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CAZyme Information: P174DRAFT_510984-t37_1-p1

You are here: Home > Sequence: P174DRAFT_510984-t37_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 Aspergillus novofumigatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
CAZyme ID P174DRAFT_510984-t37_1-p1
CAZy Family GT34
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
356 MSZS01000003|CGC20 37686.82 4.5352
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AnovofumigatusIBT16806 11729 1392255 197 11532
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in P174DRAFT_510984-t37_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH131 19 255 2.3e-100 0.9921568627450981

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
408085 GH131_N 1.54e-78 19 245 1 246
Glycoside hydrolase 131 catalytic N-terminal domain. This is the N-terminal domain found in glycoside hydrolase family 131 (GH131A) protein observed in Coprinopsis cinerea. GH131A exhibits bifunctional exo-beta-1,3-/-1,6- and endo-beta-1,4 activity toward beta-glucan. This domain is catalytic in nature though the catalytic mechanism of C. cinerea GH131A is different from that of typical glycosidases that use a pair of carboxylic acid residues as the catalytic residues. In the case of GH131A, Glu98 and His218 may form a catalytic dyad and Glu98 may activate His218 during catalysis.
236776 PRK10856 3.20e-05 276 332 184 240
cytoskeleton protein RodZ.
139494 PRK13335 5.75e-05 245 345 77 179
superantigen-like protein SSL3; Reviewed.
236776 PRK10856 3.34e-04 276 347 174 244
cytoskeleton protein RodZ.
273167 rad23 0.002 276 329 75 128
UV excision repair protein Rad23. All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.41e-158 1 264 1 262
1.05e-157 1 263 1 261
1.05e-157 1 263 1 261
1.05e-157 1 263 1 261
6.05e-157 1 259 1 257

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.73e-101 17 257 1 244
Chain A, Beta-glucanase [Podospora anserina],4LE3_B Chain B, Beta-glucanase [Podospora anserina],4LE3_C Chain C, Beta-glucanase [Podospora anserina],4LE3_D Chain D, Beta-glucanase [Podospora anserina],4LE4_A Chain A, Beta-glucanase [Podospora anserina],4LE4_B Chain B, Beta-glucanase [Podospora anserina],4LE4_C Chain C, Beta-glucanase [Podospora anserina],4LE4_D Chain D, Beta-glucanase [Podospora anserina]
1.86e-97 17 259 1 237
Chain A, Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea [Coprinopsis cinerea okayama7#130],3W9A_B Chain B, Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea [Coprinopsis cinerea okayama7#130],3W9A_C Chain C, Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea [Coprinopsis cinerea okayama7#130],3W9A_D Chain D, Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea [Coprinopsis cinerea okayama7#130]

Swiss-Prot Hits      help

P174DRAFT_510984-t37_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.009721 0.990268 CS pos: 16-17. Pr: 0.9482

TMHMM  Annotations      help

There is no transmembrane helices in P174DRAFT_510984-t37_1-p1.