|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
1-411 |
1.24e-140 |
|
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: 408.50 E-value: 1.24e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 1 MSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLPDKQSTEEAIRLLE 80
Cdd:cd16030 97 AGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 81 KMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPE 160
Cdd:cd16030 175 KLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 161 DFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPl 240
Cdd:cd16030 254 EQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTKP- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 241 paagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvelCREGQNLQKHLQlhdleeE 320
Cdd:cd16030 333 -----------------------GKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKSLVPLLK------N 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 321 PDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikVMGYSIRTVDYRYTVWVgfdpseflaNFSDIHAGELYFVDSDPL 400
Cdd:cd16030 373 PSAKWKDA---AFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPN 424
|
410
....*....|.
gi 2202692977 401 QDHNVYNDSQH 411
Cdd:cd16030 425 EWKNLANDPEY 435
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
72-408 |
5.83e-50 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 173.53 E-value: 5.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdphvpdslpPVAYNPWmdireredvqalni 151
Cdd:COG3119 134 TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL-----------PPNLAPR-------------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 152 svpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHG-EWAKYSNFDVATRVPLM 230
Cdd:COG3119 189 -----DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGlRGGKGTLYEGGIRVPLI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 231 LYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrEGQNLQK 310
Cdd:COG3119 264 VRWPGKIKA------------------------GSVSDALVSLIDLLPTLLDLAGVPIPEDL-----------DGRSLLP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 311 HLQlhdlEEEPDlfgnPRELIaYSQYPRPAdfpqwnsdkpslndikvMGYSIRTVDYRYTVWVGFDPSEflanfsdihag 390
Cdd:COG3119 309 LLT----GEKAE----WRDYL-YWEYPRGG-----------------GNRAIRTGRWKLIRYYDDDGPW----------- 351
|
330
....*....|....*...
gi 2202692977 391 ELYFVDSDPLQDHNVYND 408
Cdd:COG3119 352 ELYDLKNDPGETNNLAAD 369
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-419 |
2.01e-38 |
|
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: 143.13 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 7 FHPGISSNHSDDYPYSWSFPPYHPSsekYENTKTCKGQD----GKLHA-NLLCPVD---VADVPEGTLPDKQSTEEAIRL 78
Cdd:cd16033 63 HEHGVLNNVENAGAYSRGLPPGVET---FSEDLREAGYRngyvGKWHVgPEETPLDygfDEYLPVETTIEYFLADRAIEM 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 79 LEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPHVPDSLPPVAYNpwmDIREREDVQALNisvpygpi 158
Cdd:cd16033 140 LEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYR---RERKRWGVDTED-------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 159 pEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSNFDVATRVPLMLYVPGRT 237
Cdd:cd16033 209 -EEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKgPFMYEETYRIPLIIKWPGVI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 238 APlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrEGQNLQKHLqlhdL 317
Cdd:cd16033 288 AA------------------------GQVVDEFVSLLDLAPTILDLAGVDVPPKV-----------DGRSLLPLL----R 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 318 EEEPDlfgNPRELIaysqyprpadFPQWNSdkpslNDIKVMGYSIRTVDYRYtVWVGFDpseflanfsdihAGELYFVDS 397
Cdd:cd16033 329 GEQPE---DWRDEV----------VTEYNG-----HEFYLPQRMVRTDRYKY-VFNGFD------------IDELYDLES 377
|
410 420
....*....|....*....|..
gi 2202692977 398 DPLQDHNVYNDSQHGGLLHSLR 419
Cdd:cd16033 378 DPYELNNLIDDPEYEEILREMR 399
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
72-328 |
7.29e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 135.38 E-value: 7.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPdsLPPVAyNPWMDIRereDVQALni 151
Cdd:cd16155 108 ADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL-PENFLP--QHPFD-NGEGTVR---DEQLA-- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 152 svPYGPIPEDFQRKIRQsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLML 231
Cdd:cd16155 179 --PFPRTPEAVRQHLAE-YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNLYEHSMRVPLII 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 232 YVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIPSF-----------HVE 300
Cdd:cd16155 256 SGPG-------------------------IPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLlpvirgekkavRDT 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2202692977 301 LCREGQNLQ-----------------KHLQLHDLEEEP----DLFGNPR 328
Cdd:cd16155 311 LYGAYRDGQrairddrwkliiyvpgvKRTQLFDLKKDPdelnNLADEPE 359
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-399 |
1.30e-34 |
|
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: 130.74 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 46 GKLHANllcpvdVADVPEGTLPDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphv 125
Cdd:cd16037 96 GKLHFR------GEDQRHGFRYDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 126 pdslppvaynpwmdireredvqalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDH 205
Cdd:cd16037 157 -------------------------------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 206 GWALGEHGEWAKYSNFDVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAG 285
Cdd:cd16037 200 GDMLGERGLWGKSTMYEESVRVPMIISGPGIP-------------------------AGKRVKTPVSLVDLAPTILEAAG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 286 LPVPPRCPipsfhvelcreGQNLQkhlqlhDLEEEPDlfgnPRELIAYSQYprpadfpqwnsdkpSLNDIKVMGYSIRTV 365
Cdd:cd16037 255 APPPPDLD-----------GRSLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKG 299
|
330 340 350
....*....|....*....|....*....|....
gi 2202692977 366 DYRYTVWVGFDPseflanfsdihagELYFVDSDP 399
Cdd:cd16037 300 RWKYIYYVGYPP-------------QLFDLENDP 320
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
72-419 |
2.11e-33 |
|
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: 129.57 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENI----TLAPDPHvpDSLPPVAYNPWMDIREREDVQ 147
Cdd:cd16031 149 TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIpepeTFDDDDY--AGRPEWAREQRNRIRGVLDGR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 148 ALNisvpygpiPEDFQRKIRQsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGeWA-KYSNFDVATR 226
Cdd:cd16031 226 FDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFdKRLMYEESIR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 227 VPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrEGQ 306
Cdd:cd16031 296 VPLIIRDPRLIKA------------------------GTVVDALVLNIDFAPTILDLAGVPIPEDM-----------QGR 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 307 NLQKHLQLHDLEEEPDLFgnpreLIAYSQYPRPADFPQWnsdkpslndikvmgYSIRTVDYRYTVWVGFDPSEflanfsd 386
Cdd:cd16031 341 SLLPLLEGEKPVDWRKEF-----YYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYYGVWDEE------- 394
|
330 340 350
....*....|....*....|....*....|...
gi 2202692977 387 ihagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 419
Cdd:cd16031 395 ----ELYDLKKDPLELNNLANDPEYAEVLKELR 423
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
60-290 |
6.61e-33 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 129.40 E-value: 6.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 60 DVPEGTLPDKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPHVPDslppvaynpWmD 139
Cdd:PRK13759 174 DLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD---------W-E 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 140 IREREDVQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYS 219
Cdd:PRK13759 240 YAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGY 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2202692977 220 NFDVATRVPLMLYVPGRTAPLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 290
Cdd:PRK13759 320 PYEGSAHIPFIIYDPGGLLAGN---------------------RGTVIDQVVELRDIMPTLLDLAGGTIPD 369
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
57-404 |
4.63e-32 |
|
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: 125.37 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 57 DVADVPEGTLPDKQsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDphvpdslppvayn 135
Cdd:cd16034 146 GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN------------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 136 pwmdireredvqalnisVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW 215
Cdd:cd16034 212 -----------------VPEDKKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 216 AKYSNFDVATRVPLMLYVPGRtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPPrcpip 295
Cdd:cd16034 275 NKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPIPD----- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 296 sfhvelCREGQNLQKHLqlhdLEEEPDLFGNpreliAYSQYPRPadFPQWNSDKPSLNDIkvmgysIRTVDYRYTVWVGf 375
Cdd:cd16034 326 ------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVP--FGGGSARDGGEWRG------VRTDRYTYVRDKN- 381
|
330 340 350
....*....|....*....|....*....|.
gi 2202692977 376 dpseflanfsdihaGELYFVD--SDPLQDHN 404
Cdd:cd16034 382 --------------GPWLLFDneKDPYQLNN 398
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
88-293 |
3.94e-30 |
|
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: 118.84 E-value: 3.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 88 PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredvqalnisvpygpipedfQRKIR 167
Cdd:cd16032 134 PFFLTVSFTHPHDPYVIPQEYWDLY--------------------------------------------------VRRAR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 168 QSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPlpaagqkl 247
Cdd:cd16032 164 RAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSARVPLIISAPGRFAP-------- 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2202692977 248 fpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAGLPVPPRCP 293
Cdd:cd16032 236 -----------------RRVAEPVSLVDLLPTLVDLAGGGTAPHVP 264
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
88-419 |
2.11e-29 |
|
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: 117.61 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 88 PFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapDPHVPDsLPPVaynpwmdireREDVQAlnisvpygpipedfqrkir 167
Cdd:cd16027 143 PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKV--PPYLPD-TPEV----------REDLAD------------------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 168 qsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGehgeWAKYSNFDVATRVPLMLYVPGRTAPlpaagqkl 247
Cdd:cd16027 191 --YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGLRVPLIVRWPGKIKP-------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 248 fpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvELcrEGQNLqkhlqLHDLEEEPDlfgNP 327
Cdd:cd16027 257 ----------------GSVSDALVSFIDLAPTLLDLAGIEPPE---------YL--QGRSF-----LPLLKGEKD---PG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 328 RELIaYSQYPRpadfpqwnsdkpslNDIKVMGY-SIRTVDYRYTVwvgfdpseflaNFSDIhagELYFVDSDPLQDHNVY 406
Cdd:cd16027 302 RDYV-FAERDR--------------HDETYDPIrSVRTGRYKYIR-----------NYMPE---ELYDLKNDPDELNNLA 352
|
330
....*....|...
gi 2202692977 407 NDSQHGGLLHSLR 419
Cdd:cd16027 353 DDPEYAEVLEELR 365
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-419 |
5.59e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 117.34 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 88 PFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPdPHVPDSLPPVAYNPWMDIREREDVQALNisvpygpipEDFQRKIR 167
Cdd:cd16150 133 PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLRAKGKPSMLEGIEKQGLDRWS---------EERWRELR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 168 QSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN-F-DVATRVPLMLYVPGRTaplpaagq 245
Cdd:cd16150 200 ATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCLTRVPLIIKPPGGP-------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 246 klfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPrcpiPSFHVELCRegqnlqkhlQLHDLEEEPD--- 322
Cdd:cd16150 272 -----------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THFGRSLLP---------VLAGETEEHRdav 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 323 ------LFGNPReliAYSQYPRPADFPQWNS---DKPSLNDIKVMgysIRTVDYRYtVWVGFDPSeflanfsdihagELY 393
Cdd:cd16150 322 fseggrLHGEEQ---AMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VYRLYEPD------------ELY 382
|
330 340
....*....|....*....|....*.
gi 2202692977 394 FVDSDPLQDHNVYNDSQHGGLLHSLR 419
Cdd:cd16150 383 DLEADPLELHNLIGDPAYAEIIAEMK 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
73-289 |
1.51e-26 |
|
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: 106.37 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 73 EEAIRLLEKMKTSAsPFFLAVGYHKPHIPFRYpkefqklyplenitlapdphvpdslppvaynpwmdireredvqalnis 152
Cdd:cd16022 103 DEAIDFIERRDKDK-PFFLYVSFNAPHPPFAY------------------------------------------------ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 153 vpygpipedfqrkirqsyFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE-WAKYSNFDVATRVPLML 231
Cdd:cd16022 134 ------------------YAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGIRVPFIV 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2202692977 232 YVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVP 289
Cdd:cd16022 196 RWPGKIP------------------------AGQVSDALVSLLDLLPTLLDLAGIEPP 229
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
72-377 |
3.90e-24 |
|
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: 103.88 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDPHVPDSLPPVaYNPWMDIREREDVQA 148
Cdd:cd16028 144 TDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQHPL-LAAFLERIESLSFSP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 149 LNIsvPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVP 228
Cdd:cd16028 221 GAA--NAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 229 LMLYVPGRTAplpaagqklfpyrdpfDPASdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrEGQNL 308
Cdd:cd16028 299 LIVRDPRREA----------------DATR-----GQVVDAFTESVDVMPTILDWLGGEIPHQC-----------DGRSL 346
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2202692977 309 QKHLQlhdlEEEPdlfGNPRELIAYSQYPRPADFPQW------NSDKPSLNdikvmgySIRTVDYRYTVWVGFDP 377
Cdd:cd16028 347 LPLLA----GAQP---SDWRDAVHYEYDFRDVSTRRPqealglSPDECSLA-------VIRDERWKYVHFAALPP 407
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
170-291 |
2.81e-21 |
|
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: 92.61 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 170 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSNF-DVATRVPLMLYVPGRTaplpaagqkl 247
Cdd:cd16148 165 YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSNLyDEQLHVPLIIRWPGKE---------- 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2202692977 248 fpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 291
Cdd:cd16148 235 ---------------PGKRVDALVSHIDIAPTLLDLLGVEPPDY 263
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
8-288 |
2.89e-20 |
|
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: 90.13 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 8 HPGISSNHSDDYPYSWSFPPYHPSSEKYENTKTCKGQD----GKLHANllCPVDVADVPEgtlpdkQSTEEAIRLLEKMK 83
Cdd:cd16153 68 LTGRYPHRTGVYGFEAAHPALDHGLPTFPEVLKKAGYQtasfGKSHLE--AFQRYLKNAN------QSYKSFWGKIAKGA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 84 TSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdphvpdslppvaynpwmdiREREDvqalnisvpygpipedfq 163
Cdd:cd16153 140 DSDKPFFVRLSFLQPHTPVLPPKEF--------------------------------RDRFD------------------ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 164 rkirqsYFASVSYLDTQVGHVLSALDDLRLAH---NTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRtapl 240
Cdd:cd16153 170 ------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGILAKFTFWPQSHRVPLIVVSSDK---- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2202692977 241 paagqKLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 288
Cdd:cd16153 240 -----LKAP-------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
72-408 |
5.14e-20 |
|
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: 91.07 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpdslppvaynpwmDIREREDVQAlni 151
Cdd:cd16146 160 FDEAIDFIEENKDK--PFFAYLATNAPHGPLQVPDKYLDPYK-------------------------DMGLDDKLAA--- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 152 svpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW------AKYSNFDVAT 225
Cdd:cd16146 210 ------------------FYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFnagmrgKKGSVYEGGH 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 226 RVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIpsfhvelcrEG 305
Cdd:cd16146 272 RVPFFIRWPGKILA------------------------GKDVDTLTAHIDLLPTLLDLCGVKLPEGIKL---------DG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 306 QNLQKHLQlHDLEEEPDlfgnpRELIAYSQYPRPADFPQWNSdkpslndikvmgySIRTVDYRYtVWVGFDPSeflanfs 385
Cdd:cd16146 319 RSLLPLLK-GESDPWPE-----RTLFTHSGRWPPPPKKKRNA-------------AVRTGRWRL-VSPKGFQP------- 371
|
330 340
....*....|....*....|...
gi 2202692977 386 dihagELYFVDSDPLQDHNVYND 408
Cdd:cd16146 372 -----ELYDIENDPGEENDVADE 389
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
72-290 |
7.15e-19 |
|
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: 87.61 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAPDPHVPDslPPVAYNP-WmdIREREDVQALN 150
Cdd:cd16147 160 ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPRPPPNN--PDVSDKPhW--LRRLPPLNPTQ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 151 ISVpygpIPEDFQRKIR--QSyfasvsyLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHG-EWAKYSNFDVATRV 227
Cdd:cd16147 234 IAY----IDELYRKRLRtlQS-------VDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRlPPGKRTPYEEDIRV 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2202692977 228 PLMLYVPGrtapLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 290
Cdd:cd16147 303 PLLVRGPG----IP---------------------AGVTVDQLVSNIDLAPTILDLAGAPPPS 340
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
170-297 |
7.29e-19 |
|
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: 85.75 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 170 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK------YSNFDVATRVPLMLYVPGRTAPlpaa 243
Cdd:cd16149 144 YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngtfpLNMYDNSVKVPFIIRWPGVVPA---- 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2202692977 244 gqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVP--PRCPIPSF 297
Cdd:cd16149 220 --------------------GRVVDSLVSAYDFFPTLLELAGVDPPadPRLPGRSF 255
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
68-291 |
2.43e-17 |
|
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: 82.26 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 68 DKQSTEEAIRLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdphvpdslppvaynpwmdirere 144
Cdd:cd16035 116 DPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH--------------------------------------------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 145 DVQalnisvpYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN-FDV 223
Cdd:cd16035 151 DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNaYEE 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2202692977 224 ATRVPLMLYVPGrtaplpaagqkLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 291
Cdd:cd16035 224 ALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGVDAEAR 267
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
72-290 |
5.97e-17 |
|
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: 82.43 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplENITLAPDPHVPDSLP--PVAYNPWMDIREREDVQAL 149
Cdd:cd16156 161 TNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLHQRLWAGAKPHEDGDKG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 150 NISVPYgpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLrlAHNTIIAFTSDHGWALGEHGEWAK-YSNFDVATRVP 228
Cdd:cd16156 237 TIKHPL--------------YFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHKLWAKgPAVYDEITNIP 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2202692977 229 LMLYVPGRtapLPAAGQKLFPyrdpfdpasdwmdagrhtedlVELVSLFPTLAGLAGLPVPP 290
Cdd:cd16156 301 LIIRGKGG---EKAGTVTDTP---------------------VSHIDLAPTILDYAGIPQPK 338
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
55-290 |
1.83e-16 |
|
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: 80.67 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 55 PVDVADVPEGTLPDKQSTEEAIRLLEKmkTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslppvay 134
Cdd:cd16144 154 NPDLEDGPEGEYLTDRLTDEAIDFIEQ--NKDKPFFLYLSHYAVHTPIQARPELIEKY---------------------- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 135 npwmdireredvqalnisvpYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALGEHGE 214
Cdd:cd16144 210 --------------------EKKKKGLRKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNG-GLSTRGG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 215 WA---------KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAG 285
Cdd:cd16144 269 PPtsnaplrggKGSLYEGGIRVPLIVRWPGVIKP------------------------GSVSDVPVIGTDLYPTFLELAG 324
|
....*
gi 2202692977 286 LPVPP 290
Cdd:cd16144 325 GPLPP 329
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
68-286 |
4.93e-16 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 68 DKQSTEEAIRLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpdslppvaynpwmdireredvq 147
Cdd:pfam00884 144 DEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA---------------------------------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 148 alnISVPYGpipeDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA--- 224
Cdd:pfam00884 187 ---TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApeg 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2202692977 225 -TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 286
Cdd:pfam00884 260 gYRVPLLIWSPGGKAK------------------------GQKSEALVSHVDLFPTILDLAGI 298
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
72-294 |
4.97e-16 |
|
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: 79.14 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSasPFFLAVGYHKPHIPfrypkefqkLYPlenitlapdphvpdslppvaynpwmdireredvqalni 151
Cdd:cd16026 170 TDEAVDFIERNKDQ--PFFLYLAHTMPHVP---------LFA-------------------------------------- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 152 svpygpiPEDFQ-RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW--------AKYSNFD 222
Cdd:cd16026 201 -------SEKFKgRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGgsagplrgGKGTTWE 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2202692977 223 VATRVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPI 294
Cdd:cd16026 274 GGVRVPFIAWWPGVIP------------------------AGTVSDELASTMDLLPTLAALAGAPLPEDRVI 321
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
72-419 |
5.34e-16 |
|
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: 78.81 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYPlenitlapDPHVPdslppvaynpwmdirerEDV 146
Cdd:cd16152 110 TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERFA--------NFWVP-----------------PDL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 147 QALnisvpygpiPEDFQRKIrQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHgwalGEH-----GEWaKYSNF 221
Cdd:cd16152 164 AAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY-KRSCH 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 222 DVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPprcpiPSFHvel 301
Cdd:cd16152 229 ESSIRVPLVIYGPG-------------------------FNGGGRVEELVSLIDLPPTLLDAAGIDVP-----EEMQ--- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 302 creGQNLQKhlqlhDLEEEPDlfgnPRELIAYSQyprpadfpqwnsdkpsLNDIKVmGYSIRTVDYRYTVwVGFDPSEFL 381
Cdd:cd16152 276 ---GRSLLP-----LVDGKVE----DWRNEVFIQ----------------ISESQV-GRAIRTDRWKYSV-AAPDKDGWK 325
|
330 340 350
....*....|....*....|....*....|....*....
gi 2202692977 382 ANFSDIHAGE-LYFVDSDPLQDHNVYNDSQHGGLLHSLR 419
Cdd:cd16152 326 DSGSDVYVEDyLYDLEADPYELVNLIGRPEYREVAAELR 364
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
72-291 |
1.34e-15 |
|
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: 78.02 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDPHVPDSLPPVAYNPWmdireredvqalni 151
Cdd:cd16145 175 TDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYKYKPKDPGIYAYLPW-------------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 152 svpygpipedfqRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALGEHGEWAKYSNFDVA------- 224
Cdd:cd16145 227 ------------PQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG-PHSEGGSEHDPDFFDSNgplrgyk 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2202692977 225 -------TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPR 291
Cdd:cd16145 294 rslyeggIRVPFIARWPGKIPA------------------------GSVSDHPSAFWDFMPTLADLAGAEPPED 343
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
149-290 |
1.37e-15 |
|
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: 77.58 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 149 LNISVPYgPIP---EDFQ--RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDV 223
Cdd:cd16171 173 LNLPHPY-PSPsmgENFGsiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEG 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2202692977 224 ATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPP 290
Cdd:cd16171 252 SSHVPLLIMGPG-------------------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
152-404 |
4.01e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 76.48 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 152 SVPYGPIPEDFQRkiRQSYF-ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW-------AKYSNFDV 223
Cdd:cd16151 190 SPDWDPDDKRKKD--DPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTngrevrgGKGKTTDA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 224 ATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIpsfhvelcr 303
Cdd:cd16151 268 GTHVPLIVNWPGLI------------------------PAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL--------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 304 EGQNLQkhlqlhdleeePDLFGNP----RELIAYsqYPRpadfPQWNSDKPslndikvmgYSIRTVDYRYtvwvgfdpse 379
Cdd:cd16151 315 DGRSFA-----------PQLLGKTgsprREWIYW--YYR----NPHKKFGS---------RFVRTKRYKL---------- 358
|
250 260
....*....|....*....|....*
gi 2202692977 380 flanFSDihaGELYFVDSDPLQDHN 404
Cdd:cd16151 359 ----YAD---GRFFDLREDPLEKNP 376
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
72-294 |
6.76e-13 |
|
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: 69.50 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlAPDPHVPDslppvaynpwmdireredvqalni 151
Cdd:cd16029 168 TDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE------DKFAHIKD------------------------ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 152 svpygpipedfqrKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALGEHGEWA--------KYSNFDV 223
Cdd:cd16029 217 -------------EDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG-GPTGGGDGGsnyplrggKNTLWEG 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2202692977 224 ATRVPLMLYVPGRTaplPAAGQKlfpYRDPFDpASDWmdagrhtedlvelvslFPTLAGLAGLPVPPRCPI 294
Cdd:cd16029 283 GVRVPAFVWSPLLP---PKRGTV---SDGLMH-VTDW----------------LPTLLSLAGGDPDDLPPL 330
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
68-238 |
1.07e-12 |
|
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: 69.55 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 68 DKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIpFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredvQ 147
Cdd:COG3083 363 DRQITAQWLQWLDQ-RDSDRPWFSYLFLDAPHA-YSFPADYPKPF----------------------------------Q 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 148 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE--WAKYSNF-DVA 224
Cdd:COG3083 407 PSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFsRYQ 486
|
170
....*....|....
gi 2202692977 225 TRVPLMLYVPGRTA 238
Cdd:COG3083 487 LQVPLVIHWPGTPP 500
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
68-290 |
1.95e-12 |
|
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: 67.94 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 68 DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpdslppvAYNPWMDireredvq 147
Cdd:cd16142 132 DEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS-------------------GKGKYAD-------- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 148 alnisvpygpipedfqrkirqsyfaSVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG-----WALGEHGEW--AKYSN 220
Cdd:cd16142 185 -------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFrgEKGTT 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 221 FDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPP 290
Cdd:cd16142 240 WEGGVRVPAIVRWPGKIKP------------------------GRVSNEIVSHLDWFPTLAALAGAPDPK 285
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
72-289 |
2.72e-12 |
|
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: 68.00 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapdphvpdslppvaynpwmdireredVQALNi 151
Cdd:cd16143 158 TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQG-----------------------------------KSGAG- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 152 svPYGpipeDFqrkIRQsyfasvsyLDTQVGHVLSALDDLRLAHNTIIAFTSDHG-------WALGEHGEWA-------K 217
Cdd:cd16143 202 --PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyKELEKFGHDPsgplrgmK 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2202692977 218 YSNFDVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSLFPTLAGLAGLPVP 289
Cdd:cd16143 265 ADIYEGGHRVPFIVRWPGKI------------------------PAGSVSDQLVSLTDLFATLAAIVGQKLP 312
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
167-284 |
1.44e-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: 60.90 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 167 RQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYS----NFDVATRVPLMLYVPGrtaplpa 242
Cdd:cd00016 141 TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgkadKSHTGMRVPFIAYGPG------- 213
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2202692977 243 agqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLA 284
Cdd:cd00016 214 ------------------VKKGGVKHELISQYDIAPTLADLL 237
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
72-289 |
3.04e-10 |
|
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: 61.69 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LYPlENITLAPDPH-V 125
Cdd:cd16025 122 TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLIP-ADTKLTPRPPgV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 126 P--DSLPPvaynpwmdirEREDVQALNISVpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTS 203
Cdd:cd16025 201 PawDSLSP----------EEKKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 204 DHGwALGEHGeWAKYSNfdvaTrvPLMLYvpgrtaplpaagqKLFPY----RDPF--DPASDWMDAGRHTEDLVELVSLF 277
Cdd:cd16025 255 DNG-ASAEPG-WANASN----T--PFRLY-------------KQASHeggiRTPLivSWPKGIKAKGGIRHQFAHVIDIA 313
|
250
....*....|..
gi 2202692977 278 PTLAGLAGLPVP 289
Cdd:cd16025 314 PTILELAGVEYP 325
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
170-289 |
8.47e-10 |
|
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: 60.38 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 170 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL------GEHGEW-------AKYSNFDVATRVPLMLYVPGR 236
Cdd:cd16159 281 YGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGV 360
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2202692977 237 TAPlpaaGQKLfpyrdpfDPASDWMDagrhtedlvelvsLFPTLAGLAGLPVP 289
Cdd:cd16159 361 IPP----GSVI-------DEPTSLMD-------------IFPTVAALAGAPLP 389
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
154-290 |
1.08e-08 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 56.97 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 154 PYgPIPEDFQR------KIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwalGEHGEWAKYSNFDVATRV 227
Cdd:COG1368 398 PY-TLPEEDKKipdygkTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG---PRSPGKTDYENPLERYRV 473
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2202692977 228 PLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPP 290
Cdd:COG1368 474 PLLIYSPG-------------------------LKKPKVIDTVGSQIDIAPTLLDLLGIDYPS 511
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
66-285 |
1.13e-07 |
|
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: 53.07 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 66 LPDKQSTEEAIRLLEKMKtsASPFFLAVgyhkphipfrypkefqklyplenITLapDPHVPDSLPPVAYNPwmdirered 145
Cdd:cd16015 137 VSDESLFDQALEELEELK--KKPFFIFL-----------------------VTM--SNHGPYDLPEEKKDE--------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 146 vqalnisvpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDvAT 225
Cdd:cd16015 181 -----------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLD-LY 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 226 RVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAG 285
Cdd:cd16015 249 RTPLLIYSPGLKKP-------------------------KKIDRVGSQIDIAPTLLDLLG 283
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
166-290 |
1.45e-07 |
|
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: 53.24 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 166 IRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG-WALGE-------HGEW--------AKYSNFDVATRVPL 229
Cdd:cd16161 181 GRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKCelavgpgTGDWqgnlggsvAKASTWEGGHREPA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2202692977 230 MLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 290
Cdd:cd16161 261 IVYWPGRIP------------------------ANSTSAALVSTLDIFPTVVALAGASLPP 297
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
167-289 |
4.15e-07 |
|
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: 52.08 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 167 RQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL-------GEHGEW--AKYSNFDVATRVPLMLYVPGRT 237
Cdd:cd16157 223 RGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGHI 302
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2202692977 238 APlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVP 289
Cdd:cd16157 303 KP------------------------GQVSHQLGSLMDLFTTSLALAGLPIP 330
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
160-285 |
1.38e-06 |
|
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: 50.12 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 160 EDFQRK-IRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL---GEHGEWA-----KYSNFDVATRVPLM 230
Cdd:cd16160 213 KRFKGKsKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFI 292
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2202692977 231 LYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAG 285
Cdd:cd16160 293 AYWPGTIKP-------------------------RVSHEVVSTMDIFPTFVDLAG 322
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
164-289 |
6.69e-06 |
|
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: 48.21 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 164 RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL------GEHG--EWAKYSNFDVATRVPLMLYVPG 235
Cdd:cd16158 222 RSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPG 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2202692977 236 RTAPlpaagqklfpyrdpfdpasdwmdaGRhTEDLVELVSLFPTLAGLAGLPVP 289
Cdd:cd16158 302 RIKP------------------------GV-THELASTLDILPTIAKLAGAPLP 330
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
99-286 |
2.22e-04 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 42.61 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 99 HIPF--RYPKEFQKLYPlenitlapdphvpdslppvaynpwmdireredvqalnisVPYGPIPEDFQRKIRQSYFASVSY 176
Cdd:cd16017 154 HGPYydRYPEEFAKFTP---------------------------------------DCDNELQSCSKEELINAYDNSILY 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202692977 177 LDTQVGHVLSALDdlRLAHNTIIAFTSDHGWALGEHGEW--AKYSNFDVATRVPLMLYVPGRTAPLPAAGQKLFPYRDPF 254
Cdd:cd16017 195 TDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENGLYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPF 272
|
170 180 190
....*....|....*....|....*....|..
gi 2202692977 255 DpaSDWmdagrhtedlvelvsLFPTLAGLAGL 286
Cdd:cd16017 273 S--HDN---------------LFHTLLGLLGI 287
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
172-235 |
2.45e-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: 2.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2202692977 172 ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA-LGEHGewakYSNFDVATRVPLMLYVPG 235
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
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