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CAZyme Information: MGYG000001560_01320

You are here: Home > Sequence: MGYG000001560_01320

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 Massilioclostridium coli
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Massilioclostridium; Massilioclostridium coli
CAZyme ID MGYG000001560_01320
CAZy Family GH106
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1298 MGYG000001560_1|CGC18 143610.29 4.0732
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001560 2985330 Isolate not provided not provided
Gene Location Start: 1570506;  End: 1574402  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001560_01320.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH106 45 1006 5.5e-79 0.9575242718446602

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17132 Glyco_hydro_106 7.93e-10 206 645 351 755
alpha-L-rhamnosidase.
pfam02837 Glyco_hydro_2_N 1.56e-05 919 1011 61 153
Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.
pfam07554 FIVAR 3.93e-05 1177 1236 3 69
FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
PRK10340 ebgA 3.24e-04 925 1009 111 195
cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam07554 FIVAR 0.005 1038 1100 3 68
FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QGH70002.1 9.03e-231 19 1030 67 1113
QYN20448.1 1.83e-206 15 1036 21 1124
QNP57182.1 1.32e-187 49 1004 12 938
SDG73971.1 2.45e-187 41 1030 3 960
QHC72677.1 2.89e-185 39 1004 2 938

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6Q2F_A 4.38e-06 206 1006 410 1109
Structureof Rhamnosidase from Novosphingobium sp. PP1Y [Novosphingobium sp. PP1Y]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000492 0.502286 0.496363 0.000328 0.000285 0.000224

TMHMM  Annotations      download full data without filtering help

start end
9 31
1275 1294