ID A0A0A2VAD3_BEABA Unreviewed; 811 AA.
AC A0A0A2VAD3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=HBS1-like protein {ECO:0000313|EMBL:KGQ04846.1};
GN ORFNames=BBAD15_g9918 {ECO:0000313|EMBL:KGQ04846.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ04846.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ04846.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ04846.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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 -!- 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:KGQ04846.1}.
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DR EMBL; ANFO01001006; KGQ04846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VAD3; -.
DR STRING; 1245745.A0A0A2VAD3; -.
DR eggNOG; KOG0458; Eukaryota.
DR HOGENOM; CLU_007265_3_2_1; -.
DR Proteomes; UP000030106; 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; 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; 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; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 400..624
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 87269 MW; 2358489C65520F27 CRC64;
MASFQDDDFY DPSEDDFEEE DADGMTPEDR VAMANGTEEV KKALGENASK VTVAQIQEAL
WHYYYDVEKS AGYLQKTFIS PTPKPTPKKA ASEGTFFSAF SSSSAVAHGG ATGADPRGSE
SGGYRAGQGS FQRLAFPIFK PPHLPMDTFF SDMPWLRTPT DRHATFIAPC TPPGGLLGGS
DGGPKMSKLQ ALAAARKKKT EQKKEQENEI QAEKGLQKLS ISSQKSSGQA QIPHTSASSA
PIPMRKGTCL ESEPLSTPNT PLSSATDEPL HGMEAHVNVV DQRPTPSAFA QTLIGSALGV
RKQNQDVFAM AYASSPTYLA SAFSEPSPDD IVLAAQAKAG KKATPAVKTA PKKKADGAAK
TDTKTDDVSK KVAGLKVNDV PPPKTKGLDV VKVYEKSGAK KSTSFVVVGH VDAGKSTLMG
RLLVDLKYVD QRTVDKYKRQ AEKSGKQSFA LAWVMDQRSE ERERGVTIDI ATNYFETDKT
KYTILDAPGH RDFVPNMIAG ASQADFAVLV IDANTGAYEK GLKGQTREHI LLLRSLGLQR
IIVAVNKLDM VGWSKDRFED ITQEVTGFLT GLGFQEKNVD FVPISGLDGE NIVKEITASA
ASWYQGGTLL DALERSEPTT IRALKKPFRM AISEIFRSQQ QGTLTLAGRI DSGTIQIGDS
LAVQPSGETA YIKSIMVDTY AQDWAVAGQN VSIALTDIDP IHIRAGDILC HAASPIPCGD
TFTMRAMAFE HLMPMPVDLH RGRLHSPGQI QSIVASLDKA TGDVIKKKPK VVQPGGVARV
VIKLNEKVPL EAGQRVVIRG GGETIAAGLL E
//
