     SPGKNHSVAV FVPERKGQPA SVKVFLVPQF ASPVSQKTFF KGDKVQMKWN NLGTSVIVLA
     QTDVDKTNKS YYGETNMYIL SANGGFDARI TLDKEGPIHD VTWSPNSKEF GVVYGYMPAK
     TTVFNQRAVA THNFNLAPRN TILFSPHGRF VLVAGFGNLA GQMDIYDLEK DYAKVCTIEA
     ANSSICEWSP DGTHIMTATT SPRLRVDNGI RIYHVTGGLQ YFTEFNELYH VTWRPQSIAE
     HPLENPLGSI PTPHESATKF LATVKAPTKP AGAYRPPGAR GSSTPLHFKR EDEGGAAYIN
     TGISSTSGNM NGNGFGGRPR RQVPGAEEHV PPGAAPGGGV SLAGTGEGAD EGLSKAALKN
     KKKREAKKAK EAAEKAAGLS AGQQQDNGNN PDRKARSHSR TRSRNSPDGR APSHNRRGNS
     NSTNNYQQNR NGQAPGQNGQ RGPPPRQIQT QQPPQPAPEV APELTVTSPG GVSPQDKKIR
     SLMKKLRAID DLKMRQAGGE KLEDTQVKKI HTEESIRKDL DALGFHG
//
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