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Database: UniProt
Entry: W7HTC5_9PEZI
LinkDB: W7HTC5_9PEZI
Original site: W7HTC5_9PEZI 
ID   W7HTC5_9PEZI            Unreviewed;       260 AA.
AC   W7HTC5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Dephospho-CoA kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DRE_00334 {ECO:0000313|EMBL:EWC47366.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC47366.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC47366.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC47366.1,
RC   ECO:0000313|Proteomes:UP000024837};
RA   Liu X., Zhang W., Liu K.;
RT   "Drechslerella stenobrocha genome reveals carnivorous origination and
RT   mechanical trapping mechanism of predatory fungi.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI966410; EWC47366.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7HTC5; -.
DR   HOGENOM; CLU_057180_0_1_1; -.
DR   Proteomes; UP000024837; 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:UP000024837};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        220..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   260 AA;  28921 MW;  F29C41C3092D8580 CRC64;
     MLIIGLTGSI ATGKSTVSHI LSSPPHSLPI IDADHLAHAV VLPGTPAYRQ IIAQFASTTP
     NLLHDAATDP INSPHGASIN RRVLGQRVFG TSDENKRDIK ILNGIVHPAV RRAMAKQVLA
     AWLRGHWAAV LDVPLLFEGG LDVFCGVTLL VGTSPDVQLE RLLKRDPHLA RDDAERRIAS
     QMSLLRKKEM ADVVVWNDGS KQELEAEVAR FVQRMKGGRG WFWTVIMAGC WPVTATVVVW
     RLLGNWWHRR KLNERLRKQD
//
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