ID W6Q8C8_PENRF Unreviewed; 227 AA.
AC W6Q8C8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Elongation factor 1-beta {ECO:0000313|EMBL:CDM30494.1};
GN Name=tef5 {ECO:0000313|EMBL:CDM30494.1};
GN ORFNames=PROQFM164_S02g000643 {ECO:0000313|EMBL:CDM30494.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM30494.1};
RN [1] {ECO:0000313|EMBL:CDM30494.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM30494.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC {ECO:0000256|ARBA:ARBA00007411, ECO:0000256|RuleBase:RU003791}.
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DR EMBL; HG792016; CDM30494.1; -; Genomic_DNA.
DR AlphaFoldDB; W6Q8C8; -.
DR STRING; 1365484.W6Q8C8; -.
DR OMA; YYQAERE; -.
DR OrthoDB; 77945at2759; -.
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; IPR049720; EF1B_bsu/dsu.
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; 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}.
FT DOMAIN 105..132
FT /note="Elongation factor 1 beta central acidic region
FT eukaryote"
FT /evidence="ECO:0000259|SMART:SM01182"
FT DOMAIN 141..227
FT /note="Translation elongation factor EF1B beta/delta
FT subunit guanine nucleotide exchange"
FT /evidence="ECO:0000259|SMART:SM00888"
FT REGION 74..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 227 AA; 25223 MW; F966A8CB0DA066DA CRC64;
MGFTDFVSDA GLTLADHFLS TRSYIVGHAP SQADVVTFKA FPAAPDAAKY PNVARWHKHI
ASFEPEFPTL PGDSNAAFTV YGPETTTLPS NPKDKPEEED DDEDLFGSDS EEEDPEVVAE
RNKRLEEYKA KKAGKVKPAA KSIVTMEVKP WDDETNLEEM EANVRAIEQD GLVWGASKWV
PVGFGIRKLQ INLVVEDDKV STDELQQKIE EDEDHVQSTD IAAMQKL
//
