EF3_PNECA
ID EF3_PNECA Reviewed; 1042 AA.
AC P29551;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Elongation factor 3;
DE Short=EF-3;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P16521};
GN Name=TEF3;
OS Pneumocystis carinii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX NCBI_TaxID=4754;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1339410; DOI=10.1128/iai.60.10.4140-4145.1992;
RA Ypma-Wong M., Fonzi W.A., Sypherd P.S.;
RT "Fungus-specific translation elongation factor 3 gene present in
RT Pneumocystis carinii.";
RL Infect. Immun. 60:4140-4145(1992).
CC -!- FUNCTION: Ribosome-dependent ATPase that functions in cytoplasmic
CC translation elongation (By similarity). Required for the ATP-dependent
CC release of deacylated tRNA from the ribosomal E-site during protein
CC biosynthesis (By similarity). Stimulates the eEF1A-dependent binding of
CC aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for
CC tRNA as long as the E-site is occupied (By similarity).
CC {ECO:0000250|UniProtKB:P16521}.
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:0000250|UniProtKB:P16521}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; M87665; AAA33789.1; -; Genomic_DNA.
DR PIR; A49204; A49204.
DR AlphaFoldDB; P29551; -.
DR SMR; P29551; -.
DR PRIDE; P29551; -.
DR UniPathway; UPA00345; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; IPR021133; HEAT_type_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF5; PTHR19211:SF5; 1.
DR Pfam; PF17947; 4HB; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Elongation factor; Hydrolase; Nucleotide-binding;
KW Protein biosynthesis; Repeat; RNA-binding.
FT CHAIN 1..1042
FT /note="Elongation factor 3"
FT /id="PRO_0000093456"
FT REPEAT 9..46
FT /note="HEAT 1"
FT REPEAT 86..124
FT /note="HEAT 2"
FT REPEAT 167..204
FT /note="HEAT 3"
FT REPEAT 206..242
FT /note="HEAT 4"
FT REPEAT 243..280
FT /note="HEAT 5"
FT REPEAT 289..327
FT /note="HEAT 6"
FT DOMAIN 425..642
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 668..994
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1009..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 462..469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 702..709
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1042 AA; 117507 MW; 053BC4D60F5D2C2F CRC64;
MPGNVVSPKV LMDLIPKLKI SMQETDKNEV IKNSEQHSSV SWDPDTCENL YITLEEQIES
KDTLAREQAL KALLLTLDAT NKRVEPYLVR LLPRVLKQVG LEKVAAVRTQ ASTVAEDIIK
TMNPYAVKTI LSHVTNSIKT SGKWMEKMCA FRLLDMLVEK APCQMSYRLP ELIPILSESM
WDTRTDIKNQ ARKTMTSVCT LISNPDIDKF IPVLIDCIAQ PEKVPETIHT LGATTFVQEV
HASTLSIMVP LLYRGLNERE TTIKRKSAVI IDNMCKLVED PYIIAPFLPK LIPTLEHIKE
TIGDPECRSV VNRSLATLIR VGNVKEGKIP EVLNIAKPEN CMETLLSILK GQELVPVSDV
YLNYISCIAS QLIDEKNNEV VDWDVNISPY LQPIILKADI NCIIDQFRKR SISGFHSSSA
ESEEEEGEDL CNCEFSLAYG AKILLNRTSL NLKRGYRYGL CGPNGSGKST LLRSIFNGQL
EGFPTELKTA YVEHDIDDTE SKTSVFDFIA NDPSVVVKNK QEVISSLLEH SFTEDMLSIP
ISNLSGGWKM KLALVRAMLR QVDILLLDEP TNHLDVKNVA WLENFLTSQT HITSIIVSHD
SKFLDNVVQA IIHYEHFKLK KYMGNMSKFI TLVPSARSYQ DISMSEIEFS FPEPGYLEGV
KTKQRAICRM RDIEFQYEGT SEPQIKNVSL QVSLSSRIAV IGPNGAGKST LIKVLCGELI
PQKGEVWCHP NLRIAYVAQA AFVHLGSHEN KTPSEYIQWR YRTAEDSETI DRASRQLTEN
DEHLMNKIFK INGTSRKIQG IHSRRKLKNS YEYECSFLVG ENVGEKNERW VPLPSMNNEW
LPRGELIESH SKMVAEVDMK EALKSGSFRP LVRKEIEKHC ESFGLDAEIV THSRIKGLSG
GQKVKLVLAA GSWLKPHVIV LDEPTNYLDR DSLGALSKAL KSFEGGVVII THSVEFTKNL
TEEVWSVQNG QMTPSGHNWV QGQGTGPRLQ EQEEEDTFDA LGNKIEAKKK AKKLTSSELR
KKKKERMARR KKGEEVFSDE DD
