CAZyme Information: ASPZODRAFT_150690-t33_1-p1

Basic Information

• Species: Penicilliopsis zonata
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicilliopsis; Penicilliopsis zonata
• CAZyme ID: ASPZODRAFT_150690-t33_1-p1
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
919	KV878339|CGC8	99665.76	4.6528

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PzonataCBS506.65	10027	1073090	158	9869

• Gene Location: location=KV878339:1036848-1040072(-)

Full Sequence      

MASSGEKSVFAHFIVGNAAAMTAEQWEADIREAQRAHIDGFALNIATQDSYTDTVLQTAY
AAAETVGNFSLFLSFDYESGGAWPEDRVVSTVNTYKDSSAQFYYQGKPLVSTFEGTSNAG
DWTSIKAATGCSFIPSWTSLGQSGIQTYIDEMDGMLSWDAWPEGAQDMTTTSDEAWIEAL
GNKSYMMPVSPWFYTNLPDYSKNWLWRGDDLWHDRWQQVIELQPPLVEILTWNDYGETHY
IGPIYEAGIPTGAATYVTGNPHDDWRALLPYYIDAYKSNNQTTISTTAEKITYWYRINPS
GSGSANGTTGNDPSQGQPVVNPALVSLDKVFTTVLVAAPSTVTIQIGDADATTLRAVTAG
INHFSVPFNGQTGAVTISVQRNGEEVVSITGPAITDQKIALGLQESQQLAFHLGGQLPEA
QYVPVPSPTPSQERGRETLASASKSTVCPEAYTKPYCEFMTENPTIFHAVDTFTKQLEQH
GYRHLSERAVWTPELRRGGKYYTTRNGSALIAFVVGKEYQSGNGMGIVAGHVDALTARLK
PVSKLPNKTGFAQLAVAPYAGGLNETWWDRDLSIGGRVLVRDPITGKVETRLVKLGWPIA
RIPTLAPHFGAPSQGPFNKETQMVPIVGIDNSDLFQGGEAAQVEGSGIKPGTFAATQPPK
LVKVISGELGITDYSTIVSWELELFDSQPAQVGGLDKDLIFAGRIDDKLCCFAAQEALLA
SPDEMSPGIVKMVGMFDDEEIGSLLRQGARSNFMSSVMERITEAFAASAATYGPNLLAQT
VANSFLVSSDVIHAVNPNFANVYLENHAPRLNVGVAISADPNGHMTTDSVSTAILQRIAH
RCGATLQVFQIRNDSRSGGTIGPMTSARIGMRAIDAGIPQLSMHSIRATTGSLDPGLGVK
LFKGFFDYFEEVDKEFLDF

Enzyme Prediction     

EC	3.2.1.59:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH71	9	389	3.8e-146	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397634	Glyco_hydro_71	0.0	9	388	1	372	Glycosyl hydrolase family 71. Family of alpha-1,3-glucanases.
349908	M18_DAP	0.0	453	906	1	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.
224281	LAP4	2.57e-154	449	906	6	433	Aspartyl aminopeptidase [Amino acid transport and metabolism].
396619	Peptidase_M18	1.26e-150	459	906	1	430	Aminopeptidase I zinc metalloprotease (M18).
349892	M18	6.58e-148	454	906	2	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	1	913	49	977
QRD90422.1|GH71	0.0	5	919	54	927
BCR90909.1|GH71	6.76e-182	21	397	1	394
BCS27549.1|GH71	1.28e-178	1	396	54	466
BCS11256.1|GH71	2.38e-178	1	396	52	453

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JM6_A	7.41e-201	449	915	51	516	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	4.77e-128	450	916	6	467	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	5.25e-128	450	916	9	470	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	1.95e-127	450	916	50	511	Structure of S. cerevesiae mApe1 dodecamer [Saccharomyces cerevisiae]
5JH9_A	2.07e-127	450	916	52	513	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	1.00e-126	450	916	50	511	Vacuolar aminopeptidase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=APE1 PE=1 SV=2
sp|Q2UPZ7|DNPEP_ASPOR	5.42e-94	456	914	16	493	Aspartyl aminopeptidase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=dapA PE=1 SV=1
sp|P38821|DNPEP_YEAST	2.28e-93	445	915	11	487	Aspartyl aminopeptidase 4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=APE4 PE=1 SV=1
sp|O36014|DNPEP_SCHPO	6.68e-90	456	917	12	464	Aspartyl aminopeptidase 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=aap1 PE=1 SV=1
sp|B9RAJ0|DNPEP_RICCO	5.11e-88	459	915	20	486	Probable aspartyl aminopeptidase OS=Ricinus communis OX=3988 GN=RCOM_1506700 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000001

TMHMM  Annotations     

There is no transmembrane helices in ASPZODRAFT_150690-t33_1-p1.