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P17255 (VATA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 182. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V-type proton ATPase catalytic subunit A

Short name=V-ATPase subunit A
EC=3.6.3.14
Alternative name(s):
Vacuolar proton pump subunit A

Cleaved into the following chain:

  1. Endonuclease PI-SceI
    EC=3.1.-.-
    Alternative name(s):
    Sce VMA intein
    VMA1-derived endonuclease
    Short name=VDE
Gene names
Name:VMA1
Synonyms:CLS8, TFP1
Ordered Locus Names:YDL185W
ORF Names:D1286
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1071 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca2+ homeostasis. This is a catalytic subunit. Ref.12

PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it. Ref.12

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Subunit structure

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase. Ref.1 Ref.13

Subcellular location

Endomembrane system. Vacuole membrane Probable. Note: Membranes of various intracellular acidic compartments. Ref.14

Post-translational modification

This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.

Miscellaneous

Present with 199895 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Contains 1 DOD-type homing endonuclease domain.

Ontologies

Keywords
   Biological processHydrogen ion transport
Intron homing
Ion transport
Transport
   Cellular componentMembrane
Vacuole
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMAcetylation
Autocatalytic cleavage
Phosphoprotein
Protein splicing
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

DNA catabolic process, endonucleolytic

Traceable author statement Ref.12. Source: GOC

cellular protein metabolic process

Inferred from direct assay Ref.11. Source: SGD

intein-mediated protein splicing

Inferred from electronic annotation. Source: InterPro

intron homing

Traceable author statement Ref.12. Source: SGD

vacuolar acidification

Inferred from mutant phenotype PubMed 18048916. Source: SGD

   Cellular_componentendomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

fungal-type vacuole membrane

Inferred from direct assay PubMed 18632794. Source: UniProtKB

vacuolar proton-transporting V-type ATPase, V1 domain

Traceable author statement PubMed 10224039PubMed 9442887. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

endodeoxyribonuclease activity

Traceable author statement Ref.12. Source: SGD

protein binding

Inferred from physical interaction Ref.13PubMed 19289121. Source: IntAct

proton-transporting ATPase activity, rotational mechanism

Traceable author statement PubMed 10224039PubMed 9442887. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAV1P471042EBI-20245,EBI-25471
VMA6P323662EBI-20245,EBI-20201

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7
Chain2 – 283282V-type proton ATPase catalytic subunit A, 1st part
PRO_0000002458
Chain284 – 737454Endonuclease PI-SceI
PRO_0000002459
Chain738 – 1071334V-type proton ATPase catalytic subunit A, 2nd part
PRO_0000002460

Regions

Domain494 – 642149DOD-type homing endonuclease
Nucleotide binding257 – 2648ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.19
Modified residue1311Phosphothreonine Ref.17
Modified residue8581Phosphoserine Ref.17
Modified residue9281Phosphoserine Ref.17

Experimental info

Mutagenesis2841C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with N-362; S-737 and S-738 in X10SSS VDE. Ref.7 Ref.10 Ref.22
Mutagenesis3621H → N: Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSS VDE. Ref.7
Mutagenesis7371N → S: Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSS VDE. Ref.7 Ref.22
Mutagenesis7381C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with S-284; N-362 and S-737 in X10SSS VDE. Ref.7 Ref.10
Sequence conflict8751G → D in AAB63978. Ref.8

Secondary structure

............................................................................................. 1071
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17255 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2A4C65D2F59426FD

FASTA1,071118,637
        10         20         30         40         50         60 
MAGAIENARK EIKRISLEDH AESEYGAIYS VSGPVVIAEN MIGCAMYELV KVGHDNLVGE 

        70         80         90        100        110        120 
VIRIDGDKAT IQVYEETAGL TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKEES 

       130        140        150        160        170        180 
QSIYIPRGID TPALDRTIKW QFTPGKFQVG DHISGGDIYG SVFENSLISS HKILLPPRSR 

       190        200        210        220        230        240 
GTITWIAPAG EYTLDEKILE VEFDGKKSDF TLYHTWPVRV PRPVTEKLSA DYPLLTGQRV 

       250        260        270        280        290        300 
LDALFPCVQG GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCFAKGTN VLMADGSIEC 

       310        320        330        340        350        360 
IENIEVGNKV MGKDGRPREV IKLPRGRETM YSVVQKSQHR AHKSDSSREV PELLKFTCNA 

       370        380        390        400        410        420 
THELVVRTPR SVRRLSRTIK GVEYFEVITF EMGQKKAPDG RIVELVKEVS KSYPISEGPE 

       430        440        450        460        470        480 
RANELVESYR KASNKAYFEW TIEARDLSLL GSHVRKATYQ TYAPILYEND HFFDYMQKSK 

       490        500        510        520        530        540 
FHLTIEGPKV LAYLLGLWIG DGLSDRATFS VDSRDTSLME RVTEYAEKLN LCAEYKDRKE 

       550        560        570        580        590        600 
PQVAKTVNLY SKVVRGNGIR NNLNTENPLW DAIVGLGFLK DGVKNIPSFL STDNIGTRET 

       610        620        630        640        650        660 
FLAGLIDSDG YVTDEHGIKA TIKTIHTSVR DGLVSLARSL GLVVSVNAEP AKVDMNGTKH 

       670        680        690        700        710        720 
KISYAIYMSG GDVLLNVLSK CAGSKKFRPA PAAAFARECR GFYFELQELK EDDYYGITLS 

       730        740        750        760        770        780 
DDSDHQFLLA NQVVVHNCGE RGNEMAEVLM EFPELYTEMS GTKEPIMKRT TLVANTSNMP 

       790        800        810        820        830        840 
VAAREASIYT GITLAEYFRD QGKNVSMIAD SSSRWAEALR EISGRLGEMP ADQGFPAYLG 

       850        860        870        880        890        900 
AKLASFYERA GKAVALGSPD RTGSVSIVAA VSPAGGDFSD PVTTATLGIT QVFWGLDKKL 

       910        920        930        940        950        960 
AQRKHFPSIN TSVSYSKYTN VLNKFYDSNY PEFPVLRDRM KEILSNAEEL EQVVQLVGKS 

       970        980        990       1000       1010       1020 
ALSDSDKITL DVATLIKEDF LQQNGYSTYD AFCPIWKTFD MMRAFISYHD EAQKAVANGA 

      1030       1040       1050       1060       1070 
NWSKLADSTG DVKHAVSSSK FFEPSRGEKE VHGEFEKLLS TMQERFAEST D 

« Hide

References

« Hide 'large scale' references
[1]"Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae."
Hirata R., Ohsumi Y., Nakano A., Kawasaki H., Suzuki K., Anraku Y.
J. Biol. Chem. 265:6726-6733(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 181-196; 815-820; 826-836; 862-879; 925-936 AND 1004-1013, SUBUNIT.
Strain: ATCC 26786 / X2180-1A.
[2]"New open reading frames, one of which is similar to the nifV gene of Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of Saccharomyces cerevisiae."
Verhasselt P., Voet M., Volckaert G.
Yeast 11:961-966(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis."
Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.
Mol. Cell. Biol. 11:4876-4884(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
Strain: ATCC 208353 / W303-1A.
[6]Bienvenut W.V., Peters C.
Submitted (OCT-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-10; 52-63; 115-136; 173-178; 181-207; 220-239; 264-272; 770-784; 804-814; 826-842; 853-861; 918-937; 940-959; 1004-1014 AND 1058-1065, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides."
Mizutani R., Nogami S., Kawasaki M., Ohya Y., Anraku Y., Satow Y.
J. Mol. Biol. 316:919-929(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-6, CLEAVAGE OF INITIATOR METHIONINE, MUTAGENESIS OF CYS-284; HIS-362; ASN-737 AND CYS-738, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 274-747.
[8]"A dominant trifluoperazine resistance gene from Saccharomyces cerevisiae has homology with F0F1 ATP synthase and confers calcium-sensitive growth."
Shih C.K., Wagner R., Feinstein S., Kanik-Ennulat C., Neff N.
Mol. Cell. Biol. 8:3094-3103(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-1071.
[9]"Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase."
Kane P.M., Yamashiro C.T., Wolczyk D.F., Neff N., Goebl M., Stevens T.H.
Science 250:651-657(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SPLICING.
[10]"Mutations at the putative junction sites of the yeast VMA1 protein, the catalytic subunit of the vacuolar membrane H(+)-ATPase, inhibit its processing by protein splicing."
Hirata R., Anraku Y.
Biochem. Biophys. Res. Commun. 188:40-47(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-284 AND CYS-738.
[11]"Protein splicing of the yeast TFP1 intervening protein sequence: a model for self-excision."
Cooper A.A., Chen Y.-J., Lindorfer M.A., Stevens T.H.
EMBO J. 12:2575-2583(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-SPLICING MECHANISM.
[12]"Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae."
Gimble F.S., Thorner J.
Nature 357:301-306(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF VDE.
[13]"Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."
Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.
Nat. Cell Biol. 3:384-391(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAV1 AND RAV2.
[14]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[15]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[16]"Homing in on an endosymbiotic endonuclease."
Grivell L.A.
Curr. Biol. 2:450-452(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[17]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131; SER-858 AND SER-928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity."
Duan X., Gimble F.S., Quiocho F.A.
Cell 89:555-564(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PI-SCE I.
[21]"Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking."
Hu D., Crist M., Duan X., Quiocho F.A., Gimble F.S.
J. Biol. Chem. 275:2705-2712(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PI-SCE I.
[22]"Structural insights into the protein splicing mechanism of PI-SceI."
Poland B.W., Xu M.-Q., Quiocho F.A.
J. Biol. Chem. 275:16408-16413(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 283-741, MUTAGENESIS OF CYS-284 AND ASN-737.
[23]"High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI."
Werner E., Wende W., Pingoud A., Heinemann U.
Nucleic Acids Res. 30:3962-3971(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 284-465.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05409 Genomic DNA. Translation: AAA34664.1.
X83276 Genomic DNA. Translation: CAA58261.1.
Z74233 Genomic DNA. Translation: CAA98760.1.
Z74233 Genomic DNA. Translation: CAA98761.1. Sequence problems.
Z74233 Genomic DNA. Translation: CAA98762.1.
X58857 Genomic DNA. Translation: CAA41657.1.
M21609 Genomic DNA. Translation: AAB63978.1.
BK006938 Genomic DNA. Translation: DAA11677.1.
PIRPXBYVA. A35746.
RefSeqNP_010096.1. NM_001180245.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DFAX-ray2.00A284-737[»]
1EF0X-ray2.10A/B283-741[»]
1GPPX-ray1.35A284-736[»]
1JVAX-ray2.10A/B274-747[»]
1LWSX-ray3.50A284-737[»]
1LWTX-ray3.20A284-737[»]
1UM2X-ray2.90A/B284-737[»]
C/D274-747[»]
1VDEX-ray2.40A/B284-737[»]
ProteinModelPortalP17255.
SMRP17255. Positions 46-1063.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31859. 371 interactions.
DIPDIP-2293N.
IntActP17255. 71 interactions.
MINTMINT-641889.

Protein family/group databases

MEROPSN09.001.
REBASE2615. PI-SceI.
TCDB3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

UCD-2DPAGEP17255.

Proteomic databases

MaxQBP17255.
PaxDbP17255.
PeptideAtlasP17255.
PRIDEP17255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL185W; YDL185W; YDL185W.
GeneID851342.
KEGGsce:YDL185W.

Organism-specific databases

SGDS000002344. VMA1.

Phylogenomic databases

eggNOGCOG1372.
GeneTreeENSGT00550000074787.
HOGENOMHOG000141780.
KOK02145.
OMAVHNCGER.
OrthoDBEOG7M98QZ.

Enzyme and pathway databases

BioCycYEAST:G3O-29571-MONOMER.

Gene expression databases

GenevestigatorP17255.

Family and domain databases

Gene3D1.10.1140.10. 1 hit.
2.170.16.10. 1 hit.
3.10.28.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR028992. Hedgehog/Intein_dom.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR007868. Hom_end_hint.
IPR007869. Homing_endonuc_PI-Sce.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR004042. Intein_endonuc.
IPR006141. Intein_splice_site.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
PF05204. Hom_end. 2 hits.
PF05203. Hom_end_hint. 1 hit.
[Graphical view]
PRINTSPR00379. INTEIN.
SMARTSM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF51294. SSF51294. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF55608. SSF55608. 2 hits.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
PS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17255.
NextBio968420.
PMAP-CutDBP17255.
PROP17255.

Entry information

Entry nameVATA_YEAST
AccessionPrimary (citable) accession number: P17255
Secondary accession number(s): D6VRG7, O74301, Q9Y7W5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 182 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Intein-containing proteins

List of intein-containing protein entries