ID A0A251LIP4_MANES Unreviewed; 444 AA.
AC A0A251LIP4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=W2 domain-containing protein {ECO:0000259|PROSITE:PS51363};
GN ORFNames=MANES_02G158200 {ECO:0000313|EMBL:OAY58207.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY58207.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY58207.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY58207.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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; CM004388; OAY58207.1; -; Genomic_DNA.
DR EMBL; CM004388; OAY58208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251LIP4; -.
DR STRING; 3983.A0A251LIP4; -.
DR EnsemblPlants; OAY58207; OAY58207; MANES_02G158200.
DR EnsemblPlants; OAY58208; OAY58208; MANES_02G158200.
DR Gramene; OAY58207; OAY58207; MANES_02G158200.
DR Gramene; OAY58208; OAY58208; MANES_02G158200.
DR OMA; EDVIFGW; -.
DR OrthoDB; 5475947at2759; -.
DR Proteomes; UP000091857; Chromosome lg2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
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:SF52; EUKARYOTIC TRANSLATION INITIATION FACTOR 5-2-RELATED; 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:UP000091857}.
FT DOMAIN 288..444
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 144..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48655 MW; 351B30B8F5404BE8 CRC64;
MDLQNIGASN SDDAFYRYKM PKMITKIEGR GNGIKTNVVN MVDIAKALAR PASYTTKYFG
NELGAQSKFD EKTGTSLVNG AHDTPKLAGL LENFIKKYVQ CYGCGNPETE IVITKTQMIT
LKCAACGFVS DVDMRDKITT FILKNPPVPK KGSKDKKAMR RAEKERLKEG EAADEELKKH
KKETAKKKGG SSGSSKDGAK GISSKKKGNG SDEDHSPSHS QADENDLVIA DDDDDVQWQT
DTSLEAAKQR IQEQLSAATA DMVMLSTNEE KANSAKSPER DVKAHQNGSK SNDTLEGLVN
EIKGYLKKGG PASQLKSFLS SLSGTPQEVI NALFAALFEG LEKGFVKEVT KKKNYLAAAT
QEEGSQMLLL HTVESFCCKA GPEVVKEVPL AVKVLYDNDV LEEEFILEWY QKGVSGGNKS
SPVWKNVKPF IEWLQNAESE SEEE
//
