CAZyme Information: AN7735-T-p1

Basic Information

• Species: Aspergillus nidulans
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans
• CAZyme ID: AN7735-T-p1
• CAZy Family: GT1
• CAZyme Description: Putative endoglucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
366		37003.29	4.0989

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnidulansFGSCA4	10988	227321	276	10712

• Gene Location: location=ChrIV_A_nidulans_FGSC_A4:2536420-2537571(-)

Full Sequence      

MKYQHFSSIALAALSASTFVSAAPLAPEENGSCPAGYSPSVYYITVTAEPSSTVRPTSSA
PISSTPTSTSTSTSTSETSLTTLASTSTGDVTVTSSSTAGLIETIPAVVVNAATSTTSES
ATSTSALSISETAPTQVAVARPSTTTAAEKTSSTSTSSSSSSTSTNSGATTGEATFYGGN
LSGGTCSFTDYTLPSHLSGVAFSGQAWDNAAECGACIAVTGPNGNTVKVMVVDKCPECAQ
THLDLFESAFTTLASASEGQIPISYSITPCGITSPLILRNKSGTSAYWFSMQVVNANGAV
KSLEVSTDNGSTWQETTRSDYNFFENSSGFGTDTVDVRVTGVDGGVITVKNVSVASGESV
TADGNF

Enzyme Prediction     

No EC number prediction in AN7735-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM63	278	350	5.1e-24	0.8974358974358975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409004	DPBB_RlpA_EXP_N-like	2.18e-25	170	267	1	94	double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains. The double-psi beta-barrel (DPBB) fold is found in a divergent group of proteins, including endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), EG45-like domain containing proteins, kiwellins, Streptomyces papain inhibitor (SPI), and the N-terminal domain of plant and bacterial expansins. RlpA may work in tandem with amidases to degrade peptidoglycan (PG) in the division septum and lateral wall to facilitate daughter cell separation. An EG45-like domain containing protein from Arabidopsis thaliana, called plant natriuretic peptide A (AtPNP-A), functions in cell volume regulation. Kiwellin proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. SPI is a stress protein produced under hyperthermal stress conditions that serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes. Some expansin family proteins display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs.
409008	DPBB_EXP_N-like	2.82e-19	170	270	1	117	N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains. The plant expansin family consists of four subfamilies, alpha-expansin (EXPA), beta-expansin (EXPB), expansin-like A (EXLA), and expansin-like B (EXLB). EXPA and EXPB display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. EXPA proteins function more efficiently on dicotyledonous cell walls, whereas EXPB proteins exhibit specificity for the cell walls of monocotyledons. Expansins also affect environmental stress responses. Expansin family proteins contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This family also includes GH45 endoglucanases from mollusks. This model represents the N-terminal domain of expansins and similar proteins, which adopts a double-psi beta-barrel (DPBB) fold.
226755	YoaJ	7.26e-19	171	347	32	206	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
409010	DPBB_SPI-like	1.82e-13	170	267	1	101	double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins. Streptomyces papain inhibitor (SPI) adopts a rigid, thermo-resistant double-psi-beta-barrel (DPBB) fold that is stabilized by two cysteine bridges. SPI serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes, that is used to covalently and specifically link functional amines to glutamine donor sites of therapeutic proteins. SPI is a stress protein produced under hyperthermal stress conditions, and is able to inhibit the cysteine proteases, papain and bromelain, as well as the bovine serine protease trypsin.
409009	DPBB_EXLX1-like	4.21e-12	171	267	4	101	N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus subtilis EXLX1. This subfamily is composed of bacterial expansins including Bacillus subtilis EXLX1, also called expansin-YoaJ. Similar to plant expansins, EXLX1 contains an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. It strongly binds to crystalline cellulose via D2, and weakly binds soluble cellooligosaccharides. Bacterial expansins, which are present in some plant pathogens, have the ability to loosen plant cell walls, but with weaker activity compared to plant expansins. They may have a role in plant-bacterial interactions. This model represents the N-terminal domain of EXLX1 and similar bacterial expansins, which adopts a double-psi beta-barrel (DPBB) fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA61250.1|CBM63	4.64e-196	1	366	1	366
BCS29837.1|CBM63	6.56e-121	1	362	1	370
QMW44202.1|CBM63	5.87e-94	172	365	230	423
BAE62388.1|CBM63	5.87e-94	172	365	230	423
UDD57125.1|CBM63	5.87e-94	172	365	230	423

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5NTB_A	4.02e-06	223	261	63	101	Streptomyces papain inhibitor (SPI) [Streptomyces mobaraensis],5NTB_B Streptomyces papain inhibitor (SPI) [Streptomyces mobaraensis]

Swiss-Prot Hits     

AN7735-T-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000235	0.999743	CS pos: 22-23. Pr: 0.9760

TMHMM  Annotations     

There is no transmembrane helices in AN7735-T-p1.