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CAZyme Information: PUG3_T002934-RA-p1

You are here: Home > Sequence: PUG3_T002934-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 ultimum
Lineage Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
CAZyme ID PUG3_T002934-RA-p1
CAZy Family GH1
CAZyme Description Regulator of chromosome condensation (RCC1)
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1251 141413.73 6.3101
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GultimumBR650 14086 1223559 0 14086
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in PUG3_T002934-RA-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM47 1004 1145 6.7e-20 0.9765625

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
238008 EFh 3.09e-16 83 142 3 62
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
320029 EFh_PI-PLC 4.17e-13 84 189 4 129
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes. PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.
227511 ATS1 1.12e-12 814 974 182 319
Alpha-tubulin suppressor and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton].
238008 EFh 1.90e-12 117 193 1 62
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
227511 ATS1 6.85e-12 811 973 235 374
Alpha-tubulin suppressor and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.71e-14 995 1156 131 279
4.84e-13 995 1151 1352 1495
1.16e-12 991 1149 34 172
1.20e-12 991 1149 44 182
1.20e-12 991 1149 44 182

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.81e-14 794 989 115 308
Structure of the first RCC1-like domain of HERC2 [Homo sapiens],4L1M_B Structure of the first RCC1-like domain of HERC2 [Homo sapiens],4L1M_C Structure of the first RCC1-like domain of HERC2 [Homo sapiens]
9.81e-14 774 904 205 359
Chain A, Ultraviolet-B receptor UVR8 [Arabidopsis thaliana],6XZN_B Chain B, Ultraviolet-B receptor UVR8 [Arabidopsis thaliana]
9.81e-14 774 904 205 359
Chain A, Ultraviolet-B receptor UVR8 [Arabidopsis thaliana],6XZM_B Chain B, Ultraviolet-B receptor UVR8 [Arabidopsis thaliana]
1.28e-13 774 904 202 356
Crystal structure of the W285F mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana],4DNV_B Crystal structure of the W285F mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana],4DNV_C Crystal structure of the W285F mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana],4DNV_D Crystal structure of the W285F mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana]
1.32e-13 774 904 202 356
Crystal structure of UVB-resistance protein UVR8 [Arabidopsis thaliana],4DNW_B Crystal structure of UVB-resistance protein UVR8 [Arabidopsis thaliana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.30e-14 811 948 195 324
E3 ISG15--protein ligase HERC5 OS=Homo sapiens OX=9606 GN=HERC5 PE=1 SV=2
1.71e-13 797 973 302 487
PH, RCC1 and FYVE domains-containing protein 1 OS=Arabidopsis thaliana OX=3702 GN=PRAF1 PE=1 SV=1
8.34e-13 812 948 78 208
E3 ISG15--protein ligase Herc6 OS=Mus musculus OX=10090 GN=Herc6 PE=2 SV=1
8.78e-13 799 989 4211 4395
Probable E3 ubiquitin-protein ligase HERC2 OS=Drosophila melanogaster OX=7227 GN=HERC2 PE=1 SV=3
8.87e-13 793 972 116 290
RCC1 and BTB domain-containing protein 2 OS=Rattus norvegicus OX=10116 GN=Rcbtb2 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000050 0.000002

TMHMM  Annotations      help

There is no transmembrane helices in PUG3_T002934-RA-p1.