CAZyme Information: PYU1_T002514-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PYU1_T002514-p1
• CAZy Family: GH13
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578		63629.42	4.9895

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_SC2008:395226-397219(+)

Full Sequence      

MDASGVRLVPSHARFSEPARSFDVEPSRDDSAWQISALSTPGRSSEPTFGIMYSNNHEPA
LPKEAANMRLVVKKEDGGDARSGAYNGQYRRWPGILLLLAMVAAAVVLITAEAQKSYDDR
VARAKNYELSAKGKRAIKDGLTNTDDIISDDGQVGNPKSYTTATCQQPDYQTKDGKLYAI
AANGTEVPFAIKGVNWFGMETSLAVPFGLWENQQNGTTAYEIASFLARNNFNAVRLPISI
ENVLNNNPPAEGVINKQSNRAINIKNFISTLQSIVASLAYRKIAVLISMHTLTNAKTGGN
WFDASLGVSQDDFLTAVDTVSKNLCNSTYWNVIGLDLKNEPYDAEWGTGTDADFVIGSEK
IAKVMHTNCPKWLGFVEGVVATHTVNIDGKAVSYYDWWGGGLQKAGTNKPKFTIDNKLVW
APHYYTTAVSPQSYFYGANTETDYSTYEELSDDVLKSNIKATMTDMFGYLIEERTSAVVL
GEFAGLYTKDAHPLKTTKRTTDQTIQVMMEGGYAGGFMWSLNPESKYEYNPANVKGAFTE
GLLDDDWLTPNTEFVNAFLPMNSLANLQFLPCFEAEKK

Enzyme Prediction     

No EC number prediction in PYU1_T002514-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	186	525	4e-146	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	3.15e-18	183	530	39	371	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	3.08e-10	208	488	17	241	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABC87089.1|GH5_20	1.94e-261	67	576	66	575
ABK59036.1|GH5_20	1.94e-261	67	576	66	575
ABG80553.1|GH5_20	3.06e-261	33	577	24	577
ABG80552.1|GH5_20	3.06e-261	33	577	24	577
ABJ55765.1|GH5_20	3.95e-259	59	577	60	576

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	1.33e-37	170	549	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	1.33e-37	170	549	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	5.71e-37	170	549	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	7.81e-37	170	549	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	2.73e-36	170	549	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	2.52e-27	183	563	56	393	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P19487|GUNA_XANCP	1.16e-25	191	547	44	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	2.13e-19	164	485	618	937	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
1.000055	0.000000

TMHMM  Annotations     

Start	End
92	111