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CAZyme Information: NEUTE1DRAFT_70190-t26_1-p1

You are here: Home > Sequence: NEUTE1DRAFT_70190-t26_1-p1

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 Neurospora tetrasperma
Lineage Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora tetrasperma
CAZyme ID NEUTE1DRAFT_70190-t26_1-p1
CAZy Family GH74
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1457 156446.51 4.9790
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_NtetraspermaFGSC2508 10380 510951 0 10380
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:3 3.2.1.14:3 3.2.1.14:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 485 839 4.9e-48 0.9425675675675675

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 0.0 484 834 2 345
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 4.15e-54 485 833 3 333
Glyco_18 domain.
395573 Glyco_hydro_18 5.34e-46 486 832 4 305
Glycosyl hydrolases family 18.
119365 GH18_chitinase 2.79e-39 484 731 1 267
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.
405536 Hce2 9.44e-37 1346 1443 1 103
Pathogen effector; putative necrosis-inducing factor. The domain corresponds to the mature part of the Ecp2 effector protein from the tomato pathogen Cladopsorium fulvum. Effectors are low molecular weight proteins that are secreted by bacteria, oomycetes and fungi to manipulate their hosts and adapt to their environment. Ecp2 is a 165 amino acid secreted protein that was originally identified as a virulence factor in C. fulvum, since disruption reduces virulence of the fungus on tomato plants. We have recently determined that Ecp2 is a member of a novel, widely distributed and highly diversified within the fungal kingdom multigene superfamily, which we have designated Hce2, for Homologs of C. fulvum Ecp2 effector. Although Ecp2 is present in most organisms as a small secreted protein, the mature part of this protein can be found fused to other protein domains, including the fungal Glycoside Hydrolase family 18, Glyco_hydro_18 pfam00704 and other, unknown, protein domains. The intrinsic function of Ecp2 remains unknown but it is postulated by that it is a necrosis-inducing factor in plants that serves pathogenicity on the host.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1457 88 1528
0.0 4 1457 29 1480
0.0 2 1457 32 1488
0.0 5 1457 29 1473
0.0 5 1457 23 1458

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.27e-22 505 836 23 344
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
3.32e-22 505 836 23 344
Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
3.32e-22 505 836 23 344
Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
3.37e-22 505 836 23 344
Structure of human chitotriosidase [Homo sapiens]
3.95e-22 505 836 23 344
Crystal structure of human chitotriosidase-1 catalytic domain at 1.0 A resolution [Homo sapiens],4WK9_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (0.3mM) at 1.10 A resolution [Homo sapiens],4WKA_A Crystal structure of human chitotriosidase-1 catalytic domain at 0.95 A resolution [Homo sapiens],4WKF_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (2.5mM) at 1.10 A resolution [Homo sapiens],4WKH_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (1mM) at 1.05 A resolution [Homo sapiens],5NR8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7a [Homo sapiens],5NRA_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7g [Homo sapiens],5NRF_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7i [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.66e-100 292 838 205 716
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
5.72e-21 505 836 44 365
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
2.88e-19 487 734 43 301
Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
2.91e-19 472 734 29 302
Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1
6.87e-19 472 734 29 301
Endochitinase 1 OS=Metarhizium anisopliae OX=5530 GN=chit1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000008 0.000035

TMHMM  Annotations      download full data without filtering help

Start End
1014 1036
1167 1186