CAZyme Information: H310_04989-t26_1-p1

Basic Information

• Species: Aphanomyces invadans
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
• CAZyme ID: H310_04989-t26_1-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
577	KI913959|CGC2	63096.01	7.7221

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=KI913959:857785-859780(-)

Full Sequence      

MATSPRVTSPRAVPDDDDSQPRSPTEYKRFSSSNFVTDGSQESSTSVQEPTTKGGTLTHH
KKDGNIARERKNQPTTSNVIKSWWKRVLFLVIVVSGIMAGIVLVILKLVQQNGATSPTGT
NGGYSVPTPTSDPLAPSAGRIDDGSAFSAESFPVGVNPVKYPPQACKLPQYTSSNGKIYV
QGPNGFPQPVSIKGISWAGMETADAIPYGLWHSPTNGTTVFQLAAFLARNNFNSVRLPLC
IESILNDRRPNPDLINTAANRAINSQSYMGLLSSIIRAFAFRKMSVLLDLHTLTPTDAGG
SWTSDNLSELSYLAAVDVLATKLCNDQHWNVIGIDLKNKPYAATWGDNGPNDWAIGAPRI
ANRMLKGCPNWLAFVQGTVAKHTLRSDDNTQVFTYTDWWGGGLQNEATAPLKLSIPSKLV
YAPHYYSPSEYPQSYFVQNGVRDHDLMVGYTEYTNETLKRRVAATMSDMFGFLTQYQQGA
VVLGEFGGLYAKDAFANLTNRRVIELTMDVASQPGFAGGYVWALNPETQYEYNPSNTKGS
WQEGLVGDTWTTANGPYLTALKKLDSLPYLQPWPCVS

Enzyme Prediction     

No EC number prediction in H310_04989-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	189	528	1.2e-133	0.9912790697674418

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	5.99e-18	171	565	28	391	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	2.57e-11	209	491	17	241	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75349.1|GH5_20	3.88e-152	84	575	145	627
ABG80555.1|GH5_20	8.58e-149	137	575	196	632
ABG80554.1|GH5_20	8.58e-149	137	575	196	632
ABC87090.1|GH5_20	5.25e-146	137	575	191	627
ABK59037.1|GH5_20	5.25e-146	137	575	191	627

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	5.07e-38	184	564	22	375	Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
3VVG_A	6.97e-38	184	564	22	375	The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
2ZUM_A	3.02e-37	184	564	55	408	Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_A Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_B Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_C Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3AXX_A	4.13e-37	184	564	55	408	Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],3AXX_B Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],3AXX_C Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3QHN_A	7.73e-37	184	564	55	408	Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_B Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_C Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23548|GUN_PAEPO	2.11e-29	155	556	24	373	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	6.27e-26	189	554	61	381	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000051	0.000000

TMHMM  Annotations     

Start	End
87	109