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Protein

Isoaspartyl peptidase/L-asparaginase

Gene

asrgl1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.By similarity

Catalytic activityi

L-asparagine + H2O = L-aspartate + NH3.By similarity
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei166NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease

Names & Taxonomyi

Protein namesi
Recommended name:
Isoaspartyl peptidase/L-asparaginase (EC:3.4.19.5, EC:3.5.1.1)
Alternative name(s):
Asparaginase-like protein 1
Beta-aspartyl-peptidase
Isoaspartyl dipeptidase
L-asparagine amidohydrolase
Cleaved into the following 2 chains:
Gene namesi
Name:asrgl1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-989505. asrgl1.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004205651 – 165Isoaspartyl peptidase/L-asparaginase alpha chainAdd BLAST165
ChainiPRO_0000420566166 – 309Isoaspartyl peptidase/L-asparaginase beta chainAdd BLAST144

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

Keywords - PTMi

Autocatalytic cleavage

Interactioni

Subunit structurei

Heterodimer of an alpha and beta chain produced by autocleavage.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6GM78.
SMRiQ6GM78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 197Substrate bindingBy similarity4
Regioni217 – 220Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Phylogenomic databases

HOVERGENiHBG101662.
KOiK13051.

Family and domain databases

CDDicd04702. ASRGL1_like. 1 hit.
InterProiView protein in InterPro
IPR033844. ASRGL1_meta.
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: Complete.

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

Q6GM78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPVIVVHGG AGKIVEELDA TYRAGVKRAV LKGYDVLSQG GSALTAVEEA
60 70 80 90 100
VIVLEDEQIF NAGHGSVLNE KGDIEMDAII MDGKNLDSGA VSAIRNIANP
110 120 130 140 150
IKLARLVMEK TDHMLLTCEG ATLFAKAQGI PEVPNESLVT ERSRKRWMKN
160 170 180 190 200
LKENSNPVAD QIGLGTVGAV AIDCEGNVAC ATSTGGLTNK MVGRVGDTAC
210 220 230 240 250
IGSGGYADNN VGAVSTTGHG ESIMKVILAR LILHHMEQGK SPEEAADAGL
260 270 280 290 300
NYMKSRVGGI GGVIIVNSSG DWTAKFSTNQ MSWAAVKDDQ LHIGIYHGEN

NVTPLEKAL
Length:309
Mass (Da):32,505
Last modified:July 19, 2004 - v1
Checksum:i6CFFBEC28270C13D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC074198 mRNA. Translation: AAH74198.1.
RefSeqiNP_001086107.1. NM_001092638.1.
UniGeneiXl.7538.

Genome annotation databases

GeneIDi444536.
KEGGixla:444536.

Similar proteinsi

Entry informationi

Entry nameiASGL1_XENLA
AccessioniPrimary (citable) accession number: Q6GM78
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 19, 2004
Last modified: March 15, 2017
This is version 52 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families