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Conserved domains on  [gi|568786806|pdb|4NI3|B]
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Chain B, Alpha-fucosidase GH29

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 ...
1-434 9.96e-137

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: 402.82  E-value: 9.96e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B           1 AKADGPYEATWESTDKHnAAPEWYRDAKFGVYWHWGAFTTAQYASEWYPRNMYepdSDQRKHHTETYGPpeEWGYENFIK 80
Cdd:smart00812   1 GEAQGPYQPTWESLDKR-PLPEWFRDAKFGIFIHWGVYSVPGFGGEWYWRQPG---SPEYKHHIKNYGP--EFGYKDFAP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B          81 gakdkkgnfvQFKPVLkskggeFDPEAIIKIVKGSGARFAGPVAEHHDGFSMWDSKVNEWNPVNYGPKLDLVKLWADLVR 160
Cdd:smart00812  75 ----------QFTAEK------FDPEEWADLFKKAGAKYVVLTTKHHDGFCLWDSKYSNWNAVDTGPKRDLVGELADAVR 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         161 ENDMKLVIamhqaynYNGFFQW-APKTND-TSLQKLLGQLPRDEEDQ-LWFDKHREMLDHVQPDIIWNDFSLDSPgecgs 237
Cdd:smart00812 139 KRGLKFGL-------YHSLFDWfNPLYAGpTSSDEDSDNWPRFQEFVdDWLPQLRELVTRYKPDLLWFDGGWEAP----- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         238 fegpcaVDEQKRLEFLAYYFNRGEEWGkEVVTTYKHHDHGFRNTSAVDDWERGGPSNLVRPYWQTDDAISaSSWSYTVGI 317
Cdd:smart00812 207 ------DDYWRSKEFLAWLYNLSPVKD-TVVVNDRWGGTGCKHGGFYTDEERGAPGKLLPHPWETCTTIG-KSWGYRRNE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         318 K---YYSSKAMVHSLLDRVSKNGNMLLNISPMANGVLPEEQIKVLNDIGDFLSRYGEAVYDTRAWDIYGEGPNQVEGGSf 394
Cdd:smart00812 279 SlsdYKSPKELIRDLVDIVSKGGNLLLNVGPKADGTIPPEEEERLLEIGKWLKVNGEAIYGTRPWRIQGEGPTGEVWYT- 357
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
4NI3_B         395 taplqgnssdirfTRNKEDDVLYVTVLGWPEDNLVSVKNL 434
Cdd:smart00812 358 -------------STKKADNTLYAIVLDWPEDGEVTLKSL 384
Fucosidase_C super family cl38499
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
404-490 6.64e-10

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: 56.14  E-value: 6.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B        404 DIRFTRNKEDDVLYVTVLGWPEDNLVsvkNLGSNALVDLESLKSVELLGdkagdYVKVSEWEQSKDALDITLPSQPAESL 483
Cdd:pfam16757   8 DVWYTSKPQEKAVYAIFLEWPKDGSL---VLGSPVKTSGSTATQVTLLG-----YGEPLKWKQTSNGLKIELPQLTPDQL 79
                          90
                  ....*....|.
4NI3_B        484 ----AYVLKLT 490
Cdd:pfam16757  80 pcqwAWTLKLT 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 ...
1-434 9.96e-137

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: 402.82  E-value: 9.96e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B           1 AKADGPYEATWESTDKHnAAPEWYRDAKFGVYWHWGAFTTAQYASEWYPRNMYepdSDQRKHHTETYGPpeEWGYENFIK 80
Cdd:smart00812   1 GEAQGPYQPTWESLDKR-PLPEWFRDAKFGIFIHWGVYSVPGFGGEWYWRQPG---SPEYKHHIKNYGP--EFGYKDFAP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B          81 gakdkkgnfvQFKPVLkskggeFDPEAIIKIVKGSGARFAGPVAEHHDGFSMWDSKVNEWNPVNYGPKLDLVKLWADLVR 160
Cdd:smart00812  75 ----------QFTAEK------FDPEEWADLFKKAGAKYVVLTTKHHDGFCLWDSKYSNWNAVDTGPKRDLVGELADAVR 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         161 ENDMKLVIamhqaynYNGFFQW-APKTND-TSLQKLLGQLPRDEEDQ-LWFDKHREMLDHVQPDIIWNDFSLDSPgecgs 237
Cdd:smart00812 139 KRGLKFGL-------YHSLFDWfNPLYAGpTSSDEDSDNWPRFQEFVdDWLPQLRELVTRYKPDLLWFDGGWEAP----- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         238 fegpcaVDEQKRLEFLAYYFNRGEEWGkEVVTTYKHHDHGFRNTSAVDDWERGGPSNLVRPYWQTDDAISaSSWSYTVGI 317
Cdd:smart00812 207 ------DDYWRSKEFLAWLYNLSPVKD-TVVVNDRWGGTGCKHGGFYTDEERGAPGKLLPHPWETCTTIG-KSWGYRRNE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         318 K---YYSSKAMVHSLLDRVSKNGNMLLNISPMANGVLPEEQIKVLNDIGDFLSRYGEAVYDTRAWDIYGEGPNQVEGGSf 394
Cdd:smart00812 279 SlsdYKSPKELIRDLVDIVSKGGNLLLNVGPKADGTIPPEEEERLLEIGKWLKVNGEAIYGTRPWRIQGEGPTGEVWYT- 357
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
4NI3_B         395 taplqgnssdirfTRNKEDDVLYVTVLGWPEDNLVSVKNL 434
Cdd:smart00812 358 -------------STKKADNTLYAIVLDWPEDGEVTLKSL 384
Alpha_L_fucos pfam01120
Alpha-L-fucosidase;
3-371 3.63e-116

Alpha-L-fucosidase;


Pssm-ID: 460072  Cd Length: 333  Bit Score: 348.43  E-value: 3.63e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B          3 ADGPYEATWESTDKHnAAPEWYRDAKFGVYWHWGAFTTAQYASEWYPRNMYEPDSDQRKHHTeTYGPPEEWGYENFIKga 82
Cdd:pfam01120   2 ASGKYEPTWESLDAR-PLPEWFDDAKFGIFIHWGVYSVPAFGSEWYWRNMYIPGSPQYVEHM-KYGYPPDFGYADFAP-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         83 kdkkgnfvQFKPVLkskggeFDPEAIIKIVKGSGARFAGPVAEHHDGFSMWDSKVNEWNPVNYGPKLDLVKLWADLVREN 162
Cdd:pfam01120  78 --------QFNAEK------FDPDEWADLFKAAGAKYVVLTTKHHDGFTMWDSKYSDWNSVDVGPKRDLVGELAKAVRKQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B        163 DMKLVIAMHQA--YNYNGFFQWAPKTNDTSlqkllgqlpRDEEDQLWFDKHREMLDHVQPDIIWNDFSLDspgecgsfeg 240
Cdd:pfam01120 144 GLKFGLYYSLAdwFNPDYYPDKAGNTDRTT---------QYEYKEFTLPQLKELVTNYGPDIIWFDGDWP---------- 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B        241 pcavdeqkrleflaYYFNRGEEWGKEVVTTYKHHDHGFrnTSAVDD--------------WERGGPSNLVRPYWQTDDAI 306
Cdd:pfam01120 205 --------------EYYNQYWNSTEFLAWLYNELSPVK--TVVVNDrwgkgprhggdyqtPERGLPGELLAHPWETCTTI 268
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
4NI3_B        307 SAsSWSYTVGI-KYYSSKAMVHSLLDRVSKNGNMLLNISPMANGVLPEEQIKVLNDIGDFLSRYGE 371
Cdd:pfam01120 269 GG-SWGYRRNDqDYKSAKELIHLLVDIVSKGGNLLLNIGPTADGTIPPEAEERLLEIGKWLKVNGE 333
AfuC COG3669
Alpha-L-fucosidase [Carbohydrate transport and metabolism];
22-484 1.91e-85

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


Pssm-ID: 442886 [Multi-domain]  Cd Length: 401  Bit Score: 271.41  E-value: 1.91e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B       22 EWYRDAKFGVYWHWGAFTTAQYAsEWYPRnmyepdsdqrkhhtetYGPPEEWGYENFIKgakdkkgnfvQFKPVlkskgg 101
Cdd:COG3669  29 LWFQDAKFGIFIHWGLYSVPGGA-EWYMR----------------YGKIPKFGYKDLAK----------LFNPE------ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B      102 EFDPEAIIKIVKGSGARFAGPVAEHHDGFSMWDSKVNEWNPVNYGP-KLDLVKLWADLVRENDMKLVIAMHQAYNYNGFF 180
Cdd:COG3669  76 KFDADQWARLAKDAGAKYVVLTAKHHDGFCLWDSKYTDYNVVDNSPwKRDVVKELAEACRKEGLKFGLYYSPWDWHHPDY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B      181 QWAPKTNDTslqkllgqlprDEEDQLWFDKHREMLDHVQP-DIIWNDFSLDSPGEcgsfegpcavDEQKRLEFLAYYFNr 259
Cdd:COG3669 156 PYGPKPPDW-----------PEYLEYWLNQLKELLTNYGPiDELWFDGAWPNGKR----------QEWDSPELYALIRN- 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B      260 geeWGKEVVTTYKHHDHGFRNtsaVDDWERGGPSNLVRPYWQTDDAISaSSWSYTVGIKYYSSKAMVHSLLDRVSKNGNM 339
Cdd:COG3669 214 ---LQPEAVINDRLGLPPGPD---YVTPERGIPTEIPPGPWETCTTIG-PSWGYHEDDKYKSPEELIDILVDSVSKGGNL 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B      340 LLNISPMANGVLPEEQIKVLNDIGDFLSRYGEAVYDTRawdiygegpnqveggsftAPLQGNSSDIRFTRNkeDDVLYVT 419
Cdd:COG3669 287 LLNIGPDADGTIPEEDVERLKEIGAWLKVNGEAIYGTR------------------PKVAGLDEDTRFTTK--GNALYAI 346
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
4NI3_B      420 VLGWPEDNLVsVKNLGSNALVdleslKSVELLGDKagdyvKVSEWEQSkDALDITLPSQPAESLA 484
Cdd:COG3669 347 VLGWPENGIV-LQELALGQRV-----KSVELLGTG-----KRIRFEQT-DKLRITIPEKAPSEFA 399
Fucosidase_C pfam16757
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
404-490 6.64e-10

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: 56.14  E-value: 6.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B        404 DIRFTRNKEDDVLYVTVLGWPEDNLVsvkNLGSNALVDLESLKSVELLGdkagdYVKVSEWEQSKDALDITLPSQPAESL 483
Cdd:pfam16757   8 DVWYTSKPQEKAVYAIFLEWPKDGSL---VLGSPVKTSGSTATQVTLLG-----YGEPLKWKQTSNGLKIELPQLTPDQL 79
                          90
                  ....*....|.
4NI3_B        484 ----AYVLKLT 490
Cdd:pfam16757  80 pcqwAWTLKLT 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 ...
1-434 9.96e-137

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: 402.82  E-value: 9.96e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B           1 AKADGPYEATWESTDKHnAAPEWYRDAKFGVYWHWGAFTTAQYASEWYPRNMYepdSDQRKHHTETYGPpeEWGYENFIK 80
Cdd:smart00812   1 GEAQGPYQPTWESLDKR-PLPEWFRDAKFGIFIHWGVYSVPGFGGEWYWRQPG---SPEYKHHIKNYGP--EFGYKDFAP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B          81 gakdkkgnfvQFKPVLkskggeFDPEAIIKIVKGSGARFAGPVAEHHDGFSMWDSKVNEWNPVNYGPKLDLVKLWADLVR 160
Cdd:smart00812  75 ----------QFTAEK------FDPEEWADLFKKAGAKYVVLTTKHHDGFCLWDSKYSNWNAVDTGPKRDLVGELADAVR 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         161 ENDMKLVIamhqaynYNGFFQW-APKTND-TSLQKLLGQLPRDEEDQ-LWFDKHREMLDHVQPDIIWNDFSLDSPgecgs 237
Cdd:smart00812 139 KRGLKFGL-------YHSLFDWfNPLYAGpTSSDEDSDNWPRFQEFVdDWLPQLRELVTRYKPDLLWFDGGWEAP----- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         238 fegpcaVDEQKRLEFLAYYFNRGEEWGkEVVTTYKHHDHGFRNTSAVDDWERGGPSNLVRPYWQTDDAISaSSWSYTVGI 317
Cdd:smart00812 207 ------DDYWRSKEFLAWLYNLSPVKD-TVVVNDRWGGTGCKHGGFYTDEERGAPGKLLPHPWETCTTIG-KSWGYRRNE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         318 K---YYSSKAMVHSLLDRVSKNGNMLLNISPMANGVLPEEQIKVLNDIGDFLSRYGEAVYDTRAWDIYGEGPNQVEGGSf 394
Cdd:smart00812 279 SlsdYKSPKELIRDLVDIVSKGGNLLLNVGPKADGTIPPEEEERLLEIGKWLKVNGEAIYGTRPWRIQGEGPTGEVWYT- 357
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
4NI3_B         395 taplqgnssdirfTRNKEDDVLYVTVLGWPEDNLVSVKNL 434
Cdd:smart00812 358 -------------STKKADNTLYAIVLDWPEDGEVTLKSL 384
Alpha_L_fucos pfam01120
Alpha-L-fucosidase;
3-371 3.63e-116

Alpha-L-fucosidase;


Pssm-ID: 460072  Cd Length: 333  Bit Score: 348.43  E-value: 3.63e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B          3 ADGPYEATWESTDKHnAAPEWYRDAKFGVYWHWGAFTTAQYASEWYPRNMYEPDSDQRKHHTeTYGPPEEWGYENFIKga 82
Cdd:pfam01120   2 ASGKYEPTWESLDAR-PLPEWFDDAKFGIFIHWGVYSVPAFGSEWYWRNMYIPGSPQYVEHM-KYGYPPDFGYADFAP-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B         83 kdkkgnfvQFKPVLkskggeFDPEAIIKIVKGSGARFAGPVAEHHDGFSMWDSKVNEWNPVNYGPKLDLVKLWADLVREN 162
Cdd:pfam01120  78 --------QFNAEK------FDPDEWADLFKAAGAKYVVLTTKHHDGFTMWDSKYSDWNSVDVGPKRDLVGELAKAVRKQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B        163 DMKLVIAMHQA--YNYNGFFQWAPKTNDTSlqkllgqlpRDEEDQLWFDKHREMLDHVQPDIIWNDFSLDspgecgsfeg 240
Cdd:pfam01120 144 GLKFGLYYSLAdwFNPDYYPDKAGNTDRTT---------QYEYKEFTLPQLKELVTNYGPDIIWFDGDWP---------- 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B        241 pcavdeqkrleflaYYFNRGEEWGKEVVTTYKHHDHGFrnTSAVDD--------------WERGGPSNLVRPYWQTDDAI 306
Cdd:pfam01120 205 --------------EYYNQYWNSTEFLAWLYNELSPVK--TVVVNDrwgkgprhggdyqtPERGLPGELLAHPWETCTTI 268
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
4NI3_B        307 SAsSWSYTVGI-KYYSSKAMVHSLLDRVSKNGNMLLNISPMANGVLPEEQIKVLNDIGDFLSRYGE 371
Cdd:pfam01120 269 GG-SWGYRRNDqDYKSAKELIHLLVDIVSKGGNLLLNIGPTADGTIPPEAEERLLEIGKWLKVNGE 333
AfuC COG3669
Alpha-L-fucosidase [Carbohydrate transport and metabolism];
22-484 1.91e-85

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


Pssm-ID: 442886 [Multi-domain]  Cd Length: 401  Bit Score: 271.41  E-value: 1.91e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B       22 EWYRDAKFGVYWHWGAFTTAQYAsEWYPRnmyepdsdqrkhhtetYGPPEEWGYENFIKgakdkkgnfvQFKPVlkskgg 101
Cdd:COG3669  29 LWFQDAKFGIFIHWGLYSVPGGA-EWYMR----------------YGKIPKFGYKDLAK----------LFNPE------ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B      102 EFDPEAIIKIVKGSGARFAGPVAEHHDGFSMWDSKVNEWNPVNYGP-KLDLVKLWADLVRENDMKLVIAMHQAYNYNGFF 180
Cdd:COG3669  76 KFDADQWARLAKDAGAKYVVLTAKHHDGFCLWDSKYTDYNVVDNSPwKRDVVKELAEACRKEGLKFGLYYSPWDWHHPDY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B      181 QWAPKTNDTslqkllgqlprDEEDQLWFDKHREMLDHVQP-DIIWNDFSLDSPGEcgsfegpcavDEQKRLEFLAYYFNr 259
Cdd:COG3669 156 PYGPKPPDW-----------PEYLEYWLNQLKELLTNYGPiDELWFDGAWPNGKR----------QEWDSPELYALIRN- 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B      260 geeWGKEVVTTYKHHDHGFRNtsaVDDWERGGPSNLVRPYWQTDDAISaSSWSYTVGIKYYSSKAMVHSLLDRVSKNGNM 339
Cdd:COG3669 214 ---LQPEAVINDRLGLPPGPD---YVTPERGIPTEIPPGPWETCTTIG-PSWGYHEDDKYKSPEELIDILVDSVSKGGNL 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B      340 LLNISPMANGVLPEEQIKVLNDIGDFLSRYGEAVYDTRawdiygegpnqveggsftAPLQGNSSDIRFTRNkeDDVLYVT 419
Cdd:COG3669 287 LLNIGPDADGTIPEEDVERLKEIGAWLKVNGEAIYGTR------------------PKVAGLDEDTRFTTK--GNALYAI 346
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
4NI3_B      420 VLGWPEDNLVsVKNLGSNALVdleslKSVELLGDKagdyvKVSEWEQSkDALDITLPSQPAESLA 484
Cdd:COG3669 347 VLGWPENGIV-LQELALGQRV-----KSVELLGTG-----KRIRFEQT-DKLRITIPEKAPSEFA 399
Fucosidase_C pfam16757
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
404-490 6.64e-10

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: 56.14  E-value: 6.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4NI3_B        404 DIRFTRNKEDDVLYVTVLGWPEDNLVsvkNLGSNALVDLESLKSVELLGdkagdYVKVSEWEQSKDALDITLPSQPAESL 483
Cdd:pfam16757   8 DVWYTSKPQEKAVYAIFLEWPKDGSL---VLGSPVKTSGSTATQVTLLG-----YGEPLKWKQTSNGLKIELPQLTPDQL 79
                          90
                  ....*....|.
4NI3_B        484 ----AYVLKLT 490
Cdd:pfam16757  80 pcqwAWTLKLT 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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