CAZyme Information: ASPVEDRAFT_56129-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_56129-t33_1-p1
• CAZy Family: GH55|GH55
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1239		136293.89	5.4827

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878135:172363-176409(-)

Full Sequence      

MALQYTGDRFTIPGWNIQSTRHVQGNSTELSLPGADVSSWYRIGHRATVLGGLVEAGVYN
ESDLFYSNHLSNLNESEFHVPWLYREEFSVPPLAADQRLILDIHGVSSKADIFVNGQQVV
SRDIQNGAYAGRSYDITALVHAGVNALLIQAYPTDYLKDLAVGWADWSPYPPDMGMGVWR
AVELKLIGPVSISPPRVTTNFSHETQEPLAVSITIKTDLANYGTQAQDATVRGVIRLPDT
PLDIALFERVKLPPRSNSIITLNAVLGPAQVKVWWPAAWGSQPLYQVQLAVSLPTNALSD
QSAPTNFALRSVGSSLNAHGENEFTVNGHPFHVRGAGYAPDLFLRFDLQRLEAIFRYTLD
MGLNTIRLEGKQEHPELYHLADRMGIMLIAGWECCDKWEGWTYNEDAQGVKWRDEDYDIG
YASMLHEAEMMQPHPSMLAFLVGSDYWPDERATTRFLSALRRMNWPNPVIASASSRGHPS
QLPPSGMKMEGPYAWVPPNYWYGSEVGAAFGFGSEQGAGVGTPELSSLHRFLSSTDLETL
WTNASAGHYHLSPKGSVFHNRTIYNKALVERYGRPSGLEDYVLKAQIMDYEATRAEFEAF
AARQNASHPATGVIYWMLNSAWPSLHWQLFDYYLRPAGAYFGAKVGARQEHVVLDYGSNT
VYLVNHSLRSKGVRRVTADLIDTNGQTLVHREVTDETAPTSSKEVMSIPEIAKLKLDDVA
FLRLVLSDGFNTTLSRNVYWVTAHVDALDWDASNWYTTPVASYANYTALSNLPPATVKTS
VAVLGRPTPTLTYIEVHLENTGNTPAFFLRLTAQDPNGEELAPTAVSDILRSTSLDLAPY
EDLYRYFHAHPELSLQEESTSQTIAAKLSELNAFDIHANIGGFGLAGVLRNGPGKTVLLR
ADMDALPVKEITGLPYASTVTMRDADGVEKPVMHACGHDMHITCLLAAAEKLVHLRNSWS
GTLIVLFQPNEERGAGAQAMVDDGLYDKIPIPDYAFGQHVMRLRAGTIGSRFGTIMAAAD
SMKITVFGRGGHGSLPHHTIDPVLLAAHIVVRLQGIVSREVDPSDLGVLTVGSLQAGQTE
NIIADRADIGIDFRSVKLETREKIIASVKRIVEAECLASGSPKKPIFTPTRRFPPTVNEH
ALAARLDKEFGEYFGEAFDGDTPRTNVSEDFSTLATCRDIPCSFWFLGGVDEQLWDEATV
KGTTEEIAGNHSALFAPVIQPTMGVGVDALCVAALSYLS

Enzyme Prediction     

EC	3.2.1.165:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	58	709	1.6e-53	0.6436170212765957

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
349914	M20_Acy1-like	0.0	838	1238	1	399	M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
224390	AbgB	5.05e-116	840	1238	14	389	Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only].
349882	M20_Acy1	1.99e-114	840	1235	1	371	M20 Peptidase Aminoacylase 1 family. Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
349916	M20_Acy1-like	5.32e-106	845	1188	8	338	M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
349941	M20_Acy1_YhaA-like	5.15e-103	845	1237	17	384	M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085. Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA63395.1|GH2	0.0	1	1238	1	1266
BCS30719.1|GH2	0.0	1	828	1	828
QRD83268.1|GH2	0.0	7	828	24	841
QMW28734.1|GH2	0.0	7	828	24	841
QMW40806.1|GH2	0.0	7	828	24	841

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VZS_A	2.43e-176	7	828	49	855	Chitosan Product complex of Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2VZS_B Chitosan Product complex of Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2X05_A Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue [Amycolatopsis orientalis],2X05_B Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue [Amycolatopsis orientalis],2X09_A Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue [Amycolatopsis orientalis],2X09_B Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue [Amycolatopsis orientalis]
2VZO_A	9.38e-176	7	828	49	855	Crystal structure of Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2VZO_B Crystal structure of Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis]
2VZT_A	1.84e-175	7	828	49	855	Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine [Amycolatopsis orientalis],2VZT_B Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine [Amycolatopsis orientalis],2VZV_A Substrate Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with chitosan [Amycolatopsis orientalis],2VZV_B Substrate Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with chitosan [Amycolatopsis orientalis]
2VZU_A	9.94e-175	7	823	49	850	Complex of Amycolatopsis orientalis exo-chitosanase CsxA D469A with PNP-beta-D-glucosamine [Amycolatopsis orientalis],2VZU_B Complex of Amycolatopsis orientalis exo-chitosanase CsxA D469A with PNP-beta-D-glucosamine [Amycolatopsis orientalis]
6SLF_A	2.34e-85	821	1238	1	398	Nalpha-acylglutamine aminoacylase from Corynebacterium sp.releasing human axilla odorants co-crystallised with high affinity inhibitor [Corynebacterium striatum],6SLF_B Nalpha-acylglutamine aminoacylase from Corynebacterium sp.releasing human axilla odorants co-crystallised with high affinity inhibitor [Corynebacterium striatum],6SLF_C Nalpha-acylglutamine aminoacylase from Corynebacterium sp.releasing human axilla odorants co-crystallised with high affinity inhibitor [Corynebacterium striatum],6SLF_D Nalpha-acylglutamine aminoacylase from Corynebacterium sp.releasing human axilla odorants co-crystallised with high affinity inhibitor [Corynebacterium striatum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AUH1|EBDG_ARTBC	4.91e-292	7	828	33	845	Exo-beta-D-glucosaminidase ARB_07888 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07888 PE=1 SV=1
sp|Q4R1C4|EBDG_HYPJE	1.33e-271	7	843	30	864	Exo-beta-D-glucosaminidase OS=Hypocrea jecorina OX=51453 GN=gls93 PE=1 SV=1
sp|C0LRA7|EBDG_HYPVI	1.57e-269	7	828	28	851	Exo-beta-D-glucosaminidase OS=Hypocrea virens OX=29875 GN=gls1 PE=2 SV=1
sp|Q82NR8|EBDG_STRAW	4.10e-184	7	828	49	860	Exo-beta-D-glucosaminidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=csxA PE=1 SV=1
sp|Q56F26|EBDG_AMYOR	8.93e-176	7	828	49	855	Exo-beta-D-glucosaminidase OS=Amycolatopsis orientalis OX=31958 GN=csxA PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000019	0.000035

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_56129-t33_1-p1.