Species | Alistipes_A sp900240235 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900240235 | |||||||||||
CAZyme ID | MGYG000000170_01951 | |||||||||||
CAZy Family | PL35 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 36848; End: 38704 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL35 | 383 | 560 | 4.6e-60 | 0.9776536312849162 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam07940 | Hepar_II_III | 8.22e-09 | 383 | 519 | 20 | 152 | Heparinase II/III-like protein. This family features sequences that are similar to a region of the Flavobacterium heparinum proteins heparinase II and heparinase III. The former is known to degrade heparin and heparin sulphate, whereas the latter predominantly degrades heparin sulphate. Both are secreted into the periplasmic space upon induction with heparin. |
cd04434 | LanC_like | 5.37e-04 | 97 | 318 | 58 | 288 | 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 |
---|---|---|---|---|---|
QGA22620.1 | 0.0 | 1 | 618 | 1 | 618 |
QUT50613.1 | 7.41e-255 | 31 | 618 | 31 | 619 |
BCG53903.1 | 7.56e-250 | 12 | 606 | 8 | 603 |
QMW02098.1 | 2.23e-195 | 31 | 617 | 31 | 617 |
QJW90915.1 | 1.36e-194 | 32 | 618 | 34 | 621 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3A0O_A | 1.07e-11 | 35 | 518 | 139 | 648 | Crystalstructure of alginate lyase from Agrobacterium tumefaciens C58 [Agrobacterium fabrum str. C58],3A0O_B Crystal structure of alginate lyase from Agrobacterium tumefaciens C58 [Agrobacterium fabrum str. C58] |
3AFL_A | 1.69e-10 | 35 | 518 | 139 | 648 | Crystalstructure of exotype alginate lyase Atu3025 H531A complexed with alginate trisaccharide [Agrobacterium fabrum str. C58] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000214 | 0.999199 | 0.000145 | 0.000149 | 0.000139 | 0.000127 |
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