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Database: UniProt
Entry: A0A5N5PWX2_9PEZI
LinkDB: A0A5N5PWX2_9PEZI
Original site: A0A5N5PWX2_9PEZI 
ID   A0A5N5PWX2_9PEZI        Unreviewed;       262 AA.
AC   A0A5N5PWX2;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   08-NOV-2023, entry version 10.
DE   RecName: Full=Elongation factor 1-beta {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GE09DRAFT_1078974 {ECO:0000313|EMBL:KAB5583457.1};
OS   Coniochaeta sp. 2T2.1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5583457.1, ECO:0000313|Proteomes:UP000325492};
RN   [1] {ECO:0000313|EMBL:KAB5583457.1, ECO:0000313|Proteomes:UP000325492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5583457.1,
RC   ECO:0000313|Proteomes:UP000325492};
RX   PubMed=31572496;
RA   Mondo S.J., Jimenez D.J., Hector R.E., Lipzen A., Yan M., LaButti K.,
RA   Barry K., van Elsas J.D., Grigoriev I.V., Nichols N.N.;
RT   "Genome expansion by allopolyploidization in the fungal strain Coniochaeta
RT   2T2.1 and its exceptional lignocellulolytic machinery.";
RL   Biotechnol. Biofuels 12:229-229(2019).
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC       {ECO:0000256|ARBA:ARBA00007411, ECO:0000256|RuleBase:RU003791}.
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:KAB5583457.1}.
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DR   EMBL; VSMA01000002; KAB5583457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5PWX2; -.
DR   Proteomes; UP000325492; Unassembled WGS sequence.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd00292; EF1B; 1.
DR   Gene3D; 1.20.1050.130; -; 1.
DR   Gene3D; 3.30.70.60; -; 1.
DR   InterPro; IPR036219; eEF-1beta-like_sf.
DR   InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR   InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   PANTHER; PTHR11595; EF-HAND AND COILED-COIL DOMAIN-CONTAINING FAMILY MEMBER; 1.
DR   PANTHER; PTHR11595:SF21; ELONGATION FACTOR 1-BETA; 1.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   SMART; SM01182; EF-1_beta_acid; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF54984; eEF-1beta-like; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW   ECO:0000256|RuleBase:RU003791};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU003791};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325492}.
FT   DOMAIN          138..166
FT                   /note="Elongation factor 1 beta central acidic region
FT                   eukaryote"
FT                   /evidence="ECO:0000259|SMART:SM01182"
FT   DOMAIN          176..262
FT                   /note="Translation elongation factor EF1B beta/delta
FT                   subunit guanine nucleotide exchange"
FT                   /evidence="ECO:0000259|SMART:SM00888"
FT   REGION          123..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..150
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   262 AA;  28580 MW;  02D1010EAD99BC9E CRC64;
     MGFTDLVSDA GLASELFPPP SPAEMRSPPA GIGVANRNLS LRKVLNNWLL TRSYVVGYTP
     SQADVTTFKA LSSGPDAAKY PNAARWYKHI ASFEDEFPTL AGDATKPYTA YGPEQAEVTL
     NPAKAPAAAE EEDDDVDLFG SDDDEEEDVE AAKLREERLA EYRKKKEGGK PKPAAKSIVT
     MDVKPWDDET DMQALEAGVR GIEQDGLVWG ASKLVPVGYG VRKLQINLVV EDEKVSIDDL
     QDKIADLEDY VQSSDVVAMQ KL
//
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