|
Name |
Accession |
Description |
Interval |
E-value |
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
37-503 |
0e+00 |
|
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: 542.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSP 116
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGN---PIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 117 EHNNI-AKELQKGGYQTSVIGKWHLK----QEPAGFDYYCVLPGQGEYWNPRLKTKenwedyyGGGKTYEGFSTDIIADK 191
Cdd:cd16031 79 ASQPTyPKLLRKAGYQTAFIGKWHLGsggdLPPPGFDYWVSFPGQGSYYDPEFIEN-------GKRVGQKGYVTDIITDK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 192 TIEWIENRDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDkgpettgrsfvgqsvDNLKKRylaatadPS 271
Cdd:cd16031 152 ALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDD---------------DDYAGR-------PE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 272 LRKDFMNYPElpfsvDGLTDDEARYKTYQKYVKDFMRCGAAADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHGWF 351
Cdd:cd16031 210 WAREQRNRIR-----GVLDGRFDTPEKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 352 DKRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKGNTPDDWRKYGYYRYWD 431
Cdd:cd16031 285 DKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKPVDWRKEFYYEYYE 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110313252 432 H--SKDRPGHFGIRGERYKLAFFYGNGlksnnytpenqptQFWDFYDLKEDPNELHNAYKDPKYQDIIAGMKAE 503
Cdd:cd16031 365 EpnFHNVPTHEGVRTERYKYIYYYGVW-------------DEEELYDLKKDPLELNNLANDPEYAEVLKELRKR 425
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
37-514 |
2.01e-126 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 374.99 E-value: 2.01e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAG--- 113
Cdd:COG3119 23 RPNILFILADDLGYGDLGCYGN---PLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGyng 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 114 -LSPEHNNIAKELQKGGYQTSVIGKWHLkqepagfdyycvlpgqgeywnprlktkenwedyygggktyegFSTDIIADKT 192
Cdd:COG3119 100 gLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------------------YLTDLLTDKA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 193 IEWIE-NRDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDkgpettgrsfvgqsvdnlkkrylaatadps 271
Cdd:COG3119 138 IDFLErQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPNLAP------------------------------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 272 lrkdfmnypelpfsvdgltdDEARYKTYQKYVKDFMRCGAAADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHGW- 350
Cdd:COG3119 188 --------------------RDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLr 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 351 FDKRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKGNTPdDWRKYGYYRYW 430
Cdd:COG3119 248 GGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKA-EWRDYLYWEYP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 431 DHskdrPGHFGIRGERYKLAFFYgnglksnnytpenQPTQFWDFYDLKEDPNELHNAYKDpkYQDIIAGMKAEILAQREA 510
Cdd:COG3119 327 RG----GGNRAIRTGRWKLIRYY-------------DDDGPWELYDLKNDPGETNNLAAD--YPEVVAELRALLEAWLKE 387
|
....
gi 1110313252 511 LGDT 514
Cdd:COG3119 388 LGDP 391
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
38-509 |
3.95e-92 |
|
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: 286.33 E-value: 3.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHtSQAWGIYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVT---TLGAGL 114
Cdd:cd16027 1 PNILWIIADDL-SPDLGGYGG---NVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHglrSRGFPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 115 SPEHNNIAKELQKGGYQTSVIGKWHLKQEPAGFDyycvlpgqgeywnprlktkenweDYYGGGKTYEGFSTDIIADKTIE 194
Cdd:cd16027 77 PDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPF-----------------------DDEMRGPDDGGRNAWDYASNAAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 195 WIENRDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDkgpettgrsfvgqsvdnlkkrylaataDPSLRK 274
Cdd:cd16027 134 FLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYLPD---------------------------TPEVRE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 275 DFMNYpelpfsvdgltDDEARYktyqkyvkdfmrcgaaADDNIGKLLDYLDAAGLAENTIVIYTADqgyflgeHGW---F 351
Cdd:cd16027 187 DLADY-----------YDEIER----------------LDQQVGEILDELEEDGLLDNTIVIFTSD-------HGMpfpR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 352 DKRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKGNTpDDWRKYGY-YRYW 430
Cdd:cd16027 233 AKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEK-DPGRDYVFaERDR 311
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1110313252 431 DHSKDRPGHfGIRGERYKLAFfygnglksnNYTPEnqptqfwDFYDLKEDPNELHNAYKDPKYQDIIAGMKAEILAQRE 509
Cdd:cd16027 312 HDETYDPIR-SVRTGRYKYIR---------NYMPE-------ELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWMK 373
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-513 |
2.23e-89 |
|
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: 280.26 E-value: 2.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGgilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGV-------TTL 110
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYG---NPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVlnnvenaGAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 111 GAGLSPEHNNIAKELQKGGYQTSVIGKWHLKQEPAGFDYYCvlpgqgEYWNPrlktKENWEDYYgggktyegfstdiIAD 190
Cdd:cd16033 78 SRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEETPLDYGF------DEYLP----VETTIEYF-------------LAD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 191 KTIEWIEN-RDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDKGpettgrsfvgqsvdNLKkrylaatad 269
Cdd:cd16033 135 RAIEMLEElAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDF--------------EDK--------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 270 PSLRKDFMNYPelpfsvDGLTDDEARYKtyqKYVKDFMRCGAAADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHG 349
Cdd:cd16033 192 PYIYRRERKRW------GVDTEDEEDWK---EIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 350 WFDKRLI-FEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKGNTPDDWRKYGYYR 428
Cdd:cd16033 263 LWDKGPFmYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPEDWRDEVVTE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 429 YWDHskdrpgHFG-----IRGERYKLAFfygnglksnnytpenQPTQFWDFYDLKEDPNELHNAYKDPKYQDIIAGMKAE 503
Cdd:cd16033 343 YNGH------EFYlpqrmVRTDRYKYVF---------------NGFDIDELYDLESDPYELNNLIDDPEYEEILREMRTR 401
|
490
....*....|
gi 1110313252 504 ILAQREALGD 513
Cdd:cd16033 402 LYEWMEETGD 411
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-486 |
3.07e-89 |
|
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: 279.45 E-value: 3.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGgilEDYVHTPNIKRLAAEGTVLENClVSNS-ICTPSRATILTGQYSHVNGVTTLGAGLS 115
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAG---DDPVKTPNLDRLAKEGVVFTNA-VSNYpVCSPYRASLLTGQYPLTNGVFGNDVPLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 116 PEHNNIAKELQKGGYQTSVIGKWHL----KQEPAGFDYYCvlPG---QG-EYWnprlKTKENWEDYY--------GGGKT 179
Cdd:cd16034 77 PDAPTIADVLKDAGYRTGYIGKWHLdgpeRNDGRADDYTP--PPerrHGfDYW----KGYECNHDHNnphyydddGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 180 YEGFSTDIIADKTIEWIENR-DKSKPFMAMchfkathepfdypkrfshlyrdVDIPVPDSFYDKGPETtgrsfvgqsvdn 258
Cdd:cd16034 151 IKGYSPDAETDLAIEYLENQaDKDKPFALV----------------------LSWNPPHDPYTTAPEE------------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 259 LKKRYlaataDPSLRKDFMNYPElpfsvdgltdDEARYKTYQKYVKDFMRCGAAADDNIGKLLDYLDAAGLAENTIVIYT 338
Cdd:cd16034 197 YLDMY-----DPKKLLLRPNVPE----------DKKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 339 ADQGYFLGEHGWFDKRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKG--N 416
Cdd:cd16034 262 SDHGDMLGSHGLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGgkD 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1110313252 417 TPDDWRKYGYYRYWDH--SKDRPGHFGIRGERYKLAFFygnglksnnytpENQPtqfWDFYDLKEDPNELHN 486
Cdd:cd16034 342 DEPDSVLLQCFVPFGGgsARDGGEWRGVRTDRYTYVRD------------KNGP---WLLFDNEKDPYQLNN 398
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
37-491 |
6.40e-76 |
|
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: 244.77 E-value: 6.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDhtsQAWgiyggILEDYVHTPNIKR-LAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTL---GA 112
Cdd:cd16147 1 RPNIVLILTDD---QDV-----ELGSMDPMPKTKKlLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNsppGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 113 GLSP------EHNNIAKELQKGGYQTSVIGK--------WHLKQEPAGFDYYCVL--PGQGEYWNPRLKTKEnwedyyGG 176
Cdd:cd16147 73 GYPKfwqnglERSTLPVWLQEAGYRTAYAGKylngygvpGGVSYVPPGWDEWDGLvgNSTYYNYTLSNGGNG------KH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 177 GKTYEG-FSTDIIADKTIEWIENRDKS-KPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDKGPettgrsfvgq 254
Cdd:cd16147 147 GVSYPGdYLTDVIANKALDFLRRAAADdKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPPPNNPDV---------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 255 svdNLKKRYLAATAdpslrkdfmnypelpfsvdGLTDDEARY--KTYQKYvkdfMRCGAAADDNIGKLLDYLDAAGLAEN 332
Cdd:cd16147 217 ---SDKPHWLRRLP-------------------PLNPTQIAYidELYRKR----LRTLQSVDDLVERLVNTLEATGQLDN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 333 TIVIYTADQGYFLGEHGW-FDKRLIFEESIHMPFVIRYPKeVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSfRE 411
Cdd:cd16147 271 TYIIYTSDNGYHLGQHRLpPGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRS-CG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 412 NLKGNTpddwrkygyyrYWdhskdrpghfGIRGERYKLAFFYGnglksnnytpeNQPTQFWDFYDLKEDPNELHNAYKDP 491
Cdd:cd16147 349 DSNNNT-----------YK----------CVRTVDDTYNLLYF-----------EWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
38-408 |
1.12e-74 |
|
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: 236.18 E-value: 1.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTL---GAGL 114
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGN---PDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNvgnGGGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 115 SPEHNNIAKELQKGGYQTSVIGKWHlkqepagfdyycvlpgqgeywnprlktkenwedyygggktyegfstdiiaDKTIE 194
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH--------------------------------------------------DEAID 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 195 WIENRDKSKPFMAMCHFKATHEPFDYpkrfshlYRDVdipvpdsfydkgpettgrsfvgqsvdnlkkrylaatadpslrk 274
Cdd:cd16022 108 FIERRDKDKPFFLYVSFNAPHPPFAY-------YAMV------------------------------------------- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 275 dfmnypelpfsvdgltddearyktyqkyvkdfmrcgAAADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHGW-FDK 353
Cdd:cd16022 138 ------------------------------------SAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKK 181
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1110313252 354 RLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPETMQGRS 408
Cdd:cd16022 182 GSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
38-508 |
1.38e-70 |
|
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: 232.53 E-value: 1.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMAD----DHtsqawgiYGGILEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAG 113
Cdd:cd16028 1 RNVLFITADqwraDC-------LSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 114 LSPEHNNIAKELQKGGYQTSVIGK-----------------WHLKQEPAGFDYYCVLPGQGEywnprlktkenwedyygg 176
Cdd:cd16028 74 LDARHLTLALELRKAGYDPALFGYtdtspdprglapldprlLSYELAMPGFDPVDRLDEYPA------------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 177 gktyEGFSTDIIADKTIEWIENRDKsKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDKGPEttgrsfvgQSV 256
Cdd:cd16028 136 ----EDSDTAFLTDRAIEYLDERQD-EPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPPIRAESLAAE--------AAQ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 257 DNLKKRYLAATADPSLRKDFMNYPELpfsvDGLTDDEARyKTYqkyvkdfmrCG--AAADDNIGKLLDYLDAAGLAENTI 334
Cdd:cd16028 203 HPLLAAFLERIESLSFSPGAANAADL----DDEEVAQMR-ATY---------LGliAEVDDHLGRLFDYLKETGQWDDTL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 335 VIYTADQGYFLGEHGWFDKRLIFEESIHMPFVIRYPKE---VRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRE 411
Cdd:cd16028 269 IVFTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRReadATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLP 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 412 NLKGNTPDDWRKYGYYRYWDHSKDRPG---HFG----------IRGERYKLAFFygNGLksnnytpenqPTQfwdFYDLK 478
Cdd:cd16028 349 LLAGAQPSDWRDAVHYEYDFRDVSTRRpqeALGlspdecslavIRDERWKYVHF--AAL----------PPL---LFDLK 413
|
490 500 510
....*....|....*....|....*....|
gi 1110313252 479 EDPNELHNAYKDPKYQDIIAGMKAEILAQR 508
Cdd:cd16028 414 NDPGELRDLAADPAYAAVVLRYAQKLLSWR 443
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
37-493 |
7.50e-68 |
|
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: 225.14 E-value: 7.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAwGIYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSP 116
Cdd:cd16030 2 KPNVLFIAVDDLRPWL-GCYGG---HPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 117 EHNN---IAKELQKGGYQTSVIGK------WHLKQEPAGFDYYCVLPGQGEYWNPRLKTKENWEDYYGGGKTYEGFS--- 184
Cdd:cd16030 78 VAPDavtLPQYFKENGYTTAGVGKifhpgiPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADvpd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 185 ---TDI-IADKTIEWIENR-DKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDKG-PEttgrsfvgQSVDN 258
Cdd:cd16030 158 eayPDGkVADEAIEQLRKLkDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPLPNPFDPIDlPE--------VAWND 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 259 LKKRYlAATADPSLRKDFMNYPelpfsvdgLTDDEARyktyqKYVKDFMRCGAAADDNIGKLLDYLDAAGLAENTIVIYT 338
Cdd:cd16030 230 LDDLP-KYGDIPALNPGDPKGP--------LPDEQAR-----ELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 339 ADQGYFLGEHGWFDKRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADfsaLF---ADYAGIDYPETMQGRSFRENLKg 415
Cdd:cd16030 296 SDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVD---IYptlAELAGLPAPPCLEGKSLVPLLK- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 416 NTPDDWRKYGYYRYwdhskDRPGHFG--IRGERYKLaffygnglksnnytpenqpTQFWDF--------YDLKEDPNELH 485
Cdd:cd16030 372 NPSAKWKDAAFSQY-----PRPSIMGysIRTERYRY-------------------TEWVDFdkvgaeelYDHKNDPNEWK 427
|
....*...
gi 1110313252 486 NAYKDPKY 493
Cdd:cd16030 428 NLANDPEY 435
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
37-509 |
9.10e-67 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 223.78 E-value: 9.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGgilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSP 116
Cdd:PRK13759 6 KPNIILIMVDQMRGDCLGCNG---NKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 117 EHNN-IAKELQKGGYQTSVIGKWHLKQEPAGFDYYCVLPGQGEYWNPRLKTKENWE---DY----YGGGKTYEGFSTDI- 187
Cdd:PRK13759 83 NYKNtLPQEFRDAGYYTQCIGKMHVFPQRNLLGFHNVLLHDGYLHSGRNEDKSQFDfvsDYlawlREKAPGKDPDLTDIg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 188 ----------------------IADKTIEWIENRDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPdsfydkgpe 245
Cdd:PRK13759 163 wdcnswvarpwdleerlhptnwVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADIPDP--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 246 ttgrsFVGQsvdnlkkryLAATADPSLRKDFMNYPELPFSVDGLTDDEARYKTYQKYVkdfmrcgaaaDDNIGKLLDYLD 325
Cdd:PRK13759 234 -----HIGD---------WEYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHI----------DHQIGRFLQALK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 326 AAGLAENTIVIYTADQGYFLGEHGWFDKRLIFEESIHMPFVIRYP---KEVRAGARNKDLIENADFSALFADYAGIDYPE 402
Cdd:PRK13759 290 EFGLLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGTIPD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 403 TMQGRSFRENLKGNTPdDWRKYgyyrywdhskdrpghfgIRGEryklaffYGNGLKSNNYTPENQPTQFW-------DFY 475
Cdd:PRK13759 370 DVDGRSLKNLIFGQYE-GWRPY-----------------LHGE-------HALGYSSDNYLTDGKWKYIWfsqtgeeQLF 424
|
490 500 510
....*....|....*....|....*....|....*..
gi 1110313252 476 DLKEDPNELHNAYKDPKYQDIIAGMKAEI---LAQRE 509
Cdd:PRK13759 425 DLKKDPHELHNLSPSEKYQPRLREMRKKLvdhLRGRE 461
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
38-503 |
1.42e-66 |
|
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: 220.88 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDhtsQAWGIYGGILEDYVHTPNIKRLAAEGTVLENCLVSNSiCTPSRATILTGQYSHVNGVTTLGAG---L 114
Cdd:cd16146 1 PNVILILTDD---QGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPV-CAPTRAALLTGRYPFRTGVWHTILGrerM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 115 SPEHNNIAKELQKGGYQTSVIGKWHL-KQEP-----AGFDYYCVLPGQ--GEYWNPRLKTKENWEDYYGGG-KTYEGFST 185
Cdd:cd16146 77 RLDETTLAEVFKDAGYRTGIFGKWHLgDNYPyrpqdRGFDEVLGHGGGgiGQYPDYWGNDYFDDTYYHNGKfVKTEGYCT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 186 DIIADKTIEWIEnRDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDvdipvpdsfydkgpettgrsfvgqsvdnlkkryla 265
Cdd:cd16146 157 DVFFDEAIDFIE-ENKDKPFFAYLATNAPHGPLQVPDKYLDPYKD----------------------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 266 atadpslrkdfmnypelpfsvDGLTDDEARYktYqkyvkdfmrcGAAA--DDNIGKLLDYLDAAGLAENTIVIYTADQGY 343
Cdd:cd16146 201 ---------------------MGLDDKLAAF--Y----------GMIEniDDNVGRLLAKLKELGLEENTIVIFMSDNGP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 344 FLGEHGWFDKRL------IFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPET--MQGRSFRENLKG 415
Cdd:cd16146 248 AGGVPKRFNAGMrgkkgsVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGikLDGRSLLPLLKG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 416 NTPDDWRKYGYYRY--WDHSKDRPGHFGIRGERYKLAffygnglksnnytpeNQPTQFWDFYDLKEDPNELHNAYKdpKY 493
Cdd:cd16146 328 ESDPWPERTLFTHSgrWPPPPKKKRNAAVRTGRWRLV---------------SPKGFQPELYDIENDPGEENDVAD--EH 390
|
490
....*....|
gi 1110313252 494 QDIIAGMKAE 503
Cdd:cd16146 391 PEVVKRLKAA 400
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-486 |
1.26e-64 |
|
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: 214.77 E-value: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGGilEDYvHTPNIKRLAAEGTVLENCLvSNSICTPSRATILTGQYSHVNGVTtlGAGLSPE 117
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGG--ESY-KTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVV--FGYLDPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 118 HNNIAKELQKGGYQTSVIGKWHLKQEP--------AGFDYYCVLPGQGE---YWNPRLktkENWEDYYGGG-KTYEG-FS 184
Cdd:cd16151 75 QKTFGHLLKDAGYATAIAGKWQLGGGRgdgdypheFGFDEYCLWQLTETgekYSRPAT---PTFNIRNGKLlETTEGdYG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 185 TDIIADKTIEWIEnRDKSKPFMAMCHFKATHEPFDypkrfshlyrdvdiPVPDSfydkgpettgrsfvgqsvdnlkkryl 264
Cdd:cd16151 152 PDLFADFLIDFIE-RNKDQPFFAYYPMVLVHDPFV--------------PTPDS-------------------------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 265 aatadpslrkdfmnypelpfsvDGLTDDEARYKTYQKYVKDfMrcGAAADDNIGKLLDYLDAAGLAENTIVIYTADQGYF 344
Cdd:cd16151 191 ----------------------PDWDPDDKRKKDDPEYFPD-M--VAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTH 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 345 LGEHGWFDKRLI-------FEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPE--TMQGRSFRENLKG 415
Cdd:cd16151 246 RPITSRTNGREVrggkgktTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEdyPLDGRSFAPQLLG 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1110313252 416 NTPDDWRKYgYYRYWDHSKDRPGHFGIRGERYKLaffYGNGlksnnytpenqptqfwDFYDLKEDPNELHN 486
Cdd:cd16151 326 KTGSPRREW-IYWYYRNPHKKFGSRFVRTKRYKL---YADG----------------RFFDLREDPLEKNP 376
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-503 |
1.46e-64 |
|
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: 214.35 E-value: 1.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGGileDYVHTPNIKRLAAEGTVLENCLV----SNSICTPSRATILTGQYshVNGVTTLG- 111
Cdd:cd16155 2 KPNILFILADDQRADTIGALGN---PEIQTPNLDRLARRGTSFTNAYNmggwSGAVCVPSRAMLMTGRT--LFHAPEGGk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 112 AGLSPEHNNIAKELQKGGYQTSVIGKWHLkqepagfdyycvlpgqgeywnprlktkenwedyygggktyeGFstdiiADK 191
Cdd:cd16155 77 AAIPSDDKTWPETFKKAGYRTFATGKWHN-----------------------------------------GF-----ADA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 192 TIEWIENRDKS-KPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDKGPETTGrsfvgqsvdnlkkrylaataDP 270
Cdd:cd16155 111 AIEFLEEYKDGdKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENFLPQHPFDNG--------------------EG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 271 SLRKDFM-NYPELPFSVdgltddearyktyQKYVKDFMRCGAAADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHG 349
Cdd:cd16155 171 TVRDEQLaPFPRTPEAV-------------RQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 350 WFDKRLIFEESIHMPFVIRYPKeVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKGNTpDDWRK--YGYY 427
Cdd:cd16155 238 LMGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEK-KAVRDtlYGAY 315
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1110313252 428 RYWdhskdrpgHFGIRGERYKLAFfygnglksnnYTPENQPTQfwdFYDLKEDPNELHNAYKDPKYQDIIAGMKAE 503
Cdd:cd16155 316 RDG--------QRAIRDDRWKLII----------YVPGVKRTQ---LFDLKKDPDELNNLADEPEYQERLKKLLAE 370
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-506 |
1.73e-61 |
|
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: 207.78 E-value: 1.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSPE 117
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGS---KFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 118 HNN------------------IAKELQKGGYQTSVIGKWHLKQEPA------GFDY---YCVLPGQGEYWNPRLKTKENW 170
Cdd:cd16144 78 PDNtklipppsttrlpleevtIAEALKDAGYATAHFGKWHLGGEGGygpedqGFDVnigGTGNGGPPSYYFPPGKPNPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 171 EDYYGGGKTyegfsTDIIADKTIEWIENRdKSKPFMAMCHFKATHEPFDYPKRFShlyrdvdipvpDSFYDKGPETTGRs 250
Cdd:cd16144 158 EDGPEGEYL-----TDRLTDEAIDFIEQN-KDKPFFLYLSHYAVHTPIQARPELI-----------EKYEKKKKGLRKG- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 251 fvgqsvdnlkkrylaatadpslrkdfmnypelpfsvdgltDDEARYktyqkyvkdfmrcgAA----ADDNIGKLLDYLDA 326
Cdd:cd16144 220 ----------------------------------------QKNPVY--------------AAmiesLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 327 AGLAENTIVIYTADQGYFLGEHGWFD--------KRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGI 398
Cdd:cd16144 246 LGLADNTLVIFTSDNGGLSTRGGPPTsnaplrggKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 399 DYPE--TMQGRSFRENLKGNTPDDWRK--YGYYRYWDHSKDRPGHfGIRGERYKLAFFYGNGLksnnytpenqptqfWDF 474
Cdd:cd16144 326 PLPPpqHLDGVSLVPLLKGGEADLPRRalFWHFPHYHGQGGRPAS-AIRKGDWKLIEFYEDGR--------------VEL 390
|
490 500 510
....*....|....*....|....*....|...
gi 1110313252 475 YDLKEDPNELHN-AYKDPkyqDIIAGMKAEILA 506
Cdd:cd16144 391 YNLKNDIGETNNlAAEMP---EKAAELKKKLDA 420
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
37-486 |
3.53e-60 |
|
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: 203.83 E-value: 3.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGGilEdyVHTPNIKRLAAEGTVLENCLVSnSICTPSRATILTGQYSHVNGVTTLGAG--- 113
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGG--E--IPTPNLDALAAEGLRFTNFHTT-ALCSPTRAALLTGRNHHQVGMGTMAELatg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 114 -------LSPEHNNIAKELQKGGYQTSVIGKWHLkqepaGFDyycvlpgqgeywnprlktkenweDYYgggktyegfSTD 186
Cdd:cd16025 77 kpgyegyLPDSAATIAEVLKDAGYHTYMSGKWHL-----GPD-----------------------DYY---------STD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 187 IIADKTIEWI-ENRDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVdipvpdsfYDKGPettgrsfvgqsvDNLKKRYLA 265
Cdd:cd16025 120 DLTDKAIEYIdEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGK--------YDAGW------------DALREERLE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 266 ---------ATADPSLRkdfmnyPELPFSVDGLTDDEaryktyQKYVKDFMRCGAA----ADDNIGKLLDYLDAAGLAEN 332
Cdd:cd16025 180 rqkelglipADTKLTPR------PPGVPAWDSLSPEE------KKLEARRMEVYAAmvehMDQQIGRLIDYLKELGELDN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 333 TIVIYTADQGYfLGEHGW---------FDKRLIFEESIHMPFVIRYPKEVRA-GARNKDLIENADFSALFADYAGIDYPE 402
Cdd:cd16025 248 TLIIFLSDNGA-SAEPGWanasntpfrLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYPK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 403 T--------MQGRSFRENLKGN---TPDDWrkygyyRYWDHSkdrpGHFGIRGERYKLAFFYgnglksnnytPENQPTQF 471
Cdd:cd16025 327 TvngvpqlpLDGVSLLPTLDGAaapSRRRT------QYFELF----GNRAIRKGGWKAVALH----------PPPGWGDQ 386
|
490
....*....|....*
gi 1110313252 472 WDFYDLKEDPNELHN 486
Cdd:cd16025 387 WELYDLAKDPSETHD 401
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-482 |
2.77e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 198.92 E-value: 2.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGgilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSPE 117
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYG---HPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 118 HNNIAKELQKGGYQTSVIGKWHLKQE--PAGFDYycvlpgqgeywnprlktkenwedyygggktyegfsTDIIADKTIEW 195
Cdd:cd16037 78 VPSWGHALRAAGYETVLIGKLHFRGEdqRHGFRY-----------------------------------DRDVTEAAVDW 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 196 IENRDKS-KPFMAMCHFKATHEPFDYPKRFshlyrdvdipvpdsfydkgpettgrsfvgqsvdnlkkrylaatadpslrk 274
Cdd:cd16037 123 LREEAADdKPWFLFVGFVAPHFPLIAPQEF-------------------------------------------------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 275 dfmnypelpfsvdgltddearyktYQKYVKdfmRCGAA-------ADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGE 347
Cdd:cd16037 153 ------------------------YDLYVR---RARAAyyglvefLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGE 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 348 HGWFDKRLIFEESIHMPFVIRYPKeVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKGntPDDWRKYGYY 427
Cdd:cd16037 206 RGLWGKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEG--PDDPDRVVFS 282
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1110313252 428 RYWDHSKDRpGHFGIRGERYKLAFFYGnglksnnYTPEnqptqfwdFYDLKEDPN 482
Cdd:cd16037 283 EYHAHGSPS-GAFMLRKGRWKYIYYVG-------YPPQ--------LFDLENDPE 321
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-507 |
6.05e-54 |
|
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: 186.28 E-value: 6.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGGILEdyvHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSP 116
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLD---LTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 117 EHNNIAKELQKGGYQTSVIGKWHLKqepagfdyycvlpgqgeywnprlktkenwedyygggktyeGFSTDIIADKTIEWI 196
Cdd:cd16152 78 DEKTLAHYFRDAGYETGYVGKWHLA----------------------------------------GYRVDALTDFAIDYL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 197 ENRDKSKPFMAMCHFKathEPfdypkrfsHLYRDVDIPVpdsfydkGPEttgrsfvgqsvdNLKKRYlaatADPSLRKDF 276
Cdd:cd16152 118 DNRQKDKPFFLFLSYL---EP--------HHQNDRDRYV-------APE------------GSAERF----ANFWVPPDL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 277 mnypelpfsvdgltddEARYKTYQKYVKDFMRCGAAADDNIGKLLDYLDAAGLAENTIVIYTADQG-YFL---GEHgwfd 352
Cdd:cd16152 164 ----------------AALPGDWAEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGcHFRtrnAEY---- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 353 KRLIFEESIHMPFVIRYPKeVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKGNTPdDWRKYGYYRYwdh 432
Cdd:cd16152 224 KRSCHESSIRVPLVIYGPG-FNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVE-DWRNEVFIQI--- 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 433 SKDRPGHfGIRGERYKLAFF--YGNGLK---SNNYTPENqptqfwdFYDLKEDPNELHNAYKDPKYQDIIAGMKAEILAQ 507
Cdd:cd16152 299 SESQVGR-AIRTDRWKYSVAapDKDGWKdsgSDVYVEDY-------LYDLEADPYELVNLIGRPEYREVAAELRERLLAR 370
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-488 |
3.13e-53 |
|
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: 185.10 E-value: 3.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDhtsqaWGI-----YGGilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQY---SHVNGVTT 109
Cdd:cd16143 1 PNIVIILADD-----LGYgdiscYNP--DSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYpwrSRLKGGVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 110 LGAG---LSPEHNNIAKELQKGGYQTSVIGKWHLkqepaGFDYYcvlPGQGEYWNPRLKTKENWEDYYGGGKTYEGF--- 183
Cdd:cd16143 74 GGFSpplIEPDRVTLAKMLKQAGYRTAMVGKWHL-----GLDWK---KKDGKKAATGTGKDVDYSKPIKGGPLDHGFdyy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 184 -------STDIIADKTIEWI-ENRDKSKPFMAMCHFKATHEPFdypkrfshlyrdvdIPVPDsfydkgpettgrsFVGQS 255
Cdd:cd16143 146 fgipaseVLPTLTDKAVEFIdQHAKKDKPFFLYFALPAPHTPI--------------VPSPE-------------FQGKS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 256 vdnlkkrylaataDPSLRKDFmnypelpfsvdgltddearyktyqkyVKDFmrcgaaaDDNIGKLLDYLDAAGLAENTIV 335
Cdd:cd16143 199 -------------GAGPYGDF--------------------------VYEL-------DWVVGRILDALKELGLAENTLV 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 336 IYTADQGyflGEHGWFD-----------------KRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGI 398
Cdd:cd16143 233 IFTSDNG---PSPYADYkelekfghdpsgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQ 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 399 DYPETMQ--GRSFRENLKGNTPDDWRKYgyyrYWDHSKDrpGHFGIRGERYKLAFFYGNGLKSNNYTPENQPTQFWDFYD 476
Cdd:cd16143 310 KLPDNAAedSFSFLPALLGPKKQEVRES----LVHHSGN--GSFAIRKGDWKLIDGTGSGGFSYPRGKEKLGLPPGQLYN 383
|
490
....*....|..
gi 1110313252 477 LKEDPNELHNAY 488
Cdd:cd16143 384 LSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-411 |
1.21e-52 |
|
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: 179.67 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMAD----DHTsqawGIYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTtlGAG 113
Cdd:cd16148 1 MNVILIVIDslraDHL----GCYGY---DRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW--GGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 114 LSPEHNNIAKELQKGGYQTSVIGKW-HLKQEP---AGFDYYcvlpgqgeywnprlktkENWEDYYGGGKTYEGFSTDIIA 189
Cdd:cd16148 72 LEPDDPTLAEILRKAGYYTAAVSSNpHLFGGPgfdRGFDTF-----------------EDFRGQEGDPGEEGDERAERVT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 190 DKTIEWIENRDKSKPFMAMCHFKATHEPFDYpkrfshlyrdvdipvpdsfydkgpettgrsfvgqsvdnlkkrylaatad 269
Cdd:cd16148 135 DRALEWLDRNADDDPFFLFLHYFDPHEPYLY------------------------------------------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 270 pslrkdfmnypelpfsvdgltDDEARYktyqkyvkdfmrcgaaADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHG 349
Cdd:cd16148 166 ---------------------DAEVRY----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHG 208
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110313252 350 WFDK--RLIFEESIHMPFVIRYPKeVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRE 411
Cdd:cd16148 209 LYWGhgSNLYDEQLHVPLIIRWPG-KEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-505 |
2.70e-52 |
|
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: 183.59 E-value: 2.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGgilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSPE 117
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLG---NPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 118 HNNIAKELQKGGYQTSVIGKWHLKQEPAGFDYYCvlpgqgeywnprlktKENWEdyygggktyegfstdiIADKTIEWIE 197
Cdd:cd16150 78 EPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC---------------DSDEA----------------CVRTAIDWLR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 198 NRDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVpdsfydkgpettgrsfvgqsvdnLKKRYLAATADPSLRKDFM 277
Cdd:cd16150 127 NRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPP-----------------------RRPPGLRAKGKPSMLEGIE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 278 NYpelpfSVDGLTDDEAR--YKTYQKYVKDFmrcgaaaDDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHGwfdkrL 355
Cdd:cd16150 184 KQ-----GLDRWSEERWRelRATYLGMVSRL-------DHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYG-----L 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 356 I------FEESI-HMPFVIRYPKEVrAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENLKGnTPDDWRKY---- 424
Cdd:cd16150 247 VekwpntFEDCLtRVPLIIKPPGGP-AGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAG-ETEEHRDAvfse 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 425 -GYYR---------------YWDHS---KDRPGH---FGIRGERYKLAF-FYGNglksnnytPEnqptqfwdFYDLKEDP 481
Cdd:cd16150 325 gGRLHgeeqamegghgpydlKWPRLlqqEEPPEHtkaVMIRTRRYKYVYrLYEP--------DE--------LYDLEADP 388
|
490 500
....*....|....*....|....
gi 1110313252 482 NELHNAYKDPKYQDIIAGMKAEIL 505
Cdd:cd16150 389 LELHNLIGDPAYAEIIAEMKQRLL 412
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
37-486 |
5.71e-51 |
|
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: 179.30 E-value: 5.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDhtsQAWG---IYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQY------SHVNGV 107
Cdd:cd16026 1 KPNIVVILADD---LGYGdlgCYGS---PLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvglPGVVGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 108 TTLGAGLSPEHNNIAKELQKGGYQTSVIGKWHLKQEPA------GFDYYCVLPGQGEYWNPRLKTKENWEDYYGGGKTYE 181
Cdd:cd16026 75 PGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEflptrhGFDEYFGIPYSNDMWPFPLYRNDPPGPLPPLMENEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 182 ------GFS--TDIIADKTIEWIEnRDKSKPFmamchfkathepFDYpkrFSHLYRDVdipvpdsfydkgPETTGRSFVG 253
Cdd:cd16026 155 vieqpaDQSslTQRYTDEAVDFIE-RNKDQPF------------FLY---LAHTMPHV------------PLFASEKFKG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 254 QSVDNLkkrYlaatadpslrKDFMNypELpfsvdgltddearyktyqkyvkdfmrcgaaaDDNIGKLLDYLDAAGLAENT 333
Cdd:cd16026 207 RSGAGL---Y----------GDVVE--EL-------------------------------DWSVGRILDALKELGLEENT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 334 IVIYTADQGYFL------GEHGWFD--KRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPE--T 403
Cdd:cd16026 241 LVIFTSDNGPWLeygghgGSAGPLRggKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEdrV 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 404 MQGRSFRENLKGNTPDDWRKYGYYRYWDHSkdrpghFGIRGERYKLAFFYGNGLKSNNYTPENQPTQFWDFYDLKEDPNE 483
Cdd:cd16026 321 IDGKDISPLLLGGSKSPPHPFFYYYDGGDL------QAVRSGRWKLHLPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGE 394
|
...
gi 1110313252 484 LHN 486
Cdd:cd16026 395 TYN 397
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-486 |
1.29e-49 |
|
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: 175.86 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDhtsqaWGI-----YGgilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYS-H----VNGV 107
Cdd:cd16145 1 PNIIFILADD-----LGYgdlgcYG---QKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTgHtrvrGNSE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 108 TTLGAGLSPEHNNIAKELQKGGYQTSVIGKWHLKQ-------EPAGFD----YYCVLPGQGEYW-------------NPR 163
Cdd:cd16145 73 PGGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGpgtpghpTKQGFDyfygYLDQVHAHNYYPeylwrngekvplpNNV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 164 LKTKENWEDYYGGGKTYegfSTDIIADKTIEWI-ENRDksKPFMAMCHFKATHEPfdypkrfshlyrdvdIPVPDSFYDK 242
Cdd:cd16145 153 IPPLDEGNNAGGGGGTY---SHDLFTDEALDFIrENKD--KPFFLYLAYTLPHAP---------------LQVPDDGPYK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 243 GPETTGRSFVGQSVDNLKKRYLAATadpslrkdfmnypelpfsvdgltddearyktyqKYVkdfmrcgaaaDDNIGKLLD 322
Cdd:cd16145 213 YKPKDPGIYAYLPWPQPEKAYAAMV---------------------------------TRL----------DRDVGRILA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 323 YLDAAGLAENTIVIYTADQG---YFLGEHG--WFD--------KRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFS 389
Cdd:cd16145 250 LLKELGIDENTLVVFTSDNGphsEGGSEHDpdFFDsngplrgyKRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFM 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 390 ALFADYAGIDYPETMQGRSFRENLKGNTPDDWRKYGYYRYWDHSKDRpghfGIRGERYKLAffygnglksnNYTPENQPT 469
Cdd:cd16145 330 PTLADLAGAEPPEDIDGISLLPTLLGKPQQQQHDYLYWEFYEGGGAQ----AVRMGGWKAV----------RHGKKDGPF 395
|
490
....*....|....*..
gi 1110313252 470 QfwdFYDLKEDPNELHN 486
Cdd:cd16145 396 E---LYDLSTDPGETNN 409
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-411 |
1.58e-49 |
|
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: 171.27 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGgilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQY-----------SHVNG 106
Cdd:cd16149 1 PNILFILTDDQGPWALGCYG---NSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgihdwivEGSHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 107 VTTLGAGLSPEHNNIAKELQKGGYQTSVIGKWHLkqepagfdyycvlpgqGEywnprlktkenwedyygggktyegfstd 186
Cdd:cd16149 78 KTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHL----------------GD---------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 187 iiaDKTIEWIENRDKSKPFMAMCHFKATHEPFDYpkrfshlyrdvdipvpdsfydkgpettgrsfvgqsvdnlkkryLAA 266
Cdd:cd16149 114 ---DAADFLRRRAEAEKPFFLSVNYTAPHSPWGY-------------------------------------------FAA 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 267 TAdpslrkdfmnypelpfsvdgltddearyktyqkyvkdfmrcgaAADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLG 346
Cdd:cd16149 148 VT-------------------------------------------GVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMG 184
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1110313252 347 EHGWFDK-----RL-IFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPE--TMQGRSFRE 411
Cdd:cd16149 185 HHGIWGKgngtfPLnMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPAdpRLPGRSFAD 257
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
38-506 |
7.18e-49 |
|
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: 175.26 E-value: 7.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADdhtSQAWGIYGGILEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSPE 117
Cdd:cd16156 1 KQFIFIMTD---TQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 118 HNNIAKELQKGGYQTSVIGKWHLKqepaGFDY--YCVLPgQG---EYW-------------NPRLKTKENWEDYY---GG 176
Cdd:cd16156 78 VKTIGQRLSDNGIHTAYIGKWHLD----GGDYfgNGICP-QGwdpDYWydmrnyldelteeERRKSRRGLTSLEAegiKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 177 GKTYeGFStdiIADKTIEWIENRdKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVPDSFYDkgpettgrsfvgqsv 256
Cdd:cd16156 153 EFTY-GHR---CTNRALDFIEKH-KDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAYD--------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 257 dnlkkrylaatadpslrkDFMNYPELP--FSVDGLTDDEARYKTYQKYvkdFMRCGAAADDNIGKLLDYLDAagLAENTI 334
Cdd:cd16156 213 ------------------DLENKPLHQrlWAGAKPHEDGDKGTIKHPL---YFGCNSFVDYEIGRVLDAADE--IAEDAW 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 335 VIYTADQGYFLGEHGWFDK-RLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPETMQGRSFRENL 413
Cdd:cd16156 270 VIYTSDHGDMLGAHKLWAKgPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 414 --KGNTPDDWRKYGYYRY-WDHskDRPGHF----GIRGERYKLAFfygNGLKSNnytpenqptqfwDFYDLKEDPNELHN 486
Cdd:cd16156 350 edPEIPENRGVFVEFGRYeVDH--DGFGGFqpvrCVVDGRYKLVI---NLLSTD------------ELYDLEKDPYEMHN 412
|
490 500
....*....|....*....|
gi 1110313252 487 AYKDPKYQDIIAGMKAEILA 506
Cdd:cd16156 413 LIDDPDYADVRDQLHDELLD 432
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
38-398 |
7.65e-46 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 162.59 E-value: 7.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGGILEdyvHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSH-VNGVTTLGAGLSP 116
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRP---TTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHnFGSYVSTPVGLPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 117 EHNNIAKELQKGGYQTSVIGKWHL----KQEPA--GFDYYCVLPGQGEYWNPRLKTKENWEDYYGggktyegfSTDIIAD 190
Cdd:pfam00884 78 TEPSLPDLLKRAGYNTGAIGKWHLgwynNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGGV--------SDEALLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 191 KTIEWIENRDksKPFMAMCHFKATHEPFDYPKRFshlyrdvdipvPDSFYDKGPETTGRSfvgQSVDNlkkrYLAAtadp 270
Cdd:pfam00884 150 EALEFLDNND--KPFFLVLHTLGSHGPPYYPDRY-----------PEKYATFKPSSCSEE---QLLNS----YDNT---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 271 slrkdfmnypelpfsvdgltddeARYktyqkyvkdfmrcgaaADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHGW 350
Cdd:pfam00884 206 -----------------------LLY----------------TDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGG 246
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1110313252 351 FDKRLIF----EESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGI 398
Cdd:pfam00884 247 YLHGGKYdnapEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
38-482 |
9.64e-46 |
|
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: 163.13 E-value: 9.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGGileDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSPE 117
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGN---TVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 118 HNNIAKELQKGGYQTSVIGKWHL--KQEPAGFDYycvlpgqgeywnprlktkenweDyygggktyegfstDIIADKTIEW 195
Cdd:cd16032 78 IPTFAHYLRAAGYRTALSGKMHFvgPDQLHGFDY----------------------D-------------EEVAFKAVQK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 196 IEN---RDKSKPFMAMCHFKATHEPFDYPKRFSHLYrdvdipvpdsfydkgpettgrsfvgqsVDNLKKRYLAATAdpsl 272
Cdd:cd16032 123 LYDlarGEDGRPFFLTVSFTHPHDPYVIPQEYWDLY---------------------------VRRARRAYYGMVS---- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 273 rkdfmnypelpfsvdgltddearyktyqkYVkdfmrcgaaaDDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHG-WF 351
Cdd:cd16032 172 -----------------------------YV----------DDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGlWY 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 352 dKRLIFEESIHMPFVIRYPkEVRAGARNKDLIENADFSALFADYAGI---DYPETMQGRSFRENLKGNTpDDWRKYGYYR 428
Cdd:cd16032 213 -KMSFFEGSARVPLIISAP-GRFAPRRVAEPVSLVDLLPTLVDLAGGgtaPHVPPLDGRSLLPLLEGGD-SGGEDEVISE 289
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1110313252 429 YWDHSKDRPgHFGIRGERYKLaffygnglksnNYTPeNQPTQfwdFYDLKEDPN 482
Cdd:cd16032 290 YLAEGAVAP-CVMIRRGRWKF-----------IYCP-GDPDQ---LFDLEADPL 327
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-483 |
5.24e-42 |
|
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: 154.43 E-value: 5.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGgILEDYVHTPNIKRLAAEGTVLENCLVsNSICTPSRATILTGQYSHVNGVTTLGAGLSPE 117
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYS-LSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGKYGFRTGVLAVPDELLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 118 HNNI----AKELQKGGYQTSVIGKWHLKQEPAGF-------DYYCVLPGQGeywnprlktkenwEDYYGGGKTYEGFSTD 186
Cdd:cd16154 79 EETLlqllIKDATTAGYSSAVIGKWHLGGNDNSPnnpggipYYAGILGGGV-------------QDYYNWNLTNNGQTTN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 187 I-------IADKTIEWIENrdKSKPFMAMCHFKATHEPFDYPkrfshlyrdvdipvPDSFYDKGPettgrsfVGQSVD-- 257
Cdd:cd16154 146 SteyattkLTNLAIDWIDQ--QTKPWFLWLAYNAPHTPFHLP--------------PAELHSRSL-------LGDSADie 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 258 -NLKKRYLAATadpslrkdfmnypelpfsvdgltddearyktyqkyvkdfmrcgAAADDNIGKLLDYLDAAGLaENTIVI 336
Cdd:cd16154 203 aNPRPYYLAAI-------------------------------------------EAMDTEIGRLLASIDEEER-ENTIII 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 337 YTADQG--------YFLGEHGwfdKRLIFEESIHMPFVIrYPKEV-RAGARNKDLIENADFSALFADYAGIDYPETMQGR 407
Cdd:cd16154 239 FIGDNGtpgqvvdlPYTRNHA---KGSLYEGGINVPLIV-SGAGVeRANERESALVNATDLYATIAELAGVDAAEIHDSV 314
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1110313252 408 SFRENLKGnTPDDWRKYGYYRYwdHSKDRPGhFGIRGERYKLAFFygnglKSNNYTpenqptqfwdFYDLKEDPNE 483
Cdd:cd16154 315 SFKPLLSD-VNASTRQYNYTEY--ESPTTTG-WATRNQYYKLIES-----ENGQEE----------LYDLINDPSE 371
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
38-486 |
3.96e-41 |
|
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: 152.32 E-value: 3.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADD--------HTSqawgiyggileDYVHTPNIKRLAAEGTVLENcLVSNSICTPSRATILTGQY------SH 103
Cdd:cd16029 1 PHIVFILADDlgwndvgfHGS-----------DQIKTPNLDALAADGVILNN-YYVQPICTPSRAALMTGRYpihtgmQH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 104 VNGVTTLGAGLSPEHNNIAKELQKGGYQTSVIGKWHL-----KQEPA--GFD----YYCvlpGQGEYWNPRLKTKENWED 172
Cdd:cd16029 69 GVILAGEPYGLPLNETLLPQYLKELGYATHLVGKWHLgfytwEYTPTnrGFDsfygYYG---GAEDYYTHTSGGANDYGN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 173 YYGGGKT-----YEG-FSTDIIADKTIEWIENRDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVDIPVpdsfydkgpet 246
Cdd:cd16029 146 DDLRDNEepawdYNGtYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHI----------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 247 tgrsfvgqsvdnlkkrylaatadpslrkdfmnypelpfsvdgltDDEARyKTYQKYVKdfmrcgaAADDNIGKLLDYLDA 326
Cdd:cd16029 215 --------------------------------------------KDEDR-RTYAAMVS-------ALDESVGNVVDALKA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 327 AGLAENTIVIYTADQGyflGEHGWFD----------KRLIFEESIHMPFVIRYPK-EVRAGARNKDLIENADFSALFADY 395
Cdd:cd16029 243 KGMLDNTLIVFTSDNG---GPTGGGDggsnyplrggKNTLWEGGVRVPAFVWSPLlPPKRGTVSDGLMHVTDWLPTLLSL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 396 AGIDYPET--MQGRSFRENLKGNTP----------DDWRKYgyyrywdhskdrPGHFGIRGERYKLafFYGNGLksnnyt 463
Cdd:cd16029 320 AGGDPDDLppLDGVDQWDALSGGAPsprteillniDDITRT------------TGGAAIRVGDWKL--IVGKPL------ 379
|
490 500
....*....|....*....|...
gi 1110313252 464 penqptqfwdfYDLKEDPNELHN 486
Cdd:cd16029 380 -----------FNIENDPCERND 391
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-486 |
3.77e-40 |
|
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: 149.22 E-value: 3.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDhtsQAW---GIYGGILEDYVHTPNIKRLAAEGTVLENCLVSNSiCTPSRATILTGQYSHVNGVTT----- 109
Cdd:cd16142 1 PNILVILGDD---IGWgdlGCYGGGIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTvglpg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 110 LGAGLSPEHNNIAKELQKGGYQTSVIGKWHLKQEPA------GFDyycvlpgqgEYWNPRLKTKEnwedyygggktyegf 183
Cdd:cd16142 77 SPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGrlptdhGFD---------EFYGNLYHTID--------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 184 stDIIADKTIEWIENRDKS-KPFmamchFkathepfdypkrfshlyrdVDIPvpdsfydkgpettgrsFVGQSVDNLkkr 262
Cdd:cd16142 133 --EEIVDKAIDFIKRNAKAdKPF-----F-------------------LYVN----------------FTKMHFPTL--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 263 ylaatadpsLRKDFmnypelpfsvdgltddEARYKTYQKYvKDFMrcgAAADDNIGKLLDYLDAAGLAENTIVIYTADQG 342
Cdd:cd16142 168 ---------PSPEF----------------EGKSSGKGKY-ADSM---VELDDHVGQILDALDELGIADNTIVIFTTDNG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 343 -----YFLGEHGWF--DKRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGID--------YPETMQGR 407
Cdd:cd16142 219 peqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPdpkdkllgKDRHIDGV 298
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1110313252 408 SFRENLKGNTPDDWRKYGYYrywdHSKDRPGhfGIRGERYKLAFFYGNGLKSNNYTPENQPTqFWDFYDLKEDPNELHN 486
Cdd:cd16142 299 DQSPFLLGKSEKSRRSEFFY----FGEGELG--AVRWKNWKVHFKAQEDTGGPTGEPFYVLT-FPLIFNLRRDPKERYD 370
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-433 |
8.11e-39 |
|
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: 143.89 E-value: 8.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGGILEdyvHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVT-TLGAG--- 113
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAAL---NLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTdTLGSPmqp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 114 -LSPEHNNIAKELQKGGYQTSVIGKWHLkqepagfdyycvlpgqgeywnprlktkenwedyygGGKTYEGFSTD-IIADK 191
Cdd:cd16035 78 lLSPDVPTLGHMLRAAGYYTAYKGKWHL-----------------------------------SGAAGGGYKRDpGIAAQ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 192 TIEWIENRDKSKpfmamchfkATHEPFdypkrfshlyrdvdipvpdsfydkgpettgrsfvgqsvdnlkkrYLAATadps 271
Cdd:cd16035 123 AVEWLRERGAKN---------ADGKPW--------------------------------------------FLVVS---- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 272 lrkdFMNypelPFSVDGLTDDEARYKTYQKYvkdFMRCGAAADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGEHG-- 349
Cdd:cd16035 146 ----LVN----PHDIMFPPDDEERWRRFRNF---YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGlr 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 350 --WFdkrLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPET------MQGRSFR---ENLKGNTP 418
Cdd:cd16035 215 gkGF---NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARateappLPGRDLSpllTDADADAV 291
|
410 420
....*....|....*....|
gi 1110313252 419 DD-----WRKYGYYRYWDHS 433
Cdd:cd16035 292 RDgilftYDRYKFARYFDPP 311
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-408 |
3.66e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 135.97 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGGIL-------EDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTT 109
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNAHtgksesrLGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 110 LGAGL-SPEHNNIA--KELQKGGYQTSVIGKWHLKQepagFDYYcvlpgqgeywnprLKTkENWEDYYGGGKTYEGFSTD 186
Cdd:cd16153 81 FEAAHpALDHGLPTfpEVLKKAGYQTASFGKSHLEA----FQRY-------------LKN-ANQSYKSFWGKIAKGADSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 187 iiadktiewienrdksKPFMAMCHFKATHEPFDYPKRFSHLYrdvdipvpdsfydkgpettgrsfvgqsvdnlkkRYLAA 266
Cdd:cd16153 143 ----------------KPFFVRLSFLQPHTPVLPPKEFRDRF---------------------------------DYYAF 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 267 TAdpslrkdfmnypelpfsvdgltddearyktyqkYVkdfmrcgaaaDDNIGKLLDYLDAAGLA---ENTIVIYTADQGY 343
Cdd:cd16153 174 CA---------------------------------YG----------DAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGW 210
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1110313252 344 FLGEHGWFDKRLIFEESIHMPFVIRYP--KEVRAGARNKDLIENADFSALFADYAGID--YPETMQGRS 408
Cdd:cd16153 211 HLGEQGILAKFTFWPQSHRVPLIVVSSdkLKAPAGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRD 279
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
37-483 |
1.24e-29 |
|
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: 120.27 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDhtsQAWGIYG-GILEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVT-----TL 110
Cdd:cd16161 1 KPNFLLLFADD---LGWGDLGaNWAPNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGhnflpTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 111 GAGLSPEHNNIAKELQKGGYQTSVIGKWHLKQEPA------GFDYYCVLPgqgeywnprlktkenWEDYYGGGKTYEGFS 184
Cdd:cd16161 78 VGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREAylpnsrGFDYYFGIP---------------FSHDSSLADRYAQFA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 185 TDIIAdktiewiENRDKSKPFMAMCHFKATHEPFDYPKRFShlyrdvdipvpdsfydkgPETTGRSFVGQSVdnlkkryl 264
Cdd:cd16161 143 TDFIQ-------RASAKDRPFFLYAALAHVHVPLANLPRFQ------------------SPTSGRGPYGDAL-------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 265 aatadpslrkdfmnypelpfsvdgltddearyktyqkyvkdfmrcgAAADDNIGKLLDYLDAAGLAENTIVIYTADQG-- 342
Cdd:cd16161 190 ----------------------------------------------QEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpw 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 343 -------------YFLGEHGWFD-KRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALFADYAGIDYPET--MQG 406
Cdd:cd16161 224 evkcelavgpgtgDWQGNLGGSVaKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDG 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1110313252 407 RSFRENLKGNTPDDWRkyGYYrYWDHSKDRPGHF-GIRGERYKLAFFYGNGLKSNNYTPENQPTQFWDFYDLKEDPNE 483
Cdd:cd16161 304 KDLSPVLFGGSKTGHR--CLF-HPNSGAAGAGALsAVRCGDYKAHYATGGALACCGSTGPKLYHDPPLLFDLEVDPAE 378
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
37-428 |
8.43e-28 |
|
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: 116.03 E-value: 8.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDhtsQAWGIYGGILEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGA---- 112
Cdd:cd16157 1 KPNIILMLMDD---MGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 113 ---------GLSPEHNNIAKELQKGGYQTSVIGKWHLKQEPA------GFDYYCVLPG--QGEYWN---PRLKTKENWED 172
Cdd:cd16157 78 aytpqnivgGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQyhplkhGFDEWFGAPNchFGPYDNkayPNIPVYRDWEM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 173 YyggGKTYEGFS----------TDIIADKTIEWIEN-RDKSKPFMAMCHFKATHEPfdypkrfshLYrdvdipvpdsfyd 241
Cdd:cd16157 158 I---GRYYEEFKidkktgesnlTQIYLQEALEFIEKqHDAQKPFFLYWAPDATHAP---------VY------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 242 kgpetTGRSFVGQSvdnlkKRylaatadpslrkdfmnypelpfsvdGLTDDEARyktyqkyvkdfmrcgaAADDNIGKLL 321
Cdd:cd16157 213 -----ASKPFLGTS-----QR-------------------------GLYGDAVM----------------ELDSSVGKIL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 322 DYLDAAGLAENTIVIYTADQGYFL-------GEHGWF--DKRLIFEESIHMPFVIRYPKEVRAGARNKDLIENADFSALF 392
Cdd:cd16157 242 ESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTS 321
|
410 420 430
....*....|....*....|....*....|....*...
gi 1110313252 393 ADYAGIDYPETMQ--GRSFRENLKGNTPDDwRKYGYYR 428
Cdd:cd16157 322 LALAGLPIPSDRAidGIDLLPVLLNGKEKD-RPIFYYR 358
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
401-513 |
1.22e-27 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 106.56 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 401 PETMQGRSFRENLKGNTPDDWRKYGYYRYWD----HSKDRpgHFGIRGERYKLAFFYgnglksnnYTPEnqptqFWDFYD 476
Cdd:pfam16347 2 PADMQGKSFLPLLKGKKPKNWRDALYYHYYEypaeHAVKR--HYGVRTERYKLIHFY--------NDID-----EWELYD 66
|
90 100 110
....*....|....*....|....*....|....*..
gi 1110313252 477 LKEDPNELHNAYKDPKYQDIIAGMKAEILAQREALGD 513
Cdd:pfam16347 67 LQKDPKEMNNVYGDPEYAEVQAELKEELEELRKQYKD 103
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
37-516 |
1.30e-27 |
|
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: 116.23 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGgilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQY--------SHVNGV- 107
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFG---NDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmasSHGMRVi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 108 --TTLGAGLSPEHNNIAKELQKGGYQTSVIGKWHL---------------KQepaGFDYYCVLP----------GQGEYW 160
Cdd:cd16159 78 lfTASSGGLPPNETTFAEVLKQQGYSTALIGKWHLglhcesrndfchhplNH---GFDYFYGLPltnlkdcgdgSNGEYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 161 --NPRLKTKENWEDYYGGGKTYEGFSTDIIADKTIEwienrdkskpFMAMCHFKATHEPFDYPKRF----SHLYRDVDI- 233
Cdd:cd16159 155 lsFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFV----------FLLILSLLFISLFFLLLITNryfnCILMRNHEVv 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 234 PVPDSFydkgpETTGRSFVGQSVDNLKKRylaaTADPSLRkdFMNYPELPFSVDGLTDDEARYKtYQKYvkdfmrcGAAA 313
Cdd:cd16159 225 EQPMSL-----ENLTQRLTKEAISFLERN----KERPFLL--VMSFLHVHTALFTSKKFKGRSK-HGRY-------GDNV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 314 ---DDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGE-------HGWFD------KRLIFEESIHMPFVIRYPKEVRAGA 377
Cdd:cd16159 286 eemDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEisvggeyGGGNGgiyggkKMGGWEGGIRVPTIVRWPGVIPPGS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 378 RNKDLIENADFSALFADYAGIDYPE--TMQGRSFRENLKGNTPDDWRKYGYY---------RYwdhsKDRPGhfgirGER 446
Cdd:cd16159 366 VIDEPTSLMDIFPTVAALAGAPLPSdrIIDGRDLMPLLTGQEKRSPHEFLFHycgaelhavRY----RPRDG-----GAV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 447 YKLAFFygnglkSNNYTPEnqpTQFWDFYDL---------KEDPNELHNAYKDPK-----------YQDIIAGMKAEILA 506
Cdd:cd16159 437 WKAHYF------TPNFYPG---TEGCCGTLLcrcfgdsvtHHDPPLLFDLSADPSesnpldptdepYQEIIKKILEAVAE 507
|
570
....*....|
gi 1110313252 507 QREALGDTDQ 516
Cdd:cd16159 508 HQSSIEPVES 517
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
38-503 |
7.40e-26 |
|
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: 110.61 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDhtsqawgIYGGILEDYVH----TPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGV------ 107
Cdd:cd16158 2 PNIVLLFADD-------LGYGDLGCYGHpsssTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVypgvfy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 108 TTLGAGLSPEHNNIAKELQKGGYQTSVIGKWHLKQEP--------AGFDYYCVLP---GQGEYWN-----PRLKTkenwe 171
Cdd:cd16158 75 PGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLngtylpthQGFDHYLGIPyshDQGPCQNltcfpPNIPC----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 172 dyYGGGKTYEG----FSTDIIADKTIEW--IENR--DKSKPFMAMChfKATHEPF--DYPKRFSHLyrdvdipvpdsfyd 241
Cdd:cd16158 150 --FGGCDQGEVpcplFYNESIVQQPVDLltLEERyaKFAKDFIADN--AKEGKPFflYYASHHTHY-------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 242 kgPETTGRSFVGQSVDNlkkrylaatadpslrkdfmnypelPFSvDGLtddearyktyqkyvkdfmrcgAAADDNIGKLL 321
Cdd:cd16158 212 --PQFAGQKFAGRSSRG------------------------PFG-DAL---------------------AELDGSVGELL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 322 DYLDAAGLAENTIVIYTADQGYFL------GEHGWFD--KRLIFEESIHMPFVIRYPKEVRAGaRNKDLIENADFSALFA 393
Cdd:cd16158 244 QTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcgKGTTYEGGVREPAIAYWPGRIKPG-VTHELASTLDILPTIA 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 394 DYAGIDYPE-TMQGRSFRENLKGNTPDDWRKYGYYrYWDHSKDRpGHFGIRGERYKlAFFYGNGLKSNNYTPEN--QPTQ 470
Cdd:cd16158 323 KLAGAPLPNvTLDGVDMSPILFEQGKSPRQTFFYY-PTSPDPDK-GVFAVRWGKYK-AHFYTQGAAHSGTTPDKdcHPSA 399
|
490 500 510
....*....|....*....|....*....|....*....
gi 1110313252 471 FWD------FYDLKEDPNELHNAYKDPKYQDIIAGMKAE 503
Cdd:cd16158 400 ELTshdpplLFDLSQDPSENYNLLGLPEYNQVLKQIQQV 438
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
37-491 |
2.36e-21 |
|
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: 96.73 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADD----------HTSQAWGiyggiledyvhtpNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNG 106
Cdd:cd16160 1 KPNIVLFFADDmgygdlasygHPTQERG-------------PIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 107 V--------TTLGAGLSPEHNNIAKELQKGGYQTSVIGKWHL----------KQEPA--GFDYY-CVLPgqgeywnprlk 165
Cdd:cd16160 68 MyggtrvflPWDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLginennhsdgAHLPShhGFDFVgTNLP----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 166 tkenwedyygggktyegFSTDIIADKTIEWIENRDKSKPFmamchfkathepfdypkrfshLYRDVDIpVPDSFydkGPE 245
Cdd:cd16160 137 -----------------FTNSWACDDTGRHVDFPDRSACF---------------------LYYNDTI-VEQPI---QHE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 246 TTGRSFVGQSV----DNLKKRYlaatadpslrkdFMNYPELPFSVDGLTDDEARYKTYQKYVKDFMRCGAAAddnIGKLL 321
Cdd:cd16160 175 HLTETLVGDAKsfieDNQENPF------------FLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWA---VGEVL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 322 DYLDAAGLAENTIVIYTADQG------YFLGEHGWFD--KRLIFEESIHMPFVIRYPKEVRAGaRNKDLIENADFSALFA 393
Cdd:cd16160 240 DTLVDTGLDQNTLVFFLSDHGphveycLEGGSTGGLKggKGNSWEGGIRVPFIAYWPGTIKPR-VSHEVVSTMDIFPTFV 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 394 DYAGIDYPET--MQGRSFRENLKGNTPDDWRKYGYYrYWDHSkdrpghFGIRGERYKlAFFYGNGLKSNNYTPEN----- 466
Cdd:cd16160 319 DLAGGTLPTDriYDGLSITDLLLGEADSPHDDILYY-CCSRL------MAVRYGSYK-IHFKTQPLPSQESLDPNcdggg 390
|
490 500 510
....*....|....*....|....*....|.
gi 1110313252 467 QPTQFWDFYD------LKEDPNELHNAYKDP 491
Cdd:cd16160 391 PLSDYIVCYDcedecvTKHNPPLIFDVEKDP 421
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
38-408 |
7.26e-17 |
|
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: 82.20 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGiYGGilEDYVHTPNIKRLAAEGTVLENCLVSNSICTPSRATILTGQYSHVNGVTTLGAGLSPE 117
Cdd:cd16171 1 PNVVMVMSDSFDGRLTF-RPG--NQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 118 HNNIAKELQKGGYQTSVIGKwhlkqepagFDYYC---VLPGQGEYWN---PRLKTKEN--WEDYYGGGKTYEGFSTD-II 188
Cdd:cd16171 78 YPTWMDRLEKHGYHTQKYGK---------LDYTSghhSVSNRVEAWTrdvPFLLRQEGrpTVNLVGDRSTVRVMLKDwQN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 189 ADKTIEWIENR--DKSKPFMamchfkathepfdypkrfshLYRDVDIPVPdsfYDKgpETTGRSFvgQSVDNLKKRYLAA 266
Cdd:cd16171 149 TDKAVHWIRKEapNLTQPFA--------------------LYLGLNLPHP---YPS--PSMGENF--GSIRNIRAFYYAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 267 TADpslrkdfmnypelpfsvdgltddearyktyqkyvkdfmrcgaaADDNIGKLLDYLDAAGLAENTIVIYTADQGYFLG 346
Cdd:cd16171 202 CAE-------------------------------------------TDAMLGEIISALKDTGLLDKTYVFFTSDHGELAM 238
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1110313252 347 EHGWFDKRLIFEESIHMPFVIRYPkEVRAGARNKDLIENADFSALFADYAGIDYPETMQGRS 408
Cdd:cd16171 239 EHRQFYKMSMYEGSSHVPLLIMGP-GIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYS 299
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
37-408 |
5.79e-13 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 71.22 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADDHTSQAWGIYGGiLEDYvhTPNIKRLAAEGTVLENCLVS--NSictpSRA--TILTGQYShVNGVTTLGA 112
Cdd:COG1368 234 KPNVVVILLESFSDFFIGALGN-GKDV--TPFLDSLAKESLYFGNFYSQggRT----SRGefAVLTGLPP-LPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 113 GLSPEHNNIAKELQKGGYQTSVIgkwHlkqepagfdyycvlPGQGEYWN-----PRLK-----TKENWEDYYGGGktYeG 182
Cdd:COG1368 306 PGQNNFPSLPSILKKQGYETSFF---H--------------GGDGSFWNrdsfyKNLGfdefyDREDFDDPFDGG--W-G 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 183 FSTDIIADKTIEWIENRDksKPFMAMCHFKATHEPFDYPKRFSHLYrdvDIPvpdsfydkgpettgrsfvgqsvDNLKKR 262
Cdd:COG1368 366 VSDEDLFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEEDKKIP---DYG----------------------KTTLNN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 263 YLAAtadpslrkdfmnypelpfsvdgltddeARYktyqkyvkdfmrcgaaADDNIGKLLDYLDAAGLAENTIVIYTADQG 342
Cdd:COG1368 419 YLNA---------------------------VRY----------------ADQALGEFIEKLKKSGWYDNTIFVIYGDHG 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1110313252 343 YFLGEHGWFDKRLifeESIHMPFVIRYPKEVRaGARNKDLIENADFSALFADYAGIDYPETMQ-GRS 408
Cdd:COG1368 456 PRSPGKTDYENPL---ERYRVPLLIYSPGLKK-PKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRD 518
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
38-397 |
7.31e-13 |
|
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: 68.86 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMA---DDHTSqawgIYGGILEDYvhTPNIKRLAAEGTVLENCLVSNSICTPSRA--TILTGQYSHVNGVTTLGA 112
Cdd:cd16015 1 PNVIVILLesfSDPYI----DKDVGGEDL--TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 113 GLSPEHNNIAKELQKGGYQTSVI----------GKWHLKQepaGFD-YYCVlpgqgEYWNPRLKTKENWedyygggktye 181
Cdd:cd16015 75 YKLNPLPSLPSILKEQGYETIFIhggdasfynrDSVYPNL---GFDeFYDL-----EDFPDDEKETNGW----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 182 GFSTDIIADKTIEWIENRDKsKPFMAMCHFKATHEPFDYPKrfshlyrdvdipvpdsfydkgpettgrsfvgqsvdnlkk 261
Cdd:cd16015 136 GVSDESLFDQALEELEELKK-KPFFIFLVTMSNHGPYDLPE--------------------------------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 262 rylaatadpslrkdfmNYPELPFSVDGLTDDEARYKTYQKYvkdfmrcgaaADDNIGKLLDYLDAAGLAENTIVIYTADQ 341
Cdd:cd16015 176 ----------------EKKDEPLKVEEDKTELENYLNAIHY----------TDKALGEFIEKLKKSGLYENTIIVIYGDH 229
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1110313252 342 GYFLGEHgWFDKRLIFEESIHMPFVIRYPKEVrAGARNKDLIENADFSALFADYAG 397
Cdd:cd16015 230 LPSLGSD-YDETDEDPLDLYRTPLLIYSPGLK-KPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
38-387 |
3.10e-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: 60.51 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 38 PNILFIMADDHTSQAWGIYGGILEDyvhTPNIKRLAAEGTVLE-NC--LVSNSicTPSRATILTGQYSHVNGVTTLG--- 111
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPT---TPNLKRLASEGATFNfRSvsPPTSS--APNHAALLTGAYPTLHGYTGNGsad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 112 -------AGLSPEHNNIAKELQKGGYQTSVIGkwhlkqepagfdyycvlpgqgeywnprlktkenwedyygggktyegfs 184
Cdd:cd00016 76 pelpsraAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 185 tdiiADKTIEWIenrDKSKPFMAMCHFKATHEPFDYPKRFSHLYRDVdipvpdsfydkgpettgrsfvgqsvdnlkkryl 264
Cdd:cd00016 108 ----LLKAIDET---SKEKPFVLFLHFDGPDGPGHAYGPNTPEYYDA--------------------------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 265 aatadpslrkdfmnypelpfsvdgltddearyktyqkyVKDFmrcgaaaDDNIGKLLDYLDAAGLAENTIVIYTADQGYF 344
Cdd:cd00016 148 --------------------------------------VEEI-------DERIGKVLDALKKAGDADDTVIIVTADHGGI 182
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1110313252 345 LGEHGWFDKRLI----FEESIHMPFVIRYPKeVRAGARNKDLIENAD 387
Cdd:cd00016 183 DKGHGGDPKADGkadkSHTGMRVPFIAYGPG-VKKGGVKHELISQYD 228
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
37-370 |
4.71e-10 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 62.23 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 37 RPNILFIMADdhtsqawGIYGGILEDYVhTPNIKRLAAEGTVLENCLvSNSICTpsRATI------LTGQYSHvnGVttL 110
Cdd:COG3083 244 PPNILLIVVD-------SLRADMLDPEV-MPNLYAFAQRSLRFTNHY-SSGNST--RAGLfglfygLPGNYWD--SI--L 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 111 GAGLSPEhnnIAKELQKGGYQTSVIGKWHLKQEPagFDyycvlpgQ---GEYWNPRLKTKENWEDyygggktyegfSTDI 187
Cdd:COG3083 309 AERTPPV---LIDALQQQGYQFGLFSSAGFNSPL--FR-------QtifSDVSLPRLHTPGGPAQ-----------RDRQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 188 IADKTIEWIENRDKSKPFMAMCHFKATHEpFDYPKRFSHLYrdvdipvpdsfydkgpettgrsfvgqsvdnlkkrylaat 267
Cdd:COG3083 366 ITAQWLQWLDQRDSDRPWFSYLFLDAPHA-YSFPADYPKPF--------------------------------------- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 268 aDPSLRkdfMNYPELPFSVDGlTDDEARYKTYQKYVkdfmrcgaaaDDNIGKLLDYLDAAGLAENTIVIYTADQGYFLGE 347
Cdd:COG3083 406 -QPSED---CNYLALDNESDP-TPFKNRYRNAVHYV----------DSQIGRVLDTLEQRGLLENTIVIITADHGEEFNE 470
|
330 340 350
....*....|....*....|....*....|.
gi 1110313252 348 HG---W-----FDkrlifEESIHMPFVIRYP 370
Cdd:COG3083 471 NGqnyWghnsnFS-----RYQLQVPLVIHWP 496
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
60-422 |
6.35e-05 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 45.10 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 60 LEDYVHTPNIKRLAAEGTVLENCL-VSNSICTPSRATILTGQYSHVNGVTtlgaglspeHNNIakelqkggyqtsvigkw 138
Cdd:pfam01663 14 LDRFELTPNLAALAKEGVSAPNLTpVFPTLTFPNHYTLVTGLYPGSHGIV---------GNTF----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 139 hlkqepagFDyycvlPGQGEYWNPRLKTKENWeDYYGGGKTyegfstdiiadktieWIENRDKSkpFMAMCHF-----KA 213
Cdd:pfam01663 68 --------YD-----PKTGEYLVFVISDPEDP-RWWQGEPI---------------WDTAAKAG--VRAAALFwpgseVD 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 214 THEPFDYPKRFSHLYRDVDIPVPDSFYDKgpettgrsfvgqsvdnLKKRYLA-ATADPSLRK-DFM--NYPElpfsVDGL 289
Cdd:pfam01663 117 YSTYYGTPPRYLKDDYNNSVPFEDRVDTA----------------VLQTWLDlPFADVAAERpDLLlvYLEE----PDYA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 290 -----TDDEARYKTYQKyvkdfmrcgaaADDNIGKLLDYLDAAGLAENTIVIYTADQGY-FLGEHGWFDKRLIFEESIHM 363
Cdd:pfam01663 177 ghrygPDSPEVEDALRR-----------VDRAIGDLLEALDERGLFEDTNVIVVSDHGMtPVSDDKVIFLNDYLREKGLL 245
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1110313252 364 ------PFVIRYPKEVRAGARNKDLIEnADFSALFADYAGIDYPEtmqGRSFRENLKGNTPDDWR 422
Cdd:pfam01663 246 hlvdggPVVAIYPKARELGHVPPGEVE-EVYAELKEKLLGLRIQD---GEHLAVYLKEEIPGRLH 306
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
60-351 |
3.52e-04 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 42.57 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 60 LEDYVHTPNIKRLAAEGTV---LENCLVSNSIctPSRATILTGQYSHVNGVTtlgaglspeHN-----NIAKELQKGGYQ 131
Cdd:cd16018 16 LDRAGLTPNLKRLAEEGVRakyVKPVFPTLTF--PNHYSIVTGLYPESHGIV---------GNyfydpKTNEEFSDSDWV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 132 TSvigKWHLKQEP-------AGFDYYCVL-PG-----QGeYWNPRLKTKENWEDYYGGgktyegFSTDIIADKTIEWIEN 198
Cdd:cd16018 85 WD---PWWIGGEPiwvtaekAGLKTASYFwPGsevaiIG-YNPTPIPLGGYWQPYNDS------FPFEERVDTILEWLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313252 199 RDkskPFMAMCHFkatHEPfDYpkrFSHLYrdvdipvpdsfydkGPETtgrsfvgqsvdnlkkrylaatadpslrkdfmn 278
Cdd:cd16018 155 ER---PDLILLYF---EEP-DS---AGHKY--------------GPDS-------------------------------- 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110313252 279 yPElpfsvdgltddearyktyqkyVKDFMRcgaAADDNIGKLLDYLDAAGLAENTIVIYTADQGYF-LGEHGWF 351
Cdd:cd16018 179 -PE---------------------VNEALK---RVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHGYD 227
|
|
| |
