CAZyme Information: H257_00416-t26_2-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_00416-t26_2-p1
• CAZy Family: AA15
• CAZyme Description: hypothetical protein, variant

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
534		58543.02	8.1246

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

• Gene Location: location=KI913114:1179450-1181350(-)

Full Sequence      

MTQWRESQRLSTSSSSSCLVKPRPTEVKVAIVPAPQDKVETKREYKGRIRTWPGLVLLAI
FVTGAIVLIATSAQRAHQASKDRARVANELLFRNRSGTLLPSDILDSVIATPDDDGQVGN
PKTYPASQCAQLDYQSKNGKIVAVMTNGTEVALSIKGVNWFGMETGLAVPFGLWENQKNG
TTAFVLAAFLAANKFNAVRLPVCILSILRNTKPEKSLVNVESNRALDLTNYMTTLQSLIK
VLAYRRIGVLISLHTLTPMQSGGNWYSDALGVSKLDFLKAVDILTTNLCSNEYWNVMGLD
AKNEPFEATWAEFADGAATIGNRMLQGCPQWSIYVEGVNKGTKSVTIDGTAFSYFDWWGG
GLQGAGATPVTVTTKHKVVYAPHYYNTGVFPQPYLYGPGGVGDELDDKTLKRRVEGTSFD
MFGYLNLKQADAVVLGEFAGLYATDGHPLKTTRRVTDALIEIMLQQKCAGGFMWSLNPES
AYQYNPAPGHYTEGLLLDDWLTPNAVFVKGMAAMDAFPDLRMLPCDPTPPRRPL

Enzyme Prediction     

No EC number prediction in H257_00416-t26_2-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	150	480	5.6e-126	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	9.28e-17	146	502	38	378	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	7.96e-07	156	480	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	1.90e-195	23	525	58	571
ABL75350.1|GH5_20	2.78e-195	23	525	59	572
ABC87087.1|GH5_20	4.64e-193	9	527	51	581
ABK59035.1|GH5_20	4.64e-193	9	527	51	581
ABJ97692.1|GH5_20	5.56e-193	23	527	57	572

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	3.45e-42	145	502	20	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	4.78e-42	145	502	20	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	1.70e-41	145	502	53	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	4.44e-41	145	502	53	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	1.60e-40	145	502	53	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|P19487|GUNA_XANCP	9.39e-28	153	500	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	8.10e-26	147	506	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	4.73e-18	155	405	647	910	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P27033|GUNC_CELJU	1.60e-09	295	481	493	708	Endoglucanase C OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=celC PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999584	0.000422

TMHMM  Annotations     

Start	End
51	73