ID A0A0P1BAA1_9BASI Unreviewed; 557 AA.
AC A0A0P1BAA1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamate 5-kinase {ECO:0000313|EMBL:CEH12897.1};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH12897.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH12897.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCYA01000192; CEH12897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BAA1; -.
DR STRING; 401625.A0A0P1BAA1; -.
DR OrthoDB; 2021096at2759; -.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 2.
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; IPR005715; Glu_5kinase/COase_Synthase.
DR InterPro; IPR019797; Glutamate_5-kinase_CS.
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 PRINTS; PR00474; GLU5KINASE.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CEH12897.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 51..284
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 58439 MW; 91080D6933AB782F CRC64;
MSSRPPIHGA ATTASLVSAT LGRESSSSNK AQHDAAASTS TASAANPPRG KRIVIKLGTS
SILSSLTNQP KLSVLSSIVE TCAALRKDGH SVVIVCSGAI GMGRLRMGLN EKPKSVGERQ
ALAALGQVRL IALWDSLFAQ VGISVAQVLL TRNDLGDRPR FENAKTTLST LLSLPFSSIP
IINENDTVSV SELRFGDNDT LSAIAAGIVD ADYLFLCTDV DGLYTGNPNS NPNARRLGVV
RNVALARKAV SVDTPGSNFG TGGMQTKLIA AELATAAGVA TVILNGNQPT NILSVVARGL
PALDADQRLP NSDQGMVSSI SSLLDAEELS KVGYPPILDP PHTLFLPTSE PLAQRKWSLL
HALHPAGTLV IDEGAFARIS KPESGGRLLP AGVVGVEGTW ERMQAVRIVL RRHRIASSAE
ATGTNVERDA LHHSQAIQES MSAAALARRG LTTFIKSSDG SGATTPIHLA GEDQHAHLAE
PVLTRDAPSE LDWELIEVGR GLANYSSIES ERIKGIKSSQ ISTVLGYADS SYIVDQLALM
PTEGAPSAHR SATKGRG
//
