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Database: UniProt
Entry: A0A2C5YHU1_9HYPO
LinkDB: A0A2C5YHU1_9HYPO
Original site: A0A2C5YHU1_9HYPO 
ID   A0A2C5YHU1_9HYPO        Unreviewed;       715 AA.
AC   A0A2C5YHU1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=CDD81_7029 {ECO:0000313|EMBL:PHH66554.1};
OS   Ophiocordyceps australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH66554.1, ECO:0000313|Proteomes:UP000226192};
RN   [1] {ECO:0000313|EMBL:PHH66554.1, ECO:0000313|Proteomes:UP000226192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Map64 {ECO:0000313|EMBL:PHH66554.1,
RC   ECO:0000313|Proteomes:UP000226192};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT   behavioral manipulation genes and a possible major role for enterotoxins.";
RL   Submitted (JUN-2017) 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}.
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:PHH66554.1}.
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DR   EMBL; NJET01000007; PHH66554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5YHU1; -.
DR   STRING; 1399860.A0A2C5YHU1; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000226192; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000226192};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          281..508
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          100..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   715 AA;  78021 MW;  7AA19E8E9F7D579B CRC64;
     MADLNSWEDD PAAQQDENLA RQAQQQLGMN AQNAHAQGSF RPNVASFQPT AQTFQPGQAY
     GGNFMPQYQS QFYQQGHYPQ YNQYNQGYGG GFSQGYSQPY GAAYSPYGQQ QHGQQPPQPQ
     QPAGAQNPLA SLKSQAAGSS VTSAPQPKTV LSTEGGTKVL SIGGDTSGTK PKAKVLSIGG
     SSTPVKDKEE AKADTKVEPS NKPEAGQKAT AAKAIEKTGE KAGKPSAGTA KSSGKTSPTP
     SSGRSSPAGP GERKALRDAD VVSKDQAADV DDETLKEIYG KEHVNIIFIG HVDAGKSTLG
     GSILWSTGMV DERTMDKYKR EAKDMGRESW YLSWVMDLTK EERSKGKTVE VGRGFFETDK
     RRYSILDAPG HKTYVPNMIG GASQADVGIL VISARKGEYE TGFERGGQTR EHAMLAKTQG
     VNKLVVVINK MDDPTVEWSN ERYQECITKL SQFLKATGYN LKTDVFFMPV AAQQSMNIKE
     RLPKDVAPWW QGPSLLEYLD NMKALERKVN APFMMPINAK YRDMGTMVDG KIEAGVVKKG
     MSLVMMPRKQ AVEAAAIYGE QEEEVPIVQC GDQVRMRLKG IEEEDILPGF VLCSPKRLVH
     CVAEFEAQIR ILELKSILTS GFNCVLHVHS AIEEVTFAAL LHKLQKGTNR KSKIPPTHAK
     KGDSIIARMQ VIGGAGSVCV EKFEDYPQMG RFTLRDQGQT IAIGKITKLI TDESN
//
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