ID E5AED0_LEPMJ Unreviewed; 272 AA.
AC E5AED0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Similar to dephospho-CoA kinase {ECO:0000313|EMBL:CBY01569.1};
GN ORFNames=LEMA_P003560.1 {ECO:0000313|EMBL:CBY01569.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY01569.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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DR EMBL; FP929139; CBY01569.1; -; Genomic_DNA.
DR RefSeq; XP_003845048.1; XM_003845000.1.
DR AlphaFoldDB; E5AED0; -.
DR STRING; 985895.E5AED0; -.
DR EnsemblFungi; CBY01569; CBY01569; LEMA_P003560.1.
DR GeneID; 13285885; -.
DR eggNOG; KOG3220; Eukaryota.
DR HOGENOM; CLU_057180_0_1_1; -.
DR InParanoid; E5AED0; -.
DR OMA; RWEMYRA; -.
DR OrthoDB; 5473585at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:InterPro.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02022; DPCK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR PANTHER; PTHR10695:SF46; DEPHOSPHO-COA KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10695; DEPHOSPHO-COA KINASE-RELATED; 1.
DR Pfam; PF01121; CoaE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:CBY01569.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Transferase {ECO:0000313|EMBL:CBY01569.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 231..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 63..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 30670 MW; DEB7349853E932C1 CRC64;
MLLLGLTGSI ATGKSTVSSL LSQPPYSLPI IDADLIARQV VEPGTPGYKA IVKHFLPTTP
DLLLAPDPNS NTDTTKGRPL NRPALGRRVF GPSPTQSRDR ALLNSIVHPA VRREIYRQIL
FAYLRGHWAV VLDIPLLFES GWERYCGTIV VVGVSDPAIQ IERLRRRDGH LSEEEARNRV
LSQGGVGEKV ERCRRRGEGW GVVVWNDGDR GALEGEVRRV MDGVRRASPR WWGFLLWVCP
PLGVGAGLWS WYKMRNVQLR WEEEKRREKA RL
//
