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Database: UniProt
Entry: A0A1X2GL81_9FUNG
LinkDB: A0A1X2GL81_9FUNG
Original site: A0A1X2GL81_9FUNG 
ID   A0A1X2GL81_9FUNG        Unreviewed;       450 AA.
AC   A0A1X2GL81;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=NADH dehydrogenase I, D subunit {ECO:0000313|EMBL:ORX56372.1};
GN   ORFNames=DM01DRAFT_1334856 {ECO:0000313|EMBL:ORX56372.1};
OS   Hesseltinella vesiculosa.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX   NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX56372.1, ECO:0000313|Proteomes:UP000242146};
RN   [1] {ECO:0000313|EMBL:ORX56372.1, ECO:0000313|Proteomes:UP000242146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX56372.1,
RC   ECO:0000313|Proteomes:UP000242146};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORX56372.1}.
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DR   EMBL; MCGT01000010; ORX56372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2GL81; -.
DR   STRING; 101127.A0A1X2GL81; -.
DR   OrthoDB; 191at2759; -.
DR   Proteomes; UP000242146; 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   Reference proteome {ECO:0000313|Proteomes:UP000242146};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685}.
FT   DOMAIN          180..450
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   450 AA;  51103 MW;  DCE4890009565F47 CRC64;
     MAFASRLFAR RLAAVRPSVA MNKVSMVKPM AWRSMATTAN QAVTTITEDR EFGEALEGEE
     ETKLRNFTVN FGPQHPAAHG VLRLILELNG EEIVRADPHI GLLHRGTEKL IEYKTYLQAL
     PYFDRLDYVS MMTNEQAYSL AVEKLLNIEV PERAKYIRTL FGEITRILNH IMSVTSHAMD
     VGALTPFLWM FEEREKLMEF YERVSGARLH TAYVRPGGVA LDLPHGLLDD IQLWAEQYGD
     RIDEMEEMLS GNRIWRVRTE NIGVVTVQEA NDWGFSGVLV RGSGIKFDIR KNNPYDAYDQ
     VEFDVPIGQN GDCFDRYLCR TEEMRQSLRI ISQCINKIPE GPIKVDDWKI APPPRAAMKE
     NMEALIHHFK LYSEGYSVPA GETYTVIEAP KGEFGVFLVS DGSNRPYRCK IKAPGFAHLQ
     GSDFMSRGHL LPDMVALIGT MDIVFGEVDR
//
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