ID A7F6R1_SCLS1 Unreviewed; 65 AA.
AC A7F6R1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Complex III subunit 9 {ECO:0000256|ARBA:ARBA00044247, ECO:0000256|RuleBase:RU368056};
GN ORFNames=SS1G_13290 {ECO:0000313|EMBL:EDN98432.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN98432.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC complex plays an important role in the uptake of multiple carbon
CC sources present in different host niches.
CC {ECO:0000256|RuleBase:RU368056}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC Rieske protein, 2 core protein subunits, and additional low-molecular
CC weight protein subunits. {ECO:0000256|RuleBase:RU368056}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434,
CC ECO:0000256|RuleBase:RU368056}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU368056}.
CC -!- SIMILARITY: Belongs to the UQCR10/QCR9 family.
CC {ECO:0000256|ARBA:ARBA00007856, ECO:0000256|RuleBase:RU368056}.
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DR EMBL; CH476644; EDN98432.1; -; Genomic_DNA.
DR RefSeq; XP_001585774.1; XM_001585724.1.
DR AlphaFoldDB; A7F6R1; -.
DR STRING; 665079.A7F6R1; -.
DR GeneID; 5481770; -.
DR KEGG; ssl:SS1G_13290; -.
DR VEuPathDB; FungiDB:sscle_03g031260; -.
DR InParanoid; A7F6R1; -.
DR OMA; TWNKGKQ; -.
DR OrthoDB; 8789at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR Gene3D; 1.20.5.260; Cytochrome b-c1 complex subunit 9; 1.
DR InterPro; IPR008027; QCR9.
DR InterPro; IPR036656; QCR9_sf.
DR PANTHER; PTHR12980:SF0; CYTOCHROME B-C1 COMPLEX SUBUNIT 9; 1.
DR PANTHER; PTHR12980; UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX, SUBUNIT X; 1.
DR Pfam; PF05365; UCR_UQCRX_QCR9; 1.
DR SUPFAM; SSF81514; Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU368056}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU368056};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU368056};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Respiratory chain {ECO:0000256|RuleBase:RU368056};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368056}.
SQ SEQUENCE 65 AA; 7621 MW; 8AF7987CAFAB389F CRC64;
MPSASRPLYN FLFRKNYVFL GAVFASAFGF EMAYDSITDR VWDSINKGRQ WKDIRSRYVE
AADDE
//
