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VATA_PYRFU
ID   VATA_PYRFU              Reviewed;        1013 AA.
AC   Q8U4A6;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=V-type ATP synthase alpha chain;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase subunit A;
DE   Contains:
DE     RecName: Full=Endonuclease PI-Pfu2;
DE              EC=3.1.-.-;
DE     AltName: Full=Pfu AtpA intein;
DE     AltName: Full=Pfu VMA intein;
GN   Name=atpA; OrderedLocusNames=PF0182;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The archaeal alpha chain is a catalytic subunit.
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   -!- 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. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The intein interrupts the ATP-binding site.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AE009950; AAL80306.1; -; Genomic_DNA.
DR   RefSeq; WP_011011295.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U4A6; -.
DR   SMR; Q8U4A6; -.
DR   STRING; 186497.PF0182; -.
DR   PRIDE; Q8U4A6; -.
DR   EnsemblBacteria; AAL80306; AAL80306; PF0182.
DR   GeneID; 41711973; -.
DR   KEGG; pfu:PF0182; -.
DR   PATRIC; fig|186497.12.peg.189; -.
DR   eggNOG; arCOG00868; Archaea.
DR   eggNOG; arCOG03154; Archaea.
DR   HOGENOM; CLU_008162_1_0_2; -.
DR   OMA; CFAKGTE; -.
DR   OrthoDB; 6736at2157; -.
DR   PhylomeDB; Q8U4A6; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
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   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
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; -; 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; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022878; V-ATPase_asu.
DR   PANTHER; PTHR43607; PTHR43607; 2.
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; PF14528; LAGLIDADG_3; 1.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 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; 1.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Autocatalytic cleavage; Endonuclease;
KW   Hydrogen ion transport; Hydrolase; Intron homing; Ion transport; Nuclease;
KW   Nucleotide-binding; Protein splicing; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           1..240
FT                   /note="V-type ATP synthase alpha chain, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000002464"
FT   CHAIN           241..665
FT                   /note="Endonuclease PI-Pfu2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000002465"
FT   CHAIN           666..1013
FT                   /note="V-type ATP synthase alpha chain, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000002466"
FT   DOMAIN          392..525
FT                   /note="DOD-type homing endonuclease"
SQ   SEQUENCE   1013 AA;  113452 MW;  CAC1CB86566C81CD CRC64;
     MPAKGRIIRV TGPLVIADGM KGAKMYEVVR VGELGLIGEI IRLEGDKAVI QVYEETAGLK
     PGEPVEGTGS SLSVELGPGL LTSIYDGIQR PLEVLREKSG HFIARGISAP ALPRDKKWHF
     TPKVKVGDKV VGGDIIGEVP ETSIIVHKIM VPPGIEGEIV EIADEGEYTI EEVIAKVKTP
     SGEIKELKMY QRWPVRVKRP YKEKLPPEVP LVTGQRVIDT FFPQAKGGTA AIPGPFGSGK
     CVDGDTLILT KEFGLIKIKD LYEKLDGKGR KTVEGNEEWT ELEEPITVYG YKNGKIVEIK
     ATHVYKGASS GMIEIKTRTG RKIKVTPIHK LFTGRVTKDG LVLEEVMAMH IKPGDRIAVV
     KKIDGGEYVK LDTSSVTKIK VPEVLNEELA EFLGYVIGDG TLKPRTVAIY NNDESLLKRA
     NFLAMKLFGV SGKIVQERTV KALLIHSKYL VDFLKKLGIP GNKKARTWKV PKELLLSPPS
     VVKAFINAYI ACDGYYNKEK GEIEIVTASE EGAYGLTYLL AKLGIYATIR RKTINGREYY
     RVVISGKANL EKLGVKREAR GYTSIDVVPV DVESIYEALG RPYSELKKEG IEIHNYLSGE
     NMSYETFRKF AKVVGLEEIA ENHLQHILFD EVVEVNYISE PQEVYDITTE THNFVGGNMP
     TLLHNTVTQH QLAKWSDAQV VVYIGCGERG NEMTDVLEEF PKLKDPNTGK PLMERTVLIA
     NTSNMPVAAR EASIYTGITI AEYFRDMGYD VALMADSTSR WAEALREISG RLEEMPGEEG
     YPAYLASRLA EFYERAGRVV TLGSDYRVGS VSVIGAVSPP GGDFSEPVVQ NTLRVVKVFW
     ALDADLARRR HFPAINWLTS YSLYVDAVQD WWHKNVDPEW RRMRDKAMEL LQKEAELQEI
     VRIVGPDALP ERERAILLVA RMLREDYLQQ DAFDEVDTYC PPQKQVTMMR VLMTFYERTM
     DAISRGVPLE EIAKLPVREE IGRMKFEPDI EKIRALIDKT NEQFDELLKK YGA
 
 
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