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Protein

Uncharacterized dipeptidase C965.12

Gene

SPCC965.12

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Hydrolysis of dipeptides.PROSITE-ProRule annotation

Cofactori

Zn2+PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi31 – 311Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi144 – 1441Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi144 – 1441Zinc 2; catalyticPROSITE-ProRule annotation
Metal bindingi215 – 2151Zinc 2; catalyticPROSITE-ProRule annotation
Metal bindingi236 – 2361Zinc 2; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_273042. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_346894. Aflatoxin activation and detoxification.

Names & Taxonomyi

Protein namesi
Recommended name:
Uncharacterized dipeptidase C965.12 (EC:3.4.13.19)
Gene namesi
ORF Names:SPCC965.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC965.12.
PomBaseiSPCC965.12.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Uncharacterized dipeptidase C965.12PRO_0000314655Add
BLAST

Proteomic databases

MaxQBiO59832.

Interactioni

Protein-protein interaction databases

MINTiMINT-4676557.
STRINGi4896.SPCC965.12.1.

Structurei

3D structure databases

ProteinModelPortaliO59832.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
InParanoidiO59832.
KOiK01273.
OMAiFYQAGVR.
OrthoDBiEOG7XM371.
PhylomeDBiO59832.

Family and domain databases

InterProiIPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59832-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVDLREEKE LAQQRFKEIC KHAKIVDTHN DFPYLLRVQL RNKLQLAEFD
60 70 80 90 100
FENGLTSHTD LVKMRQGQVG VQFFSCFIEC KNPNYLYQDF DTPTTVVRDT
110 120 130 140 150
LEQIDVTRRL VCKYNNDLKF VDCADDAIAA FRNNGKIAIA LGVEGLHQVD
160 170 180 190 200
TSLAVLRQYY SLGVRYITLT HNCDNPFATA ASSITGGLPD RGLSAYGIEC
210 220 230 240 250
IFEMNRLGMM VDLSHVSHRT MHDALDVTKA PVIFSHSSAY TLTEHERNVR
260 270 280 290 300
DDVLERLKTN GGVVQVNFYQ DFIRKPGSDR ATIDDAADHI LHIIKVAGWE
310 320 330 340 350
HVGLGSDFDG IPQGPKGLED VSKYPDLICK IIERTNATNE QIEGLMGLNV
360 370 380 390 400
LRVWKKTELV ALQLSKKLEP IESSWSGRKW EFYSYAKEFP ELFPDAYKLN
410
EKSTVWNYDQ PLNIEK
Length:416
Mass (Da):47,421
Last modified:August 1, 1998 - v1
Checksum:i8EB843F4C662D625
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA19072.1.
RefSeqiNP_588522.1. NM_001023511.2.

Genome annotation databases

EnsemblFungiiSPCC965.12.1; SPCC965.12.1:pep; SPCC965.12.
GeneIDi2539107.
KEGGispo:SPCC965.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA19072.1.
RefSeqiNP_588522.1. NM_001023511.2.

3D structure databases

ProteinModelPortaliO59832.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4676557.
STRINGi4896.SPCC965.12.1.

Proteomic databases

MaxQBiO59832.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC965.12.1; SPCC965.12.1:pep; SPCC965.12.
GeneIDi2539107.
KEGGispo:SPCC965.12.

Organism-specific databases

EuPathDBiFungiDB:SPCC965.12.
PomBaseiSPCC965.12.

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
InParanoidiO59832.
KOiK01273.
OMAiFYQAGVR.
OrthoDBiEOG7XM371.
PhylomeDBiO59832.

Enzyme and pathway databases

ReactomeiREACT_273042. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_346894. Aflatoxin activation and detoxification.

Miscellaneous databases

NextBioi20800279.
PROiO59832.

Family and domain databases

InterProiIPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiDPEH2_SCHPO
AccessioniPrimary (citable) accession number: O59832
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 1, 1998
Last modified: June 24, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.