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CAZyme Information: CAP96379:RNA-p1

You are here: Home > Sequence: CAP96379:RNA-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 Penicillium rubens
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicillium; Penicillium rubens
CAZyme ID CAP96379:RNA-p1
CAZy Family GH76
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
436 Pc00c21|CGC27 48406.25 4.4901
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PrubensWisconsin54-1255 14021 500485 1464 12557
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:58 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 128 412 2.4e-61 0.9868995633187773

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 1.45e-116 30 331 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.
166449 PLN02808 1.22e-96 23 425 25 376
alpha-galactosidase
177874 PLN02229 9.02e-94 23 431 56 416
alpha-galactosidase
178295 PLN02692 2.10e-87 24 433 50 409
alpha-galactosidase
374582 Melibiase_2 6.21e-65 30 331 2 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 436 1 436
2.13e-257 11 436 10 435
3.03e-257 1 436 1 435
3.37e-243 6 436 9 447
1.32e-241 5 436 5 442

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.88e-170 20 436 2 414
Chain A, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]
3.49e-82 24 435 3 363
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
1.06e-80 23 430 2 388
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
2.27e-76 23 432 2 359
Chain A, alpha-galactosidase [Oryza sativa]
3.05e-70 24 409 24 400
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.79e-258 11 436 10 435
Probable alpha-galactosidase B OS=Penicillium simplicissimum OX=69488 GN=agl1 PE=2 SV=1
5.98e-244 6 436 9 447
Probable alpha-galactosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=aglB PE=3 SV=2
2.35e-242 5 436 5 442
Probable alpha-galactosidase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aglB PE=3 SV=1
9.54e-242 5 436 5 442
Probable alpha-galactosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglB PE=3 SV=1
6.86e-241 4 436 7 448
Probable alpha-galactosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=aglB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000219 0.999738 CS pos: 19-20. Pr: 0.9688

TMHMM  Annotations      help

There is no transmembrane helices in CAP96379:RNA-p1.