dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Arthrobotrys flagrans

Lineage

Ascomycota; Orbiliomycetes; ; Orbiliaceae; Arthrobotrys; Arthrobotrys flagrans

CAZyme ID

RVD87920.1

CAZy Family

GH76

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
645		69404.31	6.0650

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AflagransCBSH-5679	9927	N/A	30	9897

Gene Location

Enzyme Prediction help

EC	3.2.1.15:80

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH28	45	337	3.2e-62	0.8738461538461538

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395231	Glyco_hydro_28	4.36e-121	50	337	1	288	Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes are important in cell wall metabolism.
176528	PI-PLCc_BcPLC_like	2.86e-37	444	634	76	266	Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar proteins. This subfamily corresponds to the catalytic domain present in Bacillus cereus phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and its sequence homologs found in bacteria and eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Their catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This family also includes some uncharacterized eukaryotic homologs, which contains a single TIM-barrel type catalytic domain, X domain. They are similar to bacterial PI-PLCs, and distinct from typical eukaryotic PI-PLCs, which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, and strictly require Ca2+ for their catalytic activities. The prototype of this family is Bacillus cereus PI-PLC, which has a moderate thermal stability and is active as a monomer.
176500	PI-PLCc_bacteria_like	3.67e-23	442	637	80	262	Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins. This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.
215540	PLN03010	3.76e-22	88	325	122	347	polygalacturonase
177865	PLN02218	4.19e-22	50	335	95	388	polygalacturonase ADPG

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.44e-209	1	337	1	338
1.55e-131	5	337	4	330
1.68e-130	25	337	25	337
1.68e-130	25	337	25	337
2.38e-130	25	337	25	337

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.23e-131	34	337	2	304	Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_B Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_C Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_D Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_E Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_F Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_G Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini]
3.20e-129	28	337	5	311	Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
3.20e-129	28	337	5	311	Chain A, endo-polygalacturonase [Evansstolkia leycettana]
3.87e-128	34	337	2	303	Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.08e-113	32	337	1	306	Polygalacturonase From Aspergillus Aculeatus [Aspergillus aculeatus],1IB4_A Crystal Structure of Polygalacturonase from Aspergillus Aculeatus at Ph4.5 [Aspergillus aculeatus],1IB4_B Crystal Structure of Polygalacturonase from Aspergillus Aculeatus at Ph4.5 [Aspergillus aculeatus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
8.89e-128	30	337	26	330	Endopolygalacturonase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pgaB PE=2 SV=2
1.26e-127	34	337	30	330	Probable endopolygalacturonase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=pgaB PE=3 SV=1
2.51e-127	34	337	30	330	Probable endopolygalacturonase A OS=Aspergillus parasiticus OX=5067 GN=pgaA PE=2 SV=1
7.97e-126	34	337	30	330	Endopolygalacturonase A OS=Aspergillus flavus (strain ATCC MYA-384 / AF70) OX=1392242 GN=pgaA PE=2 SV=1
4.65e-125	34	337	31	331	Probable endopolygalacturonase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=pgaB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000680	0.999322	CS pos: 31-32. Pr: 0.4475

TMHMM Annotations help

There is no transmembrane helices in RVD87920.1.

You are here: Home > Sequence: RVD87920.1