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Database: UniProt
Entry: S7XJ48_SPRLO
LinkDB: S7XJ48_SPRLO
Original site: S7XJ48_SPRLO 
ID   S7XJ48_SPRLO            Unreviewed;       762 AA.
AC   S7XJ48;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=SLOPH_1985 {ECO:0000313|EMBL:EPR79054.1};
OS   Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC   Spraguea.
OX   NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR79054.1, ECO:0000313|Proteomes:UP000014978};
RN   [1] {ECO:0000313|Proteomes:UP000014978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX   PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA   Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA   Williams B.A.P.;
RT   "The genome of Spraguea lophii and the basis of host-microsporidian
RT   interactions.";
RL   PLoS Genet. 9:E1003676-E1003676(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}.
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:EPR79054.1}.
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DR   EMBL; ATCN01000420; EPR79054.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7XJ48; -.
DR   STRING; 1358809.S7XJ48; -.
DR   VEuPathDB; MicrosporidiaDB:SLOPH_1985; -.
DR   HOGENOM; CLU_002656_3_3_1; -.
DR   InParanoid; S7XJ48; -.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000014978; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   ECO:0000313|EMBL:EPR79054.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014978}.
FT   DOMAIN          179..391
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   762 AA;  86448 MW;  141C772E3C8686E1 CRC64;
     MDEKNGAGQT TDTKSQKKPK FVRKKKQKGN KQQDVVQKKD VISVPTEKEV VIENKEESTN
     EIKKEEKKEK ETEKIEPVKQ GGRRRGPNIA MIKKLAEQKQ KQEEELKKLK KQQEEEDLER
     IRKIEEEKKL AIEKQKKEKE ERELENKMKK MKLRNFLVRE KVKTVKKIEK IEEEIETDLK
     SPICCILGHV DTGKTKLLDK LRETDVQGSE AGGITQQIGA TFFPVKELKR KFNVPENNLP
     GILIIDTPGH ETFSNLRSRG SSLCDIAILV VDILHLLENQ TLESIELLKR RKTPFIIALN
     KIDRIYGWKS TNFAGFTESF EKQTDVTKEE FKRQMNDTIV KFSEIGLNTT LFSENNNEKQ
     FVSIVPTSAI TGEGIPDLIS TILKLSESFM STKMKYKDEV QCTILEVKEI DGYGSTIDVI
     LSNGILRKGD KIAVCGFDGP IITNIKSLLV PKALKEIRVK GEYMQKSEVK ASLGVKIAAL
     NLENAVAGSR IVIVKNNEEE AKKEVMQDLQ NVISKVKTEE IGVHLQSSTL GSLEALVEFV
     TSSNIPIATV GVGKLNKKDI VRASIMAEKS IEYSPLLCFD IKIDKEISEI AEKYNIKIFC
     EKIVYNLLDK YKEYSANLRN KMKDAAKSST IFPCELEILP NCVFNKRSPL VLGVEVKRGI
     LKIGTVLCII RKNVLGLGTV TSIENNKKAT EKAVVGDKVA IKIEIGSNET PRLFGRHFVQ
     EDLLYSWINR KSIDSLKKNF KEELCDDDWM LVIELKNKLD II
//
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