CAZyme Information: SPRG_12630-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_12630-t26_1-p1
• CAZy Family: GH72
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
510		56007.22	6.2299

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SparasiticaCBS223-65	20435	695850	314	20121

• Gene Location: location=KK583280:68248-70009(-)

Full Sequence      

MLHAEPPLLDDAPPTQRRRKIAMMAAAALVLLGTVVAILVWQFGGTFSDSALGTGKDKST
SPATIAPTPTRQVYSIGKIQDGSVWAPGEDRNPLSYGNQGCQLPNYVSKQGQIFVVGPDK
SETPISIKGINWFGMETINNIPFGLWTNDQNGTTLYEITAFLSRNRFNSVRLPLSVQSLL
RNTPPTAAMVHQDANAALNLTSYVSTIGSIVQALGSRGISVLLDMHNLNATEKGDAWYGN
STTSDEFLRAIDVLTSSFCHASYYNIIGVDLKNEPYGTTWGDNGPKDFRTGAATIANRML
HACSNWLAFVEGNAAKHNITVAGQTSYFFDWWGGGLREAGKFPLQLAVAQKLVYSPHYYS
PSVYPQSYLVNGGKRDGDVLVGYTEYDDATLTDVVNQSADEMFGYLRHVQDGALVLGEFG
GLFTLDAHEKKTTQRVTQNVLRMLKTPGYAGGYMWSLNPESGYEYNPSSVQGSWTEGLLE
KDWVHVNMQYLHALKIMDEMPHVQPFPCLK

Enzyme Prediction     

No EC number prediction in SPRG_12630-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	122	461	1.8e-130	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	1.05e-16	111	487	33	380	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	1.87e-16	119	421	2	238	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABC87087.1|GH5_20	1.73e-152	88	508	155	579
ABK59035.1|GH5_20	1.73e-152	88	508	155	579
ABG80550.1|GH5_20	1.43e-149	68	508	129	573
ABG80551.1|GH5_20	1.43e-149	68	508	129	573
CCA15003.1|GH5_20	1.12e-148	73	508	73	517

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	3.31e-44	122	498	25	377	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	6.38e-44	122	498	25	377	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	3.29e-43	122	498	58	410	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	3.29e-43	122	498	58	410	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	1.20e-42	122	498	58	410	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	9.88e-37	119	487	56	381	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P19487|GUNA_XANCP	2.22e-35	119	497	36	368	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	2.70e-35	103	487	35	371	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P10474|GUNB_CALSA	1.66e-31	119	421	639	937	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P50400|GUND_CELFI	1.03e-28	127	483	63	398	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000028	0.000011

TMHMM  Annotations     

Start	End
21	43