ID D0FLD0_9HYPO Unreviewed; 309 AA.
AC D0FLD0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=tef1 {ECO:0000313|EMBL:ABG77500.1};
OS Melanopsamma pomiformis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Melanopsamma.
OX NCBI_TaxID=80381 {ECO:0000313|EMBL:ABG77500.1};
RN [1] {ECO:0000313|EMBL:ABG77500.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UAMH 10484 {ECO:0000313|EMBL:ABG77500.1}, and UAMH 7750
RC {ECO:0000313|EMBL:ABG77511.1};
RA Koster B.M., Wong B., Straus N.A., Malloch D.W.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABG77500.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UAMH 10484 {ECO:0000313|EMBL:ABG77500.1}, and UAMH 7750
RC {ECO:0000313|EMBL:ABG77511.1};
RX PubMed=19422915; DOI=10.1016/j.mycres.2009.04.003;
RA Koster B., Wong B., Straus N., Malloch D.;
RT "A multi-gene phylogeny for Stachybotrys evidences lack of trichodiene
RT synthase (tri5) gene for isolates of one of three intrageneric lineages.";
RL Mycol. Res. 113:877-886(2009).
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 ---------------------------------------------------------------------------
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; DQ676611; ABG77500.1; -; Genomic_DNA.
DR EMBL; DQ676622; ABG77511.1; -; Genomic_DNA.
DR AlphaFoldDB; D0FLD0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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 InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:ABG77500.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:ABG77500.1}.
FT DOMAIN 1..131
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABG77500.1"
FT NON_TER 309
FT /evidence="ECO:0000313|EMBL:ABG77500.1"
SQ SEQUENCE 309 AA; 33304 MW; BE7CC6E228B8A757 CRC64;
DCAILIIAAG TGEFEAGISK DGQTREHALL AYTLGVKQLI VAINKMDTTN WSEARFQEII
KETSNFIKKV GYNPKTVAFV PISGFNGDNM LAASTNCPWY KGWEKETKAG KSSGKTLLEA
IDSIEPPKRP TDKPLRLPLQ DVYKIGGIGT VPVGRIETGI IKPGMVVTFA PSNVTTEVKS
VEMHHEQLTE GKPGDNVGFN VKNVSVKEIR RGNVAGDSKN DPPLGAASFQ AQVIVLNHPG
QVGAGYAPVL DCHTAHIACK FAEIQEKIDR RTGKSVESAP KFIKSGDSAI VKMVPSKPMC
VEAFTDYPP
//
