ID A0A0V0S967_9BILA Unreviewed; 1129 AA.
AC A0A0V0S967;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
DE Flags: Fragment;
GN Name=EIF5B {ECO:0000313|EMBL:KRX23296.1};
GN ORFNames=T07_10658 {ECO:0000313|EMBL:KRX23296.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX23296.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX23296.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX23296.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX23296.1}.
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; JYDL01000025; KRX23296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S967; -.
DR STRING; 6336.A0A0V0S967; -.
DR Proteomes; UP000054630; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:KRX23296.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 538..755
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 858..885
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 82..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX23296.1"
SQ SEQUENCE 1129 AA; 127727 MW; 0ED4CA6DABC788DE CRC64;
LYFKFLRQVN DRSILPLGNK DRIMASKKVV GKASTKTVKQ KVATENNYSE SDGEDEINFI
ASRPAAYTLL DLNDDADDAP DSEDSGSVKE AAEVGRKKGQ KAAKKKNKQK QKKVEKEDNL
DDLVAYIEND AISSKKPAGK KQKKKLKKAQ VDEDIDLLLA ELEQEEKGGS VPTANKQEET
KVEPVATGAD VGQADVDKAV GAVGKRAKAK AKRKQKLSES KETVDNKAEV KTTAAAAAPS
QLSDENKDMP KVKQEANVQP SPTEIKLDDA VSTVAESETK NVKKKKKGKD EKENKEKKKR
TPADLIKQAL KKRQEEEERL RQLELEEERR IAELERQREE KERLEREKKE RKKREKKEKI
EKLKKEGKYM TAEQKQKLQR QRERIEMLKQ QGVNVPEMKQ DVQTDGVKTT MKRLVYADRK
RVKKEKPTVT EVSQPKEDFP QQKARSREVS EKDDVIESWD LLDSERARLS SNDEVKMSEF
SKDPSTESET SAVSDQQQVV LEREKSAESA VVVSHQRQIS ESQRSDSLSI DMEMEQGYRS
PVICVLGHVD TGKTKILDKI RHTHVQDSEA GGITQQIGAT FVPREALVEQ TKMVKGFDGE
SLQLPGLLII DTPGHESFSN LRSRGSSLCD IAVLVVDIMH GLEMQTIESI NLLKQRKTPC
VVALNKVDRL YDWKACPNKD IRAALKAQQR NAQIEFNERV RETVLQFAQQ GLNVALFWEN
PDQEEYISLV PTSAHTGDGM GNLMQAIIGY CQSKLMDRLL FQPTLQCTVL EVKVIAGLGT
TIDVILVNGY LRVGNTIVVA GSEGPIVTQI RELLMPHPLR ELRVKNNYLH NRVVKAAQGV
KIVAKDLEKA LAGLPLLLAK KESEIEELKE ELSNSLKKIL QAVKLSERGV YVQASTLGSL
EALLEFLRAQ KIPYFGVNIG PVHKRDVVKV STMLEHDPQW AVILAFDVKV DRDAQQMADE
LEVKIFQADI IYHLQDAFLK YREELKQKKR QEFEHLAIFP CKLRVLPQHM YKTRDPIICG
VVVEAGILKV GVPLCVPSKE FIYLGNVSSI EQNHKQLQSV RKNAEVCIKI ENTTGEAPKM
FGRHFTEQDM LVSRISRETI DVCKQYFRED LQKADWQLMV ELKKVFEIL
//
