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Database: UniProt
Entry: S7RWJ3_GLOTA
LinkDB: S7RWJ3_GLOTA
Original site: S7RWJ3_GLOTA 
ID   S7RWJ3_GLOTA            Unreviewed;       439 AA.
AC   S7RWJ3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   ORFNames=GLOTRDRAFT_70547 {ECO:0000313|EMBL:EPQ59265.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ59265.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ59265.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ59265.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; KB469297; EPQ59265.1; -; Genomic_DNA.
DR   RefSeq; XP_007862303.1; XM_007864112.1.
DR   AlphaFoldDB; S7RWJ3; -.
DR   STRING; 670483.S7RWJ3; -.
DR   GeneID; 19308099; -.
DR   KEGG; gtr:GLOTRDRAFT_70547; -.
DR   eggNOG; KOG0787; Eukaryota.
DR   HOGENOM; CLU_023861_0_1_1; -.
DR   OMA; ICEAQEH; -.
DR   OrthoDB; 3058550at2759; -.
DR   Proteomes; UP000030669; 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; 2.
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:UP000030669};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT   DOMAIN          42..200
FT                   /note="Branched-chain alpha-ketoacid dehydrogenase
FT                   kinase/Pyruvate dehydrogenase kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10436"
SQ   SEQUENCE   439 AA;  50084 MW;  BF56C7CE3B48EEA0 CRC64;
     MKRLLRRAPV THGVNTERRQ STALHFYQNR QLELYASKQT KRLTLRQLVF FGRSMNEERL
     IQSGNYVRTE LPVRIAHRIR DLQALPYVVV TQEGVARVYE LYWSAFEKFR RYPEIKTLSD
     NEAFCAFLRD ILEEHAAVIP SLSLGLSLSS PYLPPDQLDS FMRRMLVSRI SRRVLAEHHI
     ALSEHFARRD SRSGDVGIID TGLNISESVN KCVKFLRDRR FDLEEDGVDM PDQDKEWPEV
     VVEGHLNAKF SYIREHLEYI VFELLKNSMR ATGLKHLDKS TLPPIHATIA ASTDEIGIRI
     SDQGMSSTSG RVIKASPQDL FSFSHTRNAA RLETSRIGAL RTVSSSKQGM KATVDEQLQW
     WKRRRRDSAP SFDVDARSDD IETEAGVAPH PRIGIGLPMS NIFARYFGGS LELISLDGWG
     TDAYIRLPKL GTNLEGIEL
//
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