ID A0A0D2AQF6_9PEZI Unreviewed; 1103 AA.
AC A0A0D2AQF6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 54.
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=PV09_00815 {ECO:0000313|EMBL:KIW08893.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW08893.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW08893.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW08893.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847530; KIW08893.1; -; Genomic_DNA.
DR RefSeq; XP_016218762.1; XM_016353609.1.
DR AlphaFoldDB; A0A0D2AQF6; -.
DR FunCoup; A0A0D2AQF6; 450.
DR STRING; 253628.A0A0D2AQF6; -.
DR GeneID; 27308788; -.
DR VEuPathDB; FungiDB:PV09_00815; -.
DR HOGENOM; CLU_002656_1_0_1; -.
DR InParanoid; A0A0D2AQF6; -.
DR OrthoDB; 4928at2759; -.
DR Proteomes; UP000053259; 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:KIW08893.1};
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:UP000053259}.
FT DOMAIN 510..728
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..70
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..84
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..213
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..447
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 121152 MW; 6F861436330DB243 CRC64;
MAPKKKGGNK KKDDNWEDEL GETIDPIAQA AQNAKADEAV QDAAAEQDNE MGGGLLAALK
KNRGKKAKKG KIVEDFVEGE DPTTDGDAAP QPVDLASKAP EEATFDDEED VFGQPMKKGK
ASKGGKQQEK EETKDDDDDG EEGGMRVKTK KEKEREKKER EKQRKKEQAA KKKTAAPAPA
ASKEPEKAVA ESKKEPAPEP VAAPAAPAAP AAGAKKKKLN PALAALQKQQ EERRRREEEA
ARLAAEEKAR IEEEERLAAE EAKRKEEQKL AKKLREKQKI EEQKKAGTYK SKAQKEAEAR
QKARLQQMVE AGGVIVGGTV GEKEKAKKPD NKKKSALKKK EEEELRLQKA KEAAEAEAAR
KQMEELRLAE EQAAKAKAEA EKAKAEAEAK AEESDGLEDW EAEADKMDGV KDSWDAESEE
EQEKKPTEAP APATKAKATV APTSTPANGK PKAPVKEEST DSEEDDSDDD SEEEEMTAAQ
KAEIKRKAEA AERRRQQHEA ALAARSKDNL RSPICCILGH VDTGKTKLLD KIRQTNVQEG
EAGGITQQIG ATYFPVEALK KKTAVVNEDG SFEFKVPGLL VIDTPGHESF TNLRSRGSSL
CNIAILVVDI MHGLEPQTLE SMRLLRERKT PFIVALNKID RLFGWKQIAN NGFQDSLRHQ
TKGCQNEFKD RLERTKLAFA EQGFNAEVFY ENKNMAKYVS LVPTSAHTGE GIPDMLKLLV
KLTQERMTSS LMYLSEVEAT VLEVKVIEGL GTTIDVVLSN GVLHEGDRIV LCGLNGAIST
NIRALLTPAE MKELRVKSAY VHNKSVKAAI GVKIAADGLE QAIAGSRLLV VGPDDDEEDL
EEEVMGDLEN LLSRISKTGR GVSVQASTLG SLEALLEFLR VSKIPVSNIS IGPVYKRDVM
QAGIMLEKAP EYAVMLCFDV KVDKEAAAYA QEVGVKIFTA DIIYHLFDAF TKHMSELAEK
KKEESKLQAV FPCVLKTVAV FNKKDPIVIG VDVIEGSLRL LTPIAAVKTS ATGTKEIVVL
GRVSSIERDH KAVNICKKGQ PSVAIKIEGS NQPMYGRHLE ESDMLYSQIS RASIDTLKEF
YRSEVSMDEW NLIRKLKPLF DVS
//
