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Database: UniProt
Entry: A0A0F4Z984_9PEZI
LinkDB: A0A0F4Z984_9PEZI
Original site: A0A0F4Z984_9PEZI 
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
//
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