ID A0A3Q1CEM5_AMPOC Unreviewed; 725 AA.
AC A0A3Q1CEM5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Elongation factor 1-delta {ECO:0000256|ARBA:ARBA00039378};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000026137.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000026137.1}
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, ECO:0000256|RuleBase:RU003791}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q1CEM5; -.
DR STRING; 80972.ENSAOCP00000026137; -.
DR Ensembl; ENSAOCT00000016916.1; ENSAOCP00000026137.1; ENSAOCG00000014204.1.
DR GeneTree; ENSGT00950000183014; -.
DR OrthoDB; 77945at2759; -.
DR Proteomes; UP000257160; Unplaced.
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; 2.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF54984; eEF-1beta-like; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000257160}.
FT DOMAIN 315..342
FT /note="Elongation factor 1 beta central acidic region
FT eukaryote"
FT /evidence="ECO:0000259|SMART:SM01182"
FT DOMAIN 606..630
FT /note="Elongation factor 1 beta central acidic region
FT eukaryote"
FT /evidence="ECO:0000259|SMART:SM01182"
FT DOMAIN 639..725
FT /note="Translation elongation factor EF1B beta/delta
FT subunit guanine nucleotide exchange"
FT /evidence="ECO:0000259|SMART:SM00888"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 528..562
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..611
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 80278 MW; 9639C25C4630C1E9 CRC64;
MSKKIPQCAV EDQSEHEQPP SHCQVDRFTK AAAGCRNKAE PGQRNGETAS SSPESGSLNG
DGKRSGKSRR RKKRSSNPEN PSEEKINKVK NEEKPEKRTS QPPDRRAGLI GLQSECANVW
FERSIYERAE SLYQCRLASS SNGTTQSKRS PPSSGKHSSS PSAVASSSAG PSCHHGDQVA
CHHVVQTVWV NKTTFDQAER RFVEESMQPS IPNSLNLPPP PNRSVAPRTP DEGYQSLAPT
PATPVIQQAA VTPTTRQSIN GLPRIPVELL RDVWLDKPLY DRAEAAFYQN LYGNNSSKRS
SCTGTSRSND HPQSLVEEEE EEEDEEVAVE EKRVVPQGKA EVFHALHPIQ EEDEPAEVPE
KEEASAAGVC YFLHPGSERV WLDKWRYDAA ESRFHGYRVD KAVKVRKDRR PEAGASSVAF
IAPLRDKKMS TVNFLAQEKI WFDKPRYDEA ERCFYERMNG SSQTTQDVGA NTILQDIARA
RENIQKSLAG LKTTLSNRGS NQPSLSQQSQ LSTSSSSAAD QGELISRIKS LELENQSLHK
VVDDLRAALS KLECRVTVLE KSPAAANPAP AAAPSVPYTN GTTVQQKTSA PVKEEDDDED
DDDIDLFGSD DDEEAEKLKE QRLKEYAEKK AKKPTLIAKS SILLDVKPWD DETDMAKLEE
CVRSVQADGL LWGTSKLVPV GYGIKKLQIA CVVEDDKVGT DMLEEEITKF EDYVQSVDVA
AFNKI
//
