ID U4UK01_DENPD Unreviewed; 1161 AA.
AC U4UK01;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=D910_11673 {ECO:0000313|EMBL:ERL94394.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL94394.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL94394.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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; KB632390; ERL94394.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UK01; -.
DR STRING; 77166.U4UK01; -.
DR Proteomes; UP000030742; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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:UP000030742}.
FT DOMAIN 570..789
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..537
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1161 AA; 129698 MW; 4BE708F4A8A4CB9C CRC64;
MGKAKKQRKG AKDDESDSEV EVETQELIVQ ASTKKSKLQK VKSGSENEQN QKSKTTKNKK
VLDSEDDEDD VPVTKVQSAF ALLQMDDSED EVPAANDESE EEEQKPVAKN KKNGNAKPEP
QQGGKKGKKN RRRKDEDDDE LERALAELGM EYAGVKKEEP VAQVEKESEP VGKKGKKKTK
SESPDENGED QAEEEPAEGG TVKTAAQKKK EKKEREKQKK MAAKTKKEGS VEDLKPEGQV
AEVSEPKPVE ATAVPANDES AEKDVNKKKK KKGKDKPVED NVTEEGQGNE GEEVVEPTAE
KAGKKKKGAK DEKDAKTKKG PPKKTLVAMQ EALKKLKEDQ ERQRQEEEER IKREEEAENA
RLEMLRLEQE RKERKKQKEK EKKERLKAEG KLLTAKQKAD RARAQALIDS LKAQGVALPD
VGEKKPVRLG TRIKPNKQKK DPAAQEIKTE EKPAEEKGEL QPQIPVESAP IVTEVDDDVK
DAWDASSDEE SEDISDSVKK DSSEEPKVEP AKDEGGSEET SSEEDSDSED GSDSEEQDDK
TAAERTREKA EERIRKRKEN ATKNQTVENL RAAIVCVLGH VDTGKTKILD KLRRTNVQDG
EAGGITQQIG ATNVPIDAIK DQIKIVKGAA DMDLKIPGLL IIDTPGHESF SNLRNRGSSL
CDIAILVVDI MHGLEPQTIE SINLLKQKKC PFIVALNKID RLYDWQTMNR KDIRDVLKSQ
ASNTQMEFDQ RSKAVIVEFA EQGLNAALFY ENPDPRSYFS LVPTSAITGE GMGNLLALIV
EYCQVKLPKR LMYSDELQAT VLEVKAIPGL GTTIDVILVN GTLKEGDTML VAGTDGPIVT
QIRSLLMPQP MRELRVKNAY VEYKEVKAAQ GVKIAAKELE KAIAGLNLYV AVKPDEVEVM
RDEVARELRS ALSSIKLQER GVYVQASTLG SLEALLEFLK VSKIPYSGIR IGPVVKKDVM
KASIMLEHEP QYATILAFDV KVEKDAQELA DSMNVEIFQA DIIYHLFDKF MAYREQLKQK
KREEFKNIAV FPCRLRVLPQ FVFNSRDPIV CGVMVEAGIL REGTPICVPS KEFVDIGIVT
SIENNHKAVE TARKGMEVCI KIDPIPGQSP KMFGRHFDET DFLVSKISRQ SIDACKDYFR
DDLVKTDWQL MVELKKIFQI L
//
