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Database: UniProt
Entry: A0A5A9P9L0_9TELE
LinkDB: A0A5A9P9L0_9TELE
Original site: A0A5A9P9L0_9TELE 
ID   A0A5A9P9L0_9TELE        Unreviewed;       468 AA.
AC   A0A5A9P9L0;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Elongation factor 1-delta {ECO:0000256|ARBA:ARBA00039378};
GN   ORFNames=E1301_Tti013173 {ECO:0000313|EMBL:KAA0718593.1};
OS   Triplophysa tibetana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Nemacheilidae; Triplophysa.
OX   NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0718593.1, ECO:0000313|Proteomes:UP000324632};
RN   [1] {ECO:0000313|EMBL:KAA0718593.1, ECO:0000313|Proteomes:UP000324632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0718593.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAA0718593.1};
RX   PubMed=30977968;
RA   Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA   Wang W., Yang R.;
RT   "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT   to the harsh high-altitude environment of the Tibetan Plateau.";
RL   Mol. Ecol. Resour. 19:1027-1036(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:KAA0718593.1}.
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DR   EMBL; SOYY01000007; KAA0718593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5A9P9L0; -.
DR   Proteomes; UP000324632; Chromosome 7.
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; 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:UP000324632}.
FT   DOMAIN          348..373
FT                   /note="Elongation factor 1 beta central acidic region
FT                   eukaryote"
FT                   /evidence="ECO:0000259|SMART:SM01182"
FT   DOMAIN          382..468
FT                   /note="Translation elongation factor EF1B beta/delta
FT                   subunit guanine nucleotide exchange"
FT                   /evidence="ECO:0000259|SMART:SM00888"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  52765 MW;  B4D42F6F118D4911 CRC64;
     MLQLGLRMEN QKGSRAKDQS TRVQTGSRSD LPKSNDGKRK RTRSYRSEQQ GSEVEGHFHL
     EPISQGVGER VWFNSSIYEQ ADVAYQTLLS SGSGTPLVPP KERIPHTLVF RSKRNTGHPY
     QEENFTYTRC FTSRREKQDS NHQRSSSEPK RAQHVTSGSR KRVYSATECA PPRRENITMS
     ALQGLAQEKI WFDKSRYDEA ERSFYEGENG IEQTPQEKEA SAILQDIAKA RENIQKSLSG
     VKTALQACKG HARSQKPRER KTSQNASKSE DQSEVISRMK SLELDNKNLH KVVDDLRAML
     SKLESRMAVL EKSQGPANKT APVAKAAPIQ KPKVAEQNGA DDNDDIDLFG SDEEDEEAER
     IKAERVKEYA ARKSKKPVLI AKSSILLDVK PWDDETEMSK LEECVRSIQM DGLLWGASKL
     VPVGYGIKKL QIGCVVEDDK VGTDILEEEI TKFEDYIQSV DIAAFNKI
//
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