E9D269 (DPEP1_COCPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative dipeptidase CPSG_03667
EC=3.4.13.19

Gene names

ORF Names:

CPSG_03667

Organism

Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus) [Complete proteome]

Taxonomic identifier

443226 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Onygenales › mitosporic Onygenales › Coccidioides › Coccidioides posadasii

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Hydrolyzes a wide range of dipeptides By similarity.
Catalytic activity	Hydrolysis of dipeptides.
Cofactor	Zinc By similarity.
Sequence similarities	Belongs to the peptidase M19 family.

Ontologies

Keywords
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidyl-peptidase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 34	34	Potential
	Chain	35 – 444	410	Putative dipeptidase CPSG_03667		PRO_0000411214
Sites
	Metal binding	67	1	Zinc 1; catalytic By similarity
	Metal binding	69	1	Zinc 1; catalytic By similarity
	Metal binding	178	1	Zinc 1; catalytic By similarity
	Metal binding	178	1	Zinc 2; catalytic By similarity
	Metal binding	250	1	Zinc 2; catalytic By similarity
	Metal binding	271	1	Zinc 2; catalytic By similarity
	Binding site	205	1	Substrate By similarity
	Binding site	282	1	Substrate By similarity
	Binding site	342	1	Substrate By similarity
Amino acid modifications
	Glycosylation	413	1	N-linked (GlcNAc...) Potential
	Disulfide bond	118 ↔ 207		By similarity

Sequences

	Sequence		Length	Mass (Da)
	E9D269 [UniParc]. Last modified April 5, 2011. Version 1. Checksum: D89082950FCE9BB2	FASTA	444	49,382
	10 20 30 40 50 60 MSQRTEHNGS WLRNAGSLLS VLACVAVLAS PASATPASAA AAATPRTDDY LKRAERILKF 70 80 90 100 110 120 TPLIDGHNDL PNFIRKTTKN QIYEGKIPFE DELPGHTDLK RLRKGRVGGQ FWSVYTPCPD 130 140 150 160 170 180 PPVPIDDPTW SVRDTLEQID VTKRLIEKYS RDLQFCGDAR CARRAFRRGK IASFLGIEGG 190 200 210 220 230 240 HQIGNSLGDL RRVYELGVRY ITVTHNCDNA FATAQSTVAD GLPDTGLMKP FGIEFVKEMN 250 260 270 280 290 300 RLGMLVDLSH VSANTMRDTL KVARAPVIFS HSSAYAVSNH LRNVPDDVLK EVAKNNGVVM 310 320 330 340 350 360 VTFVSRFVNV ENPDAADINT VVDHIFHIAK VAGWDHVGIG GDYDGTVYLP KGLEDVSKYP 370 380 390 400 410 420 HLIARVLERG ATTQQVRKLV GENILRVWTE VERIAKRLQK TELPNEAYWE GRNWTRPAKR 430 440 DLNADFEGRS VPLFTSASNG DFCD

References

[1]

"The genome sequence of Coccidioides posadasii strain Silveira." The Broad Institute Genome Sequencing Center for Infectious Disease Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J., Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E. , Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B. Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RMSCC 757 / Silveira.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GL636490 Genomic DNA. Translation: EFW19283.1.
3D structure databases
ProteinModelPortal	E9D269.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000180. Pept_M19_AS. IPR008257. Peptidase_M19. [Graphical view]
PANTHER	PTHR10443. PTHR10443. 1 hit.
Pfam	PF01244. Peptidase_M19. 1 hit. [Graphical view]
PROSITE	PS00869. RENAL_DIPEPTIDASE_1. 1 hit. PS51365. RENAL_DIPEPTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPEP1_COCPS

Accession

Primary (citable) accession number: E9D269

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	April 5, 2011
Last modified:	March 6, 2013
This is version 9 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program