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CAZyme Information: KLU90628.1

You are here: Home > Sequence: KLU90628.1

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 Magnaporthiopsis poae
Lineage Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
CAZyme ID KLU90628.1
CAZy Family GH72
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A0C4ECP8]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1471 160738.64 7.5121
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MpoaeATCC64411 12363 644358 200 12163
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KLU90628.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 135 448 5.6e-23 0.9155405405405406

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 1.26e-23 151 439 26 334
Glyco_18 domain.
395573 Glyco_hydro_18 4.67e-22 135 439 1 307
Glycosyl hydrolases family 18.
119357 GH18_zymocin_alpha 1.25e-18 135 437 1 343
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.
119365 GH18_chitinase 8.81e-17 133 439 11 322
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.
395135 Chitin_bind_1 2.05e-13 72 108 1 35
Chitin recognition protein.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.91e-298 29 1454 38 1558
1.77e-286 29 1454 38 1569
1.90e-241 104 1448 28 1445
1.90e-241 104 1448 28 1445
3.90e-159 106 1453 51 1623

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.24e-13 153 460 32 361
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
6.29e-13 153 460 32 361
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]
6.29e-13 153 460 32 361
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]
6.92e-13 153 460 32 361
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]
7.13e-13 153 460 32 361
Crystal structure of human chitotriosidase-1 (hChit1) catalytic domain in complex with compound 2-8-14 [Homo sapiens],6JK6_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 2-8-s2 [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.84e-12 153 460 53 382
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
2.35e-11 153 439 53 361
Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
2.74e-10 181 439 89 375
Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
6.86e-10 153 439 53 365
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
1.58e-09 153 439 53 365
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999146 0.000908

TMHMM  Annotations      help

There is no transmembrane helices in KLU90628.1.