CAZyme Information: SPRG_19057-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_19057-t26_1-p1
• CAZy Family: GT41
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
962		104525.79	6.8383

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

Full Sequence      

MYRASAKVSSAHNDGIWSTVWTSRNQILSGSVDEVVKSWDASSTEDNAILPVVKQFPGHV
LGTLGVAATKDGRRAATSSLDCQVRILNLETGGVEKTIDTGAGETWQVAYSPDGAFVATG
SQQGKINIINVHDEKVVQSIVVEEEKPAKASSSSDAKGKFVLSVAYSPDGKHLACSTFDG
LVAIYDIESGKQLQKYQDRTKPVRSIAYSPDGSFLLAASDDMHVNIYDVAHSSMVASVAG
HISWVLSVACSPDGKHFATGGGDRKVKIWDLAAKSCLYTFECHTDQVWSVAYNETGSRLV
SGGDDALLQLYEVSTASLAHGHIQADIRAGRVPSRGVNLGGWLVAEHWMTASSSIWNGVP
ADRASQGEYHAMSVLGHNVGDAAFESHRRSFLTQADIAQIGAAGLNTVRVPIGYWIRGCG
MLTGPLFQQCSVFAPGGLKYLDMLIQQWARAANVAVLISIHGAPGSQNGNDHSAAVMKGR
VDWPNDPVNVKVTRDLVLFLVQRYKNEQAFLGIGLLNEPDGHMNSHVLFSYYTASYNDVR
SISDCILTMMPRLYNQYAGNGDAMGDFGKGMQNVWIEWHPYLIWGYESYSEAMLLNQGID
SIAKNIANWRGHPLYFGEWSVVTPSNTFSDPNALASFRRKLVTVMNTAQGWAYWTWRADG
DGYGHKWSLRDLLRRMQYPIVRTAANAVGSSPPLSILQSNGVGLSLLTQTQSLAADPAWI
AAMGPLVAERWSYNPSTQQLQSLTSGNCLDAYFDNGLQRHVIHSYSCDGTNANQKWTLVN
HQLSNKGLCLALVDAAINTDLVANRRLVTCDSASTAQFFTLGIAVARLRIASLASLVLSA
SLTFQAPSARDTSQLWLFNHLDYTVMNQGSGQCLDAYEAKVGGAVHLYACSPGNVNQLWR
YNPLTRQLQHMGHAGYCLDVYGPPHLNTCYAMGNAAMWAQALQLEWISYPALTGGYAAVT
SS

Enzyme Prediction     

EC	-	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	385	661	6.7e-39	0.9711191335740073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238121	WD40	3.10e-54	12	312	8	289	WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
238121	WD40	2.03e-48	53	322	2	260	WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
225201	WD40	4.21e-39	7	315	149	443	WD40 repeat [General function prediction only].
293791	7WD40	7.62e-35	26	311	12	293	WD40 repeats in seven bladed beta propellers. The WD40 repeat is found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing, and cytoskeleton assembly. It typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40. Between the GH and WD dipeptides lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel beta-sheet. The WD40 sequence repeat originally described in literature forms the first three strands of one blade and the last strand in the next blade. The C-terminal WD40 repeat completes the blade structure of the N-terminal WD40 repeat to create the closed ring propeller-structure. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands, allowing them to bind either stably or reversibly.
293791	7WD40	1.47e-33	106	315	2	204	WD40 repeats in seven bladed beta propellers. The WD40 repeat is found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing, and cytoskeleton assembly. It typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40. Between the GH and WD dipeptides lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel beta-sheet. The WD40 sequence repeat originally described in literature forms the first three strands of one blade and the last strand in the next blade. The C-terminal WD40 repeat completes the blade structure of the N-terminal WD40 repeat to create the closed ring propeller-structure. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands, allowing them to bind either stably or reversibly.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG56138.1|GH5	AIG56138.1|GH5	3.96e-147	317	932	13	634
UJR33211.1|GH5	UJR33211.1|GH5	1.48e-98	313	675	20	383
UIZ29723.1|GH5	UIZ29723.1|GH5	3.23e-93	323	674	1	356
CCA15900.1|GH5	CCA15900.1|GH5	5.03e-92	314	674	93	448
AIG56251.1|GH5	AIG56251.1|GH5	7.68e-92	313	674	9	397

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EQP_A	1EQP_A	1.76e-29	335	679	10	379	Exo-b-(1,3)-glucanase From Candida Albicans [Candida albicans]
3O6A_A	3O6A_A	4.68e-29	335	679	15	384	F144Y/F258Y Double Mutant of Exo-beta-1,3-glucanase from Candida albicans at 2 A [Candida albicans]
4M80_A	4M80_A	4.68e-29	335	679	15	384	The structure of E292S glycosynthase variant of exo-1,3-beta-glucanase from Candida albicans at 1.85A resolution [Candida albicans SC5314],4M81_A The structure of E292S glycosynthase variant of exo-1,3-beta-glucanase from Candida albicans complexed with 1-fluoro-alpha-D-glucopyranoside (donor) and p-nitrophenyl beta-D-glucopyranoside (acceptor) at 1.86A resolution [Candida albicans SC5314],4M82_A The structure of E292S glycosynthase variant of exo-1,3-beta-glucanase from Candida albicans complexed with p-nitrophenyl-gentiobioside (product) at 1.6A resolution [Candida albicans SC5314]
1CZ1_A	1CZ1_A	5.81e-29	335	679	10	379	Exo-b-(1,3)-glucanase From Candida Albicans At 1.85 A Resolution [Candida albicans],1EQC_A Exo-b-(1,3)-glucanase From Candida Albicans In Complex With Castanospermine At 1.85 A [Candida albicans]
2PF0_A	2PF0_A	6.41e-29	335	679	16	385	Chain A, Hypothetical protein XOG1 [Candida albicans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A2RAR6|EXGA_ASPNC	sp|A2RAR6|EXGA_ASPNC	9.25e-33	335	679	43	403	Probable glucan 1,3-beta-glucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=exgA PE=3 SV=1
sp|Q7Z9L3|EXGA_ASPOR	sp|Q7Z9L3|EXGA_ASPOR	8.36e-32	335	679	32	393	Glucan 1,3-beta-glucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=exgA PE=1 SV=1
sp|B8N151|EXGA_ASPFN	sp|B8N151|EXGA_ASPFN	8.36e-32	335	679	32	393	Probable glucan 1,3-beta-glucosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=exgA PE=3 SV=1
sp|Q5B5X8|EXGA_EMENI	sp|Q5B5X8|EXGA_EMENI	5.03e-31	316	679	9	391	Probable glucan 1,3-beta-glucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=exgA PE=3 SV=2
sp|Q26544|WSL17_SCHMA	sp|Q26544|WSL17_SCHMA	9.54e-31	1	190	1	177	WD repeat-containing protein SL1-17 OS=Schistosoma mansoni OX=6183 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999901	0.000138

TMHMM  Annotations     

There is no transmembrane helices in SPRG_19057-t26_1-p1.