logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001042_00439

You are here: Home > Sequence: MGYG000001042_00439

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 Prevotella sp000436595
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000436595
CAZyme ID MGYG000001042_00439
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
520 MGYG000001042_24|CGC1 57416.16 5.2288
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001042 3438278 MAG Denmark Europe
Gene Location Start: 16364;  End: 17926  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001042_00439.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 131 341 8.7e-43 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 3.98e-46 23 427 12 344
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.86e-38 134 342 12 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.55e-23 134 338 30 211
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
QUT75310.1 1.38e-114 42 430 23 386
QHJ07062.1 2.76e-37 44 427 55 369
QQQ79948.1 1.83e-32 44 428 29 327
QHZ45129.1 4.00e-32 42 427 38 336
AAR45486.1 4.86e-32 42 427 2 300

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AMV_A 5.23e-22 222 427 191 398
Structuralinsights 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]
1BN8_A 6.44e-22 222 427 212 419
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
3ZSC_A 1.55e-21 61 427 17 331
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
2BSP_A 1.57e-21 222 427 212 419
ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis]
2NZM_A 3.12e-21 222 427 191 398
ChainA, Pectate lyase [Bacillus subtilis],2O04_A Chain A, Pectate lyase [Bacillus subtilis],2O0V_A Chain A, Pectate lyase [Bacillus subtilis],2O0W_A Chain A, Pectate lyase [Bacillus subtilis],2O17_A Chain A, Pectate lyase [Bacillus subtilis],2O1D_A Chain A, Pectate lyase [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q65DC2 2.21e-32 42 427 41 339
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
B1B6T1 2.21e-32 42 427 41 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 2.21e-32 42 427 41 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
P39116 3.52e-21 222 427 212 419
Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1
B1L969 8.69e-21 61 427 42 356
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.004283 0.694741 0.299876 0.000437 0.000362 0.000272

TMHMM  Annotations      download full data without filtering help

start end
13 35