ID A0A0L6USK8_9BASI Unreviewed; 443 AA.
AC A0A0L6USK8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=VP01_4038g1 {ECO:0000313|EMBL:KNZ51227.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ51227.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ51227.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ51227.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-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:KNZ51227.1}.
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DR EMBL; LAVV01009100; KNZ51227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6USK8; -.
DR STRING; 27349.A0A0L6USK8; -.
DR VEuPathDB; FungiDB:VP01_4038g1; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000037035; 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:UP000037035};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 37..210
FT /note="Branched-chain alpha-ketoacid dehydrogenase
FT kinase/Pyruvate dehydrogenase kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10436"
SQ SEQUENCE 443 AA; 50047 MW; 6BE57BFF39DD804D CRC64;
MKKLSRPKHL IAFLPRRKMS FYGNSHVLRY AEMEAAPFSL RQLIFFGKVL SRHGSNTKEL
DHSLVQGANF TRLQLPIRLA RQIREFQSLP YIVTSNPYLS ETYQIYVEAF EKIRSYPEIR
GRVDNHQWCR FLESLLNQHK VVIPKLAIGV AESANHLTNT QIEQFMTRML YSRISRRVLA
EHHIALTRQF LDDSCARPSG HNLRYLGVID TELEVGTVVE KCIQLAQNIL HLHSPISSSS
TPISVLVHGE KNAKFAYIPD HLEFIVFELL LHAFRATVSS ANRRSMDVAS LPIEVQIASA
PTHITIRISD QAGGVLQSWG PSFSDDDDEA LPPTVSRREM FSFVHLTTAN DSLKELISST
DGTMEGKVRE QVDQVHNQHH IPPSTGSKIE QVQDARLRIG LPLSSIYAQF LGGSLEMYSI
PGFSDMVLCI PKLGTTTEPN NIQ
//