logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: KID71072.1

You are here: Home > Sequence: KID71072.1

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 Metarhizium anisopliae
Lineage Ascomycota; Sordariomycetes; ; Clavicipitaceae; Metarhizium; Metarhizium anisopliae
CAZyme ID KID71072.1
CAZy Family GT31
CAZyme Description Concanavalin A-like lectin/glucanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1083 AZNF01000001|CGC15 114161.02 6.4141
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_ManisopliaeARSEF549 10891 1276135 0 10891
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KID71072.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 50 280 2.4e-85 0.9563318777292577

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
185690 GH16_fungal_Lam16A_glucanase 2.51e-153 3 301 1 293
fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Group of fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Lam16A belongs to the 'nonspecific' 1,3(4)-beta-glucanase subfamily, although beta-1,6 branching and beta-1,4 bonds specifically define where Lam16A hydrolyzes its substrates, like curdlan (beta-1,3-glucan), lichenin (beta-1,3-1,4-mixed linkage glucan), and laminarin (beta-1,6-branched-1,3-glucan).
185693 GH16_laminarinase_like 1.45e-15 63 267 54 222
Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
396406 WSC 2.07e-13 545 623 1 80
WSC domain. This domain may be involved in carbohydrate binding.
223039 PHA03307 6.72e-08 739 1070 51 406
transcriptional regulator ICP4; Provisional
237057 PRK12323 1.65e-07 880 1042 396 576
DNA polymerase III subunit gamma/tau.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1083 1 1120
1.17e-209 3 728 2 601
3.37e-189 3 635 78 526
4.30e-163 3 286 2 285
1.36e-157 3 638 2 457

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.14e-77 3 300 2 297
Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila'],5JVV_B Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila']
3.03e-72 4 300 2 295
The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_B The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_C The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_D The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila']
3.12e-72 4 300 3 296
The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_B The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_C The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_D The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDV_A The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_B The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_C The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_D The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila']
1.99e-71 4 300 1 294
The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_B The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_C The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_D The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila']
2.12e-71 4 300 3 296
The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDW_B The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDX_A The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila'],3WDX_B The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila']

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.11e-75 2 307 18 321
Endo-1,3(4)-beta-glucanase ARB_04519 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_04519 PE=3 SV=1
1.16e-73 4 301 31 326
Probable endo-1,3(4)-beta-glucanase AFLA_105200 OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=AFLA_105200 PE=3 SV=1
2.18e-73 4 301 31 326
Probable endo-1,3(4)-beta-glucanase AO090023000083 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=AO090023000083 PE=3 SV=1
3.55e-72 3 301 128 418
Probable glycosidase C21B10.07 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBC21B10.07 PE=3 SV=1
5.52e-70 3 301 31 327
Probable endo-1,3(4)-beta-glucanase AFUB_029980 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=AFUB_029980 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999932 0.000126

TMHMM  Annotations      help

There is no transmembrane helices in KID71072.1.