EF3_PHYIT
ID EF3_PHYIT Reviewed; 1038 AA.
AC D0MYB4;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Elongation factor 3 {ECO:0000303|PubMed:29300771};
DE Short=EF-3 {ECO:0000305};
DE EC=3.6.4.- {ECO:0000269|PubMed:29300771};
DE AltName: Full=Eukaryotic elongation factor 3 {ECO:0000303|PubMed:29300771};
DE Short=eEF3 {ECO:0000303|PubMed:29300771};
GN Name=TEF3 {ECO:0000305}; ORFNames=PITG_03712 {ECO:0000312|EMBL:EEY66162.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000312|Proteomes:UP000006643};
RN [1] {ECO:0000312|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000312|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29300771; DOI=10.1371/journal.pone.0190524;
RA Mateyak M.K., Pupek J.K., Garino A.E., Knapp M.C., Colmer S.F., Kinzy T.G.,
RA Dunaway S.;
RT "Demonstration of translation elongation factor 3 activity from a non-
RT fungal species, Phytophthora infestans.";
RL PLoS ONE 13:e0190524-e0190524(2018).
CC -!- FUNCTION: Ribosome-dependent ATPase that functions in cytoplasmic
CC translation elongation (PubMed:29300771). Required for the ATP-
CC dependent release of deacylated tRNA from the ribosomal E-site during
CC protein biosynthesis (By similarity). Stimulates the eEF1A-dependent
CC binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced
CC affinity for tRNA as long as the E-site is occupied (By similarity).
CC {ECO:0000250|UniProtKB:P16521, ECO:0000269|PubMed:29300771}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:29300771};
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P16521}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16521}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; DS028121; EEY66162.1; -; Genomic_DNA.
DR RefSeq; XP_002906761.1; XM_002906715.1.
DR AlphaFoldDB; D0MYB4; -.
DR SMR; D0MYB4; -.
DR STRING; 4787.PITG_03712T0; -.
DR EnsemblProtists; PITG_03712T0; PITG_03712T0; PITG_03712.
DR GeneID; 9467656; -.
DR KEGG; pif:PITG_03712; -.
DR VEuPathDB; FungiDB:PITG_03712; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_002848_0_0_1; -.
DR InParanoid; D0MYB4; -.
DR OMA; VLSEAMW; -.
DR OrthoDB; 164580at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IGI:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IGI:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR015688; Elongation_fac_3.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR19211:SF5; PTHR19211:SF5; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Elongation factor; Hydrolase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1038
FT /note="Elongation factor 3"
FT /id="PRO_0000452345"
FT REPEAT 93..131
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 133..170
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 174..211
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 213..249
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 255..287
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 292..331
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT DOMAIN 426..654
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 680..995
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1012..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 714..721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1038 AA; 115702 MW; EFB9A1170CAA32E6 CRC64;
MAPYAPTDGI SKLAIDQSKH FTEALKEALK SSADQQKVAA EKVSELVAGD ANLNLGVVSQ
ELRNALTGND ADAKVVAAHV VDDLMQKHAE RVEAYLLPLL SVFLDLLGDK KPTVRPVAQE
AALTIISSAN KNSTIRILPI LFDGLDRSKK WQTKKGALDL IAELSKVAPY QVGRCLPDII
PQVTDCMWDT RKEVKVAARD TMTKVCNVVG NMDIEPFIPA LVSCLANPTE VPECTHKLAS
TTFVKTVEAP ALAIMEPLLK RALAEGKTAV KRQAAVIIDN MCKLMDDPAE AQLFIPKLLP
GLKKVIETQA DPECREVATR AHETLFVAGG SMEVSEDELK VDYANIHKVV VESIAANPTA
VKANIDSFVV DYVTGICYFL VVSRNFNKAV FEKEITTYIK AFMKPEEIKP LANEIRDRCF
KENKSIFIED VDCDEGIPDL CNCEFSLAYG GMILLNNARL RLKRGHRYGL CGPNGCGKST
LMRAISNGQL EGFPSRDELK TVFVEHNLQA SEAELSVVDF ILVDEDLKNT PRKEVEDTLA
GVGFTAEMQA QGVGTLSGGW KMKLELARAM LQKADILLLD EPTNHLDVKN VAWLENYLTS
LTNVTSIMVS HDSGFLDTVC TNIIHYETRK LKIYKGNLSK FVEQKPEAKA YYELESENVK
FIFPEPGFLA DIKNKGKPII RLTNCSYQYP GTPKPSINNI SVTCALSSRI AVLGPNGAGK
STLIKMLTGE VEPTSGQVWK HPSMRFAYVA QHAFHHIESH LDETANQYIQ WRFQSGEDKE
LLAKETRKLS KEEKEHYKKP VNWEGEKRVL EEIVSRRKFK KSFEYELKWE KCPVDDNAWV
PREKCEKWGW DKLLQIADDR EAARANLQAR PPTAIAVQKH LDCFGLGAEF GTHSRMRGLS
GGQKVKVVLA AAMWLNPHIL VLDEPTNYLD RDSLGALASA IKEFNGGVVM ITHHNEFSSA
LTQETWNVEA GFLVIEGQQA EDKTKIEQKN EEEVTDAFGN VTKTKIKRKL TRKEKKAKDK
ARKEAEARGE YYSDSDEE
