|
Name |
Accession |
Description |
Interval |
E-value |
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
77-573 |
0e+00 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 617.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 77 TPMPSSACPMIKLMKPQSID-GMNYLYLIASAkELWKKLGvRRLSDIFCAYKRFVRFNDFVNIYFESTLFRFSKLRNFTK 155
Cdd:pfam02995 1 KPNPLRKCSKDQLLTTKSFNiTFGTYRLNIDE-LAKPRLN-ERLENLNCEYREIKRKRDSENRDGYSKLFPLRKLTQSVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 156 VDSGNITLRVWCWMDYGRLVYHDVFIFLPFPNPQKV--NNSAP--VKRLSVLILGIDSISHMHYQRYFSRVRDLIEGLPH 231
Cdd:pfam02995 79 VPVGCEILITECWEDFGKIYQKDVFNFLHDRIPPKKpkLSSTPaeVRKPSVLILGIDSLSRMNFRRSMPRTYKFLKELGW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 232 TELWGYNRVGQNSYPNLIPLLSGQsVDEVEAKSGCYgASGGTNFDRCHLLWHDFQAAGYATIFGEDSRVAGTFTYVRPGF 311
Cdd:pfam02995 159 FELQGYNKVGDNTFPNLLPLLTGK-FSEPELEADCD-PSCNGSLDKCPFIWKDFKDAGYATAFAEDWAKIGTFNYNKPGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 312 KKRPTDFYLRSVINEIHMRSTYFARGPLEIkCSGDRVYHHVLYDFIYRLLPHMQARMydrgFFAFFWQTMGVHDYFQYGE 391
Cdd:pfam02995 237 RKQPTDHYLRPLILAIEKHLTYSTRFGLNY-CLGRRPTHNYLLDYLRQFLPRYRDSP----FFGFFWSNSLSHDDFNYAS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 392 RADWEYYRIMRALKRRKILERTLVLIVSDHGLRYGPFVDTFQGMRETSLPIMVAIYPRSLRERFPLAFANLEANAHRLVT 471
Cdd:pfam02995 312 ALDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLRRTSQGMLEERLPLMSIRYPPWFRETYPQAVENLELNANRLTT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 472 TYDLHETLKDVVDLENLSDERILNRTLRLRNNHNVSLFLPIPEERSCFSARIPLHYCQCDGYVKIPWNVRSIQRIAKLAV 551
Cdd:pfam02995 392 PFDLHATLKDILHLGELSDKELQDRMKALDCPRGISLFLPIPDNRTCSDAGIPEHWCTCEPYKEVPTNDTLVQRIARSVV 471
|
490 500
....*....|....*....|....*
gi 24646132 552 ANINRLLAP---YPQCEQLELLNVE 573
Cdd:pfam02995 472 ERINEYLKThnlSPLCAPLELQKVL 496
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
200-485 |
6.67e-109 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 329.48 E-value: 6.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 200 LSVLILGIDSISHMHYQRYFSRVRD-LIEGLPHTELWGYNRVGQNSYPNLIPLLSGQSVDEVEAKsgCYGASGGTNFDRC 278
Cdd:cd16021 1 PNVLILGIDSVSRLNFKRSLPKTLKfLKSELGAVEFKGYNKVGDNTFPNLLPLLTGKSEEELPEA--RRKESCKGYLDNC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 279 HLLWHDFQAAGYATIFGEDSRVAGTFTYVRPGFKKRPTDFYLRSVINEIHMRSTYFARGPLEIKCSGDRVYHHVLYDFIY 358
Cdd:cd16021 79 PFIWKDFKKAGYVTAFAEDWPKIGTFNYRKKGFKKPPTDHYLRPFWLAAEKTTSYSTKSYCTGCRPSHKALLDYLEDFIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 359 RLLphmqarmyDRGFFAFFWQTMGVHDYFQYGERADWEYYRIMRALKRRKILERTLVLIVSDHGLRYGPFVDTFQGMRET 438
Cdd:cd16021 159 AYK--------DRPKFSFFWLSELTHDYLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIRETLQGKLEE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24646132 439 SLPIMVAIYPRSLRERFPLAFANLEANAHRLVTTYDLHETLKDVVDL 485
Cdd:cd16021 231 RLPFLSISLPKWFREKYPEAVANLKKNSNRLTTPFDLHATLLDILNL 277
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
382-422 |
9.09e-04 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 42.17 E-value: 9.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 24646132 382 GVHDYFQYGERADWEYYRIMRALKRRKILERTLVLIVSDHG 422
Cdd:COG3119 198 ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
77-573 |
0e+00 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 617.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 77 TPMPSSACPMIKLMKPQSID-GMNYLYLIASAkELWKKLGvRRLSDIFCAYKRFVRFNDFVNIYFESTLFRFSKLRNFTK 155
Cdd:pfam02995 1 KPNPLRKCSKDQLLTTKSFNiTFGTYRLNIDE-LAKPRLN-ERLENLNCEYREIKRKRDSENRDGYSKLFPLRKLTQSVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 156 VDSGNITLRVWCWMDYGRLVYHDVFIFLPFPNPQKV--NNSAP--VKRLSVLILGIDSISHMHYQRYFSRVRDLIEGLPH 231
Cdd:pfam02995 79 VPVGCEILITECWEDFGKIYQKDVFNFLHDRIPPKKpkLSSTPaeVRKPSVLILGIDSLSRMNFRRSMPRTYKFLKELGW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 232 TELWGYNRVGQNSYPNLIPLLSGQsVDEVEAKSGCYgASGGTNFDRCHLLWHDFQAAGYATIFGEDSRVAGTFTYVRPGF 311
Cdd:pfam02995 159 FELQGYNKVGDNTFPNLLPLLTGK-FSEPELEADCD-PSCNGSLDKCPFIWKDFKDAGYATAFAEDWAKIGTFNYNKPGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 312 KKRPTDFYLRSVINEIHMRSTYFARGPLEIkCSGDRVYHHVLYDFIYRLLPHMQARMydrgFFAFFWQTMGVHDYFQYGE 391
Cdd:pfam02995 237 RKQPTDHYLRPLILAIEKHLTYSTRFGLNY-CLGRRPTHNYLLDYLRQFLPRYRDSP----FFGFFWSNSLSHDDFNYAS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 392 RADWEYYRIMRALKRRKILERTLVLIVSDHGLRYGPFVDTFQGMRETSLPIMVAIYPRSLRERFPLAFANLEANAHRLVT 471
Cdd:pfam02995 312 ALDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLRRTSQGMLEERLPLMSIRYPPWFRETYPQAVENLELNANRLTT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 472 TYDLHETLKDVVDLENLSDERILNRTLRLRNNHNVSLFLPIPEERSCFSARIPLHYCQCDGYVKIPWNVRSIQRIAKLAV 551
Cdd:pfam02995 392 PFDLHATLKDILHLGELSDKELQDRMKALDCPRGISLFLPIPDNRTCSDAGIPEHWCTCEPYKEVPTNDTLVQRIARSVV 471
|
490 500
....*....|....*....|....*
gi 24646132 552 ANINRLLAP---YPQCEQLELLNVE 573
Cdd:pfam02995 472 ERINEYLKThnlSPLCAPLELQKVL 496
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
200-485 |
6.67e-109 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 329.48 E-value: 6.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 200 LSVLILGIDSISHMHYQRYFSRVRD-LIEGLPHTELWGYNRVGQNSYPNLIPLLSGQSVDEVEAKsgCYGASGGTNFDRC 278
Cdd:cd16021 1 PNVLILGIDSVSRLNFKRSLPKTLKfLKSELGAVEFKGYNKVGDNTFPNLLPLLTGKSEEELPEA--RRKESCKGYLDNC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 279 HLLWHDFQAAGYATIFGEDSRVAGTFTYVRPGFKKRPTDFYLRSVINEIHMRSTYFARGPLEIKCSGDRVYHHVLYDFIY 358
Cdd:cd16021 79 PFIWKDFKKAGYVTAFAEDWPKIGTFNYRKKGFKKPPTDHYLRPFWLAAEKTTSYSTKSYCTGCRPSHKALLDYLEDFIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 359 RLLphmqarmyDRGFFAFFWQTMGVHDYFQYGERADWEYYRIMRALKRRKILERTLVLIVSDHGLRYGPFVDTFQGMRET 438
Cdd:cd16021 159 AYK--------DRPKFSFFWLSELTHDYLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIRETLQGKLEE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24646132 439 SLPIMVAIYPRSLRERFPLAFANLEANAHRLVTTYDLHETLKDVVDL 485
Cdd:cd16021 231 RLPFLSISLPKWFREKYPEAVANLKKNSNRLTTPFDLHATLLDILNL 277
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
201-481 |
3.67e-07 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 51.65 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 201 SVLILGIDSISHMHYQRYFSRVRD------LIEGLPHTELWGYNRVGqNSYPNLIPLLSGqsVDEVEAKSGCYGASGGTN 274
Cdd:cd00016 2 HVVLIVLDGLGADDLGKAGNPAPTtpnlkrLASEGATFNFRSVSPPT-SSAPNHAALLTG--AYPTLHGYTGNGSADPEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 275 F-------DRCHLLWHDFQAAGYATIFgedsrvagtftyvrpgfkkrptdFYLRSVINEIHMRSTYFArgpleikcsgdr 347
Cdd:cd00016 79 PsraagkdEDGPTIPELLKQAGYRTGV-----------------------IGLLKAIDETSKEKPFVL------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 348 vyhhvlydFIYRLLPHMQarmydrgFFAFFWQTMGvhdYFQYGERADWEYYRIMRALKRRKILERTLVLIVSDHG----- 422
Cdd:cd00016 124 --------FLHFDGPDGP-------GHAYGPNTPE---YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGgidkg 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24646132 423 LRYGPFVDT--FQGMRETSLPiMVAIYPRSLRERfplafanleaNAHRLVTTYDLHETLKD 481
Cdd:cd00016 186 HGGDPKADGkaDKSHTGMRVP-FIAYGPGVKKGG----------VKHELISQYDIAPTLAD 235
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
285-422 |
1.10e-05 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 47.54 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 285 FQAAGYAT-IFGedsrvAGTFTYVRPGFKKRptdfylrsvINEIHMRSTYFARGPLEIKCSGDRVYHHVLyDFIyrllph 363
Cdd:cd16148 83 LRKAGYYTaAVS-----SNPHLFGGPGFDRG---------FDTFEDFRGQEGDPGEEGDERAERVTDRAL-EWL------ 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24646132 364 mQARMYDRGFFAFFwQTMGVHDYFQY-GE--RADWEYYRIMRALKRRKILERTLVLIVSDHG 422
Cdd:cd16148 142 -DRNADDDPFFLFL-HYFDPHEPYLYdAEvrYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
285-441 |
7.87e-05 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 45.11 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 285 FQAAGYATIFgedsrVAGTFTYVRPgfKKRPTDFYLRSVINEIHMRSTYFARGPLEIKCSGDRVYHHVLYDFIYRLLPHM 364
Cdd:pfam00884 86 LKRAGYNTGA-----IGKWHLGWYN--NQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLDNN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 365 qarmyDRGFFaFFWQTMGVHDYFQYGER----------------------------ADWEYYRIMRALKRRKILERTLVL 416
Cdd:pfam00884 159 -----DKPFF-LVLHTLGSHGPPYYPDRypekyatfkpsscseeqllnsydntllyTDDAIGRVLDKLEENGLLDNTLVV 232
|
170 180
....*....|....*....|....*
gi 24646132 417 IVSDHGLRYGPFVDTFQGMRETSLP 441
Cdd:pfam00884 233 YTSDHGESLGEGGGYLHGGKYDNAP 257
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
355-422 |
6.86e-04 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 41.65 E-value: 6.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24646132 355 DFIYRLLPhmqarmyDRGFFAFFWQTmGVHDYFQYG---ERADWEYYRIMRALKRRKILERTLVLIVSDHG 422
Cdd:cd16022 107 DFIERRDK-------DKPFFLYVSFN-APHPPFAYYamvSAIDDQIGRILDALEELGLLDNTLIVFTSDHG 169
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
382-422 |
9.09e-04 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 42.17 E-value: 9.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 24646132 382 GVHDYFQYGERADWEYYRIMRALKRRKILERTLVLIVSDHG 422
Cdd:COG3119 198 ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
399-422 |
3.63e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 40.12 E-value: 3.63e-03
10 20
....*....|....*....|....
gi 24646132 399 RIMRALKRRKILERTLVLIVSDHG 422
Cdd:COG1524 220 RLLDALKARGLYEGTLVIVTADHG 243
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
392-428 |
5.19e-03 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 39.41 E-value: 5.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 24646132 392 RADW-EYY-----------RIMRALKRRKILERTLVLIVSDHGlryGPF 428
Cdd:cd16027 185 REDLaDYYdeierldqqvgEILDELEEDGLLDNTIVIFTSDHG---MPF 230
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
355-422 |
9.80e-03 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 38.70 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646132 355 DFIYRllphmQArmyDRGFFAFFWQTMgVH------DYFQ-------YG---ERADWEYYRIMRALKRRKILERTLVLIV 418
Cdd:cd16026 175 DFIER-----NK---DQPFFLYLAHTM-PHvplfasEKFKgrsgaglYGdvvEELDWSVGRILDALKELGLEENTLVIFT 245
|
....
gi 24646132 419 SDHG 422
Cdd:cd16026 246 SDNG 249
|
|
| |
