Species | Saprolegnia parasitica | |||||||||||
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Lineage | Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica | |||||||||||
CAZyme ID | SPRG_21526-t26_1-p1 | |||||||||||
CAZy Family | GT60 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT71 | 180 | 410 | 8.2e-50 | 0.9924242424242424 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
402574 | Mannosyl_trans3 | 5.49e-40 | 180 | 410 | 2 | 273 | Mannosyltransferase putative. This family is conserved in fungi. Several members are annotated as being alpha-1,3-mannosyltransferase but this could not be confirmed. |
404755 | zf-C3HC4_3 | 3.93e-14 | 795 | 842 | 3 | 50 | Zinc finger, C3HC4 type (RING finger). |
319432 | RING-HC_MEX3 | 1.80e-10 | 797 | 836 | 1 | 41 | RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 family. The family includes MEX-3 family phosphoproteins have been found in vertebrates. They are mediators of post-transcriptional regulation in different organisms, and have been implicated in many core biological processes, including embryonic development, epithelial homeostasis, immune responses, metabolism, and cancer. They contain two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. They shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The RNA-binding protein MEX-3 from nematode Caenorhabditis elegans is the founding member of the MEX-3 family. Due to the lack of RING-HC finger, it is not included here. |
319634 | RING-HC_MEX3A | 1.13e-08 | 796 | 835 | 2 | 42 | RING finger, HC subclass, found in RNA-binding protein MEX3A. MEX3A, also known as RING finger and KH domain-containing protein 4 (RKHD4), is a RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It has been implicated in the regulation of tumorigenesis. It controls the polarity and stemness of intestinal epithelial cells through the post-transcriptional regulation of the homeobox transcription factor CDX2, which plays a crucial role in intestinal cell fate specification, both during normal development and in tumorigenic processes involving intestinal reprogramming. Moreover, it exhibits a transforming activity when overexpressed in gastric epithelial cells. MEX3A contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3A shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway. |
319635 | RING-HC_MEX3B | 1.17e-08 | 796 | 836 | 2 | 43 | RING finger, HC subclass, found in RNA-binding protein MEX3B. MEX3B, also known as RING finger and KH domain-containing protein 3 (RKHD3), or RING finger protein 195 (RNF195), is a RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It regulates the spatial organization of the Rap1 pathway that orchestrates Sertoli cell functions. It has a 3' long conserved untranslated region (3'LCU)-mediated fine-tuning system for mRNA regulation in early vertebrate development such as anteroposterior (AP) patterning and signal transduction. MEX3B contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3B shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
5.80e-83 | 119 | 503 | 94 | 491 | |
4.16e-82 | 107 | 508 | 119 | 545 | |
1.17e-81 | 74 | 495 | 139 | 592 | |
4.83e-80 | 95 | 501 | 684 | 1104 | |
5.49e-80 | 119 | 441 | 158 | 488 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.25e-08 | 796 | 846 | 3 | 54 | The RING domain structure of MEX-3C [Homo sapiens],5ZI6_B The RING domain structure of MEX-3C [Homo sapiens],5ZI6_C The RING domain structure of MEX-3C [Homo sapiens],5ZI6_D The RING domain structure of MEX-3C [Homo sapiens],5ZI6_E The RING domain structure of MEX-3C [Homo sapiens],5ZI6_F The RING domain structure of MEX-3C [Homo sapiens],5ZI6_G The RING domain structure of MEX-3C [Homo sapiens],5ZI6_H The RING domain structure of MEX-3C [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.49e-11 | 525 | 847 | 65 | 461 | Putative E3 ubiquitin-protein ligase XBAT35 OS=Arabidopsis thaliana OX=3702 GN=XBAT35 PE=2 SV=1 |
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1.70e-11 | 180 | 418 | 246 | 534 | Alpha-1,2-mannosyltransferase MNN21 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN21 PE=3 SV=1 |
|
3.20e-10 | 194 | 414 | 164 | 437 | Alpha-1,2-mannosyltransferase MNN5 OS=Saccharomyces cerevisiae (strain YJM789) OX=307796 GN=MNN5 PE=3 SV=1 |
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4.22e-10 | 194 | 414 | 164 | 437 | Alpha-1,2-mannosyltransferase MNN5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MNN5 PE=1 SV=2 |
|
9.40e-10 | 525 | 846 | 67 | 374 | Putative E3 ubiquitin-protein ligase XBAT34 OS=Arabidopsis thaliana OX=3702 GN=XBAT34 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000127 | 0.999909 | CS pos: 19-20. Pr: 0.9677 |
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