Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Arcanobacterium_A; | |||||||||||
CAZyme ID | MGYG000000642_00581 | |||||||||||
CAZy Family | GH95 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 141458; End: 145669 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH95 | 401 | 1204 | 1.1e-238 | 0.9695290858725761 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam14498 | Glyco_hyd_65N_2 | 6.45e-67 | 376 | 642 | 1 | 233 | Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain. |
NF033679 | DNRLRE_dom | 4.45e-07 | 84 | 274 | 4 | 164 | DNRLRE domain. The DNRLRE domain, with a length of about 160 amino acids, appears typically in large, repetitive surface proteins of bacteria and archaea, sometimes repeated several times. It occurs, notably, three times in the C-terminal region of the enzyme disaggregatase from the archaeal species Methanosarcina mazei, each time with the motif DNRLRE, for which the domain is named. Archaeal proteins within this family are described particularly well by the currently more narrowly defined Pfam model, PF06848. Note that the catalytic region of disaggregatase, in the N-terminal portion of the protein, is modeled by a different HMM, PF08480. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QSY56848.1 | 0.0 | 64 | 1242 | 52 | 1229 |
QTB91571.1 | 0.0 | 64 | 1242 | 52 | 1229 |
AXM92304.1 | 0.0 | 58 | 1242 | 270 | 1471 |
QRI58870.1 | 0.0 | 58 | 1242 | 270 | 1471 |
AFL03772.1 | 0.0 | 58 | 1242 | 270 | 1471 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2EAB_A | 0.0 | 367 | 1242 | 11 | 896 | Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum] |
2EAD_A | 0.0 | 367 | 1242 | 11 | 896 | ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum] |
2EAE_A | 0.0 | 367 | 1242 | 10 | 895 | ChainA, Alpha-fucosidase [Bifidobacterium bifidum] |
2RDY_A | 7.41e-105 | 408 | 1240 | 18 | 789 | ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125] |
4UFC_A | 2.14e-103 | 370 | 1200 | 17 | 742 | Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8L7W8 | 2.03e-83 | 395 | 1191 | 55 | 804 | Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1 |
A2R797 | 4.75e-81 | 408 | 1186 | 39 | 763 | Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1 |
Q5AU81 | 2.27e-63 | 410 | 1189 | 46 | 786 | Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1 |
Q2USL3 | 2.44e-46 | 410 | 1192 | 35 | 708 | Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.011426 | 0.986811 | 0.000598 | 0.000629 | 0.000277 | 0.000232 |
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