ID D4AKQ0_ARTBC Unreviewed; 416 AA.
AC D4AKQ0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=W2 domain-containing protein {ECO:0000259|PROSITE:PS51363};
GN ORFNames=ARB_04893 {ECO:0000313|EMBL:EFE35959.1};
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:EFE35959.1, 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 -!- 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:EFE35959.1}.
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DR EMBL; ABSU01000002; EFE35959.1; -; Genomic_DNA.
DR RefSeq; XP_003016604.1; XM_003016558.1.
DR AlphaFoldDB; D4AKQ0; -.
DR STRING; 663331.D4AKQ0; -.
DR GeneID; 9522086; -.
DR KEGG; abe:ARB_04893; -.
DR eggNOG; KOG2767; Eukaryota.
DR HOGENOM; CLU_026663_1_0_1; -.
DR OMA; YRYKMEK; -.
DR OrthoDB; 5475947at2759; -.
DR Proteomes; UP000008866; 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:UP000008866}.
FT DOMAIN 249..412
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 123..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 46252 MW; 6094CC443EC30591 CRC64;
MERLQAKIEG KGNGIKTVVV NLNSVAQSLS RPPSYLIKYF GFELGAQANS KPTDDRWIIN
GAHDAPKLQD YLDGFITKFV LCKKCKNPET DVVIKDQSII LDCKACGERS DVDPRLKLSS
FILKNQPKKG KKDKSTKKSR RERNKEKGEK ADKAENGENG EANGSPGDSN GSDMGDENGD
VGIDAHSDDE LTRRIKAEAE QIEHNDDIDD EEWAVDVSEA AVRARAQELP DDLKRTLVFN
DADGDDDGEN AVASSYDQFG SWIIEEAKKS DKGASGVSDV DIYMKAKEFG IESKHKTLSV
LAQTIFDDNI VKQIPARAGL LKKMITSERH EKALLGGTER FVGKDRPNLL PMVSSILLTY
YQHDLVSEEL LKSWGTKASK KYVDIATSKK VRKSAEKFLE WLETAESEDE SEEDDE
//
