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O14124 (DPEH1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uncharacterized dipeptidase C3A11.10c

EC=3.4.13.19
Gene names
ORF Names:SPAC3A11.10c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of dipeptides.

Cofactor

Zinc By similarity.

Subunit structure

Interacts with dil1. Ref.2

Sequence similarities

Belongs to the peptidase M19 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 Potential
Chain40 – 409370Uncharacterized dipeptidase C3A11.10c
PRO_0000314654

Sites

Metal binding671Zinc 1; catalytic By similarity
Metal binding691Zinc 1; catalytic By similarity
Metal binding1811Zinc 1; catalytic By similarity
Metal binding1811Zinc 2; catalytic By similarity
Metal binding2501Zinc 2; catalytic By similarity
Metal binding2711Zinc 2; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
O14124 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 860A95056C6B1CF1

FASTA40946,048
        10         20         30         40         50         60 
MVSDSKLELP LPVNQQKPRR RRILKVHLLI AALILSAVGY LGKGKWIWTP ERKAHFVLTH 

        70         80         90        100        110        120 
FPLIDGHNDL PIYLRENYDN RLLNISLEHL PGQTDIFRLR QGHVGGQFWS VFVECPSLDS 

       130        140        150        160        170        180 
NSSLSWNRTG EYEAVTQTLQ QIDVVKRMAL YYPKTFSLTD HSGKVKFDFL RNHISSMMGI 

       190        200        210        220        230        240 
EGLHQIAGSP SILRQFYDLG VRYATLAHNC DNVFADAAVD GKRTNKGLSP AGRDIVREMN 

       250        260        270        280        290        300 
RLGMIVDLSH TTPETMHQAL DVSVAPAFFS HSSAKGVYDH PRNVPDDVLI RVKETDGVVM 

       310        320        330        340        350        360 
VNFYPAFISP HPENATIDTV VEHIMHIANV TGSYRHIGLG GDFDGIDMVP KGLEDVSKYP 

       370        380        390        400 
DLFVKLAERG LSITELADIA GRNVLRVWKT TEDLGHSIHE PPLEWEDDF 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"High-throughput knockout screen in Schizosaccharomyces pombe identifies a novel gene required for efficient homolog disjunction during meiosis I."
Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A., Kovacikova I., Miadokova E., Ammerer G., Gregan J.
Cell Cycle 9:1802-1808(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DIL1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB16385.1.
PIRT11632.
RefSeqNP_594193.1. NM_001019617.2.

3D structure databases

ProteinModelPortalO14124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279513. 25 interactions.
MINTMINT-4670686.
STRING4896.SPAC3A11.10c-1.

Proteomic databases

MaxQBO14124.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC3A11.10c.1; SPAC3A11.10c.1:pep; SPAC3A11.10c.
GeneID2543080.
KEGGspo:SPAC3A11.10c.

Organism-specific databases

PomBaseSPAC3A11.10c.

Phylogenomic databases

eggNOGCOG2355.
HOGENOMHOG000072016.
KOK01273.
OMALGAQFWV.
OrthoDBEOG7XM371.
PhylomeDBO14124.

Family and domain databases

InterProIPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PfamPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEPS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804108.

Entry information

Entry nameDPEH1_SCHPO
AccessionPrimary (citable) accession number: O14124
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Peptidase families

Classification of peptidase families and list of entries