dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Sporothrix schenckii

Lineage

Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii

CAZyme ID

SPSK_09573-t39_1-p1

CAZy Family

GT34

CAZyme Description

cellulose-binding protein family II protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
328		35848.04	6.2201

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sschenckii1099-18	10434	1397361	141	10293

Gene Location

Enzyme Prediction help

EC	3.2.1.55:25	3.2.1.-:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH62	22	294	3.8e-126	0.9964028776978417

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
281639	Glyco_hydro_62	5.11e-158	22	294	1	272	Glycosyl hydrolase family 62. Family of alpha -L-arabinofuranosidase (EC 3.2.1.55). This enzyme hydrolyzed aryl alpha-L-arabinofuranosides and cleaves arabinosyl side chains from arabinoxylan and arabinan.
350101	GH62	2.53e-145	24	322	1	304	Glycosyl hydrolase family 62, characterized arabinofuranosidases. The glycosyl hydrolase family 62 (GH62) includes eukaryotic (mostly fungal) and prokaryotic enzymes which are characterized arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. These enzymes show significantly different substrate preference with rather low specific activity towards natural substrates and differ in catalytic efficiency. They do not act on xylose moieties in xylan that are adorned with an arabinose side chain at both O2 and O3 positions, nor do they display any non-specific arabinofuranosidase activity. The synergistic action in biomass degradation makes GH62 promising candidates for biotechnological improvements of biofuel production and in various biorefinery applications. These enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan.
350092	GH_F	1.66e-35	47	302	1	251	Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
270308	PBP2_PotD_PotF_like	3.58e-04	104	148	91	137	The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
223759	PotD	0.001	105	177	124	197	Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
7.99e-168	15	322	17	324
1.55e-165	21	322	195	494
2.15e-165	22	322	185	483
1.42e-163	22	322	185	483
6.58e-163	20	322	187	487

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.07e-169	15	322	20	327	Structure of an alpha-L-arabinofuranosidase (GH62) from Aspergillus nidulans [Aspergillus nidulans FGSC A4]
2.34e-163	20	322	81	382	Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, in the apoprotein form [Streptomyces thermoviolaceus],4O8O_A Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, bound to alpha-L-arabinose [Streptomyces thermoviolaceus],4O8P_A Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, bound to xylotetraose [Streptomyces thermoviolaceus]
6.05e-150	15	322	132	436	Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase [Streptomyces coelicolor A3(2)],3WMZ_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase ethylmercury derivative [Streptomyces coelicolor A3(2)],3WN0_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with L-arabinose [Streptomyces coelicolor A3(2)],3WN1_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with xylotriose [Streptomyces coelicolor A3(2)],3WN2_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with xylohexaose [Streptomyces coelicolor A3(2)]
5.37e-149	21	322	19	317	Structure of Fungal GH62 from Thielavia terretris [Thermothielavioides terrestris NRRL 8126]
6.64e-149	12	323	8	325	Structure of a Talaromyces pinophilus GH62 Arabinofuranosidase in complex with AraDNJ at 1.25A resolution [Talaromyces pinophilus],6F1J_B Structure of a Talaromyces pinophilus GH62 Arabinofuranosidase in complex with AraDNJ at 1.25A resolution [Talaromyces pinophilus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.42e-168	15	322	17	324	Alpha-L-arabinofuranosidase axhA-2 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=axhA-2 PE=1 SV=1
3.50e-158	19	322	25	326	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=axhA PE=3 SV=1
4.96e-158	19	322	25	326	Alpha-L-arabinofuranosidase axhA OS=Aspergillus sojae OX=41058 GN=axhA PE=2 SV=1
1.59e-156	18	322	24	326	Probable alpha-L-arabinofuranosidase axhA-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=axhA-1 PE=3 SV=2
1.07e-148	15	322	169	473	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=abfB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000264	0.999716	CS pos: 20-21. Pr: 0.9860

TMHMM Annotations help

There is no transmembrane helices in SPSK_09573-t39_1-p1.

You are here: Home > Sequence: SPSK_09573-t39_1-p1