EF3_SCHPO
ID EF3_SCHPO Reviewed; 1047 AA.
AC O94489; P78876; Q10266; Q9UUL5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Elongation factor 3;
DE Short=EF-3;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P16521};
GN Name=tef3; Synonyms=ef3; ORFNames=SPCC417.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 731-1047.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 749-1047.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9099890; DOI=10.1016/s0378-1119(96)00764-0;
RA Mita K., Morimyo M., Ito K., Sugaya K., Ebihara K., Hongo E., Higashi T.,
RA Hirayama Y., Nakamura Y.;
RT "Comprehensive cloning of Schizosaccharomyces pombe genes encoding
RT translation elongation factors.";
RL Gene 187:259-266(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 450-962, AND GENE NAME.
RC STRAIN=JY741;
RX PubMed=10361693; DOI=10.1271/bbb.63.769;
RA Uritani M., Shoumura Y., Yamada S.;
RT "Detection and analysis of translation elongation factor 3 genes from
RT various yeasts.";
RL Biosci. Biotechnol. Biochem. 63:769-772(1999).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714; SER-768; SER-783 AND
RP SER-1043, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [7]
RP FUNCTION.
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:0000250|UniProtKB:P16521};
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P16521}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA22654.1; -; Genomic_DNA.
DR EMBL; D89226; BAA13887.1; -; mRNA.
DR EMBL; D82575; BAA11573.1; -; mRNA.
DR EMBL; AB018538; BAA33896.1; -; Genomic_DNA.
DR PIR; T41343; T41343.
DR PIR; T43058; T43058.
DR PIR; T43434; T43434.
DR RefSeq; NP_588285.1; NM_001023275.2.
DR AlphaFoldDB; O94489; -.
DR SMR; O94489; -.
DR BioGRID; 275863; 10.
DR DIP; DIP-59126N; -.
DR IntAct; O94489; 1.
DR STRING; 4896.SPCC417.08.1; -.
DR iPTMnet; O94489; -.
DR MaxQB; O94489; -.
DR PaxDb; O94489; -.
DR PRIDE; O94489; -.
DR EnsemblFungi; SPCC417.08.1; SPCC417.08.1:pep; SPCC417.08.
DR GeneID; 2539295; -.
DR KEGG; spo:SPCC417.08; -.
DR PomBase; SPCC417.08; tef3.
DR VEuPathDB; FungiDB:SPCC417.08; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_002848_0_0_1; -.
DR InParanoid; O94489; -.
DR OMA; VLSEAMW; -.
DR PhylomeDB; O94489; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:O94489; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
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 GO; GO:0002182; P:cytoplasmic translational elongation; ISO:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR040533; 4HB.
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; IPR015688; Elongation_fac_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR19211:SF5; PTHR19211:SF5; 1.
DR Pfam; PF17947; 4HB; 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 PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Elongation factor; Hydrolase; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..1047
FT /note="Elongation factor 3"
FT /id="PRO_0000093457"
FT REPEAT 48..85
FT /note="HEAT 1"
FT REPEAT 91..128
FT /note="HEAT 2"
FT REPEAT 130..167
FT /note="HEAT 3"
FT REPEAT 171..208
FT /note="HEAT 4"
FT REPEAT 210..246
FT /note="HEAT 5"
FT REPEAT 247..284
FT /note="HEAT 6"
FT DOMAIN 411..647
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 673..1000
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1022..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 707..714
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 770..771
FT /note="ED -> DH (in Ref. 3; BAA11573)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="K -> P (in Ref. 3; BAA11573)"
FT /evidence="ECO:0000305"
FT CONFLICT 800..802
FT /note="TQR -> NSS (in Ref. 3; BAA11573)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="G -> R (in Ref. 3; BAA11573)"
FT /evidence="ECO:0000305"
FT CONFLICT 959
FT /note="S -> Y (in Ref. 4; BAA33896)"
FT /evidence="ECO:0000305"
FT CONFLICT 962
FT /note="F -> I (in Ref. 2; BAA13887)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="A -> S (in Ref. 2; BAA13887)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="H -> N (in Ref. 2; BAA13887)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="G -> V (in Ref. 2; BAA13887)"
FT /evidence="ECO:0000305"
FT CONFLICT 988
FT /note="G -> V (in Ref. 2; BAA13887)"
FT /evidence="ECO:0000305"
FT CONFLICT 1001..1002
FT /note="GD -> AE (in Ref. 2; BAA13887)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009..1014
FT /note="NKIEKA -> TKNEKS (in Ref. 2; BAA13887)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="A -> S (in Ref. 2; BAA13887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 115802 MW; 10F5F10DB2E867F1 CRC64;
MSAKSENKQS VKALEELLKH LTVCDAAEEA DAAKALASFV NGPIEEQDAP SQVFSAISKQ
LNDKNATARE RVLKGLEAVA NHGSVAADVE PYLVELLPAV IAKVADKQNA VRDAAIAASK
AIVRCTTPYA VKAIVPSVLE SIHTTGKWNE KMNSLQLLDV LVEVAPSQLS YSLPQIIPVV
SESMWDTKAE VKKQSKETMT KVCTLIANAD IDRFIPELIN CIAHPEEVPE TIHSLGATTF
VTEVQAPTLS IMVPLLARGL NERSTPIKRK TAVIIDNMSK LVEDPQVVAP FLPKLLPGLY
HIKDTIGDPE CRSVVQRAIT TLERVGNVVD GKIPEVSTAA NPEVCLETLK AVLGEIKVPT
NEEVIAKYVA NIAAQLVEEK DNENESWVLN ITPYLTAFID EAHIHKIVEQ LRTRSIAKIP
GGASHAEEEE EGEDLCNCEF SLAYGAKILL NRTRLRLKRG RRYGLCGPNG SGKSTLMRAI
VNGQVEGFPT HLRTVYVEHD IDESEADTPS VDFILQDPAV PIKDRDEIVK ALKENSFTDE
LINMPIGSLS GGWKMKLALT RAMFKNPDIL LLDEPTNHLD VVNVAWLENF LVNQKDVSSI
IVSHDSGFLD HVVQAIIHYE RFKLRKYLGN MSEFVKKVPS AKSYYELGAS EMEFKFPEPG
FLEGVKTKQR AIIKVQHMSF QYPGTSKPQL NDISFQVSLS SRIAVIGPNG AGKSTLIKVL
TGELLPTVGE IYQHENCRIA YVAQAAFTHL GHHPDKTPSE YIQWRFQSGE DLEAMDKASR
VISEADEEAM KNKIFKIEGT QRKILGIHSR RKLKNSYEYE CSFLVGENIG MKSERWVPMM
SSDNAWLPRG ELMETHAKMV AEVDRAEALK SGQFRPLVRK EIEEHCSLLG LDAELVSHSR
IKGLSGGQKV KLVLAACTWL RPHVIVLDEP TNYLDRDSLG ALSKGLKNFG GGVVLVTHSR
EFTEGLTEEV WAVNNGHMTP SGHNWVSGQG SGPRIQEKEE GDTFDAFGNK IEKAKKAKKL
TGAELRKKKK ERMARRKAGL EVSDDEL
