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CAZyme Information: SPRG_00039-t26_1-p1

You are here: Home > Sequence: SPRG_00039-t26_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 Saprolegnia parasitica
Lineage Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
CAZyme ID SPRG_00039-t26_1-p1
CAZy Family GT71
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
585 KK583189|CGC3 63032.37 6.2522
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SparasiticaCBS223-65 20435 695850 314 20121
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - -

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
239068 Peptidase_C1A 3.17e-65 127 334 4 210
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) similar to papain, including the mammalian CPs (cathepsins B, C, F, H, L, K, O, S, V, X and W). Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional carboxydipeptidyl activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds. Parasitic CPs act extracellularly to help invade tissues and cells, to hatch or to evade the host immune system. Mammalian CPs are primarily lysosomal enzymes with the exception of cathepsin W, which is retained in the endoplasmic reticulum. They are responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. In addition to its inhibitory role, the propeptide is required for proper folding of the newly synthesized enzyme and its stabilization in denaturing pH conditions. Residues within the propeptide region also play a role in the transport of the proenzyme to lysosomes or acidified vesicles. Also included in this subfamily are proteins classified as non-peptidase homologs, which lack peptidase activity or have missing active site residues.
395062 Peptidase_C1 2.91e-62 126 335 4 212
Papain family cysteine protease.
214761 Pept_C1 9.01e-51 126 334 4 175
Papain family cysteine protease.
240310 PTZ00200 1.88e-45 128 338 239 447
cysteine proteinase; Provisional
185513 PTZ00203 5.51e-41 78 319 76 326
cathepsin L protease; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.37e-211 11 573 11 585
2.24e-185 11 564 6 558
9.52e-183 7 582 9 580
3.44e-51 343 570 305 544
1.35e-44 341 571 250 493

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.90e-42 125 337 5 218
The 2.1 Angstrom Structure Of A Cysteine Protease With Proline Specificity From Ginger Rhizome, Zingiber Officinale [Zingiber officinale],1CQD_B The 2.1 Angstrom Structure Of A Cysteine Protease With Proline Specificity From Ginger Rhizome, Zingiber Officinale [Zingiber officinale],1CQD_C The 2.1 Angstrom Structure Of A Cysteine Protease With Proline Specificity From Ginger Rhizome, Zingiber Officinale [Zingiber officinale],1CQD_D The 2.1 Angstrom Structure Of A Cysteine Protease With Proline Specificity From Ginger Rhizome, Zingiber Officinale [Zingiber officinale]
1.16e-41 126 335 4 215
Ficin A [Ficus carica],4YYQ_B Ficin A [Ficus carica]
6.03e-41 126 338 5 221
The 2.0 A crystal structure of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of Ricinus communis endosperm [Ricinus communis],1S4V_B The 2.0 A crystal structure of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of Ricinus communis endosperm [Ricinus communis]
1.72e-40 127 335 5 216
Actinidin from Actinidia arguta planch (Sarusashi) [Actinidia arguta]
2.06e-40 126 340 7 230
Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin [Hordeum vulgare],2FO5_B Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin [Hordeum vulgare],2FO5_C Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin [Hordeum vulgare],2FO5_D Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin [Hordeum vulgare]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.40e-43 6 334 12 337
Senescence-specific cysteine protease SAG39 OS=Oryza sativa subsp. japonica OX=39947 GN=SAG39 PE=2 SV=2
5.49e-43 89 340 119 379
Cysteine protease 1 OS=Oryza sativa subsp. japonica OX=39947 GN=CP1 PE=2 SV=2
6.09e-43 6 334 12 337
Senescence-specific cysteine protease SAG39 OS=Oryza sativa subsp. indica OX=39946 GN=OsI_14861 PE=3 SV=1
1.23e-42 89 338 99 355
Cysteine protease XCP1 OS=Arabidopsis thaliana OX=3702 GN=XCP1 PE=1 SV=1
1.77e-42 89 334 105 356
Oryzain beta chain OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0670200 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000346 0.999633 CS pos: 17-18. Pr: 0.9754

TMHMM  Annotations      help

There is no transmembrane helices in SPRG_00039-t26_1-p1.