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Database: UniProt
Entry: A0A4U5UL44_COLLU
LinkDB: A0A4U5UL44_COLLU
Original site: A0A4U5UL44_COLLU 
ID   A0A4U5UL44_COLLU        Unreviewed;       725 AA.
AC   A0A4U5UL44;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Elongation factor 1-delta {ECO:0000256|ARBA:ARBA00039378};
GN   ORFNames=D9C73_009043 {ECO:0000313|EMBL:TKS74960.1};
OS   Collichthys lucidus (Big head croaker) (Sciaena lucida).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Collichthys.
OX   NCBI_TaxID=240159 {ECO:0000313|EMBL:TKS74960.1, ECO:0000313|Proteomes:UP000298787};
RN   [1] {ECO:0000313|EMBL:TKS74960.1, ECO:0000313|Proteomes:UP000298787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JT15FE1705JMU {ECO:0000313|EMBL:TKS74960.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TKS74960.1};
RA   Cai M., Xiao S.;
RT   "Genome Assembly of Collichthys lucidus.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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; CM014085; TKS74960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U5UL44; -.
DR   STRING; 240159.A0A4U5UL44; -.
DR   Proteomes; UP000298787; Chromosome 8.
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; 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.
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:UP000298787}.
FT   DOMAIN          605..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..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          531..565
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        10..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..614
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  79644 MW;  F6E4D824BE1B27CA CRC64;
     MMSKKIPQCS AVDHSENDQP PSNGQADRSA NASLGCRIKA ESSQRNGETA SSSPESGSLN
     GDGKRSGKSR RRKKRSSNPE SRPEGKVDGS KTKNEEKPDK KTTQPPDPRA GLIGLQSECA
     NVWFERSLYE RAESLYQSWL ASSSNGTTQS KRSPSAPGKA SKSPPAVAPS SSGPACHHGD
     QVACHHVVQA VWVNKTSFDQ AERRFVEESM QSIPNSLNLP LQPNRSITPR TPDEGYQSLA
     PTPATPVIQE AAVTPTNRQS INGLPRIPVE LLRDVWLEKP LYDRAEAAFY QNLYGNNSKR
     SSCASTTRSS DHPQSLVEEE EEEEEDEDVA AAAAAAEKRV VPQGKAEVFH ALLPIQEEEE
     PAEVPEKEEA ASGSGVRYFV HPDSERVWLD KWRYDAAESR FHGHSGRDAV VVKKSRRPEA
     ASVASAAPMR DNTMSSLDFL AQEKIWFDKT RYDEAERRFY ECVNGPTQPT QDVGANTILQ
     DIARARENIQ KSLAGLKKTL CNRGSAQPPP SQQPQLSSSS AADQGEIVCR IKSLELENQS
     LHKVVDDLRA ALSKLECRVA VLEKSPAAVT PAPAPSVPYT NGTTVQQKSS APAKEEEEDD
     DDIDLFGSDE DDDEAEKLKE QRLKEYAERK AKKPGIIAKS SILLDVKPWD DETDMVKLEE
     CVRSVQVDGL LWGTSKLVPV GYGIKKLQIA CVVEDDKVGT DLLEEEITKF EDYVQSVDVA
     AFNKI
//
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