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CAZyme Information: ASPSYDRAFT_95453-t33_1-p1

You are here: Home > Sequence: ASPSYDRAFT_95453-t33_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 sydowii
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii
CAZyme ID ASPSYDRAFT_95453-t33_1-p1
CAZy Family GT8
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
469 KV878600|CGC4 50075.22 6.0995
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AsydowiiCBS593.65 13717 1036612 138 13579
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in ASPSYDRAFT_95453-t33_1-p1.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
406865 AMPK1_CBM 1.56e-44 224 311 1 85
Glycogen recognition site of AMP-activated protein kinase. AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.
398422 AMPKBI 3.20e-31 395 463 1 69
5'-AMP-activated protein kinase beta subunit, interaction domain. This region is found in the beta subunit of the 5'-AMP-activated protein kinase complex, and its yeast homologs Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex. This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known. The isoamylase N-terminal domain (pfam02922) is sometimes found in proteins belonging to this family.
214973 AMPKBI 2.17e-30 364 463 7 99
5'-AMP-activated protein kinase beta subunit, interation domain. This region is found in the beta subunit of the 5'-AMP-activated protein kinase complex, and its yeast homologues Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex. This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known. The isoamylase N-terminal domain is sometimes found in proteins belonging to this family.
199889 E_set_AMPKbeta_like_N 8.05e-26 225 304 1 79
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit. E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.
223021 PHA03247 1.31e-06 9 214 2703 2907
large tegument protein UL36; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 469 1 468
1.24e-202 1 469 1 458
6.69e-200 1 467 1 456
6.69e-200 1 467 1 456
1.61e-191 1 468 1 459

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.05e-36 224 463 4 251
Crystal structure of the heterotrimer core of the S. cerevisiae AMPK homolog SNF1 [Saccharomyces cerevisiae],2QLV_E Crystal structure of the heterotrimer core of the S. cerevisiae AMPK homolog SNF1 [Saccharomyces cerevisiae]
5.13e-23 222 463 10 203
Structure of AMPK in complex with STAUROSPORINE inhibitor and in the absence of a synthetic activator [Rattus norvegicus],4QFR_B Structure of AMPK in complex with Cl-A769662 activator and STAUROSPORINE inhibitor [Rattus norvegicus],4QFS_B Structure of AMPK in complex with Br2-A769662core activator and STAUROSPORINE inhibitor [Rattus norvegicus],5KQ5_B AMPK bound to allosteric activator [Rattus norvegicus],5UFU_B Structure of AMPK bound to activator [Rattus norvegicus]
7.04e-23 222 463 10 203
Structure of AMPK bound to activator [Rattus norvegicus],6E4U_B Structure of AMPK bound to activator [Rattus norvegicus],6E4W_B Structure of AMPK bound to activator [Rattus norvegicus]
9.65e-23 222 463 10 203
AMPK bound to allosteric activator [Rattus norvegicus]
1.15e-22 223 463 2 197
Chain B, 5'-AMP-activated protein kinase subunit beta-2 [Homo sapiens],7JHH_B Chain B, 5'-AMP-activated protein kinase subunit beta-2 [Homo sapiens],7JIJ_B Chain B, 5'-AMP-activated protein kinase subunit beta-2 [Homo sapiens],7M74_B Chain B, 5'-AMP-activated protein kinase subunit beta-2 [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.32e-38 213 462 92 294
5'-AMP-activated protein kinase subunit beta OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=amk2 PE=1 SV=2
7.45e-35 211 463 146 415
SNF1 protein kinase subunit beta-3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GAL83 PE=1 SV=1
4.92e-34 224 463 164 411
SNF1 protein kinase subunit beta-2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SIP2 PE=1 SV=3
3.08e-22 222 463 76 269
5'-AMP-activated protein kinase subunit beta-1 OS=Rattus norvegicus OX=10116 GN=Prkab1 PE=1 SV=4
3.08e-22 222 463 76 269
5'-AMP-activated protein kinase subunit beta-1 OS=Mus musculus OX=10090 GN=Prkab1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000067 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in ASPSYDRAFT_95453-t33_1-p1.