logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004547_01715

You are here: Home > Sequence: MGYG000004547_01715

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
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; ;
CAZyme ID MGYG000004547_01715
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
868 95682.79 4.6897
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004547 2604006 MAG France Europe
Gene Location Start: 351;  End: 2957  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004547_01715.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 224 415 3.3e-35 0.8316831683168316

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 9.34e-29 226 493 97 343
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 6.73e-19 225 418 12 190
Amb_all domain.
pfam18283 CBM77 2.27e-17 689 791 1 104
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.
pfam00544 Pec_lyase_C 5.52e-12 299 414 89 211
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.
cd14256 Dockerin_I 3.24e-08 807 865 2 57
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBF42492.1 5.04e-234 28 663 30 675
CDR31241.1 3.40e-120 34 522 329 837
ACR71161.1 9.14e-110 1 786 1 881
ADU23076.1 3.74e-107 38 468 761 1207
QEH68115.1 1.68e-74 38 504 40 487

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 5.14e-22 163 491 24 322
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]
2QX3_A 8.83e-15 280 497 108 330
Structureof pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris],2QX3_B Structure of pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris]
2QY1_A 2.13e-14 280 497 108 330
ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris]
2QXZ_A 2.13e-14 280 497 108 330
ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris]
5AMV_A 6.89e-14 231 398 128 302
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
Q65DC2 3.31e-18 188 423 81 281
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
B1B6T1 3.31e-18 188 423 81 281
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 3.31e-18 188 423 81 281
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
P0C1C1 2.29e-15 229 422 109 286
Pectate lyase 2 OS=Pectobacterium carotovorum OX=554 GN=pel2 PE=3 SV=1
Q6CZT3 7.32e-15 264 422 136 286
Pectate lyase 2 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel2 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
0.000831 0.998070 0.000310 0.000381 0.000209 0.000170

TMHMM  Annotations      download full data without filtering help

start end
7 29