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Database: UniProt
Entry: A0A0A2V2X4_PARBA
LinkDB: A0A0A2V2X4_PARBA
Original site: A0A0A2V2X4_PARBA 
ID   A0A0A2V2X4_PARBA        Unreviewed;       574 AA.
AC   A0A0A2V2X4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
GN   ORFNames=PAAG_11418 {ECO:0000313|EMBL:KGQ01843.1};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:KGQ01843.1, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:KGQ01843.1, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293995; KGQ01843.1; -; Genomic_DNA.
DR   RefSeq; XP_015703333.1; XM_015847071.1.
DR   AlphaFoldDB; A0A0A2V2X4; -.
DR   STRING; 502779.A0A0A2V2X4; -.
DR   GeneID; 9099279; -.
DR   KEGG; pbl:PAAG_11418; -.
DR   VEuPathDB; FungiDB:PAAG_11418; -.
DR   eggNOG; KOG0052; Eukaryota.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   OMA; RDMGQTV; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
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   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd03693; EF1_alpha_II; 1.
DR   CDD; cd03705; EF1_alpha_III; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   NCBIfam; TIGR00483; EF-1_alpha; 1.
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   Pfam; PF01096; TFIIS_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:KGQ01843.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:KGQ01843.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00472}.
FT   DOMAIN          84..158
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   DOMAIN          120..355
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   574 AA;  63406 MW;  668C04986CADAF08 CRC64;
     MTRNDLPDRD RLYISVCPNC SNALTISRAE PTSRYPLGVN RFECRTCPYQ YILDRTYYER
     TEMKRKEVAD VLGGKDEWKN ADSIGTQCPA EGCDGDRAFF YQLQIRSADE PMTTFLKEEK
     THINLVVIGH VDSGKSTTTG HLIYKCGGID SRTIEKFEKE AEELGKKSFK YAWVLDKLKA
     ERERGITIDI ALWKFETPKY NVTVIDAPGH RDFIKNMITG TSQADCAILI IAAGTGEFEA
     GISKDGQTRE HALLAFTLGV KQLIVAINKM DTTKWSETRF NEIIKEVTNF IKKVGYNPKT
     VPFVPISGFE GDNMIEPSAN CPWYKGWSKE TAQGKYSGKT LLEAIDAIEP PTRPTDKPLR
     LPLQDVYKIS GIGTVPVGRV ETGVIKPGMV VTFAPANVTT EVKSVEMHHQ QLTAGNPGDN
     VGFNVKNVSV KEVRRGNVAG DSKNDPPKGC DSFNAQVIVL NHPGQVGAGY APVLDCHTAH
     IACKFAELLE KIDRRTGKSV ENNPKFIKSG DAAIVKMIPS KPMCVEAFTE YPPLGRFAVR
     DMRRTVAVGV IKSVVKSDKA GGKVTKAAQK ATKK
//
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