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Database: UniProt
Entry: F1LF12_ASCSU
LinkDB: F1LF12_ASCSU
Original site: F1LF12_ASCSU 
ID   F1LF12_ASCSU            Unreviewed;       245 AA.
AC   F1LF12;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial {ECO:0000256|ARBA:ARBA00017279};
DE   AltName: Full=Complex I-42kD {ECO:0000256|ARBA:ARBA00032828};
DE   AltName: Full=NADH-ubiquinone oxidoreductase 42 kDa subunit {ECO:0000256|ARBA:ARBA00032628};
DE   Flags: Fragment;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY48716.1};
RN   [1] {ECO:0000313|EMBL:ADY48716.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I), that is believed not to be
CC       involved in catalysis. Complex I functions in the transfer of electrons
CC       from NADH to the respiratory chain. The immediate electron acceptor for
CC       the enzyme is believed to be ubiquinone.
CC       {ECO:0000256|ARBA:ARBA00003195}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA10 subunit family.
CC       {ECO:0000256|ARBA:ARBA00008606}.
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DR   EMBL; JI182191; ADY48716.1; -; mRNA.
DR   AlphaFoldDB; F1LF12; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:InterPro.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR031314; DNK_dom.
DR   InterPro; IPR015828; NDUFA10.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR   PANTHER; PTHR10513:SF15; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 10, MITOCHONDRIAL; 1.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000543; NADH_UQ_42KD; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Ubiquinone {ECO:0000313|EMBL:ADY48716.1}.
FT   DOMAIN          11..215
FT                   /note="Deoxynucleoside kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01712"
FT   NON_TER         245
FT                   /evidence="ECO:0000313|EMBL:ADY48716.1"
SQ   SEQUENCE   245 AA;  29644 MW;  9E7C5436E0F31AA8 CRC64;
     MPEFKMEDIL IDRYNNDMRK FYHLFPKRFR IPDMEMFYKD PMSDMSAVMR DRIFNCRFDQ
     YLNAVAHILN TGQGVVLERS PHSDFVFANA MRAKNYIGPE YFKHYFYVRK TALPKLHFWP
     HLVVYLDAPV SVCLQNIRKE GNVNKVSVLD EIYLKTIEDS YKDSLREFQK HSKILVYDWS
     KRGDTDTIVE DIERMDFDFF EWHSGDVFEE WFELIDEVSW AGWRIYVTQK YKARSQAFFQ
     TRIVH
//
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