ID F7VRN4_SORMK Unreviewed; 1099 AA.
AC F7VRN4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=SMAC_01718 {ECO:0000313|EMBL:CCC08170.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC08170.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC08170.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC08170.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC08170.1}.
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DR EMBL; CABT02000005; CCC08170.1; -; Genomic_DNA.
DR RefSeq; XP_003348696.1; XM_003348648.1.
DR AlphaFoldDB; F7VRN4; -.
DR STRING; 771870.F7VRN4; -.
DR GeneID; 10806162; -.
DR KEGG; smp:SMAC_01718; -.
DR VEuPathDB; FungiDB:SMAC_01718; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_1_0_1; -.
DR InParanoid; F7VRN4; -.
DR OMA; EFAVMLC; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000001881; 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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT DOMAIN 504..722
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..470
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 120994 MW; 0B6E26474CCBB501 CRC64;
MAPKKKGNKK ANDDWEAELG ESIAPVNNGA AADAAAEPAA DEDASGGGGL MERMRKAKEK
RKKKGIVDDW EAELGETAPG AEKPAEEAVP DLSAKVAEEA NLDDEFALPE KKGKGGKGKQ
QQQQQQKAAP AAAAAKKDED AADEDGPRVL TKAEKEKLKK EREKQRKKEQ AAAKKKGTTP
AAATKAEPAA KEEKKAETPS PVSTPAPAPA AEAAGGKKKK LPAHLLALQK QQEELRRRQE
EEAKLLAEEK ARIEEEERLA AEEAKRKEEE RARKKEKEKQ RIEQLKKEGK FMTKAQREEK
ARNERKLQQM LAAGIKVNAL EGEEPKKKPV YDDKKKKAAN KKRDEEKALA EAAERARLAA
EALAKEQEEK ARIEREKAEK EAAAKAAAAK AAAEESVDED WEAAVASDKE DVKDSWDADS
DEEEDSKKDA PKSAAANGKA DAKKDDKSES DSEEDSEEES EDESSDDEEA TARQLEEARR
KKEAAERREK AHQAALAARS ADNLRSPICC ILGHVDTGKT KLLDKIRQTN VQEGEAGGIT
QQIGATYFPV EAIKQKTAVV NRDGKFEFKV PGLLIIDTPG HESFSNLRSR GSSLCNIAIL
VVDIMHGLEP QTLESMKLLR DRKTPFIVAL NKIDRLYGWK KIENNGFQES LALQNKAVQN
EFKNRLEQTK LAFAEQGFNS ELFYQNKSMA KYVSLIPTSA HTGEGIPDML KLIVQLTQER
MVGSLMYLSE VQATVLEVKA IEGFGMTIDV ILTNGILKEG DRIILCGTEG VIKTNIRALL
TPAPLRELRL KSQYVHNKEV KAALGVKISA PGLEGAIAGS RLLVVGPDDD EDDLEDEVEA
DLASLFSRVE KSGRGVSVQA STLGSLEALL DFLKDCKIPV ANVGIGPVYK RDVMQCGIML
EKAPDYAVML CFDVKVDKEA QEYADQQGVK IFTADIIYHL FDSFNKHMDE LLEKKKEESK
MLAVFPCVLS PVAVFNKSGP IVIGVDVVDG SLRINTPISA VRQNAVTGAK EIIDLGRVTS
IERDHKQIPV CKKGQPSVAI KIEMGGNQPT YGRHLEEKDM LYSKISRASI NCLKEFYRKD
VTNDEWQLII KMKSMFEIA
//
