CAZyme Information: H310_04725-t26_1-p1

Basic Information

• Species: Aphanomyces invadans
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
• CAZyme ID: H310_04725-t26_1-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1286		143207.83	6.2289

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AinvadansNJM9701	15416	N/A	168	15248

• Gene Location: location=KI913958:1879117-1884199(+)

Full Sequence      

MRIHTAAIAATATVASMVTALTPKEEYLIFEDDFDSGFDLSVWKHDITLGGNGNREFEVY
VNSRNNSYVKDGKLHLRATLTDEAYGRDSIEGGVMDLWGTSPYSSCSSPQFAGCRKEANG
FDILPPVQSARIQTMESFSFKYGRVEVRTKLPRGDWLWPGIWMMAKDNRYGPWPSSGELD
IMESRGNGPDYKDDKGDPIGNNRFSACFHFGPAWNKDGYPVAVNDTKALPNHRSYGDEFH
TFGFYWDEDEMYAYVDKPENVVTRVADYGKKSFWDIGLESGAWNASDSYNNFQEGPINAP
FDQEMYLIMNVAVGGTSIAKGFLDSGYFPDGQGNKPWHTNDSFPAANFYHQKDKWFPSWT
TNEDMTTTTSGRSSDFSAMQIDSVKVWGIRGLTTSTKSKNEIHRYDDKTTATTTMDCSAT
CPHASSVPTCLEPSTSTCFATTSACFPGTTPCALPAERLVFHDSFDEDRLDLTKWQHEIT
MTGDRTSFMHMSTEDPTNSHVKNGRLVIKPTLSAPVVGFLDNSTVDLWGTSPANQCTSNY
NFGCLQTGNAEKILPPIRSAMLRTEKSFSFRYGRVEVRAKIPTGQWLRPVFRLLPKFDSY
GEWPQSGEIVLFEGRDEGRAVESRVHFGPFNMSTGSSRQVTPLPAPAATNVGSEQSDDRD
AFHVYGLFWDESDLYMYVDSRDNIVSRVEGYGTASLWKSQWGDNESSPYREQRVQAPFDQ
HFYLSLGLRVGGNDGFFPDNIGNKPWNDTSTRHKETFDKALNEWSPTWNAKADSSSLEID
QVSVWATSTASSWTYHGAFDREPEPEAEKLLFSDSFATLDMRRWKPEITMNTGGEFQMYV
NHRQVGFVRNKTLLLRPALSSDIIGNWSLFQGYIDMWGTDLPSKCTAAAASGCGHLNTPQ
DMAPPIHSASFRTAESFSFRYGHVQITATLPAHADYLLPRLRLIPLTSGHAWLDIAVTRT
LPQHHKTTQTVATGYCTNATSCDVAYHEIEPHSTHVYGVIWDATDVVVYLDTPSHVVWHR
PTPPSMHEDMFLVAQVGVGGISSLPHYAFGTFNNQDPSAALPVPWNASAPYPHTQFYRAK
DQWWPSWANKTLNDGHTVGDHSALQVHAVHVWSVRGTKWRAHRVVGDPDVAASLVQVKSP
TAKHEKVVAFTAAYTGTIPLPDHSLVDKLKASLAGLFPGSHHTLYGPVVRGGNVITATVQ
FDPTPSTAIKENTAARGEFKLEETQALVQLHSQGPDSTVDISSPRRTWLWVVGGGLVLAG
VLLFAVSVGTKILRRRMYTSIPERVL

Enzyme Prediction     

EC	3.2.1.39:2	3.2.1.39:2	3.2.1.-:2	3.2.1.39:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	32	387	2.1e-101	0.9968354430379747
GH16	463	785	3e-82	0.9968354430379747
GH16	814	1013	6.7e-28	0.6772151898734177

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185694	GH16_CCF	2.82e-135	28	387	1	329	Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
185694	GH16_CCF	1.45e-85	459	786	1	330	Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
185688	GH16_beta_GRP	2.34e-69	28	388	1	321	beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16. Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
185688	GH16_beta_GRP	1.25e-57	459	786	1	321	beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16. Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
185693	GH16_laminarinase_like	3.01e-56	30	316	1	212	Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAD7089073.1|GH16_4	2.43e-127	28	786	45	728
BAG32349.1|GH16_4	1.89e-87	24	387	37	369
BAG32350.1|GH16_4	1.95e-83	24	387	37	369
AGA16572.1|GH16_4	2.08e-83	28	389	40	374
ABL63380.1|GH16_4	3.72e-83	28	387	48	386

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	5.46e-22	28	315	20	238	Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4DFS_B Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
3AZX_A	6.05e-22	28	315	12	230	Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZX_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZZ_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3B00_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B01_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8]
3ATG_A	3.63e-21	28	315	5	214	endo-1,3-beta-glucanase from Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A	5.04e-19	28	315	9	218	The crystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]
6T2N_AAA	1.30e-16	126	329	129	291	Chain AAA, Glycoside hydrolase family 16 protein [Akkermansia muciniphila],6T2N_BBB Chain BBB, Glycoside hydrolase family 16 protein [Akkermansia muciniphila]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8N0N3|BGBP_PENMO	1.09e-80	28	387	32	359	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
sp|Q9NL89|BGBP_BOMMO	4.91e-32	458	786	184	494	Beta-1,3-glucan-binding protein OS=Bombyx mori OX=7091 PE=1 SV=1
sp|Q76DI2|BGBP_TENMO	9.74e-32	29	386	169	478	Beta-1,3-glucan-binding protein OS=Tenebrio molitor OX=7067 GN=GRP PE=1 SV=1
sp|P23903|E13B_NIACI	2.31e-31	28	315	425	654	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
sp|Q0E666|BGBP1_GALME	2.81e-30	28	389	179	490	Beta-1,3-glucan-binding protein 1 OS=Galleria mellonella OX=7137 GN=bgrp1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000385	0.999591	CS pos: 20-21. Pr: 0.9693

TMHMM  Annotations     

Start	End
1247	1269