ID J5JX28_BEAB2 Unreviewed; 443 AA.
AC J5JX28;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE SubName: Full=Glutamate 5-kinase {ECO:0000313|EMBL:EJP66846.1};
GN ORFNames=BBA_04139 {ECO:0000313|EMBL:EJP66846.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP66846.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP66846.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP66846.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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DR EMBL; JH725158; EJP66846.1; -; Genomic_DNA.
DR RefSeq; XP_008597458.1; XM_008599236.1.
DR AlphaFoldDB; J5JX28; -.
DR STRING; 655819.J5JX28; -.
DR GeneID; 19887151; -.
DR HOGENOM; CLU_025400_1_1_1; -.
DR InParanoid; J5JX28; -.
DR OrthoDB; 2021096at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04242; AAK_G5K_ProB; 1.
DR CDD; cd21157; PUA_G5K; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 2.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR HAMAP; MF_00456; ProB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR041739; G5K_ProB.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR011529; Glu_5kinase.
DR InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR InterPro; IPR019797; Glutamate_5-kinase_CS.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR NCBIfam; TIGR01027; proB; 1.
DR PANTHER; PTHR43654; GLUTAMATE 5-KINASE; 1.
DR PANTHER; PTHR43654:SF3; GLUTAMATE 5-KINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01472; PUA; 1.
DR PIRSF; PIRSF000729; GK; 2.
DR PRINTS; PR00474; GLU5KINASE.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EJP66846.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 323..420
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 443 AA; 47764 MW; D29F0486064ED53B CRC64;
MTAKASCIRR AQPLTVVIKL GTSSIVDEKT HEPLLPILTL IVDTAVKLRK EGHRVVIVSS
GAIGVGLRRM DVDRRPKHLA QLQALAAIGQ CRLISLWDSL FSHLDQPVAQ ILLTRNDIAD
RTRYLNAQNT FNELLDIGVI PIVNENDTLA VSEIKFGDND TLSAITAAMI HADMLFLMTD
VDCLYDKNPR TNPDARAIEV VDDIGALEAD VSSAGSSLGT GGMMTKIIAA KLGTSAGVTT
IITRSSNPGN ILGIVNYLYS SPRSSVIDDP ENGNSLSRTA SLNLMAPSGV GFNGPPLHTR
FLPSSDPIRD RHFWLLHTPS PHGTVYIDAG AHKALLGKAG LLPVGVVDVE GNFASHEPVR
IVAVNRRKTP GPDGKMWDGV PEEIGRALVN YASSEISRIM GHQSVEIGEL LGYADSEYVA
HRSHIAFVRN NSRPVSPTMM SMV
//
