CAZyme Information: H257_07695-t26_2-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_07695-t26_2-p1
• CAZy Family: GH43
• CAZyme Description: hypothetical protein, variant

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
498		54678.37	6.6352

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

• Gene Location: location=KI913129:656230-658292(+)

Full Sequence      

MEDSRRSTNDLGASFSRGSIAFTRDDRSARFEVDVVQPDHQVVLAPLRIGEEGDDHVYIT
ASTENSNSYHSSSHDNPPSSSLSSRPTGINTQYSAHPTVFERPTDVDATSDYRLYDLPSR
GVQPITITYVEETSRSESPKDYKGRLRVWPGLMLLLSIFTLSSVAIAFGAKKSYDSSKSR
MISVQAAAAKRRAIQDGLGDDISEVADDGVVNNPRTYTTKSCSLPNYQSKNGQIVAVSPN
GTEVAVGIKGVNWFGMETLNAVPFGLWQNDQNGTTVFDIASFLQRNGFNSVRLPVSVGHL
LDDTPPAVGLVNRQANRAMNLKSYMTTIQSIVQAMGYRQITVLISMHTLLPNDNSGGLWY
DKNIPEALVLKSFDLLAKGLCSDTYWNVIGIDLKNEPHLATWGDGIPATDWALGAAKLGN
HMLSVCPQWVGFVEGINGGPQTGIIDGKSWVYYNWWGGGLQGAATKAVEFNVPHKLVYSP
HYYTVCIFRYRERPHLAA

Enzyme Prediction     

No EC number prediction in H257_07695-t26_2-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	243	486	6e-98	0.7005813953488372

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	3.16e-15	248	488	47	275	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	1.87e-09	265	484	17	196	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75350.1|GH5_20	2.73e-120	137	483	77	421
ABG76934.1|GH5_20	3.63e-120	137	483	71	415
ABJ97692.1|GH5_20	3.62e-118	137	483	75	419
ABC87088.1|GH5_20	3.49e-117	132	483	69	419
ABC87087.1|GH5_20	6.58e-117	132	488	78	432

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	5.77e-36	240	483	22	266	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	1.10e-35	240	483	22	266	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	4.29e-35	240	483	55	299	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	4.29e-35	240	483	55	299	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]
3QHM_A	4.29e-35	240	483	55	299	Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_B Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_C Crystal analysis of the complex structure, E342A-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	5.55e-34	221	483	32	275	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	5.58e-32	240	488	56	286	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P19487|GUNA_XANCP	8.33e-26	246	488	42	268	Major extracellular endoglucanase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=engXCA PE=1 SV=2
sp|P50400|GUND_CELFI	1.70e-18	248	488	63	311	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
sp|P10474|GUNB_CALSA	2.01e-17	246	489	645	897	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000053	0.000000

TMHMM  Annotations     

Start	End
148	170