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Database: UniProt
Entry: A0A0F7ZLD0_9HYPO
LinkDB: A0A0F7ZLD0_9HYPO
Original site: A0A0F7ZLD0_9HYPO 
ID   A0A0F7ZLD0_9HYPO        Unreviewed;       717 AA.
AC   A0A0F7ZLD0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=HIM_04348 {ECO:0000313|EMBL:KJZ76266.1};
OS   Hirsutella minnesotensis 3608.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX   NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ76266.1, ECO:0000313|Proteomes:UP000054481};
RN   [1] {ECO:0000313|EMBL:KJZ76266.1, ECO:0000313|Proteomes:UP000054481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3608 {ECO:0000313|EMBL:KJZ76266.1,
RC   ECO:0000313|Proteomes:UP000054481};
RX   PubMed=25359922; DOI=10.1093/gbe/evu241;
RA   Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA   Bushley K.E., Xiang M., Liu X.;
RT   "Comparative genomics and transcriptomics analyses reveal divergent
RT   lifestyle features of nematode endoparasitic fungus Hirsutella
RT   minnesotensis.";
RL   Genome Biol. Evol. 6:3077-3093(2014).
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; KQ030512; KJZ76266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7ZLD0; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000054481; 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:UP000054481};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          283..510
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   717 AA;  78088 MW;  92E6D40E73A81231 CRC64;
     MSDLNSWEDD PAAQDDELSR QAKQQLNMNP QNPAQAQGGF RPGVASFQPG AQSFQPGQAY
     GGNFAPGYQQ QQYYQQGYYP QYGQQQGFNQ YNQGYGGGFS QGYNQGYGAG YPQYGQQGQQ
     PPQPQQPAAA QAPAAAPKQP AADATAAAPK PVLTKEGGTK VLSIGGDTSA PKPKAKVLSI
     GGSSAPAKEK EEAKAEVKTE PSNTPEAGQK ATAAKAIEKT GEKAGKAAAG ASKTTGKTSP
     TPSSGRSSPS GPGEKKAQRD ADAVAKEQTA DVDQETLKEI YGKEHVNIIF IGHVDAGKST
     LGGSILWTTG MVDERTMDKY KKEAKDLGRE SWYLSWVMDL TKEERSKGKT VEVGRGFFET
     EKRRYSILDA PGHKTYVPNM IGGASQADVG ILVISARKGE YETGFERGGQ TREHAMLAKT
     QGVNKLVVVI NKMDDPTVEW SQERYNECTT KLSQFLKATG YNLKTDVFFM PVAAQQSQNI
     KDRIPKDLAP WWEGPSLLEY LDNMTALERK LNAPFMMPVN AKYRDMGTMV DGKIEAGVVK
     KGMNLVMMPR KQSVEAAALY GEQEDEVQFL QCGDQVRMRL KGIEEEDILP GFVLCSPKRL
     VHCVAEFEAQ IRILELKSIL TSGFNCVLHV HSAIEEVTFA ALLHKLQKGT NRKSKLPPTH
     AKRGDSIIAR MQVIGGAGSV CVEKFEDYPQ MGRFTLRDQG QTIAIGKITK LITEESN
//
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