ID A0A2Y9E5P4_TRIMA Unreviewed; 1128 AA.
AC A0A2Y9E5P4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Elongation factor-like GTPase 1 isoform X2 {ECO:0000313|RefSeq:XP_004387565.1};
GN Name=LOC101346010 {ECO:0000313|RefSeq:XP_004387565.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004387565.1};
RN [1] {ECO:0000313|RefSeq:XP_004387565.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_004387565.1; XM_004387508.3.
DR AlphaFoldDB; A0A2Y9E5P4; -.
DR GeneID; 101346010; -.
DR KEGG; tmu:101346010; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|RefSeq:XP_004387565.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|RefSeq:XP_004387565.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT DOMAIN 17..367
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 431..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 126093 MW; EBDF9D2D41F79DF2 CRC64;
MVLNSLDKMI QLQKNTANIR NICVLAHVDH GKTTLADCLI SSNGIISSRL AGKLRYMDSR
KDEQIRGITM KSSAISLHYT KDNEEYLINL IDSPGHVDFS SEVSTAVRIC DGCIIVVDAV
EGVCPQTQAV LRQAWLENIR PVLVINKIDR LIVELKFAPQ EAYSHLKNIL EQINALTGAL
FTSKVLEERA ERETESQGNS SSEQGEQVYD WSTGLENTDD SHLYFSPDQG NVVFTSAIDG
WGFGIEHFAE IYSQKIGIKK EVLLKTLWGD YYINMKAKRI MKVDQAKGKK PLFVQLILEN
IWSLYDAVLK KDKEKIDKIV TSLGLKIGAR EARHSDPKVQ ISAICSQWLP ISHAVLAMVC
QKLPSPLDIT AERVEKLMCT GSQTFDSLPP ETQALKAAFM KCGSEDTAPV IIFVSKMFAV
DAKALPQNKP RPLTQAEIAQ RRERARQRHA EKLAAAQGQA PLEPTQDGSV LETNPKGEEL
RGNEEQVESM TPKPVPQEES NQESFVAFAR VFSGVARRGK KIFVLGPKYS PVEFLQRVPL
GFSAPPDDLP PVPHMAYCTL ENLYLLMGRE LEDLEEVPPG NVLGIGGLQD FVLKSATLCS
LPSCPPFIPL NFEATPIVRV AVEPKHPSEM PHLVKGMKLL NQADPCVQIL IQETGEHVLV
TAGEVHLQRC LDDLKERFAK IQISVSEPII PFRETITKPP KVDMVNEEIG KQQKVAVIHQ
TKEDQSKIPE GIQVDSDGLV TLTTPNKLAT LSVRAMPLPE EVTQILEENS DLIRSIQQLT
SSLNEGRNTQ MIHQKTLEKI WEFKGKLEQH LTGRKWRNVV DQIWSFGPRK CGPNILVNKN
EDLQNSVWPG PVSKASKEVT KYRDLGNSIV SGFQLATLSG PMCEEPLMGV CFVLEKWDLS
KFEGQGANDK QNQEQSDLVK EGQRGDETRS SGDENQELQD GCPEPCEKRT VQKGEASLSD
CYGPFSGQLI ATMKEACRYA LQVKPQRLMA AMYTCDIMAT GDVLGRVYAV LSKREGRVLQ
EEMKEGTDMF IIKAVLPVAE SFGFADEIRK RTSGLASPQL VFSHWEIIPS DPFWVPTTEE
EYLHFGEKAD SENQARKYMN AVRKRKGLYV EEKIVEHAEK QRTLSKNK
//
