CAZyme Information: PWY79592.1

Basic Information

• Species: Aspergillus heteromorphus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus heteromorphus
• CAZyme ID: PWY79592.1
• CAZy Family: GH28
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
931	MSFL01000015|CGC1	101366.69	4.9121

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AheteromorphusCBS117.55	11436	1448321	306	11130

• Gene Location: location=MSFL01000015:193998-197532(+)

Full Sequence      

MLFAFLISLLLLVGAPAVAATVPQHVFAHFIVGNADAMNSTQWESDITEARAAHIDGFAL
NIAMNCDYNDAVLEKAYAAAEKVGNFTLFLSFDYESDGAWPADQVISTINEYKSRTAQHY
YQGKPLVSTFAGSANAGDWSSIKSATGCFFVPSWTDLGQTGIQEYVDTIDGFFSWDAWPV
GATNKTTVSDVAWMDALPGKAYMMPISPWFYTNLPQWSKNWLWRGDDLWHTRWEQAAELQ
PAFVEIITWNDYGEAHYIGPIHEAGLPTGSASYVMGNPHDAWRTLLPHYIDAYRGGVNGS
NSTSLSYDDKVVYWYHVNPSDAGSANGTTGNNPSMGETAMNPGLLAQDMVFVTALVNSTS
QVYVQIGSSEPTVLQATGGLNQYSVPFNGQTGAVQVSIRRNGKQVVSATGREITEECEDG
NKTVMGFREAAMAYRPSSYGQLPDPVQDYSPKPTATATAPRPATSTAVNPEDYSKPYCDF
MTNNPTIFHAVDGFTKQLESQGYKRLPEREAWKLERGGKYYTSRNASAFIAFSIGSDYQS
GNGMAIVAGHIDALTAKLKPVSKLPTKAGYVQLGVAPYAGALNETWWDRDLAIGGRVLVR
DPSSGKVESKLVKLDWPIARIPTLAPHFGAPSQGPFNKETQMVPIVGVDNSDLFKQATTA
SPFEAGTFAATQPEKLVKVISSELGITDYRTILNWELELYDSQPAQLGGLEKDLIFAGRI
DDKLCCFAAQEALLASPDNTSPGSVKMVGMFDDEEIGSLLRQGARSNFMSSVMERITEAF
APNYGPNVLAQTVANSFFVSSDVIHAVNPNFLNVYLENHAPRLNVGVAVSTDSNGHMTTD
SVSHAFIKRVADRCGSTLQVFQIRNDSRSGGTIGPMTSSRIGMRAIDVGIPQLSMHSIRA
TTGKLDPGLGVQLFKGFFDHFEAVDKEFADF

Enzyme Prediction     

EC	3.2.1.59:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH71	26	408	2e-143	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
349908	M18_DAP	0.0	475	918	2	438	M18 peptidase aspartyl aminopeptidase. Peptidase M18 family, aspartyl aminopeptidase (DAP; EC 3.4.11.21) subfamily, is widely distributed in bacteria and eukaryotes. DAP cleaves only unblocked N-terminal acidic amino-acid residues. It is a cytosolic enzyme and is highly conserved; for example, the human enzyme has 51% identity to an aspartyl aminopeptidase-like protein in Arabidopsis thaliana. The mammalian DAP is highly selective for hydrolysis of N-terminal aspartate or glutamate residues from peptides. Unlike glutamyl aminopeptidase (M42), DAP does not cleave simple aminoaryl-arylamide substrates. Although there is lack of understanding of the function of this enzyme, it is thought to act in concert with other aminopeptidases to facilitate protein turnover because of their restricted specificities for the N-terminal aspartic and glutamic acid, which cannot be cleaved by any other aminopeptidases. The mammalian aspartyl aminopeptidase is possibly contributing to the catabolism of peptides, including those produced by the proteasome. It may also trim the N-terminus of peptides that are intended for the MHC class I system. In humans, DAP has been implicated in the specific function of converting angiotensin II to the vasoactive angiotensin III within the brain. Saccharomyces cerevisiae aminopeptidase I (Ape1) is involved in protein degradation in vacuoles (the yeast lysosomes) where it is transported by the unique cytoplasm-to-vacuole targeting (Cvt) pathway under vegetative growth conditions and by the autophagy pathway during starvation. Its N-terminal propeptide region, which mediates higher-order complex formation, serves as a scaffolding cargo critical for the assembly of the Cvt vesicle for vacuolar delivery. Pseudomonas aeruginosa aminopeptidase (PaAP) shows that its activity is dependent on Co2+ rather than Zn2+, and is thus a cocatalytic cobalt peptidase rather than a zinc-dependent peptidase.
397634	Glyco_hydro_71	1.41e-180	26	407	1	372	Glycosyl hydrolase family 71. Family of alpha-1,3-glucanases.
224281	LAP4	8.61e-153	470	920	6	435	Aspartyl aminopeptidase [Amino acid transport and metabolism].
396619	Peptidase_M18	4.94e-148	480	918	1	430	Aminopeptidase I zinc metalloprotease (M18).
349892	M18	9.36e-146	474	918	1	429	M18 peptidase aminopeptidase family. Peptidase M18 aminopeptidase family is widely distributed in bacteria and eukaryotes, but only the yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized to date. Yeast aminopeptidase I is active only in its dodecameric form with broad substrate specificity, acting on N-terminal leucine and most other amino acids. In contrast, the mammalian aspartyl aminopeptidase is highly selective for hydrolysis of N-terminal Asp or Glu residues from peptides. These enzymes have two catalytic zinc ions at the active site.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA58990.1|GH71	0.0	18	925	49	977
QRD90422.1|GH71	0.0	16	931	39	927
BCS11256.1|GH71	1.01e-194	13	421	47	459
BCR98944.1|GH71	1.01e-194	13	421	47	459
CAK40416.1|GH71	7.93e-188	32	421	16	409

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JM6_A	1.74e-196	424	929	8	518	Structure of Chaetomium thermophilum mApe1 [Thermochaetoides thermophila],5JM6_B Structure of Chaetomium thermophilum mApe1 [Thermochaetoides thermophila],5JM6_C Structure of Chaetomium thermophilum mApe1 [Thermochaetoides thermophila],5JM6_D Structure of Chaetomium thermophilum mApe1 [Thermochaetoides thermophila],5JM6_E Structure of Chaetomium thermophilum mApe1 [Thermochaetoides thermophila],5JM6_F Structure of Chaetomium thermophilum mApe1 [Thermochaetoides thermophila]
4R8F_A	6.19e-124	469	930	4	469	Crystal structure of yeast aminopeptidase 1 (Ape1) [Saccharomyces cerevisiae S288C],4R8F_B Crystal structure of yeast aminopeptidase 1 (Ape1) [Saccharomyces cerevisiae S288C],4R8F_C Crystal structure of yeast aminopeptidase 1 (Ape1) [Saccharomyces cerevisiae S288C],4R8F_D Crystal structure of yeast aminopeptidase 1 (Ape1) [Saccharomyces cerevisiae S288C]
5JGF_A	6.82e-124	469	930	7	472	Crystal structure of mApe1 [Saccharomyces cerevisiae S288C],5JGF_B Crystal structure of mApe1 [Saccharomyces cerevisiae S288C],5JGF_C Crystal structure of mApe1 [Saccharomyces cerevisiae S288C],5JGF_D Crystal structure of mApe1 [Saccharomyces cerevisiae S288C]
5JM9_A	2.50e-123	469	930	48	513	Structure of S. cerevesiae mApe1 dodecamer [Saccharomyces cerevisiae]
5JH9_A	2.66e-123	469	930	50	515	Crystal structure of prApe1 [Saccharomyces cerevisiae S288C],5JH9_B Crystal structure of prApe1 [Saccharomyces cerevisiae S288C],5JH9_C Crystal structure of prApe1 [Saccharomyces cerevisiae S288C],5JH9_D Crystal structure of prApe1 [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P14904|AMPL_YEAST	1.28e-122	469	930	48	513	Vacuolar aminopeptidase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=APE1 PE=1 SV=2
sp|P38821|DNPEP_YEAST	3.61e-96	472	927	17	487	Aspartyl aminopeptidase 4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=APE4 PE=1 SV=1
sp|B9RAJ0|DNPEP_RICCO	5.52e-94	479	927	19	486	Probable aspartyl aminopeptidase OS=Ricinus communis OX=3988 GN=RCOM_1506700 PE=2 SV=2
sp|Q2UPZ7|DNPEP_ASPOR	9.68e-93	477	926	16	493	Aspartyl aminopeptidase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=dapA PE=1 SV=1
sp|O36014|DNPEP_SCHPO	3.10e-89	477	927	12	462	Aspartyl aminopeptidase 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=aap1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000277	0.999684	CS pos: 19-20. Pr: 0.9789

TMHMM  Annotations     

There is no transmembrane helices in PWY79592.1.