A2RI32

PR
Gene name
pepN (lap, llmg_0319)
Protein name
Aminopeptidase N
Names
Alanine aminopeptidase, Lysyl aminopeptidase, Lys-AP
Species
Lactococcus lactis subsp cremoris (strain MG1363)
KEGG Pathway
llm:llmg_0319
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)

166-235 (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 A2RI32

Entry ID Method Resolution Chain Position Source
AF-A2RI32-F1 Predicted AlphaFoldDB

No variants for A2RI32

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2RI32

No associated diseases with A2RI32

3 regional properties for A2RI32

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 216 - 434 IPR014782
domain ERAP1-like C-terminal domain 509 - 821 IPR024571
domain Aminopeptidase N-like, N-terminal domain 11 - 180 IPR045357

Functions

Description
EC Number 3.4.11.2 Aminopeptidases
Subcellular Localization
  • Cytoplasm
  • It may be secreted through an unknown mechanism
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
MAVKRLIETF VPENYKIFLD IDRKTKKIKG QVAITGEAKD TVVSFHTKGL HFNKVRAFSV
70 80 90 100 110 120
DTNFIENEED EEIVVKIGET GRVTVSFEYE AELTDNMMGI YPSYYEVNGE KKMLIGTQFE
130 140 150 160 170 180
SHFARQAFPS IDEPEAKATF DLSVKFDEEE GDIIVSNMPE LLNINGIHVF ERTVKMSSYL
190 200 210 220 230 240
LAFVFGELQY KKGKTKSGVE VGAFATKAHS QAALDFPLDI AIRSIEFYED YYQTPYPLPH
250 260 270 280 290 300
SWHIALPDFS AGAMENWGCI TYREVCMLVD PENATIQSKQ YVATVIAHEL AHQWFGDLVT
310 320 330 340 350 360
MQWWDDLWLN ESFANNMEYV CMDALEPSWN VWESFSISEA NMALNRDATD GVQSVHVEVT
370 380 390 400 410 420
HPDEIGTLFD PAIVYAKGSR LMVMLRKWLG DEDFAAGLAL YFKRHQYGNT VGDNLWDALA
430 440 450 460 470 480
EVSGKDVAAF MHSWVNQPGY PVVTAEVVDD TLILSQKQFF VGEGVDKGRL WNVPLNTNWT
490 500 510 520 530 540
GLPDLLSSEK VEIPGFAALK TKNNGKALFL NDANMAHYII DYKGALLTDL LSEVESLENV
550 560 570 580 590 600
TKFQILQDRK LLAKAGVISY ADVVNILPSF TNEESYLVNT GLSQLISELE LFVDEDSETE
610 620 630 640 650 660
KAFQSLVGKL FAKNYARLGW DKVAGESAGD ESLRGIVLSK TLYSENADAK TKASQIFAAH
670 680 690 700 710 720
KENLASIPAD IRPIVLNNEI KTTNSAELVK TYRETYIKTS LQEFKRELEG AVALIKDEKV
730 740 750 760 770 780
IAELLESFKN ADIVKPQDIA FSWFYLLRND FSQDAAWAWE KANWAFLEEK LGGDMSYDKF
790 800 810 820 830 840
VIYPGNTFKT ADKLAEYKAF FEPKLENQGL KRSIEMAIKQ ITARVALIDS QKAAVDKAIT
DIAEKL