ID A0A395I631_ASPHC Unreviewed; 425 AA.
AC A0A395I631;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=W2 domain-containing protein {ECO:0000259|PROSITE:PS51363};
GN ORFNames=BO97DRAFT_240987 {ECO:0000313|EMBL:RAL15246.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL15246.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL15246.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL15246.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC {ECO:0000256|ARBA:ARBA00010397}.
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DR EMBL; KZ824272; RAL15246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395I631; -.
DR STRING; 1450537.A0A395I631; -.
DR VEuPathDB; FungiDB:BO97DRAFT_240987; -.
DR OrthoDB; 5475947at2759; -.
DR Proteomes; UP000248961; 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:UP000248961}.
FT DOMAIN 259..421
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 147..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47271 MW; C321642D05D7997E CRC64;
MATVNIRRDV SDPFYRYKME RLQSKIEGKG NGIKTVIVNL NSVAQSLARP PAYVIKYFGF
ELGAQANAKP TDDRWIINGA HDAPKLQDYL DGFISKFVLC KKCKNPETDV NIKDEKIFLD
CKACGQRSDV DSRLKLSTFI LRDVASGKGG KKDKASKKDR RERKKDKNKA ANGDNNGSPG
DSNSDNGDEE NGDVALEAGS DDELTRRIKA QAQNIEAEDE IDDDDWAVDV SEEAVKARAK
ELPDDLKRTL VLEDADEDGA DGPSAYDELG SWVIETAEKN GGVTGVSDVD IYMKAKEYGI
ENKHKTLAVL AQTIFDDKIV KQIPARAGLL KKLITSERHE KAFLGGTERF VGKDRPELIG
QVPAILLKYY EHDLISEDTL KAWGSKASKK YVDISTSKKV RKAAEPFLEW LENAESEEES
EEDDE
//
