ID   A0A3F3QA99_9EURO        Unreviewed;       727 AA.
AC   A0A3F3QA99;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit {ECO:0000256|ARBA:ARBA00015765};
DE   AltName: Full=ERF-3 {ECO:0000256|ARBA:ARBA00031881};
DE   AltName: Full=ERF2 {ECO:0000256|ARBA:ARBA00030845};
DE   AltName: Full=Polypeptide release factor 3 {ECO:0000256|ARBA:ARBA00029585};
DE   AltName: Full=Translation release factor 3 {ECO:0000256|ARBA:ARBA00030210};
GN   ORFNames=BDQ94DRAFT_138519 {ECO:0000313|EMBL:RDH36088.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH36088.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH36088.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH36088.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR   EMBL; KZ852038; RDH36088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3QA99; -.
DR   STRING; 1341132.A0A3F3QA99; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000253729; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR   GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:InterPro.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd03704; eRF3_C_III; 1.
DR   CDD; cd04089; eRF3_II; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003285; Sup35.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   PANTHER; PTHR23115:SF36; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   PRINTS; PR01343; YEASTERF.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000313|EMBL:RDH36088.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          280..513
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   727 AA;  77978 MW;  93ECBB6CE924CF6D CRC64;
     MADQTPDSWE DELSRQTEGV RLNPNAQGRP QPQAPSFHPG AATFTPGAAS FVPGQAYQPY
     GGGFPQYGQY GQQAYGGYPY DQQQQAYAQY GAYAQQPGGF NNNQIYNQQY GGYQQQQQQP
     RQAAAPAAAQ PAQPAPKPAA SNAAPPKAKV LSIGGASNSP AAPKTKVLSI GTPSPAPTSS
     TPSSTSGAAT PGDTKGAAAV EAAAKVTASK AIEKTEKKAD AKAAASGKSS PTPSGRSSPG
     RSSPARGEAA KAARNADAVA MEQQADVDEA TLKEIYGEKK EHVNIVFIGH VDAGKSTLGG
     SILYVTGMVD ERTLEKYKRD AKEAGRETWY LSWALDLTNE ERAKGKTVEV GRAHFQLPVK
     GADGSTITRH FSILDAPGHK SYVHHMIGGA SQADVGVLVI SARKGEYETG FEKGGQTREH
     ALLARNTGVK TLIVAVNKMD DPTVEWSKAR FDECTVKVGK YLENLGYKKS DLFFMPISAQ
     RTTGIKDRVP TDLAPWYGGP SLLEFLSEMK VPERKINAPF MMPISAKYRD MGTMVEGRIE
     SGVLKKNGSC IMMPNRTKVE IAALYGETED EIPTATCGDQ VRLRLRGVEE EDILPGFVLC
     SPKRLVNCVK TFEAKIRILD LKSILTAGYN CVMHVHSAVE EVTVAALLHK CEPGTGRRSK
     RPPPFASKGQ TIIARLEVTS TAGAVCVERF EDYNQMGRFT LRDQGQTVAI GMITKLISAE
     EVAQAQA
//