logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: PIW_T009684-RA-p1

You are here: Home > Sequence: PIW_T009684-RA-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 Globisporangium iwayamae
Lineage Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
CAZyme ID PIW_T009684-RA-p1
CAZy Family GT1
CAZyme Description Superoxide dismutase [Cu-Zn]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
589 66141.79 6.6341
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034 14874 1223558 0 14874
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT60 338 565 3.9e-60 0.7090909090909091

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
371506 GlcNAc 5.16e-49 287 565 6 349
Glycosyltransferase (GlcNAc). GlcNAc is an enzyme that carries out the first glycosylation step of hydroxylated Skp1, a ubiquitous eukaryotic protein, in the cytoplasm.
238186 Cu-Zn_Superoxide_Dismutase 2.47e-47 3 148 2 143
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].
395033 Sod_Cu 5.23e-47 11 151 3 137
Copper/zinc superoxide dismutase (SODC). superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.
166027 PLN02386 7.29e-43 1 154 1 150
superoxide dismutase [Cu-Zn]
178248 PLN02642 1.89e-30 3 156 9 158
copper, zinc superoxide dismutase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.13e-163 220 588 1 385
9.85e-138 207 588 12 412
8.77e-48 279 588 113 458
7.17e-38 274 589 63 402
1.33e-36 263 588 49 397

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.08e-36 4 157 4 152
X-ray Crystal Structure of an Alvinella pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex [Alvinella pompejana],3F7L_A X-ray Crystal Structure of Alvinella pompejana Cu,Zn Superoxide Dismutase [Alvinella pompejana]
2.71e-35 1 154 1 150
Crystal Structure of Superoxide Dismutase from P. atrosanguina [Potentilla atrosanguinea],2Q2L_B Crystal Structure of Superoxide Dismutase from P. atrosanguina [Potentilla atrosanguinea]
1.57e-34 1 155 4 156
Chain A, Superoxide dismutase [Cu-Zn] [Thermochaetoides thermophila DSM 1495],6ZS1_B Chain B, Superoxide dismutase [Cu-Zn] [Thermochaetoides thermophila DSM 1495],6ZS1_C Chain C, Superoxide dismutase [Cu-Zn] [Thermochaetoides thermophila DSM 1495],6ZS1_D Chain D, Superoxide dismutase [Cu-Zn] [Thermochaetoides thermophila DSM 1495],6ZS1_E Chain E, Superoxide dismutase [Cu-Zn] [Thermochaetoides thermophila DSM 1495],6ZS1_F Chain F, Superoxide dismutase [Cu-Zn] [Thermochaetoides thermophila DSM 1495],6ZS1_G Chain G, Superoxide dismutase [Cu-Zn] [Thermochaetoides thermophila DSM 1495],6ZS1_H Chain H, Superoxide dismutase [Cu-Zn] [Thermochaetoides thermophila DSM 1495]
1.92e-34 3 155 3 152
Mouse SOD1 [Mus musculus],3GTT_B Mouse SOD1 [Mus musculus],3GTT_C Mouse SOD1 [Mus musculus],3GTT_D Mouse SOD1 [Mus musculus],3GTT_E Mouse SOD1 [Mus musculus],3GTT_F Mouse SOD1 [Mus musculus]
2.09e-34 3 157 5 156
Structure of the cytosolic Cu,Zn SOD from S. mansoni [Schistosoma mansoni],1TO4_B Structure of the cytosolic Cu,Zn SOD from S. mansoni [Schistosoma mansoni],1TO4_C Structure of the cytosolic Cu,Zn SOD from S. mansoni [Schistosoma mansoni],1TO4_D Structure of the cytosolic Cu,Zn SOD from S. mansoni [Schistosoma mansoni],1TO5_A Structure of the cytosolic Cu,Zn SOD from S. mansoni [Schistosoma mansoni],1TO5_B Structure of the cytosolic Cu,Zn SOD from S. mansoni [Schistosoma mansoni],1TO5_C Structure of the cytosolic Cu,Zn SOD from S. mansoni [Schistosoma mansoni],1TO5_D Structure of the cytosolic Cu,Zn SOD from S. mansoni [Schistosoma mansoni]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.48e-36 1 154 1 149
Superoxide dismutase [Cu-Zn] 2 OS=Zea mays OX=4577 GN=SODCC.1 PE=2 SV=2
4.28e-36 1 156 1 154
Superoxide dismutase [Cu-Zn] OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=SOD1 PE=1 SV=1
2.14e-35 1 154 3 152
Superoxide dismutase [Cu-Zn] OS=Pinus sylvestris OX=3349 GN=SODCC PE=2 SV=1
2.79e-35 1 154 1 150
Superoxide dismutase [Cu-Zn] OS=Carica papaya OX=3649 GN=SODCC PE=2 SV=1
4.09e-35 1 156 1 154
Superoxide dismutase [Cu-Zn] OS=Claviceps purpurea (strain 20.1) OX=1111077 GN=SOD1 PE=3 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000058 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
209 231