CAZyme Information: ACLA_008190-t26_1-p1

Basic Information

• Species: Aspergillus clavatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
• CAZyme ID: ACLA_008190-t26_1-p1
• CAZy Family: AA7
• CAZyme Description: chitin binding domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
248	DS027051|CGC5	27285.83	6.5932

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AclavatusNRRL1	9428	344612	287	9141

• Gene Location: location=DS027051:825990-826794(+)

Full Sequence      

MKPFATLVAFALATCVAGHGYMYIPTSRTRLGHEAGVDTCPECAILEPVQAWPSLDSAKV
GRSGPCGYNARDSIDYNQPTKNWGSKPVSAFKAGQEIEVQWCVDHNGDHGGMFTYRICQD
QKLVSKFLDPSYMPTEAEKQAAEDCFEKGILPCTDVNGQKCSYSPDCKQGEPCWRNDWFT
CDAFDGAKCKGVDNAALNSCKTTIAGGYTVTKKVKLPNYVSNHTLLSWKWNSFQTPQIYL
SCADISIS

Enzyme Prediction     

EC	1.14.99.55:5

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA13	19	247	1.1e-137	0.9956896551724138

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
412056	AA13_LPMO-like	1.93e-160	19	248	1	233	AA13 lytic polysaccharide monooxygenase, and similar proteins. This family contains starch-degrading (also called starch-active) lytic polysaccharide monooxygenase (LPMO), a representative of the new CAZy AA13 family and classified as an auxiliary activity enzyme. This enzyme acts on alpha-linked glycosidic bonds and displays a binding surface that is quite different from those of LPMOs acting on beta-linked glycosidic bonds, indicating that the AA13 family proteins interact with their substrate in a distinct fashion. The active site contains an amino-terminal histidine-ligated mononuclear copper. This enzyme generates aldonic acid-terminated malto-oligosaccharides from retrograded starch and significantly boosts the conversion of this recalcitrant substrate to maltose by beta-amylase.
397269	LPMO_10	0.006	19	120	1	117	Lytic polysaccharide mono-oxygenase, cellulose-degrading. This domain is found associated with a wide variety of cellulose binding domains. This is a family of two very closely related proteins that together act as both a C1- and a C4-oxidising lytic polysaccharide mono-oxygenase, degrading cellulose. This domain is also found in baculoviral spheroidins and spindolins, protein of unknown function.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW44617.1|AA13	1.62e-154	1	247	1	250
QMW32587.1|AA13	1.62e-154	1	247	1	250
QRD84087.1|AA13	1.62e-154	1	247	1	250
UDD57602.1|AA13	1.62e-154	1	247	1	250
BAE61982.1|AA13|1.14.99.55	1.48e-152	4	247	32	278

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4OPB_A	2.86e-147	20	247	2	232	AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae [Aspergillus oryzae RIB40],5LSV_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7J_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7K_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7N_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],6TBQ_A AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae partially in Cu(II) state [Aspergillus oryzae RIB40],6TBR_A Glycosylated AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae in P1 space group [Aspergillus oryzae RIB40],6TBR_B Glycosylated AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae in P1 space group [Aspergillus oryzae RIB40],6TC4_A AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae measured with SSX [Aspergillus oryzae RIB40]

Swiss-Prot Hits     

ACLA_008190-t26_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000256	0.999715	CS pos: 18-19. Pr: 0.9784

TMHMM  Annotations     

There is no transmembrane helices in ACLA_008190-t26_1-p1.