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Database: UniProt
Entry: A0A139IMN1_9PEZI
LinkDB: A0A139IMN1_9PEZI
Original site: A0A139IMN1_9PEZI 
ID   A0A139IMN1_9PEZI        Unreviewed;       591 AA.
AC   A0A139IMN1;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=AC579_6261 {ECO:0000313|EMBL:KXT15822.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT15822.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT15822.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT15822.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KXT15822.1}.
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DR   EMBL; LFZO01000050; KXT15822.1; -; Genomic_DNA.
DR   EMBL; LFZO01000050; KXT15825.1; -; Genomic_DNA.
DR   EMBL; LFZO01000050; KXT15826.1; -; Genomic_DNA.
DR   EMBL; LFZO01000050; KXT15827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IMN1; -.
DR   Proteomes; UP000073492; Unassembled 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   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; 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:SF188; HBS1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 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   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          172..396
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          82..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  63740 MW;  9E90D734EAEFD996 CRC64;
     MQRVKNVNYD EDDLYSDEEG YEDGQDAQGY TAEDKDNFAN LTPVVRAELE EAGIPVPSTQ
     IEEALWHYYW DVGKSVAYLK NSRTPRQADP QQQQQQQEQE QEAKKNKPKS KFDEAQQKSA
     DIAEKAKATK STNGLAKKTA ALKLDAIAPA HPKLKSKGLD VPSIWAKERS KRASAAFVVI
     GHVDHGKSTL MGRLLLDTGA VAQRDIDKYK KQATEMGKAS FALAWVMDTG SEERARGVTV
     DIAQHHFSTD SVDFTILDAP GHRDFVPNMI GGASMADLAV LVVDANQLES GMKGQTREHI
     LLAHAVGLRR IVVAVNKLDA STPAWSEEAF RNVREEVLKL LATTGFSRDN VAVIPCSGLS
     GENVISAPPE KSEAAWARAK HPTLLQQLEK SASSSVSAEL VKAPARMQVA DVFRGGITSP
     ISISGLLRSG SLQTGETIIV QPSGESALVK GIEVQGASKE WTVAGQIPTL HLQDIDAQHL
     RSGDVACGGD KPVKVVKNVI AQVTAFESLL PQDADVHIGR LHAPGHISQL FSTLNAKDEA
     IKKKPRIVKA GQRAVIRLGL DNGVPLEAGD RIVLRSEGNT IAAGTVQQVG S
//
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