y
Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.007G063900.1 |
Family | GH29 |
Protein Properties | Length: 495 Molecular Weight: 56099.9 Isoelectric Point: 7.0345 |
Chromosome | Chromosome/Scaffold: 07 Start: 5630097 End: 5632192 |
Description | alpha-L-fucosidase 1 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH29 | 49 | 347 | 0 |
SQIKWQQREIVMFLHFGVNTFTDKEWGTGKENPAIFNPTGLNTTQWATVAADAGISLMILTAKHHDGFCLWPSKYTDHSVISSPWQGGKGDVVQDFVNAA TAQGIDVGIYLSPWDRHDPRYGNDLLYNQYYLAQLQELLKKYQNVREIWFDGAKGPKAKNMSYYFSDWFSMVKELQSSINIFSDAGPDVRWVGEETGSAG YTCWSTINRTSLSIGNPNITRYLRSGDPKGTDWVPAECDISIRPGWFWHKSESPKKLSLLLDVYYNSVGRNCVLLLNVPPNKTGLITDVDAQRLKEFRS |
Full Sequence |
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Protein Sequence Length: 495 Download |
MSMMVRLRLW WSSLFIIFTL LFQQLRFCTS GSVQTPVPPL PILPLPTYSQ IKWQQREIVM 60 FLHFGVNTFT DKEWGTGKEN PAIFNPTGLN TTQWATVAAD AGISLMILTA KHHDGFCLWP 120 SKYTDHSVIS SPWQGGKGDV VQDFVNAATA QGIDVGIYLS PWDRHDPRYG NDLLYNQYYL 180 AQLQELLKKY QNVREIWFDG AKGPKAKNMS YYFSDWFSMV KELQSSINIF SDAGPDVRWV 240 GEETGSAGYT CWSTINRTSL SIGNPNITRY LRSGDPKGTD WVPAECDISI RPGWFWHKSE 300 SPKKLSLLLD VYYNSVGRNC VLLLNVPPNK TGLITDVDAQ RLKEFRSAID TIFHHNLAED 360 GSIKVSSERM GFGAENMVDS DHLWSYWAPE DDGGEKEHWI EIWAREGNLL RFNVIAIQEA 420 IGLGQRIKGH QIYVDGKLMV EATTVGYKRL HRLDAGEVHA RVVRITITQT RALPLISSIG 480 LYFDPFSHSK FTVT* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd08666 | APC10-HECTD3 | 0.001 | 362 | 407 | 46 | + APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination. This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases. | ||
smart00812 | Alpha_L_fucos | 6.0e-21 | 84 | 345 | 281 | + 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. | ||
pfam01120 | Alpha_L_fucos | 5.0e-22 | 60 | 345 | 309 | + Alpha-L-fucosidase. | ||
COG3669 | COG3669 | 3.0e-51 | 50 | 482 | 444 | + Alpha-L-fucosidase [Carbohydrate transport and metabolism] |
Gene Ontology | |
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GO Term | Description |
GO:0004560 | alpha-L-fucosidase activity |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002270630.1 | 0 | 49 | 488 | 22 | 461 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002270674.1 | 0 | 37 | 492 | 7 | 464 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002318264.1 | 0 | 50 | 492 | 41 | 485 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002322431.1 | 0 | 15 | 488 | 7 | 482 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510887.1 | 0 | 11 | 486 | 5 | 480 | alpha-l-fucosidase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3eyp_B | 0 | 41 | 482 | 5 | 454 | A Chain A, Crystal Structure Of Putative Alpha-L-Fucosidase From Bacteroides Thetaiotaomicron |
PDB | 3eyp_A | 0 | 41 | 482 | 5 | 454 | A Chain A, Crystal Structure Of Putative Alpha-L-Fucosidase From Bacteroides Thetaiotaomicron |
PDB | 3ues_B | 0 | 46 | 477 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
PDB | 3ues_A | 0 | 46 | 477 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
PDB | 3mo4_B | 0 | 46 | 477 | 21 | 473 | A Chain A, The Crystal Structure Of An Alpha-(1-3,4)-Fucosidase From Bifidobacterium Longum Subsp. Infantis Atcc 15697 |