GenomeNet

Database: UniProt
Entry: M3J1C0_CANMX
LinkDB: M3J1C0_CANMX
Original site: M3J1C0_CANMX 
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}.
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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
//
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