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Database: UniProt
Entry: A0A0C9U317_PAXIN
LinkDB: A0A0C9U317_PAXIN
Original site: A0A0C9U317_PAXIN 
ID   A0A0C9U317_PAXIN        Unreviewed;       475 AA.
AC   A0A0C9U317;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=protein-synthesizing GTPase {ECO:0000256|ARBA:ARBA00011986};
DE            EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
GN   ORFNames=PAXINDRAFT_80444 {ECO:0000313|EMBL:KIJ13676.1};
OS   Paxillus involutus ATCC 200175.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ13676.1, ECO:0000313|Proteomes:UP000053647};
RN   [1] {ECO:0000313|EMBL:KIJ13676.1, ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ13676.1,
RC   ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
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; KN819349; KIJ13676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9U317; -.
DR   HOGENOM; CLU_027154_0_1_1; -.
DR   OrthoDB; 1512042at2759; -.
DR   Proteomes; UP000053647; 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:UP000053647}.
FT   DOMAIN          47..255
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  51784 MW;  12B54265D9F57CA8 CRC64;
     MSDEETLQKH HEDSESEDSD DEVDDVPKID IDPSTLTPLS PEVISKQATI NLGTIGHVAH
     GKSTVVKAIS GVMTVRFKNE LVRNITIKLG YANAKIYKCE NEACPRPGCY RSYRSDKEDN
     PPCERPGCGH RMKLVRHVSF VDCPGHDILM ATMLNGAAVM DAALLLIAGN ETCPQPQTSE
     HLAAVEIMKL ENIIILQNKV DLIKEAQALE HQKSIAAFVK GTVAESSPIV PISAQLKYNI
     DAVNEYIVKR IPIPIRDFTS DPRLIVIRSF DVNKPGAEVD DLKGGVAGGS ILTGVLRIGQ
     EVEIRPGIVT KDSAGRNRCK PIFSKIVSLH AESNHLSFAV PGGLIGVGTK IDPTLCRADR
     LVGQVLGEVG KLPKVYTELE ISLFLLRRLL GVRTEDKKQT KVSKLTKNEL LLINIGSTST
     GGRVLSVKGD LAKIQLTSPA CTEVGEKVAL SRRIEKHWRL VGWGSVQRGT VLELD
//
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