ID A0A3B3II77_ORYLA Unreviewed; 1195 AA.
AC A0A3B3II77;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 34.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
GN Name=eif5b {ECO:0000313|Ensembl:ENSORLP00000043524.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000043524.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000043524.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000043524.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000043524.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000043524.1};
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Plays a role in translation initiation. Ribosome-dependent
CC GTPase that promotes the joining of the 60S ribosomal subunit to the
CC pre-initiation complex to form the 80S initiation complex with the
CC initiator methionine-tRNA in the P-site base paired to the start codon.
CC Together with eIF1A (EIF1AX), actively orients the initiator
CC methionine-tRNA in a conformation that allows 60S ribosomal subunit
CC joining to form the 80S initiation complex. Is released after formation
CC of the 80S initiation complex. Its GTPase activity is not essential for
CC ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A
CC (EIF1AX) ejection quickly followed by EIF5B release to form elongation-
CC competent ribosomes. In contrast to its procaryotic homolog, does not
CC promote recruitment of Met-rRNA to the small ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00053410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + phosphate + H(+); 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:0000256|ARBA:ARBA00051990};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00051990};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000256|ARBA:ARBA00001944};
CC -!- SUBUNIT: Interacts through its C-terminal domain (CTD) with the CTD of
CC eIF1A (EIF1AX) or with the CTD of EIF5 (mutually exclusive) through a
CC common binding site. Interacts with eIF1A (EIF1AX) from the location of
CC the start codon by the 43S complex until the formation of the 80S
CC complex. Interacts with ANXA5 in a calcium and phospholipid-dependent
CC manner. {ECO:0000256|ARBA:ARBA00061781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733}.
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DR RefSeq; XP_023820144.1; XM_023964376.1.
DR AlphaFoldDB; A0A3B3II77; -.
DR STRING; 8090.ENSORLP00000043524; -.
DR Ensembl; ENSORLT00000040353.1; ENSORLP00000043524.1; ENSORLG00000001525.2.
DR GeneID; 101167431; -.
DR GeneTree; ENSGT00940000163243; -.
DR InParanoid; A0A3B3II77; -.
DR OrthoDB; 4928at2759; -.
DR Proteomes; UP000001038; Chromosome 2.
DR Bgee; ENSORLG00000001525; Expressed in testis and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; 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:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd16266; IF2_aeIF5B_IV; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR FunFam; 2.40.30.10:FF:000013; eukaryotic translation initiation factor 5B; 1.
DR FunFam; 2.40.30.10:FF:000026; Eukaryotic translation initiation factor 5B; 1.
DR FunFam; 3.40.50.10050:FF:000002; Eukaryotic translation initiation factor 5B; 1.
DR FunFam; 3.40.50.300:FF:000112; Eukaryotic translation initiation factor 5B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd.
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 NCBIfam; NF003078; PRK04004.1; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038}.
FT DOMAIN 604..821
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 28..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..96
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..149
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..195
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..290
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..545
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..572
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1195 AA; 134406 MW; A8A60280A9391909 CRC64;
MGKKQKKAGE DSAKDDGVDI DALAAEIEGA GAAKEQKGKK KKKGAKKEEF DEDEILKELE
ELSLETQGGK KTDTTEDVEA LEPPRPEKKK TRKGKKGGGS PEDEKAEDAN EDKNEEDKKA
PPAALPDDSD DDSSSRSRLK TKGGKKGGKK ASVSEEEDPA EDKDVKKGAQ KEDDSEEDEE
FAFKMDKKKK NKGKAAKAES EDEEEQDEEA GGFKMKTAAQ KKAEKKEREK KKKEEERMKL
KKQKEKEGNV EAKKEPETKA VEATPPQATS EAVPEEVEGV EPAAEADEGE GEKKKKDKKK
KKGEKEEEKK KKGPSKATVK AMQETLAKMK EEEERLKREE EERQKRLEEL EKQRQEQERL
EQERKEKKKQ KEKERKERLK KEGKLLTKAQ KEAKLRAEAM LSMLQAQGVE VPSKDTVPKK
KPVYGDKRRK KPNTHTPEET STVTSPTSET PEPIAMETEA ETVPAPQPEV KPEAVVDNWE
KFASDEEKVK NRRSRQEADL KKVHIEVKEE TTGPPQPPAS EEDEEDEEEE EEDNDEDESE
DDVDAEKEAP PAIQSKKKVV SEDESSESED DDGRTKEERL YDRAKRRIEK RRAENLKNTD
TERLRAPVVC VLGHVDTGKT KILDKLRHTH VQDGEAGGIT QQIGATNVPK ETIEEQTKMV
KNFLRESIRI PGMLIIDTPG HESFSNLRNR GSSLCDIAIL VVDIMHGLEP QTLESINLLK
EKKCPFIVAL NKIDRLYDWK KSPETDVVTT LKKQKKNTKD EFDERTKAII VEFAQQGLNA
ALFYENKDPR TFVSLVPTSA HSGDGMGNLI ALLVDLTQTM LARRLAHCDE LRAQVMEVKA
LPGMGTTIDV ILINGCLREG ETIIVPGVDG PIVTQIRGLL LPPPLKELRV KSQYEKHKEV
STSQGVKILG KDLEKTLAGL PLLVAHKEDE IPVLRDELVR ELKQTLSSIK LEEKGVYVQA
STLGSLEALL EFLRTSKVPY AGINIGPVHK KDVMKASTML EHDPQYAVIL AFDVKVERES
QEMADSLGVR IFAAEIIYHL FDAFTKYREE YKKAKQDEFK NIAVFPAKLR VLPQFIFNSR
DPIVMGVSVE AGVLKQGTPL CVPSKGFVDI GIVTSIEVNH KSVDSAKKGQ EICIKIEPIP
GESPKMYGRH FEATDIIVSK ITRASIDALK NWFRDEMQKS DWQLIMELKK TFEII
//
