CAZyme Information: SPRG_12186-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_12186-t26_1-p1
• CAZy Family: GH6
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
546		58933.28	5.7861

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=KK583263:109315-111014(+)

Full Sequence      

MRPSEDIMAVPETAANVGDGKSVRRKQKFGGRRSVWPGALALTLGILGAIGGLSYWGVTS
HQDMLNRQPNNADLALIYGSGTTITDGSGTTTNSSALPLSVTNPTEYEDKGCAQINYVTN
NNQIIMQTSSSNKPLVFKGVNWRGMEGWDHVITGLWDGARDGNTLYQIGSFLAKNGFNAV
RFPIDVDATARNIMVKTNFNTNSQRALASLNRYIQVLTALTEGLGQFQIAVVFDFNTRSV
ADLNQTDRSVMDWSLRNSSDDLQGNGWENINVKLAQYELAVQGLATAMCNAKHWNVVGID
VKDVPAGASGQWDGDEKTNWSSFATKVGNAILKACPQWLVFVQGMTTSSKFGSDDAAKTI
TDWPGASLSSAVQSPITLSTPNKVVYAPPFWTPSLYPQPYFFKESKGLSMLSSYTEFPDA
ASLQASIDDAMTKMFTGLLTSTTAPVVLSYFGGLYGTDDLYPKGTASRVIDCIINRMTSG
DKPIAGGFWYALNPDQSWPHPGPNSSIPQSGGLLDATWRAANPNQLAATTKMNDMPGLGL
VTCDPR

Enzyme Prediction     

No EC number prediction in SPRG_12186-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	133	495	7.7e-98	0.9912790697674418

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	3.76e-08	125	494	35	361	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
UIZ25210.1|GH5_20	1.17e-105	25	543	39	540
CCA23923.1|GH5_20	2.77e-105	5	543	20	535
ABG80555.1|GH5_20	4.03e-71	23	543	137	632
ABG80554.1|GH5_20	4.03e-71	23	543	137	632
ABC87090.1|GH5_20	9.88e-71	25	543	134	627

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	9.08e-25	124	518	17	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]
3VVG_A	1.66e-24	124	518	17	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]
3QHN_A	2.25e-24	124	518	50	394	Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_B Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_C Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]
2ZUM_A	4.07e-24	124	518	50	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	4.07e-24	124	518	50	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23548|GUN_PAEPO	6.90e-18	117	522	39	371	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P50400|GUND_CELFI	1.27e-17	130	519	56	399	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
sp|P19487|GUNA_XANCP	6.67e-16	118	526	28	362	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|P54583|GUN1_ACIC1	1.98e-15	130	522	57	381	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P10474|GUNB_CALSA	5.19e-08	133	459	643	944	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
0.999754	0.000240

TMHMM  Annotations     

Start	End
34	56