CAZyme Information: H310_01382-t26_1-p1

Basic Information

• Species: Aphanomyces invadans
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
• CAZyme ID: H310_01382-t26_1-p1
• CAZy Family: GH16|GH16|GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
548		60259.64	6.8660

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AinvadansNJM9701	15416	N/A	168	15248

• Gene Location: location=KI913953:1673392-1675333(-)

Full Sequence      

MADHGTATDAADDHRLNMNQWRESVRLSSSSSSTCLGKPRPSEVKVVIVPACQAKIESHR
EYKGRIRTWPGLLLVFVCVVSAIAIITTSAFRAHASSTERTQKVNELLFRNKSGTLLPSD
VMDSVIGSPADDGQVGNPKTYPTSQCAQLDYQSKNGKIVAVTKNGTEVAISIKGVNWFGM
ETGLAVPFGLWENQKNGTTAFVLAAFLAANKFNAVRLPVCIQSILRNTKPAKSLVNVESN
RALDLTNYMTMLQSIIKVLAFRRIGVLISLHTLTTMQSGGNWYSDALGVSKADFLEAVDI
LTQSLCTNEYWNVMGLDAKNEPHEATWAEFAEGATIIGNRMLEGCPNWSIYVEGVNDGTK
SVTIDGTAFKYFDWWGGGLQQARANPVTLQTPHKVVYAPHYYNTGVFPQPYLYGPGGVRD
ELDDQTLKRRIQGTSFDMFGHVNKRQTDAVVMGEFAGLYATDAHPLKTTKRVTDLLIEIM
LEEKYAGGFMWSLNPESAYQYNPSPGHYTEGLLLDDWLTPNAVFLKGLAAMDAFPDLRML
PCVPTTSA

Enzyme Prediction     

No EC number prediction in H310_01382-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	167	497	4.9e-130	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	4.88e-17	162	539	37	398	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	3.51e-08	173	497	6	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABC87086.1|GH5_20	5.56e-201	40	542	58	571
ABL75350.1|GH5_20	4.67e-200	24	548	38	580
ABJ97692.1|GH5_20	1.00e-199	9	544	33	572
ABC87087.1|GH5_20	1.94e-198	26	544	51	581
ABK59035.1|GH5_20	1.94e-198	26	544	51	581

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	4.27e-42	164	519	22	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	5.91e-42	164	519	22	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	8.06e-42	140	519	32	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	8.06e-42	140	519	32	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	2.90e-41	140	519	32	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|P23548|GUN_PAEPO	9.13e-28	151	521	39	371	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P19487|GUNA_XANCP	1.43e-27	170	517	42	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|P54583|GUN1_ACIC1	1.22e-25	164	523	56	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	4.68e-22	161	498	638	972	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|Q05332|GUNG_ACET2	7.00e-12	165	519	57	431	Endoglucanase G OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000045	0.000001

TMHMM  Annotations     

Start	End
69	91