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Database: UniProt
Entry: A0A094HK02_9PEZI
LinkDB: A0A094HK02_9PEZI
Original site: A0A094HK02_9PEZI 
ID   A0A094HK02_9PEZI        Unreviewed;       520 AA.
AC   A0A094HK02;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=protein-synthesizing GTPase {ECO:0000256|ARBA:ARBA00011986};
DE            EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
GN   ORFNames=V502_05712 {ECO:0000313|EMBL:KFZ15227.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ15227.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ15227.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFZ15227.1}.
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DR   EMBL; JPKE01002175; KFZ15227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HK02; -.
DR   STRING; 1420915.A0A094HK02; -.
DR   HOGENOM; CLU_027154_0_1_1; -.
DR   OrthoDB; 1512042at2759; -.
DR   Proteomes; UP000029308; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029308}.
FT   DOMAIN          89..298
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  56332 MW;  A8EBCD9306B27A3B CRC64;
     MATQGDKFGN DMESDSGSEQ GSPNLGATND VEDNDNIPDM PLKSNLKRPT AAKENAPVVV
     RPILPPQTEP KDLDVKSLTP LTPEIIARQA TINIGTIGHV AHGKSTVVKA ISGVQTVRFK
     NELERNITIK LGYANAKIYK CDFEECPRPG CFRSYKSEKE VDPPCEREGC PGTYRLLRHV
     SFVDCPGHDI LMSTMLSGAA VMDAALLLIA GNETCPQPQT SEHLAAIEIM KLDKIIILQN
     KVDLMREDGA LQHYQSILKF IRGTVADRSP IIPISAQLKF NIDAINEAIV STIPVPPRDF
     SQDPQMIIIR SFDVNKPGAE IDELKGGVAG GSILHGVIKL GDEIEIRPGI VTRDDKGAIQ
     CTPIFSRIVT LNSENNELKY AVPGGLIGVG TRIDPTLCRA DRLVGFVLGL KGRLPDIYTE
     IEVNYYLLRR LLGVKTADGK QAKVAKLAKN EVLMVNIGST ATGAKVVAVR QDAAKLVLTS
     PACTNTGEKV ALSRRIEKHW RLIGWATIAA GVTLEPSASS
//
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