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Database: UniProt
Entry: A0A1J7IS22_9PEZI
LinkDB: A0A1J7IS22_9PEZI
Original site: A0A1J7IS22_9PEZI 
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
//
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