dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: An15g00910-T-p1

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Basic Information help

Species

Aspergillus niger

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger

CAZyme ID

An15g00910-T-p1

CAZy Family

GT90

CAZyme Description

Ortholog(s) have AMP-activated protein kinase activity, receptor signaling complex scaffold activity

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
458		49416.86	6.1944

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerCBS513-88	14403	425011	346	14057

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in An15g00910-T-p1.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
406865	AMPK1_CBM	2.19e-42	217	304	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.
214973	AMPKBI	3.06e-31	349	452	3	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.
398422	AMPKBI	4.58e-31	384	452	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.
199889	E_set_AMPKbeta_like_N	3.15e-24	218	298	1	80	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	5.44e-05	8	166	2618	2779	large tegument protein UL36; Provisional

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
0.0	1	458	1	458
0.0	1	457	1	457
0.0	1	457	1	457
2.66e-223	1	456	1	458
1.84e-221	1	456	1	459

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
9.42e-38	217	452	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]
8.91e-23	215	452	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]
1.22e-22	215	452	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]
1.68e-22	215	452	10	203	AMPK bound to allosteric activator [Rattus norvegicus]
2.30e-22	215	452	10	203	AMP-activated protein kinase bound to pharmacological activator R734 [Homo sapiens],6C9G_B AMP-activated protein kinase bound to pharmacological activator R739 [Homo sapiens],6C9H_B non-phosphorylated AMP-activated protein kinase bound to pharmacological activator R734 [Homo sapiens],6C9J_B AMP-activated protein kinase bound to pharmacological activator R734 [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.49e-39	150	451	16	294	5'-AMP-activated protein kinase subunit beta OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=amk2 PE=1 SV=2
1.66e-35	217	452	164	411	SNF1 protein kinase subunit beta-2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SIP2 PE=1 SV=3
6.22e-35	170	452	127	415	SNF1 protein kinase subunit beta-3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GAL83 PE=1 SV=1
3.86e-22	215	452	76	269	5'-AMP-activated protein kinase subunit beta-1 OS=Mus musculus OX=10090 GN=Prkab1 PE=1 SV=2
5.28e-22	215	452	76	269	5'-AMP-activated protein kinase subunit beta-1 OS=Rattus norvegicus OX=10116 GN=Prkab1 PE=1 SV=4

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000051	0.000000

TMHMM Annotations help

There is no transmembrane helices in An15g00910-T-p1.