ID A0A319F652_ASPSB Unreviewed; 1060 AA.
AC A0A319F652;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:PYI00663.1};
GN ORFNames=BO78DRAFT_424273 {ECO:0000313|EMBL:PYI00663.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI00663.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI00663.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI00663.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ826441; PYI00663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319F652; -.
DR STRING; 1448318.A0A319F652; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000313|EMBL:PYI00663.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 5..278
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 195..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..470
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 195..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1060 AA; 117341 MW; 028A6EB6AAF031CE CRC64;
MPVVNVDDLI CILAHVDHGK TSLTDSLIAT NGIISPKLAG KIRYLDSRPD EQLRGITMES
SAISLFFSMM RRPAPDAAPV PKEYLINLID SPGHIDFSSE VSTASRLCDG AVVLVDAVEG
VCSQTVTVLR QTWVEQLKPI LVINKIDRLV TELKMSPSEA YSHMSKLLEQ VNAVIGSFYQ
GERMEEDLQW RERMEERANA SAARDKDRSN DEPTAEYEER DDEDLYFAPE KNNVIFCSAV
DGWAFTIRQF AVIYEKKLGI KRTILEKVLW GDYYLDPKTK RVLGQKHLKG RALKPMFVQL
VLDSIWAAYE ATIGAGTGKG DPALLEKITK SLNINIPAYI LRSRDPKNIM TTLFSMWLPL
STAVLVSVIE YLPSPPAAQA TRLPALIEES PGAQFVDQKV KDAMVNFKTQ KDEPVIAYVS
KMMAIPESEL MSSKKRAGAA MSADEAREIA RKKREEIAKM QAEANGDQAD DFSRITSAFE
RTSLSDKQTA DDEEKEDPEH LVGFARLYSG TLSVGDSVYV LAPKFSPENP HASPEPRKVT
VTDLYLLMGR SLEPLQSVPA GVVFGIGGLA GHVLKTGTLS SQIEGSINLA GVSLNTPPIV
RVALEPTNPA DLSKMVTGLR LLEQSDPCAQ YEVLPSGEHV ILTAGELHLE RCIKDLRERF
AKCEIQTGQT IVPYRETIIS APEMASPKNS ELGRGGILAV SPSKQLTMRL RVVPLPSAVT
EFFSKHVGTI KRLQTEKRTA AEAQSSEEAT NGTTESDVSD ATDEARESTS LSLKDFKEEL
TKIFDEEVTD DKGLWKDVVD RITAFGPRRI GPNILVDATE VNTCEKFLLD DPKQQPTVNA
DTSSREALFV RDFCDKIAHA FQLATGQGPL CQEPMQGVAV FLEDLSVNAN DEDLDLGRLT
GESIRLVRDS ISQGFLDWSP RIMLAMYSCE IQASTEVLGR VYGVITRRRG RILSEIMKEG
TPFFTILALL PVAESFGFAE EIRKRTSGAA QPQLIFAGFE ALDEDPFWVP ATEEELEDLG
ELADRENVAK RYMDAVRRRK GLVVQGRKLI DAEKQKTLKK
//
