IF5_MAIZE
ID IF5_MAIZE Reviewed; 451 AA.
AC P55876; Q9SBX1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN Name=EIF5;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9240471; DOI=10.1006/bbrc.1997.6990;
RA Lopez Ribera I.R., Ruiz-Avila L., Puigdomenech P.;
RT "The eukaryotic translation initiation factor-5, elF-5, a protein from Zea
RT mays, containing a zinc-finger structure, binds nucleic acids in a zinc-
RT dependent manner.";
RL Biochem. Biophys. Res. Commun. 236:510-516(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=10580155; DOI=10.1016/s0378-1119(99)00438-2;
RA Lopez Ribera I.R., Puigdomenech P.;
RT "Structure, organization and expression of the eukaryotic translation
RT initiation factor 5, eIF-5, gene in Zea mays.";
RL Gene 240:355-359(1999).
CC -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]).
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; X99517; CAA67868.1; -; mRNA.
DR EMBL; AJ132240; CAA10616.1; -; Genomic_DNA.
DR PIR; JC5595; JC5595.
DR AlphaFoldDB; P55876; -.
DR SMR; P55876; -.
DR STRING; 4577.GRMZM2G165917_P02; -.
DR PaxDb; P55876; -.
DR PRIDE; P55876; -.
DR MaizeGDB; 66866; -.
DR eggNOG; KOG2767; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P55876; baseline and differential.
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 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; PTHR23001; 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; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..451
FT /note="Eukaryotic translation initiation factor 5"
FT /id="PRO_0000212524"
FT DOMAIN 290..449
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 143..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 339
FT /note="P -> L (in Ref. 2; CAA10616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 48912 MW; AB6D5AC15F8EB661 CRC64;
MALQNIGASN RDDAFYRYKM PRMITKIEGR GNGIKTNVVN MVDIAKALAR PASYTTKYFG
CELGAQSKFD EKTGISLVNG AHDTAKLAGL LEVFIKKYVQ CYGCGNPETE ILISKTQMIS
LKCAACGFVS DVDMRDKLTT FILKNPPEQK KGGKDKKAMR RAEKERLKEG EAADEEQKKL
KKDAKKKGSK DSTAKGLKKK ATTATGSDED HSSSPTRSHD GDKAAADDDD DDVQWQTDTS
IEAAKQRMQE QLSAATAEMV MLSTEETEKK MKQPTHKDGS TNGSAKEIPN DKPAVTKPSP
YEELIGDIKA SLGSAPTPSQ LKAVLASSTL PPQDVMNAPL EALFGGVGKG FTKEVVKNKK
YLAVAVPDEG AQTLLVQAIE AFGGKCNPEA LKEVPVVLKA LYDGDILDEE TIVDWYNDAV
AAGKDSQVVK NAKPFVEWLQ SAESDEEGDD E