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Database: UniProt
Entry: M1K5D2_ENCCN
LinkDB: M1K5D2_ENCCN
Original site: M1K5D2_ENCCN 
ID   M1K5D2_ENCCN            Unreviewed;       659 AA.
AC   M1K5D2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=ECU09_0070 {ECO:0000313|EMBL:AGE96208.1};
OS   Encephalitozoon cuniculi (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=6035 {ECO:0000313|EMBL:AGE96208.1};
RN   [1] {ECO:0000313|EMBL:AGE96208.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23376943; DOI=10.1128/EC.00307-12;
RA   Selman M., Sak B., Kvac M., Farinelli L., Weiss L.M., Corradi N.;
RT   "Extremely Reduced Levels of Heterozygosity in the Vertebrate Pathogen
RT   Encephalitozoon cuniculi.";
RL   Eukaryot. Cell 12:496-502(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; KC513614; AGE96208.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1K5D2; -.
DR   VEuPathDB; MicrosporidiaDB:AEWD_090070; -.
DR   VEuPathDB; MicrosporidiaDB:AEWQ_090080; -.
DR   VEuPathDB; MicrosporidiaDB:AEWR_090070; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_0070; -.
DR   VEuPathDB; MicrosporidiaDB:M970_090070; -.
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:AGE96208.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          72..286
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   659 AA;  73229 MW;  AE5AA697E82362A4 CRC64;
     MGKKNRRDDD YLNTLLGSAD KGNKERRKDP EDSEEIGKSV SKMSVGEAQK SSKHNERETG
     TRLNNREKPS EFKSPICCIL GHVDTGKTKL LDKLRESNVQ EEEAGGITQQ IGATFFPVSE
     LFRKCGKRES KLPGILVIDT PGHESFANLR TRGSSLCNLA ILVVDIVHGI EAQTLESIEL
     LRKRRTPFVV ALNKIDRLYG WKSTPFGGIK EILKKQSKAT INDFKKRLDN TVVAFAEMGL
     NAKLFYENTD QKRFVSLVPT SAISGEGIPD LISLILELSE KYMGSKMKIK NEVECTVLEV
     KNAEGFGVTI DAILSNGMLK EGDRIGVCGF NGPIVTTIKA LLMPQPLKEL RVKSQYIMVK
     EVRASLGIKI AAGGLEKAIA GSRVLIVEDN EEEVKRALET DLESVFSSIE LSQEGVHVVS
     STLGSLEALI SFLKTSKIPI LGASIGTVKK KDMIIVASMA KKHKEYAAIL CFDVVLEKEI
     RDMASSMKVR VFEAKTIYHL LDSYLKFVDE EKEKDKKMYM DQAVFPVELS IVPKCIFNSR
     SPLVVGVHVQ EGILKIGTPL CVFKEGETTR LGVVTSIENN KEAAKEAVKG QKVAIKIEAK
     PNLPPRMFGR HFGQDDILYS LVTRESISVL KKHFSSELTE DLIRLLNKLE NKFGVFYLL
//
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