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CAZyme Information: CAP94412:RNA-p1

You are here: Home > Sequence: CAP94412: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 CAP94412:RNA-p1
CAZy Family GH43
CAZyme Description exo-arabinanase abnx-Penicillium chrysogenum
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
378 Pc00c18|CGC8 41694.73 4.9229
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

No EC number prediction in CAP94412:RNA-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH93 44 352 1.9e-120 0.990228013029316

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
271234 Sialidase_non-viral 1.28e-05 53 258 152 335
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
271234 Sialidase_non-viral 0.003 53 151 21 125
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
271234 Sialidase_non-viral 0.006 77 218 115 243
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.95e-283 1 378 1 378
2.95e-283 1 378 1 378
2.57e-252 1 378 1 378
1.57e-212 3 378 5 380
3.37e-199 1 378 1 375

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.61e-270 24 378 1 355
High resolution structure of Penicillium chrysogenum alpha-L-arabinanase [Penicillium chrysogenum],3A72_A High resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobiose [Penicillium chrysogenum]
6.41e-136 28 378 10 365
Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],5M1Z_A Chain A, Exo-1,5-alpha-L-arabinofuranobiosidase [Fusarium graminearum]
9.09e-136 28 378 10 365
Chain A, Alpha-l-arabinofuranosidase [Fusarium graminearum]
5.21e-135 28 378 10 365
Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_B Chain B, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_C Chain C, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum]
5.99e-134 28 377 10 364
Chain A, ALPHA-L-ARABINOFURANOSIDASE [Fusarium graminearum]

Swiss-Prot Hits      help

CAP94412:RNA-p1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.004220 0.995757 CS pos: 20-21. Pr: 0.7456

TMHMM  Annotations      help

There is no transmembrane helices in CAP94412:RNA-p1.