logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001375_01010

You are here: Home > Sequence: MGYG000001375_01010

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 Ruminococcus_F champanellensis
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_F; Ruminococcus_F champanellensis
CAZyme ID MGYG000001375_01010
CAZy Family GH146
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1075 118747.87 5.0079
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001375 2513436 Isolate not provided not provided
Gene Location Start: 1141618;  End: 1144845  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001375_01010.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH146 45 568 8.2e-176 0.9940357852882704

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07944 Glyco_hydro_127 2.18e-135 43 568 1 503
Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
COG3533 COG3533 3.76e-95 44 572 12 505
Uncharacterized conserved protein, DUF1680 family [Function unknown].
cd14256 Dockerin_I 2.18e-16 1020 1072 1 54
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.
pfam00404 Dockerin_1 3.01e-14 1021 1072 1 53
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.
cd14253 Dockerin 7.66e-09 1021 1072 1 53
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL17203.1 0.0 1 1075 1 1075
ADL33431.1 2.18e-266 36 815 2 777
AZK46778.1 2.85e-215 36 778 12 732
QSF44176.1 2.40e-209 36 780 16 738
AIQ16786.1 5.17e-207 36 784 16 746

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6YQH_AAA 2.09e-94 39 792 28 792
ChainAAA, Acetyl-CoA carboxylase, biotin carboxylase [Bacteroides thetaiotaomicron VPI-5482]
5OPJ_A 1.82e-91 39 792 28 792
Beta-L-arabinofuranosidase[Bacteroides thetaiotaomicron]
5MQO_A 6.98e-16 187 609 196 644
Glycosidehydrolase BT_1003 [Bacteroides thetaiotaomicron]
3WRE_A 2.49e-07 184 514 145 508
Thecrystal structure of native HypBA1 from Bifidobacterium longum JCM 1217 [Bifidobacterium longum subsp. longum JCM 1217],3WRG_A The complex structure of HypBA1 with L-arabinose [Bifidobacterium longum subsp. longum JCM 1217]
3WKW_A 2.51e-07 184 514 145 508
Crystalstructure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum ligand free form [Bifidobacterium longum subsp. longum JCM 1217],3WKX_A Crystal structure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum arabinose complex form [Bifidobacterium longum subsp. longum JCM 1217],7BZL_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7DIF_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7EXV_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7EXW_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
E8MGH8 1.37e-06 184 514 145 508
Non-reducing end beta-L-arabinofuranosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA1 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
0.000452 0.998488 0.000275 0.000317 0.000221 0.000190

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001375_01010.