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Database: UniProt
Entry: N1QNU4_SPHMS
LinkDB: N1QNU4_SPHMS
Original site: N1QNU4_SPHMS 
ID   N1QNU4_SPHMS            Unreviewed;       577 AA.
AC   N1QNU4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=GTP_EFTU-domain-containing protein {ECO:0000313|EMBL:EMF17624.1};
GN   ORFNames=SEPMUDRAFT_146596 {ECO:0000313|EMBL:EMF17624.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF17624.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF17624.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF17624.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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};
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DR   EMBL; KB456260; EMF17624.1; -; Genomic_DNA.
DR   RefSeq; XP_016765745.1; XM_016903756.1.
DR   AlphaFoldDB; N1QNU4; -.
DR   STRING; 692275.N1QNU4; -.
DR   GeneID; 27900893; -.
DR   eggNOG; KOG0458; Eukaryota.
DR   HOGENOM; CLU_007265_3_2_1; -.
DR   OMA; FRMAISE; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000016931; 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:0006417; P:regulation of translation; 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; 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: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; 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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          158..382
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..26
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  62191 MW;  C3C7D6F392AD09D2 CRC64;
     MQRVKNIDYD DDDVYSDEEE YAEEGPGEYS AEDKENFAAL TPVVRAELDE AGIPATTKQI
     EDALWHYYWD VGKSVAYLKN SKAPQQPKQQ VAKKEKPKSK FDEAAEQSAV IADKVKQTQP
     PANGLAKKAE ALKLDPTPKL KSKGLDVPKL WQEEKSKRKS AAFVVIGHVD HGKSTLMGRL
     LLDTGAVAQR DVDKYKKQAT EMGKASFALA WVMDTGSEER QRGVTVDIAQ HHFKSGDVDF
     TILDAPGHRD FVPNMIGGAS MADMGVLVVD ANQLESGMKG QTREHILLAH AVGLQKIVVA
     VNKLDSTSQP WDQSIFKAVS AEVRKVLMET GFSKDNISVV PCSGLSGENV VKAPSESSEA
     GWVKKNHPTL IQQLEQSVAE STSVEVVLKP LRLQIADVFR GGIQNPVSIS GLVRSGNVQV
     GESIIIQPSG EKATVKGIEL AGVSKEWAAA GDIAALHLAD IEPQHLRSGD IVCGSSKPVS
     VAKNIIAKVQ AIDALLPQGV DVHVGRLHVP GQINQLFSII NAKDEVLKKK PRIVKAGQRA
     VVRIALDDGA PLEVGDRVVV RAEGSTVAAG VVENVGR
//
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