CAZyme Information: PTTG_05735-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_05735-t43_1-p1
• CAZy Family: GH35
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
590		65287.34	9.6057

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

• Gene Location: location=ADAS02000174.1:46831-49142(-)

Full Sequence      

MLATLQGGSLFVLLTVVIHQAHGSPKVPATASAQPATKSTLSPVSGTYFGWSSWSLQAYK
GKGYGYDWLTEKNIKAQADILSKEFSQLGYNRINLDSGWQDAELDKYGRTILNRKTFPKG
INDLSSYLAQRKLKLGLYYLPGIDARAVNNKAVVMNSKYTADQIIQCPDKDALGCNRNTP
NAFNAGMALNYSHPGAQMYINSVVDGLYSWGVSYVKIAGVVPGSLIDPPEWWKYNTTADL
MAWRKAIDDLYHQKWQKQGRDPIWLGASWKIPTSAGSTMEKYADSFRVEQDIEAYSETQM
TTFDRVIRNAKTAALWSSVDSNRKWKGVRDLDSILVSDMTVAECKTMVTIWAMFGSVIYL
GDDLTKLPEARKALVKNPEVLKLAILASTNQARLDGFNPSVSGTRTTTAKPLRQSLKSVE
RLEVNPVQEDYQITSRDCDEMAEKRQLVVQYGLKQKVVDSDTLHQSCLKASTSGKSGRLQ
ARAVDGANPDQWSLQTWVLEQGQGDIYVAVVNAGQQTAGDKPAKVQISLSKLKTLQKSPR
IKQMTGGHYAVRDLWASKDLSPVAFQGTIDVTLETHGSTLLKFTPISPPK

Enzyme Prediction     

No EC number prediction in PTTG_05735-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	207	393	1.2e-22	0.6899563318777293

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	4.75e-61	50	391	4	270	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
269892	GH36	7.19e-14	50	376	5	291	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
177874	PLN02229	1.51e-11	50	383	66	322	alpha-galactosidase
166449	PLN02808	7.02e-11	50	394	35	297	alpha-galactosidase
178295	PLN02692	7.75e-11	50	138	59	140	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL77684.1|CBM35|GH27	5.17e-55	13	393	24	388
BCM93998.1|GH27	7.61e-54	48	381	35	354
QUQ67322.1|CBM35|GH27	1.04e-51	26	585	23	456
SDS59418.1|CBM35|GH27	3.95e-51	21	393	45	399
QIZ00458.1|CBM35|GH27	2.05e-50	29	381	38	384

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NXK_A	3.07e-19	50	381	28	351	Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
4NX0_A	1.74e-18	50	381	28	351	Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
1UAS_A	3.17e-11	50	381	12	267	Chain A, alpha-galactosidase [Oryza sativa]
3CC1_A	7.69e-11	50	383	15	340	Chain A, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
3HG3_A	2.85e-10	69	383	33	288	Chain A, Alpha-galactosidase A [Homo sapiens],3HG3_B Chain B, Alpha-galactosidase A [Homo sapiens],3TV8_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3TV8_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C8VJZ7|AGAL8_EMENI	3.76e-18	50	384	84	407	Putative alpha-galactosidase 8 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agl8 PE=5 SV=2
sp|Q92451|AGAL3_HYPJE	4.22e-18	23	309	166	433	Alpha-galactosidase 3 OS=Hypocrea jecorina OX=51453 GN=agl3 PE=1 SV=1
sp|Q8RX86|AGAL2_ARATH	4.68e-11	50	381	43	298	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
sp|Q9FXT4|AGAL_ORYSJ	2.12e-10	50	381	67	322	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
sp|Q9URZ0|AGAL_SCHPO	3.01e-10	50	394	36	331	Alpha-galactosidase mel1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mel1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000246	0.999717	CS pos: 23-24. Pr: 0.9769

TMHMM  Annotations     

There is no transmembrane helices in PTTG_05735-t43_1-p1.