Species | Cellulosilyticum sp900556665 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Cellulosilyticaceae; Cellulosilyticum; Cellulosilyticum sp900556665 | |||||||||||
CAZyme ID | MGYG000000555_01051 | |||||||||||
CAZy Family | PL9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2955; End: 7175 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL9 | 690 | 1055 | 1.8e-119 | 0.9813333333333333 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam07833 | Cu_amine_oxidN1 | 6.53e-18 | 1326 | 1404 | 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 | 7.06e-14 | 1268 | 1356 | 15 | 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 | 6.71e-06 | 1374 | 1406 | 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. |
COG3401 | FN3 | 6.03e-04 | 165 | 405 | 97 | 328 | Fibronectin type 3 domain [General function prediction only]. |
pfam13229 | Beta_helix | 6.43e-04 | 768 | 906 | 18 | 141 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ACZ98649.1 | 0.0 | 391 | 1376 | 5 | 993 |
QEH68113.1 | 0.0 | 2 | 1377 | 80 | 1455 |
ADZ82419.1 | 0.0 | 2 | 1377 | 80 | 1460 |
ANC32378.1 | 3.41e-205 | 2 | 1085 | 58 | 1129 |
ANJ26032.1 | 8.50e-199 | 8 | 1079 | 65 | 1126 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1RU4_A | 2.25e-19 | 695 | 967 | 18 | 293 | ChainA, Pectate lyase [Dickeya chrysanthemi] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P22751 | 1.03e-42 | 354 | 973 | 86 | 646 | Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1 |
P0C1A6 | 2.05e-20 | 695 | 967 | 43 | 318 | Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1 |
P0C1A7 | 1.59e-18 | 695 | 967 | 43 | 318 | 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 |
---|---|---|---|---|---|
1.000077 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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