IF2P_DICDI
ID IF2P_DICDI Reviewed; 1045 AA.
AC Q54XP6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Eukaryotic translation initiation factor 5B;
DE Short=eIF-5B;
DE EC=3.6.5.3;
DE AltName: Full=Translation initiation factor IF-2;
GN Name=eif5b; ORFNames=DDB_G0278815;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Plays a role in translation initiation. Translational GTPase
CC that catalyzes the joining of the 40S and 60S subunits to form the 80S
CC initiation complex with the initiator methionine-tRNA in the P-site
CC base paired to the start codon. GTP binding and hydrolysis induces
CC conformational changes in the enzyme that renders it active for
CC productive interactions with the ribosome. The release of the enzyme
CC after formation of the initiation complex is a prerequisite to form
CC elongation-competent ribosomes. {ECO:0000250|UniProtKB:P39730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P39730};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC Note=Binds 1 monovalent cation per monomer in the active site.
CC Structural cofactor that stabilizes the GTP-bound 'on' state. May also
CC act as a transition state stabilizer of the hydrolysis reaction.
CC {ECO:0000250|UniProtKB:G0S8G9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39730}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000024; EAL68009.1; -; Genomic_DNA.
DR RefSeq; XP_641984.1; XM_636892.1.
DR AlphaFoldDB; Q54XP6; -.
DR SMR; Q54XP6; -.
DR STRING; 44689.DDB0234259; -.
DR PaxDb; Q54XP6; -.
DR PRIDE; Q54XP6; -.
DR EnsemblProtists; EAL68009; EAL68009; DDB_G0278815.
DR GeneID; 8621716; -.
DR KEGG; ddi:DDB_G0278815; -.
DR dictyBase; DDB_G0278815; eIF5b.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_3_2_1; -.
DR InParanoid; Q54XP6; -.
DR OMA; RDVMMAG; -.
DR PhylomeDB; Q54XP6; -.
DR Reactome; R-DDI-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q54XP6; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:dictyBase.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Initiation factor; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1045
FT /note="Eukaryotic translation initiation factor 5B"
FT /id="PRO_0000328179"
FT DOMAIN 458..675
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..474
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 492..496
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 531..534
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 585..588
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 653..655
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 1..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1045 AA; 115835 MW; D6F82472E3DE3683 CRC64;
MGPKQRVRKD NYWDSGEADK DREEAEKLHK KGQQQSDSDS DSDDIPISKK KPTSKFAPVD
ESSSESEESS SEEEVQKKPS KPAAKQSKKV APTNNKKKPV VESSSSEEEE SESESEESSE
EDTKKKPSKP AAKQSKKVAP TNNNNNKKKP VVESSSEESE SESEESSSEE DTKKKPSKPA
AKQNKKAPAK KAAAVESSSE SEEESSSSEE EEKPTKPTQN NNNKKNNAKK PPAAKPSAAK
QQAKKPAPKK PEEPEVLSGF LLKQRQEEER IAREKEEKRI REEEEKKRAA EQKIIDDEKA
RLKSIENSKK RAEKKEKQAG AAAEADRMAK LAKLGVNISA VGEKKEKSTN KTKSGGKKQN
QVSSITESVE KLKIEEPTSA PKDDVVEVMD SWDNDDYETV EEIQKKKEEE AKRKEEEEEA
QRLAAKEEKK KAKAAAAAAA AALIPTTDPT TTFADKSYRS PIICILGHVD TGKTSLLDKI
RNTNVQGGEA RGITQQIGAS FIPVDAIKEQ TKSFAEKIKM DFKLPGLLLI DTPGHESFNN
LRSRGSGLCD LAILVIDIMH GLQAQTLESI NLLRMRKTPF IVALNKVDRI YDWKPCVNTD
FKEAYKIQSK SAAQEFDYKV KDIIAALAGQ ELNAELYWRN KDHRKYVSLV PTSANTGEGI
SDLMLVVIQL MQKLMLDKVE FTNQLQCTLL EVKVIEGFGT TIDVVLVNGT LNEGDKIVVS
GFNGPIETSI RSLLTPPPLR ESRVKSQFIN HKSIRAAMGI KIVAPGLEKA VPGTSLHVVG
PNDDIEKIRA EAKREVDSVL NDVETSGIGV SVQASTLGSL EAFLNFLKKI KIPVANVAIG
PVHKKHIMNA SIMLDKDPKY AILLAFDVKI EESAIQAANE MKVQVLSDET IYLFEEKLKK
HFGAIKEKLR AETASICVWP CILEVTNVFR NSNPILVGVR VKEGTLRIGT PICVPESNCA
DVGKVIGIKL NEKDVTLAKK DDVVSVAIDD NNTKTTIYRH FDDKKQWMSK ITRESLDALK
EGWSEDLTKQ DIQLLKFMKT VYKIQ
