ID M3J1C0_CANMX Unreviewed; 1021 AA.
AC M3J1C0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Eukaryotic translation initiation factor 5B, putative {ECO:0000313|EMBL:EMG45638.1};
GN ORFNames=G210_4160 {ECO:0000313|EMBL:EMG45638.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG45638.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG45638.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG45638.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOGT01002403; EMG45638.1; -; Genomic_DNA.
DR AlphaFoldDB; M3J1C0; -.
DR STRING; 1245528.M3J1C0; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_1_0_1; -.
DR OMA; EFAVMLC; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd01887; IF2_eIF5B; 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; 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 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; 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 Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:EMG45638.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT DOMAIN 422..640
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..359
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 113930 MW; C551D9CD3475ACF9 CRC64;
MAKKGKKGQA GGDFWDDEDI EQDQPQAEEF GTTETPEPST EEPSNDQPEE ASAEDISGDF
LSSIRKNKQK KAQKEEEEKT SNGAPKLLSK KEKEKLKKEA EKQKKKEMAQ KKKTQQASKK
EQIKEANKQN AAAAAASTSS SVSATPEPES IEDKAEPVEK AKPAKKGKKA PAGLAALKKQ
LELKKQLEEE QRRLEEEEEQ KRLEEERLAA EEEAKKEAAR AAKKERERLK KEQLKAEGKL
LTKKQKEEKK LQERRRQQLL QAGNVTVAGL NKTADDEATP KPKKVVYTKK KSTKPKTFIQ
KSTQAKAPVK KDEDDEEEAL VDDWEKMALD DDEPVAEDWD ADFKDEEEEE VAAEEPEPKE
DDEAAAKALE AEKERLAKAE QARKEKEERA RKLKQEEEEK SKALAAAASS TTTTAAVPEK
ELRSPICVIL GHVDTGKTKL LDKIRQTNVQ GGEAGGITQQ IGATYFPVDA IKQKTAVMAK
YEKQTFDVPG LLIIDTPGHE SFTNLRSRGS SLCNIAILVI DIMHGLEQQT LESIRLLRDR
KAPFIVALNK IDRLYDWKEI PNNSFRDSFA HQTKSVQAEF QNRYDQIKLA LAEQGLNSEL
YFQNKNMAKY VSIVPTSAVT GEGVPDLLWL LLELTQKRMS KQLMYLSKVA ATILEVKVVE
GFGYTIDVVL SNGVLKEGDR IVLCGLNGPI ATNIRALLTP PPSRELRIKS EYVHHKQVKA
ALGVKIAAND LEKAVAGSRL LVVGEDDDEE EMMDEVMDDL TGLLDSVDTS GKGVVVQAST
LGSLEALLDF LKDMKIPVMS IGLGPVYKRD VMKASTMLEK APELAVMLCF DVKVDKEAEQ
YADEQNIKIF NADIIYHLFD AFTAYQSKLL EARRKEFMDF AVFPCVLKTI QIINKRNPML
IGVDVVEGTV RVGTPICAVR TDPVTKQPNV MVLGKVVSLE VNHKPSDSVK KGQTAAGVAM
RLENPSSAQP VWGRHVDETD NLYSMISRKS IDTLKDPAFR DTVSREDWLL IKKLKPVFDI
K
//