Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for D4DE18

Entry ID Method Resolution Chain Position Source
AF-D4DE18-F1 Predicted AlphaFoldDB

No variants for D4DE18

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for D4DE18

No associated diseases with D4DE18

3 regional properties for D4DE18

Type Name Position InterPro Accession
active_site Aspartic peptidase, active site 289 - 300 IPR001969
domain Peptidase family A1 domain 94 - 399 IPR033121
domain Aspergillopepsin-like catalytic domain 94 - 398 IPR034163

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
aspartic-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.

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
MWHSPFFTAF TLFLGFFTLT LALPTNSLAT TGRFTVEQRL IKTFESNWPP KELWRGLRKH
70 80 90 100 110 120
HRPLPPAVSR IATHRGPSAN GTVKVTPDEY NTEFVNEITI GNNTLFVDID TGSSDFWVFS
130 140 150 160 170 180
SQLPERSQLN HRIYHPEKTG TKLSKQIWEI GYGDGTGAAG NVFLDKASLA GLEVPSQAVQ
190 200 210 220 230 240
AATWVSYQFA DQTVTDGVIG FGFDHFNGVT PKKQKTWFGN IMERLEKPIF TACLKHKAPG
250 260 270 280 290 300
FYDFGFIDRT KHIGNPSYLP VDNSRGWWET TFNGFSTGRN DNSTYRFRAV VDTGTTFSLL
310 320 330 340 350 360
PREITEQYYS LITGSTFDRE NGGWTFPCNT TLPEFAIHIN DYKAIVPGEH INWAQIPGTN
370 380 390 400
TCFGGIQSVD RSPAVLGGSF LKSQFVIFDH DGPKMGFAAQ R