logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000272_02658

You are here: Home > Sequence: MGYG000000272_02658

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 hominis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella hominis
CAZyme ID MGYG000000272_02658
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
522 57571.72 6.3819
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000272 3991064 Isolate China Asia
Gene Location Start: 1516;  End: 3084  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000272_02658.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 132 341 6.9e-44 0.8415841584158416

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 3.61e-37 134 342 12 190
Amb_all domain.
COG3866 PelB 8.66e-36 44 427 33 344
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 2.85e-22 119 338 11 211
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-121 42 428 23 384
QNH62939.1 1.08e-38 63 427 77 378
QHJ07062.1 1.54e-38 65 369 66 327
CAW79729.1 2.74e-35 30 427 29 339
QAW31065.1 2.74e-35 30 427 29 339

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 3.91e-24 63 343 12 251
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]
2QXZ_A 1.12e-20 209 347 110 255
ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris]
2QY1_A 1.12e-20 209 347 110 255
ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris]
1BN8_A 1.68e-20 17 318 2 318
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
2BSP_A 4.05e-20 17 318 2 318
ChainA, PROTEIN (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
B1B6T1 5.49e-36 30 427 29 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 5.49e-36 30 427 29 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 5.49e-36 30 427 29 339
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 4.30e-20 63 340 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
P39116 9.18e-20 17 318 2 318
Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 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
0.000885 0.997529 0.000758 0.000313 0.000254 0.000233

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000272_02658.