ID A0A0G2E2S2_9EURO Unreviewed; 786 AA.
AC A0A0G2E2S2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative elongation factor tu gtp binding domain protein {ECO:0000313|EMBL:KKY16661.1};
GN ORFNames=UCRPC4_g05844 {ECO:0000313|EMBL:KKY16661.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY16661.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY16661.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY16661.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY16661.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY16661.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-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;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
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}.
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:KKY16661.1}.
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DR EMBL; LCWF01000158; KKY16661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2E2S2; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; cd01883; EF1_alpha; 1.
DR CDD; cd16267; HBS1-like_II; 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; IPR031157; G_TR_CS.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
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; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR23115:SF309; ELONGATION FACTOR EF-1 SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04630)-RELATED; 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; PF08938; HBS1_N; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW ECO:0000313|EMBL:KKY16661.1}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 376..603
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 86025 MW; 29B815D6030848C5 CRC64;
MAVDDDELFD DEDYDNDFGS EAGDGDGDGD GLTEHDREQL RMGTIEVRKQ LGPEFDVTDN
DIQESLWHYY YDIAKTVTYL KNKRTQSQKK TSQKGAAMTH ATAPVCGLTK SPSFSTEDFF
QDCPWLNVPI DRLAVFEPVR VPIRGGLLGG SSSEPKMSKL AALAAKRRQK ENEKLAKTDV
TEDSSNKSSY IASLEKLRLG SNTQKTVKPD PTQLLKENSS KLNHEKRTKP RAPSKHSPTP
EPDIPTVQTE LTTPTDLPPV IVSRAEPSAF ARVLTGTTNF WPHLRQLPDS LLNRPFLSHK
SPHTDTKPFD FTDPSPDDIV INAQKSKATK SAKSKTPAQQ QDNLAQGVKQ LSVSSQPVSK
SKGIDVVSEY KKKTSKPAAN FVVIGHVDAG KSTLMGRLLY DLKAIDSRTM EKYKKEAEKI
GKGSFAFAWV LDQGSEERER GVTIDVATNK FETDKTSFTI LDAPGHQDFV PNMIAGASQA
DFAVLVIDAS TGRFESGLKG QTKEHALLAR SLGVQRIIVA VNKMDAAHWS QDRFTDIQQQ
IAAFLISAGF KQQNLAFVPC SGLQGDNILQ KSGDKNAAWY QGGTLVQELD QSEPTTHAID
KPLRMPIADV FRGGIQNPLS ISGRIESGSV QNGEVIKIMP SGELAGIKGI EVDNEPAEWA
VAGQNVNLHL VDIDPIHLRS GDVVCSQKSP ITNIDTFSAK ILAFQHLMPM HLDIHRGRLH
VAGRISQLVA TLDKSTGAVI KKKPKVIQPG SLVQVQVELT RSVPLEAPAR IVMRSEGHTI
AAGIMQ
//
