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CAZyme Information: MGYG000001332_00635

You are here: Home > Sequence: MGYG000001332_00635

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_00635
CAZy Family GH106
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1324 146702.75 4.1321
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001332 3406391 Isolate not provided not provided
Gene Location Start: 743346;  End: 747320  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001332_00635.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH106 59 837 1.4e-73 0.808252427184466

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17132 Glyco_hydro_106 2.40e-19 215 794 334 872
alpha-L-rhamnosidase.
pfam07554 FIVAR 1.54e-04 1187 1255 2 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.
pfam17996 CE2_N 0.007 960 1024 42 108
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QGH71057.1 4.61e-304 12 1057 38 1140
AHF25191.1 7.45e-280 45 1048 49 1152
QGH70002.1 1.14e-136 9 1010 45 1089
SDG73971.1 2.32e-133 56 1010 5 936
QYN20448.1 1.96e-128 19 1016 18 1093

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5MQM_A 1.15e-06 331 1022 463 1077
Glycosidehydrolase BT_0986 [Bacteroides thetaiotaomicron],5MQN_A Glycoside hydrolase BT_0986 [Bacteroides thetaiotaomicron]
5MWK_A 1.15e-06 331 1022 463 1077
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
T2KNA8 1.64e-14 56 566 29 520
Putative beta-glucuronidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22040 PE=2 SV=1
P26831 7.81e-07 1083 1262 1384 1575
Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH PE=1 SV=2

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
0.000737 0.998181 0.000345 0.000283 0.000223 0.000188

TMHMM  Annotations      download full data without filtering help

start end
20 42
1298 1317