|
Name |
Accession |
Description |
Interval |
E-value |
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
45-308 |
1.07e-158 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 449.31 E-value: 1.07e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVP 123
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDqIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 124 LDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVtrcalDFRDGEEVA 203
Cdd:cd16029 81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGND-----DLRDNEEPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 204 TGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPY----DFIQDKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16029 156 WDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYedkfAHIKDEDRRTYAAMVSALDESVGN 235
|
250 260
....*....|....*....|....*....
gi 2217355829 280 VTAALKSSGLWNNTVFIFSTDNGEQKWFG 308
Cdd:cd16029 236 VVDALKAKGMLDNTLIVFTSDNGGPTGGG 264
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
45-302 |
2.00e-71 |
|
uncharacterized arylsulfatase; 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: 293765 [Multi-domain] Cd Length: 409 Bit Score: 227.05 E-value: 2.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIiwpCQPSCVP 123
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPiLKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTI---LGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 124 LDEKLLPQLLKEAGYTTHMVGKWHLGM---YRkeclPTRRGFDTYF---GYLLGSEDYYSHErctliDALNVTRcaldFR 197
Cdd:cd16146 78 LDETTLAEVFKDAGYRTGIFGKWHLGDnypYR----PQDRGFDEVLghgGGGIGQYPDYWGN-----DYFDDTY----YH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 198 DGEEVATgykNMYSTNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPY-DFIQDKNRHHYAGMVSLMDEA 276
Cdd:cd16146 145 NGKFVKT---EGYCTDVFFDEAIDFIEEN-KDKPFFAYLATNAPHGPLQVPDKYLDPYkDMGLDDKLAAFYGMIENIDDN 220
|
250 260
....*....|....*....|....*.
gi 2217355829 277 VGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16146 221 VGRLLAKLKELGLEENTIVIFMSDNG 246
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
35-310 |
2.40e-71 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 226.30 E-value: 2.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 35 PGSGAGASRPPHLVFLLADDLGWNDVGFHGS-RIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHq 112
Cdd:COG3119 14 AAAAAAAAKRPNILFILADDLGYGDLGCYGNpLIKTPNIDRLAAEGVRFTNAYvTSPVCSPSRASLLTGRYPHRTGVTD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 113 iIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLgmyrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrc 192
Cdd:COG3119 93 -NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 193 aldfrdgeevatgyknmYSTNIFTKRAIALITNH-PPEKPLFLYLALQSVHEPLQVPEEYLKPYD--------------- 256
Cdd:COG3119 128 -----------------YLTDLLTDKAIDFLERQaDKDKPFFLYLAFNAPHAPYQAPEEYLDKYDgkdiplppnlaprdl 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355829 257 --FIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGEqkWFGCH 310
Cdd:COG3119 191 teEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGP--SLGEH 244
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
44-302 |
5.07e-70 |
|
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: 223.21 E-value: 5.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLGWNDVGFHGS-RIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSC 121
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSpLIKTPNIDRLAAEGVRFTDFYaAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGMyRKECLPTRRGFDTYFGYLlgsedyYSHERCTLIDALNVTRCALDFRDGEE 201
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGH-QPEFLPTRHGFDEYFGIP------YSNDMWPFPLYRNDPPGPLPPLMENE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 202 VATGYKNMYS--TNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPydfiqdKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16026 154 EVIEQPADQSslTQRYTDEAVDFIERN-KDQPFFLYLAHTMPHVPLFASEKFKGR------SGAGLYGDVVEELDWSVGR 226
|
250 260
....*....|....*....|...
gi 2217355829 280 VTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16026 227 ILDALKELGLEENTLVIFTSDNG 249
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
45-312 |
2.80e-66 |
|
uncharacterized arylsulfatase 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: 293764 [Multi-domain] Cd Length: 415 Bit Score: 214.00 E-value: 2.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGS-RIRTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQ----IRTGLQHQIIWPCQ 118
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQkKIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLHTghtrVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 119 PscvplDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYL--LGSEDYYSHErctLIDalNVTRCALD- 195
Cdd:cd16145 81 P-----DDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLdqVHAHNYYPEY---LWR--NGEKVPLPn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 196 ----FRDGEEVATGYKNMYSTNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHH------ 265
Cdd:cd16145 151 nvipPLDEGNNAGGGGGTYSHDLFTDEALDFIREN-KDKPFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGIYAYlpwpqp 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217355829 266 ---YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGEQKWFGCHSD 312
Cdd:cd16145 230 ekaYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHD 279
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
45-303 |
2.44e-64 |
|
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: 203.44 E-value: 2.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGLQHqiiWPCQPSCV 122
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPdIKTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRHGVRG---NVGNGGGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 123 PLDEKLLPQLLKEAGYTTHMVGKWHlgmyrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrcaldfrdgeev 202
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 203 atgyknmystniftKRAIALITNHPPEKPLFLYLALQSVHEPLqvpeeylkpydfiqdknrhHYAGMVSLMDEAVGNVTA 282
Cdd:cd16022 103 --------------DEAIDFIERRDKDKPFFLYVSFNAPHPPF-------------------AYYAMVSAIDDQIGRILD 149
|
250 260
....*....|....*....|.
gi 2217355829 283 ALKSSGLWNNTVFIFSTDNGE 303
Cdd:cd16022 150 ALEELGLLDNTLIVFTSDHGD 170
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
45-302 |
3.10e-62 |
|
uncharacterized arylsulfatase 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: 293763 [Multi-domain] Cd Length: 421 Bit Score: 203.54 E-value: 3.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGL-QHQIIWPCQPSC 121
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKfYETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYPARLGItDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 122 -----------VPLDEKLLPQLLKEAGYTTHMVGKWHLGMyRKECLPTRRGFDTYFGY-LLGSEDYYSHERCTLIDALNv 189
Cdd:cd16144 81 tklipppsttrLPLEEVTIAEALKDAGYATAHFGKWHLGG-EGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 190 trcalDFRDGEevatgyknmYSTNIFTKRAIALITNHPpEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRH----- 264
Cdd:cd16144 159 -----DGPEGE---------YLTDRLTDEAIDFIEQNK-DKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRKgqknp 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 2217355829 265 HYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16144 224 VYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNG 261
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
45-304 |
7.08e-62 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 199.19 E-value: 7.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSRIR-TPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHQIIWPcqpscV 122
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPtTPFLDRLAEEGLLFSNFYsGGTLTAPSRFALLTGLPPHNFGSYVSTPVG-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 123 PLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKEClPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNvtrcaldfrdgeev 202
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS-PCNLGFDKFFGRNTGSDLYADPPDVPYNCSGG-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 203 atgyknMYSTNIFTKRAIALITNhpPEKPLFLYLALQSVHEPLQVPEEYLKPY----DFIQDKNRHH--YAGMVSLMDEA 276
Cdd:pfam00884 141 ------GVSDEALLDEALEFLDN--NDKPFFLVLHTLGSHGPPYYPDRYPEKYatfkPSSCSEEQLLnsYDNTLLYTDDA 212
|
250 260
....*....|....*....|....*...
gi 2217355829 277 VGNVTAALKSSGLWNNTVFIFSTDNGEQ 304
Cdd:pfam00884 213 IGRVLDKLEENGLLDNTLVVYTSDHGES 240
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-302 |
1.35e-59 |
|
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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 195.51 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPScvp 123
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGEsYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 124 ldeklLPQLLKEAGYTTHMVGKWHLGMYR-KECLPTRRGFDTYFGY-LLGSEDYYSHERctlidalNVTRCAldfRDGEE 201
Cdd:cd16151 78 -----FGHLLKDAGYATAIAGKWQLGGGRgDGDYPHEFGFDEYCLWqLTETGEKYSRPA-------TPTFNI---RNGKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 202 VATgYKNMYSTNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLQV--PEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16151 143 LET-TEGDYGPDLFADFLIDFIERN-KDQPFFAYYPMVLVHDPFVPtpDSPDWDPDDKRKKDDPEYFPDMVAYMDKLVGK 220
|
250 260
....*....|....*....|...
gi 2217355829 280 VTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16151 221 LVDKLEELGLRENTIIIFTGDNG 243
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
45-302 |
4.55e-59 |
|
uncharacterized arylsulfatase 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: 293762 [Multi-domain] Cd Length: 395 Bit Score: 194.73 E-value: 4.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHG--SRIRTPHLDALAAGGV-LLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSC 121
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpdSKIPTPNIDRLAAEGMrFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGM--YRKECL-------------------PTRRGFDTYFGyllgsedyysher 180
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKWHLGLdwKKKDGKkaatgtgkdvdyskpikggPLDHGFDYYFG------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 181 ctlIDALNVTRcaldfrdgeevatgyknmystnIFTKRAIALITNHP-PEKPLFLYLALQSVHEPLQVPEEYLK-----P 254
Cdd:cd16143 148 ---IPASEVLP----------------------TLTDKAVEFIDQHAkKDKPFFLYFALPAPHTPIVPSPEFQGksgagP 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2217355829 255 Y-DFIQDknrhhyagmvslMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16143 203 YgDFVYE------------LDWVVGRILDALKELGLAENTLVIFTSDNG 239
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
44-302 |
8.58e-59 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; 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: 293749 [Multi-domain] Cd Length: 402 Bit Score: 194.20 E-value: 8.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQH----QIIWPCQP 119
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTmaelATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 120 SCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMyrkeclptrrgfdtyfgyllgsEDYysherctlidalnvtrcaldfrdg 199
Cdd:cd16025 82 GYLPDSAATIAEVLKDAGYHTYMSGKWHLGP----------------------DDY------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 200 eevatgyknmYSTNIFTKRAIALI-TNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDK----------------- 261
Cdd:cd16025 116 ----------YSTDDLTDKAIEYIdEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKYDAgwdalreerlerqkelg 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217355829 262 ---------NRHH----------------------YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16025 186 lipadtkltPRPPgvpawdslspeekklearrmevYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNG 257
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
45-302 |
4.37e-55 |
|
uncharacterized arylsulfatase 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: 293761 [Multi-domain] Cd Length: 372 Bit Score: 183.89 E-value: 4.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSRI----RTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLqHQIIWPCQPS 120
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgrgaPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGL-TTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 121 CVPLDEKLLPQLLKEAGYTTHMVGKWHLGMyRKECLPTRRGFDTYFGYLLgsedyyshercTLIDAlnvtrcaldfrdge 200
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGD-EDGRLPTDHGFDEFYGNLY-----------HTIDE-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 201 evatgyknmystnIFTKRAIALIT-NHPPEKPLFLYLALQSVHEPLQVPEEYLKpydfiQDKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16142 134 -------------EIVDKAIDFIKrNAKADKPFFLYVNFTKMHFPTLPSPEFEG-----KSSGKGKYADSMVELDDHVGQ 195
|
250 260
....*....|....*....|...
gi 2217355829 280 VTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16142 196 ILDALDELGIADNTIVIFTTDNG 218
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
43-308 |
1.42e-51 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 176.18 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 43 RPPHLVFLLADDLGWNDVGFHGSRI-RTPHLDALAAGGVLLDN-YYTQPLCTPSRSQLLTGRYQIRTGlqhqiIWPCQPS 120
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIvKTPNIDRLAKEGVRFDNaFVTTSICAPSRASILTGQYSHRHG-----VTDNNGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 121 CVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKEClptRRGFDtYFGYLLGSEDYYsherctliDALNVTRCALDFRDGe 200
Cdd:cd16031 76 LFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLP---PPGFD-YWVSFPGQGSYY--------DPEFIENGKRVGQKG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 201 evatgyknmYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPY--------------------DFIQ- 259
Cdd:cd16031 143 ---------YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYedvtipepetfddddyagrpEWARe 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217355829 260 -------------------DKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG----EQKWFG 308
Cdd:cd16031 214 qrnrirgvldgrfdtpekyQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGfflgEHGLFD 285
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-310 |
8.07e-51 |
|
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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 173.52 E-value: 8.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHqiiwpcqpSCV 122
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDpVKTPNLDRLAKEGVVFTNAVsNYPVCSPYRASLLTGQYPLTNGVFG--------NDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 123 PL--DEKLLPQLLKEAGYTTHMVGKWHL-GMYRKECL-------PTRR-GFDTYFGYllGSEDYYSHerctlidalnvtr 191
Cdd:cd16034 74 PLppDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRaddytppPERRhGFDYWKGY--ECNHDHNN------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 192 cALDFRDGEEvaTGYKNMYSTNIFTKRAIALITNH-PPEKPLFLYLALQSVHEP-LQVPEEYLKPYDFIQDKNR------ 263
Cdd:cd16034 139 -PHYYDDDGK--RIYIKGYSPDAETDLAIEYLENQaDKDKPFALVLSWNPPHDPyTTAPEEYLDMYDPKKLLLRpnvped 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217355829 264 -----------HHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGEQkwFGCH 310
Cdd:cd16034 216 kkeeaglredlRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM--LGSH 271
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
45-302 |
9.34e-51 |
|
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: 172.31 E-value: 9.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQ--HQIIWPcqpsc 121
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFtTAPVCSPSRSALLTGLYPHQNGAHglRSRGFP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGmyrkeclptrrgfdtyFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDgee 201
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYN----------------PDAVFPFDDEMRGPDDGGRNAWDYASNAADFLN--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 202 vatgyknmystniftkraialitNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYD--------FIQD--KNRH---HYAG 268
Cdd:cd16027 137 -----------------------RAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDpekvkvppYLPDtpEVREdlaDYYD 193
|
250 260 270
....*....|....*....|....*....|....
gi 2217355829 269 MVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16027 194 EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG 227
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
44-302 |
1.21e-49 |
|
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: 293776 [Multi-domain] Cd Length: 466 Bit Score: 171.88 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLGWNDVGFHGSRIR-TPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGL----QH------ 111
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSReTPNLDRMAAEGMLFTDFYSaNPLCSPSRAALLTGRLPIRNGFyttnAHarnayt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 112 -QIIwpcqPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGmYRKECLPTRRGFDTYFGY---LLGSEDYYSHERCTLI-DA 186
Cdd:cd16157 81 pQNI----VGGIPDSEILLPELLKKAGYRNKIVGKWHLG-HRPQYHPLKHGFDEWFGApncHFGPYDNKAYPNIPVYrDW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 187 LNVTRCALDFRDgeEVATGYKNMysTNIFTKRAIALITN-HPPEKPLFLYLALQSVHEPLQVPEEylkpydFIQDKNRHH 265
Cdd:cd16157 156 EMIGRYYEEFKI--DKKTGESNL--TQIYLQEALEFIEKqHDAQKPFFLYWAPDATHAPVYASKP------FLGTSQRGL 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 2217355829 266 YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16157 226 YGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNG 262
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
44-302 |
3.77e-49 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 168.80 E-value: 3.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLGWNDVGFHG--SRIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGLQHQIIwPCQPS 120
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVGHNFL-PTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 121 CVPLDEKLLPQLLKEAGYTTHMVGKWHLGmYRKECLPTRRGFDTYFGYLlgsedyYSHerctliDALNVTRCAldfrdge 200
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLG-QREAYLPNSRGFDYYFGIP------FSH------DSSLADRYA------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 201 EVATGyknmystniFTKRAIAlitnhpPEKPLFLYLALQSVHEPLQVPEEYLKPydfiqDKNRHHYAGMVSLMDEAVGNV 280
Cdd:cd16161 140 QFATD---------FIQRASA------KDRPFFLYAALAHVHVPLANLPRFQSP-----TSGRGPYGDALQEMDDLVGQI 199
|
250 260
....*....|....*....|..
gi 2217355829 281 TAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16161 200 MDAVKHAGLKDNTLTWFTSDNG 221
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-302 |
2.04e-43 |
|
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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 153.10 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYYTQ-----PLCTPSRSQLLTGRYqirtglqhqiIW--- 115
Cdd:cd16155 3 PNILFILADDQRADTIGALGnPEIQTPNLDRLARRGTSFTNAYNMggwsgAVCVPSRAMLMTGRT----------LFhap 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 116 PCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHlgmyrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrcald 195
Cdd:cd16155 73 EGGKAAIPSDDKTWPETFKKAGYRTFATGKWH------------------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 196 frdgeevatgyknmystNIFTKRAIALITNHP-PEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQ--------------- 259
Cdd:cd16155 105 -----------------NGFADAAIEFLEEYKdGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETiplpenflpqhpfdn 167
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217355829 260 -----------------DKNRHHYA---GMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16155 168 gegtvrdeqlapfprtpEAVRQHLAeyyAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG 230
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
45-304 |
2.52e-42 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. 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: 293779 [Multi-domain] Cd Length: 445 Bit Score: 152.20 E-value: 2.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHG--SRIRTPhLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGL--QHQIIWPCQP 119
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGhpTQERGP-IDDMAAEGIRFTQAYsADSVCTPSRAALLTGRLPIRSGMygGTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 120 SCVPLDEKLLPQLLKEAGYTTHMVGKWHLGM--YRKE---CLPTRRGFDtYFGYLLgseDYYSHERCT----LIDALNVT 190
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGIneNNHSdgaHLPSHHGFD-FVGTNL---PFTNSWACDdtgrHVDFPDRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 191 RCALDFRDgEEVATGYKNMYSTNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLqvpeeYLKPyDFIQDKNRHHYAGMV 270
Cdd:cd16160 157 ACFLYYND-TIVEQPIQHEHLTETLVGDAKSFIEDN-QENPFFLYFSFPQTHTPL-----FASK-RFKGKSKRGRYGDNI 228
|
250 260 270
....*....|....*....|....*....|....
gi 2217355829 271 SLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGEQ 304
Cdd:cd16160 229 NEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPH 262
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
44-302 |
3.17e-42 |
|
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 152.60 E-value: 3.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSC 121
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGhPSSSTPNLDRLAANGLRFTDFYsSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGM-YRKECLPTRRGFDTYFGYLlgsedyYSHERCTLIDA-------------- 186
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVgLNGTYLPTHQGFDHYLGIP------YSHDQGPCQNLtcfppnipcfggcd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 187 LNVTRCALdFRDGEEVA-----TGYKNMYSTniFTKRAIAliTNHPPEKPLFLYLALQSVHEPlQVPEEylkpyDFIQDK 261
Cdd:cd16158 155 QGEVPCPL-FYNESIVQqpvdlLTLEERYAK--FAKDFIA--DNAKEGKPFFLYYASHHTHYP-QFAGQ-----KFAGRS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2217355829 262 NRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16158 224 SRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG 264
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
44-302 |
2.76e-40 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 147.82 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGV-LLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQ-----IIWP 116
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGnDTIRTPNIDRLAKEGVkLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrvILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 117 CQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECL-----PTRRGFDTYFGYLL----------GSEDYYSHER- 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNdfchhPLNHGFDYFYGLPLtnlkdcgdgsNGEYDLSFDPl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 181 ----------CTLIDALNVTRCALDFRDGEEVATGY----------------------KN-------MYSTNI---FTKR 218
Cdd:cd16159 161 fplltafvliTALTIFLLLYLGAVSKRFFVFLLILSllfislfflllitnryfncilmRNhevveqpMSLENLtqrLTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 219 AIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLkpydfiqDKNRH-HYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIF 297
Cdd:cd16159 241 AISFLERN-KERPFLLVMSFLHVHTALFTSKKFK-------GRSKHgRYGDNVEEMDWSVGQILDALDELGLKDNTFVYF 312
|
....*
gi 2217355829 298 STDNG 302
Cdd:cd16159 313 TSDNG 317
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-304 |
1.67e-36 |
|
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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 133.82 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGlqhqiIWpcqPSCV 122
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGhPVVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETG-----VW---DNAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 123 PLDEKL--LPQLLKEAGYTTHMVGKWHlgmYRKECLPTrrGFDtyfgyllgsedyysHERctlidalNVTRCALDFrdge 200
Cdd:cd16037 73 PYDGDVpsWGHALRAAGYETVLIGKLH---FRGEDQRH--GFR--------------YDR-------DVTEAAVDW---- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 201 evatgyknmystniftkraiaLITNHPPEKPLFLYLALQSVHEPLQVPEEYlkpYDFIQDKNRHHYAGMVSLMDEAVGNV 280
Cdd:cd16037 123 ---------------------LREEAADDKPWFLFVGFVAPHFPLIAPQEF---YDLYVRRARAAYYGLVEFLDENIGRV 178
|
250 260
....*....|....*....|....
gi 2217355829 281 TAALKSSGLWNNTVFIFSTDNGEQ 304
Cdd:cd16037 179 LDALEELGLLDNTLIIYTSDHGDM 202
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-302 |
1.76e-35 |
|
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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 132.09 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGW---NDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGlqhqIIWPcqPSC 121
Cdd:cd16154 1 PNILLIIADDQGLdssAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTG----VLAV--PDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 122 VPLDEKLLPQLLKE----AGYTTHMVGKWHLGmyrkECLPTRR---GFDTYFGYLLGS-EDYYSHERCTLIDALNVTRca 193
Cdd:cd16154 75 LLLSEETLLQLLIKdattAGYSSAVIGKWHLG----GNDNSPNnpgGIPYYAGILGGGvQDYYNWNLTNNGQTTNSTE-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 194 ldfrdgeevatgyknmYSTNIFTKRAIALITNHppEKPLFLYLALQSVHEPLQVPEEYLKPYDF------IQDKNRHHYA 267
Cdd:cd16154 149 ----------------YATTKLTNLAIDWIDQQ--TKPWFLWLAYNAPHTPFHLPPAELHSRSLlgdsadIEANPRPYYL 210
|
250 260 270
....*....|....*....|....*....|....*
gi 2217355829 268 GMVSLMDEAVGNVTAALKSSGLwNNTVFIFSTDNG 302
Cdd:cd16154 211 AAIEAMDTEIGRLLASIDEEER-ENTIIIFIGDNG 244
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-310 |
1.84e-35 |
|
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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 132.73 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSRI-RTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCV 122
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 123 -PLDEKLLPQLLKEAGYTTHMVGKWHLGmyrKECLPTRRGFDTYFGYllgsedyysherctlidalnvtrcaldfrdgEE 201
Cdd:cd16033 81 lPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFDEYLPV-------------------------------ET 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 202 VATGYknmystniFTKRAIALITNH-PPEKPLFLYLALQSVHEPLQVPEEYL--------------------KPYdfIQD 260
Cdd:cd16033 127 TIEYF--------LADRAIEMLEELaADDKPFFLRVNFWGPHDPYIPPEPYLdmydpediplpesfaddfedKPY--IYR 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217355829 261 KNR-----------------HHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGEqkWFGCH 310
Cdd:cd16033 197 RERkrwgvdtedeedwkeiiAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGD--ALGAH 261
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-310 |
2.52e-35 |
|
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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 131.58 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLGWNDVGFHGSRI-RTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGLQHQIIwpcqpsC 121
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLdLTPNLDALAEEGVLFENAFTpQPVCGPARACLQTGLYPTETGCFRNGI------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRkeclptrrgfdtyfgyllgsedyysherctlIDALnvtrcaldfrdgee 201
Cdd:cd16152 75 LPADEKTLAHYFRDAGYETGYVGKWHLAGYR-------------------------------VDAL-------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 202 vatgyknmystnifTKRAIALITNHPPEKPLFLYLAL-----QSVHEPLQVPEEYLKPY----------DFIQDKNRHH- 265
Cdd:cd16152 110 --------------TDFAIDYLDNRQKDKPFFLFLSYlephhQNDRDRYVAPEGSAERFanfwvppdlaALPGDWAEELp 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217355829 266 -YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNgeqkwfGCH 310
Cdd:cd16152 176 dYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH------GCH 215
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-313 |
1.26e-31 |
|
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: 119.57 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGS-RIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYqirtGLQHQIIWPcqpscv 122
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYdRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLY----PFYHGVWGG------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 123 PLDEK--LLPQLLKEAGYTTHMVGKWHLgmyrkecLPTRRGFDTYFgyllgseDYYsherctlidalnvtrcalDFRDGE 200
Cdd:cd16148 71 PLEPDdpTLAEILRKAGYYTAAVSSNPH-------LFGGPGFDRGF-------DTF------------------EDFRGQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 201 EVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPlqvpeeYLkpydfiqdknrhhYAGMVSLMDEAVGNV 280
Cdd:cd16148 119 EGDPGEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEP------YL-------------YDAEVRYVDEQIGRL 179
|
250 260 270
....*....|....*....|....*....|....*...
gi 2217355829 281 TAALKSSGLWNNTVFIFSTDNGEQ-----KWFGCHSDL 313
Cdd:cd16148 180 LDKLKELGLLEDTLVIVTSDHGEEfgehgLYWGHGSNL 217
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-302 |
2.52e-30 |
|
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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 115.41 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYqirtGLQHQII-----WPC 117
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGnSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRM----PSQHGIHdwiveGSH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 118 QPSCVPLD----EKLLPQLLKEAGYTTHMVGKWHLGMYrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrcA 193
Cdd:cd16149 77 GKTKKPEGylegQTTLPEVLQDAGYRCGLSGKWHLGDD-----------------------------------------A 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 194 LDFrdgeevatgyknmystniftkraiaLITNHPPEKPLFLYLALQSVHEPlqvpeeylkpydfiqdknrHHYAGMVSLM 273
Cdd:cd16149 116 ADF-------------------------LRRRAEAEKPFFLSVNYTAPHSP-------------------WGYFAAVTGV 151
|
250 260
....*....|....*....|....*....
gi 2217355829 274 DEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16149 152 DRNVGRLLDELEELGLTENTLVIFTSDNG 180
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
44-302 |
3.20e-30 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 118.42 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLGWNDVGFHGSRirtPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHQIIwPCqpSCV 122
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMP---KTKKLLADQGTTFTNAFvTTPLCCPSRASILTGQYAHNHGVTNNSP-PG--GGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 123 P------LDEKLLPQLLKEAGYTTHMVGKwHLGMYRKECLPTR--RGFDTYFGYLLGSEDYYSHerctlidalnvtrcaL 194
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGK-YLNGYGVPGGVSYvpPGWDEWDGLVGNSTYYNYT---------------L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 195 DFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPE-KPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNR---------- 263
Cdd:cd16147 139 SNGGNGKHGVSYPGDYLTDVIANKALDFLRRAAADdKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRpppnnpdvsd 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217355829 264 -HHY--------AGMV------------SLM--DEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16147 219 kPHWlrrlpplnPTQIayidelyrkrlrTLQsvDDLVERLVNTLEATGQLDNTYIIYTSDNG 280
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
44-302 |
4.11e-30 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 118.83 E-value: 4.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 44 PPHLVFLLADDLgwND-VGFHGSR-IRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGLQ--HQIIWPCQ 118
Cdd:cd16030 2 KPNVLFIAVDDL--RPwLGCYGGHpAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTGVYdnNSYFRKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 119 PscvplDEKLLPQLLKEAGYTTHMVGK-WHlgMYRKECLPTRRGFDTYFgYLLGSEDYYSHERCTLIDALNVTRCALDFr 197
Cdd:cd16030 80 P-----DAVTLPQYFKENGYTTAGVGKiFH--PGIPDGDDDPASWDEPP-NPPGPEKYPPGKLCPGKKGGKGGGGGPAW- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 198 dgeEVATGYKNMYSTNIFTKRAIALITN-HPPEKPLFLylalqSV-----HEPLQVPEEYLKPYDF-------------- 257
Cdd:cd16030 151 ---EAADVPDEAYPDGKVADEAIEQLRKlKDSDKPFFL-----AVgfykpHLPFVAPKKYFDLYPLesiplpnpfdpidl 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217355829 258 --------------------------------IQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd16030 223 pevawndlddlpkygdipalnpgdpkgplpdeQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG 299
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-319 |
1.36e-29 |
|
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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 116.95 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVG-FHGSRIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTG--LQHQIIWPCQPS 120
Cdd:cd16150 1 PNIVIFVADQLRADSLGhLGNPAAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGWYPHVNGhrTLHHLLRPDEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 121 cvpldeklLPQLLKEAGYTTHMVGKWHlgmyrkeCLPTRRGFDTYfgyllgsedyysherCTLIDAlnvtrcaldfrdge 200
Cdd:cd16150 81 --------LLKTLKDAGYHVAWAGKND-------DLPGEFAAEAY---------------CDSDEA-------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 201 evatgyknmystniFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYD-------------------FIQDK 261
Cdd:cd16150 117 --------------CVRTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDreklpprrppglrakgkpsMLEGI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 262 NRHH---------------YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGE--------QKWFGCHSDLRVKFP 318
Cdd:cd16150 183 EKQGldrwseerwrelratYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDytgdyglvEKWPNTFEDCLTRVP 262
|
.
gi 2217355829 319 F 319
Cdd:cd16150 263 L 263
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
45-330 |
3.77e-26 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 106.12 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSRI-RTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGlqhqiIW--PCQ-P 119
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVvKTPNLDRLAARGVVFDNAYCNsPLCAPSRASMMTGRLPSRIG-----AYdnAAEfP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 120 SCVPldekLLPQLLKEAGYTTHMVGKWHLgmyrkeCLPtrrgfDTYFGYllgseDYysherctliDalnvtrcaldfrdg 199
Cdd:cd16032 76 ADIP----TFAHYLRAAGYRTALSGKMHF------VGP-----DQLHGF-----DY---------D-------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 200 EEVAtgYKnmystnifTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYlkpYDFIQDKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16032 113 EEVA--FK--------AVQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQEY---WDLYVRRARRAYYGMVSYVDDKVGQ 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217355829 280 VTAALKSSGLWNNTVFIFSTDNGE----------QKWF--GCHSDLRVKFPFSEQASAVLRPV 330
Cdd:cd16032 180 LLDTLERTGLADDTIVIFTSDHGDmlgerglwykMSFFegSARVPLIISAPGRFAPRRVAEPV 242
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
49-304 |
5.63e-26 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 107.34 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 49 FLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRtglqHQIIWpcqpSCVPLD- 125
Cdd:cd16028 5 FITADQWRADCLSCLGhPLVKTPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRYLMN----HRSVW----NGTPLDa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 126 -EKLLPQLLKEAGYTTHMVGKWHL-----GMYRKeclptrrgfDTYFGYLLGSEDYYSHerctlidalnvtRCALDFRDG 199
Cdd:cd16028 77 rHLTLALELRKAGYDPALFGYTDTspdprGLAPL---------DPRLLSYELAMPGFDP------------VDRLDEYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 200 EEVATGYknmystniFTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPYD-----------FIQDKNRHH--- 265
Cdd:cd16028 136 EDSDTAF--------LTDRAIEYLDER-QDEPWFLHLSYIRPHPPFVAPAPYHALYDpadvpppiraeSLAAEAAQHpll 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217355829 266 ---------------------------------YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGEQ 304
Cdd:cd16028 207 aaflerieslsfspgaanaadlddeevaqmratYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ 278
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
45-319 |
6.87e-26 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 107.45 E-value: 6.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTG-LQHQiiwpcqpSC 121
Cdd:PRK13759 7 PNIILIMVDQMRGDCLGCNGNKaVETPNLDMLASEGYNFENAYSAvPSCTPARAALLTGLSQWHHGrVGYG-------DV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 122 VPLDEK-LLPQLLKEAGYTTHMVGKWHLGMYRKEClptrrGFDTYF---GYlLGSEDYYSHERCTLID-----------A 186
Cdd:PRK13759 80 VPWNYKnTLPQEFRDAGYYTQCIGKMHVFPQRNLL-----GFHNVLlhdGY-LHSGRNEDKSQFDFVSdylawlrekapG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 187 LNVTRCALDFRDGEEVATGYK---NMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLK---------- 253
Cdd:PRK13759 154 KDPDLTDIGWDCNSWVARPWDleeRLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDmykdadipdp 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 254 -----PYDFIQDKN-------------------RHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGEQkwFGC 309
Cdd:PRK13759 234 higdwEYAEDQDPEggsidalrgnlgeeyarraRAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM--LGD 311
|
330
....*....|
gi 2217355829 310 HSDLRVKFPF 319
Cdd:PRK13759 312 HYLFRKGYPY 321
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
45-311 |
1.53e-25 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; 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: 293775 [Multi-domain] Cd Length: 468 Bit Score: 106.31 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVG-FHGSRIRTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYqirtglqhqiiwPCQ---- 118
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcYGNKAMKTPNLDRLAAEGVRFDSAYTtQPVCGPARSGLFTGLY------------PHTngsw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 119 PSCVPLDE--KLLPQLLKEAGYTTHMVGKWHLGmyrkeclptrrGFDtYFGYllG------SEDYYSHERCTLiDALN-- 188
Cdd:cd16156 69 TNCMALGDnvKTIGQRLSDNGIHTAYIGKWHLD-----------GGD-YFGN--GicpqgwDPDYWYDMRNYL-DELTee 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 189 ---VTRCALDFRDGEEVATGYknMYSTNIfTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPY-DFIQDKNR- 263
Cdd:cd16156 134 errKSRRGLTSLEAEGIKEEF--TYGHRC-TNRALDFIEKH-KDEDFFLVVSYDEPHHPFLCPKPYASMYkDFEFPKGEn 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217355829 264 ----------HH---------------------YAGMVSLMDEAVGNVTAALKSSGlwNNTVFIFSTDNGEQkwFGCHS 311
Cdd:cd16156 210 ayddlenkplHQrlwagakphedgdkgtikhplYFGCNSFVDYEIGRVLDAADEIA--EDAWVIYTSDHGDM--LGAHK 284
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-302 |
3.05e-24 |
|
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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 99.76 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGS-----------RIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGL-QH 111
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNahtgksesrlgYVESPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGVyGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 112 QIIWPcQPSCVPLdekLLPQLLKEAGYTTHMVGKWHLGMYRKeclptrrgfdtyfgYLlgsedyysherctliDALNVTr 191
Cdd:cd16153 82 EAAHP-ALDHGLP---TFPEVLKKAGYQTASFGKSHLEAFQR--------------YL---------------KNANQS- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 192 caldfrdgeevatgYKNMYSTNIFTKRaialitnhpPEKPLFLYLALQSVHEPLQVPEEYlkpydfiqdKNRHHYAGMVS 271
Cdd:cd16153 128 --------------YKSFWGKIAKGAD---------SDKPFFVRLSFLQPHTPVLPPKEF---------RDRFDYYAFCA 175
|
250 260 270
....*....|....*....|....*....|....
gi 2217355829 272 LMDEAVGNVTAALKSSGLWN---NTVFIFSTDNG 302
Cdd:cd16153 176 YGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHG 209
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
69-300 |
1.81e-15 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 75.41 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 69 TPHLDALAAGGVLLDNYYTQPLCTP-SRSQ--LLTGRYQI--RTGLQHQIIWPCQPScvpldeklLPQLLKEAGYTTHMV 143
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGtANGEfeVLTGLPPLplGSGSYTLYKLNPLPS--------LPSILKEQGYETIFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 144 GKWHLGMYRkeclptRRGFDTYFGYllgsEDYYSHErctlidalnvtrcalDFRDGEEVATGYknMYSTNIFTKRAIALI 223
Cdd:cd16015 98 HGGDASFYN------RDSVYPNLGF----DEFYDLE---------------DFPDDEKETNGW--GVSDESLFDQALEEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 224 TNHPpEKPLFLYLA-LQSvHEPLQVPEEYLKPYDFIQDKNRH--HYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTD 300
Cdd:cd16015 151 EELK-KKPFFIFLVtMSN-HGPYDLPEEKKDEPLKVEEDKTEleNYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGD 228
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
70-307 |
3.42e-15 |
|
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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 74.94 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 70 PHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPscvPLDEKL--LPQLLKEAGYTTHMVGKW 146
Cdd:cd16035 27 PARERLAANGLSFENHYTaACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQP---LLSPDVptLGHMLRAAGYYTAYKGKW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 147 HLGmyrkeclptrrgfdtyfGYLLGSEDYysherctlidalnvtrcaldfrDGeevatgyknmystnIFTKRAIALITNH 226
Cdd:cd16035 104 HLS-----------------GAAGGGYKR----------------------DP--------------GIAAQAVEWLRER 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 227 PPE----KPLFLYLAL---QSVHEPLQVPEEYLKPYDFiqdknrhhYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFST 299
Cdd:cd16035 131 GAKnadgKPWFLVVSLvnpHDIMFPPDDEERWRRFRNF--------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTS 202
|
250
....*....|....*.
gi 2217355829 300 DNGE--------QKWF 307
Cdd:cd16035 203 DHGEmggahglrGKGF 218
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
37-297 |
2.03e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 73.92 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 37 SGAGASRPPHLVFLLADDLGWNDVGFHGSRIR-TPHLDALAAGGVLLDNYYTQplcTP--SRSQ--LLTGRYQ------I 105
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDvTPFLDSLAKESLYFGNFYSQ---GGrtSRGEfaVLTGLPPlpggspY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 106 RTGLQHQiiwpcQPScvpldeklLPQLLKEAGYTTHMvgkWH---LGMYRkeclptRRGFDTYFGYllgsEDYYSHErct 182
Cdd:COG1368 304 KRPGQNN-----FPS--------LPSILKKQGYETSF---FHggdGSFWN------RDSFYKNLGF----DEFYDRE--- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 183 lidalnvtrcalDFRDGEEVATGYKNMYstniFTKRAIALITNHPpeKPLFLYLALQSVHEPLQVPEEYLKPYDFiQDKN 262
Cdd:COG1368 355 ------------DFDDPFDGGWGVSDED----LFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEEDKKIPDY-GKTT 415
|
250 260 270
....*....|....*....|....*....|....*
gi 2217355829 263 RHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIF 297
Cdd:COG1368 416 LNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVI 450
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
45-302 |
2.58e-10 |
|
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: 59.74 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVG-FHGSRIRTPHLDALAAGGVLLD--NYYTQPLCTPSRSQLLTGRYQIRTGL-QHQIIWPCQPS 120
Cdd:cd00016 1 KHVVLIVLDGLGADDLGkAGNPAPTTPNLKRLASEGATFNfrSVSPPTSSAPNHAALLTGAYPTLHGYtGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 121 CV---PLDEKLLPQLLKEAGYTTHMVGkwhlgmyrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrcALDFr 197
Cdd:cd00016 81 RAagkDEDGPTIPELLKQAGYRTGVIG------------------------------------------------LLKA- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 198 dgeevatgyknmystniftkraialITNHPPEKPLFLYLALQSVHEPLqvpeeylkpydfiQDKNRHH--YAGMVSLMDE 275
Cdd:cd00016 112 -------------------------IDETSKEKPFVLFLHFDGPDGPG-------------HAYGPNTpeYYDAVEEIDE 153
|
250 260
....*....|....*....|....*..
gi 2217355829 276 AVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:cd00016 154 RIGKVLDALKKAGDADDTVIIVTADHG 180
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
39-302 |
7.38e-08 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 53.21 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 39 AGASRPPHLVFLLADDLGWNDVGFHgsriRTPHLDALAAGGVLLDNYYTQ-PLCT-PSRSQLLTGRYQIRTG-------- 108
Cdd:COG1524 18 AAAPPAKKVVLILVDGLRADLLERA----HAPNLAALAARGVYARPLTSVfPSTTaPAHTTLLTGLYPGEHGivgngwyd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 109 --LQHQIIWPCQPSCVPLDEKLLP-----QLLKEAGYTTHMVGKWHLGMYrkeclptrrgfdtyfgyllgsedyysherc 181
Cdd:COG1524 94 peLGRVVNSLSWVEDGFGSNSLLPvptifERARAAGLTTAAVFWPSFEGS------------------------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 182 TLIDAlnvtrcALDFR-DGEEVATGYknmYSTNIFT-KRAIALITNHPPEkplFLYLALQSVheplqvpeeylkpydfiq 259
Cdd:COG1524 144 GLIDA------ARPYPyDGRKPLLGN---PAADRWIaAAALELLREGRPD---LLLVYLPDL------------------ 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217355829 260 DKNRHHY-------AGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:COG1524 194 DYAGHRYgpdspeyRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
45-303 |
9.00e-08 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. 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: 293781 [Multi-domain] Cd Length: 366 Bit Score: 52.93 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYqirTGLQHQiiWPcQPSCV 122
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQvVDLPYINFMKQHGSVFLNAYTNsPICCPSRAAMWSGLF---THLTES--WN-NYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 123 PLDEKLLPQLLKEAGYTTHMVGKwhlgmyrkeclptrrgfdtyfgyllgsEDYYS--HERCTLIDALNVTRCALDFRDGE 200
Cdd:cd16171 75 DPNYPTWMDRLEKHGYHTQKYGK---------------------------LDYTSghHSVSNRVEAWTRDVPFLLRQEGR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355829 201 EVATGYKNMYSTNIF------TKRAIALITNHPP--EKPLFLYLALQSVHEplqVPEEYLKPyDFIQDKN-RHHYAGMVS 271
Cdd:cd16171 128 PTVNLVGDRSTVRVMlkdwqnTDKAVHWIRKEAPnlTQPFALYLGLNLPHP---YPSPSMGE-NFGSIRNiRAFYYAMCA 203
|
250 260 270
....*....|....*....|....*....|..
gi 2217355829 272 LMDEAVGNVTAALKSSGLWNNTVFIFSTDNGE 303
Cdd:cd16171 204 ETDAMLGEIISALKDTGLLDKTYVFFTSDHGE 235
|
|
| |
