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Database: UniProt
Entry: M5FNC7_DACPD
LinkDB: M5FNC7_DACPD
Original site: M5FNC7_DACPD 
ID   M5FNC7_DACPD            Unreviewed;       221 AA.
AC   M5FNC7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Elongation factor 1-beta {ECO:0000313|EMBL:EJT97215.1};
GN   ORFNames=DACRYDRAFT_25315 {ECO:0000313|EMBL:EJT97215.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT97215.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJT97215.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT97215.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH795878; EJT97215.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5FNC7; -.
DR   STRING; 1858805.M5FNC7; -.
DR   HOGENOM; CLU_050172_0_2_1; -.
DR   OMA; YRWYKHI; -.
DR   OrthoDB; 77945at2759; -.
DR   Proteomes; UP000030653; 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; 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; 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:UP000030653}.
FT   DOMAIN          99..126
FT                   /note="Elongation factor 1 beta central acidic region
FT                   eukaryote"
FT                   /evidence="ECO:0000259|SMART:SM01182"
FT   DOMAIN          135..221
FT                   /note="Translation elongation factor EF1B beta/delta
FT                   subunit guanine nucleotide exchange"
FT                   /evidence="ECO:0000259|SMART:SM00888"
FT   REGION          85..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..106
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   221 AA;  24074 MW;  52530BA3697013C7 CRC64;
     MANFNGLPAL EAHLKSRSYV DGHVPSQADV GVFNSLGSAP SPAEFPHSAR WYKHIQSYAS
     EHATLPGDKA SSSKLFSAAS AVPAKPAVKE EEEEEEIDLF GSDDEEADAE AERIKQERVA
     AYNAKKANKP KAAAKSVVTL DVKPWDDETD MVALESSVRS IEQPGLVWGA SKLVAIGYGI
     KKLQITLVIE DELVSLDELQ EKLAEFDDYI QSTDVQAMQK L
//
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