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Database: UniProt
Entry: A0A1L9VRC8_ASPGL
LinkDB: A0A1L9VRC8_ASPGL
Original site: A0A1L9VRC8_ASPGL 
ID   A0A1L9VRC8_ASPGL        Unreviewed;      1069 AA.
AC   A0A1L9VRC8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=ASPGLDRAFT_23654 {ECO:0000313|EMBL:OJJ86462.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ86462.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878892; OJJ86462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9VRC8; -.
DR   STRING; 1160497.A0A1L9VRC8; -.
DR   VEuPathDB; FungiDB:ASPGLDRAFT_23654; -.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000184300; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184300}.
FT   DOMAIN          476..694
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..39
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1069 AA;  118818 MW;  ECBF5F410F3F408A CRC64;
     MAPKKKGNKR QEQDWEAELG EDAPAAEPQP EEEPAAEGVE EETSGSGGLL AALRKNKTKK
     AKKGKQDNDF VEGEDPTEEA NDAVDLASKA PQEGSFEDEE EDVFAGNQKS AKAAAAAAKA
     KKTEEPEGEF RVKSKKEKEK EKKEREKQRK KEQAATKKKP GDNKKEPAKQ AASPKDEASP
     EPSPAATPAP ELAGGGKKKK LPPHLAAIQK QQEALRKQRE EEERIRAEER AALEEQRVLD
     EEEERQKEEA RQKKKEKEKE KKEQLRREGK LLSKAQREAQ QHNEIRMKQM LAAGVGTVAG
     LEANQAEKKR PVYDTKKKKG PKKQEEDLEA AAARAKAQRE AEEERRKKEE EERKAKEEAE
     AAAAAAAAAA QEQESEGEDW EKMADADDVK DSWDAPSDEE GEKPKAAAKE SEKPAETAAP
     KKDESESESE SESESESEDE EQSAAKRAVA QRKAEAAERR KRQHEEAMAA RSKDNLRSPI
     CCILGHVDTG KTKLLDKIRQ TNVQEGEAGG ITQQIGATYF PVDALQTKTA VVNKDGKFEF
     KIPGLLIIDT PGHESFSNLR SRGSSLCNIA ILVVDIMHGL EPQTLESMRL LRDRRTPFIV
     ALNKIDRLYG WKKIDNNGFQ DSLAMQNKGV QNEFRTRLDH TKLLFAEQGF NSELFYENKS
     MSRNVSLVPT SAHTGEGIPD MLKLLTTLTQ ERMTNALMYL SEIECTVLEV KVIEGLGTTI
     DVVLSNGILR EGDRVVLCGL NGPISTNIRA LLTPAPLKEL RLKSAYVHNK EVKASLGVKI
     AANDLEQAIA GSRLMVVGPD DDEEDIEEEV MSDLEQLLSK VSKDQRGVSV QASTLGSLEA
     LLEFLRVSKI PVANISIGPV YKRDVMMAGT MLEKAKEFAV MLCFDVKVDK EAYAYAEEVG
     VKVFTADIIY HLFDDFTKHM AELTEQRKEE SKLLAVFPCV LKPVAVFNKK DPIVIGVDVI
     EGSLRMNAPL CAIKTNATGQ KEILDIGRVV SIERDHKPVQ VTKRGQPSVA VKIEGSNQPM
     YGRHLEEKDQ LYSRISRASI DTLKEFYRPE VSMEEWALVK KLKPVFEIP
//
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