Q2U1F3

EV
Gene name
lapA (AO090011000052)
Protein name
Leucine aminopeptidase A
Names
EC 3.4.11.- , Leucyl aminopeptidase A , LAPA
Species
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
KEGG Pathway
aor:AO090011000052
EC number
3.4.11.-: Aminopeptidases
Protein Class
METALLOPEPTIDASE M28 FAMILY MEMBER (PTHR12147)

Descriptions

Leucyl aminopeptidase A from Aspergillus oryzae RIB40 (AO-LapA) is an exo-acting peptidase. AO-Lap is secreted as a zymogen by the host and requires enzymatic cleavage of the autoinhibitory propeptide to reveal its full activity.

Autoinhibitory domains (AIDs)

19-79 (Propeptide) EV

Target domain

80-377 (Aminopeptidase domain)

Relief mechanism

Cleavage, Ligand binding, Others

Assay

Structural analysis, Deletion assay, Split protein assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

4 structures for Q2U1F3

Entry ID Method Resolution Chain Position Source
6ZEP X-ray 161 A A 1-377 PDB
6ZEQ X-ray 197 A A 1-377 PDB
7OEZ X-ray 248 A A 77-377 PDB
AF-Q2U1F3-F1 Predicted AlphaFoldDB

No variants for Q2U1F3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2U1F3

No associated diseases with Q2U1F3

11 regional properties for Q2U1F3

Type Name Position InterPro Accession
domain RNA polymerase sigma-70 159 - 172 IPR000943-1
domain RNA polymerase sigma-70 183 - 191 IPR000943-2
domain RNA polymerase sigma-70 307 - 319 IPR000943-3
domain RNA polymerase sigma-70 328 - 354 IPR000943-4
domain RNA polymerase sigma factor 70, region 1.1 24 - 80 IPR007127
domain RNA polymerase sigma-70 region 3 214 - 290 IPR007624
domain RNA polymerase sigma-70 region 2 135 - 204 IPR007627
domain RNA polymerase sigma-70 region 4 303 - 356 IPR007630
domain RNA polymerase sigma-70 region 1.2 97 - 129 IPR009042
domain RNA polymerase sigma factor RpoD, C-terminal 131 - 367 IPR012760
domain RNA polymerase sigma-70 like domain 133 - 356 IPR014284

Functions

Description
EC Number 3.4.11.- Aminopeptidases
Subcellular Localization
  • Secreted
PANTHER Family PTHR12147 METALLOPEPTIDASE M28 FAMILY MEMBER
PANTHER Subfamily PTHR12147:SF26 ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1
PANTHER Protein Class metalloprotease
protease
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.

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.
metal ion binding Binding to a metal ion.
metalloexopeptidase activity Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of 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
MRFLPCIATL AATASALAIG DHVRSDDQYV LELAPGQTKV VTEAEKWALR AEGKRFFDIT
70 80 90 100 110 120
ERASSLELAS NKKQKLAVTY PDSVQHNETV QNLIKSLDKK NFETVLQPFS EFHNRYYKSD
130 140 150 160 170 180
NGKKSSEWLQ GKIQEIISAS GAKGVTVEPF KHSFPQSSLI AKIPGKSDKT IVLGAHQDSI
190 200 210 220 230 240
NLDSPSEGRA PGADDDGSGV VTILEAFRVL LTDEKVAAGE APNTVEFHFY AGEEGGLLGS
250 260 270 280 290 300
QDIFEQYSQK SRDVKAMLQQ DMTGYTKGTT DAGKPESIGI ITDNVDENLT KFLKVIVDAY
310 320 330 340 350 360
CTIPTVDSKC GYGCSDHASA TKYGYPAAFA FESAFGDDSP YIHSADDTIE TVNFDHVLQH
370
GRLTLGFAYE LAFADSL