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CAZyme Information: ALNC14_116950:RNA-p1

You are here: Home > Sequence: ALNC14_116950:RNA-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 Albugo laibachii
Lineage Oomycota; NA; ; Albuginaceae; Albugo; Albugo laibachii
CAZyme ID ALNC14_116950:RNA-p1
CAZy Family GT4
CAZyme Description phosphatidylinositol kinase putative
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1366 155456.47 8.8283
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AlaibachiiNc14 14629 890382 180 14449
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in ALNC14_116950:RNA-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 1235 1361 1e-27 0.5058823529411764

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
173825 ascorbate_peroxidase 8.62e-61 1237 1365 136 253
Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
406545 N_BRCA1_IG 1.51e-41 564 661 1 101
Ig-like domain from next to BRCA1 gene. Domain present between positions 365-485 in the human next to BRCA1 gene 1 protein Q14596 (NBR1_HUMAN) Distant homology and fold prediction analysis suggests this domain has an immunoglobulin like fold and is distantly homologous to domains involved in cell adhesion such as CARDB (PF07705). JCSG construct was crystalized confirming the domain boundaries
271343 NBR1_like 4.53e-41 557 662 5 112
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins. NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.
178218 PLN02608 2.72e-37 1228 1361 117 243
L-ascorbate peroxidase
178467 PLN02879 1.38e-30 1225 1363 128 248
L-ascorbate peroxidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.29e-42 1233 1364 198 329
8.06e-40 1237 1364 220 348
3.22e-38 1237 1364 4 132
1.63e-37 1237 1366 220 350
1.63e-37 1237 1366 220 350

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.50e-34 1237 1361 133 258
Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
9.68e-34 1237 1361 133 258
Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
1.02e-33 1237 1361 133 258
Structure of Leishmania major peroxidase D211R mutant (high res) [Leishmania major],5ALA_A Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major],5ALA_B Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major]
1.05e-33 1237 1361 134 259
The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin]
1.05e-33 1237 1361 134 259
The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin],3RIW_B The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.52e-48 922 1211 262 549
Phosphatidylinositol 4-kinase gamma 4 OS=Oryza sativa subsp. japonica OX=39947 GN=PI4KG4 PE=1 SV=1
4.87e-46 853 1188 181 532
Phosphatidylinositol 4-kinase gamma 4 OS=Arabidopsis thaliana OX=3702 GN=PI4KG4 PE=1 SV=1
2.46e-45 923 1209 263 560
Phosphatidylinositol 4-kinase gamma 3 OS=Arabidopsis thaliana OX=3702 GN=PI4KG3 PE=2 SV=1
8.37e-42 907 1202 154 462
Phosphatidylinositol 4-kinase gamma 7 OS=Arabidopsis thaliana OX=3702 GN=PI4KG7 PE=1 SV=2
3.40e-41 910 1202 149 458
Phosphatidylinositol 4-kinase gamma 6 OS=Arabidopsis thaliana OX=3702 GN=PI4KG6 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000060 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in ALNC14_116950:RNA-p1.