CAZyme Information: PYU1_T009031-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PYU1_T009031-p1
• CAZy Family: GT1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
350		38517.94	4.7848

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_SC1987:241717-242961(-)

Full Sequence      

MCYEIASFLARNNFNSVRLPISLASVLHDTAPDLAFVNASENRALRLDNYTSTLQSIIKA
FAYRQISVLISVDATTKAGTNISEEGYLHAIDKLTSSLCTSSYWNVLGLDLRSESGQNTT
WGDGSATDFRAAATRIGNRMLQGCPSWLVFVRGIHESDDHLETGETYGFDAWSRGGGLSK
TKEFPVTLSIPDKVVYAPHFYLPGVVPSANDVYTQRDSATELSDAELQETVRDAFDRMIG
QLATEPERPAIVLSGFGGLYLEDKSSYRTSQRTVDYTVKLISEALGLIGGYAWALNPETS
FTRHGQAAQEGLVTSDWRTANEPYLEALESLNEIPHLSATQCFPLNSSRR

Enzyme Prediction     

No EC number prediction in PYU1_T009031-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	2	299	8e-88	0.9011627906976745

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	7.08e-06	4	300	77	364	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA19804.1|GH5_20	3.40e-86	3	349	166	527
CCA15003.1|GH5_20	5.59e-85	3	343	163	518
CCA25494.1|GH5_20	5.59e-85	3	343	163	518
ABG80550.1|GH5_20	2.44e-83	3	348	218	579
ABG80551.1|GH5_20	2.44e-83	3	348	218	579

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	5.56e-23	14	331	65	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]
3W6M_A	5.56e-23	14	331	65	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]
3QHM_A	8.31e-23	14	331	98	408	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]
2ZUM_A	1.13e-22	14	331	98	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	1.53e-22	14	331	98	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23548|GUN_PAEPO	6.81e-18	11	328	88	378	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	6.19e-14	14	330	99	393	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
0.999948	0.000076

TMHMM  Annotations     

There is no transmembrane helices in PYU1_T009031-p1.