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Database: UniProt
Entry: A0A2N5S7D9_9BASI
LinkDB: A0A2N5S7D9_9BASI
Original site: A0A2N5S7D9_9BASI 
ID   A0A2N5S7D9_9BASI        Unreviewed;       822 AA.
AC   A0A2N5S7D9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=PCANC_23963 {ECO:0000313|EMBL:PLW09139.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW09139.1, ECO:0000313|Proteomes:UP000235388};
RN   [1] {ECO:0000313|EMBL:PLW09139.1, ECO:0000313|Proteomes:UP000235388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW09139.1};
RA   Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA   Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA   Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT   "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT   Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL   Submitted (NOV-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:PLW09139.1}.
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DR   EMBL; PGCJ01001121; PLW09139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5S7D9; -.
DR   STRING; 200324.A0A2N5S7D9; -.
DR   Proteomes; UP000235388; 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:UP000235388};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          384..610
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..323
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   822 AA;  90006 MW;  6768DB35EE1E56EF CRC64;
     MRAPVTRLQE WTLSAAKPEP RSHSLQSLAR SPTTSTFNPI ENKREEDIHM NPNANSFQGF
     RPGANSFVPG GGAPPPPGSS NPQQQQQQQP PAPDGSQPPY PGYYPGQGYG SSHPNYPQHG
     APQNYGYHQQ YQQHHHLQQQ QQHQHQYQYP GGYGAPQQYY NHHPQQAPQS QYNRHHPHPK
     QQQQQQQQQQ APDNWEEEAP PRPATQPPQA SSGATATVNS NGSKTLSLSS TTRLKQMSAN
     SDKPAVVSLN IGGKKKDTPP APAPAAKTDS KLSSTARSQT PTQANKKVIT IGGSSSSTTT
     KSPAPTPPSE SITPEPPSAD PAPASTPAVE ATLAAATKTL TIGETRRPVL DADAIKNEVE
     AAVDSETLRD LYESKKDDVK EEGKPHANIV FIGHVDAGKS TMGGNILYLT GMVDKRTMEK
     LEKEAKDAGK ESWYLSWALD STIQERAQGK TVEIGRAYFE TDARRYTILD APGHKTYVPA
     MISGASQADI AILVISARKG EFETGFERGG QTREHAMLVK TTGVSKLVVV INKMDDITVE
     WDQTRYDEIV NKLTPFLKLS GFNPAKDITF IPVSGYTGAN IKDRLSKEKC SWYDGPSLLE
     LLDNMKLTDR KYNAPLMMPI SEKYKDMGAV VVGKLESGKV SKGEAVLMMP NKTPAEVSAI
     YNEMEDEIPR ALCGDNVRIR LKGIEDEDIM CGFVLTDAHK PIHTVTRFEA QLAILDSKNI
     ICAGYGAVMH VHTLAEECTL SALLHYYDKK TGKKSRRPPQ FAKKGMKVVA LLETAALISV
     ETFKDHPQLG RFTLRDEGKT IAIGKITKLL ESANPDDAST KT
//
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