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CAZyme Information: MGYG000003515_01280

You are here: Home > Sequence: MGYG000003515_01280

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 sp900769275
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900769275
CAZyme ID MGYG000003515_01280
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
809 87764.84 4.6591
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003515 2052370 MAG Fiji Oceania
Gene Location Start: 10634;  End: 13063  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003515_01280.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 212 380 1.4e-32 0.8366336633663366
CBM77 593 697 2.9e-22 0.9611650485436893

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 3.54e-46 196 502 82 345
Pectate lyase [Carbohydrate transport and metabolism].
pfam18283 CBM77 1.13e-29 591 699 4 108
Carbohydrate binding module 77. This domain is the non-catalytic carbohydrate binding module 77 (CBM77) present in Ruminococcus flavefaciens. CBMs fulfil a critical targeting function in plant cell wall depolymerisation. In CBM77, a cluster of conserved basic residues (Lys1092, Lys1107 and Lys1162) confer calcium-independent recognition of homogalacturonan.
smart00656 Amb_all 1.94e-24 219 382 17 190
Amb_all domain.
pfam00544 Pec_lyase_C 8.32e-11 219 378 35 211
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
QUT73893.1 1.88e-189 2 713 4 693
QNT67442.1 5.61e-161 28 701 115 773
BCJ94010.1 9.08e-158 18 697 40 710
QKS45759.1 5.69e-157 18 702 33 685
AIQ50255.1 8.44e-157 4 702 14 732

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FU5_A 1.10e-16 594 697 12 109
Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens]
3VMV_A 1.03e-14 185 380 47 248
Crystalstructure 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B1B6T1 5.42e-18 160 386 59 280
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q65DC2 5.42e-18 160 386 59 280
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
Q8GCB2 5.42e-18 160 386 59 280
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
P72242 2.43e-06 255 376 156 308
Pectate lyase OS=Pseudomonas amygdali pv. lachrymans OX=53707 GN=pelP 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
0.000377 0.998914 0.000196 0.000175 0.000152 0.000152

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003515_01280.