Q10730

PR
Gene name
pepN
Protein name
Aminopeptidase N
Names
Alanine aminopeptidase, Lysyl aminopeptidase, Lys-AP
Species
Lactobacillus helveticus (Lactobacillus suntoryeus)
KEGG Pathway
EC number
3.4.11.2: Aminopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

313-385 (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 Q10730

Entry ID Method Resolution Chain Position Source
AF-Q10730-F1 Predicted AlphaFoldDB

6 variants for Q10730

Variant ID(s) Position Change Description Diseaes Association Provenance
39 F>I strain: 53/7 [UniProt] No
44 L>F strain: 53/7 [UniProt] No
342 S>A strain: 53/7 [UniProt] No
455 K>R strain: 53/7 [UniProt] No
496 S>N strain: 53/7 [UniProt] No
527 H>L strain: 53/7 [UniProt] No

No associated diseases with Q10730

3 regional properties for Q10730

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 217 - 435 IPR014782
domain ERAP1-like C-terminal domain 510 - 817 IPR024571
domain Aminopeptidase N-like, N-terminal domain 11 - 181 IPR045357

Functions

Description
EC Number 3.4.11.2 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.

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.
metallopeptidase activity Catalysis of the hydrolysis of peptide bonds 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.
zinc ion binding Binding to a zinc ion (Zn).

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
MAVKRFYKTF HPEHYDLRIN VNRKNKTING TSTITGDVFE NPVLINQKFM TIDSVKVDGK
70 80 90 100 110 120
NVDFDVIEKD EAIKIKTGVT GKAVIEIAYS APLTDTMMGI YPSYYELEGK KKQIIGTQFE
130 140 150 160 170 180
TTFARQAFPC VDEPEAKATF SLALKWDEQD GEVALANMPE VEVDKDGYHH FEETVRMSSY
190 200 210 220 230 240
LVAFAFGELQ SKTTHTKDGV LIGVYATKAH KPKELDFALD IAKRAIEFYE EFYQTKYPLP
250 260 270 280 290 300
QSLQLALPDF SAGAMENWGL VTYREAYLLL DPDNTSLEMK KLVATVITHE LAHQWFGDLV
310 320 330 340 350 360
TMKWWDNLWL NESFANMMEY LSVDGLEPDW HIWEMFQTSE ASSALNRDAT DGVQPIQMEI
370 380 390 400 410 420
NDPADIDSVF DSAIVYAKGS RMLVMVRSLL GDDALRKGLK YYFDHHKFGN ATGDDLWDAL
430 440 450 460 470 480
STATDLDIGK IMHSWLKQPG YPVVNAFVAE DGHLKLTQKQ FFIGEGEDKG RQWQIPLNAN
490 500 510 520 530 540
FDAPKIMSDK EIDLGSYKVL REEAGHPLRL NVGNNSHFIV EYDKTLHDDI LSDVNELDPI
550 560 570 580 590 600
DKLQLLQDLR LLAEGKQISY ASIVPLLVKF ADSKSSLVIN ALYTTAAKLR QFVEPESNEE
610 620 630 640 650 660
KNLKKLYDLL SKDQVARLGW EVKPGESDED VQIRPYELSA SLYAENADSI KAAHQIFTEN
670 680 690 700 710 720
EDNLEALNAD IRPYVLINEV KNFGNAELVD KLIKEYQRTA DPSYKVDLRS AVTSTKDLAA
730 740 750 760 770 780
IKAIVGDFEN ADVVKPQDLC DWYRGLLANH YGQQAAWDWI REDWDWLDKT VGGDMEFAKF
790 800 810 820 830 840
ITVTAGVFHT PERLKEFKEF FEPKINVPLL SREIKMDVKV IESKVNLIEA EKDAVNDAVA
KAID