ID A0A2T5M7S0_9EURO Unreviewed; 477 AA.
AC A0A2T5M7S0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=NADH-quinone oxidoreductase subunit D domain-containing protein {ECO:0000259|Pfam:PF00346};
GN ORFNames=P175DRAFT_0497702 {ECO:0000313|EMBL:PTU24582.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU24582.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU24582.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU24582.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|RuleBase:RU003685}.
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:PTU24582.1}.
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DR EMBL; MSFN02000001; PTU24582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5M7S0; -.
DR VEuPathDB; FungiDB:P175DRAFT_0497702; -.
DR OrthoDB; 191at2759; -.
DR Proteomes; UP000244073; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR NCBIfam; TIGR01962; NuoD; 1.
DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003685};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685}.
FT DOMAIN 205..465
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 53461 MW; A8A9BE03471CB8CD CRC64;
MAVSFARLAG NAPKTLCLRP SGIARNTTIP RSRSIATSIP RRAAEATSYQ ATRLIPTDPS
FTHLANKGPS ESETPAALES EAEGVDRKIR HYTVNFGPQH PAAHGVLRLI LELNGEEIVR
SDPHVGLLHR GTEKLIEYKT YMQALPYFDR LDYVSMMTNE QCFSLAVEKL LNIEIPERAK
YIRTLFGEMT RVLNHLMSVL SHAMDVGALT PFLWGFEERE KLMEFYERVS GARLHAAYVR
PGGVSQDIPL GLLDDIYQWA TQFGDRIDET EELLTDNRIW KARTQGVGVV SAADALNMSF
TGVMLRGSGV PWDIRKSQPY DAYDKVEFDV PVGVNGDCYD RYLCRMEEFR QSLRIIHQCL
NQIPAGPVRV EDYKISPPPR AAMKEGMESL IHHFLLFSKG YAVPPGETYS AIEAPKGEMG
VFLVSDGSER PYRCKIRAPG FAHLGGFDQI SRGHLLADAV AIIGECRDNY HPTFKLR
//
