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Protein

Probable rhamnogalacturonate lyase C

Gene

rglC

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity).By similarity

Catalytic activityi

Cleaves the alpha-1,4 linkage of RG-I backbone between a rhamnose and a galacturonate, thereby creating an unsaturated bond between carbons 4 and 5 of the galacturonate residue.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiPL4. Polysaccharide Lyase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable rhamnogalacturonate lyase C (EC:4.2.2.-)
Gene namesi
Name:rglC
ORF Names:AO090113000057
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000039438022 – 695Probable rhamnogalacturonate lyase CAdd BLAST674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi28N-linked (GlcNAc...)Sequence analysis1
Glycosylationi96N-linked (GlcNAc...)Sequence analysis1
Glycosylationi118N-linked (GlcNAc...)Sequence analysis1
Glycosylationi144N-linked (GlcNAc...)Sequence analysis1
Glycosylationi199N-linked (GlcNAc...)Sequence analysis1
Glycosylationi285N-linked (GlcNAc...)Sequence analysis1
Glycosylationi532N-linked (GlcNAc...)Sequence analysis1
Glycosylationi638N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ2U5P7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 4 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000217023.
OMAiIYWGKYD.
OrthoDBiEOG092C0TP2.

Family and domain databases

CDDicd10316. RGL4_M. 1 hit.
Gene3Di2.60.120.260. 1 hit.
2.60.40.1120. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR014766. CarboxyPept_regulatory_dom.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR029413. RG-lyase_II.
IPR029411. RG-lyase_III.
[Graphical view]
PfamiPF14683. CBM-like. 1 hit.
PF14686. fn3_3. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF74650. SSF74650. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q2U5P7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLPSRKALA FLACLASHSV ALLTTSENST HFNLANDRFS IALAKSNGHI
60 70 80 90 100
VDVQLDGQDL LGPVDGNAGK GPYLDCSCIP SGFWTPGSGA HLELINGTDS
110 120 130 140 150
TGTAYGGLYM SATYAGTNQT LSQWFFLRGE ETGLHAFSRV TYFNETTPSL
160 170 180 190 200
RSLGELRTLF RPSTDLWTHF STSDGNYGPK PLGSNSGLVV QDATTYIGNV
210 220 230 240 250
TDDPYVSQYS DYFTKYTLAE SWRNHDVHGL FSDGSSSSDG STFGAWLVHN
260 270 280 290 300
TVETYYGGPL HSDLVVDGIV YNYLVSGHHG APTPNLTHGF DRTWGPQFYY
310 320 330 340 350
FNRGDSETTL ADLRADAAKY ADPEWNAEFY DSIADHIPNF TPSTGRTTFK
360 370 380 390 400
GKVSLPKGAK RPIIVLSEDG QDFQLNVFNT ESLQYWAEID KSGSFSIPRV
410 420 430 440 450
VEGTYRITIY ADEIFGWFIQ DHVKVLKSQS KDYSFTWKEE SAGKEIWRIG
460 470 480 490 500
IPDKSSGEYL HGYAPDTSKP LQPEQHRIYW GKYDYPADFP EGINFHVGKS
510 520 530 540 550
DPSQDLNYIH WAFFPSQGNH LRTEPYYDNV NNWTVTFDLT ADQLHNTNTA
560 570 580 590 600
TFTVQIAGAK TANGNAKWTP VEGKYSNLPW TVNVNGRYES TWVIPYWRSG
610 620 630 640 650
SCGVRSAVSC QNIEQKFAFP SKNLQEGKNE FVLSLPFNAS STETALLPDA
660 670 680 690
LYVQARVMGS RLDPARPAPN PLVNSNLGFG RDNPIMEFSN NRIIT
Length:695
Mass (Da):77,249
Last modified:January 24, 2006 - v1
Checksum:iE6032805EBE4EE1A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007166 Genomic DNA. Translation: BAE63118.1.

Genome annotation databases

EnsemblFungiiBAE63118; BAE63118; AO090113000057.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007166 Genomic DNA. Translation: BAE63118.1.

3D structure databases

ProteinModelPortaliQ2U5P7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL4. Polysaccharide Lyase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE63118; BAE63118; AO090113000057.

Phylogenomic databases

HOGENOMiHOG000217023.
OMAiIYWGKYD.
OrthoDBiEOG092C0TP2.

Family and domain databases

CDDicd10316. RGL4_M. 1 hit.
Gene3Di2.60.120.260. 1 hit.
2.60.40.1120. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR014766. CarboxyPept_regulatory_dom.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR029413. RG-lyase_II.
IPR029411. RG-lyase_III.
[Graphical view]
PfamiPF14683. CBM-like. 1 hit.
PF14686. fn3_3. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF74650. SSF74650. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRGLC_ASPOR
AccessioniPrimary (citable) accession number: Q2U5P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.