Species | Saprolegnia parasitica | |||||||||||
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Lineage | Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica | |||||||||||
CAZyme ID | SPRG_15973-t26_1-p1 | |||||||||||
CAZy Family | GT20 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM47 | 119 | 235 | 5.7e-19 | 0.8984375 |
CBM20 | 4 | 87 | 6e-17 | 0.8555555555555555 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
237999 | CAP_ED | 4.75e-17 | 363 | 477 | 1 | 115 | effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels |
395557 | CBM_20 | 6.19e-17 | 3 | 87 | 2 | 82 | Starch binding domain. |
215006 | CBM_2 | 1.03e-15 | 3 | 91 | 2 | 87 | Starch binding domain. |
119437 | CBM20 | 3.88e-14 | 4 | 87 | 2 | 81 | The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. |
197516 | cNMP | 4.66e-12 | 363 | 470 | 1 | 107 | Cyclic nucleotide-monophosphate binding domain. Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
6.83e-13 | 65 | 238 | 519 | 694 | |
8.26e-13 | 89 | 240 | 576 | 725 | |
9.99e-13 | 94 | 240 | 924 | 1064 | |
8.27e-12 | 89 | 252 | 152 | 309 | |
1.61e-11 | 93 | 238 | 911 | 1052 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.05e-09 | 361 | 462 | 20 | 114 | M. loti cyclic-nucleotide binding domain mutant displaying inverted ligand selectivity, cyclic-GMP bound [Mesorhizobium japonicum MAFF 303099],4MUV_B M. loti cyclic-nucleotide binding domain mutant displaying inverted ligand selectivity, cyclic-GMP bound [Mesorhizobium japonicum MAFF 303099] |
|
3.49e-09 | 361 | 462 | 16 | 110 | Chain A, cyclic nucleotide binding domain [Mesorhizobium japonicum MAFF 303099],1U12_B Chain B, cyclic nucleotide binding domain [Mesorhizobium japonicum MAFF 303099] |
|
3.49e-09 | 361 | 462 | 16 | 110 | M.loti ion channel cylic nucleotide binding domain [Mesorhizobium loti],1VP6_C M.loti ion channel cylic nucleotide binding domain [Mesorhizobium loti] |
|
3.64e-09 | 361 | 462 | 18 | 112 | M. loti cyclic-nucleotide binding domain, cyclic-GMP bound [unidentified],3CL1_B M. loti cyclic-nucleotide binding domain, cyclic-GMP bound [unidentified] |
|
3.80e-09 | 361 | 462 | 20 | 114 | Chain A, Mll3241 protein [unidentified],2KXL_A Solution structure of a bacterial cyclic nucleotide-activated K+ channel binding domain in the unliganded state [Mesorhizobium loti] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.13e-07 | 361 | 462 | 233 | 327 | Cyclic nucleotide-gated potassium channel mll3241 OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=mll3241 PE=1 SV=1 |
|
2.99e-06 | 308 | 466 | 204 | 359 | cAMP-dependent protein kinase type I-alpha regulatory subunit OS=Rattus norvegicus OX=10116 GN=Prkar1a PE=1 SV=2 |
|
2.99e-06 | 308 | 466 | 204 | 359 | cAMP-dependent protein kinase type I-alpha regulatory subunit OS=Mus musculus OX=10090 GN=Prkar1a PE=1 SV=3 |
|
5.24e-06 | 308 | 466 | 203 | 358 | cAMP-dependent protein kinase type I-alpha regulatory subunit OS=Bos taurus OX=9913 GN=PRKAR1A PE=1 SV=2 |
|
5.25e-06 | 308 | 466 | 204 | 359 | cAMP-dependent protein kinase type I-alpha regulatory subunit OS=Homo sapiens OX=9606 GN=PRKAR1A PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.998738 | 0.001298 |
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