CAZyme Information: KAG1685053.1

Basic Information

• Species: Phytophthora capsici
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora capsici
• CAZyme ID: KAG1685053.1
• CAZy Family: AA17
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
580		64495.30	4.2949

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcapsiciLT1534	28579	763924	5206	23373

• Gene Location: location=JADEVP010000204:41476-43218(-)

Full Sequence      

MEVTRPMMNVAPADDPHAASFSRTSDYSSGNFSAHLDSSQGPRLSSAVGPGGQRQTEMKL
KAADLDDLQPEQSKDYKGRRRTWPGLLFLLLLIGGAATIIVLQAKETSDLFSVNKEKYER
QQADKRKIKDGMEDDQVIISDDGQVGNPKEYPDMGCELPDYQSKNGQIVAVSKNGTEVPV
GIKGVNWFGMETGLAIPFGLWENMDNGTSVYEVAAFLARNKFNSVRLPVCIKNILNDVAP
EKSLINLNTNRAMNISTYITTIQSVVEALGYRKITVLISLHTLDPKKSGGAWFSEDLGVS
EDEFLSAVDILTKNLCGSKYWNVIGLDLKNEPHECSWGGEDPDWQKGATLIGNRMLEDCP
NWLAFVEGIAGSGTISLNGQEDEVYFDWWGGGMENAGDFPITFDVENKLVWSPHYYNTGV
SPAWYLYASGTQNAEGGRDDYVELDDETLKTNVEKTMEKMFGYLIKTDPNTAMVMGEYAG
LYGKDAHPKLTTKRTTDFTMEVMLKDKYAGAYMWSLNPESAYQYNPADTYGHFTEGLLED
DWLTPNKVFMEGIAAMDEMENLQMFPCFPQEVEGSSSEEE

Enzyme Prediction     

No EC number prediction in KAG1685053.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	177	520	1e-144	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	2.25e-18	174	558	39	392	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	2.31e-07	212	520	28	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABG76934.1|GH5_20	0.0	1	580	1	579
ABC87088.1|GH5_20	0.0	2	578	3	581
UIZ24396.1|GH5_20	0.0	3	577	41	617
ABJ97692.1|GH5_20	0.0	2	580	6	583
ABL75350.1|GH5_20	0.0	2	572	6	577

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	1.76e-41	161	544	8	363	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]
3W6M_A	2.43e-41	161	544	8	363	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]
2ZUM_A	8.59e-41	161	544	41	396	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	1.18e-40	161	544	41	396	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]
3QHO_A	4.19e-40	161	544	41	396	Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHO_B Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHO_C Crystal analysis of the complex structure, Y299F-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|P54583|GUN1_ACIC1	2.34e-32	161	548	46	383	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P23548|GUN_PAEPO	2.15e-29	161	547	39	372	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P19487|GUNA_XANCP	1.09e-26	180	542	42	354	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|P10474|GUNB_CALSA	5.30e-20	171	434	638	909	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
1.000057	0.000000

TMHMM  Annotations     

Start	End
82	104