ID Q2NLH5_9HYPO Unreviewed; 307 AA.
AC Q2NLH5; B2CBJ1;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=EF1-alpha {ECO:0000313|EMBL:AAY43936.1};
GN Synonyms=TEF1alpha {ECO:0000313|EMBL:ACB06594.1};
OS Moelleriella libera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=324773 {ECO:0000313|EMBL:AAY43936.1};
RN [1] {ECO:0000313|EMBL:AAY43936.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P.C. 445 {ECO:0000313|EMBL:AAY43936.1};
RX PubMed=16279420;
RA Chaverri P., Bischoff J.F., Liu M., Hodge K.T.;
RT "A new species of Hypocrella, H. macrostroma, and its phylogenetic
RT relationships to other species with large stromata.";
RL Mycol. Res. 109:1268-1275(2005).
RN [2] {ECO:0000313|EMBL:ACB06594.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P.C. 444 {ECO:0000313|EMBL:ACB06594.1};
RX PubMed=18490956;
RA Chaverri P., Liu M., Hodge K.T., Hodge;
RT "A monograph of the entomopathogenic genera Hypocrella, Moelleriella, and
RT Samuelsia gen. nov. (Ascomycota, Hypocreales, Clavicipitaceae), and their
RT aschersonia-like anamorphs in the Neotropics.";
RL Stud. Mycol. 60:1-66(2008).
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}.
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DR EMBL; AY986925; AAY43936.1; -; Genomic_DNA.
DR EMBL; EU392662; ACB06594.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NLH5; -.
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:AAY43936.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:AAY43936.1}.
FT DOMAIN 1..131
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY43936.1"
FT NON_TER 307
FT /evidence="ECO:0000313|EMBL:AAY43936.1"
SQ SEQUENCE 307 AA; 33162 MW; C20B655FFAE739AD CRC64;
DCAILIIAAG TGEFEAGISK DGQTREHALL AYTLGVKQLI VAINKMDTAK WAEARYQEII
KETSNFIKKV GYNPKTVAFV PISGFNGDNM LQASTNCPWY KGWEKETKAG KTTGKTLLEA
IDSIEPPKRP TDKPLRLPLQ DVYKIGGIGT VPVGRIETGV LKPGMVVTFA PSNVTTEVKS
VEMHHEQLAE GVPGDNVGFN VKNVSVKDIR RGNVAGDTKN DPPQGAASFD AQVIVLNHPG
QVGAGYAPVL DCHTAHIACK FAEIREKIDR RTGKAVEEAP KFIKSGDSAI VKMVPSKPMC
VEAFTDY
//