CAZyme Information: P170DRAFT_451719-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_451719-t37_1-p1
• CAZy Family: GH51
• CAZyme Description: barwin-like endoglucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
402	MSFO01000001|CGC38	41024.55	4.1523

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000001:277136-278400(-)

Full Sequence      

MKYQSLVSLGLAALGTTSVSASPLFHHRDNGQCPPGYSPSVYYITVTAEATPTSTSSVEL
TTTVSSSSSTTSTSETTVSTTQTPIQPTYHTLVEIPPPVTTEAPVTTQAEAAPVETTTPA
EPSTTSSAVEQQPTVVVVSSEAPAAPAPSTTEAEAPVVAVPTTTQAAKPAATTAASSSSS
SNSNSNAGSSSSSSSSSSSGSSGAVNSGKATFYGGNVSGGACSFTGYTIPSSLFGTALSQ
ARWNDASSCGACVSVKGPDGNNVKAMIVDKCPECESNHLDLFETAFSELASTSEGIIPID
WSFVPCGIDSPITLKNKEGTSAYWFSMQVVNANEPVSSLEVSTDGGSTWQETTRSDYNFF
ENESGFGAETVDVRVTSQSGGKIHVKNVGCSSGTEKEATSNF

Enzyme Prediction     

No EC number prediction in P170DRAFT_451719-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM63	315	383	8.9e-24	0.8461538461538461

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409004	DPBB_RlpA_EXP_N-like	3.61e-32	209	303	4	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	1.52e-21	210	306	5	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	1.16e-19	210	380	35	203	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
409010	DPBB_SPI-like	9.98e-14	209	303	4	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	1.34e-12	210	301	7	99	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
QMW44202.1|CBM63	8.89e-109	1	401	1	423
BAE62388.1|CBM63	8.89e-109	1	401	1	423
UDD57125.1|CBM63	8.89e-109	1	401	1	423
QRD83608.1|CBM63	9.47e-109	1	401	1	425
QMW32176.1|CBM63	9.47e-109	1	401	1	425

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JCW_A	7.80e-26	208	402	5	198	Crystal structure of Clavibacter michiganensis expansin in complex with cellopentaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4JCW_B Crystal structure of Clavibacter michiganensis expansin in complex with cellopentaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4JJO_A crystal structure of apo-clavibacter Michiganensis expansin [Clavibacter michiganensis]
4JS7_A	3.96e-25	208	402	5	198	Crystal structure of D78N mutant apo form of clavibacter michiganensis expansin [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4L48_A Crystal structure of d78n mutant clavibacter michiganensis expansin in complex with cellohexaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4L48_C Crystal structure of d78n mutant clavibacter michiganensis expansin in complex with cellohexaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4PNY1|EXP11_ORYSJ	1.36e-10	206	391	28	235	Expansin-A11 OS=Oryza sativa subsp. japonica OX=39947 GN=EXPA11 PE=2 SV=2
sp|Q40637|EXPA3_ORYSJ	2.17e-09	207	391	30	240	Expansin-A3 OS=Oryza sativa subsp. japonica OX=39947 GN=EXPA3 PE=2 SV=2
sp|O22874|EXPA8_ARATH	1.27e-08	203	380	28	229	Expansin-A8 OS=Arabidopsis thaliana OX=3702 GN=EXPA8 PE=2 SV=1
sp|Q2QP13|EXP26_ORYSJ	1.30e-08	208	375	85	260	Expansin-A26 OS=Oryza sativa subsp. japonica OX=39947 GN=EXPA26 PE=2 SV=1
sp|Q9FMA0|EXP14_ARATH	1.74e-08	202	387	27	234	Expansin-A14 OS=Arabidopsis thaliana OX=3702 GN=EXPA14 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000326	0.999673	CS pos: 21-22. Pr: 0.9643

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_451719-t37_1-p1.