ID A0A3F3Q1P9_9EURO Unreviewed; 1065 AA.
AC A0A3F3Q1P9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BDQ94DRAFT_144483 {ECO:0000313|EMBL:RDH33088.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH33088.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH33088.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH33088.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ852048; RDH33088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3Q1P9; -.
DR STRING; 1341132.A0A3F3Q1P9; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000253729; 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:UP000253729}.
FT DOMAIN 471..689
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..467
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 93..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..284
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..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 118098 MW; CF9ED6F4845AE305 CRC64;
MAPKKKGNKR QEEDWEAELG ESAPAAGGEA EAPAAEEGAP ADEDAGMGGG GLLAALRKNK
NKKAKKGKPV NDFVEGEDAT QEANGDADFA SKQPEEGTFD EDDVFAGKAK PKKAAAAPEP
KPAEEEEGGF RVKSKKEKER EKKEREKQRK REQAAKKKTA APAEKAQPAK VEPEKKEEAA
PAPAAAPVPE TGGKKKKIPA HLLAIQKQQE ALRKQREEEE RLLAEAQAAE EERRRIEEEE
EKKREEARQR KKEKEKEKKE QLRKEGKLLT KAQREAKERN ERRMQQMLAA GVGKVAGLEE
GQAEKKRPVY ENRKKRGPKK QEDDLEAAAA RAKAQREAEE ERRRKEEEEK KAKAEAEAAA
AAAAAAGGEE SELDDWEKAA DAEEVKDSWD APSDEEEEKP ATNGKATEKP ASKEDEEDES
EDDSDESSDE DSEDEEQSAA QKAIAQRKAE AAERRKKQHE EAMAARSKDN LRSPICCILG
HVDTGKTKLL DKIRQTNVQE GEAGGITQQI GATYFPVDAL RQKTAVVNKD GQFEFKIPGL
LIIDTPGHES FSNLRSRGSS LCNIAILVVD IMHGLEPQTL ESMRLLRDRR TPFIVALNKI
DRLYGWKKID NNGFQESLAL QNKGVQNEFR TRLERTKLLF AEQGFNSELF YENKSMARNV
SLVPTSAHTG EGIPDMLKLL TTLTQERMTN SLMYLSEVEC TVLEVKVIEG LGTTIDVVLS
NGILREGDRI VLCGLNGPIS TNIRALLTPA PLKELRLKSQ YVHNKEVKAA LGVKIAANDL
EQAIAGSRLM VVGPDDDEED IEEEVMSDLE NLLSKVSRDQ RGVSVQASTL GSLEALLEFL
RVSKIPVANI SIGPVYKRDV MMAGTMLEKA KEYAVMLCFD VKVDKEAAAY ADEVGVKIFT
ADIIYHLFDD FTKHMAELTE RRKEESKMLA VFPCVLKTVA VFNKKDPIVI GVDVAEGSLR
LHTPVAAVKA NPETGAKEII DLGRVVSIER DHKPIQVCKR GQPSVAVKIE GSNQPMYGRQ
LEDKDTLYSH ISRASIDTLK EFYRSDVSME EWGLVKKLKP VFDIP
//
