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CAZyme Information: MGYG000004464_00569

You are here: Home > Sequence: MGYG000004464_00569

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 Barnesiella sp900542255
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp900542255
CAZyme ID MGYG000004464_00569
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
835 MGYG000004464_6|CGC1 91374.02 4.1422
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004464 2487387 MAG Israel Asia
Gene Location Start: 1928;  End: 4435  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004464_00569.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 168 353 2.8e-41 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 6.23e-30 198 352 34 186
Amb_all domain.
COG3866 PelB 7.68e-28 34 414 19 342
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 1.89e-15 192 352 48 211
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.
pfam13205 Big_5 4.35e-05 664 763 12 106
Bacterial Ig-like domain.
pfam12733 Cadherin-like 0.002 450 507 14 85
Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AAW84045.1 1.82e-129 85 422 1 331
QVJ81552.1 6.62e-112 49 415 48 421
ADE83376.1 1.31e-111 49 415 48 421
ABG58437.1 4.66e-40 126 672 34 604
AHJ96631.1 1.01e-36 141 415 79 364

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1VBL_A 9.96e-16 194 403 146 361
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
1PXZ_A 2.44e-13 199 354 122 270
ChainA, Major pollen allergen Jun a 1 [Juniperus ashei],1PXZ_B Chain B, Major pollen allergen Jun a 1 [Juniperus ashei]
3ZSC_A 1.78e-11 172 329 63 214
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5AMV_A 6.92e-08 204 331 150 298
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 7.35e-08 204 331 171 319
BacillusSubtilis 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
A2QV36 3.11e-22 204 416 118 322
Probable pectate lyase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=plyA PE=3 SV=1
Q9C2Z0 3.11e-22 204 416 118 322
Pectate lyase A OS=Aspergillus niger OX=5061 GN=plyA PE=1 SV=1
A1CYB8 2.69e-20 205 415 117 319
Probable pectate lyase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=plyA PE=3 SV=1
Q5AVN4 7.86e-19 187 416 106 326
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
B8NE46 2.36e-18 204 416 116 320
Probable pectate lyase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyA 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
0.008113 0.968212 0.022606 0.000476 0.000292 0.000276

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004464_00569.