dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Exophiala spinifera

Lineage

Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera

CAZyme ID

KIW09927.1

CAZy Family

AA1

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
896		96523.00	5.0787

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EspiniferaCBS89968	12110	N/A	61	12049

Gene Location

Enzyme Prediction help

No EC number prediction in KIW09927.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH64	161	534	3.4e-90	0.9591280653950953

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185759	GH64-GluB-like	3.93e-142	156	534	1	368	glycoside hydrolase family 64: beta-1,3-glucanase B (GluB)-like. This subfamily is represented by GluB, beta-1,3-glucanase B , from Lysobacter enzymogenes Strain N4-7 and related bacterial and ascomycete proteins. GluB is a member of the glycoside hydrolase family 64 (GH64) involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. GluB possesses the conserved Glu and Asp residues required to cleave substrate beta-1,3-glucans. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Based on the structure of laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis, which belongs to the same family as GluB but to a different subfamily, this cd is a two-domain model. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain.
406796	Glyco_hydro_64	3.19e-135	154	534	1	370	Beta-1,3-glucanase. Family 64 glycoside hydrolases have beta-1,3-glucanase activity.
185755	GH64-LPHase-like	7.31e-65	156	534	1	352	glycoside hydrolase family 64: laminaripentaose-producing, beta-1,3-glucanase (LPHase)-like. This subfamily is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain.
185753	GH64-like	2.71e-30	168	535	15	319	glycosyl hydrolase 64 family. This family is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain, and in the Salinispora tropica CNB-440, coagulation factor 5/8 C-terminal domain (FA58C) protein, they are positioned C-terminal of two FA58C domains which are proposed to function as cell surface-attached, carbohydrate-binding domain. This FA58C-containing protein has an internal peptide deletion (of approx. 44 residues) in the LPHase domain II.
223730	Aes	1.48e-23	677	891	113	312	Acetyl esterase/lipase [Lipid transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
2.79e-101	150	534	62	438
1.32e-97	167	535	91	450
1.64e-95	156	539	73	449
3.70e-94	156	534	157	529
4.54e-94	153	534	70	443

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.62e-14	628	871	74	291	Crystal structure of the mutant S202W/I203F of the esterase E40 [uncultured bacterium],5GMS_B Crystal structure of the mutant S202W/I203F of the esterase E40 [uncultured bacterium]
2.68e-14	628	871	76	293	Crystal structure of the mutant M3+S202W/I203F of the esterase E40 [uncultured bacterium],5GMR_B Crystal structure of the mutant M3+S202W/I203F of the esterase E40 [uncultured bacterium],5GMR_C Crystal structure of the mutant M3+S202W/I203F of the esterase E40 [uncultured bacterium],5GMR_D Crystal structure of the mutant M3+S202W/I203F of the esterase E40 [uncultured bacterium]
4.49e-14	637	833	66	242	Crystal structure of Esterase/Lipase from uncultured bacterium [uncultured bacterium]
5.23e-14	637	833	79	255	Structural and Functional Analysis of a Hormone-Sensitive Lipase like EstE5 from a Metagenome Library [uncultured bacterium],3G9T_A Crystal structure of EstE5, was soaked by p-nitrophenyl butyrate for 5sec [uncultured bacterium],3G9U_A Crystal structure of EstE5, was soaked by p-nitrophenyl butyrate for 5min [uncultured bacterium],3G9Z_A Crystal structure of EstE5, was soaked by p-nitrophenyl caprylate [uncultured bacterium],3H17_A Crystal structure of EstE5-PMSF (I) [uncultured bacterium],3H18_A Crystal structure of EstE5-PMSF (II) [uncultured bacterium],3H19_A Crystal structure of EstE5, was soaked by methyl alcohol [uncultured bacterium],3H1A_A Crystal structure of EstE5, was soaked by ethyl alcohol [uncultured bacterium],3H1B_A Crystal structure of EstE5, was soaked by isopropyl alcohol [uncultured bacterium],3L1H_A Crystal structure of EstE5, was soaked by FeCl3 [uncultured bacterium],3L1I_A Crystal structure of EstE5, was soaked by CuSO4 [uncultured bacterium],3L1J_A Crystal structure of EstE5, was soaked by ZnSO4 [uncultured bacterium]
8.89e-14	628	871	78	295	Crystal structure of an esterase from the bacterial hormone-sensitive lipase (HSL) family [environmental samples],4XVC_B Crystal structure of an esterase from the bacterial hormone-sensitive lipase (HSL) family [environmental samples],4XVC_C Crystal structure of an esterase from the bacterial hormone-sensitive lipase (HSL) family [environmental samples],4XVC_D Crystal structure of an esterase from the bacterial hormone-sensitive lipase (HSL) family [environmental samples],4XVC_E Crystal structure of an esterase from the bacterial hormone-sensitive lipase (HSL) family [environmental samples],4XVC_F Crystal structure of an esterase from the bacterial hormone-sensitive lipase (HSL) family [environmental samples],4XVC_G Crystal structure of an esterase from the bacterial hormone-sensitive lipase (HSL) family [environmental samples],4XVC_H Crystal structure of an esterase from the bacterial hormone-sensitive lipase (HSL) family [environmental samples]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.65e-09	614	794	87	255	Arylacetamide deacetylase OS=Bos taurus OX=9913 GN=AADAC PE=2 SV=1
1.23e-08	640	794	83	224	Carboxylesterase NlhH OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=nlhH PE=3 SV=1
1.23e-08	640	794	83	224	Carboxylesterase NlhH OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=nlhH PE=1 SV=1
3.46e-08	635	833	69	248	Esterase OS=Acinetobacter venetianus (strain ATCC 31012 / DSM 23050 / BCRC 14357 / CCUG 45561 / CIP 110063 / KCTC 2702 / LMG 19082 / RAG-1) OX=1191460 GN=est PE=3 SV=2
1.28e-06	641	794	107	255	Arylacetamide deacetylase OS=Homo sapiens OX=9606 GN=AADAC PE=1 SV=5

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.200551	0.799438	CS pos: 43-44. Pr: 0.7202

TMHMM Annotations help

There is no transmembrane helices in KIW09927.1.

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