ID A0CNW2_PARTE Unreviewed; 966 AA.
AC A0CNW2;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=GSPATT00008921001 {ECO:0000313|EMBL:CAK72479.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK72479.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK72479.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK72479.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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; CT868119; CAK72479.1; -; Genomic_DNA.
DR RefSeq; XP_001439876.1; XM_001439839.1.
DR AlphaFoldDB; A0CNW2; -.
DR STRING; 5888.A0CNW2; -.
DR EnsemblProtists; CAK72479; CAK72479; GSPATT00008921001.
DR GeneID; 5025661; -.
DR KEGG; ptm:GSPATT00008921001; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_3_0_1; -.
DR InParanoid; A0CNW2; -.
DR OMA; EFAVMLC; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 371..591
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 111071 MW; CCF3FF14B2A0DEFD CRC64;
MSKFLQEESE GSDQEPQNEG SKFLQVEEEN EAEEQVALKD EGPKNTKKET KKNKNKKNDS
DDELDKILAS KAPQEQELDE EAKKKAEKKK EKKAKQAEKK KNVPEQQPQQ QQAQVPEKKP
EKPGKKLNAA AQKALEMQKI KEEEQRKIRE EEERLRKLEE ERIRIEQEEE ERRKQEEEKR
RQDKQKKKDE LLKKGEYKTK KQLEEEEKLK FMREQLGIKV DDAGNKSNIV KKKKKQPGQQ
NQQVEATVQK PEETVQPEQK VEQKQPEKQQ QAAEIKQQPQ KQQQQQQQQQ QQQQKVKEEV
TIKQNEVEDI ESWEQFVEEG EAEQLQQEKD KQEKQQVEDQ KRQQEQQILQ QSYSSTIKKE
ILDLYKPVGE LRSPICCILG HVDTGKTTLL DKIRNTNVQE GEAGGITQQI GATFFPAKKL
KEELIKTQQF YPVDCNIPGL LIIDTPGHES FSNLRTRGSS LCDLAILVID LMHGLENQTL
ESLELLKLRK TPFIIALNKI DRCVEWKNKK NASSYYQLQN QTKNCKMDYD TKRQQVITQL
AEKGFNVAFF WENEDPKTYI SVVPTSGFTG EGIPDLLSVI VKYTSVYMKN KIKVKEQFNC
TVLEKKVTEG HGTTIDCLLI DGQIKKDDKI ILAGFQGPIV TKVRALLTPH PMKEMRVKGE
YIHHDIIYAS MGLKISAVGL EEAMAGSQMY LANSQEDIDR ATEIINNEME EVKKYIKLQN
QGVGVAASTL GSLEALLQYL NSQDIPVSYV SVGPVSKDDV MKALKNVLLE DVNRRKKEYA
CMLVFDVKIL PDAQKFAEEN QIKIFEANII YHLFTKFTEF IKQVKEERKK KEAADVVFPS
LLKIVRIINT KEPLILGVEV EQGILKTGTP LCIYDQNSNK NKIGIVETIE LNHKSLKEAR
ATTGAVALRI GTNQAIQAGK QITLETKLAS LITRRAIDIL KEHYREDLTL DDWQLVKDLK
LFLNIV
//
