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CAZyme Information: PTTG_00700-t43_1-p1

You are here: Home > Sequence: PTTG_00700-t43_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Puccinia triticina
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
CAZyme ID PTTG_00700-t43_1-p1
CAZy Family AA5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
446 ADAS02000106.1|CGC1 49675.98 6.2336
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

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:15

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 126 396 3.1e-77 0.9694323144104804

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 7.21e-145 29 318 1 271
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.
177874 PLN02229 6.71e-117 17 393 51 390
alpha-galactosidase
178295 PLN02692 2.69e-113 23 361 50 355
alpha-galactosidase
166449 PLN02808 3.51e-112 22 402 25 366
alpha-galactosidase
374582 Melibiase_2 4.97e-90 28 318 1 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.20e-170 1 393 1 390
6.43e-170 1 393 1 390
1.97e-166 20 380 17 374
1.19e-157 20 393 16 385
1.48e-157 18 393 14 385

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.16e-150 22 442 2 392
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
1.84e-126 9 407 7 416
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]
2.96e-125 9 407 7 416
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_B Chain B, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_C Chain C, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_D Chain D, Alpha-galactosidase 1 [Saccharomyces cerevisiae]
6.65e-94 22 348 2 311
Chain A, alpha-galactosidase [Oryza sativa]
3.07e-89 22 363 2 310
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.49e-142 13 395 17 395
Alpha-galactosidase mel1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mel1 PE=3 SV=1
3.95e-133 23 393 23 396
Alpha-galactosidase OS=Lachancea cidri OX=29831 GN=MEL PE=3 SV=1
4.39e-130 1 422 1 430
Alpha-galactosidase OS=Saccharomyces pastorianus (strain ATCC 76529 / Carlsberg bottom yeast no.1 / CBS 1513 / CLIB 176 / NBRC 1167 / NCYC 396 / NRRL Y-12693) OX=1073566 GN=MEL PE=3 SV=1
1.42e-128 23 393 24 397
Alpha-galactosidase OS=Saccharomyces mikatae OX=114525 GN=MEL PE=3 SV=1
6.46e-127 23 422 24 430
Alpha-galactosidase OS=Saccharomyces paradoxus OX=27291 GN=MEL PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000475 0.999500 CS pos: 20-21. Pr: 0.9747

TMHMM  Annotations      help

There is no transmembrane helices in PTTG_00700-t43_1-p1.