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 Q135P8

Entry ID Method Resolution Chain Position Source
AF-Q135P8-F1 Predicted AlphaFoldDB

No variants for Q135P8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q135P8

No associated diseases with Q135P8

3 regional properties for Q135P8

Type Name Position InterPro Accession
domain Xaa-Pro dipeptidyl-peptidase-like domain 184 - 501 IPR000383
domain Xaa-Pro dipeptidyl-peptidase, C-terminal 515 - 754 IPR013736
domain X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain 1 - 145 IPR015251

Functions

Description
EC Number 3.4.11.1 Aminopeptidases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
manganese ion binding Binding to a manganese ion (Mn).
metalloaminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

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
MPDAVKVGFV PFSAAARGTL VVFCDDTLKF GSVTGKALGA AASTVKRAVA ASQFKGKSGS
70 80 90 100 110 120
ALDLLAPEGL KVGRLIVIGT GKAAALKDND IVKLGGAVAG KLSTGDSAVT VIAELPGGAM
130 140 150 160 170 180
RPEQAAAVAS GIRLRAYKFD RYKTKKKDDD ADAANANVSI AVADVAAAKK AFAPDSHVVD
190 200 210 220 230 240
GVILARELVN EPPNVLYPEE FAKRAAQLRK LGVQVEILDV KAMTRLKMGA LLGVSQGSAH
250 260 270 280 290 300
PGRTVIMRWN GGKRGAQPVA FVGKGVCFDT GGISIKPSAS MEDMKGDMGG AACVVGLMHA
310 320 330 340 350 360
LAARKAKINV IGAIGLVENM PDGNAQRPGD IVTSMSGQTI EIINTDAEGR LVLADVLWYV
370 380 390 400 410 420
AQKHKPKFMV DLATLTGAIM VALGTDHAGL FSNNDELAER LTAAGLSTGE RVWRMPLGPE
430 440 450 460 470 480
YDKQIDSQFA DMKNTGSRNG GSITAAQFLQ RFVDNTPWAH LDIAGTAMGA PKSDINHSWG
490
SGYGVRLLNA LVAEHYEAKK