|
Name |
Accession |
Description |
Interval |
E-value |
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
47-478 |
0e+00 |
|
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: 607.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSDIE-TPTLDRLAAEGVKLENYYIQPICTPSRSQLLTGRYQIHTGLQHSIIRPRQPNCLP 125
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIkTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 126 LDQVTLPQKLQEAGYSTHMVGKWHLGFYRKECLPTRRGFDTFLGSLTGNVDYYTYDNCDGPGVCGFDLHEGENVAWGLSG 205
Cdd:cd16029 81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGNDDLRDNEEPAWDYNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 206 QYSTMLYAQRVSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRYRSMG----NVARRKYAAMVTCMDEAVRNITWAL 281
Cdd:cd16029 161 TYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFahikDEDRRTYAAMVSALDESVGNVVDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 282 KRYGFYNNSVIIFSSDNGGQT--FSGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKR-RTSRALVHITDWYPTLVGLA 358
Cdd:cd16029 241 KAKGMLDNTLIVFTSDNGGPTggGDGGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPPKRgTVSDGLMHVTDWLPTLLSLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 359 GGTVSVADGLDGYDVWPAISEGRASPRTEILHNIDPlynharhgsleggfgIWNTAVQAAIRVGEWKLLTGDPgygdwip 438
Cdd:cd16029 321 GGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDD---------------ITRTTGGAAIRVGDWKLIVGKP------- 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 584042845 439 pqtlaafpgswwnlermasarqavwLFNISADPYEREDLA 478
Cdd:cd16029 379 -------------------------LFNIENDPCERNDLA 393
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
35-498 |
3.63e-100 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 308.73 E-value: 3.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 35 ASEQPSVAPPQPPHIIFILTDDQGYHDVGYHGS-DIETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQIHTGLQ 112
Cdd:COG3119 12 LAAAAAAAAAKRPNILFILADDLGYGDLGCYGNpLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHRTGVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 113 HsiIRPRQPNCLPLDQVTLPQKLQEAGYSTHMVGKWHLgfyrkeclptrrgfdtflgsltgnvdyytydncdgpgvcgfd 192
Cdd:COG3119 92 D--NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 193 lhegenvawglsgqYSTMLYAQR-VSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRYRSMGNV------------- 258
Cdd:COG3119 128 --------------YLTDLLTDKaIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPlppnlaprdltee 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 259 ----ARRKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTFSGGsnwpLRGRKGTYWEGGVRGLGFVHSPLL 334
Cdd:COG3119 194 elrrARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHG----LRGGKGTLYEGGIRVPLIVRWPGK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 335 KRKRRTSRALVHITDWYPTLVGLAGgtVSVADGLDGYDVWPAISEGRASPRteilhniDPLYNHarhgsleggfgIWNTA 414
Cdd:COG3119 270 IKAGSVSDALVSLIDLLPTLLDLAG--VPIPEDLDGRSLLPLLTGEKAEWR-------DYLYWE-----------YPRGG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 415 VQAAIRVGEWKLLTGDPGYGDWippqtlaafpgswwnlermasarqavWLFNISADPYEREDLAGQRPDVVRALLARLVD 494
Cdd:COG3119 330 GNRAIRTGRWKLIRYYDDDGPW--------------------------ELYDLKNDPGETNNLAADYPEVVAELRALLEA 383
|
....
gi 584042845 495 YNRT 498
Cdd:COG3119 384 WLKE 387
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
46-478 |
7.61e-100 |
|
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: 308.34 E-value: 7.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 46 PPHIIFILTDDQGYHDVGYHGS-DIETPTLDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLQHSIIRPRQPNC 123
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSpLIKTPNIDRLAAEGVRFTDFYAaAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 124 LPLDQVTLPQKLQEAGYSTHMVGKWHLGFyRKECLPTRRGFDTFLGSLTGN-VDYYTYDNCDGPGvCGFDLHEGENVAWG 202
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGH-QPEFLPTRHGFDEYFGIPYSNdMWPFPLYRNDPPG-PLPPLMENEEVIEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 203 LSGQYS-TMLYAQRVSHILASHSPrQPLFLYVAFQAVHTPLQSPREylYRYRSMGNVarrkYAAMVTCMDEAVRNITWAL 281
Cdd:cd16026 159 PADQSSlTQRYTDEAVDFIERNKD-QPFFLYLAHTMPHVPLFASEK--FKGRSGAGL----YGDVVEELDWSVGRILDAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 282 KRYGFYNNSVIIFSSDNG---GQTFSGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWYPTLVGLA 358
Cdd:cd16026 232 KELGLEENTLVIFTSDNGpwlEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 359 GGTVSVADGLDGYDVWPAISEGRASPRTEILHnidplynHARHGSLEggfgiwntavqaAIRVGEWKLLTgDPGYGDWIP 438
Cdd:cd16026 312 GAPLPEDRVIDGKDISPLLLGGSKSPPHPFFY-------YYDGGDLQ------------AVRSGRWKLHL-PTTYRTGTD 371
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 584042845 439 PQTLAAFPgswwnlermasaRQAVWLFNISADPYEREDLA 478
Cdd:cd16026 372 PGGLDPTK------------LEPPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-495 |
2.94e-95 |
|
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: 297.15 E-value: 2.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSD-IETPTLDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLQHSI--------- 115
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKfYETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 116 ---IRPRQPNCLPLDQVTLPQKLQEAGYSTHMVGKWHLGFyRKECLPTRRGFDTFLGSlTGNVDYYTYDncDGPGVCGFD 192
Cdd:cd16144 81 tklIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGG-EGGYGPEDQGFDVNIGG-TGNGGPPSYY--FPPGKPNPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 193 LHEGENvawglsGQYSTMLYAQRVSHILASHSpRQPLFLYVAFQAVHTPLQSPREYLYRYRSMGNVARRK-----YAAMV 267
Cdd:cd16144 157 LEDGPE------GEYLTDRLTDEAIDFIEQNK-DKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRKGqknpvYAAMI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 268 TCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTFSGG---SNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRAL 344
Cdd:cd16144 230 ESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGpptSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 345 VHITDWYPTLVGLAGGTVSVADGLDGYDVWPAIsEGRASPRTEilhniDPLYNHARHGSLEGGFgiwntaVQAAIRVGEW 424
Cdd:cd16144 310 VIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLL-KGGEADLPR-----RALFWHFPHYHGQGGR------PASAIRKGDW 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584042845 425 KLLtgdpgygdwippqtlaafpgSWWNlermasaRQAVWLFNISADPYEREDLAGQRPDVVRALLARLVDY 495
Cdd:cd16144 378 KLI--------------------EFYE-------DGRVELYNLKNDIGETNNLAAEMPEKAAELKKKLDAW 421
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
47-492 |
5.46e-93 |
|
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: 290.99 E-value: 5.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGS-DIETPTLDRLAAEGVKLENYYIQPICTPSRSQLLTGRYQIHTGLQHSII-RPRqpncL 124
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNpILKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTILgRER----M 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 PLDQVTLPQKLQEAGYSTHMVGKWHLGF---YRkeclPTRRGFDTFLGSLTGNVDYYTydncDGPGVCGFD---LHEGEN 198
Cdd:cd16146 77 RLDETTLAEVFKDAGYRTGIFGKWHLGDnypYR----PQDRGFDEVLGHGGGGIGQYP----DYWGNDYFDdtyYHNGKF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 199 VAwglSGQYST-------MLYAQRVSHilashsprQPLFLYVAFQAVHTPLQSPREYLYRYRSMG-NVARRKYAAMVTCM 270
Cdd:cd16146 149 VK---TEGYCTdvffdeaIDFIEENKD--------KPFFAYLATNAPHGPLQVPDKYLDPYKDMGlDDKLAAFYGMIENI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 271 DEAVRNITWALKRYGFYNNSVIIFSSDNGGQT-FSGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITD 349
Cdd:cd16146 218 DDNVGRLLAKLKELGLEENTIVIFMSDNGPAGgVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHID 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 350 WYPTLVGLAGGTVSVADGLDGYDVWPAISEGRASPRTEIL--HNIDPLYNHARHGsleggfgiwntavQAAIRVGEWKLL 427
Cdd:cd16146 298 LLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLftHSGRWPPPPKKKR-------------NAAVRTGRWRLV 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584042845 428 TGDPgygdwippqtlaafpgswWNLErmasarqavwLFNISADPYEREDLAGQRPDVVRALLARL 492
Cdd:cd16146 365 SPKG------------------FQPE----------LYDIENDPGEENDVADEHPEVVKRLKAAY 401
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-478 |
4.18e-79 |
|
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: 254.43 E-value: 4.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSD--IETPTLDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLQHSIIRPRQPNC 123
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDskIPTPNIDRLAAEGMRFTDAHSpSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 124 LPLDQVTLPQKLQEAGYSTHMVGKWHLG--FYRKECLPTRRGFDTflgsltgNVDYYTyDNCDGPGVCGFDLHegenvaW 201
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKWHLGldWKKKDGKKAATGTGK-------DVDYSK-PIKGGPLDHGFDYY------F 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 202 GLS-GQYSTMLYAQRVSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRYrSMGnvarrKYAAMVTCMDEAVRNITWA 280
Cdd:cd16143 147 GIPaSEVLPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGKS-GAG-----PYGDFVYELDWVVGRILDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 281 LKRYGFYNNSVIIFSSDNGGQTFSGG---------SNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWY 351
Cdd:cd16143 221 LKELGLAENTLVIFTSDNGPSPYADYkelekfghdPSGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 352 PTLVGLAGGTVSVADGLDGYDVWPA-ISEGRASPRTEILHnidplynHARHGSLeggfgiwntavqaAIRVGEWKLL--T 428
Cdd:cd16143 301 ATLAAIVGQKLPDNAAEDSFSFLPAlLGPKKQEVRESLVH-------HSGNGSF-------------AIRKGDWKLIdgT 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 584042845 429 GDPGYGDWIPPQTLAAFPGSwwnlermasarqavwLFNISADPYEREDLA 478
Cdd:cd16143 361 GSGGFSYPRGKEKLGLPPGQ---------------LYNLSTDPGESNNLY 395
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-482 |
5.85e-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: 293764 [Multi-domain] Cd Length: 415 Bit Score: 252.13 E-value: 5.85e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSD-IETPTLDRLAAEGVKLENYY-IQPICTPSRSQLLTGRyqiHTGlqHSIIR----PRQ 120
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKkIKTPNLDRLAAEGMRFTQHYaGAPVCAPSRASLLTGL---HTG--HTRVRgnsePGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 121 PNCLPLDQVTLPQKLQEAGYSTHMVGKWHLGFYRKECLPTRRGFDTFLGSLTGNV--DYYT---YDNCDG---PGVCGFD 192
Cdd:cd16145 76 QDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLDQVHahNYYPeylWRNGEKvplPNNVIPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 193 LHEGENVAWGlSGQYSTMLYAQR-VSHILASHSprQPLFLYVAFQAVHTPLQSPRE----------YLYRYRSMGNVARR 261
Cdd:cd16145 156 LDEGNNAGGG-GGTYSHDLFTDEaLDFIRENKD--KPFFLYLAYTLPHAPLQVPDDgpykykpkdpGIYAYLPWPQPEKA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 262 kYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGqTFSGG---------SNWPLRGRKGTYWEGGVRGLGFVHSP 332
Cdd:cd16145 233 -YAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGP-HSEGGsehdpdffdSNGPLRGYKRSLYEGGIRVPFIARWP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 333 LLKRKRRTSRALVHITDWYPTLVGLAGgtVSVADGLDGYDVWPAI-SEGRASPRteilhniDPLYnharhgsleggFGIW 411
Cdd:cd16145 311 GKIPAGSVSDHPSAFWDFMPTLADLAG--AEPPEDIDGISLLPTLlGKPQQQQH-------DYLY-----------WEFY 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584042845 412 NTAVQAAIRVGEWKLLtgdpgygdwippqtlaafpgswwnleRMASARQAVWLFNISADPYEREDLAGQRP 482
Cdd:cd16145 371 EGGGAQAVRMGGWKAV--------------------------RHGKKDGPFELYDLSTDPGETNNLAAQHP 415
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
47-372 |
7.23e-77 |
|
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: 243.11 E-value: 7.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGS-DIETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQIHTGLQHSIIRPRQpncL 124
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNpDIKTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRHGVRGNVGNGGG---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 PLDQVTLPQKLQEAGYSTHMVGKWHlgfyrkeclptrrgfdtflgsltgnvdyytydncdgpgvcgfdlhegenvawgls 204
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 205 gqystmlyaQRVSHILASHSPRQPLFLYVAFQAVHTPLqspreylyryrsmgnvarrKYAAMVTCMDEAVRNITWALKRY 284
Cdd:cd16022 103 ---------DEAIDFIERRDKDKPFFLYVSFNAPHPPF-------------------AYYAMVSAIDDQIGRILDALEEL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 285 GFYNNSVIIFSSDNGGQTFSGGsnwpLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWYPTLVGLAGgtVSV 364
Cdd:cd16022 155 GLLDNTLIVFTSDHGDMLGDHG----LRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAG--IEP 228
|
....*...
gi 584042845 365 ADGLDGYD 372
Cdd:cd16022 229 PEGLDGRS 236
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-478 |
1.28e-73 |
|
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: 239.36 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSDI----ETPTLDRLAAEGVKLENYYIQPICTPSRSQLLTGRYQIHTGLqHSIIRPRQPN 122
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgrgaPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGL-TTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 123 CLPLDQVTLPQKLQEAGYSTHMVGKWHLGfYRKECLPTRRGFDTFLGSLtgnvdYYTYDncdgpgvcgfdlhegenvawg 202
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLG-DEDGRLPTDHGFDEFYGNL-----YHTID--------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 203 lsgQYSTmlyAQRVSHILASHSPRQPLFLYVAFQAVHTP-LQSPReylYRYRSMGNvarRKYAAMVTCMDEAVRNITWAL 281
Cdd:cd16142 133 ---EEIV---DKAIDFIKRNAKADKPFFLYVNFTKMHFPtLPSPE---FEGKSSGK---GKYADSMVELDDHVGQILDAL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 282 KRYGFYNNSVIIFSSDNGGQTFS--GGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWYPTLVGLAG 359
Cdd:cd16142 201 DELGIADNTIVIFTTDNGPEQDVwpDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 360 GTVSVADG------LDGYDVWPAIS-EGRASPRTEILhnidplynharhgsleggfgIWNTAVQAAIRVGEWKL--LTGD 430
Cdd:cd16142 281 APDPKDKLlgkdrhIDGVDQSPFLLgKSEKSRRSEFF--------------------YFGEGELGAVRWKNWKVhfKAQE 340
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 584042845 431 PGYGDWIPPQTLAAFPgswwnlermasarqavWLFNISADPYEREDLA 478
Cdd:cd16142 341 DTGGPTGEPFYVLTFP----------------LIFNLRRDPKERYDVT 372
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
45-477 |
4.08e-67 |
|
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: 223.09 E-value: 4.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 45 QPPHIIFILTDDQGYHDVGYHGSDIETPTLDRLAAEGVKLENYYIQPICTPSRSQLLTGRYQIHTGL-QHSIIRPRQPNC 123
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMgTMAELATGKPGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 124 ---LPLDQVTLPQKLQEAGYSTHMVGKWHLgfyrkeclptrrGFDTFlgsltgnvdyytydncdgpgvcgfdlhegenva 200
Cdd:cd16025 81 egyLPDSAATIAEVLKDAGYHTYMSGKWHL------------GPDDY--------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 201 wglsgqYSTMLYAQR-VSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRYR-------------------SMGNV-- 258
Cdd:cd16025 116 ------YSTDDLTDKaIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKgkydagwdalreerlerqkELGLIpa 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 259 -------------------------ARRK--YAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGqtfSGGSNW-- 309
Cdd:cd16025 190 dtkltprppgvpawdslspeekkleARRMevYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGA---SAEPGWan 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 310 ----PLRGRKGTYWEGGVRGLGFVHSP-LLKRKRRTSRALVHITDWYPTLVGLAGGTV-SVADG-----LDGYDVWPAIS 378
Cdd:cd16025 267 asntPFRLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYpKTVNGvpqlpLDGVSLLPTLD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 379 EGRASPRTEILHnidplYNHARHgsleggfgiwntavqAAIRVGEWKLLTGDPGYGDwippqtlaafPGSWwnlermasa 458
Cdd:cd16025 347 GAAAPSRRRTQY-----FELFGN---------------RAIRKGGWKAVALHPPPGW----------GDQW--------- 387
|
490
....*....|....*....
gi 584042845 459 rqavWLFNISADPYEREDL 477
Cdd:cd16025 388 ----ELYDLAKDPSETHDL 402
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
46-477 |
1.18e-62 |
|
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: 210.79 E-value: 1.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 46 PPHIIFILTDDQGYHDVGYHG--SDIETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQIHTGLQHSIIrPRQPN 122
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVGHNFL-PTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 123 CLPLDQVTLPQKLQEAGYSTHMVGKWHLGfYRKECLPTRRGFDTFLGSltgnvdyytydncdgPGVCGFDLhegenvawg 202
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLG-QREAYLPNSRGFDYYFGI---------------PFSHDSSL--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 203 lsgqysTMLYAQRVSHILASHSPR-QPLFLYVAFQAVHTPLQSPREYLYRYRsmgnvARRKYAAMVTCMDEAVRNITWAL 281
Cdd:cd16161 135 ------ADRYAQFATDFIQRASAKdRPFFLYAALAHVHVPLANLPRFQSPTS-----GRGPYGDALQEMDDLVGQIMDAV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 282 KRYGFYNNSVIIFSSDNG---------GQTFSGG--SNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDW 350
Cdd:cd16161 204 KHAGLKDNTLTWFTSDNGpwevkcelaVGPGTGDwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 351 YPTLVGLAGGTVSVADGLDGYDVWPAISEGRASPRTEILHNIDPlynHARHGSLEggfgiwntavqaAIRVGEWKLLtgd 430
Cdd:cd16161 284 FPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSG---AAGAGALS------------AVRCGDYKAH--- 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 584042845 431 pgygdWIPPQTLAAFPGSWWNLErmasaRQAVWLFNISADPYEREDL 477
Cdd:cd16161 346 -----YATGGALACCGSTGPKLY-----HDPPLLFDLEVDPAESFPL 382
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
47-359 |
1.87e-61 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 204.96 E-value: 1.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSDIE-TPTLDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLQHSIirprqPNCL 124
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPtTPFLDRLAEEGLLFSNFYSgGTLTAPSRFALLTGLPPHNFGSYVST-----PVGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 PLDQVTLPQKLQEAGYSTHMVGKWHLGFYRKEClPTRRGFDTFLGSLTGNVDYYTYDNCDGpgvcgfdlhegenvaWGLS 204
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS-PCNLGFDKFFGRNTGSDLYADPPDVPY---------------NCSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 205 GQYSTMLYAQRVSHILASHSprQPLFLYVAFQAVHTPLQSPREYLYRYRSM------GNVARRKYAAMVTCMDEAVRNIT 278
Cdd:pfam00884 140 GGVSDEALLDEALEFLDNND--KPFFLVLHTLGSHGPPYYPDRYPEKYATFkpsscsEEQLLNSYDNTLLYTDDAIGRVL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 279 WALKRYGFYNNSVIIFSSDNGGQTFSGGsNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWYPTLVGLA 358
Cdd:pfam00884 218 DKLEENGLLDNTLVVYTSDHGESLGEGG-GYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLA 296
|
.
gi 584042845 359 G 359
Cdd:pfam00884 297 G 297
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
47-492 |
3.15e-58 |
|
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: 198.89 E-value: 3.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSDIETPTLDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLQHsiIRPRQPNcLP 125
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTtAPVCSPSRSALLTGLYPHQNGAHG--LRSRGFP-LP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 126 LDQVTLPQKLQEAGYSTHMVGKWHLGFyrkeclPTRRGFDTFLGSLTGNVDYYTYdncdgpgvcgfdlhegenvawglsg 205
Cdd:cd16027 78 DGVKTLPELLREAGYYTGLIGKTHYNP------DAVFPFDDEMRGPDDGGRNAWD------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 206 qystmlYAQRVSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRYRSM----------GNVARR---KYAAMVTCMDE 272
Cdd:cd16027 127 ------YASNAADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEkvkvppylpdTPEVREdlaDYYDEIERLDQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 273 AVRNITWALKRYGFYNNSVIIFSSDNGGQtFSGGsnwplrgrKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWYP 352
Cdd:cd16027 201 QVGEILDELEEDGLLDNTIVIFTSDHGMP-FPRA--------KGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 353 TLVGLAGGTVSvaDGLDGYDVWPAISEGRASPRTEIL---HNIDPLYNHARhgsleggfgiwntavqaAIRVGEWKLLtg 429
Cdd:cd16027 272 TLLDLAGIEPP--EYLQGRSFLPLLKGEKDPGRDYVFaerDRHDETYDPIR-----------------SVRTGRYKYI-- 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584042845 430 dpgygdwippqtlaafpgswWNLERMAsarqavwLFNISADPYEREDLAGQRP--DVVRALLARL 492
Cdd:cd16027 331 --------------------RNYMPEE-------LYDLKNDPDELNNLADDPEyaEVLEELRAAL 368
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-426 |
4.85e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 193.20 E-value: 4.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVG-YHGSDIETPTLDRLAAEGVKLENYYIQPICTPSRSQLLTGRYQIHTGLQHsiirprqpNCLP 125
Cdd:cd16151 1 PNIILIMADDLGYECIGcYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVF--------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 126 LDQVTLPQKLQEAGYSTHMVGKWHLG-FYRKECLPTRRGFDTFL--GSLTGNVDYYTYDNCDGPGVCGFDLHEGEnvawg 202
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGgGRGDGDYPHEFGFDEYClwQLTETGEKYSRPATPTFNIRNGKLLETTE----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 203 lsGQYSTMLYAQrvsHIL--ASHSPRQPLFLYVAFQAVHTPLQ----SPREYLYRYRSMGNvaRRKYAAMVTCMDEAVRN 276
Cdd:cd16151 148 --GDYGPDLFAD---FLIdfIERNKDQPFFAYYPMVLVHDPFVptpdSPDWDPDDKRKKDD--PEYFPDMVAYMDKLVGK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 277 ITWALKRYGFYNNSVIIFSSDNG----GQTFSGGSNwpLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWYP 352
Cdd:cd16151 221 LVDKLEELGLRENTIIIFTGDNGthrpITSRTNGRE--VRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLP 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584042845 353 TLVGLAGGTVSVADGLDGYDVWPAISEGRASPRTEIlhnidpLYNHARHGsleggfgiWNTAVQAAIRVGEWKL 426
Cdd:cd16151 299 TLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREW------IYWYYRNP--------HKKFGSRFVRTKRYKL 358
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
45-492 |
2.93e-54 |
|
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: 189.66 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 45 QPPHIIFILTDDQGYHDVGYHGSDI-ETPTLDRLAAEGVKLEN-YYIQPICTPSRSQLLTGRYQIHTGlqhsiIRPRQPN 122
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIvKTPNIDRLAKEGVRFDNaFVTTSICAPSRASILTGQYSHRHG-----VTDNNGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 123 CLPLDQVTLPQKLQEAGYSTHMVGKWHLGFYRKEClptRRGFDTFLgSLTGNVDYYTYDNCDGPGVCGfdlHEGenvawg 202
Cdd:cd16031 76 LFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLP---PPGFDYWV-SFPGQGSYYDPEFIENGKRVG---QKG------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 203 lsgqYSTMLYAQRVSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRYR---------------------------SM 255
Cdd:cd16031 143 ----YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEdvtipepetfddddyagrpewareqrnRI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 256 GNVAR-------------RKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGgqtFSGGSnwplRGR--KGTYWE 320
Cdd:cd16031 219 RGVLDgrfdtpekyqrymKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG---FFLGE----HGLfdKRLMYE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 321 GGVRGLGFVHSPLLKRKRRTSRALVHITDWYPTLVGLAGgtVSVADGLDGYDVWPAISEGRASPRTEilhniDPLYNHar 400
Cdd:cd16031 292 ESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAG--VPIPEDMQGRSLLPLLEGEKPVDWRK-----EFYYEY-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 401 hgsLEGGFGIWNTAVQaAIRVGEWKLLTgdpgygdwippqtlaaFPGSWWNLErmasarqavwLFNISADPYEREDLAG- 479
Cdd:cd16031 363 ---YEEPNFHNVPTHE-GVRTERYKYIY----------------YYGVWDEEE----------LYDLKKDPLELNNLANd 412
|
490
....*....|....
gi 584042845 480 -QRPDVVRALLARL 492
Cdd:cd16031 413 pEYAEVLKELRKRL 426
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
46-413 |
6.66e-54 |
|
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: 189.99 E-value: 6.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 46 PPHIIFILTDDQGYHDVGYHGS-DIETPTLDRLAAEGVKLENYY-IQPICTPSRSQLLTGRYQIHTGLQHSIIRPRQP-- 121
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEpSRETPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 122 -----NCLPLDQVTLPQKLQEAGYSTHMVGKWHLGfYRKECLPTRRGFDTFLGSltGNVDYYTYDNCDGPGVCGFDlheg 196
Cdd:cd16157 81 pqnivGGIPDSEILLPELLKKAGYRNKIVGKWHLG-HRPQYHPLKHGFDEWFGA--PNCHFGPYDNKAYPNIPVYR---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 197 envAWGLSGQYS--------------TMLYAQR-VSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLyryrsmGNVARR 261
Cdd:cd16157 154 ---DWEMIGRYYeefkidkktgesnlTQIYLQEaLEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFL------GTSQRG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 262 KYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTFS----GGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRK 337
Cdd:cd16157 225 LYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISapeqGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKP 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584042845 338 RRTSRALVHITDWYPTLVGLAGGTVSVADGLDGYDVWPAISEGRASPRTEILHNIDPLYNhARHGSLEGGFGIWNT 413
Cdd:cd16157 305 GQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGDELMA-VRLGQYKAHFWTWSN 379
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-477 |
2.73e-52 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 183.54 E-value: 2.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSD-IETPTLDRLAAEGVKLENYY-IQPICTPSRSQLLTGRYQIHTGLQHsiirprqpNCL 124
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDpVKTPNLDRLAKEGVVFTNAVsNYPVCSPYRASLLTGQYPLTNGVFG--------NDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 PL--DQVTLPQKLQEAGYSTHMVGKWHL-GFYRKECL-------PTRR-GFDTFLGSLTGNvDYYT---YDNcdgpgvcg 190
Cdd:cd16034 74 PLppDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRaddytppPERRhGFDYWKGYECNH-DHNNphyYDD-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 191 fdlhEGENVAWGlsgQYSTMLYAQR-VSHILASHSPRQPLFLYVAFQAVHTPLQS-PREYLYRYRSMGNVAR-------- 260
Cdd:cd16034 145 ----DGKRIYIK---GYSPDAETDLaIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRpnvpedkk 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 261 ---------RKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTFSGGsnwplRGRKGTYWEGGVRGLGFVHS 331
Cdd:cd16034 218 eeaglredlRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHG-----LMNKQVPYEESIRVPFIIRY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 332 PLLKRKRRTSRALVHITDWYPTLVGLAGgtVSVADGLDGYDvwpaISEGRASPRTEILHNIDPLYNHArhgslEGGFGIW 411
Cdd:cd16034 293 PGKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRD----LSPLLLGGKDDEPDSVLLQCFVP-----FGGGSAR 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584042845 412 NTAVQAAIRVGEWklltgdpgygdwippqTLAAFPGSWWnlermasarqavWLFNISADPYEREDL 477
Cdd:cd16034 362 DGGEWRGVRTDRY----------------TYVRDKNGPW------------LLFDNEKDPYQLNNL 399
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
46-385 |
8.53e-52 |
|
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: 184.57 E-value: 8.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 46 PPHIIFILTDDQGYHDVGYHGSDIE-TPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQIHTGLQHSIIRPRQPNC 123
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSsTPNLDRLAANGLRFTDFYSSsPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 124 LPLDQVTLPQKLQEAGYSTHMVGKWHLGF-YRKECLPTRRGFDTFLG-----------SLTGnvdYYTYDNCDG---PGV 188
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVgLNGTYLPTHQGFDHYLGipyshdqgpcqNLTC---FPPNIPCFGgcdQGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 189 CGFDLHEGENV----AW--GLSGQYSTMLYaqrvSHILASHSPRQPLFLYVAFQAVHTPLQSPREYlyryrsMGNVARRK 262
Cdd:cd16158 158 VPCPLFYNESIvqqpVDllTLEERYAKFAK----DFIADNAKEGKPFFLYYASHHTHYPQFAGQKF------AGRSSRGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 263 YAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTF---SGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRR 339
Cdd:cd16158 228 FGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMrksRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGV 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 584042845 340 TsRALVHITDWYPTLVGLAGGTV-SVAdgLDGYDVWPAISEGRASPR 385
Cdd:cd16158 308 T-HELASTLDILPTIAKLAGAPLpNVT--LDGVDMSPILFEQGKSPR 351
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-492 |
2.21e-50 |
|
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: 177.76 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHG-SDIETPTLDRLAAEGVKLENYYIQ-----PICTPSRSQLLTGRYQIHTglqhsiirPRQ 120
Cdd:cd16155 3 PNILFILADDQRADTIGALGnPEIQTPNLDRLARRGTSFTNAYNMggwsgAVCVPSRAMLMTGRTLFHA--------PEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 121 PNC-LPLDQVTLPQKLQEAGYSTHMVGKWHLGFyrkeclptrrgFDtflgsltgnvdyytydncdgpgvcgfdlhegenv 199
Cdd:cd16155 75 GKAaIPSDDKTWPETFKKAGYRTFATGKWHNGF-----------AD---------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 200 awglsgqystmlyaQRVSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRY------------------RSMGNVA-- 259
Cdd:cd16155 110 --------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYppetiplpenflpqhpfdNGEGTVRde 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 260 ---------------RRKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGgqtFSGGSNwPLRGRKGTYwEGGVR 324
Cdd:cd16155 176 qlapfprtpeavrqhLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG---LAVGSH-GLMGKQNLY-EHSMR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 325 glgfvhSPLL-----KRKRRTSRALVHITDWYPTLVGLAGgtVSVADGLDGYDVWPAISEGRASPRteilhniDPLYNHA 399
Cdd:cd16155 251 ------VPLIisgpgIPKGKRRDALVYLQDVFPTLCELAG--IEIPESVEGKSLLPVIRGEKKAVR-------DTLYGAY 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 400 RHGsleggfgiwntavQAAIRVGEWKLLTGDPGygdwippqtlaafpgswwnLERMAsarqavwLFNISADPYEREDLAG 479
Cdd:cd16155 316 RDG-------------QRAIRDDRWKLIIYVPG-------------------VKRTQ-------LFDLKKDPDELNNLAD 356
|
490
....*....|....*
gi 584042845 480 QR--PDVVRALLARL 492
Cdd:cd16155 357 EPeyQERLKKLLAEL 371
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
47-389 |
5.07e-50 |
|
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: 178.78 E-value: 5.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSDIETPT-LDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLqHSIIRPRQPNC- 123
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGpIDDMAAEGIRFTQAYSaDSVCTPSRAALLTGRLPIRSGM-YGGTRVFLPWDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 124 --LPLDQVTLPQKLQEAGYSTHMVGKWHLGF--YRKE---CLPTRRGFDtFLGSltgNVDYYTYDNCDG---------PG 187
Cdd:cd16160 81 ggLPKTEVTMAEALKEAGYTTGMVGKWHLGIneNNHSdgaHLPSHHGFD-FVGT---NLPFTNSWACDDtgrhvdfpdRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 188 VCgFDLHEGENVAWGLSGQYSTMLYAQ-RVSHILASHspRQPLFLYVAFQAVHTPLQSPREylYRYRSMgnvaRRKYAAM 266
Cdd:cd16160 157 AC-FLYYNDTIVEQPIQHEHLTETLVGdAKSFIEDNQ--ENPFFLYFSFPQTHTPLFASKR--FKGKSK----RGRYGDN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 267 VTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQT---FSGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRtSRA 343
Cdd:cd16160 228 INEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeycLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRV-SHE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 584042845 344 LVHITDWYPTLVGLAGGTVSVADGLDGYDVWPAISEGRASPRTEIL 389
Cdd:cd16160 307 VVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDIL 352
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
46-504 |
2.72e-44 |
|
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: 164.77 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 46 PPHIIFILTDDQGYHDVGYHGSD-IETPTLDRLAAEGVKLE-NYYIQPICTPSRSQLLTGRYQIHTGLQHS-----IIRP 118
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDtIRTPNIDRLAKEGVKLThHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrvILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 119 RQPNCLPLDQVTLPQKLQEAGYSTHMVGKWHLGFYRKECL-----PTRRGFDTFLGSLTGNvdyytYDNCDGPGVCGFDl 193
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNdfchhPLNHGFDYFYGLPLTN-----LKDCGDGSNGEYD- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 194 HEGENVAWGLSG----QYSTMLYAQRVSHI-------------------------------------------------- 219
Cdd:cd16159 155 LSFDPLFPLLTAfvliTALTIFLLLYLGAVskrffvfllilsllfislfflllitnryfncilmrnhevveqpmslenlt 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 220 --LASHS-------PRQPLFLYVAFQAVHTPLQSPREYLyryrsmGNVARRKYAAMVTCMDEAVRNITWALKRYGFYNNS 290
Cdd:cd16159 235 qrLTKEAisflernKERPFLLVMSFLHVHTALFTSKKFK------GRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 291 VIIFSSDNGG--------QTFSGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWYPTLVGLAGGTV 362
Cdd:cd16159 309 FVYFTSDNGGhleeisvgGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 363 SVADGLDGYDVWPAIS-EGRASPRTEILHNIDPLYNHARHGSLEGGfgiwntavqaAIrvgeWKLLTGDPgygDWIPPQT 441
Cdd:cd16159 389 PSDRIIDGRDLMPLLTgQEKRSPHEFLFHYCGAELHAVRYRPRDGG----------AV----WKAHYFTP---NFYPGTE 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584042845 442 LAAFPGSWWNLERMASARQAVWLFNISADPYEREDLAGQ---RPDVVRALLARLVDYNRTAIPVRY 504
Cdd:cd16159 452 GCCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPTdepYQEIIKKILEAVAEHQSSIEPVES 517
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-497 |
9.30e-44 |
|
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: 159.70 E-value: 9.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 46 PPHIIFILTDDQGYHDVGYHGSDIE-TPTLDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLQHSIIRprqpnc 123
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDlTPNLDALAEEGVLFENAFTpQPVCGPARACLQTGLYPTETGCFRNGIP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 124 LPLDQVTLPQKLQEAGYSTHMVGKWHLGFYRkeclptrrgfdtflgsltgnVDYYTyDncdgpgvcgfdlhegenvawgl 203
Cdd:cd16152 75 LPADEKTLAHYFRDAGYETGYVGKWHLAGYR--------------------VDALT-D---------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 204 sgqystmlYAQRvshILASHSPRQPLFLYVAF-----QAVHTPLQSPREYLYRYRSM---GNVARRK---------YAAM 266
Cdd:cd16152 112 --------FAID---YLDNRQKDKPFFLFLSYlephhQNDRDRYVAPEGSAERFANFwvpPDLAALPgdwaeelpdYLGC 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 267 VTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQtfsggsnwpLRGRKGTY----WEGGVR------GLGFvhspllkR 336
Cdd:cd16152 181 CERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH---------FRTRNAEYkrscHESSIRvplviyGPGF-------N 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 337 KRRTSRALVHITDWYPTLVGLAGgtVSVADGLDGYDVWPAISEGRASPRTEILhnidplynharhgsleggFGIWNTAVQ 416
Cdd:cd16152 245 GGGRVEELVSLIDLPPTLLDAAG--IDVPEEMQGRSLLPLVDGKVEDWRNEVF------------------IQISESQVG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 417 AAIRVGEWKLLTGDPGYGDWippqtlaafpgswwnLERMASARQAVWLFNISADPYEREDLAGQRP--DVVRALLARLVD 494
Cdd:cd16152 305 RAIRTDRWKYSVAAPDKDGW---------------KDSGSDVYVEDYLYDLEADPYELVNLIGRPEyrEVAAELRERLLA 369
|
...
gi 584042845 495 YNR 497
Cdd:cd16152 370 RMA 372
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-417 |
1.76e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 156.36 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYhDV--GYH-GSDI-ETPTLDRLAAEGVKLENYYIQPICTPSRSQLLTGRYQIHTGlqhsIIRPrqPN 122
Cdd:cd16154 1 PNILLIIADDQGL-DSsaQYSlSSDLpVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTG----VLAV--PD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 123 CLPLDQVTLPQKL----QEAGYSTHMVGKWHLGfyrkECLPTRR---GFDTFLGSLTGNV-DYYtydncdgpgvcgfdlh 194
Cdd:cd16154 74 ELLLSEETLLQLLikdaTTAGYSSAVIGKWHLG----GNDNSPNnpgGIPYYAGILGGGVqDYY---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 195 egenvAWGL--SGQYSTM-LYAQRVSHILAS---HSPRQPLFLYVAFQAVHTPLQSP------REYLYRYRSMGNVARRK 262
Cdd:cd16154 134 -----NWNLtnNGQTTNStEYATTKLTNLAIdwiDQQTKPWFLWLAYNAPHTPFHLPpaelhsRSLLGDSADIEANPRPY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 263 YAAMVTCMD-EAVR---NITWALKrygfyNNSVIIFSSDNGGQTFSGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKR 338
Cdd:cd16154 209 YLAAIEAMDtEIGRllaSIDEEER-----ENTIIIFIGDNGTPGQVVDLPYTRNHAKGSLYEGGINVPLIVSGAGVERAN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 339 RTSRALVHITDWYPTLVGLAGGTVS-VADGLDGYdvwPAISEGRASPRTeilhnidplYNHArhgSLEGGFGIWNTAVQA 417
Cdd:cd16154 284 ERESALVNATDLYATIAELAGVDAAeIHDSVSFK---PLLSDVNASTRQ---------YNYT---EYESPTTTGWATRNQ 348
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-370 |
2.05e-40 |
|
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: 147.39 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHG-SDIETPTLDRLAAEGVKLENYY-IQPICTPSRSQLLTGRYQ----IHTGL-QHSIIRPR 119
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGnSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRMPsqhgIHDWIvEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 120 QPNCLPLDQVTLPQKLQEAGYSTHMVGKWHLGfyrkeclptrrgfdtflgsltgnvdyytydncdgpgvcgfdlhegenv 199
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 200 awglsgqystmlyAQRVSHILASHSPRQPLFLYVAFQAVHTPLQspreylyryrsmgnvarrkYAAMVTCMDEAVRNITW 279
Cdd:cd16149 113 -------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------------YFAAVTGVDRNVGRLLD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 280 ALKRYGFYNNSVIIFSSDNGgqtFSGGSN---------WPLrgrkgTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDW 350
Cdd:cd16149 161 ELEELGLTENTLVIFTSDNG---FNMGHHgiwgkgngtFPL-----NMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDF 232
|
330 340
....*....|....*....|
gi 584042845 351 YPTLVGLAGGTVSVADGLDG 370
Cdd:cd16149 233 FPTLLELAGVDPPADPRLPG 252
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
47-494 |
4.38e-40 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 152.13 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSD-IETPTLDRLAAEGVKLEN-YYIQPICTPSRSQLLTGRYQIHTGlqhsiiRPRQPNCL 124
Cdd:PRK13759 7 PNIILIMVDQMRGDCLGCNGNKaVETPNLDMLASEGYNFENaYSAVPSCTPARAALLTGLSQWHHG------RVGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 PLD-QVTLPQKLQEAGYSTHMVGKWHLGFYRKEClptrrGFDTFL---GSLTG--NVDYYTYDNCD---------GPGV- 188
Cdd:PRK13759 81 PWNyKNTLPQEFRDAGYYTQCIGKMHVFPQRNLL-----GFHNVLlhdGYLHSgrNEDKSQFDFVSdylawlrekAPGKd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 189 -----CGFDLHEGENVAWGLSGQY-STMLYAQRVSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRYR--------- 253
Cdd:PRK13759 156 pdltdIGWDCNSWVARPWDLEERLhPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYKdadipdphi 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 254 ------------------SMGNV-------ARRKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTfsGGSN 308
Cdd:PRK13759 236 gdweyaedqdpeggsidaLRGNLgeeyarrARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDML--GDHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 309 WplrGRKGTYWEGGVRGLGFVHSP---LLKRKRRTSRALVHITDWYPTLVGLAGGTvsVADGLDGYDVWPAISEGRASPR 385
Cdd:PRK13759 314 L---FRKGYPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGT--IPDDVDGRSLKNLIFGQYEGWR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 386 TEIlhnidplynHARHGSLEGGFGiWNTAvqaairvGEWKLLtgdpgygdwippqtlaafpgsWWnlermaSARQAVWLF 465
Cdd:PRK13759 389 PYL---------HGEHALGYSSDN-YLTD-------GKWKYI---------------------WF------SQTGEEQLF 424
|
490 500 510
....*....|....*....|....*....|.
gi 584042845 466 NISADPYEREDLAG--QRPDVVRALLARLVD 494
Cdd:PRK13759 425 DLKKDPHELHNLSPseKYQPRLREMRKKLVD 455
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-494 |
4.07e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 148.14 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSDI-ETPTLDRLAAEGVKLENYY-IQPICTPSRSQLLTGRYQIHTGLQHSIIRP--RQPN 122
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNAYtPSPVCCPARASLLTGLYPHEHGVLNNVENAgaYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 123 cLPLDQVTLPQKLQEAGYSTHMVGKWHLGfyrKECLPTRRGFDTFLGSLTgNVDYYTydncdgpgvcgfdlhegenvawg 202
Cdd:cd16033 81 -LPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFDEYLPVET-TIEYFL----------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 203 lsgqystmlyAQRVSHILASHSPR-QPLFLYVAFQAVHTPLQSPREYL-------------------------YRYRSMG 256
Cdd:cd16033 133 ----------ADRAIEMLEELAADdKPFFLRVNFWGPHDPYIPPEPYLdmydpediplpesfaddfedkpyiyRRERKRW 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 257 NV----------ARRKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGqtfSGGSNwplRG-RKGTY-WEGGVR 324
Cdd:cd16033 203 GVdtedeedwkeIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGD---ALGAH---RLwDKGPFmYEETYR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 325 GLGFVHSPLLKRKRRTSRALVHITDWYPTLVGLAGgtVSVADGLDGYDVWPaISEGRASP--RTEILHNIdplynharHG 402
Cdd:cd16033 277 IPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAG--VDVPPKVDGRSLLP-LLRGEQPEdwRDEVVTEY--------NG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 403 SLEGGFgiwntavQAAIRVGEWKLLTGDPGYGDwippqtlaafpgswwnlermasarqavwLFNISADPYEREDLAGQRP 482
Cdd:cd16033 346 HEFYLP-------QRMVRTDRYKYVFNGFDIDE----------------------------LYDLESDPYELNNLIDDPE 390
|
490
....*....|....
gi 584042845 483 --DVVRALLARLVD 494
Cdd:cd16033 391 yeEILREMRTRLYE 404
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-472 |
3.97e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 143.07 E-value: 3.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSD-IETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQIHTGLQHsiirprqpNCL 124
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPvVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETGVWD--------NAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 PLD--QVTLPQKLQEAGYSTHMVGKWHlgfYRKECLPTrrGFDtflgsltgnvdyytYDncdgpgvcgfdlhegENVAwg 202
Cdd:cd16037 73 PYDgdVPSWGHALRAAGYETVLIGKLH---FRGEDQRH--GFR--------------YD---------------RDVT-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 203 lsgqystmlyaQRVSHILASHSPR-QPLFLYVAFQAVHTPLQSPREYLYRYRsmgNVARRKYAAMVTCMDEAVRNITWAL 281
Cdd:cd16037 117 -----------EAAVDWLREEAADdKPWFLFVGFVAPHFPLIAPQEFYDLYV---RRARAAYYGLVEFLDENIGRVLDAL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 282 KRYGFYNNSVIIFSSDNGGQTFSGGSNWplrgrKGTYWEGGVR------GLGFVHSpllkrkrRTSRALVHITDWYPTLV 355
Cdd:cd16037 183 EELGLLDNTLIIYTSDHGDMLGERGLWG-----KSTMYEESVRvpmiisGPGIPAG-------KRVKTPVSLVDLAPTIL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 356 GLAGgtVSVADGLDGYDVWPAISEGRASPRT---EilhnidplYnHArHGSLEGGFgiwntavqaAIRVGEWKLLTgdpg 432
Cdd:cd16037 251 EAAG--APPPPDLDGRSLLPLAEGPDDPDRVvfsE--------Y-HA-HGSPSGAF---------MLRKGRWKYIY---- 305
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 584042845 433 YGDWiPPQtlaafpgswwnlermasarqavwLFNISADPY 472
Cdd:cd16037 306 YVGY-PPQ-----------------------LFDLENDPE 321
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
46-375 |
7.47e-35 |
|
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: 135.76 E-value: 7.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 46 PPHIIFILTDDQgyhDVGYHGSDIETPTLDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLQHsIIRPrqPNCL 124
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMPKTKKLLADQGTTFTNAFVtTPLCCPSRASILTGQYAHNHGVTN-NSPP--GGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 P------LDQVTLPQKLQEAGYSTHMVGKwHLGFYRKECLPTR--RGFDTFLGSLTGNVDYYTYDNCDGPGVCGFDLHeg 196
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGK-YLNGYGVPGGVSYvpPGWDEWDGLVGNSTYYNYTLSNGGNGKHGVSYP-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 197 envawglsGQYSTMLYAQR-VSHILASHSPRQPLFLYVAFQAVHTPLQSPREYLYRYR---------------------- 253
Cdd:cd16147 152 --------GDYLTDVIANKaLDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFPnvtapprpppnnpdvsdkphwl 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 254 ------SMGNVAR-----RKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNG---GQtFSggsnwpLRGRKGTYW 319
Cdd:cd16147 224 rrlpplNPTQIAYidelyRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQ-HR------LPPGKRTPY 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584042845 320 EGGVRglgfVhsPLLKR-----KRRTSRALVHITDWYPTLVGLAGGTV-SVADGLDGYDVWP 375
Cdd:cd16147 297 EEDIR----V--PLLVRgpgipAGVTVDQLVSNIDLAPTILDLAGAPPpSDMDGRSCGDSNN 352
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-372 |
1.63e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 126.34 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGS-----------DIETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQIHTG---- 110
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNahtgksesrlgYVESPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGvygf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 111 -LQHSIIRPRQPnclpldqvTLPQKLQEAGYSTHMVGKWHlgfyrkeclptrrgFDTFLgSLTGNvDYYTYDNCDGpgvc 189
Cdd:cd16153 82 eAAHPALDHGLP--------TFPEVLKKAGYQTASFGKSH--------------LEAFQ-RYLKN-ANQSYKSFWG---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 190 gfdlhegeNVAWGLsgqystmlyaqrvshilashSPRQPLFLYVAFQAVHTPLQSPREYLYRYRsmgnvarrkYAAMVTC 269
Cdd:cd16153 134 --------KIAKGA--------------------DSDKPFFVRLSFLQPHTPVLPPKEFRDRFD---------YYAFCAY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 270 MDEAVRNITWALKRYGFYN---NSVIIFSSDNGGQTFSGGSNwplrgRKGTYWEGGVRG-LGFVHSPLLKRKRRTSRA-L 344
Cdd:cd16153 177 GDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGIL-----AKFTFWPQSHRVpLIVVSSDKLKAPAGKVRHdF 251
|
330 340
....*....|....*....|....*...
gi 584042845 345 VHITDWYPTLVGLAGGTVSVADGLDGYD 372
Cdd:cd16153 252 VEFVDLAPTLLAAAGVDVDAPDYLDGRD 279
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
47-389 |
5.41e-31 |
|
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: 123.07 E-value: 5.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDdQGYHDV--GYHGSDIETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYqihtglqhsiirPRQPNC 123
Cdd:cd16032 1 PNILLIMAD-QLTAAAlpAYGNTVVKTPNLDRLAARGVVFDNAYCNsPLCAPSRASMMTGRL------------PSRIGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 124 ------LPLDQVTLPQKLQEAGYSTHMVGKWHlgfyrkeclptrrgfdtFLG--SLTGnvdyYTYDncdgpgvcgfdlhe 195
Cdd:cd16032 68 ydnaaeFPADIPTFAHYLRAAGYRTALSGKMH-----------------FVGpdQLHG----FDYD-------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 196 gENVAWglsgqystmlYAQRVSHILASHSPRQPLFLYVAFQAVHTPLQSPREY--LYRYRsmgnvARRKYAAMVTCMDEA 273
Cdd:cd16032 113 -EEVAF----------KAVQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQEYwdLYVRR-----ARRAYYGMVSYVDDK 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 274 VRNITWALKRYGFYNNSVIIFSSDNG---GQtfsggsnwplRGR--KGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHIt 348
Cdd:cd16032 177 VGQLLDTLERTGLADDTIVIFTSDHGdmlGE----------RGLwyKMSFFEGSARVPLIISAPGRFAPRRVAEPVSLV- 245
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 584042845 349 DWYPTLVGLAGG-TVSVADGLDGYDVWPAISEGRASPRTEIL 389
Cdd:cd16032 246 DLLPTLVDLAGGgTAPHVPPLDGRSLLPLLEGGDSGGEDEVI 287
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-375 |
1.70e-28 |
|
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: 114.57 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVG-YHGSDIETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQIHTGLQHSIIRPRQPncl 124
Cdd:cd16148 1 MNVILIVIDSLRADHLGcYGYDRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGVWGGPLEPDDP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 pldqvTLPQKLQEAGYSTHMVGKW-HLGFYRkeclPTRRGFDTFLGsltgnvdyytydncdgpgvcgFDLHEGENVAWGL 203
Cdd:cd16148 78 -----TLAEILRKAGYYTAAVSSNpHLFGGP----GFDRGFDTFED---------------------FRGQEGDPGEEGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 204 SGQYSTMlyaQRVSHILASHSPRQPLFLYVAFQAVHTPlqspreylYRYRsmgnvarrkyaAMVTCMDEAVRNITWALKR 283
Cdd:cd16148 128 ERAERVT---DRALEWLDRNADDDPFFLFLHYFDPHEP--------YLYD-----------AEVRYVDEQIGRLLDKLKE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 284 YGFYNNSVIIFSSDNG------GQTFSGGSNW-------PLrgrkgtyweggvrglgFVHSPLLKRKRRTSrALVHITDW 350
Cdd:cd16148 186 LGLLEDTLVIVTSDHGeefgehGLYWGHGSNLydeqlhvPL----------------IIRWPGKEPGKRVD-ALVSHIDI 248
|
330 340
....*....|....*....|....*
gi 584042845 351 YPTLVGLAGGTVSvaDGLDGYDVWP 375
Cdd:cd16148 249 APTLLDLLGVEPP--DYSDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
45-370 |
2.03e-25 |
|
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: 109.20 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 45 QPPHIIFILTDDQGyHDVG-YHGSDIETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQIHTGLQ--HSIIRPRQ 120
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGcYGGHPAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTGVYdnNSYFRKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 121 PnclplDQVTLPQKLQEAGYSTHMVGK-WHLGFYRKECLPtrRGFDTFLGSLTGNVDYYTYDNCDGPGVCGFDLHEGENV 199
Cdd:cd16030 80 P-----DAVTLPQYFKENGYTTAGVGKiFHPGIPDGDDDP--ASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 200 AWGLSGQYSTMLYAQRVSHILASHSPR-QPLFLYVAFQAVHTPLQSPREYLYRY-------------------------- 252
Cdd:cd16030 153 ADVPDEAYPDGKVADEAIEQLRKLKDSdKPFFLAVGFYKPHLPFVAPKKYFDLYplesiplpnpfdpidlpevawndldd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 253 -RSMGNV-------------------ARRKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGgqtFSGG--SNWp 310
Cdd:cd16030 233 lPKYGDIpalnpgdpkgplpdeqareLRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG---WHLGehGHW- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 311 lrgRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALVHITDWYPTLVGLAGgtVSVADGLDG 370
Cdd:cd16030 309 ---GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEG 363
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-400 |
3.15e-25 |
|
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: 106.14 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVgYHGSDIET--PTLDRLAAEGVKLENYYI-QPICTPSRSQLLTGRYQIHTGLQHSIIRPRQPNc 123
Cdd:cd16035 1 PNILLILTDQERYPPP-WPAGWAALnlPARERLAANGLSFENHYTaACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 124 LPLDQVTLPQKLQEAGYSTHMVGKWHLGfyrkeclptrrgfdtflgsltgnvdyytydncdgpgvcgfdlhegeNVAWGl 203
Cdd:cd16035 79 LSPDVPTLGHMLRAAGYYTAYKGKWHLS----------------------------------------------GAAGG- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 204 sGQYSTMLYAQRVSHILASHSP----RQPLFLYVAF---QAVHTPLQSPREYLYRyrsmgnvaRRKYAAMVTCMDEAVRN 276
Cdd:cd16035 112 -GYKRDPGIAAQAVEWLRERGAknadGKPWFLVVSLvnpHDIMFPPDDEERWRRF--------RNFYYNLIRDVDRQIGR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 277 ITWALKRYGFYNNSVIIFSSDNGGQTFSGGsnwpLRGRKGTYWEGGVRGLGFVHSPLLKRKRRTSRALV-HItDWYPTLV 355
Cdd:cd16035 183 VLDALDASGLADNTIVVFTSDHGEMGGAHG----LRGKGFNAYEEALHVPLIISHPDLFGTGQTTDALTsHI-DLLPTLL 257
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 584042845 356 GLAGG----TVSVADGLDGYDVWPAISEGRASP-RTEILHNIDpLYNHAR 400
Cdd:cd16035 258 GLAGVdaeaRATEAPPLPGRDLSPLLTDADADAvRDGILFTYD-RYKFAR 306
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
47-253 |
2.26e-24 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 106.31 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVG-YHGSDIETPTLDRLAAEGVKLEN-YYIQPICTPSRSQLLTGRYQiHTGLQHSiirprqpNCL 124
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcYGNKAMKTPNLDRLAAEGVRFDSaYTTQPVCGPARSGLFTGLYP-HTNGSWT-------NCM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 PL-DQV-TLPQKLQEAGYSTHMVGKWHLG----FYRKECLPtrrGFDTflgsltgnvDYYtYDncdgpGVCGFD-LHEGE 197
Cdd:cd16156 73 ALgDNVkTIGQRLSDNGIHTAYIGKWHLDggdyFGNGICPQ---GWDP---------DYW-YD-----MRNYLDeLTEEE 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584042845 198 NVAWGL---SGQYSTM----LYAQRVSH----ILASHSpRQPLFLYVAFQAVHTPLQSPREYLYRYR 253
Cdd:cd16156 135 RRKSRRgltSLEAEGIkeefTYGHRCTNraldFIEKHK-DEDFFLVVSYDEPHHPFLCPKPYASMYK 200
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-359 |
4.95e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 104.62 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSD-IETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRY---QIHTGLQHsIIRPRQP 121
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPaAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGWYphvNGHRTLHH-LLRPDEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 122 NCLpldqvtlpQKLQEAGYSTHMVGKWHlgfyrkeCLPTRRGFDTFLGSLTGNVDYytydncdgpgvcgfdlhegeNVAW 201
Cdd:cd16150 80 NLL--------KTLKDAGYHVAWAGKND-------DLPGEFAAEAYCDSDEACVRT--------------------AIDW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 202 glsgqystmlyaqrvshiLASHSPRQPLFLYVAFQAVHTPLQSPREYLYRY-------------RSMGNVARRK------ 262
Cdd:cd16150 125 ------------------LRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIdreklpprrppglRAKGKPSMLEgiekqg 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 263 ---------------YAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTfsggsnwplrgrkGTY-----WEGG 322
Cdd:cd16150 187 ldrwseerwrelratYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT-------------GDYglvekWPNT 253
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 584042845 323 VRGLgFVHSPLLKR-----KRRTSRALVHITDWYPTLVGLAG 359
Cdd:cd16150 254 FEDC-LTRVPLIIKppggpAGGVSDALVELVDIPPTLLDLAG 294
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
69-497 |
1.74e-19 |
|
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: 91.17 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 69 IETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGRYQihtgLQHSIIRPRQPncLPLDQVTLPQKLQEAGYSTHMVGK 147
Cdd:cd16028 24 VKTPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRYL----MNHRSVWNGTP--LDARHLTLALELRKAGYDPALFGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 148 WHLGfyrkeclPTRRGFDTFLGSLTGnvdyytydncDGPGVCGFD---LHEGenVAWGLSgqySTMLYAQRVSHILASHs 224
Cdd:cd16028 98 TDTS-------PDPRGLAPLDPRLLS----------YELAMPGFDpvdRLDE--YPAEDS---DTAFLTDRAIEYLDER- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 225 PRQPLFLYVAFQAVHTPLQSPREY--LYRYRSMGNVARRK---------------------------------------- 262
Cdd:cd16028 155 QDEPWFLHLSYIRPHPPFVAPAPYhaLYDPADVPPPIRAEslaaeaaqhpllaaflerieslsfspgaanaadlddeeva 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 263 -----YAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQtfsGGSNWpLRGrKGTYWEGGvrglgfVHSPLLKRK 337
Cdd:cd16028 235 qmratYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ---LGDHW-LWG-KDGFFDQA------YRVPLIVRD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 338 RRTSR---------ALVHITDWYPTLVGLAGGTVSVAdgLDGYDVWPAISEGRAS-PRTEILHNIDplYNHARHGSLEGG 407
Cdd:cd16028 304 PRREAdatrgqvvdAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGAQPSdWRDAVHYEYD--FRDVSTRRPQEA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 408 FGI-WNTAVQAAIRVGEWKLLTgdpgYGDwIPPQtlaafpgswwnlermasarqavwLFNISADPYEREDLAGqRPD--- 483
Cdd:cd16028 380 LGLsPDECSLAVIRDERWKYVH----FAA-LPPL-----------------------LFDLKNDPGELRDLAA-DPAyaa 430
|
490
....*....|....
gi 584042845 484 VVRALLARLVDYNR 497
Cdd:cd16028 431 VVLRYAQKLLSWRM 444
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
47-359 |
5.84e-16 |
|
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: 78.49 E-value: 5.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFI----LTDDqgYHDVGYHGSDIeTPTLDRLAAEGVKLENYYiQPICTP--SRSQ--LLTGRYQIHTGLQHSIIRP 118
Cdd:cd16015 1 PNVIVIllesFSDP--YIDKDVGGEDL-TPNLNKLAKEGLYFGNFY-SPGFGGgtANGEfeVLTGLPPLPLGSGSYTLYK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 119 RQPnclpldQVTLPQKLQEAGYSTHMVGKWHLGFY-RKECLPtRRGFDTFlgsltgnvdyYTYDNcdgpgvcgFDLHEGE 197
Cdd:cd16015 77 LNP------LPSLPSILKEQGYETIFIHGGDASFYnRDSVYP-NLGFDEF----------YDLED--------FPDDEKE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 198 NVAWGLSGQYstmLYaQRVSHILASHSPrQPLFLYVafqaV----HTPLQSPREYLYRYRSMGNVAR--RKYAAMVTCMD 271
Cdd:cd16015 132 TNGWGVSDES---LF-DQALEELEELKK-KPFFIFL----VtmsnHGPYDLPEEKKDEPLKVEEDKTelENYLNAIHYTD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 272 EAVRN-ITWaLKRYGFYNNSVIIFSSD---NGGQTFSGGSNWPLRGRKGTYweggvrglgFVHSPLLKRKRRTSRALVHI 347
Cdd:cd16015 203 KALGEfIEK-LKKSGLYENTIIVIYGDhlpSLGSDYDETDEDPLDLYRTPL---------LIYSPGLKKPKKIDRVGSQI 272
|
330
....*....|..
gi 584042845 348 tDWYPTLVGLAG 359
Cdd:cd16015 273 -DIAPTLLDLLG 283
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
47-358 |
3.15e-13 |
|
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: 69.37 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSDIE-TPTLDRLAAEGVKLENYYIQPIC--TPSRSQLLTGRYQIHTGL-QHSIIRPRQPN 122
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPtTPNLKRLASEGATFNFRSVSPPTssAPNHAALLTGAYPTLHGYtGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 123 C---LPLDQVTLPQKLQEAGYSTHMVGKWhlgfyrkeclptrrgfdtflgsltgnvdyytydncdgpgvcgfdlhegenv 199
Cdd:cd00016 81 RaagKDEDGPTIPELLKQAGYRTGVIGLL--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 200 awglsgqysTMLYAQRVSHilashsprqPLFLYVAFQAVHTPLQSPREYLYRYrsmgnvarrkyAAMVTCMDEAVRNITW 279
Cdd:cd00016 110 ---------KAIDETSKEK---------PFVLFLHFDGPDGPGHAYGPNTPEY-----------YDAVEEIDERIGKVLD 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584042845 280 ALKRYGFYNNSVIIFSSDNGGqTFSGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKrRTSRALVHITDWYPTLVGLA 358
Cdd:cd00016 161 ALKKAGDADDTVIIVTADHGG-IDKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKG-GVKHELISQYDIAPTLADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
32-359 |
6.55e-12 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 68.14 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 32 PTEASEQPSVAPPQPPHIIFILTDDQGYHDVGYHGSDIE-TPTLDRLAAEGVKLENYYiqpictpsrSQllTGR-----Y 105
Cdd:COG1368 220 KSNRPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDvTPFLDSLAKESLYFGNFY---------SQ--GGRtsrgeF 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 106 QIHTGL----QHSIIRPRQPNclplDQVTLPQKLQEAGYSTHMvgkWH---LGFY-RKECLPtRRGFDTFlgsltgnVDY 177
Cdd:COG1368 289 AVLTGLpplpGGSPYKRPGQN----NFPSLPSILKKQGYETSF---FHggdGSFWnRDSFYK-NLGFDEF-------YDR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 178 YTYDNcdgpgvcgfdlheGENVAWGLSGQYstmlYAQRVSHILASHSprQPLFLYVAFQAVHTPLQSPREYlYRYRSMGN 257
Cdd:COG1368 354 EDFDD-------------PFDGGWGVSDED----LFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEED-KKIPDYGK 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 258 VARRKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGqtFSGGSNW----------PLrgrkgtyweggvrglg 327
Cdd:COG1368 414 TTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP--RSPGKTDyenpleryrvPL---------------- 475
|
330 340 350
....*....|....*....|....*....|..
gi 584042845 328 FVHSPLLKRKRRTSRALVHItDWYPTLVGLAG 359
Cdd:COG1368 476 LIYSPGLKKPKVIDTVGSQI-DIAPTLLDLLG 506
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
47-471 |
9.01e-11 |
|
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: 63.71 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 47 PHIIFILTDDQGYHDVGYHGSD-IETPTLDRLAAEGVKLENYYIQ-PICTPSRSQLLTGryqIHTGLQHSIirpRQPNCL 124
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQvVDLPYINFMKQHGSVFLNAYTNsPICCPSRAAMWSG---LFTHLTESW---NNYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 125 PLDQVTLPQKLQEAGYSTHMVGKwhlgfyrkeclptrrgFDTFLG--SLTGNVDYYTYDncdgpgvCGFDL-HEGENVAw 201
Cdd:cd16171 75 DPNYPTWMDRLEKHGYHTQKYGK----------------LDYTSGhhSVSNRVEAWTRD-------VPFLLrQEGRPTV- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 202 GLSGQYSTM-----------LYAQRVSHILASHSprQPLFLYVAFQAVHtPLQSPreylyryrSMGNVA------RRKYA 264
Cdd:cd16171 131 NLVGDRSTVrvmlkdwqntdKAVHWIRKEAPNLT--QPFALYLGLNLPH-PYPSP--------SMGENFgsirniRAFYY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 265 AMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTFSGGSNWplrgrKGTYWEGGvrglgfVHSPLLK-----RKRR 339
Cdd:cd16171 200 AMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFY-----KMSMYEGS------SHVPLLImgpgiKAGQ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584042845 340 TSRALVHITDWYPTLVGLAGgtVSVADGLDGYDVWPAISEgrASPRTEILHNIDPLYNHAR-HGSleggfgiwN-TAVQA 417
Cdd:cd16171 269 QVSDVVSLVDIYPTMLDIAG--VPQPQNLSGYSLLPLLSE--SSIKESPSRVPHPDWVLSEfHGC--------NvNASTY 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 584042845 418 AIRVGEWKLLT-GDpgyGDWIPPQtlaafpgswwnlermasarqavwLFNISADP 471
Cdd:cd16171 337 MLRTNSWKYIAyAD---GNSVPPQ-----------------------LFDLSKDP 365
|
|
| |
