logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004403_01792

You are here: Home > Sequence: MGYG000004403_01792

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 Agathobacter sp900550545
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Agathobacter; Agathobacter sp900550545
CAZyme ID MGYG000004403_01792
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
582 MGYG000004403_19|CGC1 62761.96 9.8426
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004403 2627762 MAG Israel Asia
Gene Location Start: 6290;  End: 8038  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004403_01792.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4193 LytD 8.28e-23 120 337 45 245
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism].
cd14256 Dockerin_I 1.41e-14 518 575 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.
pfam12733 Cadherin-like 5.36e-08 365 436 5 88
Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain.
pfam00404 Dockerin_1 2.39e-07 519 572 1 54
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.
cd14256 Dockerin_I 2.98e-04 504 540 21 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
CBK92679.1 1.29e-173 39 561 229 768
ACR76042.1 2.30e-171 39 561 229 768
CBK91761.1 4.60e-171 39 561 229 768
AEN96074.1 1.24e-154 35 557 210 737
ACR71571.1 5.19e-106 36 554 120 664

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6FXO_A 3.44e-13 123 337 37 244
ChainA, Bifunctional autolysin [Staphylococcus aureus subsp. aureus Mu50]
6FXP_A 3.01e-09 113 337 31 246
ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus Mu50],6FXP_B Chain B, Uncharacterized protein [Staphylococcus aureus subsp. aureus Mu50]
6U0O_B 6.02e-09 113 337 61 276
ChainB, LYZ2 domain-containing protein [Staphylococcus aureus subsp. aureus NCTC 8325]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8CPQ1 3.10e-12 123 337 1128 1335
Bifunctional autolysin OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=atl PE=3 SV=1
Q5HQB9 7.09e-12 123 337 1128 1335
Bifunctional autolysin OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=atl PE=3 SV=1
O33635 7.09e-12 123 337 1128 1335
Bifunctional autolysin OS=Staphylococcus epidermidis OX=1282 GN=atl PE=1 SV=1
Q5HH31 1.21e-11 123 337 1049 1256
Bifunctional autolysin OS=Staphylococcus aureus (strain COL) OX=93062 GN=atl PE=3 SV=1
Q8NX96 1.59e-11 123 337 1049 1256
Bifunctional autolysin OS=Staphylococcus aureus (strain MW2) OX=196620 GN=atl 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
0.000538 0.998492 0.000251 0.000315 0.000202 0.000162

TMHMM  Annotations      download full data without filtering help

start end
7 26