Species | Clostridium sp900766315 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900766315 | |||||||||||
CAZyme ID | MGYG000003396_01351 | |||||||||||
CAZy Family | CBM61 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 24594; End: 28445 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH53 | 205 | 568 | 4.5e-91 | 0.9912280701754386 |
CBM61 | 63 | 194 | 3e-27 | 0.9716312056737588 |
CBM61 | 921 | 1057 | 1.5e-24 | 0.9716312056737588 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3867 | GanB | 5.88e-78 | 203 | 576 | 39 | 398 | Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism]. |
pfam07745 | Glyco_hydro_53 | 1.70e-76 | 205 | 569 | 2 | 333 | Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold. |
pfam13620 | CarboxypepD_reg | 1.45e-13 | 748 | 829 | 1 | 81 | Carboxypeptidase regulatory-like domain. |
pfam13620 | CarboxypepD_reg | 1.27e-11 | 662 | 742 | 1 | 81 | Carboxypeptidase regulatory-like domain. |
cd11308 | Peptidase_M14NE-CP-C_like | 9.05e-07 | 663 | 742 | 2 | 76 | Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain. This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QJS18184.1 | 5.37e-287 | 34 | 662 | 3 | 627 |
AGI39701.1 | 4.92e-264 | 57 | 1059 | 344 | 1350 |
AGC68692.1 | 4.92e-264 | 57 | 1059 | 344 | 1350 |
ANW99026.1 | 6.91e-264 | 57 | 1059 | 344 | 1350 |
ANX01554.1 | 1.91e-263 | 57 | 1059 | 344 | 1350 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7OSK_A | 2.76e-56 | 203 | 570 | 50 | 392 | ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230] |
1R8L_A | 3.05e-47 | 203 | 576 | 24 | 395 | Thestructure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1R8L_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1UR0_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR0_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],2CCR_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2CCR_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis] |
2GFT_A | 1.89e-46 | 203 | 576 | 24 | 395 | ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis] |
4BF7_A | 4.39e-38 | 192 | 529 | 9 | 324 | Emericillanidulans endo-beta-1,4-galactanase [Aspergillus nidulans] |
6GPA_A | 1.27e-36 | 199 | 520 | 3 | 286 | Beta-1,4-galactanasefrom Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482],6GPA_B Beta-1,4-galactanase from Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q65CX5 | 2.98e-46 | 203 | 576 | 49 | 420 | Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1 |
P48843 | 7.25e-45 | 199 | 578 | 2 | 355 | Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1 |
O07013 | 1.70e-44 | 203 | 575 | 53 | 423 | Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1 |
Q9Y7F8 | 1.69e-37 | 205 | 557 | 21 | 348 | Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus tubingensis OX=5068 GN=galA PE=2 SV=1 |
Q5B153 | 3.11e-37 | 192 | 529 | 9 | 324 | Arabinogalactan endo-beta-1,4-galactanase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=galA PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.841779 | 0.141694 | 0.015578 | 0.000657 | 0.000108 | 0.000178 |
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