| Basic Information | |
|---|---|
| Species | Fragaria vesca |
| Cazyme ID | mrna28904.1-v1.0-hybrid |
| Family | GH29 |
| Protein Properties | Length: 572 Molecular Weight: 64264.7 Isoelectric Point: 6.3781 |
| Chromosome | Chromosome/Scaffold: 3 Start: 16763429 End: 16766669 |
| Description | alpha-L-fucosidase 1 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH29 | 99 | 395 | 0 |
| QLQWQLGHMAMFLHFGPNTFTDSEWGTGHVDPSVFNPTNLNATQWVQVAKDSGFSRVILTAKHHDGFCLWPTDYTNYSVSSSPWRNGGGDVVGELAKAAK DAGIGLGLYLSPWDRHEQCYGNTLEYNEFYMGQMTELLTRYGNIKEVWLDGAKGEGEKDMDYFFDSWFSLIHQHQPGAVIFSDAGPDTRWVGDEAGVAGS TCWSLFNRSSAKIGDTDFQYSRGGDPFGHDWVPAECDVSIRPGWFWHSSQVPKSARTLLELYCKSVGRNCLLLLNVPPNSSGLISAEDIEVLKEFSE | |||
| Full Sequence |
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| Protein Sequence Length: 572 Download |
| MWTCQQPLYF ASEFGVNLPK SKEATQPLQL HLSLFESLSL THIMIMKNKK NTHTPIPSSI 60 PRLHLLLLLS LSLSSTSCSS SLLKKPPPLP ILPLPSAPQL QWQLGHMAMF LHFGPNTFTD 120 SEWGTGHVDP SVFNPTNLNA TQWVQVAKDS GFSRVILTAK HHDGFCLWPT DYTNYSVSSS 180 PWRNGGGDVV GELAKAAKDA GIGLGLYLSP WDRHEQCYGN TLEYNEFYMG QMTELLTRYG 240 NIKEVWLDGA KGEGEKDMDY FFDSWFSLIH QHQPGAVIFS DAGPDTRWVG DEAGVAGSTC 300 WSLFNRSSAK IGDTDFQYSR GGDPFGHDWV PAECDVSIRP GWFWHSSQVP KSARTLLELY 360 CKSVGRNCLL LLNVPPNSSG LISAEDIEVL KEFSELRRSI FSQNLAKDAK IRASSTRGSA 420 NNSWFNPYNV VEEGFHSYWA PEENQSNWVL YFDLQELVSF NILLVEEPIH MGQRVIKFHL 480 QILNENGEWN KVTNGTTVGY RRLLQFPIVK SRNLRFVIEK SRAEPLISYL GLYMDPFSTL 540 SNISDSTTQT SINSSQILPH IDFNHSQIAV L* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01120 | Alpha_L_fucos | 5.0e-37 | 109 | 393 | 320 | + Alpha-L-fucosidase. | ||
| smart00812 | Alpha_L_fucos | 2.0e-39 | 133 | 393 | 282 | + Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis. | ||
| COG3669 | COG3669 | 2.0e-65 | 101 | 533 | 448 | + Alpha-L-fucosidase [Carbohydrate transport and metabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004560 | alpha-L-fucosidase activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0007155 | cell adhesion |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ues_B | 0 | 95 | 528 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
| PDB | 3ues_A | 0 | 95 | 528 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
| PDB | 3mo4_B | 0 | 95 | 528 | 21 | 473 | A Chain A, The Crystal Structure Of An Alpha-(1-3,4)-Fucosidase From Bifidobacterium Longum Subsp. Infantis Atcc 15697 |
| PDB | 3mo4_A | 0 | 95 | 528 | 21 | 473 | A Chain A, The Crystal Structure Of An Alpha-(1-3,4)-Fucosidase From Bifidobacterium Longum Subsp. Infantis Atcc 15697 |
| PDB | 3uet_B | 0 | 95 | 528 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis D172aE217A MUTANT COMPLEXED WITH LACTO-N- Fucopentaose Ii |
| Hydropathy |
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| Sequence Alignments (This image is cropped. Click for full image.) |
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