ID L2GN16_VITCO Unreviewed; 713 AA.
AC L2GN16;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
GN ORFNames=VICG_01079 {ECO:0000313|EMBL:ELA41895.1};
OS Vittaforma corneae (strain ATCC 50505) (Microsporidian parasite) (Nosema
OS corneum).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vittaforma.
OX NCBI_TaxID=993615 {ECO:0000313|EMBL:ELA41895.1, ECO:0000313|Proteomes:UP000011082};
RN [1] {ECO:0000313|Proteomes:UP000011082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50505 {ECO:0000313|Proteomes:UP000011082};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Didier E., Bowers L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Vittaforma corneae strain ATCC 50505.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; JH370137; ELA41895.1; -; Genomic_DNA.
DR RefSeq; XP_007604525.1; XM_007604463.1.
DR AlphaFoldDB; L2GN16; -.
DR STRING; 993615.L2GN16; -.
DR GeneID; 19881790; -.
DR VEuPathDB; MicrosporidiaDB:VICG_01079; -.
DR HOGENOM; CLU_002656_3_3_1; -.
DR InParanoid; L2GN16; -.
DR OMA; FRQSKPA; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000011082; 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; cd16266; IF2_aeIF5B_IV; 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; IPR029459; EFTU-type.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:ELA41895.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000011082}.
FT DOMAIN 131..343
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..83
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 79921 MW; 54BE7B49400BDF7F CRC64;
MDKEDNQAKD KLKKDKRPEP KITQTVQKAP PKPGAKGVSL AQIKAMQLAK LEQERQIQEA
KAKAEEQAQA RRLEAERLKT LKKESEIIEK AEKQKTADIS AYMRRLTFKQ PEQKEKTTEP
TNANKYEISN YKSPICCILG HVDTGKTKLL DKLRESNVQG SEVGGITQQI GATFFPSEAL
AKKCKLALPD LPGLLIIDTP GHESFSNLRS RGSSICNLAI LVVDIMHGLE RQTLESISLL
RTKRTPFIVA LNKIDRIVNW KSENYRSFKS SLESQEKYTQ QEFRSLLENT VGQFAAQGIN
AALFSENTEP RRIISLVPTS AISGEGIPDL IGLILDLSMK FMMEKMKVKQ DAECTVLEVK
NVEGYGVTID VILSNGTLKE GDRIGLCGFE GPIVTVIKTL LLPQPLRELR VKSQYEIVKE
VRASIGVKIF ASNLESAVAG SKLYVIENND AEIIKLLEDD LNSVISSIET VEQGVHVTAS
TIGSLEALLS FLKSENVPVS SVSLGKLKKK DIIRISSMLD KRFRQILCFE VDIDNELLDF
AESQGVKVFT AQIIYHLLDK YNKYCEDVTT LDKNLHSGEG IFPCCLRILP NCVFNARSPL
VLGVLVEKGT LKVNTPICVF KDSSYVKLGT VTSIEEKKKS VAKAEKGKQV AVKIEVGKDE
TSKMFERHFN MDDLLYSIVT RHSIDILKEY FKDELQQDHL ELLFYLKKKF EIL
//
