ID W6ZZJ1_9APIC Unreviewed; 981 AA.
AC W6ZZJ1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, 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=C922_03253 {ECO:0000313|EMBL:EUD66337.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD66337.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD66337.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD66337.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-2013) 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}.
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DR EMBL; KI965472; EUD66337.1; -; Genomic_DNA.
DR RefSeq; XP_008817067.1; XM_008818845.1.
DR AlphaFoldDB; W6ZZJ1; -.
DR EnsemblProtists; EUD66337; EUD66337; C922_03253.
DR GeneID; 20038527; -.
DR VEuPathDB; PlasmoDB:C922_03253; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000030640; 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; 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:EUD66337.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 395..611
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 19..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 110361 MW; C276764D4677194D CRC64;
MSKNKKGKKK DDLDAILAEF GFDGKREDEV KDQKENGEAG AEVGAGAGAG AGGGATPAGE
EQNEAIKMSK SKKKKEKQKQ KKEQMKSKEN DEEGEEAEAK KGTAEQPADA ANDAANDAAN
EAADDAAKKN KKKKKKDKEK TKEQKGTSGM SEMAKAAAER LRLLKEYEEK KREEEKRKQE
EEEERIRKEE EEREKKRLAK LEKKMQLKKD GKLLSAKAKE EKKKKELYLK TLKESGVLIE
PKEKAKAEII NIDLNKTKAF LKKKKNKTNA HTSGMANLNN NAEETGGTTP KGNKPDDAEK
KVDPKEIVVD DWEDFLNVDE EKKKEKEPNE QQGNEKTDRE RNKSKEAKQS QGKKGTKGDA
LSTKKGKKKT DASKSNGNEK NNNAQDDDSD HESEYRSAIV CILGHVDTGK TKLLDKLRHT
NVQDNEAGGI TQQIGATFFP KDILDKEIKK VDESIKCMSK GIMIIDTPGH ESFYNLRKRG
SSLCDIAILV IDLMHGLEQQ TKESIQILKQ RNCPFVIALN KIDRLYMWNR NDWSPFNSTF
KNQKENTQEE FQDRLKNILN ELAEQGLNCH LYWENPNPRK YVSIVPTSAI TGEGIADLIM
ILVKLTQNFM LKNIEYHEKL ECTVLEVKNI EGLGTTIDVI LTNGVLKESD TIVLCGINGP
IVTVIRALLT PQPLKEIRIK NEYVHHKSIK ACIGVKISAN GLEEVLCGTS LFVANNTDEV
EDYKSKAMTD VSDVFNHVDK SGVGLYVMAS TLGSLEALLI FLKDSKIPVF AVNIGTVQKK
DVKKASVMRE KGKPEYSVIL AFDVKIDPEA EKEAQILGVE IMQRDIIYHL FDAFTNYIKK
IEEEKKQSKL TDAIFPCELS IVNDCVFNKK DPIVIGVKVD CGILKIGTPL YIPEKSLKIG
NVVSILLNKK TCEKAKKGDE VSIKICGEPH ITFGRHFDFN QKIYSKITRE SIDVLKEYFR
SELTMEDWRL VVQLKKIFNI I
//
