Q59485

PR
Gene name
pepX
Protein name
Xaa-Pro dipeptidyl-peptidase
Names
X-Pro dipeptidyl-peptidase, X-prolyl-dipeptidyl aminopeptidase, X-PDAP
Species
Lactobacillus helveticus (Lactobacillus suntoryeus)
KEGG Pathway
EC number
3.4.14.11: Dipeptidyl-peptidases and tripeptidyl-peptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

226-304 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for Q59485

Entry ID Method Resolution Chain Position Source
6NFF X-ray 200 A A 1-793 PDB
AF-Q59485-F1 Predicted AlphaFoldDB

No variants for Q59485

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q59485

No associated diseases with Q59485

2 regional properties for Q59485

Type Name Position InterPro Accession
domain Peptidase M17, leucyl aminopeptidase, C-terminal 184 - 488 IPR000819
domain Peptidase M17, leucyl aminopeptidase, N-terminal 22 - 146 IPR008283

Functions

Description
EC Number 3.4.14.11 Dipeptidyl-peptidases and tripeptidyl-peptidases
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.

3 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
dipeptidyl-peptidase activity Catalysis of the hydrolysis of N-terminal dipeptides from a polypeptide chain.
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
MKYNQYAYVE TDFQQQVKEL IDINFLPKNY QVWDFSSLLA KLVKNAIAEA KTDAAKNAKL
70 80 90 100 110 120
AEFAVSDHQT LADFLKEKPT EIGTKQFYNV ALQLLGYHVH YDYDFADPTG FMQRNALPFL
130 140 150 160 170 180
QDISDNQKLI SAFYRLLNTR AKNGQILLDV MAGKGYFTQF WGQNKFKFFN GKSIPVFDTN
190 200 210 220 230 240
KVIREVVYVE TDLDTDHDGK SDLIQVTVFR PEETNKGLKV PALYTASPYF GGIIANEKRN
250 260 270 280 290 300
HNVDENLSDS TEWNDPQYVH SPIVKAEKPD GSSRPATEEA VHKSSYPLNE YMLARGFASV
310 320 330 340 350 360
FAGAIGTRGS DGVRITGAPE ETESAAAVIE WLHGDRVAYT DRTRTVQTTA DWCNGNIGMT
370 380 390 400 410 420
GRSYLGTLQI AIATTGVKGL KTVVSEAAIS SWYDYYREHG LVIAPEACQG EDLDLLAETC
430 440 450 460 470 480
QSNLWDAGSY LKIKPEYDKM QKQLREKEDR NTGQYSDFWE ARNYRHHADG IKCSWISVHG
490 500 510 520 530 540
LNDWNVKPKN VYKIWQLVKK MPMKHHLFLH QGPHYNMNNL VSIDFTDLMN LWFVHELLGI
550 560 570 580 590 600
ENNAYNQWPT VMIQDNLQAD KWHEEPDWSN DLGQEKIYYP TDEGELFQDG NGKAQKSFTD
610 620 630 640 650 660
VGGIEFKKAG ISESDWQYKF ICGDEKWAKP SLRFETDEFT HPTTIVGRPE VKVRVSASLP
670 680 690 700 710 720
KGEISVALVE LGERQRLTAT PKFLMHGGQE LGYRFGTDTL QEFVPDKKTK AKLITKAHMN
730 740 750 760 770 780
LQNFKDMKKP EAIDADKFYD LDFLLQPTYY TIPSGSKLAL IIYSTDQGMT KRPLEDETYT
790
IDLANTEIKF YEK