VATA_CANTR
ID VATA_CANTR Reviewed; 1088 AA.
AC P38078;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000303|PubMed:8463270};
DE Short=V-ATPase subunit A;
DE EC=7.1.2.2 {ECO:0000250|UniProtKB:P17255};
DE AltName: Full=Vacuolar proton pump subunit A;
DE Contains:
DE RecName: Full=Endonuclease PI-CtrI;
DE EC=3.1.-.-;
DE AltName: Full=Ctr VMA intein;
DE AltName: Full=VMA1-derived endonuclease;
DE Short=VDE;
GN Name=VMA1;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX PubMed=8463270; DOI=10.1016/s0021-9258(18)53185-9;
RA Gu H.H., Xu J., Gallagher M., Dean G.E.;
RT "Peptide splicing in the vacuolar ATPase subunit A from Candida
RT tropicalis.";
RL J. Biol. Chem. 268:7372-7381(1993).
CC -!- FUNCTION: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase
CC (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC that hydrolyzes ATP and a membrane integral complex (V0) that
CC translocates protons (By similarity). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments (By
CC similarity). {ECO:0000250|UniProtKB:P17255}.
CC -!- FUNCTION: VDE is an endonuclease that can cleave at a site present in a
CC VMA1 allele that lacks the derived endonuclease segment of the open
CC reading frame; cleavage at this site only occurs during meiosis and
CC initiates 'homing', a genetic event that converts a VMA1 allele lacking
CC VDE into one that contains it. {ECO:0000250|UniProtKB:P17255}.
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:0000250|UniProtKB:P17255};
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1). {ECO:0000250|UniProtKB:P17255}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Membranes of
CC various intracellular acidic compartments.
CC {ECO:0000250|UniProtKB:P17255}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the VDE intervening region (intein)
CC followed by peptide ligation.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; M64984; AAB03895.1; -; Genomic_DNA.
DR PIR; A46080; A46080.
DR AlphaFoldDB; P38078; -.
DR SMR; P38078; -.
DR MEROPS; N09.001; -.
DR PRIDE; P38078; -.
DR VEuPathDB; FungiDB:CTMYA2_051490; -.
DR VEuPathDB; FungiDB:CTRG_02148; -.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.10.28.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR007868; Hom_end_hint.
DR InterPro; IPR007869; Homing_endonuc_PI-Sce.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; PTHR43607; 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 Pfam; PF05204; Hom_end; 1.
DR Pfam; PF05203; Hom_end_hint; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF55608; SSF55608; 2.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Autocatalytic cleavage; DNA-binding; Endonuclease;
KW Hydrogen ion transport; Hydrolase; Intron homing; Ion transport; Membrane;
KW Nuclease; Nucleotide-binding; Protein splicing; Translocase; Transport;
KW Vacuole.
FT CHAIN 1..283
FT /note="V-type proton ATPase catalytic subunit A, 1st part"
FT /id="PRO_0000002455"
FT CHAIN 284..754
FT /note="Endonuclease PI-CtrI"
FT /id="PRO_0000002456"
FT CHAIN 755..1088
FT /note="V-type proton ATPase catalytic subunit A, 2nd part"
FT /id="PRO_0000002457"
FT DOMAIN 485..662
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 1088 AA; 119154 MW; 77258751E455B62A CRC64;
MAGALENARK EIKRLSLDDT NESQYGQIYS VSGPVVIAEN MIGCAMYELV KVGHDNLVGE
VIRINGDKAT IQVYEETAGV TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKDES
QSIYIPRGID VPALSRTVQY DFTPGQLKVG DHITGGDIFG SIYENSLLDD HKILLPPRAR
GTITSIAEAG SYNVEEPVLE VEFDGKKHKY SMMHTWPVRV PRPVAEKLTA DHPLLTGQRV
LDSLFPCVQG GTTCIPGAFG CGKTVISQSL SKFSNSDVII YVGCFTKGTQ VMMADGADKS
IESIEVGDKV MGKDGMPREV VGLPRGYDDM YKVRQLSSTR RNAKSEGLMD FTVSADHKLI
LKTKQDVKIA TRKIGGNTYT GVTFYVLEKT KTGIELVKAK TKVFGHHIHG QNGAEEKAAT
FAAGIDSKEY IDWIIEARDY VQVDEIVKTS TTQMINPVHF ESGKLGNWLH EHKQNKSLAP
QLGYLLGTWA GIGNVKSSAF TMNSKDDVKL ATRIMNYSSK LGMTCSSTES GELNVAENEE
EFFNNLGAEK DEAGDFTFDE FTDAMDELTI NVHGAAASKK NNLLWNALKS LGFRAKSTDI
VKSIPQHIAV DDIVVRESLI AGLVDAAGNV ETKSNGSIEA VVRTSFRHVA RGLVKIAHSL
GIESSINIKD THIDAAGVRQ EFACIVNLTG APLAGVLSKC ALARNQTPVV KFTRDPVLFN
FDLIKSAKEN YYGITLAEET DHQFLLSNMA LVHNCGERGN EMAEVLMEFP ELFTEISGRK
EPIMKRTTLV ANTSNMPVAA REASIYTGIT LAEYFRDQGK NVSMIADSSS RWAEALREIS
GRLGEMPADQ GFPAYLGAKL ASFYERAGKA TALGSPDRVG SVSIVAAVSP AGGDFSDPVT
TSTLGITQVF WGLDKKLAQR KHFPSINTSV SYSKYTNVLN KYYDSNYPEF PQLRDKIREI
LSNAEELEQV VQLVGKSALS DSDKITLDVA TLIKEDFLQQ NGYSSYDAFC PIWKTFDMMR
AFISYYDEAQ KAIANGAQWS KLAESTSDVK HAVSSAKFFE PSRGQKEGEK EFGDLLTTIS
ERFAEASE
