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Database: UniProt
Entry: A0A0F0I6Y7_ASPPU
LinkDB: A0A0F0I6Y7_ASPPU
Original site: A0A0F0I6Y7_ASPPU 
ID   A0A0F0I6Y7_ASPPU        Unreviewed;       681 AA.
AC   A0A0F0I6Y7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KJK63509.1};
GN   ORFNames=P875_00065050 {ECO:0000313|EMBL:KJK63509.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK63509.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK63509.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KJK63509.1}.
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DR   EMBL; JZEE01000556; KJK63509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I6Y7; -.
DR   STRING; 1403190.A0A0F0I6Y7; -.
DR   Proteomes; UP000033540; 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; 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:UP000033540};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        90..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          532..567
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   681 AA;  76042 MW;  55976B526BEF5210 CRC64;
     MSAVLLRSRP DQTALRRIGV LSSRLYSSKP PRPTRLTTSR ALLLCQNSVP QCLASRAFVN
     SHHSIRHQST APESTDASRK SSFRNAFFKT FAYCGFFIVM SGAAVVAFFI YDATTYREHS
     SAEDIPVSEL ALNPRRGGPK NLPVADVLVG DYDSEVMTEQ KDKPRLVILG TGWGSIALLK
     QLNPGDYHVT VVSPTNYFLF TPMLPSATVG TLGLRSLVEP VRRIVQRVNG HFLKGEAVDV
     EFSEKLVEVS GVDANGQKQN FYVPYDKLVI GVGCTTNPHG VKGLENCHFL KTIDDARQIK
     NQVLDNMELA CLPTTSDEER KRLLSFVVCG GGPTGVEFAA ELFDLLNEDL LYSFPKILRN
     EISVHIIQSR THILNTYDEA LSKYAEARFA RDHVDVLTNS RVKEVRDDKV VFTQMEDGKP
     VLKEIPMGFC LWSTGVAPAE ICKKLSAKLD SQNNKHALET DSHLRLIGAP LGDVYAIGDC
     STVQNNVADH IVSFLRTIAW EKGKDPEKLH LTFREWRDVA NRVKKRFPQA SNHLRRLDRL
     FEQYDKDHSG TLEFGELSEL LHQIDNKLTS LPATAQRANQ QGEYLGRKLT KIAAALPGMR
     ANEIDHGDLD EAVYKAFKYK HLGSLAYISN AAVFDFGGMN FSGGVLAMYL WRSVYFAESV
     SLRTRCMLAM DWAKRALFGR G
//
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