ID A0A1V6PT07_9EURO Unreviewed; 269 AA.
AC A0A1V6PT07;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Dephospho-CoA kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENANT_c043G06525 {ECO:0000313|EMBL:OQD79837.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD79837.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD79837.1}.
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DR EMBL; MDYN01000043; OQD79837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PT07; -.
DR STRING; 416450.A0A1V6PT07; -.
DR OrthoDB; 5473585at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 228..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 269 AA; 29424 MW; FF26CCB7F18012F8 CRC64;
MLIIGLTGSI ATGKSTVSTI LSTAPYSLPI IDADVLARKV VEPGTAGYKA IVNYFGPSTP
DLLLEDGTNP SGKPLNRPAL GRRVFGSTEE RKRDRGVLNG IVHPAVRWEV YKALIYHYLR
GQWAVVLDVP LLFESGMDLI CGTVIVVGVH NPEIQMARLR ARDAHLTAED AENRVRSQGD
VRMKAMQAEF RGTTTARGVV VWNDADREEL EKAVKGAMAS ITASSPRWWA WALLVAPPVG
VGVAAWNLVV NFATKKGWEK KKNEEKARL
//
