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Protein

Isoaspartyl peptidase/L-asparaginase

Gene
N/A
Organism
Lupinus arboreus (Tree lupine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Also has L-asparaginase activity, which is used to liberate stored nitrogen during seed development.

Catalytic activityi

Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei174NucleophileBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Protease

Protein family/group databases

MEROPSiT02.A01

Names & Taxonomyi

Protein namesi
Recommended name:
Isoaspartyl peptidase/L-asparaginase (EC:3.4.19.5)
Alternative name(s):
L-asparagine amidohydrolase
Cleaved into the following 2 chains:
OrganismiLupinus arboreus (Tree lupine)
Taxonomic identifieri3872 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeGenisteaeLupinus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000045454‹1 – 173Isoaspartyl peptidase/L-asparaginase subunit alphaAdd BLAST›173
ChainiPRO_0000045455174 – 306Isoaspartyl peptidase/L-asparaginase subunit betaAdd BLAST133

Post-translational modificationi

Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei173 – 174Cleavage; by autolysisBy similarity2

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PRIDEiP30362

Expressioni

Tissue specificityi

Developing seeds.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.

Structurei

3D structure databases

ProteinModelPortaliP30362
SMRiP30362
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni202 – 205Substrate bindingBy similarity4
Regioni224 – 227Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Family and domain databases

InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000246 Peptidase_T2
PANTHERiPTHR10188 PTHR10188, 1 hit
PfamiView protein in Pfam
PF01112 Asparaginase_2, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30362-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PPERRKPREE GLRHCLQIGV EALKARKSPL DVVELVVREL ENNEHFNAGI
60 70 80 90 100
GSVLTNSGTV EMEASIMDGK SMKCGAVSGL STVLNPISLA RLVMEKTPHM
110 120 130 140 150
YLAFQGAQDF AKQQGVETVD SSHFITAENV ERLKLAIEAN RVQIDYSQYN
160 170 180 190 200
YTQPVQDDAE KELPVANGDS QIGTVGCVAV DSQGNLASAT STGGLVNKMV
210 220 230 240 250
GRIGDTPLIG AGTYANELCA VSATGKGEAI IQATVARDVA ALMEFKGLSL
260 270 280 290 300
KEAADYVVHE RTPKGTVGLI AVSAAGEIAM PFNTTGMFRA CATEDGNSEI

AIWPPA
Length:306
Mass (Da):32,463
Last modified:April 1, 1993 - v1
Checksum:i9E0E19F64B30A2F2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52588 mRNA Translation: CAA36824.1
PIRiS22523

Similar proteinsi

Entry informationi

Entry nameiASPG_LUPAR
AccessioniPrimary (citable) accession number: P30362
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: May 23, 2018
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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