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CAZyme Information: MGYG000001542_02992

You are here: Home > Sequence: MGYG000001542_02992

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 Paenibacillus_A sp900069005
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005
CAZyme ID MGYG000001542_02992
CAZy Family GH136
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2274 MGYG000001542_36|CGC2 243079.1 4.4821
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001542 5846629 Isolate not provided not provided
Gene Location Start: 173881;  End: 180705  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001542_02992.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH136 1029 1610 4.6e-92 0.9918533604887984

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 1.78e-28 2187 2272 1 93
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam07833 Cu_amine_oxidN1 6.70e-18 2162 2217 38 93
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam09479 Flg_new 1.99e-12 1613 1678 1 65
Listeria-Bacteroides repeat domain (List_Bact_rpt). This model describes a conserved core region of about 43 residues, which occurs in at least two families of tandem repeats. These include 78-residue repeats which occur from 2 to 15 times in some proteins of Bacteroides forsythus ATCC 43037, and 70-residue repeats found in families of internalins of Listeria species. Single copies are found in proteins of Fibrobacter succinogenes, Geobacter sulfurreducens, and a few other bacteria.
pfam07833 Cu_amine_oxidN1 3.18e-08 2242 2274 1 33
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam05345 He_PIG 3.81e-08 1869 1941 1 83
Putative Ig domain. This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AZS16171.1 0.0 1 2274 1 2280
AIQ24130.1 0.0 1 2274 1 2257
AIQ74599.1 0.0 1 2274 1 2265
AIQ35957.1 0.0 1 2274 1 2258
AWV33927.1 0.0 1 2274 1 2265

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6KQT_A 9.44e-13 1031 1399 247 617
CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - native protein [Eubacterium ramulus ATCC 29099]
4M03_A 1.62e-07 1762 1938 19 193
ChainA, Serine-rich adhesin for platelets [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
P0DJ97 7.13e-13 1611 1679 661 729
Putative Gly-rich membrane protein Bcell_0380 OS=Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) OX=649639 GN=Bcell_0380 PE=4 SV=1
P0DJ98 1.17e-11 1611 1679 81 149
Putative membrane protein Bcell_0381 OS=Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) OX=649639 GN=Bcell_0381 PE=4 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
0.000302 0.998787 0.000322 0.000233 0.000187 0.000151

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001542_02992.