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Database: UniProt
Entry: A0A178ADN4_9PLEO
LinkDB: A0A178ADN4_9PLEO
Original site: A0A178ADN4_9PLEO 
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
//
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