ID A0A0G4MSF6_9PEZI Unreviewed; 413 AA.
AC A0A0G4MSF6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, 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=BN1708_007339 {ECO:0000313|EMBL:CRK37149.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK37149.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK37149.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK37149.1};
RA Wang D.B., Wang M.;
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}.
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DR EMBL; CVQH01024638; CRK37149.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4MSF6; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000044602; 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:UP000044602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 61..225
FT /note="Branched-chain alpha-ketoacid dehydrogenase
FT kinase/Pyruvate dehydrogenase kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10436"
FT REGION 392..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 46017 MW; 84E1C633C11D88BF CRC64;
MLTIALPKAG RRCRLSSTLA SPTTRTTTAT PQTPPQCRHI NNSAWRAVSV LDEWVAREAR
PISLRQLMVF GRSLTEARLL SSANYVRTEL PTRIAHRIRD MQQLPYGVVT NPHISDVYQL
YHNAFDTFRK VKEVKTLEEN DHLCSIIGKM LKTHLTVIPK LAMGILESNG HIDPAVLDHF
MNTILRSRIS RRVIAEQHLA LTETFGADWF SPGAKLHESD FIGEVFIKCV ARDVVERCSS
AVEKLARSTY GPDVRVPEIK INGHLDASFP FILSHIEYII GELLRNAVQA VIERQQRLAA
EGGLDATTAA HHQQQPPPPP IEVTICEAQQ HVMIRISDQG GGIPTNELPY LWSFSSGPQS
RRRLENLRRV PKLAATMQEL HVSDELGRAD LKTPSYESSL ASLTGXSGAP CST
//
