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Database: UniProt
Entry: A0A2N5S545_9BASI
LinkDB: A0A2N5S545_9BASI
Original site: A0A2N5S545_9BASI 
ID   A0A2N5S545_9BASI        Unreviewed;       406 AA.
AC   A0A2N5S545;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=W2 domain-containing protein {ECO:0000259|PROSITE:PS51363};
GN   ORFNames=PCANC_05255 {ECO:0000313|EMBL:PLW55117.1}, PCASD_25073
GN   {ECO:0000313|EMBL:PLW08364.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW08364.1, ECO:0000313|Proteomes:UP000235392};
RN   [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW55117.1}, and 12SD80
RC   {ECO:0000313|EMBL:PLW08364.1};
RA   Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA   Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA   Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT   "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT   Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC       {ECO:0000256|ARBA:ARBA00010397}.
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:PLW08364.1}.
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DR   EMBL; PGCI01001069; PLW08364.1; -; Genomic_DNA.
DR   EMBL; PGCJ01000036; PLW55117.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5S545; -.
DR   STRING; 200324.A0A2N5S545; -.
DR   OrthoDB; 5475947at2759; -.
DR   Proteomes; UP000235388; Unassembled WGS sequence.
DR   Proteomes; UP000235392; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd11561; W2_eIF5; 1.
DR   Gene3D; 1.25.40.180; -; 1.
DR   Gene3D; 2.20.25.350; -; 1.
DR   Gene3D; 3.30.30.170; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045196; IF2/IF5.
DR   InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR   InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR   InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR   InterPro; IPR003307; W2_domain.
DR   PANTHER; PTHR23001; EUKARYOTIC TRANSLATION INITIATION FACTOR; 1.
DR   PANTHER; PTHR23001:SF7; EUKARYOTIC TRANSLATION INITIATION FACTOR 5; 1.
DR   Pfam; PF01873; eIF-5_eIF-2B; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF100966; Translation initiation factor 2 beta, aIF2beta, N-terminal domain; 1.
DR   SUPFAM; SSF75689; Zinc-binding domain of translation initiation factor 2 beta; 1.
DR   PROSITE; PS51363; W2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT   DOMAIN          248..405
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          150..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  45079 MW;  ED864435356EBBA3 CRC64;
     MAVGIVNIGK DARGDMFHRY KMPVLQVKVE GKGNGIKTVI PNMSDIARSL ARPPTYITKF
     FGCELGAQTT FDEKYDRYIV NGAHQADRLR ELLDVFIDKF VLCSSCKNPE TELMIVGRDE
     LIWRDCKACG HRGHVDNRHK LCTFILKNPP ESSKKKSKRD KVSSKAAGDA AAAAPEGGSS
     SDDGHNSQDE LTKRIEGEAV DAKTAEATST LKDQDWSADT SAEAVKARMK SLEAGVQNGL
     SLGDDDDEEN PGGPYALFSD WILSNRDSVS DLDIILKAKE LGIEKKHKTV QILAQNLFTE
     NAVKEVSKHH ALFAKMVSSE KHQKSLLGGI EQLCGEAYPS LVPLGVPKII MEFYQADILE
     EEVIKQWGTH VSKKYVDKEV SKRVRRACEP LLKWLDEAED EDEDDE
//
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