P17255 (VATA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1071 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Hydrogen ion transport Intron homing Ion transport Transport
Cellular component	Membrane Vacuole
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Acetylation Autocatalytic cleavage Phosphoprotein Protein splicing
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro 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_component	endomembrane 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_function	ATP 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 proton-transporting ATPase activity, rotational mechanism Traceable author statement PubMed 10224039PubMed 9442887. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAV1	P47104	2	EBI-20245,EBI-25471

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6 Ref.7

Chain

2 – 283

282

V-type proton ATPase catalytic subunit A, 1st part

PRO_0000002458

Chain

284 – 737

454

Endonuclease PI-SceI

PRO_0000002459

Chain

738 – 1071

334

V-type proton ATPase catalytic subunit A, 2nd part

PRO_0000002460

Regions

Domain

494 – 642

149

DOD-type homing endonuclease

Nucleotide binding

257 – 264

8

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

16

1

Phosphoserine Ref.19

Modified residue

131

1

Phosphothreonine Ref.17 Ref.19

Modified residue

166

1

Phosphoserine Ref.18

Modified residue

376

1

Phosphoserine Ref.18

Modified residue

448

1

Phosphoserine Ref.19

Modified residue

771

1

Phosphothreonine Ref.19

Modified residue

777

1

Phosphoserine Ref.19

Modified residue

845

1

Phosphoserine Ref.19

Modified residue

858

1

Phosphoserine Ref.19

Modified residue

928

1

Phosphoserine Ref.19

Experimental info

Mutagenesis

284

1

C → 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

Mutagenesis

362

1

H → N: Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSS VDE. Ref.7

Mutagenesis

737

1

N → S: Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSS VDE. Ref.7 Ref.22

Mutagenesis

738

1

C → 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 conflict

875

1

G → D in AAB63978. Ref.8

Secondary structure

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1071

Helix Strand Turn

Details...

Beta strand

290 – 293

4

Beta strand

298 – 300

3

Helix

301 – 303

3

Beta strand

309 – 312

4

Beta strand

315 – 322

8

Beta strand

325 – 335

11

Beta strand

343 – 345

3

Beta strand

347 – 349

3

Beta strand

355 – 359

5

Beta strand

363 – 369

7

Beta strand

372 – 379

8

Beta strand

382 – 396

15

Beta strand

398 – 400

3

Beta strand

402 – 414

13

Helix

415 – 417

3

Helix

420 – 431

12

Beta strand

434 – 443

10

Helix

444 – 449

6

Helix

452 – 457

6

Beta strand

459 – 462

4

Turn

471 – 474

4

Beta strand

479 – 481

3

Beta strand

485 – 487

3

Helix

488 – 501

14

Beta strand

506 – 514

9

Helix

516 – 528

13

Beta strand

531 – 533

3

Beta strand

534 – 537

4

Turn

541 – 543

3

Beta strand

544 – 548

5

Turn

556 – 559

4

Helix

570 – 575

6

Beta strand

579 – 584

6

Helix

588 – 591

4

Helix

595 – 609

15

Beta strand

610 – 613

4

Beta strand

619 – 625

7

Helix

627 – 639

13

Beta strand

643 – 650

8

Helix

654 – 656

3

Beta strand

657 – 659

3

Beta strand

661 – 669

9

Helix

672 – 678

7

Turn

684 – 686

3

Helix

693 – 695

3

Beta strand

700 – 702

3

Beta strand

704 – 719

16

Beta strand

721 – 723

3

Beta strand

727 – 729

3

Beta strand

733 – 735

3

Sequences

	Sequence		Length	Mass (Da)
	P17255 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2A4C65D2F59426FD	FASTA	1,071	118,637
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, 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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, MASS SPECTROMETRY. Strain: YAL6B.
[18]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-376, MASS SPECTROMETRY.
[19]	"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 SER-16; THR-131; SER-448; THR-771; SER-777; SER-845; SER-858 AND SER-928, MASS SPECTROMETRY.
[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.

Web resources

Description of Sce VMA in Inbase

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.

PIR

PXBYVA. A35746.

RefSeq

NP_010096.1. NM_001180245.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DFA	X-ray	2.00	A	284-737	[»]
1EF0	X-ray	2.10	A/B	285-741	[»]
1GPP	X-ray	1.35	A	284-736	[»]
1JVA	X-ray	2.10	A/B	274-747	[»]
1LWS	X-ray	3.50	A	284-737	[»]
1LWT	X-ray	3.20	A	284-737	[»]
1UM2	X-ray	2.90	A/B	285-737	[»]
			C/D	274-747	[»]
1VDE	X-ray	2.40	A/B	284-737	[»]

ProteinModelPortal

P17255.

SMR

P17255. Positions 46-1058.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2293N.

IntAct

P17255. 84 interactions.

MINT

MINT-641889.

Protein family/group databases

MEROPS

N09.001.

REBASE

2615. PI-SceI.

TCDB

3.A.2.2.3. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

2D gel databases

UCD-2DPAGE

P17255.

Proteomic databases

PaxDb

P17255.

PeptideAtlas

P17255.

PRIDE

P17255.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDL185W; YDL185W; YDL185W.

GeneID

851342.

KEGG

sce:YDL185W.

Organism-specific databases

SGD

S000002344. VMA1.

Phylogenomic databases

eggNOG

COG1372.

GeneTree

ENSGT00550000074787.

HOGENOM

HOG000141780.

KO

K02145.

OMA

VHNCGER.

OrthoDB

EOG4PP1R4.

Enzyme and pathway databases

BioCyc

YEAST:G3O-29571-MONOMER.

Gene expression databases

ArrayExpress

P17255.

Genevestigator

P17255.

GermOnline

YDL185W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.1140.10. 1 hit.
3.10.28.10. 1 hit.

InterPro

IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_a/bsu_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1_bsu/V1_C.
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]

Pfam

PF00006. 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]

PRINTS

PR00379. INTEIN.

SMART

SM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]

SUPFAM

SSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF55608. SSF55608. 2 hits.

PROSITE

PS00152. ATPASE_ALPHA_BETA. 1 hit.
PS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P17255.

NextBio

968420.

PMAP-CutDB

P17255.

Entry information

Entry name

VATA_YEAST

Accession

Primary (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:	May 29, 2013
This is version 171 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program