dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: XP_001904121.1

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Basic Information help

Species

Podospora anserina

Lineage

Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina

CAZyme ID

XP_001904121.1

CAZy Family

GT66

CAZyme Description

Podospora anserina S mat+ genomic DNA chromosome 5, supercontig 1 [Source:UniProtKB/TrEMBL;Acc:B2AEN2]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
447		48087.08	5.7218

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PanserinaSmat	10888	515849	370	10518

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in XP_001904121.1.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
380801	PFM_jacalin-like	8.08e-13	192	338	1	150	pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin domain, and similar aerolysin-type beta-barrel pore-forming proteins. Jacalin-like lectins are sugar-binding protein domains. Proteins having these lectin domains may bind mono- or oligosaccharides with high specificity. Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).
187706	Jacalin_like	3.01e-08	40	163	1	121	Jacalin-like lectin domain. Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.
187711	Jacalin_EEP	4.21e-06	36	172	1	134	Jacalin-like lectin domains of putative endonucleases/exonucleases/phosphatases and related proteins. Members of this taxonomically diverse family co-occur with metal-dependent endonucleases/exonucleases/phosphatases. They have not been functionally characterized.
212030	LysM	5.26e-06	396	429	2	35	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
187710	griffithsin_like	1.11e-05	72	171	28	128	Jacalin-like lectin domain of griffithsin and related proteins. Griffithsin is a lectin isolated from a red alga, which has shown potential as an inhibitor of viral entry, exhibiting antiviral activity against HIV and SARS. The biological functions of griffithsin and griffithsin-like proteins with respect to their source organisms are not known.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
3.32e-299	1	447	1	447
6.75e-13	340	444	529	632
1.54e-10	335	444	579	687
5.98e-10	367	447	553	631
6.05e-10	367	447	565	643

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
9.47e-28	35	275	11	249	Chain A, Natterin-like protein [Lethenteron camtschaticum],5ZU4_B Chain B, Natterin-like protein [Lethenteron camtschaticum],6IUL_A Chain A, Natterin-like protein [Lethenteron camtschaticum],6IUL_B Chain B, Natterin-like protein [Lethenteron camtschaticum]
2.93e-25	35	333	30	326	Crystal structure of Dln1 complexed with sucrose [Danio rerio],4ZNO_B Crystal structure of Dln1 complexed with sucrose [Danio rerio],4ZNQ_A Crystal structure of Dln1 complexed with Man(alpha1-2)Man [Danio rerio],4ZNQ_B Crystal structure of Dln1 complexed with Man(alpha1-2)Man [Danio rerio],4ZNR_A Crystal structure of Dln1 complexed with Man(alpha1-3)Man [Danio rerio],4ZNR_B Crystal structure of Dln1 complexed with Man(alpha1-3)Man [Danio rerio],5DI0_A Crystal structure of Dln1 [Danio rerio],5DI0_B Crystal structure of Dln1 [Danio rerio]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.08e-24	35	333	10	306	Aerolysin-like protein OS=Danio rerio OX=7955 GN=aep1 PE=1 SV=1
5.57e-10	386	445	380	437	Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03699 PE=1 SV=2
1.96e-07	380	443	355	419	LysM domain-containing protein ARB_01155/01156 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01155/01156 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000457	0.999530	CS pos: 21-22. Pr: 0.9794

TMHMM Annotations help

There is no transmembrane helices in XP_001904121.1.