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Database: UniProt
Entry: C5FHY4_ARTOC
LinkDB: C5FHY4_ARTOC
Original site: C5FHY4_ARTOC 
ID   C5FHY4_ARTOC            Unreviewed;       712 AA.
AC   C5FHY4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000256|ARBA:ARBA00018860};
DE            EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN   ORFNames=MCYG_01783 {ECO:0000313|EMBL:EEQ28964.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ28964.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001741};
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00029433}. Vacuole membrane
CC       {ECO:0000256|ARBA:ARBA00029427}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00029427}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00029427}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; DS995702; EEQ28964.1; -; Genomic_DNA.
DR   RefSeq; XP_002848849.1; XM_002848803.1.
DR   AlphaFoldDB; C5FHY4; -.
DR   STRING; 554155.C5FHY4; -.
DR   GeneID; 9223106; -.
DR   VEuPathDB; FungiDB:MCYG_01783; -.
DR   eggNOG; KOG1352; Eukaryota.
DR   HOGENOM; CLU_008162_3_0_1; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 5473187at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR   CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR   CDD; cd01134; V_A-ATPase_A; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR005725; ATPase_V1-cplx_asu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022878; V-ATPase_asu.
DR   NCBIfam; TIGR01042; V-ATPase_V1_A; 1.
DR   PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR   PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF16886; ATP-synt_ab_Xtn; 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-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          123..185
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          201..323
FT                   /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT                   /evidence="ECO:0000259|Pfam:PF16886"
FT   DOMAIN          332..557
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   REGION          41..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  77985 MW;  7D4C27C809B68C2C CRC64;
     MILGLGRPSL RPQPSLLDLV HRKKGASVSI VDACSALLKQ HQEDRTPPDS FDTNIDIDIT
     TSTNNDSNIS NDPDTEDSYS VDSSDIESIS SLSSSHIETR SPPVMAPKNS KPAEAGDEQK
     GVVFSISGPV IVAENMIGCA MYEMCHVGND NIVGEVIRIS GDQATIQVYE ETAGVTVGDP
     VIRTGKPLSV ELGPGLMETI YDGIQRPLKT ISEASESIYI PRGVALPALD RKKKWDFKPA
     GLKVGDHITG GDVWGTVFEN SLLHDHKILL PPRARGTITR ISGPGSFTVE EKLLEVEFNG
     KKTEYSMMHV WPVRVPRPVN EKLASDSPFI VGQRVLDSLF PGVQGGTICI PGAFGCGKTV
     ISQSVSKFSN SDIIVYVGCG ERGNEMAEVL MDFPELTITI DGRKEPIMKR TCLIANTSNM
     PVAAREASIY TGITVAEYFR DQGKHVAMMA DSSSRWAEAL REISGRLGEM PADQGFPAYL
     GAKLASFYER AGQTIALGSP ERKGSVSIVG AVSPPGGDFA DPVTSSTLNI VQVFWGLDKK
     LAQRKHFPSI NTSISYSKYT GILDKYYTKE HPEFPRLRDK IKELLSNSEE LDQVVQLVGK
     SALGDADKIT LDVATLLKED FLQQNGYSDY DQFCPLWKTE YMMKAFVSYY DESQKAIAQG
     QSWAKVREAT SAIQTALRNM KFEVPDDEKE VTAKYEKILQ DMSEKFASVS DE
//
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