ID A0A1S9DRS8_ASPOZ Unreviewed; 443 AA.
AC A0A1S9DRS8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=OAory_01082520 {ECO:0000313|EMBL:OOO11782.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO11782.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO11782.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO11782.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU366032}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000256|ARBA:ARBA00006155, ECO:0000256|RuleBase:RU366032}.
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:OOO11782.1}.
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DR EMBL; MKZY01000003; OOO11782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DRS8; -.
DR VEuPathDB; FungiDB:AO090102000525; -.
DR eggNOG; KOG0787; Eukaryota.
DR Proteomes; UP000190312; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.140.20; Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR PANTHER; PTHR11947:SF25; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU366032};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU366032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366032};
KW Reference proteome {ECO:0000313|Proteomes:UP000190312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 54..221
FT /note="Branched-chain alpha-ketoacid dehydrogenase
FT kinase/Pyruvate dehydrogenase kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10436"
FT DOMAIN 270..419
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF02518"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 50604 MW; A251393FB89B48C0 CRC64;
MLRSHPAGRW HAFRQACAPK CRPYSGLHQL QPHNPPPWRP VSALDEWVER DIRPISLRQL
TFFGRTLTES RLISSANYVR TELPTRLAHR LRDIQRLPYV VVANPHLSLV YELYYKAFER
FRTIPEIKTL DDNDKFCDIL RKTLQEHLVV IPRLAMGVLE CRALLPADVL DQFMNTLLRA
RISRRVIAEQ HLALTETFNS PWHFPGSQDR TDVNADYVGE VFLKCNAKEV IERCGKLAQD
MMRQASGTDK IPEISVQGHL DATFPYMLSH LEYIIGELLR NSIQAVSEKY NGLPEKPPPI
EVLICEAPQH VIMRISDQGG GIPREVLPYL WSFNKGPHSK ARLQNLEQVP AMAATMQELT
VPKERKRADK ETFRESSLDT LTSRPPNLRL GMGLPMSRVY AEYWAGSLEL HSLEGYGVDA
FLQISKLGNK NEQVTTRASI DAV
//