ID E6ZNG8_SPORE Unreviewed; 972 AA.
AC E6ZNG8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Related to translation elongation factor HBS1 {ECO:0000313|EMBL:CBQ68819.1};
GN ORFNames=sr15101 {ECO:0000313|EMBL:CBQ68819.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ68819.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ68819.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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 -!- 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}.
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DR EMBL; FQ311433; CBQ68819.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZNG8; -.
DR EnsemblFungi; CBQ68819; CBQ68819; sr15101.
DR VEuPathDB; FungiDB:sr15101; -.
DR eggNOG; KOG0458; Eukaryota.
DR HOGENOM; CLU_007265_3_2_1; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000008867; Chromosome 12.
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 CDD; cd04093; HBS1_C_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; IPR031157; G_TR_CS.
DR InterPro; IPR015033; HBS1-like_N.
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 InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 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:0000313|EMBL:CBQ68819.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:CBQ68819.1};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 533..757
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 86..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 101040 MW; 55CA2D02B8F52F2C CRC64;
MSRHRAVRNL DLDEELAEDD YYDDDPYDNL SPEDHDAMTE AYAQTLDVLG PISSNGFTER
EIKDILWDAY FDVDSAVTQL VEEKSRREAK AEKDRQKQES GEMQLDVDDE QPTIEAFKHL
SLQRDRRAEI RAGRGMPRGK AQGLRGLATG GRAGMARRNL AGLAPDFVRQ PQAVAGSSSS
SASSGSSKPV SKLSALAARS SAKRPAETAP VEAASRPRPA SPARSASPAS SSSPAVPASN
APAARTSKLA ALAAARSGAS ASASRPAAPA CSPTAEAADA PPAKSLSKLQ QRMLANKQQR
QAATPEAKEA AAAQAADEEA RARPQTCYGS DLPIACLFPT ADAAAEAKLG PAATASSGTA
LASISAIAGS SKHATDQLVA PLSQLRRVPG GSPFALYVQG SDEGSGVAVE SVRKAFAGPS
PDDVVMRARE GTRLAAKKAA AAANASVPTS GTSTPLARKA AVGQAAKAAA SKPGGTTVSQ
LRNEIASLDI HAGSSSRAAS SAGSAAPSAV STPMGIAHER IIDEYRKRER EGKAELSLVV
VGHVDAGKST LMGRMLLELG SLSQREYSSN ERASQKIGKG SFAYAWALDS SEEERERGVT
IDIAQDHFST LHRTFTLLDA PGHRDFIPNM ISGAAQADSA LLVVDSIQGA FEAGFGPNGQ
TREHALLVRS LGVQQLVVVV NKLDAVGYSQ ARYDEIVGKV KPFLTSCGFD AAKLKFVPCG
GSVGENLAVR EEGGALSEWY SGPTLVEVLD ALEPPARQLD APLRLPVTNV FKGQTAIASG
VAVSGRVVSG IVQIGDRLRP VPGDESGIVR AIEVDTESVP WAVAGANATV YLSGIDQIQL
SVGAVLCTPS APIALCDTFV AQILVFEPTY PLVAGTSIEL FHHSANIAAA LTELVSILDK
TSGGVIKKKP RVLTKGCTAL VRVTVKAGGM AGQSSGIPLE DARANKEMAR VLMRMNGETV
AAGIVVEAHA AG
//
