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CAZyme Information: FOMG_03215-t38_1-p1

You are here: Home > Sequence: FOMG_03215-t38_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 oxysporum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
CAZyme ID FOMG_03215-t38_1-p1
CAZy Family AA7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
336 36946.64 7.3571
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Foxysporum26406 20033 1089452 372 19661
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in FOMG_03215-t38_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 80 253 4.4e-107 0.9943181818181818

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 5.19e-57 83 252 12 186
Amb_all domain.
226384 PelB 1.79e-51 56 335 62 344
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 7.98e-35 81 252 28 211
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.04e-257 1 336 1 336
3.68e-253 1 336 1 336
3.73e-249 1 336 1 339
2.69e-239 21 336 6 324
7.17e-231 1 336 1 336

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.13e-39 29 335 3 325
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]
2.49e-32 85 335 130 415
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
9.62e-30 42 335 21 331
Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
2.98e-26 32 252 10 276
Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
5.33e-26 85 230 125 296
Structural insights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.40e-56 9 335 14 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1
9.40e-56 9 335 14 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
9.40e-56 9 335 14 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
1.80e-55 32 316 44 307
Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1
9.73e-55 1 260 1 266
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000237 0.999726 CS pos: 17-18. Pr: 0.9813

TMHMM  Annotations      help

There is no transmembrane helices in FOMG_03215-t38_1-p1.