Species | Phocaeicola coprocola | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola coprocola | |||||||||||
CAZyme ID | MGYG000001306_03049 | |||||||||||
CAZy Family | PL10 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 246225; End: 247841 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL10 | 119 | 402 | 5.9e-131 | 0.9963636363636363 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
TIGR02474 | pec_lyase | 9.51e-22 | 119 | 379 | 1 | 262 | pectate lyase, PelA/Pel-15E family. Members of this family are isozymes of pectate lyase (EC 4.2.2.2), also called polygalacturonic transeliminase and alpha-1,4-D-endopolygalacturonic acid lyase. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
pfam09492 | Pec_lyase | 1.93e-21 | 119 | 383 | 1 | 265 | Pectic acid lyase. Members of this family are isozymes of pectate lyase (EC:4.2.2.2), also called polygalacturonic transeliminase and alpha-1,4-D-endopolygalacturonic acid lyase. |
cd04434 | LanC_like | 0.006 | 84 | 200 | 3 | 134 | Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ADY38157.1 | 9.03e-298 | 1 | 534 | 1 | 536 |
QJR66990.1 | 4.00e-292 | 33 | 534 | 35 | 536 |
QJR71330.1 | 4.00e-292 | 33 | 534 | 35 | 536 |
QUT87327.1 | 4.00e-292 | 33 | 534 | 35 | 536 |
QJR62731.1 | 4.00e-292 | 33 | 534 | 35 | 536 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1R76_A | 3.32e-13 | 106 | 377 | 81 | 368 | ChainA, pectate lyase [Niveispirillum irakense] |
1GXM_A | 3.74e-11 | 112 | 384 | 37 | 300 | Family10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus],1GXM_B Family 10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus],1GXN_A Family 10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus] |
1GXO_A | 3.79e-10 | 112 | 384 | 37 | 300 | MutantD189A of Family 10 polysaccharide lyase from Cellvibrio cellulosa in complex with trigalaturonic acid [Cellvibrio japonicus] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000543 | 0.661836 | 0.336818 | 0.000281 | 0.000259 | 0.000219 |
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