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Conserved domains on  [gi|71997700|ref|NP_510020|]
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Putative alpha-L-fucosidase [Caenorhabditis elegans]

Protein Classification

alpha-L-fucosidase( domain architecture ID 13925297)

alpha-L-fucosidase is a glycoside hydrolase 29 family protein that catalyzes the hydrolysis of an alpha-L-fucoside to form L-fucose and an alcohol

CAZY:  GH29
EC:  3.2.1.51
Gene Ontology:  GO:0004560|GO:0005975
SCOP:  3000313

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Alpha_L_fucos smart00812
Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that ...
12-377 0e+00

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.


:

Pssm-ID: 214829  Cd Length: 384  Bit Score: 520.70  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700     12 HLANCDYTPDWESLDNRPLPSWYDDSKFGIFCHWGLYSVPAFRSEWMWWywkgtQPDKDVVNFVDKNYKPGTTYADFAKD 91
Cdd:smart00812   1 GEAQGPYQPTWESLDKRPLPEWFRDAKFGIFIHWGVYSVPGFGGEWYWR-----QPGSPEYKHHIKNYGPEFGYKDFAPQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700     92 FTAEYFNANQFAETVKTSGARYFVFTSKHHEGFTMWPSRTSwNWNSMDIGPKRDIVGELRDAFKKTDVHFGLYFSQFEWF 171
Cdd:smart00812  76 FTAEKFDPEEWADLFKKAGAKYVVLTTKHHDGFCLWDSKYS-NWNAVDTGPKRDLVGELADAVRKRGLKFGLYHSLFDWF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    172 HPMFLD--------DGKFNTTFYPEQVsYPQMIDIVTKYNPEVVWSDGEWDKSDDYWKAKEFLAWLYNSSPVKDQVVVND 243
Cdd:smart00812 155 NPLYAGptssdedsDNWPRFQEFVDDW-LPQLRELVTRYKPDLLWFDGGWEAPDDYWRSKEFLAWLYNLSPVKDTVVVND 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    244 RWGtGTMGKHGGFMTYSDHYDPGKLLEKKWENCMTLDKhSWGNRRDMKASEVNTAYEIIEQLARTIACNGNLLLNVGPNM 323
Cdd:smart00812 234 RWG-GTGCKHGGFYTDEERGAPGKLLPHPWETCTTIGK-SWGYRRNESLSDYKSPKELIRDLVDIVSKGGNLLLNVGPKA 311
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 71997700    324 HGQIPAIFEDRLEEIGRFVNITSEAIFGTRPWIHQNDTSASNVWYTSKYSSGKK 377
Cdd:smart00812 312 DGTIPPEEEERLLEIGKWLKVNGEAIYGTRPWRIQGEGPTGEVWYTSTKKADNT 365
Fucosidase_C super family cl38499
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
358-463 7.57e-05

Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif.


The actual alignment was detected with superfamily member pfam16757:

Pssm-ID: 465259  Cd Length: 90  Bit Score: 41.50  E-value: 7.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700   358 QNDTSASNVWYTSKYSSGKkplknlyqnVYnfqleehTIVYAWILDTSHEQFELKSVKTTKNTTATILGTDVVLTGFEES 437
Cdd:pfam16757   1 QNDTVTPDVWYTSKPQEKA---------VY-------AIFLEWPKDGSLVLGSPVKTSGSTATQVTLLGYGEPLKWKQTS 64
                          90       100
                  ....*....|....*....|....*.
gi 71997700   438 DSMIILSSKIDWKKLPRRDIIVLKIE 463
Cdd:pfam16757  65 NGLKIELPQLTPDQLPCQWAWTLKLT 90
 
Name Accession Description Interval E-value
Alpha_L_fucos smart00812
Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that ...
12-377 0e+00

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.


Pssm-ID: 214829  Cd Length: 384  Bit Score: 520.70  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700     12 HLANCDYTPDWESLDNRPLPSWYDDSKFGIFCHWGLYSVPAFRSEWMWWywkgtQPDKDVVNFVDKNYKPGTTYADFAKD 91
Cdd:smart00812   1 GEAQGPYQPTWESLDKRPLPEWFRDAKFGIFIHWGVYSVPGFGGEWYWR-----QPGSPEYKHHIKNYGPEFGYKDFAPQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700     92 FTAEYFNANQFAETVKTSGARYFVFTSKHHEGFTMWPSRTSwNWNSMDIGPKRDIVGELRDAFKKTDVHFGLYFSQFEWF 171
Cdd:smart00812  76 FTAEKFDPEEWADLFKKAGAKYVVLTTKHHDGFCLWDSKYS-NWNAVDTGPKRDLVGELADAVRKRGLKFGLYHSLFDWF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    172 HPMFLD--------DGKFNTTFYPEQVsYPQMIDIVTKYNPEVVWSDGEWDKSDDYWKAKEFLAWLYNSSPVKDQVVVND 243
Cdd:smart00812 155 NPLYAGptssdedsDNWPRFQEFVDDW-LPQLRELVTRYKPDLLWFDGGWEAPDDYWRSKEFLAWLYNLSPVKDTVVVND 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    244 RWGtGTMGKHGGFMTYSDHYDPGKLLEKKWENCMTLDKhSWGNRRDMKASEVNTAYEIIEQLARTIACNGNLLLNVGPNM 323
Cdd:smart00812 234 RWG-GTGCKHGGFYTDEERGAPGKLLPHPWETCTTIGK-SWGYRRNESLSDYKSPKELIRDLVDIVSKGGNLLLNVGPKA 311
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 71997700    324 HGQIPAIFEDRLEEIGRFVNITSEAIFGTRPWIHQNDTSASNVWYTSKYSSGKK 377
Cdd:smart00812 312 DGTIPPEEEERLLEIGKWLKVNGEAIYGTRPWRIQGEGPTGEVWYTSTKKADNT 365
Alpha_L_fucos pfam01120
Alpha-L-fucosidase;
14-347 7.90e-160

Alpha-L-fucosidase;


Pssm-ID: 460072  Cd Length: 333  Bit Score: 455.90  E-value: 7.90e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    14 ANCDYTPDWESLDNRPLPSWYDDSKFGIFCHWGLYSVPAFRSEWMWWYWKGtQPDKDVVNFVDKNYKPGTTYADFAKDFT 93
Cdd:pfam01120   2 ASGKYEPTWESLDARPLPEWFDDAKFGIFIHWGVYSVPAFGSEWYWRNMYI-PGSPQYVEHMKYGYPPDFGYADFAPQFN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    94 AEYFNANQFAETVKTSGARYFVFTSKHHEGFTMWPSRTSWnWNSMDIGPKRDIVGELRDAFKKTDVHFGLYFSQFEWFHP 173
Cdd:pfam01120  81 AEKFDPDEWADLFKAAGAKYVVLTTKHHDGFTMWDSKYSD-WNSVDVGPKRDLVGELAKAVRKQGLKFGLYYSLADWFNP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700   174 MFLDDgKFNTTFYPEQVSY-----PQMIDIVTKYNPEVVWSDGEWD-KSDDYWKAKEFLAWLYNS-SPVKdQVVVNDRWG 246
Cdd:pfam01120 160 DYYPD-KAGNTDRTTQYEYkeftlPQLKELVTNYGPDIIWFDGDWPeYYNQYWNSTEFLAWLYNElSPVK-TVVVNDRWG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700   247 TGTMgkHGGFMTYSDHYDPGKLLEKKWENCMTLDKhSWGNRRDMkaSEVNTAYEIIEQLARTIACNGNLLLNVGPNMHGQ 326
Cdd:pfam01120 238 KGPR--HGGDYQTPERGLPGELLAHPWETCTTIGG-SWGYRRND--QDYKSAKELIHLLVDIVSKGGNLLLNIGPTADGT 312
                         330       340
                  ....*....|....*....|.
gi 71997700   327 IPAIFEDRLEEIGRFVNITSE 347
Cdd:pfam01120 313 IPPEAEERLLEIGKWLKVNGE 333
AfuC COG3669
Alpha-L-fucosidase [Carbohydrate transport and metabolism];
33-442 3.92e-95

Alpha-L-fucosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442886 [Multi-domain]  Cd Length: 401  Bit Score: 293.37  E-value: 3.92e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700  33 WYDDSKFGIFCHWGLYSVPAFRsEWMWWYWKGTQPDkdvvnfvdknykpgttYADFAKDFTAEYFNANQFAETVKTSGAR 112
Cdd:COG3669  30 WFQDAKFGIFIHWGLYSVPGGA-EWYMRYGKIPKFG----------------YKDLAKLFNPEKFDADQWARLAKDAGAK 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700 113 YFVFTSKHHEGFTMWPSRTSwNWNSMDIGP-KRDIVGELRDAFKKTDVHFGLYFSQFEWFHPMFLDDGKFNTTfyPE--Q 189
Cdd:COG3669  93 YVVLTAKHHDGFCLWDSKYT-DYNVVDNSPwKRDVVKELAEACRKEGLKFGLYYSPWDWHHPDYPYGPKPPDW--PEylE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700 190 VSYPQMIDIVTKYNP-EVVWSDGEWDKS-DDYWKAKEFLAWLYNSSPvkdQVVVNDRWGtgtMGKHGGFMTySDHYDPGK 267
Cdd:COG3669 170 YWLNQLKELLTNYGPiDELWFDGAWPNGkRQEWDSPELYALIRNLQP---EAVINDRLG---LPPGPDYVT-PERGIPTE 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700 268 LLEKKWENCMTLDkHSWGNRRDMKaseVNTAYEIIEQLARTIACNGNLLLNVGPNMHGQIPAIFEDRLEEIGRFVNITSE 347
Cdd:COG3669 243 IPPGPWETCTTIG-PSWGYHEDDK---YKSPEELIDILVDSVSKGGNLLLNIGPDADGTIPEEDVERLKEIGAWLKVNGE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700 348 AIFGTRPWIHQNDTsasNVWYTSKyssgkkplknlyqnvynfqleeHTIVYAWILDTSHEQFELKSVKTTKN-TTATILG 426
Cdd:COG3669 319 AIYGTRPKVAGLDE---DTRFTTK----------------------GNALYAIVLGWPENGIVLQELALGQRvKSVELLG 373
                       410
                ....*....|....*.
gi 71997700 427 TDVVLTgFEESDSMII 442
Cdd:COG3669 374 TGKRIR-FEQTDKLRI 388
Fucosidase_C pfam16757
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
358-463 7.57e-05

Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif.


Pssm-ID: 465259  Cd Length: 90  Bit Score: 41.50  E-value: 7.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700   358 QNDTSASNVWYTSKYSSGKkplknlyqnVYnfqleehTIVYAWILDTSHEQFELKSVKTTKNTTATILGTDVVLTGFEES 437
Cdd:pfam16757   1 QNDTVTPDVWYTSKPQEKA---------VY-------AIFLEWPKDGSLVLGSPVKTSGSTATQVTLLGYGEPLKWKQTS 64
                          90       100
                  ....*....|....*....|....*.
gi 71997700   438 DSMIILSSKIDWKKLPRRDIIVLKIE 463
Cdd:pfam16757  65 NGLKIELPQLTPDQLPCQWAWTLKLT 90
 
Name Accession Description Interval E-value
Alpha_L_fucos smart00812
Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that ...
12-377 0e+00

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.


Pssm-ID: 214829  Cd Length: 384  Bit Score: 520.70  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700     12 HLANCDYTPDWESLDNRPLPSWYDDSKFGIFCHWGLYSVPAFRSEWMWWywkgtQPDKDVVNFVDKNYKPGTTYADFAKD 91
Cdd:smart00812   1 GEAQGPYQPTWESLDKRPLPEWFRDAKFGIFIHWGVYSVPGFGGEWYWR-----QPGSPEYKHHIKNYGPEFGYKDFAPQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700     92 FTAEYFNANQFAETVKTSGARYFVFTSKHHEGFTMWPSRTSwNWNSMDIGPKRDIVGELRDAFKKTDVHFGLYFSQFEWF 171
Cdd:smart00812  76 FTAEKFDPEEWADLFKKAGAKYVVLTTKHHDGFCLWDSKYS-NWNAVDTGPKRDLVGELADAVRKRGLKFGLYHSLFDWF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    172 HPMFLD--------DGKFNTTFYPEQVsYPQMIDIVTKYNPEVVWSDGEWDKSDDYWKAKEFLAWLYNSSPVKDQVVVND 243
Cdd:smart00812 155 NPLYAGptssdedsDNWPRFQEFVDDW-LPQLRELVTRYKPDLLWFDGGWEAPDDYWRSKEFLAWLYNLSPVKDTVVVND 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    244 RWGtGTMGKHGGFMTYSDHYDPGKLLEKKWENCMTLDKhSWGNRRDMKASEVNTAYEIIEQLARTIACNGNLLLNVGPNM 323
Cdd:smart00812 234 RWG-GTGCKHGGFYTDEERGAPGKLLPHPWETCTTIGK-SWGYRRNESLSDYKSPKELIRDLVDIVSKGGNLLLNVGPKA 311
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 71997700    324 HGQIPAIFEDRLEEIGRFVNITSEAIFGTRPWIHQNDTSASNVWYTSKYSSGKK 377
Cdd:smart00812 312 DGTIPPEEEERLLEIGKWLKVNGEAIYGTRPWRIQGEGPTGEVWYTSTKKADNT 365
Alpha_L_fucos pfam01120
Alpha-L-fucosidase;
14-347 7.90e-160

Alpha-L-fucosidase;


Pssm-ID: 460072  Cd Length: 333  Bit Score: 455.90  E-value: 7.90e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    14 ANCDYTPDWESLDNRPLPSWYDDSKFGIFCHWGLYSVPAFRSEWMWWYWKGtQPDKDVVNFVDKNYKPGTTYADFAKDFT 93
Cdd:pfam01120   2 ASGKYEPTWESLDARPLPEWFDDAKFGIFIHWGVYSVPAFGSEWYWRNMYI-PGSPQYVEHMKYGYPPDFGYADFAPQFN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700    94 AEYFNANQFAETVKTSGARYFVFTSKHHEGFTMWPSRTSWnWNSMDIGPKRDIVGELRDAFKKTDVHFGLYFSQFEWFHP 173
Cdd:pfam01120  81 AEKFDPDEWADLFKAAGAKYVVLTTKHHDGFTMWDSKYSD-WNSVDVGPKRDLVGELAKAVRKQGLKFGLYYSLADWFNP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700   174 MFLDDgKFNTTFYPEQVSY-----PQMIDIVTKYNPEVVWSDGEWD-KSDDYWKAKEFLAWLYNS-SPVKdQVVVNDRWG 246
Cdd:pfam01120 160 DYYPD-KAGNTDRTTQYEYkeftlPQLKELVTNYGPDIIWFDGDWPeYYNQYWNSTEFLAWLYNElSPVK-TVVVNDRWG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700   247 TGTMgkHGGFMTYSDHYDPGKLLEKKWENCMTLDKhSWGNRRDMkaSEVNTAYEIIEQLARTIACNGNLLLNVGPNMHGQ 326
Cdd:pfam01120 238 KGPR--HGGDYQTPERGLPGELLAHPWETCTTIGG-SWGYRRND--QDYKSAKELIHLLVDIVSKGGNLLLNIGPTADGT 312
                         330       340
                  ....*....|....*....|.
gi 71997700   327 IPAIFEDRLEEIGRFVNITSE 347
Cdd:pfam01120 313 IPPEAEERLLEIGKWLKVNGE 333
AfuC COG3669
Alpha-L-fucosidase [Carbohydrate transport and metabolism];
33-442 3.92e-95

Alpha-L-fucosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442886 [Multi-domain]  Cd Length: 401  Bit Score: 293.37  E-value: 3.92e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700  33 WYDDSKFGIFCHWGLYSVPAFRsEWMWWYWKGTQPDkdvvnfvdknykpgttYADFAKDFTAEYFNANQFAETVKTSGAR 112
Cdd:COG3669  30 WFQDAKFGIFIHWGLYSVPGGA-EWYMRYGKIPKFG----------------YKDLAKLFNPEKFDADQWARLAKDAGAK 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700 113 YFVFTSKHHEGFTMWPSRTSwNWNSMDIGP-KRDIVGELRDAFKKTDVHFGLYFSQFEWFHPMFLDDGKFNTTfyPE--Q 189
Cdd:COG3669  93 YVVLTAKHHDGFCLWDSKYT-DYNVVDNSPwKRDVVKELAEACRKEGLKFGLYYSPWDWHHPDYPYGPKPPDW--PEylE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700 190 VSYPQMIDIVTKYNP-EVVWSDGEWDKS-DDYWKAKEFLAWLYNSSPvkdQVVVNDRWGtgtMGKHGGFMTySDHYDPGK 267
Cdd:COG3669 170 YWLNQLKELLTNYGPiDELWFDGAWPNGkRQEWDSPELYALIRNLQP---EAVINDRLG---LPPGPDYVT-PERGIPTE 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700 268 LLEKKWENCMTLDkHSWGNRRDMKaseVNTAYEIIEQLARTIACNGNLLLNVGPNMHGQIPAIFEDRLEEIGRFVNITSE 347
Cdd:COG3669 243 IPPGPWETCTTIG-PSWGYHEDDK---YKSPEELIDILVDSVSKGGNLLLNIGPDADGTIPEEDVERLKEIGAWLKVNGE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700 348 AIFGTRPWIHQNDTsasNVWYTSKyssgkkplknlyqnvynfqleeHTIVYAWILDTSHEQFELKSVKTTKN-TTATILG 426
Cdd:COG3669 319 AIYGTRPKVAGLDE---DTRFTTK----------------------GNALYAIVLGWPENGIVLQELALGQRvKSVELLG 373
                       410
                ....*....|....*.
gi 71997700 427 TDVVLTgFEESDSMII 442
Cdd:COG3669 374 TGKRIR-FEQTDKLRI 388
Fucosidase_C pfam16757
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
358-463 7.57e-05

Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif.


Pssm-ID: 465259  Cd Length: 90  Bit Score: 41.50  E-value: 7.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997700   358 QNDTSASNVWYTSKYSSGKkplknlyqnVYnfqleehTIVYAWILDTSHEQFELKSVKTTKNTTATILGTDVVLTGFEES 437
Cdd:pfam16757   1 QNDTVTPDVWYTSKPQEKA---------VY-------AIFLEWPKDGSLVLGSPVKTSGSTATQVTLLGYGEPLKWKQTS 64
                          90       100
                  ....*....|....*....|....*.
gi 71997700   438 DSMIILSSKIDWKKLPRRDIIVLKIE 463
Cdd:pfam16757  65 NGLKIELPQLTPDQLPCQWAWTLKLT 90
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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