ID A0A178ADN4_9PLEO Unreviewed; 231 AA.
AC A0A178ADN4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE SubName: Full=NADH-quinone oxidoreductase {ECO:0000313|EMBL:OAK95815.1};
GN ORFNames=IQ06DRAFT_329174 {ECO:0000313|EMBL:OAK95815.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK95815.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK95815.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK95815.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00009173, ECO:0000256|RuleBase:RU004464}.
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DR EMBL; KV441721; OAK95815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178ADN4; -.
DR STRING; 765868.A0A178ADN4; -.
DR InParanoid; A0A178ADN4; -.
DR OrthoDB; 33762at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR Gene3D; 3.40.50.12280; -; 1.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR NCBIfam; TIGR01957; nuoB_fam; 1.
DR PANTHER; PTHR11995; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU004464};
KW Iron {ECO:0000256|RuleBase:RU004464};
KW Iron-sulfur {ECO:0000256|RuleBase:RU004464};
KW Metal-binding {ECO:0000256|RuleBase:RU004464};
KW NAD {ECO:0000256|RuleBase:RU004464};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 106..214
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT REGION 35..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 25421 MW; 326EC08B643D21B8 CRC64;
MLSTTRSAAS MALRAKPATA LLPFRAGSAA FLSSSSSDKA TTMKTPATIP GNPGTPPPMK
AARREVPLPS QEGKKGAMQY ALTTLDQVAN WARQSSLWPM TFGLACCAVE MMHLSTPRYD
QDRLGIIFRA SPRQSDVMIV AGTLTNKMAP ALRQVYDQMP DPRWVISMGS CANGGGYYHY
SYSVTRGCDR IVPVDIYVPG CPPTAEALMY GIFQLQKKMR HTKITRMWYR K
//