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CAZyme Information: P168DRAFT_343243-t37_1-p1

You are here: Home > Sequence: P168DRAFT_343243-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 campestris
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
CAZyme ID P168DRAFT_343243-t37_1-p1
CAZy Family GT71
CAZyme Description fibronectin type III domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1011 110596.11 4.7305
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AcampestrisIBT28561 9929 1392248 173 9756
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in P168DRAFT_343243-t37_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH135 472 703 1.2e-21 0.9535864978902954

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
403383 Spherulin4 1.04e-47 476 711 1 238
Spherulation-specific family 4. This protein is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 250 and 398 amino acids in length. There is a conserved NPG sequence motif and there are two completely conserved G residues that may be functionally important. Starvation will often induce spherulation - the production of spores - and this process may involve DNA-methylation. Changes in the methylation of spherulin4 are associated with the formation of spherules, but these changes are probably transient. Methylation of the gene accompanies its transcriptional activation, and spherulin4 mRNA is only detectable in late spherulating cultures and mature spherules. It is a spherulation-specific protein.
238861 SEST_like 6.35e-26 57 311 1 224
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxylic acid.
238020 FN3 1.37e-06 736 817 3 93
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
406036 MU117 7.35e-04 961 993 1 31
Meiotically up-regulated gene family. This protein was identified as being up-regulated during meiosis in S.pombe. This family of proteins is found in largely in plants and fungi. Proteins in this family are typically between 128 and 920 amino acids in length.
238870 SGNH_hydrolase_like_1 0.001 58 152 1 80
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 986 1 1024
0.0 1 986 1 1024
1.26e-126 462 960 490 990
2.13e-123 11 464 9 463
2.15e-123 11 464 9 463

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.77e-13 61 177 7 110
Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297 [Streptomyces albidoflavus]
6.77e-09 61 164 6 96
Crystal structure of extracelular lipase from Streptomyces rimosus at 1.7A resolution [Streptomyces rimosus],5MAL_B Crystal structure of extracelular lipase from Streptomyces rimosus at 1.7A resolution [Streptomyces rimosus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.97e-09 61 164 40 130
Lipase 1 OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO1725 PE=1 SV=1
5.21e-08 61 164 40 130
Lipase OS=Streptomyces rimosus OX=1927 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000799 0.999187 CS pos: 21-22. Pr: 0.9647

TMHMM  Annotations      help

There is no transmembrane helices in P168DRAFT_343243-t37_1-p1.