|
Name |
Accession |
Description |
Interval |
E-value |
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
33-436 |
1.62e-170 |
|
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: 484.70 E-value: 1.62e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDfGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQA---LPSD 109
Cdd:cd16027 1 PNILWIIADDLSPDL-GGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRgfpLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 110 QVMFPKELRKAGYYTAATGKWHLGRAARSAFDRIEDCRPGGE-------EKWVGFIQERPKDKPFMMWFASHDAHRDWDP 182
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGrnawdyaSNAADFLNRAKKGQPFFLWFGFHDPHRPYPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 183 SSASPPHV-PADAVIPPYMVDTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGRPFPRCKTWLYD 261
Cdd:cd16027 160 GDGEEPGYdPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFPRAKGTLYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 262 SGIKPPFIVHWPHQLaKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTKSEVRDVVFAEHNWHD-TEAH 340
Cdd:cd16027 240 SGLRVPLIVRWPGKI-KPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGRDYVFAERDRHDeTYDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 341 ERMVRKGPWMYIRNARPefagwvqvhhkyasyeallegqaqgsltpaqadvllaprpaEMLFNVEKDPHQLNNLADSPEH 420
Cdd:cd16027 319 IRSVRTGRYKYIRNYMP-----------------------------------------EELYDLKNDPDELNNLADDPEY 357
|
410
....*....|....*.
gi 1395161673 421 SEPLRLMRAALDEWQE 436
Cdd:cd16027 358 AEVLEELRAALDAWMK 373
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
15-441 |
8.08e-130 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 381.92 E-value: 8.08e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 15 IMAALTVVSSVHAENPPPPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYP 94
Cdd:COG3119 6 LLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 95 HNTG----APELHQALPSDQVMFPKELRKAGYYTAATGKWHLGRAarsafDRIEDcrpggeeKWVGFIQER-PKDKPFMM 169
Cdd:COG3119 86 HRTGvtdnGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYLT-----DLLTD-------KAIDFLERQaDKDKPFFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 170 WFASHDAHRDWDPSsasPPHV----PADAVIPPYMV----DTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTL 241
Cdd:COG3119 154 YLAFNAPHAPYQAP---EEYLdkydGKDIPLPPNLAprdlTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 242 IFFLADNG-----RPFPRCKTWLYDSGIKPPFIVHWPHQLaKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPL 316
Cdd:COG3119 231 VVFTSDNGpslgeHGLRGGKGTLYEGGIRVPLIVRWPGKI-KAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 317 IKNTKSEVRDVVFAEHNWHdteAHERMVRKGPWMYIRNARPEfagwvqvhhkyasyeallegqaqgsltpaqadvllapr 396
Cdd:COG3119 310 LTGEKAEWRDYLYWEYPRG---GGNRAIRTGRWKLIRYYDDD-------------------------------------- 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1395161673 397 PAEMLFNVEKDPHQLNNLADspEHSEPLRLMRAALDEWQERTGDT 441
Cdd:COG3119 349 GPWELYDLKNDPGETNNLAA--DYPEVVAELRALLEAWLKELGDP 391
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
32-433 |
1.18e-100 |
|
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: 308.69 E-value: 1.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQAL-PSDQ 110
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLfDASQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 111 VMFPKELRKAGYYTAATGKWHLG---RAARSAFDRIE---------DCRPGGEEKWVG---------------FIQERPK 163
Cdd:cd16031 82 PTYPKLLRKAGYQTAFIGKWHLGsggDLPPPGFDYWVsfpgqgsyyDPEFIENGKRVGqkgyvtdiitdkaldFLKERDK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 164 DKPFMMwFASHDA-HRDWDPSsasPPHVP--ADAVIPP-------------------------YMVDTEGTRQD----LA 211
Cdd:cd16031 162 DKPFCL-SLSFKApHRPFTPA---PRHRGlyEDVTIPEpetfddddyagrpewareqrnrirgVLDGRFDTPEKyqryMK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 212 AYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNG-----------RpfprcktWLYDSGIKPPFIVHWPhQLAKPG 280
Cdd:cd16031 238 DYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGfflgehglfdkR-------LMYEESIRVPLIIRDP-RLIKAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 281 SACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTKSEV-RDVVFAEHNWHDTEAHERmvrkgPWMYIRNARpef 359
Cdd:cd16031 310 TVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKPVDwRKEFYYEYYEEPNFHNVP-----THEGVRTER--- 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395161673 360 agwvqvhHKYASYeallegqaqgsltPAQADvllaprpAEMLFNVEKDPHQLNNLADSPEHSEPLRLMRAALDE 433
Cdd:cd16031 382 -------YKYIYY-------------YGVWD-------EEELYDLKKDPLELNNLANDPEYAEVLKELRKRLEE 428
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
33-312 |
1.50e-89 |
|
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: 273.16 E-value: 1.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTG---APELHQALPSD 109
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGvrgNVGNGGGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 110 QVMFPKELRKAGYYTAATGKWHlGRAARsafdriedcrpggeekwvgFIQERPKDKPFMMWFASHDahrdwdpssaspPH 189
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGKWH-DEAID-------------------FIERRDKDKPFFLYVSFNA------------PH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 190 vpadaviPPYmvdtegtrqdlaAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNG-----RPFPRCKTWLYDSGI 264
Cdd:cd16022 129 -------PPF------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGdmlgdHGLRGKKGSLYEGGI 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1395161673 265 KPPFIVHWPHQLaKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTS 312
Cdd:cd16022 190 RVPFIVRWPGKI-PAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
33-434 |
1.49e-78 |
|
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: 251.31 E-value: 1.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTG-------------- 98
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGitdvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 99 ----APELHQALPSDQVMFPKELRKAGYYTAATGKWHLGRAARSA-----FD--------------------RIEDCRPG 149
Cdd:cd16144 81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGpedqgFDvniggtgnggppsyyfppgkPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 150 GEEKW---------VGFIQERpKDKPFMMWFASHDAHRdwdpssaspPHVPADAVIPPY--MVDTEGTRQDLAAYYDEVQ 218
Cdd:cd16144 161 PEGEYltdrltdeaIDFIEQN-KDKPFFLYLSHYAVHT---------PIQARPELIEKYekKKKGLRKGQKNPVYAAMIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 219 RLDRYVGLVVEELKQQGVYENTLIFFLADNG-----RPFPRC-------KTWLYDSGIKPPFIVHWPHQlAKPGSACDAL 286
Cdd:cd16144 231 SLDESVGRILDALEELGLADNTLVIFTSDNGglstrGGPPTSnaplrggKGSLYEGGIRVPLIVRWPGV-IKPGSVSDVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 287 ISSIDIAPTVLEAAGVAVPE--TVQGTSLMPLIKNTKSE-VRDVVFaehnWHdtEAHERM--------VRKGPWMYIRNa 355
Cdd:cd16144 310 VIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLLKGGEADlPRRALF----WH--FPHYHGqggrpasaIRKGDWKLIEF- 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161673 356 rpefagwvqvhhkyasYEallegqaQGSLtpaqadvllaprpaeMLFNVEKDPHQLNNLADspEHSEPLRLMRAALDEW 434
Cdd:cd16144 383 ----------------YE-------DGRV---------------ELYNLKNDIGETNNLAA--EMPEKAAELKKKLDAW 421
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-440 |
3.96e-78 |
|
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: 249.83 E-value: 3.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTG-------APELHQA 105
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGvlnnvenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 106 LPSDQVMFPKELRKAGYYTAATGKWHLGrAARSAFDRiedcrpgGEEKWV-------GFIQERPK---------DKPFMM 169
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVG-PEETPLDY-------GFDEYLpvettieYFLADRAIemleelaadDKPFFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 170 WFASHDAHrdwDPSSASPPHV----PADAVIPP-------------------YMVDT---EGTRQDLAAYYDEVQRLDRY 223
Cdd:cd16033 153 RVNFWGPH---DPYIPPEPYLdmydPEDIPLPEsfaddfedkpyiyrrerkrWGVDTedeEDWKEIIAHYWGYITLIDDA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 224 VGLVVEELKQQGVYENTLIFFLADNG-----------RPFPrcktwlYDSGIKPPFIVHWPhQLAKPGSACDALISSIDI 292
Cdd:cd16033 230 IGRILDALEELGLADDTLVIFTSDHGdalgahrlwdkGPFM------YEETYRIPLIIKWP-GVIAAGQVVDEFVSLLDL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 293 APTVLEAAGVAVPETVQGTSLMPLIKNTKSE-VRDVVFAEHNWHDTEAHERMVRKGPWMYIRNarpefagwvqvhhkyas 371
Cdd:cd16033 303 APTILDLAGVDVPPKVDGRSLLPLLRGEQPEdWRDEVVTEYNGHEFYLPQRMVRTDRYKYVFN----------------- 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161673 372 yeallegqaqgsltPAQADVllaprpaemLFNVEKDPHQLNNLADSPEHSEPLRLMRAALDEWQERTGD 440
Cdd:cd16033 366 --------------GFDIDE---------LYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETGD 411
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-431 |
1.23e-75 |
|
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: 242.08 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQ----CSPSRCSMITGRYPHNtgAPELHQ-ALP 107
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH--APEGGKaAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 108 SDQVMFPKELRKAGYYTAATGKWHLGRAarsafdriedcrpggeEKWVGFIQERPK-DKPFMMWFASHDAHrdwDPSSAS 186
Cdd:cd16155 81 SDDKTWPETFKKAGYRTFATGKWHNGFA----------------DAAIEFLEEYKDgDKPFFMYVAFTAPH---DPRQAP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 187 PP---HVPADAVIPP--YMV---------------------DTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENT 240
Cdd:cd16155 142 PEyldMYPPETIPLPenFLPqhpfdngegtvrdeqlapfprTPEAVRQHLAEYYAMITHLDAQIGRILDALEASGELDNT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 241 LIFFLADNGRPFPR----CKTWLYDSGIKPPFIVHWPhqLAKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPL 316
Cdd:cd16155 222 IIVFTSDHGLAVGShglmGKQNLYEHSMRVPLIISGP--GIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 317 IKNTKSEVRDVVF-AEHNWHdteaheRMVRKGPWMYIRnarpefagwvqvhhkyasyeallegqaqgslTPAQADVLLap 395
Cdd:cd16155 300 IRGEKKAVRDTLYgAYRDGQ------RAIRDDRWKLII-------------------------------YVPGVKRTQ-- 340
|
410 420 430
....*....|....*....|....*....|....*.
gi 1395161673 396 rpaemLFNVEKDPHQLNNLADSPEHSEPLRLMRAAL 431
Cdd:cd16155 341 -----LFDLKKDPDELNNLADEPEYQERLKKLLAEL 371
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
32-414 |
4.72e-75 |
|
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: 241.58 E-value: 4.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPnIRTPNVDALASDGLRFNNAYlATSQCSPSRCSMITGRYPHNTGA---PELHQA--- 105
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHQVGMgtmAELATGkpg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 106 ----LPSDQVMFPKELRKAGYYTAATGKWHLGRAARSAFDRIEDcrpggeeKWVGFIQE-RPKDKPFMMWFASHDAHrdw 180
Cdd:cd16025 80 yegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPDDYYSTDDLTD-------KAIEYIDEqKAPDKPFFLYLAFGAPH--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 181 dpssasPPH----------------------------------VPADAVIPPYMVDTEG------TRQDLAAYYDEV--- 217
Cdd:cd16025 150 ------APLqapkewidkykgkydagwdalreerlerqkelglIPADTKLTPRPPGVPAwdslspEEKKLEARRMEVyaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 218 --QRLDRYVGLVVEELKQQGVYENTLIFFLADNG------------RPFPRCKTWLYDSGIKPPFIVHWPHQLAKPGSAC 283
Cdd:cd16025 224 mvEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaepgwanasnTPFRLYKQASHEGGIRTPLIVSWPKGIKAKGGIR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 284 DALISSIDIAPTVLEAAGVAVPETV--------QGTSLMPLIKNTKS-EVRDVVFAEHNWHdteaheRMVRKGPWMYIRN 354
Cdd:cd16025 304 HQFAHVIDIAPTILELAGVEYPKTVngvpqlplDGVSLLPTLDGAAApSRRRTQYFELFGN------RAIRKGGWKAVAL 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395161673 355 ARP--EFAGWvqvhhkyasyeallegqaqgsltpaqadvllaprpaeMLFNVEKDPHQLNNL 414
Cdd:cd16025 378 HPPpgWGDQW-------------------------------------ELYDLAKDPSETHDL 402
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-414 |
3.43e-73 |
|
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: 236.70 E-value: 3.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQALPSDQVM 112
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPPDAPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 113 FPKELRKAGYYTAATGKWHLG----RAARSAFDRIEDCRPGGEEKWVG-------------------------------- 156
Cdd:cd16034 82 IADVLKDAGYRTGYIGKWHLDgperNDGRADDYTPPPERRHGFDYWKGyecnhdhnnphyydddgkriyikgyspdaetd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 157 ----FIQER-PKDKPFMMWFASHDAHRDWDpsSASPPHV----PADAV----IPPYMVDTEGTRQDLAAYYDEVQRLDRY 223
Cdd:cd16034 162 laieYLENQaDKDKPFALVLSWNPPHDPYT--TAPEEYLdmydPKKLLlrpnVPEDKKEEAGLREDLRGYYAMITALDDN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 224 VGLVVEELKQQGVYENTLIFFLAD-------NGRPFprcKTWLYDSGIKPPFIVHWPHQLaKPGSACDALISSIDIAPTV 296
Cdd:cd16034 240 IGRLLDALKELGLLENTIVVFTSDhgdmlgsHGLMN---KQVPYEESIRVPFIIRYPGKI-KAGRVVDLLINTVDIMPTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 297 LEAAGVAVPETVQGTSLMPLIKNTKSEVRDVVFAEhnWHDTEAHERMVRKGPWMYIRNARpefagwvqvhHKYASYEall 376
Cdd:cd16034 316 LGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSVLLQ--CFVPFGGGSARDGGEWRGVRTDR----------YTYVRDK--- 380
|
410 420 430
....*....|....*....|....*....|....*...
gi 1395161673 377 egqaqgsltpaqadvllapRPAEMLFNVEKDPHQLNNL 414
Cdd:cd16034 381 -------------------NGPWLLFDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-443 |
1.53e-72 |
|
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: 235.59 E-value: 1.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQALPSDQVM 112
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 113 FPKELRKAGYYTAATGKWHL--GRAARSAFdriEDCRPGGEEKWVGFIQERPKDKPFMM----------------WFASH 174
Cdd:cd16150 81 LLKTLKDAGYHVAWAGKNDDlpGEFAAEAY---CDSDEACVRTAIDWLRNRRPDKPFCLylplifphppygveepWFSMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 175 DAhrdwdpsSASPPHVPADAVIPPYMVDTEGTR-QDL------------AAYYDEVQRLDRYVGLVVEELKQQGVYENTL 241
Cdd:cd16150 158 DR-------EKLPPRRPPGLRAKGKPSMLEGIEkQGLdrwseerwrelrATYLGMVSRLDHQFGRLLEALKETGLYDDTA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 242 IFFLADNGrpfprckTWLYDSGI-------------KPPFIVHWPHQLakPGSACDALISSIDIAPTVLEAAGVAVPETV 308
Cdd:cd16150 231 VFFFSDHG-------DYTGDYGLvekwpntfedcltRVPLIIKPPGGP--AGGVSDALVELVDIPPTLLDLAGIPLSHTH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 309 QGTSLMPLIKNTKSEVRDVVFAE--HNWHDTEAHERMvrkgpwmyirnarpefagwvqvHHKYASYEALLEGQAQGSL-T 385
Cdd:cd16150 302 FGRSLLPVLAGETEEHRDAVFSEggRLHGEEQAMEGG----------------------HGPYDLKWPRLLQQEEPPEhT 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395161673 386 PAQA----DVLLAPRPAEM--LFNVEKDPHQLNNLADSPEHSEPLRLMRAALDEWQERTGDTTP 443
Cdd:cd16150 360 KAVMirtrRYKYVYRLYEPdeLYDLEADPLELHNLIGDPAYAEIIAEMKQRLLRWMVETSDVVP 423
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-434 |
2.98e-70 |
|
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: 228.27 E-value: 2.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYlaTSQ--CSPSRCSMITGRYPHNTGAPELHQALPSD 109
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAF--TPQpvCGPARACLQTGLYPTETGCFRNGIPLPAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 110 QVMFPKELRKAGYYTAATGKWHLGRAARSAF-DRIEDcrpggeekwvgFIQERPKDKPFMMwFASH-------DAHRDWD 181
Cdd:cd16152 79 EKTLAHYFRDAGYETGYVGKWHLAGYRVDALtDFAID-----------YLDNRQKDKPFFL-FLSYlephhqnDRDRYVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 182 PSSASPPHvpADAVIPPYMVDTEGT-RQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGRPFpRCKTWLY 260
Cdd:cd16152 147 PEGSAERF--ANFWVPPDLAALPGDwAEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHF-RTRNAEY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 261 -----DSGIKPPFIVHWPHqlAKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTKSEVRDVVFAEHnwh 335
Cdd:cd16152 224 krschESSIRVPLVIYGPG--FNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWRNEVFIQI--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 336 dTEAH-ERMVRKGPWMYIRNArPEFAGWvqvhhKYASYEALLEgqaqgsltpaqadvllaprpaEMLFNVEKDPHQLNNL 414
Cdd:cd16152 299 -SESQvGRAIRTDRWKYSVAA-PDKDGW-----KDSGSDVYVE---------------------DYLYDLEADPYELVNL 350
|
410 420
....*....|....*....|
gi 1395161673 415 ADSPEHSEPLRLMRAALDEW 434
Cdd:cd16152 351 IGRPEYREVAAELRERLLAR 370
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
33-415 |
9.85e-70 |
|
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: 227.47 E-value: 9.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYG-HPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPelHQALPS--- 108
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLK--GGVLGGfsp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 109 -----DQVMFPKELRKAGYYTAATGKWHLG---------RAARSAFDRIEDCR-----------------PGGE------ 151
Cdd:cd16143 79 pliepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkKAATGTGKDVDYSKpikggpldhgfdyyfgiPASEvlptlt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 152 EKWVGFIQE-RPKDKPFMMWFASHDAHRdwdpssaspPHVPadaviPPYMVDtegtRQDLAAYYDEVQRLDRYVGLVVEE 230
Cdd:cd16143 159 DKAVEFIDQhAKKDKPFFLYFALPAPHT---------PIVP-----SPEFQG----KSGAGPYGDFVYELDWVVGRILDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 231 LKQQGVYENTLIFFLADNG------------------RPFPRCKTWLYDSGIKPPFIVHWPHQLaKPGSACDALISSIDI 292
Cdd:cd16143 221 LKELGLAENTLVIFTSDNGpspyadykelekfghdpsGPLRGMKADIYEGGHRVPFIVRWPGKI-PAGSVSDQLVSLTDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 293 APTVLEAAGVAVPETVQ--GTSLMPLIKNTKSEVRDvvfaEHNWHDTEAHERMVRKGPWMYIrnarpefagwvqvhhkya 370
Cdd:cd16143 300 FATLAAIVGQKLPDNAAedSFSFLPALLGPKKQEVR----ESLVHHSGNGSFAIRKGDWKLI------------------ 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1395161673 371 syealLEGQAQGSLTPAQADVllAPRPAEMLFNVEKDPHQLNNLA 415
Cdd:cd16143 358 -----DGTGSGGFSYPRGKEK--LGLPPGQLYNLSTDPGESNNLY 395
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
33-434 |
5.23e-69 |
|
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: 225.89 E-value: 5.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSqCSPSRCSMITGRYPHNTGAPELHQA---LPSD 109
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPV-CAPTRAALLTGRYPFRTGVWHTILGrerMRLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 110 QVMFPKELRKAGYYTAATGKWHLG-----RAARSAFD--------------------RIEDC--RPGGEEKWVG------ 156
Cdd:cd16146 80 ETTLAEVFKDAGYRTGIFGKWHLGdnypyRPQDRGFDevlghggggigqypdywgndYFDDTyyHNGKFVKTEGyctdvf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 157 ------FIQERpKDKPFMMwFASHDAhrdwdpssaspPHVP---ADAVIPPYmvDTEGTRQDLAAYYDEVQRLDRYVGLV 227
Cdd:cd16146 160 fdeaidFIEEN-KDKPFFA-YLATNA-----------PHGPlqvPDKYLDPY--KDMGLDDKLAAFYGMIENIDDNVGRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 228 VEELKQQGVYENTLIFFLADNGRPFPRC----------KTWLYDSGIKPPFIVHWPHQLaKPGSACDALISSIDIAPTVL 297
Cdd:cd16146 225 LAKLKELGLEENTIVIFMSDNGPAGGVPkrfnagmrgkKGSVYEGGHRVPFFIRWPGKI-LAGKDVDTLTAHIDLLPTLL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 298 EAAGVAVPETVQ--GTSLMPLIKNTKSEVRDVVFAEHNWHDTEAHERM----VRKGPWMYirnarpefagwvqVHHKYAS 371
Cdd:cd16146 304 DLCGVKLPEGIKldGRSLLPLLKGESDPWPERTLFTHSGRWPPPPKKKrnaaVRTGRWRL-------------VSPKGFQ 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395161673 372 YEallegqaqgsltpaqadvllaprpaemLFNVEKDPHQLNNLADspEHSEPLRLMRAALDEW 434
Cdd:cd16146 371 PE---------------------------LYDIENDPGEENDVAD--EHPEVVKRLKAAYEAW 404
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
32-415 |
4.89e-67 |
|
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: 220.51 E-value: 4.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTG------APELHQA 105
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGlpgvvgPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 106 LPSDQVMFPKELRKAGYYTAATGKWHLGRAA-----RSAFDR--------------------IEDCRPGGE--------- 151
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPeflptRHGFDEyfgipysndmwpfplyrndpPGPLPPLMEneevieqpa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 152 ----------EKWVGFIqERPKDKPFMMWFAsHDAhrdwdpssaspPHVPADAviPPymvDTEGTRQDlAAYYDEVQRLD 221
Cdd:cd16026 161 dqssltqrytDEAVDFI-ERNKDQPFFLYLA-HTM-----------PHVPLFA--SE---KFKGRSGA-GLYGDVVEELD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 222 RYVGLVVEELKQQGVYENTLIFFLADNGRPFPRCKTW------------LYDSGIKPPFIVHWPHQLaKPGSACDALISS 289
Cdd:cd16026 222 WSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGgsagplrggkgtTWEGGVRVPFIAWWPGVI-PAGTVSDELAST 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 290 IDIAPTVLEAAGVAVPETVQ--GTSLMPLIKNTKSEVRDVVFAEHNWHDTEAhermVRKGPWMYIrnarpefagwvqVHH 367
Cdd:cd16026 301 MDLLPTLAALAGAPLPEDRVidGKDISPLLLGGSKSPPHPFFYYYDGGDLQA----VRSGRWKLH------------LPT 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1395161673 368 KYASYeallegqaqgsltPAQADVLLAPRPAEMLFNVEKDPHQLNNLA 415
Cdd:cd16026 365 TYRTG-------------TDPGGLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
33-358 |
1.18e-65 |
|
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: 217.46 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNT-----GAPELHQALP 107
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTrvrgnSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 108 SDQVMFPKELRKAGYYTAATGKWHLGRAARSA------FD-----------------------------------RIEDC 146
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGhptkqgFDyfygyldqvhahnyypeylwrngekvplpnnvippLDEGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 147 RPGGE----------EKWVGFIQERpKDKPFMMWFASHDAHRDWDPSSASPPHVPADaviPPYMVDTEGTRQDLAAYYDE 216
Cdd:cd16145 161 NAGGGggtyshdlftDEALDFIREN-KDKPFFLYLAYTLPHAPLQVPDDGPYKYKPK---DPGIYAYLPWPQPEKAYAAM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 217 VQRLDRYVGLVVEELKQQGVYENTLIFFLADNG-----RPFPRCKTW------------LYDSGIKPPFIVHWPhQLAKP 279
Cdd:cd16145 237 VTRLDRDVGRILALLKELGIDENTLVVFTSDNGphsegGSEHDPDFFdsngplrgykrsLYEGGIRVPFIARWP-GKIPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 280 GSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTKSEVRD--VVFAEHNWHdteaHERMVRKGPWMYIRNARP 357
Cdd:cd16145 316 GSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGKPQQQQHdyLYWEFYEGG----GAQAVRMGGWKAVRHGKK 391
|
.
gi 1395161673 358 E 358
Cdd:cd16145 392 D 392
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-409 |
7.68e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 209.71 E-value: 7.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQALPSDQVM 112
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 113 FPKELRKAGYYTAATGKWH-LGRAARSAFDRIEDCrpggEEKWVGFIQER-PKDKPFMMWfashdahrdwdpSSASPPHv 190
Cdd:cd16037 81 WGHALRAAGYETVLIGKLHfRGEDQRHGFRYDRDV----TEAAVDWLREEaADDKPWFLF------------VGFVAPH- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 191 padaviPPYMVDTEG----TRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNG-----RPFPRcKTWLYD 261
Cdd:cd16037 144 ------FPLIAPQEFydlyVRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGdmlgeRGLWG-KSTMYE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 262 SGIKPPFIVHWPhqLAKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTkSEVRDVVFAEHNWHDTEAHE 341
Cdd:cd16037 217 ESVRVPMIISGP--GIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGP-DDPDRVVFSEYHAHGSPSGA 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161673 342 RMVRKGPWMYIrnarpefagwvqvhhKYASYEallegqaqgsltpaqadvllaprpaEMLFNVEKDPH 409
Cdd:cd16037 294 FMLRKGRWKYI---------------YYVGYP-------------------------PQLFDLENDPE 321
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-356 |
4.26e-63 |
|
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: 209.76 E-value: 4.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYlATSQCSPSRCSMITGRYPHNTGApeLHQALPSDQVM 112
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYV--VFGYLDPKQKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 113 FPKELRKAGYYTAATGKWHLGRA-------ARSAFD-------------------RIEDCRPGGEEK----------WVG 156
Cdd:cd16151 78 FGHLLKDAGYATAIAGKWQLGGGrgdgdypHEFGFDeyclwqltetgekysrpatPTFNIRNGKLLEttegdygpdlFAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 157 FI---QERPKDKPFMMWFASHDAHRDWDPssaSPPHVPADavippymVDTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQ 233
Cdd:cd16151 158 FLidfIERNKDQPFFAYYPMVLVHDPFVP---TPDSPDWD-------PDDKRKKDDPEYFPDMVAYMDKLVGKLVDKLEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 234 QGVYENTLIFFLADNG--RPFPRC---------KTWLYDSGIKPPFIVHWPHQLaKPGSACDALISSIDIAPTVLEAAGV 302
Cdd:cd16151 228 LGLRENTIIIFTGDNGthRPITSRtngrevrggKGKTTDAGTHVPLIVNWPGLI-PAGGVSDDLVDFSDFLPTLAELAGA 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161673 303 AVPE--TVQGTSLMPLIKNTKSEVRD--VVFAEHNWHDTEAHeRMVRKGPWMYIRNAR 356
Cdd:cd16151 307 PLPEdyPLDGRSFAPQLLGKTGSPRRewIYWYYRNPHKKFGS-RFVRTKRYKLYADGR 363
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
33-437 |
1.47e-59 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 203.36 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTG-------APELHQa 105
Cdd:PRK13759 7 PNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGrvgygdvVPWNYK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 106 lpsdqVMFPKELRKAGYYTAATGK--WHLGRA----------------AR----SAFDRIEDCRPGGEEK---------- 153
Cdd:PRK13759 86 -----NTLPQEFRDAGYYTQCIGKmhVFPQRNllgfhnvllhdgylhsGRnedkSQFDFVSDYLAWLREKapgkdpdltd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 154 -----------------------WVG-----FIQERPKDKPFMMWFASHDAHRDWDPSS--------------------- 184
Cdd:PRK13759 161 igwdcnswvarpwdleerlhptnWVGsesieFLRRRDPTKPFFLKMSFARPHSPYDPPKryfdmykdadipdphigdwey 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 185 ASPPHVPADAVIPPY-MVDTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNG---------Rpfpr 254
Cdd:PRK13759 241 AEDQDPEGGSIDALRgNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGdmlgdhylfR---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 255 cKTWLYDSGIKPPFIVHWPHQLAKP--GSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTKSEVRDVVFAEH 332
Cdd:PRK13759 317 -KGYPYEGSAHIPFIIYDPGGLLAGnrGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFGQYEGWRPYLHGEH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 333 NWHDTEAHermvrkgpwmYIrnarpefagwVQVHHKYasyeallegqaqgsltpaqadVLLAPRPAEMLFNVEKDPHQLN 412
Cdd:PRK13759 396 ALGYSSDN----------YL----------TDGKWKY---------------------IWFSQTGEEQLFDLKKDPHELH 434
|
490 500
....*....|....*....|....*.
gi 1395161673 413 NLADSPEHSEPLRLMRAAL-DEWQER 437
Cdd:PRK13759 435 NLSPSEKYQPRLREMRKKLvDHLRGR 460
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
33-440 |
1.07e-57 |
|
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: 197.48 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNtgapelHQA------L 106
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMN------HRSvwngtpL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 107 PSDQVMFPKELRKAGYYTAATGKWHL-----GRAARSAFDRI-EDCRPGGE-------------------EKWVGFIQER 161
Cdd:cd16028 75 DARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSyELAMPGFDpvdrldeypaedsdtafltDRAIEYLDER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 162 PkDKPFMM----------WFASHDAHRDWDPSSASPPH----VPADAVIPPYM--------------------VDTEGTR 207
Cdd:cd16028 155 Q-DEPWFLhlsyirphppFVAPAPYHALYDPADVPPPIraesLAAEAAQHPLLaaflerieslsfspgaanaaDLDDEEV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 208 QDL-AAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGRP----FPRCKTWLYDSGIKPPFIVHWPHQLAKP--G 280
Cdd:cd16028 234 AQMrATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQlgdhWLWGKDGFFDQAYRVPLIVRDPRREADAtrG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 281 SACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTKSEV-RDVVFAEHNWHDTEaHERMVRK--------GPWMy 351
Cdd:cd16028 314 QVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSDwRDAVHYEYDFRDVS-TRRPQEAlglspdecSLAV- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 352 IRNARpefagwvqvhHKYASYEALlegqaqgsltpaqadvllapRPaeMLFNVEKDPHQLNNLADSPEHSEPLRLMRAAL 431
Cdd:cd16028 392 IRDER----------WKYVHFAAL--------------------PP--LLFDLKNDPGELRDLAADPAYAAVVLRYAQKL 439
|
....*....
gi 1395161673 432 DEWQERTGD 440
Cdd:cd16028 440 LSWRMRHAD 448
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-315 |
1.18e-56 |
|
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: 188.99 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYP-----------HNTGAPE 101
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPsqhgihdwiveGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 102 LHQALPSDQVMFPKELRKAGYYTAATGKWHLGRaarsafDRIEDcrpggeekwvgFIQERPKDKPFMM---WFASHDAHr 178
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLGD------DAADF-----------LRRRAEAEKPFFLsvnYTAPHSPW- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 179 dwdpssaspphvpadavippymvdtegtrqdlaAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGRpfpRC--- 255
Cdd:cd16149 143 ---------------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGF---NMghh 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395161673 256 -------KTW---LYDSGIKPPFIVHWPHQLaKPGSACDALISSIDIAPTVLEAAGVAVPETVQ--GTSLMP 315
Cdd:cd16149 187 giwgkgnGTFplnMYDNSVKVPFIIRWPGVV-PAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFAD 257
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
32-420 |
3.41e-55 |
|
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: 190.48 E-value: 3.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISaDDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTG----APELHQALP 107
Cdd:cd16030 2 KPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGvydnNSYFRKVAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 108 sDQVMFPKELRKAGYYTAATGK---------------W--HLGRAARSAFDRIEDCRPGGEEKWVGFI------------ 158
Cdd:cd16030 81 -DAVTLPQYFKENGYTTAGVGKifhpgipdgdddpasWdePPNPPGPEKYPPGKLCPGKKGGKGGGGGpaweaadvpdea 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 159 ---------------QERPKDKPFMM----------------WFASHDAHRDWDPSSASPPHVPADAV-----IPPYM-- 200
Cdd:cd16030 160 ypdgkvadeaieqlrKLKDSDKPFFLavgfykphlpfvapkkYFDLYPLESIPLPNPFDPIDLPEVAWndlddLPKYGdi 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 201 -----------VDTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGrpf----prCKTWLYDSGIK 265
Cdd:cd16030 240 palnpgdpkgpLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGwhlgehghwGKHTLFEEATR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 266 PPFIVHWPHqLAKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTKSEVRDVVFaeHNWHDTEAHERMVR 345
Cdd:cd16030 320 VPLIIRAPG-VTKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLKNPSAKWKDAAF--SQYPRPSIMGYSIR 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395161673 346 KGPWMYIRnarpefagWVQVHHKYasyeallegqaqgsltpaqadvllaprpAEMLFNVEKDPHQLNNLADSPEH 420
Cdd:cd16030 397 TERYRYTE--------WVDFDKVG----------------------------AEELYDHKNDPNEWKNLANDPEY 435
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-315 |
5.42e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 182.36 E-value: 5.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGApeLHQALPSDQVM 112
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV--WGGPLEPDDPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 113 FPKELRKAGYYTAA-------TGKWHLGRAARSAFDRIEDCRPGGEE----------KWVGFIQERPKDKPFMMWFASHD 175
Cdd:cd16148 79 LAEILRKAGYYTAAvssnphlFGGPGFDRGFDTFEDFRGQEGDPGEEgderaervtdRALEWLDRNADDDPFFLFLHYFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 176 AHRdwdpssaspphvpadavipPYMvdtegtrqdlaaYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLAD-------N 248
Cdd:cd16148 159 PHE-------------------PYL------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDhgeefgeH 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395161673 249 GRpfprckTW-----LYDSGIKPPFIVHWPHQlaKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMP 315
Cdd:cd16148 208 GL------YWghgsnLYDEQLHVPLIIRWPGK--EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
33-302 |
1.20e-53 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 182.24 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGA-PELHQALPSDQV 111
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSyVSTPVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 112 MFPKELRKAGYYTAATGKWHLGRAARSAF---------------------DRIEDCRPGGE-------EKWVGFIQErpK 163
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWHLGWYNNQSPcnlgfdkffgrntgsdlyadpPDVPYNCSGGGvsdeallDEALEFLDN--N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 164 DKPFMMWFASHDAHrdwDPSSASPPHVPADAVIPPYmvdTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIF 243
Cdd:pfam00884 159 DKPFFLVLHTLGSH---GPPYYPDRYPEKYATFKPS---SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395161673 244 FLADNGRPFPRCKTWL--------YDSGIKPPFIVHWPHQLAKPGSAcDALISSIDIAPTVLEAAGV 302
Cdd:pfam00884 233 YTSDHGESLGEGGGYLhggkydnaPEGGYRVPLLIWSPGGKAKGQKS-EALVSHVDLFPTILDLAGI 298
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
33-415 |
5.41e-51 |
|
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: 177.34 E-value: 5.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIR---TPNVDALASDGLRFNNAYlATSQCSPSRCSMITGRYPHNTG-----APELHQ 104
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFY-VEPSCTPGRAAFITGRHPIRTGlttvgLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 105 ALPSDQVMFPKELRKAGYYTAATGKWHLGRAARS-----AFDRIEDCRPGG-----EEKWVGFIQERPK-DKPFMMWFAS 173
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRlptdhGFDEFYGNLYHTideeiVDKAIDFIKRNAKaDKPFFLYVNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 174 HDAHrdwdpssasPPHVPADavippymvDTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGrpfP 253
Cdd:cd16142 160 TKMH---------FPTLPSP--------EFEGKSSGKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNG---P 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 254 RCKTWlYDSGIKP---------------PFIVHWPHQLaKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMP--- 315
Cdd:cd16142 220 EQDVW-PDGGYTPfrgekgttweggvrvPAIVRWPGKI-KPGRVSNEIVSHLDWFPTLAALAGAPDPKDKLLGKDRHidg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 316 -------LIKNTKSEvRDVVFaehnWHdTEAHERMVRKGPWMYIRNARPEFAGWvqvhhkyasyeallegqaqgslTPAQ 388
Cdd:cd16142 298 vdqspflLGKSEKSR-RSEFF----YF-GEGELGAVRWKNWKVHFKAQEDTGGP----------------------TGEP 349
|
410 420
....*....|....*....|....*..
gi 1395161673 389 ADVLLAPrpaeMLFNVEKDPHQLNNLA 415
Cdd:cd16142 350 FYVLTFP----LIFNLRRDPKERYDVT 372
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
32-410 |
1.71e-49 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 173.81 E-value: 1.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPN-IRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTG-----APELHQA 105
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGvghnfLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 106 LPSDQVMFPKELRKAGYYTAATGKWHLGR------AARsAFDRI------EDCRPGGE--EKWVGFIQE-RPKDKPFMMW 170
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQreaylpNSR-GFDYYfgipfsHDSSLADRyaQFATDFIQRaSAKDRPFFLY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 171 FAShdAHRdwdpssasppHVPaDAVIPPYMVDTEGTrqdlAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGR 250
Cdd:cd16161 160 AAL--AHV----------HVP-LANLPRFQSPTSGR----GPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 251 PFPRCK----------------------TWlyDSGIKPPFIVHWPHQLaKPGSACDALISSIDIAPTVLEAAGVAVPET- 307
Cdd:cd16161 223 WEVKCElavgpgtgdwqgnlggsvakasTW--EGGHREPAIVYWPGRI-PANSTSAALVSTLDIFPTVVALAGASLPPGr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 308 -VQGTSLMPLIKNTKSEVRDVVFaehNWHDTEAHER---MVRKGPwmyirnarpefagwvqvhhkYASYEALLEGQAQ-G 382
Cdd:cd16161 300 iYDGKDLSPVLFGGSKTGHRCLF---HPNSGAAGAGalsAVRCGD--------------------YKAHYATGGALACcG 356
|
410 420
....*....|....*....|....*...
gi 1395161673 383 SLTPAQadvllaPRPAEMLFNVEKDPHQ 410
Cdd:cd16161 357 STGPKL------YHDPPLLFDLEVDPAE 378
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
33-352 |
3.03e-49 |
|
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: 171.61 E-value: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQALPSDQVM 112
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 113 FPKELRKAGYYTAATGKWHL-GRAARSAFDRIEDcrpggeekwVGF--IQE-----RPKDK-PFMMWfashdahrdwdpS 183
Cdd:cd16032 81 FAHYLRAAGYRTALSGKMHFvGPDQLHGFDYDEE---------VAFkaVQKlydlaRGEDGrPFFLT------------V 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 184 SASPPHVPadAVIPPYMVDTEgTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNG-----RP--FPRCk 256
Cdd:cd16032 140 SFTHPHDP--YVIPQEYWDLY-VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGdmlgeRGlwYKMS- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 257 twLYDSGIKPPFIVHWPHQLAkpGSACDALISSIDIAPTVLEAAGVAVP---ETVQGTSLMPLIKNTKSEVRDVVFAEHN 333
Cdd:cd16032 216 --FFEGSARVPLIISAPGRFA--PRRVAEPVSLVDLLPTLVDLAGGGTAphvPPLDGRSLLPLLEGGDSGGEDEVISEYL 291
|
330
....*....|....*....
gi 1395161673 334 WHDTEAHERMVRKGPWMYI 352
Cdd:cd16032 292 AEGAVAPCVMIRRGRWKFI 310
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
33-413 |
4.46e-48 |
|
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: 171.84 E-value: 4.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTG--APE--LHQ---- 104
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGmyGGTrvFLPwdig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 105 ALPSDQVMFPKELRKAGYYTAATGKWHLGRAARSA-----------FDRIED---------CRPGGE------------- 151
Cdd:cd16160 82 GLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHsdgahlpshhgFDFVGTnlpftnswaCDDTGRhvdfpdrsacfly 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 152 --------------------EKWVGFIQERpKDKPFMMWFashdahrdwdpsSASPPHVPADAvippyMVDTEGTRQDlA 211
Cdd:cd16160 162 yndtiveqpiqhehltetlvGDAKSFIEDN-QENPFFLYF------------SFPQTHTPLFA-----SKRFKGKSKR-G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 212 AYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGRPFPRC------------KTWLYDSGIKPPFIVHWPHQLaKP 279
Cdd:cd16160 223 RYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCleggstgglkggKGNSWEGGIRVPFIAYWPGTI-KP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 280 GSAcDALISSIDIAPTVLEAAGVAVPET--VQGTSLMP-LIKNTKSEVRDVVFAehnwhdTEAHERMVRKGPWmyirnar 356
Cdd:cd16160 302 RVS-HEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDlLLGEADSPHDDILYY------CCSRLMAVRYGSY------- 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161673 357 pefagwvQVHHKYASY--EALLEGQAQGSLTPAQ-------ADVLLAPRPAEMLFNVEKDP---HQLNN 413
Cdd:cd16160 368 -------KIHFKTQPLpsQESLDPNCDGGGPLSDyivcydcEDECVTKHNPPLIFDVEKDPgeqYPLQP 429
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
32-419 |
6.99e-47 |
|
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: 169.16 E-value: 6.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGA------PELHQA 105
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVypgvfyPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 106 LPSDQVMFPKELRKAGYYTAATGKWHLGRAARSA-------FDRI-------------------------EDCRPGG--- 150
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTylpthqgFDHYlgipyshdqgpcqnltcfppnipcfGGCDQGEvpc 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 151 --------EEKWVGFIQERPK---------------DKPFMMWFASHDAHRdwdpssaspphvpadaviPPYMVDTEGTR 207
Cdd:cd16158 161 plfynesiVQQPVDLLTLEERyakfakdfiadnakeGKPFFLYYASHHTHY------------------PQFAGQKFAGR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 208 QDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGRPFPR-----------C-KTWLYDSGIKPPFIVHWPHQ 275
Cdd:cd16158 223 SSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRksrggnagllkCgKGTTYEGGVREPAIAYWPGR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 276 LaKPGSAcDALISSIDIAPTVLEAAGVAVPE-TVQGTSLMPLIKNTKSEVRDVVFaehnwhdteahermvrkgpwMYIRN 354
Cdd:cd16158 303 I-KPGVT-HELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPRQTFF--------------------YYPTS 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161673 355 ARPEFAGWVQVHHKY-ASYeaLLEGQAQGSLTPAQADVLLAPRPAE---MLFNVEKDPHQLNNLADSPE 419
Cdd:cd16158 361 PDPDKGVFAVRWGKYkAHF--YTQGAAHSGTTPDKDCHPSAELTSHdppLLFDLSQDPSENYNLLGLPE 427
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
33-355 |
2.02e-46 |
|
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: 165.80 E-value: 2.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYlATSQCSPSRCSMITGRYPHNTG------APELHQAL 106
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGmqhgviLAGEPYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 107 PSDQVMFPKELRKAGYYTAATGKWHLGRAARSA------FDR-----------------------IEDCRPGGEEKWVGF 157
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtptnrgFDSfygyyggaedyythtsggandygNDDLRDNEEPAWDYN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 158 ---------------IQERPKDKPFMMWFASHDAHrdwdpssaSPPHVPADAVIPPYMVDTEGTRQDLAAYYDEVQRLDR 222
Cdd:cd16029 160 gtystdlftdravdiIENHDPSKPLFLYLAFQAVH--------APLQVPPEYADPYEDKFAHIKDEDRRTYAAMVSALDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 223 YVGLVVEELKQQGVYENTLIFFLADNGRP---------FP-R-CKTWLYDSGIKPPFIVHWPHQLAKPGSACDALISSID 291
Cdd:cd16029 232 SVGNVVDALKAKGMLDNTLIVFTSDNGGPtgggdggsnYPlRgGKNTLWEGGVRVPAFVWSPLLPPKRGTVSDGLMHVTD 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161673 292 IAPTVLEAAGVAVPETVQ--GTSLMPLIKNTKSEVRDVVFaeHNWHD--TEAHERMVRKGPWMYIRNA 355
Cdd:cd16029 312 WLPTLLSLAGGDPDDLPPldGVDQWDALSGGAPSPRTEIL--LNIDDitRTTGGAAIRVGDWKLIVGK 377
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
32-418 |
4.64e-44 |
|
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: 159.64 E-value: 4.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGcyghPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGApeLHQALPS--- 108
Cdd:cd16147 1 RPNIVLILTDDQDVELGS----MDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGV--TNNSPPGggy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 109 --------DQVMFPKELRKAGYYTAATGK--------------------WH-LGRAAR-----SAFDRIEdcRPGGE--- 151
Cdd:cd16147 75 pkfwqnglERSTLPVWLQEAGYRTAYAGKylngygvpggvsyvppgwdeWDgLVGNSTyynytLSNGGNG--KHGVSypg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 152 --------EKWVGFIQE-RPKDKPFMMWFASHDAHRDWDP----------SSASPPHVPADAVI---PPYMVDTEGTRQD 209
Cdd:cd16147 153 dyltdviaNKALDFLRRaAADDKPFFLVVAPPAPHGPFTPapryanlfpnVTAPPRPPPNNPDVsdkPHWLRRLPPLNPT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 210 LAAYYDEVQR--------LDRYVGLVVEELKQQGVYENTLIFFLADNG------RpFPRCKTWLYDSGIKPPFIVHWPHq 275
Cdd:cd16147 233 QIAYIDELYRkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlgqhR-LPPGKRTPYEEDIRVPLLVRGPG- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 276 lAKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTksevrdvvfaehnwhdteahermvrkgpWMYIRNA 355
Cdd:cd16147 311 -IPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRSCGDSNNNT----------------------------YKCVRTV 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395161673 356 RPEFAGWVQVhhkYASYEalLEgqaqgsltpaqadvllaprpaemLFNVEKDPHQLNNLADSP 418
Cdd:cd16147 362 DDTYNLLYFE---WCTGF--RE-----------------------LYDLTTDPYQLTNLAGDL 396
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
32-436 |
8.03e-43 |
|
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: 158.01 E-value: 8.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYP------------HNTGA 99
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPirngfyttnahaRNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 100 P-ELHQALPSDQVMFPKELRKAGYYTAATGKWHLGRAA-----RSAFDR---IEDCRPG--------------------- 149
Cdd:cd16157 81 PqNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPqyhplKHGFDEwfgAPNCHFGpydnkaypnipvyrdwemigr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 150 -----------GE--------EKWVGFIQ-ERPKDKPFMMWFASHDAHrdwDPSSASPPHVpadavippymvdteGTRQD 209
Cdd:cd16157 161 yyeefkidkktGEsnltqiylQEALEFIEkQHDAQKPFFLYWAPDATH---APVYASKPFL--------------GTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 210 lAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNGR-------------PFPRCKTWLYDSGIKPPFIVHWPHQL 276
Cdd:cd16157 224 -GLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAalisapeqggsngPFLCGKQTTFEGGMREPAIAWWPGHI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 277 aKPGSACDALISSIDIAPTVLEAAGVAVPE--TVQGTSLMPLIKNTKSEVRDVVFAEHNwhdteahERM-VRKGPWmyir 353
Cdd:cd16157 303 -KPGQVSHQLGSLMDLFTTSLALAGLPIPSdrAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMaVRLGQY---- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 354 naRPEFAGWVQVHHKYASYEALLEGQ-AQGSLTPAQADVLLAPrpaeMLFNVEKDPHQLNNL-ADSPEHSEPLRLMRAAL 431
Cdd:cd16157 371 --KAHFWTWSNSWEEFRKGINFCPGQnVPGVTTHNQTDHTKLP----LLFHLGRDPGEKYPIsFKSAEYKQAMPRISKVV 444
|
....*
gi 1395161673 432 DEWQE 436
Cdd:cd16157 445 QQHQK 449
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-313 |
1.88e-41 |
|
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: 149.45 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHP----------NIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPEL 102
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAhtgksesrlgYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 103 ---HQALPSDQVMFPKELRKAGYYTAATGKWHLGraarsAFDRIEDCRPGGEEKWVGFIQERPK-DKPFMMWFASHDahr 178
Cdd:cd16153 82 eaaHPALDHGLPTFPEVLKKAGYQTASFGKSHLE-----AFQRYLKNANQSYKSFWGKIAKGADsDKPFFVRLSFLQ--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 179 dwdpssaspPHVPadaVIPPymvdtEGTRqDLAAYYDEVQRLDRYVGLVVEELKQQGVY---ENTLIFFLADNGrpfprc 255
Cdd:cd16153 154 ---------PHTP---VLPP-----KEFR-DRFDYYAFCAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHG------ 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395161673 256 ktW-LYDSGI-----------KPPFIVHWPHQLAKP-GSACDALISSIDIAPTVLEAAGVAV--PETVQGTSL 313
Cdd:cd16153 210 --WhLGEQGIlakftfwpqshRVPLIVVSSDKLKAPaGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDL 280
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-329 |
3.25e-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: 144.27 E-value: 3.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQA-----LP 107
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSpmqplLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 108 SDQVMFPKELRKAGYYTAATGKWHLGRAARSAFDRieDcrPGGEEKWVGFIQERPK----DKPfmmWFAShdahrdwdpS 183
Cdd:cd16035 81 PDVPTLGHMLRAAGYYTAYKGKWHLSGAAGGGYKR--D--PGIAAQAVEWLRERGAknadGKP---WFLV---------V 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 184 SASPPHvpaDAVIPPYmvDTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNG---------RPFPR 254
Cdd:cd16035 145 SLVNPH---DIMFPPD--DEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGemggahglrGKGFN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 255 CktwlYDSGIKPPFIVHWPHQLAKPGSaCDALISSIDIAPTVLEAAGVAVPETV------QGTSLMPLIKNTKS-EVRDV 327
Cdd:cd16035 220 A----YEEALHVPLIISHPDLFGTGQT-TDALTSHIDLLPTLLGLAGVDAEARAteapplPGRDLSPLLTDADAdAVRDG 294
|
..
gi 1395161673 328 VF 329
Cdd:cd16035 295 IL 296
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
32-436 |
7.64e-36 |
|
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: 139.35 E-value: 7.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQ------- 104
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGmrvilft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 105 ----ALPSDQVMFPKELRKAGYYTAATGKWHLG--RAARSAFDR-----------------IEDCRPGGEEK-------- 153
Cdd:cd16159 81 assgGLPPNETTFAEVLKQQGYSTALIGKWHLGlhCESRNDFCHhplnhgfdyfyglpltnLKDCGDGSNGEydlsfdpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 154 ------------------------------------------WVGFIQ-------------------------------- 159
Cdd:cd16159 161 fplltafvlitaltiflllylgavskrffvfllilsllfislFFLLLItnryfncilmrnhevveqpmslenltqrltke 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 160 -----ERPKDKPFMMWFASHDAHRDWDPSsaspphvpadavipPYMVDtegtRQDLAAYYDEVQRLDRYVGLVVEELKQQ 234
Cdd:cd16159 241 aisflERNKERPFLLVMSFLHVHTALFTS--------------KKFKG----RSKHGRYGDNVEEMDWSVGQILDALDEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 235 GVYENTLIFFLADNGrpfprckTWLY------------------------DSGIKPPFIVHWPHQLaKPGSACDALISSI 290
Cdd:cd16159 303 GLKDNTFVYFTSDNG-------GHLEeisvggeygggnggiyggkkmggwEGGIRVPTIVRWPGVI-PPGSVIDEPTSLM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 291 DIAPTVLEAAGVAVPE--TVQGTSLMPLIKNTKsevrdvvfaEHNWHDTEAHermvRKGPWMYIRNARPEFAGWV-QVHH 367
Cdd:cd16159 375 DIFPTVAALAGAPLPSdrIIDGRDLMPLLTGQE---------KRSPHEFLFH----YCGAELHAVRYRPRDGGAVwKAHY 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 368 KYASYEALLEGQAQGSLTPAQADVLLAPRPAEmLFNVEKDPHQLNNL-ADSPEHSEPLRLMRAALDEWQE 436
Cdd:cd16159 442 FTPNFYPGTEGCCGTLLCRCFGDSVTHHDPPL-LFDLSADPSESNPLdPTDEPYQEIIKKILEAVAEHQS 510
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
33-441 |
2.80e-35 |
|
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: 137.13 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQALPSDQVM 112
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 113 FPKELRKAGYYTAATGKWHLG----------------------------------RAARSAFDRIEDCRPGGEEKW---- 154
Cdd:cd16156 81 IGQRLSDNGIHTAYIGKWHLDggdyfgngicpqgwdpdywydmrnyldelteeerRKSRRGLTSLEAEGIKEEFTYghrc 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 155 ----VGFIqERPKDKPFMMWFASHDAHrdwDPSSASPPHVP--ADAVIPpymvdtegtrqDLAAYYD------EVQRL-- 220
Cdd:cd16156 161 tnraLDFI-EKHKDEDFFLVVSYDEPH---HPFLCPKPYASmyKDFEFP-----------KGENAYDdlenkpLHQRLwa 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 221 -------------------------DRYVGLVVEELKQqgVYENTLIFFLADNGRPFPRCKTWL-----YDSGIKPPFIV 270
Cdd:cd16156 226 gakphedgdkgtikhplyfgcnsfvDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLWAkgpavYDEITNIPLII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 271 HWPhQLAKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKNTKSEVRDVVFAEHNWHDTEaHERMvrkGPWM 350
Cdd:cd16156 304 RGK-GGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDPEIPENRGVFVEFGRYEVD-HDGF---GGFQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 351 YIRnarpefaGWVQVHHKYASYeaLLEgqaqgsltpaqadvllaprpAEMLFNVEKDPHQLNNLADSPEHSEPLRLMRAA 430
Cdd:cd16156 379 PVR-------CVVDGRYKLVIN--LLS--------------------TDELYDLEKDPYEMHNLIDDPDYADVRDQLHDE 429
|
490
....*....|.
gi 1395161673 431 LDEWQERTGDT 441
Cdd:cd16156 430 LLDYMNETRDP 440
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-356 |
1.97e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 127.08 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYG----HPNirTPNVDALASDGLRFNNAYlATSQCSPSRCSMITGRYPHNTG--APELHQAL 106
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSlssdLPV--TPTLDSLANSGIVFDNLW-ATPACSPTRATILTGKYGFRTGvlAVPDELLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 107 PSDQVMFP--KELRKAGYYTAATGKWHLGrAARSAFDriedcRPGGEEKWVGFIQERPKDkpFMMW--------FASHDA 176
Cdd:cd16154 78 SEETLLQLliKDATTAGYSSAVIGKWHLG-GNDNSPN-----NPGGIPYYAGILGGGVQD--YYNWnltnngqtTNSTEY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 177 HR--------DWDPSSASP---------PHVPADAviPP---YMVDTEGTRQDLAA----YY-DEVQRLDRYVGLVVEEL 231
Cdd:cd16154 150 ATtkltnlaiDWIDQQTKPwflwlaynaPHTPFHL--PPaelHSRSLLGDSADIEAnprpYYlAAIEAMDTEIGRLLASI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 232 KQQgVYENTLIFFLADNGRPFP---------RCKTWLYDSGIKPPFIVHwPHQLAKPGSACDALISSIDIAPTVLEAAGV 302
Cdd:cd16154 228 DEE-ERENTIIIFIGDNGTPGQvvdlpytrnHAKGSLYEGGINVPLIVS-GAGVERANERESALVNATDLYATIAELAGV 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1395161673 303 AVPETVQGTSLMPLIKNTKSEVRDVVFAEhNWHDTEAhermvrkgpWMYIRNAR 356
Cdd:cd16154 306 DAAEIHDSVSFKPLLSDVNASTRQYNYTE-YESPTTT---------GWATRNQY 349
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
33-300 |
1.60e-27 |
|
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: 110.20 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFN-NAYLATSQCSPSRCSMITGRYPHNTGA----------PE 101
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNfRSVSPPTSSAPNHAALLTGAYPTLHGYtgngsadpelPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 102 LHQALPSDQVMFPKELRKAGYYTAATGkwhlgraarsafdrIEDcrpggeekwvgFIQERPKDKPFMMWFasHDAHRDWd 181
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG--------------LLK-----------AIDETSKEKPFVLFL--HFDGPDG- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 182 PSSASPPHVPAdavippymvdtegtrqdlaaYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLADNG--------RPFP 253
Cdd:cd00016 133 PGHAYGPNTPE--------------------YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGgidkghggDPKA 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1395161673 254 RCKTWLYDSGIKPPFIVHWPHqlAKPGSACDALISSIDIAPTVLEAA 300
Cdd:cd00016 193 DGKADKSHTGMRVPFIAYGPG--VKKGGVKHELISQYDIAPTLADLL 237
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
33-352 |
1.69e-26 |
|
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: 110.32 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAPELHQALPSDQVM 112
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 113 FPKELRKAGYYTAATGKWHLGRAARSAFDRIEdcrpggeeKW---VGFI--QE-RPKdkPFMMWFASHD--AHRDW---D 181
Cdd:cd16171 81 WMDRLEKHGYHTQKYGKLDYTSGHHSVSNRVE--------AWtrdVPFLlrQEgRPT--VNLVGDRSTVrvMLKDWqntD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 182 PSSASPPHVPADAVIP-----------PYMVDTEG-----TRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFL 245
Cdd:cd16171 151 KAVHWIRKEAPNLTQPfalylglnlphPYPSPSMGenfgsIRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 246 ADNG------RPFprCKTWLYDSGIKPPFIVHWPHqlAKPGSACDALISSIDIAPTVLEAAGVAVPETVQGTSLMPLIKN 319
Cdd:cd16171 231 SDHGelamehRQF--YKMSMYEGSSHVPLLIMGPG--IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1395161673 320 TKSEVRDVVFAEHNWHDTEAH-------ERMVRKGPWMYI 352
Cdd:cd16171 307 SSIKESPSRVPHPDWVLSEFHgcnvnasTYMLRTNSWKYI 346
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
31-314 |
3.35e-22 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 99.73 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 31 PPPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPSRCSMITGRYPHNTGAP---ELHQALP 107
Cdd:COG1368 233 KKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGSPykrPGQNNFP 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 108 SdqvmFPKELRKAGYYTAA--TGK---WHLGRAARSA-FDRI---EDCRPGGEEKWvG---------FIQE-RPKDKPFM 168
Cdd:COG1368 313 S----LPSILKKQGYETSFfhGGDgsfWNRDSFYKNLgFDEFydrEDFDDPFDGGW-GvsdedlfdkALEElEKLKKPFF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 169 MWFASHDAHRDWDpssaspphVPADaviPPYMVDTEGTrqDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLAD- 247
Cdd:COG1368 388 AFLITLSNHGPYT--------LPEE---DKKIPDYGKT--TLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDh 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161673 248 NGRPFPRCKTWLYDSGIKPPFIVHWPHQlaKPGSACDALISSIDIAPTVLEAAGVAVPETVQ-GTSLM 314
Cdd:COG1368 455 GPRSPGKTDYENPLERYRVPLLIYSPGL--KKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRDLL 520
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
33-301 |
9.08e-19 |
|
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: 86.20 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 33 PNVIVFIG---DDISADDFGcyGHPNIrTPNVDALASDGLRFNNAYlatSQCSPSR-----CSMITGRYPHNTGAPELHQ 104
Cdd:cd16015 1 PNVIVILLesfSDPYIDKDV--GGEDL-TPNLNKLAKEGLYFGNFY---SPGFGGGtangeFEVLTGLPPLPLGSGSYTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 105 ALPSDQVMFPKELRKAGYYTAA--TGK---WHLGRAARSA-FDRIEDCR--PGGEEKWVG----------FIQER---PK 163
Cdd:cd16015 75 YKLNPLPSLPSILKEQGYETIFihGGDasfYNRDSVYPNLgFDEFYDLEdfPDDEKETNGwgvsdeslfdQALEEleeLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 164 DKPFMMWFASHDAHRDWDPssaspphvpaDAVIPPYMVDTEGTRQDLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIF 243
Cdd:cd16015 155 KKPFFIFLVTMSNHGPYDL----------PEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIV 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395161673 244 FLADNGRPFPRCKTWLYDSGI---KPPFIVHWPHQLAKPGSacDALISSIDIAPTVLEAAG 301
Cdd:cd16015 225 IYGDHLPSLGSDYDETDEDPLdlyRTPLLIYSPGLKKPKKI--DRVGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
16-249 |
3.30e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 52.44 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 16 MAALTVVSSVHAENPPPPNVIVFIGDDISADDFGcyghpNIRTPNVDALASDGLRFNN---AYLATSqcSPSRCSMITGR 92
Cdd:COG1524 7 LLLASLLAAAAAAAPPAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPltsVFPSTT--APAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 93 YPHNTG----------APELHQALPSDQVMFPK-----------ELRKAGYYTAATGKWHLGRAA--RSAFDRIEDCR-- 147
Cdd:COG1524 80 YPGEHGivgngwydpeLGRVVNSLSWVEDGFGSnsllpvptifeRARAAGLTTAAVFWPSFEGSGliDAARPYPYDGRkp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 148 ----PGGEEKWVGFIQERPKDKP---FMMWFAS--HDAHRdWDPSSAspphvpadavippymvdtegtrqdlaAYYDEVQ 218
Cdd:COG1524 160 llgnPAADRWIAAAALELLREGRpdlLLVYLPDldYAGHR-YGPDSP--------------------------EYRAALR 212
|
250 260 270
....*....|....*....|....*....|.
gi 1395161673 219 RLDRYVGLVVEELKQQGVYENTLIFFLADNG 249
Cdd:COG1524 213 EVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
35-249 |
2.16e-06 |
|
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: 49.73 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 35 VIVFIGDDISADDFGCYGHpnirTPNVDALASDGLRFNNAY-LATSQCSPSRCSMITGRYPHNTGapelhqaLPSDQVMF 113
Cdd:pfam01663 1 LLVISLDGFRADYLDRFEL----TPNLAALAKEGVSAPNLTpVFPTLTFPNHYTLVTGLYPGSHG-------IVGNTFYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 114 PKELRKAGYYTAATGKWHL-------------GRAARSAF--------DRIEDCRPGG-EEKW-VGFIQERPKDKPFM-M 169
Cdd:pfam01663 70 PKTGEYLVFVISDPEDPRWwqgepiwdtaakaGVRAAALFwpgsevdySTYYGTPPRYlKDDYnNSVPFEDRVDTAVLqT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 170 WFASHDAHRDWDPssaspPHVPAdAVIPpyMVDTEGTRQ--DLAAYYDEVQRLDRYVGLVVEELKQQGVYENTLIFFLAD 247
Cdd:pfam01663 150 WLDLPFADVAAER-----PDLLL-VYLE--EPDYAGHRYgpDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSD 221
|
..
gi 1395161673 248 NG 249
Cdd:pfam01663 222 HG 223
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
32-125 |
8.00e-05 |
|
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: 44.54 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 32 PPNVIVFIGDDISADDFGCYGHPNIRTPNVDALASDGLRFNNAYLATSQCSPS-RCsMITGRYPHNTGAPELHQALPSdq 110
Cdd:cd16017 2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVISCGTSTAVSlPC-MLSFANRENYDRAYYQENLID-- 78
|
90
....*....|....*
gi 1395161673 111 vMFpkelRKAGYYTA 125
Cdd:cd16017 79 -LA----KKAGYKTY 88
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
57-301 |
1.43e-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: 43.73 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 57 RTPNVDALASDGLRFNNAYLAT-SQCSPSRCSMITGRYPHNTG-------APELHQAL-PSDQVMFPKELR--------- 118
Cdd:cd16018 21 LTPNLKRLAEEGVRAKYVKPVFpTLTFPNHYSIVTGLYPESHGivgnyfyDPKTNEEFsDSDWVWDPWWIGgepiwvtae 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 119 KAGYYTAATGkWhlgraarsafdriedcrPGGEEKWVGFIQERPKDKPFMMWFASHDAHRDwdpssaspphvPADAVI-- 196
Cdd:cd16018 101 KAGLKTASYF-W-----------------PGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEE-----------RVDTILew 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 197 ----PP-----YMVDTEGTRQDLAAYYDEV----QRLDRYVGLVVEELKQQGVYENTLIFFLADNG---------RPfpr 254
Cdd:cd16018 152 ldleRPdlillYFEEPDSAGHKYGPDSPEVnealKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGmtdvgthgyDN--- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1395161673 255 cktwlYDSGIKPPFIVHWP--HQLAKPGSacdalISSIDIAPTVLEAAG 301
Cdd:cd16018 229 -----ELPDMRAIFIARGPafKKGKKLGP-----FRNVDIYPLMCNLLG 267
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
304-440 |
1.07e-03 |
|
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: 38.38 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 304 VPETVQGTSLMPLIK-NTKSEVRDVVFAEhnWHDTEAhERMVRK--GpwmyIRNARpefagWVQVHHkyasYEALLEGQa 380
Cdd:pfam16347 1 IPADMQGKSFLPLLKgKKPKNWRDALYYH--YYEYPA-EHAVKRhyG----VRTER-----YKLIHF----YNDIDEWE- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161673 381 qgsltpaqadvllaprpaemLFNVEKDPHQLNNLADSPEHSEPLRLMRAALDEWQERTGD 440
Cdd:pfam16347 64 --------------------LYDLQKDPKEMNNVYGDPEYAEVQAELKEELEELRKQYKD 103
|
|
| |
