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CAZyme Information: NEUDI_157304T0-p1

You are here: Home > Sequence: NEUDI_157304T0-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 Neurospora discreta
Lineage Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora discreta
CAZyme ID NEUDI_157304T0-p1
CAZy Family GH16
CAZyme Description Mannosyl-oligosaccharide alpha-1,2-mannosidase and related glycosyl hydrolases
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
965 108089.73 5.1525
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_NdiscretaFGSC8579 10345 510953 397 9948
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 216 963 2.1e-183 0.9932735426008968

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396217 Glyco_hydro_47 0.0 216 963 3 453
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 1.83e-84 144 964 13 519
glycoside hydrolase family 47 protein; Provisional
411607 Chlamy_inclu_1 0.003 37 111 18 95
inclusion-associated protein. Proteins of this family are inclusion-associated proteins in Chlamydia. It has been shown that protein CPj0783, which is identical to the HMM seed protein WP_010892266, was localized on Chlamydial inclusion. CPj0783 interacted with host Huntingtin-protein14, which may play an important role in disturbing the vesicle transport system to escape host lysosomal or autophagosomal degradation.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 965 1 882
1.76e-314 1 965 1 898
3.49e-312 1 965 1 971
6.22e-283 87 965 109 1043
1.00e-274 5 964 5 1026

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.97e-35 210 961 25 465
Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus],5KKB_B Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus]
5.71e-35 210 961 23 463
Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases) [Mus musculus]
4.34e-34 206 960 4 470
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-34 206 960 39 505
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]
1.95e-32 218 406 16 193
Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.81e-35 190 962 24 507
Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mns1B PE=1 SV=1
1.81e-35 190 962 24 507
Probable mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=mns1B PE=3 SV=2
1.06e-33 169 661 158 508
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Homo sapiens OX=9606 GN=MAN1A2 PE=1 SV=1
1.06e-33 183 661 158 508
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Mus musculus OX=10090 GN=Man1a2 PE=1 SV=1
2.10e-33 210 961 200 640
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA OS=Mus musculus OX=10090 GN=Man1a1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000037 0.000007

TMHMM  Annotations      download full data without filtering help

Start End
7 26