CAZyme Information: PYU1_T002515-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PYU1_T002515-p1
• CAZy Family: GH131
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
595		65467.67	5.1535

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GultimumDAOMBR144	15430	431595	140	15290

• Gene Location: location=PultDAOMBR144_SC2008:391510-393554(+)

Full Sequence      

MAEYAQQKPHYAPVRPSALDPHEQYSSGKYRSTIVTTEQGSGNSFYDSHPSSASDSLMLS
GGGLNTTFAGRATEMKLTAFEPDGGMPDERPRDYKGRYRRWPGVVLFLALVGAAVALITL
HAINKSDTAAENQTRFEFASQNKRKIQDGLNNSVDLIDDDGQVGNPKKYPDMGCELPNYL
SKNGQIIAQSKNGTEVPVAIKGVNWFGMETGMRIPFGLWENSENGTSTYEISSFLARNKF
NSVRLPVCIKSILDDIPPSKDLINMNTNRAMNVSTYMSTIKSIVKALAYRHVTVMISLHT
LDTKVSGGAWYSDKLDVTEDQFLEAVDMLTSNLCSEEYWNILGLDLKNEPHECSWGGAAP
DWQKGATLIGNHMLKGCKNWMAFVEGINKQHTFNMATVSNGTAKRTYFDWWGGGLQGVAS
GPVVLATEGKVVYAPHYYNTGVNPADYLYGGGTLGAASALLDYVELDDETLKNNVEATFN
DMFGYIAKDKKDAVVLGEFAGLYGKDQHPKLTTKRTTDFTIQAMLDAGLAGGYMWSLNPE
SAYQFNPADTYGHFTEGLLSDDWLSPNKVFLEGMAKMDALPDLRAFPCFPQEVST

Enzyme Prediction     

No EC number prediction in PYU1_T002515-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	195	541	2.7e-142	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	2.39e-18	192	571	39	384	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	1.40e-08	201	501	6	238	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABC87086.1|GH5_20	3.64e-270	71	595	58	578
ABL75350.1|GH5_20	1.44e-267	71	595	59	579
ABC87087.1|GH5_20	3.53e-265	71	595	65	586
ABK59035.1|GH5_20	3.53e-265	71	595	65	586
ABJ97692.1|GH5_20	4.84e-264	71	593	57	575

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	2.49e-35	192	563	22	361	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	3.41e-35	192	563	22	361	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	9.89e-35	192	563	55	394	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	1.35e-34	192	563	55	394	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	4.63e-34	192	563	55	394	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|P19487|GUNA_XANCP	5.03e-30	198	565	42	356	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|P23548|GUN_PAEPO	4.42e-29	179	568	39	372	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	7.05e-26	179	569	46	383	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P10474|GUNB_CALSA	4.63e-21	197	554	644	1005	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
0.999959	0.000085

TMHMM  Annotations     

Start	End
101	123