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CAZyme Information: QSL66615.1

You are here: Home > Sequence: QSL66615.1

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 Pneumocystis wakefieldiae
Lineage Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis wakefieldiae
CAZyme ID QSL66615.1
CAZy Family GT50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1331 CP054544|CGC1 155174.85 7.8815
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Pwakefieldiae2A 3223 N/A 41 3182
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in QSL66615.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT22 14 391 8.3e-94 0.9948586118251928

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
341064 M1_APN-Q_like 0.0 533 922 54 442
Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1). This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.
223385 PepN 3.93e-170 540 1317 85 859
Aminopeptidase N [Amino acid transport and metabolism].
396150 Peptidase_M1 7.84e-101 703 920 1 220
Peptidase family M1 domain. Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase, this enzyme also has an aminopeptidase activity.
341065 M1_APN 1.94e-94 598 920 120 437
Peptidase M1 family including aminopeptidase N catalytic domain. This model represents the catalytic domain of bacterial and eukaryotic aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.
341058 M1 7.85e-90 549 907 64 413
Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 hydrolase. The model represents the catalytic domains of M1 peptidase family members including aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile upon activation during catalysis. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. APN expression is dysregulated in many inflammatory diseases and is enhanced in numerous tumor cells, making it a lead target in the development of anti-cancer and anti-inflammatory drugs. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different, but overlapping sites. The activity and physiological relevance of the aminopeptidase in LTA4H is as yet unknown, while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4), a potent chemotaxin that is fundamental to the inflammatory response of mammals.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1331 1 1331
2.09e-109 25 493 30 503
2.89e-109 25 493 30 503
2.89e-109 25 493 30 503
2.04e-105 17 493 33 523

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.95e-118 541 1324 88 877
Crystal structure of human aminopeptidase A [Homo sapiens],4KX8_A Crystal structure of human aminopeptidase A complexed with amastatin [Homo sapiens],4KX9_A Crystal structure of human aminopeptidase A complexed with arginine [Homo sapiens],4KXA_A Crystal structure of human aminopeptidase A complexed with aspartate and calcium [Homo sapiens],4KXB_A Crystal structure of human aminopeptidase A complexed with bestatin [Homo sapiens],4KXC_A Crystal structure of human aminopeptidase A complexed with glutamate [Homo sapiens],4KXD_A Crystal structure of human aminopeptidase A complexed with glutamate and calcium [Homo sapiens]
2.72e-108 554 1323 95 872
Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity. [Homo sapiens],5MJ6_B Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity. [Homo sapiens]
4.22e-108 554 1322 96 872
Crystal Structure of Human Insulin Regulated Aminopeptidase with Alanine in Active Site [Homo sapiens],4P8Q_B Crystal Structure of Human Insulin Regulated Aminopeptidase with Alanine in Active Site [Homo sapiens],4PJ6_A Crystal Structure of Human Insulin Regulated Aminopeptidase with Lysine in Active Site [Homo sapiens],4PJ6_B Crystal Structure of Human Insulin Regulated Aminopeptidase with Lysine in Active Site [Homo sapiens]
5.37e-108 554 1323 126 903
Insulin regulated aminopeptidase [Homo sapiens],5C97_B Insulin regulated aminopeptidase [Homo sapiens],6YDX_A Insulin-regulated aminopeptidase complexed with a macrocyclic peptidic inhibitor [Homo sapiens],6YDX_B Insulin-regulated aminopeptidase complexed with a macrocyclic peptidic inhibitor [Homo sapiens]
5.37e-108 554 1323 126 903
Crystal structure of insulin regulated aminopeptidase in complex with ligand [Homo sapiens],4Z7I_B Crystal structure of insulin regulated aminopeptidase in complex with ligand [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.09e-270 545 1328 89 882
Aminopeptidase 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ape1 PE=3 SV=1
1.17e-257 531 1327 126 922
Aminopeptidase 2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=APE2 PE=1 SV=3
1.09e-250 524 1327 149 951
Aminopeptidase 2, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=APE2 PE=1 SV=4
3.37e-242 533 1327 62 854
Alanine/arginine aminopeptidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=AAP1 PE=1 SV=2
1.65e-165 534 1322 116 910
Puromycin-sensitive aminopeptidase OS=Mus musculus OX=10090 GN=Npepps PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000004 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
7 25
61 80
87 109
119 138
145 162
172 194
207 229
259 281
286 303
307 329
336 353