ID A0A2B7Z2W4_9EURO Unreviewed; 871 AA.
AC A0A2B7Z2W4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Translation elongation factor Tu {ECO:0000313|EMBL:PGH27701.1};
GN ORFNames=AJ80_00488 {ECO:0000313|EMBL:PGH27701.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH27701.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH27701.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH27701.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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 -!- 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:PGH27701.1}.
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DR EMBL; PDNA01000004; PGH27701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7Z2W4; -.
DR STRING; 1447883.A0A2B7Z2W4; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000224634; 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 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; 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 Elongation factor {ECO:0000313|EMBL:PGH27701.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:PGH27701.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000224634};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 459..686
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 93697 MW; 03063204AE3E5533 CRC64;
MSRHRVKAIS YDSDGLDDDD YDNEAGGDGG DNNTELSPED REQMRLATIE VRQLLASEMP
PVSAEEQEIW ESLWHYYYDV GKAVGYLRKK YKPDTTEKSA KKQQQQGKVK GKGMMASSYP
LPPPPPAVAL STTSCSAAAS FSAVDFFKDS PWLNIPAHRR AEILVEPLYP RLGLLGGAPE
GGGKMSKLAA LAAARKKRES EKKMANGSPS SAESPSQTPE EEPRSTSISL LDRLGSGGRS
SSQLPSENRM AAKLPLRKFD RGLNRAPPPP PPRDTTPKSA AAPAATAATL PERPLPKRVS
PDHGKESTEL APPQEKSVGS AVTVSVTATR AEPSTFATTI VGRGRNNSTN LEEPSDNLQE
SIDVMSNLLG GRNLLLTEVF NFAGPSPDDV VLNAQSAAKG NKAKRSTTAA TTAAAKAALK
KKSPTDLADE VNGLSVQESV KVKSKNLDVL AEYRKAQRKK AANFVVIGHV DAGKSTLMGR
LLFDLKAIDQ RTMDKYRREA DKIGKGSFAL AWVLDQGSEE RARGVTIDIA TNKFETEHTN
FTILDAPGHR DFVPNMIAGA SQADFAVLVV DASTGKFESG LKGQTKEHAL LVRSMGVAKI
VVVVNKMDSV GWTKDRFDEI QQQISAFLTT AGFQPKNISF VPCSGLRGDN VTQRADDKAA
SWYTGRTLIE ELETSEPYTY ALDKPLRMTI ADVFRAGVQN PLSISGRLDA GTLQVGDTIT
TMPISEKATI KAIEIDNGEP SDWAVAGQNV TLHLTDIDPT HLRTGDIICT PTTPIRNITS
FTAKVLAFDH LTPMHIDVHR GRLHVPGRIA KLVAVLDKAT GAAVGKKKLK IVAPGSVARI
VVEMDMPIPL EAPGRVVLRA GGETVAAGLL E
//
