ID A0A452ICJ8_9SAUR Unreviewed; 725 AA.
AC A0A452ICJ8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Elongation factor 1-delta {ECO:0000256|ARBA:ARBA00039378};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000025227.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000025227.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A452ICJ8; -.
DR Ensembl; ENSGAGT00000028718.1; ENSGAGP00000025227.1; ENSGAGG00000018441.1.
DR Proteomes; UP000291020; 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; 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.
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:UP000291020}.
FT DOMAIN 603..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 53..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 81393 MW; 1AD2EC1A54C8BBC3 CRC64;
MRTRKLPYPL EKVWLDKHQY DEAERLHYER EATLAASATE ECQEVEAMNS VCHDDPVEGE
LKDMKRVRNG KKQKKRKRSP KTKSLVSKVD FVLTGLLADG VWYDKPFFDH AENMFRKKLA
DDLTQKAPET ELAAEQPALV SWSEEAVPDV HKPRKNPAAL HCTHASLIAC HHVIQDVWVN
KFNFDEAEKV FVERSQSFVH PHFLDLPSVR WNSDYGDVDQ RTPDEGYITA LSTPATPATP
CLSTDVVVHS GASFVTSLPS PACQTINGKP QILSLQALIS GVWLEKPIYD DAEKCFYENM
TDGHPPGKVR PQERSRPEAL KSSRKDKKGR SPGKRMNSRH VEFTTNPSLP KDAEYPPLTW
YFLHKDSEHL WLSKPTYDSA ESQYYASEAL KMSSRQDNSR VPELSLAKPS QPASRAASVP
SSETKKMAAD FLMHEKIWFD KFKYDDAEKR YYEQMNGPVA SPSCQQRKTI LDSPQEAPPA
HSKRKSGRLT SASTTSSAGP AGDQNELVTR IANLEVENQN LHSVIADLQL AISKLETRLN
TLEKCSTSHH PSATPPTQHV TPMKKVESPA APSKKVELPS APPAKKVGPS EADDEDEDDD
IDLFGSGDEE EDQEAAKVRE ERLRQYAEKK SKKPGLIAKS SILLDVKPWD DETDMAKMED
CVRSIQMDGL VWGASKLVPV GYGIKKLQIQ CVVEDDKVGT DILEEEITKF EDYVQSVDIA
AFNKI
//
