ID A0A1J7IS22_9PEZI Unreviewed; 498 AA.
AC A0A1J7IS22;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JUN-2023, entry version 25.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=CONLIGDRAFT_361997 {ECO:0000313|EMBL:OIW30278.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW30278.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW30278.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW30278.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
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}.
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DR EMBL; KV875097; OIW30278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7IS22; -.
DR STRING; 1408157.A0A1J7IS22; -.
DR InParanoid; A0A1J7IS22; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000182658; 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; 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 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:UP000182658};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 76..240
FT /note="Branched-chain alpha-ketoacid dehydrogenase
FT kinase/Pyruvate dehydrogenase kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10436"
FT REGION 386..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 56111 MW; D17C0F0D63CED3B8 CRC64;
MPLKLQNSTA SLRLRPSTGI CCRRGPFAGT LQLQLQPCVT QDQPRSRTQF RYSHSHPPKW
RPVSVLDDWV AKEARPISLR QLMVFGRSLS ESRLISSANY VRTELPTRIA HRIRDMQQLP
YVVVTNSNIS EVYDLYYLAF DTFRKVKEIK TLEDNEKFCK TINSMLKAHL TVIPKLAMGI
LECGGLMKSE DLDRFMNTIL RSRISRRVIA EQHLALTETF HADWFSPGAK LSDSEFIGEV
FLACVAKDVI ERCGKAIHEI ARLAYGEDVP LPKIKVEGHL DAQFPYILSH LEYIIGELLR
NSVQSVVERY QRTPPEKRPQ TIPDIEVTIC ESPQNVTFRI SDQGGGVPRE VMPYLWSFSK
GPQTERLLEN LSQVPQMAAT MQELQVKEAD EHHRATHALK TKHSSSKHDG SSGGETPSYG
DSINPSASHG NSLSTLSRRP PNLRLGMGLP LSRVYAEYWA GSLTLHSLEG YGVDAFLQVS
KLGNKNEQLT TRASMDAI
//