ID A0A0G2E3N5_9EURO Unreviewed; 631 AA.
AC A0A0G2E3N5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=UCRPC4_g05320 {ECO:0000313|EMBL:KKY17687.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY17687.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY17687.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY17687.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY17687.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY17687.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY17687.1}.
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DR EMBL; LCWF01000137; KKY17687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2E3N5; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000053317; 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 CDD; cd03141; GATase1_Hsp31_like; 1.
DR Gene3D; 3.40.50.880; -; 1.
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; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR11947:SF20; [3-METHYL-2-OXOBUTANOATE DEHYDROGENASE [LIPOAMIDE]] KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; 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.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS50109; HIS_KIN; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyruvate {ECO:0000313|EMBL:KKY17687.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 202..390
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 631 AA; 68676 MW; BDAF29AC498261CE CRC64;
MSDEEDEALI ASANFTLSLL PARLAYRIQC LRNLPFIVVS NPHISKIYSN YLHSLSTLLP
YQKRHIKSIA EVAEFTEVMD DLVRTHSNTI PTLARGFMEC RKYISPAEVT NFLEEHLRAR
IGTRLIAEQH IALHMESLPD SEPGEKDRND SHYIGVIDTQ LCPADIVRSC EDSVAEVCEL
KYGVRPSVII NGQIDATFAH VPVHLEYILT ELLKNAFRAT IESENQREPI EVTIAAASDA
SQKGLGELKQ IMLDQATARH LMKNNEELDS AKCDNGVGRV DTIEPAAPAA PSITIRIRDR
GGGISPDVLP NIWSYSFTTF GDKEAASVDA GASDGMSTLS RGSGNQSSLA GLGYGLPLSR
AYAEYFGGGI SVQSLFGWGT DVYLTLQDLH NPFKPNAMSP RPKLLVVLTS HAKLGNLDKE
TGWYLPEFAH PYWKLEPHVD LVVASPAGGE APLDPSSVEM FKNDEESQRF LKEKQDLWKK
TEKLSDFKGK TGEFAGIYYP GGHGPMFDLA SDPTSIELAR DFYESGKVVS AVCHGPAALV
NVKLSDGSYL IAGQPVTGFS NVEEDQVGLS SAMPFLLETD LQKNSGGKFE KADEPWGVKV
VVSGKGGKLL TGQNPASAGP LGEAIVKALK A
//
