(data stored in ACNUC27125 zone)

HOGENOM: ASHGO_8_PE7

ID   ASHGO_8_PE7                          STANDARD;      PRT;   76 AA.
AC   ASHGO_8_PE7; Q75G38;
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; (ASHGO_8.PE7).
GN   Name=ATP9; OrderedLocusNames=AMI007W; ORFNames=AgATP9;
OS   ASHBYA GOSSYPII ATCC 10895.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ASHGO_8.PE7.
CC       Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-
CC       1056) mitochondrion, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:ATP9_ASHGO
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. In yeast, the
CC       dimeric form of ATP synthase consists of 18 polypeptides: alpha,
CC       beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d,
CC       E (Tim11), f, g, h, i, j and k.
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; Q75G38; -.
DR   EMBL; AE016821; AAS50174.1; -; Genomic_DNA.
DR   RefSeq; NP_987084.1; NC_005789.1.
DR   ProteinModelPortal; Q75G38; -.
DR   STRING; Q75G38; -.
DR   GeneID; 2760770; -.
DR   GenomeReviews; AE016821_GR; AMI007W.
DR   KEGG; ago:AGOS_AMI007W; -.
DR   NMPDR; fig|33169.1.peg.4725; -.
DR   AGD; AMI007W; -.
DR   eggNOG; fuNOG12572; -.
DR   OrthoDB; EOG4J9R8T; -.
DR   BioCyc; AGOS-XXX-01:AGOS-XXX-01-004725-MON; -.
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; ASHGO_8.PE7; -.
KW   AAS50174.1003186affold_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;
     MQLVLAAKYI GAGISTIGLL GAGIGIAIVF AALIQGVSRN PSMKDTLFQF AILGFAISEA
     TGLFCLMISF LLLYGV
//

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