ID A0A2K3Q9N1_9HYPO Unreviewed; 455 AA.
AC A0A2K3Q9N1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Elongation factor 1-gamma 1 {ECO:0000313|EMBL:PNY24265.1};
DE Flags: Fragment;
GN ORFNames=TCAP_05790 {ECO:0000313|EMBL:PNY24265.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY24265.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY24265.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY24265.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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:PNY24265.1}.
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; NRSZ01000930; PNY24265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3Q9N1; -.
DR STRING; 45235.A0A2K3Q9N1; -.
DR OrthoDB; 159792at2759; -.
DR Proteomes; UP000236621; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR CDD; cd03044; GST_N_EF1Bgamma; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 1.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR PANTHER; PTHR43986:SF13; GLUTATHIONE S-TRANSFERASE AN1595-RELATED; 1.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|PROSITE-
KW ProRule:PRU00519};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000236621};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..116
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 121..247
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 294..455
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 249..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PNY24265.1"
SQ SEQUENCE 455 AA; 51068 MW; DB5AF5D77F0A0864 CRC64;
AAGIENFLRA PPLLFAASST SRPPVIPAEF INPEKMAFGT LFTTADNPRS TAIKVVAKAN
NLDLKIVEAD TTKPSSEHLK ANGLGKIPSF IGEDGYALSE CIAIAIYITS QNEKTTLLGK
TKQDYASILK WMSLFNSEIV PNMGNWFLPL IGKAPYNKKS VDDASKAVQK AIVVIEKHLV
RHTYLVGERI TLADLFCAAL LYRGFQYFFD QQWRQQNPAV TRWYETVVNQ PIYSAVAKKL
DFLEKPALTN TAPKKADQPK KADQPKKADQ PKEAPKPAAA PADAEEEPAA APKAKHPCEA
LPKSSFALDE WKRHYSNNET PEALKWFWEN VPLEEDYSIW RCDYKYNDEL TLTFMSNNLI
GGFNARLEGS RKYLFGCASV YGVKNDSVIQ GAFVIRGQEF EPVFDVAPDY ECYHIIKLDP
KKAEDREFLE AQWSWEKPVT VNGKEYPHAA GKVFK
//