Species | UMGS1441 sp900543365 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; UMGS1441 sp900543365 | |||||||||||
CAZyme ID | MGYG000000967_00138 | |||||||||||
CAZy Family | PL9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 30496; End: 36648 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL9 | 1412 | 1833 | 2.4e-96 | 0.9813333333333333 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam07833 | Cu_amine_oxidN1 | 6.53e-20 | 1947 | 2046 | 3 | 90 | 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 | 5.66e-07 | 2019 | 2050 | 1 | 32 | 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 | 6.36e-06 | 1918 | 1985 | 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. |
pfam07523 | Big_3 | 0.004 | 735 | 793 | 4 | 57 | Bacterial Ig-like domain (group 3). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ANX00231.1 | 2.68e-160 | 294 | 1797 | 6 | 1225 |
AGI38277.1 | 1.81e-159 | 294 | 1797 | 6 | 1225 |
AGC67199.1 | 1.81e-159 | 294 | 1797 | 6 | 1225 |
ANW97669.1 | 1.81e-159 | 294 | 1797 | 6 | 1225 |
BAC87940.1 | 6.44e-159 | 294 | 1797 | 6 | 1225 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1RU4_A | 6.15e-33 | 1413 | 1706 | 13 | 295 | ChainA, Pectate lyase [Dickeya chrysanthemi] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P22751 | 6.05e-56 | 980 | 1708 | 59 | 644 | Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1 |
P0C1A6 | 6.03e-34 | 1413 | 1803 | 38 | 398 | Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1 |
P0C1A7 | 5.34e-32 | 1413 | 1706 | 38 | 320 | Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000272 | 0.998986 | 0.000196 | 0.000185 | 0.000173 | 0.000148 |
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