ID A0A2V5II42_9EURO Unreviewed; 720 AA.
AC A0A2V5II42;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 22-FEB-2023, entry version 15.
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=BP00DRAFT_421710 {ECO:0000313|EMBL:PYI36358.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI36358.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI36358.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI36358.1,
RC ECO:0000313|Proteomes:UP000248817};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ825465; PYI36358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5II42; -.
DR Proteomes; UP000248817; 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; 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; 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 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 279..509
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..188
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 720 AA; 77538 MW; DA0CA09980A5062B CRC64;
MANQTPESWE DELSRQTEGV NLNNGGRRPQ QQFNYQGSTF TPGAASFTPG AASFVPGQQS
YGGYPQYGQQ YGYQQQQQQQ QQPYGQYGGQ YGAYAQQPGY NQYYNNQQQQ YGGYQQQPQQ
AQQPQQQPKP AAPKPAAKVL SIGAEPKAKV LSLSGASDSP NAPKTKVLSI GGTSASPSPA
TSGTATPGDT KGAAAADAAA KVTASKAIEK TEKKADAKAA ASGKSSPAPA SGRSSPGRSS
PSRAEVAKAA RHADAVAQEQ KADVDEATLN ELYGELEKKE HVNVVFIGHV DAGKSTLGGC
ILVATGMVDE RTLEKYKRDA KEMGRETWYL SWALDLNPEE RAKGKTVEVG RAHFDLQLKN
GVTRSCSILD APGHKAYVHH MIGGATQADV GVLVISARKG EYETGFEKGG QTREHALLAR
NTGVRKLVIA VNKMDDPTVE WSEERFKVCT TKVAKFLEAL GYAKADLTFM PISAQTMVNI
KDRVTKDVCP WYDGPSLLEY LGDMELPPRK LNAPFAMAIS AKYRDMGTMV EGKIDSGIVK
KGSQMVVVPG LAKCEVAALY GETEDEIATG SCGDQVRMRL RGVEEEDLLP GFVLCSPRRL
VHSVHSFEAK IKLLEIKGIL SAGFNCVMHV HSAVEEVTIA ALLHKLEPGT GRRSKKAPAF
ASKGMTVIAR VEVTSTAGQV CCEPFSYSEQ MGRFTLRDQG QTIAIGMITK LIENEEVVAE
//