Q9Y8E3

PR
Gene name
AO090011000795-A
Protein name
Dipeptidyl-peptidase 5
Names
Alanyl dipeptidyl peptidase, Dipeptidyl-peptidase V, DPP V, DppV
Species
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
KEGG Pathway
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-74 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9Y8E3

Entry ID Method Resolution Chain Position Source
AF-Q9Y8E3-F1 Predicted AlphaFoldDB

No variants for Q9Y8E3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9Y8E3

No associated diseases with Q9Y8E3

2 regional properties for Q9Y8E3

Type Name Position InterPro Accession
domain Peptidase S9, prolyl oligopeptidase, catalytic domain 491 - 702 IPR001375
repeat WD40-like beta propeller 292 - 308 IPR011659

Functions

Description
EC Number
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

1 GO annotations of molecular function

Name Definition
serine-type peptidase activity Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGALRWLSIA ATASTALALN PEGLISAPRR SEAIPNPSGD VAVFSQSQYS FKTHKTTSQW
70 80 90 100 110 120
NVLDLKSGDI KLLTNDSDVS EIVWLGSDDS TVLYVNGTNA DIPGGVELWV SDISDFANGY
130 140 150 160 170 180
KAASLPASFS GFKVVTTDSG DVRYVAYAES WANGTAYNEE LVAKPLSSAR IYDSIYVRHW
190 200 210 220 230 240
DYYLTTRFNA VFSGTLKKSE GKGKATYKAD GDLKNLVSPV KNAESPYPPF GGASDYDLSP
250 260 270 280 290 300
DGKWVAFKSK AHDIPRANYT TAYIFLVPHD GSKTAVPING PDSPGTPEGV KGDAGSPVFS
310 320 330 340 350 360
PDSKKIAYWQ MADESYEADH RTLYVYTVGS EETIPSLAAD WDRSLDSVKW ADDDNLIIGV
370 380 390 400 410 420
EDAGRSRLFS IPADAGDDYK PKNFTDGGVV SAYYQLPDST YLVTSTAIWT SWNVYIASPE
430 440 450 460 470 480
KGVIKTLATA NKIDPELKGL GPEIVDEFYY EGNWTKIQAF VIYPENFDKS KSYPLLYYIH
490 500 510 520 530 540
GGPQSSWLDS WSTRWNPKVF ADQGYVVVAP NPTGSSGFGD ALQDAIQNQW GGYPYEDLVK
550 560 570 580 590 600
GWEYVNENFD FIDTDNGVAA GASYGGFMIN WIQGSDLGRK FKALVSHDGT FVADAKVSTE
610 620 630 640 650 660
ELWFMQHEFN GTFWDNRENY RRWDPSAPER ILKFSTPMLI IHSDLDYRLP VSEGLSLFNI
670 680 690 700 710 720
LQERGVPSRF LNFPDENHWV QNKENSLVWH QQVLGWLNKY SGVEESNEDA VSLDNTVIPV
VDYNP