IF5_PHAVU
ID IF5_PHAVU Reviewed; 443 AA.
AC P48724;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN Name=EIF5;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Floyd Z.E., Bartlett S.G.;
RT "Nucleotide sequence of a cDNA encoding eukaryotic initiation factor 5 in
RT bean.";
RL (er) Plant Gene Register PGR95-092(1995).
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; L47221; AAA92861.1; -; mRNA.
DR PIR; T11804; T11804.
DR AlphaFoldDB; P48724; -.
DR SMR; P48724; -.
DR STRING; 3885.XP_007139199.1; -.
DR eggNOG; KOG2767; Eukaryota.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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.
FT CHAIN 1..443
FT /note="Eukaryotic translation initiation factor 5"
FT /id="PRO_0000212525"
FT DOMAIN 284..443
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 147..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar 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"
SQ SEQUENCE 443 AA; 48912 MW; A34E6AE094C376AD CRC64;
MALQNIGAGN SDDAFYRYKM PRMVTKIEGR GNGIKTNVVN MVDIAKRLAR PASYTTKYFG
CELGAQSKFD EKTGTSHVNG AHETAKLAGL LEIFIKKYVQ CYGCGNPETE ILITKNQMIQ
LKCAACGFVS DVDMRDKLTT FIVKNPPEVK KGSKDKKAMR RAEKERLKEG EAADEELKKV
KKEVKKKGSS SAKDGTAKST ISKKKGSGSD EDRRSPTHKQ IEEKEEAKDE DDDDDDGVQW
LTDTSLDASR QRIKEQLSAV TADMVMLTTD EPEKKKKAAS NQNGGSQNGN SKNYGTVVAE
VKANLKKGFG ASELLSHLAA LPVPAQEKMS ALVEALFEGT EKGFGRETLK KKNYFAAAVA
EEGSQILLLH AIEEFCCKPN SNALKEVALV LKTLYDADVL EEEAIVLWYQ KGLKGDNKNS
KIWKNAQPFI DWLQNAESES DEE
