ID A0A0B4HW59_METMF Unreviewed; 837 AA.
AC A0A0B4HW59;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Elongation factor Tu GTP binding domain protein {ECO:0000313|EMBL:KIE03661.1};
DE Flags: Fragment;
GN ORFNames=MAJ_00192 {ECO:0000313|EMBL:KIE03661.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KIE03661.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KIE03661.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KIE03661.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KIE03661.1}.
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DR EMBL; AZNE01000001; KIE03661.1; -; Genomic_DNA.
DR RefSeq; XP_014582654.1; XM_014727168.1.
DR AlphaFoldDB; A0A0B4HW59; -.
DR HOGENOM; CLU_007265_3_2_1; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000031176; 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; 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:KIE03661.1}; 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:UP000031176};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 426..648
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIE03661.1"
SQ SEQUENCE 837 AA; 90327 MW; 152080CC637A2432 CRC64;
MAPANFYDDD DLYDGNDYEE DQEEELSPED KQAMEEGTAH VKKALGANAS KVTVKQIQEA
LWHYYYDVEK SAAYLTKTFI APPPPKPTPK KAPESKLHEF SFSSSLGLFV RSAGAASALP
LSNSPQTPET LPLPPCRTFS YRTNSIILQS EFDDMPWLNT PESRQATLIA PSEPRGGLLG
GAGDAPKMSK LQALAAARKK KNDEKKEQAK ASETESGMKR LSITDDSQKG NTKGASSPAK
RLRGPDMQAS SRPILGRGDS RSESSQNTQS SAAPVEVIAP QKESGKPNQY PPVQREEQDE
DAELAPACAP SAFAKTLFGP APEDRQANRP DFFAMPYAAS SSFLATAFSN PSPDDIVLAA
QAKAGKKTAA PVKAASIVVK KDKNVDAVSK VVDVANGVSN LRVSDAPPPK SKGLDVAKEY
EKSNRKKSIS FVVVGHVDAG KSTLMGRLLL ELKYVQERTV DKYRRQAEKT GKQSFALAWV
MDQRTEERER GVTIDIATNH FETPNTKFTI LDAPGHRDFV PNMIAGASQA DFAVLVVDAN
TGAYEKGLKG QTREHVLLLR SLGVQRLIVA VNKLDMVGWS KDRFDEISQQ VMGFLTGLGF
QSKLVSFIPI SGLNGDNIAS EMKDATAAWY QGPTLLASLE DSEPSSARAI TKPFRMSISE
VFRSQQQGTT TLAGRIEAGN IQIGDAVIVQ PSGEGTYIKS IMVDTEAQEW AVAGQSVTIA
LTDIDPVHIR VGDILCGTVN PISVGDTFTL KAMAFEHLMP MPVDLHRGRL HAAGQIQSIP
ATLDKATGEV IKKKPKVVQP GSVARVTIKL GSKVPLEKGQ RVVLRSGGET IAAGLLE
//
