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CAZyme Information: XP_001911727.1

You are here: Home > Sequence: XP_001911727.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Podospora anserina
Lineage Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
CAZyme ID XP_001911727.1
CAZy Family GH94
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:B2B6X7]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1019 CU640366|CGC9 111619.05 6.9649
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_001911727.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 465 794 3e-38 0.9256756756756757

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 2.46e-171 465 795 1 344
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753 Glyco_18 6.69e-42 465 795 1 333
Glyco_18 domain.
395573 Glyco_hydro_18 2.72e-33 465 794 1 305
Glycosyl hydrolases family 18.
119351 GH18_chitolectin_chitotriosidase 7.66e-29 496 799 29 344
This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
119365 GH18_chitinase 7.03e-27 467 698 2 267
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1019 1 1019
0.0 1 1019 1 1019
8.55e-196 15 979 10 1023
5.98e-191 15 979 10 1022
3.49e-187 35 998 35 1061

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.23e-24 469 798 7 344
Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
6.35e-23 469 798 7 344
Crystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVG_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)5 (CAD1-E647L-(GlcNAc)5) from Ostrinia furnacalis [Ostrinia furnacalis]
1.17e-21 464 798 1 337
Crystal structure of signalling protein from goat SPG-40 in the presense of N,N',N''-triacetyl-chitotriose at 2.6A resolution [Capra hircus]
1.58e-21 464 798 1 337
Crystal Structure of the goat signalling protein (SPG-40) complexed with a designed peptide Trp-Pro-Trp at 3.2A resolution [Capra hircus],1ZBW_A Crystal structure of the complex formed between signalling protein from goat mammary gland (SPG-40) and a tripeptide Trp-Pro-Trp at 2.8A resolution [Capra hircus],1ZU8_A Crystal structure of the goat signalling protein with a bound trisaccharide reveals that Trp78 reduces the carbohydrate binding site to half [Capra hircus],2AOS_A Protein-protein Interactions of protective signalling factor: Crystal structure of ternary complex involving signalling protein from goat (SPG-40), tetrasaccharide and a tripeptide Trp-pro-Trp at 2.9 A resolution [Capra hircus],2B31_A Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel [Capra hircus],2DSZ_A Three dimensional structure of a goat signalling protein secreted during involution [Capra hircus],2DT0_A Crystal structure of the complex of goat signalling protein with the trimer of N-acetylglucosamine at 2.45A resolution [Capra hircus],2DT1_A Crystal Structure Of The Complex Of Goat Signalling Protein With Tetrasaccharide At 2.09 A Resolution [Capra hircus],2DT2_A Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 2.9A resolution [Capra hircus],2DT3_A Crystal structure of the complex formed between goat signalling protein and the hexasaccharide at 2.28 A resolution [Capra hircus],2O92_A Crystal structure of a signalling protein (SPG-40) complex with tetrasaccharide at 3.0A resolution [Capra hircus],2OLH_A Crystal structure of a signalling protein (SPG-40) complex with cellobiose at 2.78 A resolution [Capra hircus]
5.15e-21 464 798 1 337
Crystal structure of signalling protein from sheep(SPS-40) at 3.0A resolution using crystal grown in the presence of polysaccharides [Ovis aries],1ZBK_A Recognition of specific peptide sequences by signalling protein from sheep mammary gland (SPS-40): Crystal structure of the complex of SPS-40 with a peptide Trp-Pro-Trp at 2.9A resolution [Ovis aries],1ZL1_A Crystal structure of the complex of signalling protein from sheep (SPS-40) with a designed peptide Trp-His-Trp reveals significance of Asn79 and Trp191 in the complex formation [Ovis aries],2DPE_A Crystal structure of a secretory 40KDA glycoprotein from sheep at 2.0A resolution [Ovis aries],2DSU_A Binding of chitin-like polysaccharide to protective signalling factor: Crystal structure of the complex formed between signalling protein from sheep (SPS-40) with a tetrasaccharide at 2.2 A resolution [Ovis aries],2DSV_A Interactions of protective signalling factor with chitin-like polysaccharide: Crystal structure of the complex between signalling protein from sheep (SPS-40) and a hexasaccharide at 2.5A resolution [Ovis aries],2DSW_A Binding of chitin-like polysaccharides to protective signalling factor: crystal structure of the complex of signalling protein from sheep (SPS-40) with a pentasaccharide at 2.8 A resolution [Ovis aries],2FDM_A Crystal structure of the ternary complex of signalling glycoprotein frm sheep (SPS-40)with hexasaccharide (NAG6) and peptide Trp-Pro-Trp at 3.0A resolution [Ovis aries],2G41_A Crystal structure of the complex of sheep signalling glycoprotein with chitin trimer at 3.0A resolution [Ovis aries],2G8Z_A Crystal structure of the ternary complex of signalling protein from sheep (SPS-40) with trimer and designed peptide at 2.5A resolution [Ovis aries]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.58e-68 328 792 227 708
Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
8.49e-24 451 798 9 367
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
2.07e-22 451 798 9 367
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
3.70e-22 451 798 9 367
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
9.38e-22 451 827 9 398
Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000265 0.999711 CS pos: 17-18. Pr: 0.9766

TMHMM  Annotations      help

There is no transmembrane helices in XP_001911727.1.