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CAZyme Information: MGYG000004903_00745

You are here: Home > Sequence: MGYG000004903_00745

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 Blautia sp900555025
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp900555025
CAZyme ID MGYG000004903_00745
CAZy Family GH30
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1128 MGYG000004903_14|CGC1 125595.64 4.1432
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004903 2530621 MAG China Asia
Gene Location Start: 14825;  End: 18211  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004903_00745.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH30 36 539 4.3e-131 0.9956140350877193

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14587 Glyco_hydr_30_2 3.20e-24 36 385 4 354
O-Glycosyl hydrolase family 30.
cd14256 Dockerin_I 2.50e-09 1066 1119 2 55
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.
cd14253 Dockerin 7.74e-07 1066 1120 1 55
Dockerin repeat domain. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.
pfam17996 CE2_N 1.21e-04 601 692 19 99
Carbohydrate esterase 2 N-terminal. This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyses the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.
pfam00404 Dockerin_1 4.44e-04 1066 1107 1 42
Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWY99102.1 0.0 1 1127 1 1359
QIB57138.1 0.0 1 1127 1 1347
QMW80085.1 0.0 1 1127 1 1347
ADL05173.1 1.06e-277 36 924 44 1192
ASU27677.1 6.45e-121 109 978 302 1029

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A401ETL2 1.28e-30 15 517 14 589
Exo-beta-1,6-galactobiohydrolase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=bl1,6Gal 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
0.000478 0.998762 0.000207 0.000217 0.000174 0.000149

TMHMM  Annotations      download full data without filtering help

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