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Database: UniProt
Entry: A6QUB2_AJECN
LinkDB: A6QUB2_AJECN
Original site: A6QUB2_AJECN 
ID   A6QUB2_AJECN            Unreviewed;       615 AA.
AC   A6QUB2;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
GN   ORFNames=HCAG_00968 {ECO:0000313|EMBL:EDN03104.1};
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:EDN03104.1, 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).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC       {ECO:0000256|ARBA:ARBA00004137}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00005272}.
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DR   EMBL; CH476655; EDN03104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6QUB2; -.
DR   STRING; 339724.A6QUB2; -.
DR   VEuPathDB; FungiDB:HCAG_00968; -.
DR   HOGENOM; CLU_021377_1_1_1; -.
DR   OMA; QNNRHAL; -.
DR   OrthoDB; 48029at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR   Gene3D; 3.50.50.100; -; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR045024; NDH-2.
DR   PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR43706:SF50; NADH DEHYDROGENASE (UBIQUINONE)-RELATED; 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SMART; SM00054; EFh; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          462..497
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   615 AA;  69561 MW;  367F3741F1058C33 CRC64;
     MGNLFTTSSH YEFILLRSRT VRIIYNLFAY CGIFVVIGGV LVVGFFVYDA TTYRHDLSFD
     NIQVSELALN PRLGGPKNLP IADVLIDDHD SEAMREQRDK PKLVILGTGW GSVSLLKTLR
     PGDYHVTVVS PVNYFLFTPM LPSATVGTIG LRSLVEPVRS IVQRVRGHFL RAEAVDVEFS
     EKLVEVSQLD SNGQERRFYL PYDKLVIGVG STTNPHGVKG LEHCNFLKSI DDARKIKNKV
     LDNLELACLP STSDEERRRL LSFVVCGGGP TGVEFAAEIF DMLNEDLLRS FPRILRNEIS
     VHLIQSRSHI LNTYDQTLSE YAERRFANDQ VDVLTNSRVK EVKKDKILFT QIEDGKPILK
     ELPMGFSQST FCKQLAEKLN SQTNKLTLLT DSHLRVNGTP MGDVYAIGDC SSVQNNVADH
     IITFLRTIAW EKGKDPEKVH LTFAEWRNVA QRVKRRFPQA SGHLRRLDRL FEQYDKDRSG
     TLDFDELREL LVQIDSKLTS LPATAQRANQ QGKYLGLKFN KIAQAMPGMK ANEIDYGDLD
     EAVYKAFQYK HLGSLAYIGN AAIFDFNGMS WGGGLLGVYL WRSIYFAQSV SLRTRILLAM
     DWSKRAIFGR DMTSF
//
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