ID A0A1V8UKV6_9PEZI Unreviewed; 555 AA.
AC A0A1V8UKV6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
GN ORFNames=B0A51_06254 {ECO:0000313|EMBL:OQO24161.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO24161.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|EMBL:OQO24161.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCFEE 5018 {ECO:0000313|EMBL:OQO24161.1};
RX PubMed=28684563;
RA Coleine C., Masonjones S., Selbmann L., Zucconi L., Onofri S., Pacelli C.,
RA Stajich J.E.;
RT "Draft Genome Sequences of the Antarctic Endolithic Fungi Rachicladosporium
RT antarcticum CCFEE 5527 and Rachicladosporium sp. CCFEE 5018.";
RL Genome Announc. 5:e00397-17(2017).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003551}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU000339}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQO24161.1}.
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DR EMBL; NAEU01000349; OQO24161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UKV6; -.
DR STRING; 1974281.A0A1V8UKV6; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00962; atpA; 1.
DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003551};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003551};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003551};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU000339};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000339}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003551};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT DOMAIN 67..133
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 190..418
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 425..549
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
SQ SEQUENCE 555 AA; 59825 MW; DA89224982C854A6 CRC64;
MFRTALRTSA RAAGALSATS RVSAQRATPA ITQSFARTYA SDKASPTEVT SILEQRIRGV
QEESGLAETG RVLSVGDGIA RVHGMQNIQA EELVEFASGV KGMCMNLEAG QVGVVLFGSD
RLVKEGETVK RTGQIVEVPV GMELLGRVVD ALGNPIDGKG PLNASGTRRA QMKAPGILPR
RSVNQPVQTG LKSVDAMVPI GRGQRELIIG DRQTGKTAVA LDAILNQKRW NVTNDETKKL
YVIYVAVGQK RSTVAQLVQT LEANDAMKYT CIVAATASEA APLQYIAPFT GCSIGEYFRD
NGKHAVIIYD DLSKQAVAYR QMSLLLRRFG LPKPPGREAY PGDVFYLHSR LLERAAKMSD
KHGGGSLTAL PIIETQGGDV SAYIPTNVIS ITDGQIFLEA ELFYKGVRPA INVGLSVSRV
GSAAQLKAMK QVAGSLKLFL AQYREVAAFA QFGSDLDAAT KQTLNRGERL TELLKQKQYS
PMAVNEMVPL IYAGVNGHLD SVPVAKILQW EADFVAHLKS NESDLLATID KEGALSKDLE
AKLKNVVVTF TKAFT
//
