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Protein

Pectate lyase 1

Gene
N/A
Organism
Cupressus arizonica (Arizona cypress) (Callitropsis arizonica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Has pectate lyase activity.By similarity

Catalytic activityi

Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi170 – 1701CalciumBy similarity
Metal bindingi194 – 1941CalciumBy similarity
Metal bindingi198 – 1981CalciumBy similarity
Active sitei250 – 2501Sequence Analysis

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. pectate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. pectin catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectate lyase 1 (EC:4.2.2.2)
Alternative name(s):
Major pollen allergen Cup a 1
Allergen: Cup a 1
OrganismiCupressus arizonica (Arizona cypress) (Callitropsis arizonica)
Taxonomic identifieri49011 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaeCupressalesCupressaceaeHesperocyparis

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei256. Cup a 1.
3232. Cup a 1.0101.
895. Cup a 1.02.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 367346Pectate lyase 1PRO_0000212997Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 45By similarity
Disulfide bondi128 ↔ 147By similarity
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi306 ↔ 312By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR018082. AmbAllergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
PRINTSiPR00807. AMBALLERGEN.
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9SCG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPCLVAVL VFLCAIVSCY SDNPIDSCWR GDSNWDQNRM KLADCVVGFG
60 70 80 90 100
SSTMGGKGGE IYTVTSSEDN PVNPTPGTLR YGATREKALW IIFSQNMNIK
110 120 130 140 150
LQMPLYVAGY KTIDGRGADV HLGNGGPCLF MRKASHVILH GLHIHGCNTS
160 170 180 190 200
VLGDVLVSES IGVEPVHAQD GDAITMRNVT NAWIDHNSLS DCSDGLIDVT
210 220 230 240 250
LGSTGITISN NHFFNHHKVM LLGHDDTYDD DKSMKVTVAF NQFGPNAGQR
260 270 280 290 300
MPRARYGLVH VANNNYDQWN IYAIGGSSNP TILSEGNSFT APNESYKKEV
310 320 330 340 350
TKRIGCETTS ACANWVWRST RDAFTNGAYF VSSGKAEDTN IYNSNEAFKV
360
ENGNAAPQLT QNAGVVA
Length:367
Mass (Da):39,776
Last modified:April 16, 2014 - v2
Checksum:i0138EE8653B1ABDB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521S → L in CAC37790 (Ref. 1) Curated
Sequence conflicti68 – 681E → D in CAC37790 (Ref. 1) Curated
Sequence conflicti108 – 1081A → N in ABK78766 (PubMed:19902388).Curated
Sequence conflicti119 – 1191D → V in CAB62551 (PubMed:11122214).Curated
Sequence conflicti133 – 1331K → T in CAC37790 (Ref. 1) Curated
Sequence conflicti232 – 2321K → I in CAC37790 (Ref. 1) Curated
Sequence conflicti293 – 2931N → S in CAC37790 (Ref. 1) Curated
Sequence conflicti308 – 3081T → S in CAC37790 (Ref. 1) Curated
Sequence conflicti319 – 3191S → F in CAC37790 (Ref. 1) Curated
Sequence conflicti338 – 3381D → E in CAC37790 (Ref. 1) Curated
Sequence conflicti367 – 3671A → T in CAC37790 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278498 mRNA. Translation: CAC37790.2.
EF079863 mRNA. Translation: ABK78766.1.
AJ243570 mRNA. Translation: CAB62551.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278498 mRNA. Translation: CAC37790.2.
EF079863 mRNA. Translation: ABK78766.1.
AJ243570 mRNA. Translation: CAB62551.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei256. Cup a 1.
3232. Cup a 1.0101.
895. Cup a 1.02.
CAZyiPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR018082. AmbAllergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
PRINTSiPR00807. AMBALLERGEN.
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning of Cupressus Arizonica major allergen."
    Butteroni C., Di Felice G., Pini C.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pollen.
  2. "A modified protocol for RNA isolation from high polysaccharide containing Cupressus arizonica pollen. Applications for RT-PCR and phage display library construction."
    Pico de Coana Y., Parody N., Fernandez-Caldas E., Alonso C.
    Mol. Biotechnol. 44:127-132(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-367.
    Tissue: Pollen.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-367, ALLERGEN.

Entry informationi

Entry nameiPLY1_CUPAR
AccessioniPrimary (citable) accession number: Q9SCG9
Secondary accession number(s): A0T2M2, Q93XL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 16, 2014
Last modified: November 26, 2014
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.