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Database: UniProt
Entry: A6QSI3_AJECN
LinkDB: A6QSI3_AJECN
Original site: A6QSI3_AJECN 
ID   A6QSI3_AJECN            Unreviewed;       277 AA.
AC   A6QSI3;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Dephospho-CoA kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HCAG_00339 {ECO:0000313|EMBL:EDN02475.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN02475.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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DR   EMBL; CH476655; EDN02475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6QSI3; -.
DR   STRING; 339724.A6QSI3; -.
DR   VEuPathDB; FungiDB:HCAG_00339; -.
DR   HOGENOM; CLU_057180_0_1_1; -.
DR   OMA; RWEMYRA; -.
DR   OrthoDB; 5473585at2759; -.
DR   Proteomes; UP000009297; 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   PANTHER; PTHR10695:SF46; DEPHOSPHO-COA KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10695; DEPHOSPHO-COA KINASE-RELATED; 1.
DR   Pfam; PF01121; CoaE; 2.
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:UP000009297};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        236..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          62..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   277 AA;  30404 MW;  5EB2E51FD815B737 CRC64;
     MLLIGLTGSI ATGKSTVSAL LSAPPYNLPI IDADLLARKV VEPGTPGYRA IVDYFGPTTP
     DLLLPDDPDD PDDKHKPKAT TQAHGRPLNR PVLGRRVFGD TAERKRDRAV LNRIVHPAVR
     WEIYRALLRH YLRGHWAVVL DVPLLFESGL DALCGTVVVV GVSDAAVQVA RLRARDAHLS
     AEDAEARVKS QGDVRGKVAR AEARGGLVVW NDGDRAALEA AVREAMRTVA ATSPQWWAWV
     LLLVPPLGVA VAAWNLAVNY RGRRRWEEAE RVRRAKL
//
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