CAZyme Information: PPTG_08508-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_08508-t26_1-p1
• CAZy Family: GH17
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
673		75958.41	5.0995

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PparasiticaINRA-310	23240	761204	119	23121

• Gene Location: location=KI669574:495837-497858(+)

Full Sequence      

MASHSEPTAYGTSSLASDERLSARAAARRKWIRWGIIGASTGIIVIGLVVLGISFHSAKS
TVSTASPNEEEIECFQSSNIDNVTNMMEPIKGLKWKLGGEKTTDSFIAIDVDTKYQEIMG
FGGAFTEAAALQFHKLPKDKQEEVLTLYFDKNKGSAYNFGRVPMGSCDFSMGSYNFAETE
NDMELKDFDVDVTHDTEMIIPFIKRALKRRPDMKMFLAPWSPPAWMKRSSSDYNASMLGS
VKPVGLRDDRRAPWALYFSKFITAYKKHGIDFWGLSPQNEPEFAAPWEACAYNPEYEAEF
IGEFLGPVLERDHPGLTLMVFDHNRNNVQHWAEVIYNHPTASKYVDGMAFHWYEDGGERY
MDGVEYPEHLNDTHFIDPNRFMLASESCNCPGVAVGKDAWFRAQRYGHDIMSDLNNHVAG
WVDWNLLLDHTGGPNHKGNLCDAPIILTKNETDFIIQPMYYFIQHFSKFIPVGSRRVDVE
VAARFEKPGDAQLYVDYQSSLATCDGSSRQMIHKTDDNKMQVTNTPFCLNMVPTPSKGRE
IRLVECQWTQQTWTFEEDTNRIRIDDYCLSLSRGSTENGVRITADKCEPDVAPHQQWTFN
AEDGTMRSKASTSNQCVTTGYSFVQAAAFVTPENRKVLVVLNENTEPADFQVQVGDAVLD
TSVLAGAIRTYVW

Enzyme Prediction     

No EC number prediction in PPTG_08508-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH30	106	482	1.7e-137	0.8653846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
307945	Glyco_hydro_30	3.52e-95	118	470	1	348	Glycosyl hydrolase family 30 TIM-barrel domain.
227807	XynC	7.80e-54	107	478	36	344	O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis].
407314	Glyco_hydro_30C	3.03e-09	618	671	9	63	Glycosyl hydrolase family 30 beta sandwich domain.
396577	Glyco_hydro_59	1.82e-05	137	287	20	149	Glycosyl hydrolase family 59.
238092	RICIN	1.57e-04	522	618	6	98	Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ligand binding occurs on exposed surfaces of the compact domain sturcture.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ22523.1|CBM13|GH30_1	0.0	5	669	5	673
CCA14291.1|GH30_1	3.84e-183	70	673	82	681
CAG4717758.1|GH30_1	1.04e-117	114	480	71	429
CAG4715443.1|GH30_1	1.34e-108	41	479	15	460
AID57155.1|GH30_1	5.17e-103	114	553	62	514

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1OGS_A	2.22e-82	103	511	63	468	human acid-beta-glucosidase [Homo sapiens],1OGS_B human acid-beta-glucosidase [Homo sapiens],1Y7V_A Chain A, Glucosylceramidase [Homo sapiens],1Y7V_B Chain B, Glucosylceramidase [Homo sapiens],2F61_A Crystal structure of partially deglycosylated acid beta-glucosidase [Homo sapiens],2F61_B Crystal structure of partially deglycosylated acid beta-glucosidase [Homo sapiens],2J25_A Partially deglycosylated glucoceramidase [Homo sapiens],2J25_B Partially deglycosylated glucoceramidase [Homo sapiens],2NSX_A Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_B Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_C Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_D Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NT0_A Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_B Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_C Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_D Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT1_A Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_B Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_C Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_D Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],3GXD_A Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_B Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_C Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_D Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXF_A Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_B Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_C Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_D Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXI_A Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_B Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_C Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_D Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXM_A Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_B Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_C Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_D Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3RIK_A The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_B The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_C The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_D The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_A The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_B The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_C The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_D The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],6MOZ_A Structure of acid-beta-glucosidase in complex with an aromatic pyrrolidine iminosugar inhibitor [Homo sapiens],6MOZ_B Structure of acid-beta-glucosidase in complex with an aromatic pyrrolidine iminosugar inhibitor [Homo sapiens],6Q1N_A Glucocerebrosidase in complex with pharmacological chaperone IMX8 [Homo sapiens],6Q1N_B Glucocerebrosidase in complex with pharmacological chaperone IMX8 [Homo sapiens],6Q1P_A Glucocerebrosidase in complex with pharmacological chaperone norIMX8 [Homo sapiens],6Q1P_B Glucocerebrosidase in complex with pharmacological chaperone norIMX8 [Homo sapiens],6Q6K_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol activity based probe with Cy5 tag (ME569) [Homo sapiens],6Q6K_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol activity based probe with Cy5 tag (ME569) [Homo sapiens],6Q6L_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656) [Homo sapiens],6Q6L_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656) [Homo sapiens],6Q6N_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with biphenyl-cyclophellitol inhibitor (ME655) [Homo sapiens],6Q6N_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with biphenyl-cyclophellitol inhibitor (ME655) [Homo sapiens],6TJJ_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6TJJ_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YTP_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YTP_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YUT_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YUT_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YV3_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YV3_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6Z39_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6Z39_BBB Chain BBB, Glucosylceramidase [Homo sapiens]
2WKL_A	2.22e-82	103	511	63	468	Velaglucerase alfa [Homo sapiens],2WKL_B Velaglucerase alfa [Homo sapiens],5LVX_A Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_B Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_C Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_D Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],6TJK_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6TJK_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],6TJQ_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6TN1_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6YTR_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6YTR_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],6Z3I_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],7NWV_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],7NWV_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens]
2V3D_A	2.75e-82	103	511	65	470	acid-beta-glucosidase with N-butyl-deoxynojirimycin [Homo sapiens],2V3D_B acid-beta-glucosidase with N-butyl-deoxynojirimycin [Homo sapiens],2V3E_A acid-beta-glucosidase with N-nonyl-deoxynojirimycin [Homo sapiens],2V3E_B acid-beta-glucosidase with N-nonyl-deoxynojirimycin [Homo sapiens],2V3F_A acid-beta-glucosidase produced in carrot [Homo sapiens],2V3F_B acid-beta-glucosidase produced in carrot [Homo sapiens],2VT0_A X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells [Homo sapiens],2VT0_B X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells [Homo sapiens],2WCG_A X-ray structure of acid-beta-glucosidase with N-octyl(cyclic guanidine)-nojirimycin in the active site [Homo sapiens],2WCG_B X-ray structure of acid-beta-glucosidase with N-octyl(cyclic guanidine)-nojirimycin in the active site [Homo sapiens],2XWD_A X-Ray Structure Of Acid-Beta-Glucosidase With 5n,6o-(N'-(N- Octyl)imino)nojirimycin In The Active Site [Homo sapiens],2XWD_B X-Ray Structure Of Acid-Beta-Glucosidase With 5n,6o-(N'-(N- Octyl)imino)nojirimycin In The Active Site [Homo sapiens],2XWE_A X-ray Structure Of Acid-beta-glucosidase With 5n,6s-(n'-(n- Octyl)imino)-6-thionojirimycin In The Active Site [Homo sapiens],2XWE_B X-ray Structure Of Acid-beta-glucosidase With 5n,6s-(n'-(n- Octyl)imino)-6-thionojirimycin In The Active Site [Homo sapiens]
3KE0_A	3.11e-82	103	511	63	468	Chain A, Glucosylceramidase [Homo sapiens],3KE0_B Chain B, Glucosylceramidase [Homo sapiens],3KEH_A Chain A, Glucocerebrosidase [Homo sapiens],3KEH_B Chain B, Glucocerebrosidase [Homo sapiens]
6T13_A	6.19e-82	103	511	102	507	Chain A, Glucosylceramidase [Homo sapiens],6T13_B Chain B, Glucosylceramidase [Homo sapiens],6T13_C Chain C, Glucosylceramidase [Homo sapiens],6T13_D Chain D, Glucosylceramidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G5ECR8|GLCM3_CAEEL	1.32e-90	93	481	79	461	Putative glucosylceramidase 3 OS=Caenorhabditis elegans OX=6239 GN=gba-3 PE=3 SV=1
sp|Q9UB00|GLCM4_CAEEL	2.73e-82	102	481	83	458	Putative glucosylceramidase 4 OS=Caenorhabditis elegans OX=6239 GN=gba-4 PE=3 SV=2
sp|O16580|GLCM1_CAEEL	6.50e-70	107	478	87	453	Putative glucosylceramidase 1 OS=Caenorhabditis elegans OX=6239 GN=gba-1 PE=1 SV=2
sp|O16581|GLCM2_CAEEL	8.12e-65	103	523	83	505	Putative glucosylceramidase 2 OS=Caenorhabditis elegans OX=6239 GN=gba-2 PE=3 SV=2
sp|Q8J0I9|GUN16_TRIHA	2.06e-20	66	474	26	420	Endo-1,6-beta-D-glucanase BGN16.3 OS=Trichoderma harzianum OX=5544 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999986	0.000058

TMHMM  Annotations     

Start	End
31	53