ID A0A0M8N7C3_9HYPO Unreviewed; 1079 AA.
AC A0A0M8N7C3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 18-JUN-2025, entry version 43.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
GN ORFNames=ESCO_005246 {ECO:0000313|EMBL:KOS21480.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21480.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS21480.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000256|ARBA:ARBA00048107};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KOS21480.1}.
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DR EMBL; LGSR01000008; KOS21480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N7C3; -.
DR STRING; 150374.A0A0M8N7C3; -.
DR OrthoDB; 4928at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
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 FunFam; 2.40.30.10:FF:000013; eukaryotic translation initiation factor 5B; 1.
DR FunFam; 2.40.30.10:FF:000026; Eukaryotic translation initiation factor 5B; 1.
DR FunFam; 3.40.50.10050:FF:000002; Eukaryotic translation initiation factor 5B; 1.
DR FunFam; 3.40.50.300:FF:000112; Eukaryotic translation initiation factor 5B; 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.
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; NF003078; PRK04004.1; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:KOS21480.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT DOMAIN 484..702
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..127
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 117865 MW; C6A0857F1954AFF1 CRC64;
MAPKKKGNKH AQDDWEAELG ESIAPAAAAP AATDDANGGN DDDNDAAARA GGLMAIMRKN
KEKRKKKGVV DDEPEPETAP AAPAEDLAAK APVEASLDDE FALPQKKGKG GKGGNAAKGK
QAPAAAAHND DDDDDAAAAA GEEPGRILTK AEKEKLKKER EKQRKKEQSA KKKGATPAAA
PAKVSEPAKA AKDAPAAAPE PAAPAPAEAA GGKKKKIPAH LALIQKQQEE IRRRQEEQER
LEAEAKAHAE EEEKRLAEEA KRKEEQKAVK KQKEKERIEQ LKKEGKFLTK AQKEEKARNE
KKLQQMLAAG IKVGPQDDGA EPKKKPVYDN KKKKGRNDKK DEEAALAEAA ERARIQAEKA
LKEAEEKAAR ERAEAEAKAA ALKKAAESDI EDDWEAAAAE DDDDVKDSWD ADTDEEAEKK
AAAKADGKPA SEEDESESDE SESESEDEAL SRAKQLEAQR KKEAAERREK AHQAALAARS
KDDLRSPICC ILGHVDTGKT KLLDKIRQTN VQEGEAGGIT QQIGATYFPV EAIKQKTAVV
NKDNSFEFKV PGLLVIDTPG HESFSNLRSR GSSLCNIAIL VVDIMHGLEP QTLESMRMLR
ERKTPFIVAL NKIDRLYGWK KVDNNGFRES LALQNKAVHN EFKNRLEATK LAFSEQGFNS
ELFYENKSMA KFVSLVPTSA HTGEGIPDML KLIVQLTQER MVGSLMYLSE VQATVLEVKA
IEGFGMTIDV ILSNGILREG DRIVLCGTEG AIVTNIRALL TPAPLRELRL KSAYVHNKEV
KAALGVKISA PGLEGAIAGS RLMVIGPDDD EEDICDEVES DLANLLSRVE TSGRGVSVQA
STLGSLEALL DFLKDCKIPV ANVGIGPVYK RDIMQCGIML EKAPDYAVML CFDVKVDKEA
QAYADEQGIK IFTADIIYHL FDNFTAHMDA MLEKKKEESK MLAVFPCVLK PVAIFNKTSP
IVVGIDVVEG QLKINTPIAA VKTNPTTNAR EVVPIGRVTS IERDHKQIPV CKKGQPSVAV
KIEMGGHQPV YGRHLEEDDL LYSQVSRASI DCLKEFYRKD VSNEEWQLII KLKPLFDVN
//
