C7ZIE1 (DPEP2_NECH7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative dipeptidase NECHADRAFT_87110
EC=3.4.13.19

Gene names

ORF Names:

NECHADRAFT_87110

Organism

Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) (Fusarium solani subsp. pisi) [Reference proteome]

Taxonomic identifier

660122 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Nectria › Nectria haematococca complex › Nectria haematococca › Fusarium solani subsp. pisi

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
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.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the peptidase M19 family.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane 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
	Chain	1 – 482	482	Putative dipeptidase NECHADRAFT_87110		PRO_0000411218
Regions
	Transmembrane	41 – 61	21	Helical; Potential
Sites
	Metal binding	90	1	Zinc 1; catalytic By similarity
	Metal binding	92	1	Zinc 1; catalytic By similarity
	Metal binding	201	1	Zinc 1; catalytic By similarity
	Metal binding	201	1	Zinc 2; catalytic By similarity
	Metal binding	272	1	Zinc 2; catalytic By similarity
	Metal binding	293	1	Zinc 2; catalytic By similarity
	Binding site	228	1	Substrate By similarity
	Binding site	304	1	Substrate By similarity
	Binding site	364	1	Substrate By similarity
Amino acid modifications
	Glycosylation	18	1	N-linked (GlcNAc...) Potential
	Disulfide bond	141 ↔ 230		By similarity

Sequences

	Sequence		Length	Mass (Da)
	C7ZIE1 [UniParc]. Last modified October 13, 2009. Version 1. Checksum: 3D8CB979589319B5	FASTA	482	54,050
	10 20 30 40 50 60 MADTQTPNLQ NTAEGDANTS AENERSLTVR ANHQSQNTRS WLRYPFLVAG IALFLGPFSF 70 80 90 100 110 120 FWPREGPIDS KDYVERTKRV LKTTPLIDGH NDLPWQLRIE LHNRIYDGRV DLSKKLLGHT 130 140 150 160 170 180 DIQRMRQGMV GGQFWSVYVD CDTQQQHFED PSWVVRDTLE QIDVTRRFVN EHPEHLQYCD 190 200 210 220 230 240 TPACAREAFK SGRISSMIGI EGGHQVGGSI GAIRQMFNLG ARYITLTHNC DNAFGTSAST 250 260 270 280 290 300 VAAGGADQGL FKLGYDAVKE MNRLGMMVDL SHVSHQTMRD VLGVTRAPVI FSHSGAYAVE 310 320 330 340 350 360 PHLRHAPDDV LRLVKQNGGI VMAVFVNRFL NMKNPDQATI HDVVDHILHI AEVCGWECVG 370 380 390 400 410 420 IGSDFSGTPF VPVGLEDVSK FPDLIQLLME RGATDQQIRL LAGENILRVW GKIEQRAKEL 430 440 450 460 470 480 QAGGEKPIEA EYEGRNWHKG MKNSPWMLRR SRDEALVNGA ADQPFMFNVD SEGKHNPVVK QV

References

[1]

"The genome of Nectria haematococca: contribution of supernumerary chromosomes to gene expansion." Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C., Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C., Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M., Nelson D.R., Straney D. , Napoli C.A., Barker B.M., Gribskov M., Rep M., Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L., Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E., Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E., VanEtten H.D. PLoS Genet. 5:E1000618-E1000618(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GG698930 Genomic DNA. Translation: EEU36188.1.
RefSeq	XP_003041901.1. XM_003041855.1.
3D structure databases
ProteinModelPortal	C7ZIE1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	NechaT87110; NechaP87110; NechaG87110.
GeneID	9674281.
KEGG	nhe:NECHADRAFT_87110.
Phylogenomic databases
KO	K01273.
OrthoDB	EOG4T7CBW.
Family and domain databases
InterPro	IPR008257. Peptidase_M19. [Graphical view]
PANTHER	PTHR10443. PTHR10443. 1 hit.
Pfam	PF01244. Peptidase_M19. 1 hit. [Graphical view]
PROSITE	PS00869. RENAL_DIPEPTIDASE_1. False negative. PS51365. RENAL_DIPEPTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPEP2_NECH7

Accession

Primary (citable) accession number: C7ZIE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	October 13, 2009
Last modified:	October 3, 2012
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program