logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001770_01928

You are here: Home > Sequence: MGYG000001770_01928

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 sp900313215
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900313215
CAZyme ID MGYG000001770_01928
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
523 MGYG000001770_59|CGC1 57414.52 6.8341
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001770 3003526 MAG Denmark Europe
Gene Location Start: 15831;  End: 17402  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001770_01928.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 132 341 1.4e-43 0.8415841584158416

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 3.07e-38 134 342 12 190
Amb_all domain.
COG3866 PelB 3.82e-37 24 427 13 344
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 5.70e-23 119 338 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 1.04e-122 42 428 23 384
QNH62939.1 4.16e-39 63 427 77 378
QHJ07062.1 4.14e-38 65 427 66 369
AAR45486.1 4.36e-36 42 427 2 300
CAW79729.1 5.54e-36 19 427 18 339

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 8.48e-25 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 1.53e-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 1.53e-20 209 347 110 255
ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris]
1VBL_A 5.29e-20 83 338 91 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
5AMV_A 6.11e-20 167 427 150 398
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B1B6T1 1.11e-36 19 427 18 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 1.11e-36 19 427 18 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 1.11e-36 19 427 18 339
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 1.29e-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
Q2TZY0 1.07e-19 63 328 45 240
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 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
0.001151 0.995987 0.001943 0.000363 0.000287 0.000255

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001770_01928.