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CAZyme Information: FPRN_02001-t42_1-p1

You are here: Home > Sequence: FPRN_02001-t42_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 Fusarium proliferatum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
CAZyme ID FPRN_02001-t42_1-p1
CAZy Family AA5
CAZyme Description related to small s protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1142 FCQG01000001|CGC4 127411.90 7.2817
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FproliferatumNRRL62905 15602 N/A 348 15254
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.10:25

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 111 296 2.2e-87 0.9946524064171123

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 9.04e-59 109 298 1 190
Amb_all domain.
226384 PelB 1.73e-21 66 301 28 280
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 1.56e-20 115 294 23 211
Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.
405210 HeLo 4.59e-08 376 426 117 166
Prion-inhibition and propagation. This N-terminal region, HeLo, has a prion-inhibitory effect in cis on its own prion-forming domain (PFD) and in trans on HET-s prion propagation. The domain is found exclusively in the fungal kingdom. Its structure, as it occurs in the HET-s/HET-S proteins, consists of two bundles of alpha-helices that pack into a single globular domain. The domain boundary determined from its structure and from protease-resistance experiments overlaps with the C-terminal prion-forming domain of HET-s (PF11558. The HeLo domains of HET-s and HET-S are very similar and their few differences (and not the prion-forming domains) determine the compatibility-phenotype of the fungi in which the proteins are expressed. The mechanism of the HeLo domain-function in heterokaryon-incompatibility is still under investigation, however the HeLo domain is found in similar protein architectures as other cell death and apoptosis-inducing domains. The only other HeLo protein to which a function has been associated is LopB from L. maculans. Although its specific role in L. maculans is unknown, LopB- mutants have impaired ability to form lesions on oilseed rape. The HeLo domain is not related to the HET domain (PF06985) which is another domain involved in heterokaryon incompatibility.
404168 Beta_helix 4.14e-04 172 296 1 112
Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.92e-266 1 377 1 377
4.92e-266 1 377 1 377
4.92e-266 1 377 1 377
4.92e-266 1 377 1 377
4.13e-262 1 377 1 377

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.17e-131 25 359 7 341
Pectin Lyase B [Aspergillus niger]
6.31e-131 24 375 6 357
Pectin Lyase A [Aspergillus niger]
4.78e-130 24 375 6 357
Pectin Lyase A [Aspergillus niger],1IDJ_B Pectin Lyase A [Aspergillus niger]
4.30e-13 26 297 5 249
Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5]
1.85e-10 26 294 12 330
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.07e-137 1 370 1 372
Probable pectin lyase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=pelA PE=3 SV=1
2.26e-136 16 375 17 377
Pectin lyase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=pelB PE=2 SV=1
6.44e-135 25 361 25 361
Probable pectin lyase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=pelA PE=3 SV=1
6.44e-135 25 361 25 361
Probable pectin lyase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=pelB PE=3 SV=1
9.62e-134 25 375 26 376
Probable pectin lyase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pelA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000221 0.999742 CS pos: 19-20. Pr: 0.9762

TMHMM  Annotations      help

There is no transmembrane helices in FPRN_02001-t42_1-p1.