ID A0A1Y3BVP9_EURMA Unreviewed; 771 AA.
AC A0A1Y3BVP9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=BLA29_002400 {ECO:0000313|EMBL:OTF83984.1};
OS Euroglyphus maynei (Mayne's house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF83984.1, ECO:0000313|Proteomes:UP000194236};
RN [1] {ECO:0000313|EMBL:OTF83984.1, ECO:0000313|Proteomes:UP000194236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF83984.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:OTF83984.1};
RA Arlian L.G., Morgan M.S., Rider S.D.;
RT "Genome Survey of Euroglyphus maynei.";
RL Submitted (MAR-2017) 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:OTF83984.1}.
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DR EMBL; MUJZ01001281; OTF83984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3BVP9; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000194236; 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 Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:OTF83984.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000194236}.
FT DOMAIN 181..396
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..120
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OTF83984.1"
SQ SEQUENCE 771 AA; 86968 MW; 3ABE13E41D58D471 CRC64;
QRLEKERLEK ERKEKKKQKE KERKLRLKKE GKLLSSKQKA DLLRAKMSLQ LLKESGQAVI
GKTRKEGRLD KQDSAEDESK SDNISEPKDD DNNTEPLDDA EMVDEEEDQV EEEEFPDDWE
NIVIEDRKKK QQQQRQNAME NKKSSNKSTN DTTTGGSNKS SIDPDLSLST SNPASRPPEK
FRSPIICVLG HVDTGKTKLL DYIRKTHIQD NEAGGITQQI GATFVPPTAI NEQCKHVKSK
SELKIPGLLI IDTPGHESFS NLRSRGSSLC DIAILVIDIM HGLEKQTIES LNLLKSRKTP
FVVALNKIDR LYEWRSNVRK DVEDLINSQQ SNTKHEFNTL KQKVIVQLAE QSINAALFYE
NPDPRTYISL VPTSAHTGDG MGNLINLITH FTQTLMAKRI NYLLDPLDAT VLEVKAIPGL
GTTIDVVLVN GKLREGDKIV LAGHDGPIVT QIRALLVPQP LKELRVKSPY EELRIVYGSV
GVKIAAHDLE KAVAGLNLYV AHNEAELERL KTMCWNQFGS AMKAIKCSDK GVYVQASTLG
ALEALLQFLK DSKIPYSGVR IGPIAKRDVM KASIMLEHSP DNAAILAFDV KIDRDAQELA
DQLGVKIFMA DIIYHLFDQF TAYKENLRKQ RKEQNRHLAV FPCKLRILPN CIFNKRDPIV
LGVHVEAGTI VSGTPISVPT KELDLIGRVT TIEHDHKTVD QAKTGDEVCI KIEHCTSDAP
KLFGRHFDAN DLLYSRITRE SIDIMKEYFR DDLEKSDWQL MIELKKLFKI V
//
