GenomeNet

Database: UniProt
Entry: A0A132ALN1_SARSC
LinkDB: A0A132ALN1_SARSC
Original site: A0A132ALN1_SARSC 
ID   A0A132ALN1_SARSC        Unreviewed;       462 AA.
AC   A0A132ALN1;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN   ORFNames=QR98_0099210 {ECO:0000313|EMBL:KPM11350.1};
OS   Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC   Sarcoptidae; Sarcoptinae; Sarcoptes.
OX   NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM11350.1, ECO:0000313|Proteomes:UP000616769};
RN   [1] {ECO:0000313|EMBL:KPM11350.1, ECO:0000313|Proteomes:UP000616769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM11350.1};
RX   PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA   Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT   "Draft genome of the scabies mite.";
RL   Parasit. Vectors 8:585-585(2015).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982, ECO:0000256|RuleBase:RU000325}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC       ECO:0000256|RuleBase:RU000325}.
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:KPM11350.1}.
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   EMBL; JXLN01016985; KPM11350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A132ALN1; -.
DR   VEuPathDB; VectorBase:SSCA003076; -.
DR   OMA; VACTFES; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000616769; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd03693; EF1_alpha_II; 1.
DR   CDD; cd03705; EF1_alpha_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00483; EF-1_alpha; 1.
DR   PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|RuleBase:RU000325,
KW   ECO:0000313|EMBL:KPM11350.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000325};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW   ECO:0000313|EMBL:KPM11350.1}.
SQ   SEQUENCE   462 AA;  50680 MW;  269044FA571A5E2E CRC64;
     MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQDMG KGSFKYAWVL
     DKLKAERERG ITIDITLWKF ETPKYYVTVI DAPGHRDFIK NMITGTSQAD VAVLIVAAGT
     GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDTTEP PFSQSRFEEI QKEVSAYVKK
     IGYNPATVAF VPISGWNGDN MLEPSTNMNW FKGWSIERKG QKMEGKTLLQ ALDAQEPPTR
     PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APAGITTEVK SVEMHHEALQ
     EAVPGDNVGF NVKNVSVKEL RRGYVAGDSK DNPPKGCEEF TAQVIVLNHP GQISNGYTPV
     LDCHTAHIAC KFREIKEKCD RRSGKKLEDM PKSIKSGDAA IIDLAPTKPM CVETFTEFPP
     LGRFAVRDMR QTVAVGVIKS VKPKEAAGGK VTKAAEKAQK KK
//
DBGET integrated database retrieval system