logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001332_01319

You are here: Home > Sequence: MGYG000001332_01319

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 methylpentosum
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Massilioclostridium; Massilioclostridium methylpentosum
CAZyme ID MGYG000001332_01319
CAZy Family GH106
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1274 140031.53 4.1967
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001332 3406391 Isolate not provided not provided
Gene Location Start: 72620;  End: 76444  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001332_01319.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH106 489 990 2.2e-61 0.5424757281553398
GH106 38 451 1.7e-58 0.39927184466019416

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17132 Glyco_hydro_106 1.47e-40 192 784 349 872
alpha-L-rhamnosidase.
pfam07554 FIVAR 2.51e-04 1163 1221 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
QTU60664.1 2.59e-152 34 1012 40 963
QTU52635.1 2.59e-152 34 1012 40 963
QTU44519.1 2.59e-152 34 1012 40 963
CBG74689.1 2.59e-152 34 1012 40 963
QJS99441.1 1.25e-151 38 1012 56 1012

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6Q2F_A 4.60e-23 192 987 408 1100
Structureof Rhamnosidase from Novosphingobium sp. PP1Y [Novosphingobium sp. PP1Y]
5MQM_A 4.23e-10 179 987 346 1059
Glycosidehydrolase BT_0986 [Bacteroides thetaiotaomicron],5MQN_A Glycoside hydrolase BT_0986 [Bacteroides thetaiotaomicron]
5MWK_A 9.55e-10 179 987 346 1059
Glycosidehydrolase BT_0986 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
E8MGH9 5.15e-08 1090 1231 1667 1811
Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 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
0.000755 0.550811 0.447146 0.000531 0.000440 0.000288

TMHMM  Annotations      download full data without filtering help

start end
7 29
1248 1270