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Protein

Probable dipeptidyl peptidase 3

Gene

YOL057W

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi460 – 4601Zinc; catalyticBy similarity
Active sitei461 – 4611By similarity
Metal bindingi465 – 4651Zinc; catalyticBy similarity
Metal bindingi517 – 5171Zinc; catalyticBy similarity

GO - Molecular functioni

  • dipeptidyl-peptidase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • metallopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  • proteolysis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33468-MONOMER.
BRENDAi3.4.14.4. 984.

Protein family/group databases

MEROPSiM49.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable dipeptidyl peptidase 3 (EC:3.4.14.4)
Alternative name(s):
Dipeptidyl aminopeptidase III
Dipeptidyl arylamidase III
Dipeptidyl peptidase III
Short name:
DPP III
Gene namesi
Ordered Locus Names:YOL057W
ORF Names:O1232
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL057W.
SGDiS000005418. YOL057W.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 711711Probable dipeptidyl peptidase 3PRO_0000078243Add
BLAST

Proteomic databases

MaxQBiQ08225.

Interactioni

Protein-protein interaction databases

BioGridi34344. 11 interactions.
MINTiMINT-624789.

Structurei

Secondary structure

1
711
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 143Combined sources
Turni18 – 214Combined sources
Helixi22 – 243Combined sources
Helixi27 – 4115Combined sources
Helixi44 – 518Combined sources
Helixi55 – 6814Combined sources
Turni69 – 713Combined sources
Helixi78 – 9720Combined sources
Beta strandi99 – 1013Combined sources
Turni103 – 1053Combined sources
Helixi115 – 12410Combined sources
Helixi133 – 1364Combined sources
Helixi143 – 1453Combined sources
Helixi148 – 1503Combined sources
Helixi154 – 1596Combined sources
Turni160 – 1634Combined sources
Turni167 – 1704Combined sources
Beta strandi171 – 1733Combined sources
Helixi175 – 1773Combined sources
Beta strandi184 – 1874Combined sources
Helixi191 – 20010Combined sources
Helixi202 – 2054Combined sources
Beta strandi212 – 2187Combined sources
Beta strandi221 – 2277Combined sources
Turni236 – 2383Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi252 – 2598Combined sources
Helixi261 – 27515Combined sources
Helixi281 – 29616Combined sources
Helixi299 – 31012Combined sources
Beta strandi316 – 32510Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi336 – 3438Combined sources
Helixi346 – 35712Combined sources
Helixi359 – 3657Combined sources
Beta strandi366 – 3683Combined sources
Helixi370 – 3723Combined sources
Beta strandi384 – 39310Combined sources
Beta strandi397 – 4015Combined sources
Helixi405 – 4106Combined sources
Beta strandi414 – 4185Combined sources
Helixi419 – 4279Combined sources
Turni439 – 4413Combined sources
Helixi442 – 46625Combined sources
Beta strandi472 – 4743Combined sources
Beta strandi477 – 4804Combined sources
Beta strandi482 – 4843Combined sources
Beta strandi491 – 4933Combined sources
Helixi504 – 5085Combined sources
Helixi509 – 5113Combined sources
Helixi512 – 52716Combined sources
Helixi531 – 5366Combined sources
Helixi542 – 56221Combined sources
Helixi563 – 5664Combined sources
Turni569 – 5713Combined sources
Helixi577 – 59115Combined sources
Beta strandi592 – 5954Combined sources
Beta strandi598 – 6036Combined sources
Beta strandi610 – 6145Combined sources
Helixi616 – 6183Combined sources
Turni619 – 6213Combined sources
Helixi622 – 63918Combined sources
Helixi643 – 65311Combined sources
Helixi658 – 6614Combined sources
Helixi664 – 6696Combined sources
Beta strandi676 – 6783Combined sources
Beta strandi681 – 6844Combined sources
Beta strandi690 – 6934Combined sources
Helixi699 – 71012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CSKX-ray1.95A1-711[»]
ProteinModelPortaliQ08225.
SMRiQ08225. Positions 2-711.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08225.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M49 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000007335.
HOGENOMiHOG000187784.
InParanoidiQ08225.
KOiK01277.
OMAiGEWEGFA.
OrthoDBiEOG7SJDCW.

Family and domain databases

InterProiIPR005317. Dipeptidyl-peptase3.
[Graphical view]
PIRSFiPIRSF007828. Dipeptidyl-peptidase_III. 1 hit.

Sequencei

Sequence statusi: Complete.

Q08225-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHFFADHDA PLSMLSVKTE YFPQLTDKEQ KYAHFMSKAS HAGSRVVMRQ
60 70 80 90 100
VSHESEPIFD LILAIHSKLN GKYPEDDITQ KQQTGLYLEY VSQFLSNLGN
110 120 130 140 150
FKSFGDTKFI PRCEVKFFKQ LLELAKINPC SSPLTLSPVD VNHEFTSHHL
160 170 180 190 200
FSTINELIDI GIYHVEEKAA LLGFPSQGYT SAYYLGLPVT PEDMALLKEQ
210 220 230 240 250
LFAELAILPE NTRINKVGEN SFQIWVASEN VKNQITETYP SGQITLSNAV
260 270 280 290 300
TKVEFIFGDH SREMRLVASY LKEAQKFAAN DTQKAMLQEY INHFVTGSSQ
310 320 330 340 350
AHKEAQKLWV KDISPVIETN IGFIETYREP SGIIGEFESL VAIQNKERTA
360 370 380 390 400
KFSSLVNNAE EFISLLPWSK DYEKPIFNPP DFTSLEVLTF TGSGIPAGIN
410 420 430 440 450
IPNYDDVRLK IGFKNVSLGN ILSAAAKSSS KHPPSFISQE DRPIFEKYQS
460 470 480 490 500
DSFEVQVGIH ELLGHGSGKL LTEFTDGFNF DKENPPLGLD GKPVSTYYKV
510 520 530 540 550
GETWGSKFGQ LAGPFEECRA EVIAMFLLTN KKILDIFGFH DVESQDKVIY
560 570 580 590 600
AGYLQMARAG LLALEYWNPK TGKWGQPHMQ ARFSIMKTFM KHSTDKNFLK
610 620 630 640 650
LEMNSTNDDF AIKLDKSLIK TAGHECVKDY LKHLHVYKCS GDVEQGSKYF
660 670 680 690 700
IDRSTVTPDL ASLRDIVLSK RLPRRQFIQS NSYIDDNNKV TLKEYDETPQ
710
GMLQSFLDRE L
Length:711
Mass (Da):80,510
Last modified:November 1, 1996 - v1
Checksum:iC8FEBD32834FA683
GO

Sequence cautioni

The sequence CAA62529.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91067 Genomic DNA. Translation: CAA62529.1. Different initiation.
Z74798 Genomic DNA. Translation: CAA99065.1.
Z74799 Genomic DNA. Translation: CAA99066.1.
BK006948 Genomic DNA. Translation: DAA10726.1.
PIRiS66749.
RefSeqiNP_014584.1. NM_001183312.1.

Genome annotation databases

EnsemblFungiiYOL057W; YOL057W; YOL057W.
GeneIDi854097.
KEGGisce:YOL057W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91067 Genomic DNA. Translation: CAA62529.1. Different initiation.
Z74798 Genomic DNA. Translation: CAA99065.1.
Z74799 Genomic DNA. Translation: CAA99066.1.
BK006948 Genomic DNA. Translation: DAA10726.1.
PIRiS66749.
RefSeqiNP_014584.1. NM_001183312.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CSKX-ray1.95A1-711[»]
ProteinModelPortaliQ08225.
SMRiQ08225. Positions 2-711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34344. 11 interactions.
MINTiMINT-624789.

Protein family/group databases

MEROPSiM49.004.

Proteomic databases

MaxQBiQ08225.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL057W; YOL057W; YOL057W.
GeneIDi854097.
KEGGisce:YOL057W.

Organism-specific databases

EuPathDBiFungiDB:YOL057W.
SGDiS000005418. YOL057W.

Phylogenomic databases

GeneTreeiENSGT00390000007335.
HOGENOMiHOG000187784.
InParanoidiQ08225.
KOiK01277.
OMAiGEWEGFA.
OrthoDBiEOG7SJDCW.

Enzyme and pathway databases

BioCyciYEAST:G3O-33468-MONOMER.
BRENDAi3.4.14.4. 984.

Miscellaneous databases

EvolutionaryTraceiQ08225.
PROiQ08225.

Family and domain databases

InterProiIPR005317. Dipeptidyl-peptase3.
[Graphical view]
PIRSFiPIRSF007828. Dipeptidyl-peptidase_III. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of a 26 kb region on the left arm of yeast chromosome XV."
    Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
    Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90843 / S288c / FY73.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDPP3_YEAST
AccessioniPrimary (citable) accession number: Q08225
Secondary accession number(s): O94146, Q05663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3260 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.