ID A0A364MRY5_9PLEO Unreviewed; 1948 AA.
AC A0A364MRY5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=DDE83_008921 {ECO:0000313|EMBL:RAR01389.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR01389.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU366032}. Peroxisome
CC {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AKT2 hydrolase
CC family. {ECO:0000256|ARBA:ARBA00005668}.
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:RAR01389.1}.
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DR EMBL; QGDH01000274; RAR01389.1; -; Genomic_DNA.
DR STRING; 183478.A0A364MRY5; -.
DR Proteomes; UP000249619; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; 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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR PANTHER; PTHR11947:SF20; [3-METHYL-2-OXOBUTANOATE DEHYDROGENASE [LIPOAMIDE]] KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU366032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366032}; Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 783..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1725..1931
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 322..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1948 AA; 209259 MW; 41137FCBE3B6B4E0 CRC64;
MFAFISAKPV WYLLACSSIL FLFYSPVGFW FGGQNRIISE RYPESLRAIF STETIDALSH
DPRLHDALFS LTEAIARSST DLGKRFNSEG LRSFGRNLTD GVGHVRSKFQ LDVKRRDLLD
DISGAFGDLM GPGGAGLNLT GGLTDILGSL GDSIAGSLGT PALFLGIGLG MGTTTGLNLT
DMEEAGAIAS RIATAYNSSA TGANLAAQQL GSGLSQQVIP SFGSNDISLG PAAFALASGI
GNATAVGLGL TQTRFEPSPD SSIEGVAGNF GLGVAMPIVS NFDFQALMQS LGNSSSATKL
MQQLPRIAAA AGIGLGKGAR NGLGLKSDDN NKQSGRAQKR QFKNGTASSG SNIPRAVKLF
AKGLSQSFIQ GSNFSNLNSA VSAAFPDSFD LQAMLGPLAA GAGAGIGTGA AIGFNFKPVD
TTSTIAGNIT KDEQQTALAA EAFTQNLLSN FLVNSSAIQK AKQFIADSPS QVFKGVDGAK
AAEGFARGTI EGVMSAMSSV GGLKNLISGD VPTDAFENVP VLSPTQFNDS VNGAAVGFAR
GLTGKATILV AAIARNFTPG SQSASDDIPG RKRSIGTEHE EASVVELDSL STRQAQQPGG
DQLPLAIDPA TAQMGAQKFI DSVTCQGMGG IASAALGIMS TSKPEMKMMD IAMGNTGIPL
DPTVLQVLPR GPITISSEGN MFEIVIESQS VKINGQALIP FAVLTGLHVL FSGLAFLAFL
PVYLVLGVVW RFSVLTGYPV NEAKNRKWRM GFLITFAILS VAGIILGMVG MGSASHFRDT
HGIMGLICLI ILFPTVGFSV VRLRTTLSHP APSAFVGIKG PIALAKSSER IYLISGIGSQ
LLLGLGQFAF LQGFATLRAI SLCVVDTVLT SASVAGLVSI VLMVQISATA LVGIRAWLEQ
HIAKKEAAGA TPTLPSGMKT HSRSDTIATF GFDRKEPPPA LNLNSTRPSV FSRKTEELKG
AEDNGISTPF NFRKEGSINE REPREDPFLS PEERLNYQER GIYNPKTGGY SYAAPTSGPD
GDYYNMAATY GERRPSSGIF DPQLSPRPPI VVTGPKTNNV STMDLWPPPM ADADRLYMTQ
KTQKTVSINM AAEEISPDFP FEKKHVKTLD SSMAYVDTGT PNQAKITVVF VHGNPTSSYL
WRNIIPHVSP IARCVAPDLV GFGDSGKMPS NGYYIREQVE YFEAFMEAVV AADEKVVFVV
HDWGSALGFD WARKHALRVA GLVFMEFVNL ALTTDNFDGW EERMKKMRDP DTGHKLVIEE
NYFVEFILKY HGTSSVVPEA VMEHYRRPFA NPADREPQWR MPNEIPLEGR APDVGKLVWE
AWDWLKAGNN QVPKLMFWVE PGMLLAPQSV KEVAEWLGDP KVVGLGPCGH FPQEEYPHRI
GEETRRFVDE ILEAHPSITT PSLSRRRVIG DASTQRSATV TLRACRKHGA NAAAPHHPVA
GDTTVLSAHG EENKQRAVCP RKQPPEAPHQ DGHGQGHLAP GEPPTASADA RRSRQVSFFP
HKLHCACRVA GQTLANQGRV RNRHGRPPLT TQQLLTSANF TLSTLPARLA HRIQSLRNLP
FIVVSNPHVS KIHSNYMHSL STLLPWAEQE IKTLEEEVKF TEVMADLVQT HANTISILAR
GFLEARKYIS PKDVTRFLDE HLRARIGTRL IAEQHLSLHF SSQPHCEVMH HADDNPGFIG
VIDTRLKPAR IVDHCANVVG EICELKYGVR PTIVINGEPE YEFAHVPVHL EYIITELLKN
AFRATVESGM EREPIEVTIA PLPELLPEDR EAEDKAAEDV RDGRLDNHDQ GNVDEASQRF
TGNTAPTSPP TASNILPLKH STPGVTIRIR DRGGGISPEN LGHIWDYSFT TFNDAQASST
LSGGSGSHSG NGMDALNAFS GAGGDGANSL AGLGYGLPLG RAYAEYFGGG IAVQSLWGWG
TDVYLSLRGV GRVDTMQEAR ESARKRQS
//
