(data stored in ACNUC27125 zone)

HOGENOM: CAGLA1_1_PE9

ID   CAGLA1_1_PE9                         STANDARD;      PRT;   76 AA.
AC   CAGLA1_1_PE9; Q85Q98;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP synthase subunit 9, mitochondrial;AltName:
DE   Full=Lipid-binding protein; (CAGLA1_1.PE9).
GN   Name=ATP9;
OS   CANDIDA GLABRATA CBS 138.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces; mitosporic
OC   Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAGLA1_1.PE9.
CC       Candida glabrata (strain ATCC 2001 / NRRL Y-65 / CBS 138 / IFO 0622)
CC       mitochondrion, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:ATP9_CANGA
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(0)
CC       domain. A homomeric c-ring of probably 10 subunits is part of the
CC       complex rotary element.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC   -!- GENE_FAMILY: HOG000235245 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q85Q98; -.
DR   EMBL; AJ511533; CAD54425.1; -; Genomic_DNA.
DR   RefSeq; NP_818784.1; NC_004691.1.
DR   ProteinModelPortal; Q85Q98; -.
DR   GeneID; 807026; -.
DR   GenomeReviews; AJ511533_GR; ATP9.
DR   KEGG; cgr:CaglfMp10; -.
DR   OrthoDB; EOG4J9R8T; -.
DR   PhylomeDB; Q85Q98; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR000454; ATPase_F0-cplx_csu.
DR   InterPro; IPR020537; ATPase_F0-cplx_csu_DDCD_BS.
DR   InterPro; IPR002379; ATPase_F0/V0-cplx_csu.
DR   Gene3D; G3DSA:1.20.20.10; ATPase_F0/V0_c; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; ATPase_F0/V0_c; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
DR   HOGENOMDNA; CAGLA1_1.PE9; -.
KW   CAD54425.149200367fold_1320000031;
KW   ATP synthase subunit 9, mitochondrial ;
KW   CF(0); Complete proteome; Hydrogen ion transport; Ion transport;
KW   Lipid-binding; Membrane; Mitochondrion; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   76 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQLALAAKYI GAGISTIGLI GAGIGIGIVF AALINGVSRN PSLKDTLFSY SILGMALSEA
     TGLFCLMISF MLLFAV
//

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