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Database: UniProt
Entry: F0W8P7_9STRA
LinkDB: F0W8P7_9STRA
Original site: F0W8P7_9STRA 
ID   F0W8P7_9STRA            Unreviewed;       979 AA.
AC   F0W8P7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
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   Name=AlNc14C36G3173 {ECO:0000313|EMBL:CCA17504.1};
GN   ORFNames=ALNC14_036470 {ECO:0000313|EMBL:CCA17504.1};
OS   Albugo laibachii Nc14.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA17504.1};
RN   [1] {ECO:0000313|EMBL:CCA17504.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA   Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA   Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA   Jones J.D.;
RT   "Gene gain and loss during evolution of obligate parasitism in the white
RT   rust pathogen of Arabidopsis thaliana.";
RL   PLoS Biol. 9:e1001094-e1001094(2011).
RN   [2] {ECO:0000313|EMBL:CCA17504.1}
RP   NUCLEOTIDE SEQUENCE.
RA   MacLean D.;
RL   Submitted (FEB-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; FR824081; CCA17504.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0W8P7; -.
DR   EnsemblProtists; CCA17504; CCA17504; ALNC14_036470.
DR   HOGENOM; CLU_002656_2_0_1; -.
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   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          389..607
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..286
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  109775 MW;  2B3750242851D4F3 CRC64;
     MAPKKGKKTK RPAGNEANKN ATTDNDLDTL LNEFTPSPDV NNDAHEKAAN EADTEAPKSS
     QNTADETEAA AAAFLKSMGV DAQAASSEKK DKKKKKPKKK AAASEESHPK SNEKKPPSAA
     AKLLLERQEA IRAQQERIEK ERLEQERILR EEEEKRLEEE RRLEEIKKKK REAKAAKIER
     QKKEGTYMTK AQKQKAAKAQ AALEAMQHSN NVVVGNNEEK KKVVYSNRKK GKAVVDQTKT
     DSEGKEKVDA QAETVTVEEA EPKENEEAPN EAEAPDAWDN EDWESSEIIA SLEDKLQLNG
     SADGSERKDD EVEDLLVVEQ RKEKEILRLQ GIALLKRQQE LKEVQERQAE EEHIRSKAQQ
     EADRKKREAA DRRRVREEKA LANVSADDLR SPICCIMGHV DTGKTKLLDN IRRTKVQDGE
     AGGITQQIGA TFFPVEAIKQ RTERLAKTMK LEYRLPGLLV IDTPGHESFT NLRSRGTSLC
     DIAILVVDIM HGLEPQTLES LRLLRQKKAP FIVALNKIDR CYGWKVMADM PIQEALKHQN
     EHVIREFEDR TKEIIVEFAK QKLNAEIYWK NNDLAHTVSL IPTSAISGEG VPDLLMMLTK
     LSQDRMAKSL AYVDILQCTV LEVKVLEGLG TTIDTILVNG KLNEGDTIVV CTLDGPVVTH
     IRSLLTPHPM KEIRVKGEYV HHSTMKAAMG IKICANGLEK AVAGTQIHVV GPDDDVEELK
     DSVMSDLTGI LDSVKATKRG VMVQASTLGA LEALLEFLRT CDPPIPVACV NIGPVHKKDV
     MRASVQLEHQ PEYATVLAFD VKVHHDATEL AQELGVRIFT ADIIYHLFDQ FTAYMDNFRS
     TRREEVADIA VFPCVLKILP NCVFNKKDPI ILGVDVEEGV LKIGTPLVVP NAGMLFVGKV
     SSIEREHKEV DRAKKGMSVA VRIENESNVT YGRHFDHKHR LFSRLTRQSI DALKENFRDD
     LAKEDWQLVI KLKKVFDII
//
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