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CAZyme Information: MGYG000000695_00785

You are here: Home > Sequence: MGYG000000695_00785

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 sp000436035
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000436035
CAZyme ID MGYG000000695_00785
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
519 MGYG000000695_7|CGC2 56849.61 6.4954
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000695 3484843 MAG Kazakhstan Asia
Gene Location Start: 53845;  End: 55404  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000695_00785.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 127 337 3.4e-43 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 4.88e-40 6 423 1 344
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 3.97e-37 130 338 12 190
Amb_all domain.
pfam00544 Pec_lyase_C 2.08e-22 130 334 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 1.10e-120 38 436 23 393
QNH62939.1 1.52e-40 59 343 77 318
QHJ07062.1 4.13e-40 61 341 66 305
AAR45486.1 1.09e-35 38 423 2 300
SCA88301.1 2.36e-35 22 423 20 334

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 7.09e-24 59 336 12 248
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]
5AMV_A 7.56e-21 218 423 191 398
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 9.16e-21 218 423 212 419
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
2QY1_A 1.50e-20 184 343 100 255
ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris]
2QXZ_A 1.50e-20 184 343 100 255
ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B1B6T1 5.27e-36 38 423 41 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 5.27e-36 38 423 41 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 5.27e-36 38 423 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
Q00645 1.79e-22 59 336 45 260
Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB PE=1 SV=1
Q0CBV0 8.11e-22 59 311 44 233
Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB 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
0.000628 0.998129 0.000347 0.000336 0.000285 0.000221

TMHMM  Annotations      download full data without filtering help

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