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Database: UniProt
Entry: A0A0D1ZB81_9EURO
LinkDB: A0A0D1ZB81_9EURO
Original site: A0A0D1ZB81_9EURO 
ID   A0A0D1ZB81_9EURO        Unreviewed;       476 AA.
AC   A0A0D1ZB81;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   ORFNames=PV07_10632 {ECO:0000313|EMBL:KIW24956.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW24956.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW24956.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW24956.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847045; KIW24956.1; -; Genomic_DNA.
DR   RefSeq; XP_016245172.1; XM_016397981.1.
DR   AlphaFoldDB; A0A0D1ZB81; -.
DR   STRING; 569365.A0A0D1ZB81; -.
DR   GeneID; 27349826; -.
DR   VEuPathDB; FungiDB:PV07_10632; -.
DR   HOGENOM; CLU_023861_4_1_1; -.
DR   OrthoDB; 3058550at2759; -.
DR   Proteomes; UP000054466; 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   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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT   DOMAIN          269..455
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   476 AA;  52534 MW;  2E385315DC9C519E CRC64;
     MLKTAFRRRA LPLSFGQRRW TTQNTEEPFP PDINEWSHPP SNASISDEEI QRLAAQPRRP
     LTLADLVRHG KPPLRDSALL SSANFTLSLL PARLAHRIQA LRNLPFIVVS NPNVSKIYNN
     YLHSLSTLEP FYKKPIETIE EEMKFTEAMA DLVRTHSNTI PVLAQGFLQC RKYVDPAEVT
     RFLDQHLRAR IGTRLVAEQH LALHMASTGD AAKQKPDPTH VGVIDLALRP ADIVRRCEGF
     VNEVCEYKYG VRVSLVINGD QDAEFAHIPM HLEYIITELL KNAFRATIEN GAEKEPIEVT
     IASAPDVQTT KLESLKKLSV SKENAYDFSQ EGLDEYCASS DEDVLDALNS AAPYITLRIR
     DRGGGIPPDA LPNIWSYSFT TFNNEEAAAA ANAGSDGSEG LSAISNSGTN QSSIAGLGYG
     LPLGRAYAEY FGGGIAVQSM YGWGTDVYLT LQGIGNTQEL KDAPNGFEEL EKEMGD
//
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