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}.
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; 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
//