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Database: UniProt
Entry: A0A1E3QQP9_9ASCO
LinkDB: A0A1E3QQP9_9ASCO
Original site: A0A1E3QQP9_9ASCO 
ID   A0A1E3QQP9_9ASCO        Unreviewed;       732 AA.
AC   A0A1E3QQP9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=BABINDRAFT_161656 {ECO:0000313|EMBL:ODQ80009.1};
OS   Babjeviella inositovora NRRL Y-12698.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX   NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ80009.1, ECO:0000313|Proteomes:UP000094336};
RN   [1] {ECO:0000313|Proteomes:UP000094336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) 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; KV454431; ODQ80009.1; -; Genomic_DNA.
DR   RefSeq; XP_018985337.1; XM_019128936.1.
DR   AlphaFoldDB; A0A1E3QQP9; -.
DR   STRING; 984486.A0A1E3QQP9; -.
DR   GeneID; 30146789; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000094336; 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; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 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:UP000094336};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          307..531
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  80034 MW;  1A67C97D842F20FE CRC64;
     MSENAQGSTP ESLSNDMQNA SISTPGNRFD SAKAPVFTPG ASFTPGEPAA FVPGQGQYTN
     YNQGYNAQQG YNSNQGGYKN YNQGQGYNNY NQGQQGGYKN YNQGQQGGYN NYQQGYNQQQ
     GYNQQQGYNN YNQQQGYNNN RGYNQGGYTN YNQQQPQQGG AMSLEDYKKQ QQASLNSLNK
     PIKKTVLKLD ASSGIKLANA TKPAEKKEES PKEEAKEAAV EKEEVKVAKE AKIAPPAATA
     APAAAVAPAA AVAPAAAVAP AAAVSASPAV SALPSKASTP VASVDALIKE QEDEVDVEVV
     NDMFGGKDHV SIIFMGHVDA GKSTMGGNIL YLTGSVDKRT VDKYEREAKE AGRQGWYLSW
     VMDTNKEERN DGKTIEVGKA YFETEKRRYT LLDAPGHKMY VSEMIGGASQ ADIGILVISA
     RKGEYETGFE KGGQTREHAL LAKTQGVNKI IVAINKMDDV TVAWSKERYD ECCSKLGQYL
     RGIGYAKDDI IFMPVSGYTG AGLKERVSPE ECPWYSGPAL LEYLDTMKTL DRHINAPFML
     PIAGKMKDMG TIVEGKIESG HVKKGQNLVV MPNKTTIEVL SIFNETEQEC DIAYCGEQVR
     MKLRGIEEED LSQGYVLTSV KNPVKTVTRF EAQVAMVELK SILSNGFSCV MHVHTAIEEV
     TFVELKHKLE KGTNRKSKKP PAFAKKGMKI IAILETTEPV CMETYAEYPQ MGRFTLRDQG
     TTIAIGKITK LL
//
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