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Database: UniProt
Entry: A0A498HFN5_MALDO
LinkDB: A0A498HFN5_MALDO
Original site: A0A498HFN5_MALDO 
ID   A0A498HFN5_MALDO        Unreviewed;      1307 AA.
AC   A0A498HFN5;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE            EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN   ORFNames=DVH24_028284 {ECO:0000313|EMBL:RXH68137.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH68137.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH68137.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH68137.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000864};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC         Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000256|ARBA:ARBA00000891};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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}. Peroxisome
CC       {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00005272}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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:RXH68137.1}.
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DR   EMBL; RDQH01000343; RXH68137.1; -; Genomic_DNA.
DR   STRING; 3750.A0A498HFN5; -.
DR   Proteomes; UP000290289; Chromosome 17.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR   Gene3D; 3.50.50.100; -; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR045024; NDH-2.
DR   InterPro; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00756; PPR; 2.
DR   PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR43706:SF48; NADH:UBIQUINONE REDUCTASE (NON-ELECTROGENIC); 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF13041; PPR_2; 1.
DR   Pfam; PF13812; PPR_3; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SMART; SM00054; EFh; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51375; PPR; 3.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 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   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          1..144
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          728..763
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REPEAT          1117..1151
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   REPEAT          1152..1186
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   REPEAT          1187..1221
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
SQ   SEQUENCE   1307 AA;  145712 MW;  B287A0722BDAD53A CRC64;
     MAKIFKINQT EANINRVVGT SNGYMSPEYT RDMTIFSEKL DVFSFGVLLL EIVSGKKNAA
     FYHFEHSPTL AGWAWELWKE GRGMEVIDES VRETCRPDEA LRCIHVGFLC VQEAPADRPT
     MSSVIRMLQS TEATSLPPSK KPAFSTYRNS SFVPSSQTPT SFSHSSVTTS LPEAMDTEPI
     SLFEFSIILL HVFPKSRISV AVDTISENNS LSGGIFELGF KSGQLSNYYI GIWYSKHVVS
     ERTIVWVANR DIHFQSIVGD YKWKEECCFL LISKFSNSCR MELWKEGKGK EVMMDQQGKH
     GGLIHVGFLC VQEAPDDRLT TSSVVHMLQG NEATPPSLSK KPAFSMWGQS FFETASRLFH
     QRSSLSKILV VVTVSGGGLA TFHETKPVHT VYADSAQEAE TSRKKKVVVL GTGWAGVSFL
     KNLRSSSYDV EVVSPKNYFM FTPLLPSVTC GTVEARSIVE PIRKITEKKG LDVEFREAEC
     YRIDPKNKKV LCRSTQHSNL GLKEAEFSVD YDYLIVAMGA KTNTFNTPGV EQYAHFLKGI
     EDAVRIRQTV IDCFERASLP SASEEEKKKL LSFVCVGGGP AGVEFAAELH DFVKDDLAKL
     YPSVTGYVKI TVIEASDHIL NMFDKRITAF AEGKFFRDGI DVKTGSLVVK LTDKEVSAKD
     RDTGKISNIP YGMVLWATGI GPRPEIIDFM KQIGQTNRRV LATDEWLRVE GCDGVYALGD
     CATVNQRRVV DDIVSIFRKA DKDNSGTLSL EEFQEVMEDL MVRYPQLSLH LKSKHMRNID
     ELLENSWKNP KDEIDIETFK AALSQADSQM KNLPATAQVA AQQGAYLADC FNRMEECEKY
     PEGPLKFRDV GRHRFQPFRY KHFGMFAPLG GEQTAAHLPG DWVSIGQSTQ WLWYSQASEL
     AHKGAGGFGL GKAIYFRKGH QCLRCYIAAA ASDVRALTFL PNSAPIRRPN HNPPPFSTSV
     DPPLFSTATR FISSSRTSSS PEQEATLNQI LSSIQNAATL LESLYENRLF LSPKSFNSVL
     VAAAAESGDL SLLSQLLQVA IASSQPLNSA CFLTVAKAFA KSDDCAELLR LTKQVMELTA
     PSMTVINRIL FAFGECGETE KALLIFSQMK TLAFVPDLYT HNTVLEILGC AGRIDELVGQ
     FGVMKEAGIV PDVVSYNTVL NNLRKLGKFD VCLFYFKEMG ENGVEADLLT YTAVIESLGR
     SGNVEEALRF FDEMKAREIR PSLYVYRSLI TNLKKMGKVD LALSLTEEMN SCDSELAGPM
     DFKRNKRFEM ICIKHDSNST VFFEQSCSYL QTDDTQITGP NYFEQSS
//
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