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Database: UniProt
Entry: H2UBH0_TAKRU
LinkDB: H2UBH0_TAKRU
Original site: H2UBH0_TAKRU 
ID   H2UBH0_TAKRU            Unreviewed;       453 AA.
AC   H2UBH0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Elongation factor 1-delta {ECO:0000256|ARBA:ARBA00039378};
GN   Name=LOC101071471 {ECO:0000313|Ensembl:ENSTRUP00000034288.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000034288.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000034288.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000034288.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC       {ECO:0000256|ARBA:ARBA00007411}.
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DR   AlphaFoldDB; H2UBH0; -.
DR   STRING; 31033.ENSTRUP00000072005; -.
DR   Ensembl; ENSTRUT00000034414.3; ENSTRUP00000034288.3; ENSTRUG00000013449.3.
DR   eggNOG; KOG1668; Eukaryota.
DR   GeneTree; ENSGT00950000183014; -.
DR   HOGENOM; CLU_047136_0_0_1; -.
DR   TreeFam; TF313134; -.
DR   Proteomes; UP000005226; Chromosome 22.
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; 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; 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:SF26; ELONGATION FACTOR 1-DELTA; 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   PROSITE; PS00824; EF1BD_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT   DOMAIN          340..365
FT                   /note="Elongation factor 1 beta central acidic region
FT                   eukaryote"
FT                   /evidence="ECO:0000259|SMART:SM01182"
FT   DOMAIN          374..451
FT                   /note="Translation elongation factor EF1B beta/delta
FT                   subunit guanine nucleotide exchange"
FT                   /evidence="ECO:0000259|SMART:SM00888"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          272..306
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        17..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  50253 MW;  F2E0177EE5883A25 CRC64;
     MGDPLPNLPH ALPLGDLSLS SNPSLERSKN PSLERSIIKS KAQFGRVRRH SRLSQSESSG
     AEEEWLSPSA DATSSYARSP FLQCIPAQGL MYHRSAFEQA ESTDQCWARS NSNEVLSSSP
     RSPNTRSYFG SQSGLSRSLH QNKGHPAAPM KSSGTHHHQS IRGRNRTSSE TEPRAKSSKT
     PTQRKRGLSE TESWTLRDNI NMSGLQCLAS ENVWFDKHRF DEAEKRFYEG ANGPAPQQQQ
     VKTATHQAKG RHQKRQHRNS SSHGDQELVS RMKSLELENQ SLHKVVENMK AALQKLESRV
     AVLEKAPTKA AVPCAKAAPV QAAPVKQVAN GDDDDDDLDL FGSDEEDEDT ARIKQERLDA
     YAAKKSKKPA LIAKSSILLD VKPWDDETDM SMLEKCVRSV QMDGLLWGAS KLVPVGYGIK
     KLQINCVVED DKVGTDILEE EITKFEDFLP ISS
//
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