logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004854_01896

You are here: Home > Sequence: MGYG000004854_01896

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; Oscillospirales; Ruminococcaceae; Ruminococcus;
CAZyme ID MGYG000004854_01896
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
906 100188.12 4.5806
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004854 2725669 MAG Spain Europe
Gene Location Start: 111611;  End: 114331  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004854_01896.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 224 439 7.5e-31 0.8960396039603961
CBM13 566 715 1.6e-20 0.7978723404255319

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 8.87e-29 173 514 30 340
Pectate lyase [Carbohydrate transport and metabolism].
pfam14200 RicinB_lectin_2 1.88e-17 594 681 4 89
Ricin-type beta-trefoil lectin domain-like.
smart00656 Amb_all 2.14e-15 244 439 17 187
Amb_all domain.
cd14256 Dockerin_I 1.80e-13 848 904 1 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.
pfam00544 Pec_lyase_C 1.99e-09 235 435 26 209
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
CBL17651.1 0.0 30 904 31 893
CDM70399.1 7.63e-120 4 694 3 694
AUO18238.1 1.09e-118 26 694 25 705
CBL17517.1 1.57e-98 501 903 450 849
CBL16296.1 3.11e-91 548 870 613 945

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 1.32e-07 175 448 2 256
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34819 5.56e-16 175 518 34 339
Pectin lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pelB PE=3 SV=1
P94449 5.56e-16 175 518 34 339
Pectin lyase OS=Bacillus subtilis OX=1423 GN=pelB 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
0.000244 0.999087 0.000201 0.000173 0.000151 0.000133

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004854_01896.