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CAZyme Information: SAPIO_CDS10803-t41_1-p1

You are here: Home > Sequence: SAPIO_CDS10803-t41_1-p1

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 Scedosporium apiospermum
Lineage Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum
CAZyme ID SAPIO_CDS10803-t41_1-p1
CAZy Family AA7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
866 JOWA01000176|CGC1 97471.44 5.5374
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SapiospermumIHEM14462 10920 N/A 2544 8376
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113:7

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH47 102 572 2.4e-161 0.9955156950672646

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396217 Glyco_hydro_47 0.0 102 572 2 453
Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
240427 PTZ00470 4.17e-126 92 575 70 521
glycoside hydrolase family 47 protein; Provisional
395844 Aminotran_4 1.02e-14 634 856 14 216
Amino-transferase class IV. The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.
169002 PRK07546 1.97e-13 652 860 12 208
hypothetical protein; Provisional
238800 ADCL_like 5.03e-05 772 851 145 221
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.20e-210 44 578 53 575
5.76e-207 30 574 34 588
4.80e-206 42 578 51 575
2.51e-204 44 574 45 569
1.86e-200 46 582 53 575

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.85e-73 92 569 3 470
Penicillium citrinum alpha-1,2-mannosidase complex with glycerol [Penicillium citrinum],2RI8_B Penicillium citrinum alpha-1,2-mannosidase complex with glycerol [Penicillium citrinum],2RI9_A Penicillium citrinum alpha-1,2-mannosidase in complex with a substrate analog [Penicillium citrinum],2RI9_B Penicillium citrinum alpha-1,2-mannosidase in complex with a substrate analog [Penicillium citrinum]
7.20e-73 92 569 38 505
Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KKT_B Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KRE_A Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRE_B Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_A Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_B Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum]
4.97e-67 91 569 2 448
Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5.80e-67 91 569 7 453
Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
5.85e-67 49 569 24 531
Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.60e-75 92 571 37 506
Probable mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mns1B PE=3 SV=1
1.76e-74 83 571 31 513
Mannosyl-oligosaccharide alpha-1,2-mannosidase OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CPSG_02648 PE=1 SV=1
1.08e-73 87 571 35 509
Probable mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mns1B PE=3 SV=1
1.49e-73 87 571 35 509
Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus phoenicis OX=5063 GN=mns1B PE=2 SV=1
3.70e-72 92 569 38 505
Mannosyl-oligosaccharide alpha-1,2-mannosidase OS=Penicillium citrinum OX=5077 GN=MSDC PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.910137 0.089884

TMHMM  Annotations      help

There is no transmembrane helices in SAPIO_CDS10803-t41_1-p1.