ID A0A0F4Z984_9PEZI Unreviewed; 1000 AA.
AC A0A0F4Z984;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-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=TD95_001145 {ECO:0000313|EMBL:KKA27072.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA27072.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA27072.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA27072.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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:KKA27072.1}.
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DR EMBL; LAEV01001896; KKA27072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4Z984; -.
DR OrthoDB; 4928at2759; -.
DR Proteomes; UP000033483; 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 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:UP000033483}.
FT DOMAIN 406..624
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..144
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..371
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1000 AA; 109951 MW; 74E5D253EEB41375 CRC64;
MAPKKKGGKK AAMEDWENEL GEAAPGVAPA DAPAAADPVD DAGEAEEENA GGGGLMAIMR
RKQKQKKEAA PPPPADNAEP GRLLTKSEKE KLKKEREKQR KKEQAAAKKK SGPAPAAQKA
EPAKAEVKEA TPEPVAEPVA APETGGSKKK IPAHLRLIQK QQEERRKREE EAAAAAAAEK
ARLEELERKE AEEARRREEV KAAKKQREKE RIEQLKREGK FLTKAQREEK ARNERKLQQM
LAAGIKVGAM EDEEKETDKK KKADQRKKGR GGPSKVDEQK ALEEAAERAR LEAEAIAKAA
ADKAAAEKAK AEEEAKAAAA AKAAEEDDVK DSWDASSDEE DEEQEDEKKA DGKADDDDND
DDDEESEDEE AVSQRVAAEA QRKKEAAERR EKAHQAALAA RSADNLRSPI CCILGHVDTG
KTKLLDKVRQ TNVQEGEAGG ITQQIGATYF PVEAIKQKTQ VVNKDNSFEF KVPGLLIIDT
PGHESFSNLR SRGSSLCNIA ILVVDIMHGL EQQTLESMKI LRDRKTPFIV ALNKIDRLYG
WEKIDNNGFR ASLEHQASSV QNEFHNRLQQ TKLAFAEQGF NAELFYENRN MSRNVSLVPT
SAHTGEGVPD LLKLLLQLTQ ERMVGSLMYL SEVQATVLEV KAIEGFGMTI DVILSNGVLH
EGDRIVLCGT EGAIVTNIRA LLTPAPMREL RVRGAYVHNK EVKAAMGVKI SAPGLEGAIA
GSRLMVVGPD DDEDDLIDEV ESDLATLFSR VETTGRGVSV QASTLGSLEA LLDFLKDCKI
PVATVGIGPV YKRDILQTGI MLEKSPDHAV MLCFDVKVDK EAQQYADENG IKIFQADIIY
HLFDAFTKHQ AEMLEKKKEE SKMLAVFPCV LNTVAVFNKT TPIVIGVDVI EGQLKINTPL
AAVRTGSNGQ KEIVPIGRVT SIERDHKQVP VCKKGQPSVA VKIEMGSSQP TYGRQLEEPD
RIYSLISRAS IDCLKNFYRA DVTNEEWLLI KKLKPVFDID
//