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Database: UniProt
Entry: A0A0D2DHC6_9EURO
LinkDB: A0A0D2DHC6_9EURO
Original site: A0A0D2DHC6_9EURO 
ID   A0A0D2DHC6_9EURO        Unreviewed;       513 AA.
AC   A0A0D2DHC6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=protein-synthesizing GTPase {ECO:0000256|ARBA:ARBA00011986};
DE            EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
GN   ORFNames=PV05_01787 {ECO:0000313|EMBL:KIW61697.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW61697.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW61697.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW61697.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001874};
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DR   EMBL; KN847317; KIW61697.1; -; Genomic_DNA.
DR   RefSeq; XP_013322281.1; XM_013466827.1.
DR   AlphaFoldDB; A0A0D2DHC6; -.
DR   STRING; 348802.A0A0D2DHC6; -.
DR   GeneID; 25323695; -.
DR   HOGENOM; CLU_027154_0_1_1; -.
DR   OrthoDB; 1512042at2759; -.
DR   Proteomes; UP000054342; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   CDD; cd01888; eIF2_gamma; 1.
DR   CDD; cd03688; eIF2_gamma_II; 1.
DR   CDD; cd15490; eIF2_gamma_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; IPR015256; eIF2g_C.
DR   InterPro; IPR044127; eIF2g_dom_2.
DR   InterPro; IPR044128; eIF2g_GTP-bd.
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   PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
DR   Pfam; PF09173; eIF2_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
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   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:KIW61697.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT   DOMAIN          83..291
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  55504 MW;  039E0B4CB66CA6F5 CRC64;
     MATNGDLPSD DEFSQPGTPP GDENDVEEIE ETNQPPKSAL KKGTSAPIPE PQVARPPLPE
     QPDPKDLDIS KLTPLSPEII ARQATINIGT IGHVAHGKST VVKAISGVQT VRFKNELERN
     ITIKLGYANA KIYKCDNPEC PRPTCYKSYK SEKEVDPPCE REGCGGTYRL LRHVSFVDCP
     GHDILMSTML SGAAVMDAAL LLIAGNETCP QPQTSEHLAA IEIMKLSHII ILQNKVDLMR
     EEGAQQHFES ILKFIKGTVA DGSPIIPISA QLKYNIDAIN EYLVTKIPVP IRNFQAAPHM
     IVIRSFDVNK PGAEIEDLKG GVAGGSILTG VLKLGDEIEI RPGIITKDAM GQTVCRPIMS
     RVVSLFAEHN DLKFAVPGGL IGVGTRVDPT LCRADRLVGH VLGLRGNLPE IYMELEVNYF
     LLRRLLGVKT ADGKQAKVAK LAKNEVLMVN IGSTATGAKV MGVKADAAKL TLTNPACTAI
     GEKIALSRRI EKHWRLIGWA NIVAGNTIEP ETS
//
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