ID B0XNB5_ASPFC Unreviewed; 1068 AA.
AC B0XNB5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=AFUB_004370 {ECO:0000313|EMBL:EDP55740.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP55740.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP55740.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP55740.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XNB5; -.
DR EnsemblFungi; EDP55740; EDP55740; AFUB_004370.
DR VEuPathDB; FungiDB:AFUB_004370; -.
DR HOGENOM; CLU_002656_1_0_1; -.
DR PhylomeDB; B0XNB5; -.
DR Proteomes; UP000001699; 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 ECO:0000313|EMBL:EDP55740.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 474..692
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..469
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 90..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 118708 MW; 1358D715D82B9750 CRC64;
MAPKKKGNRK QDDDWEAELG ESIAPVSEQP KDATPADAAP EEDDMGGGLL AALRKNKNKK
AKKGKPVNDF VEGEDATEQA NGDVDFSSKQ PEEGTVDQED VFAGKKKQKP AKATPPAPAS
VEGDGEIRVK TKKEKEREKK EREKQRKREQ ALKKKATAPE PKAEPAKAEK KEQAAPAAAA
APTPPAAAPE APGKKKKLPA HLAAIQRQQE ALRRQREEEE RRLAEEKAAE EERLRREAEE
EKKREEARQR RKEKEREKKE QLRREGKLLT KAQKEAKERN ELRLKQMLAA GVGKVAGLEE
PGIEKKKPVY DNRKRKGLKK QEEDLEAAAA RARAQREAEE ERRRKEEEEK KAKAEAEAAA
AAAAAGDEES EVDDWEKAAE AEEEVKDSWD APSEDEGEKP ATNGVAKPAA APQQKAEVHE
SESEDDSEDD SESESEDEEK SAAQKAIAQR KAEAAERRKK QHEEALAARS KDNLRSPICC
ILGHVDTGKT KLLDKIRQTN VQEGEAGGIT QQIGATYFPV DALRQKTAVV NKDGKFEFKI
PGLLVIDTPG HESFSNLRSR GSSLCNIAIL VVDIMHGLEP QTLESMRLLR ERKTPFIVAL
NKIDRLYGWK KIDNNGFQDS LAMQSKGVQN EFRTRLEHTK LLFAEQGFNA ELYYENKSMA
RNVSLVPTSA HTGEGIPDML KLLTTLTQER MTNSLMYLSE VECTVLEVKV IEGLGTTIDV
VLSNGILREG DRIVLCGLNG PIATNIRALL TPAPLKELRL KSQYVHNKEV KAALGVKIAA
NDLEHAIAGS RLMVVGPDDD EEDIEEEVMS DLENLLSKVS RDQRGVSVQA STLGSLEALL
EFLRVSKIPV ANISIGPVYK RDVMMCGTML EKAKEYAVML CFDVKVDKEA AAYAEEVGVK
IFTADIIYHL FDDFTKHMAE LTEKRKEESK LLAVFPCVLR PVAVFNKKDP IVIGLDVIEG
SLRMHTPISA VKTNPTTGAK EIIDLGRVVS IERDHKPIQV CKKGQPSVAV KIEGANQPMY
GRQLEEKDTL YSHISRASID TLKEFYRSDV SMEEWALIKK LKPVFDIP
//
