|
Name |
Accession |
Description |
Interval |
E-value |
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
74-507 |
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: 613.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLENYYVQPICTPSRSQFITGKYQIHTGLQHSIIRPTQPNCLP 152
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDqIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 153 LDNATLPQKLKEVGYSTHMVGKWHLGFYRKDCMPTKRGFDTFFGSLLGSGDYYTHYKCDSPGVCGYDLYENDNAAWDYdN 232
Cdd:cd16029 81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGNDDLRDNEEPAWDY-N 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 233 GIYSTQMYTQRVQQILATHDPTKPLFLYVAYQAVHSPLQAPGRYFEHY----RSIININRRRYAAMLSCLDEAIHNVTLA 308
Cdd:cd16029 160 GTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYedkfAHIKDEDRRTYAAMVSALDESVGNVVDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 309 LKRYGFYNNSIIIYSSDNGGQPTAG--GSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNK-GTVCKELVHITDWYPTLISL 385
Cdd:cd16029 240 LKAKGMLDNTLIVFTSDNGGPTGGGdgGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 386 AEGQIDEDIQLDGYDIWETISEGLRSPRVDILHNIDPIYTkakngswaagygiwnTAIQSAIRVQHWKLLTGNPgysdwv 465
Cdd:cd16029 320 AGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDITR---------------TTGGAAIRVGDWKLIVGKP------ 378
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 77416378 466 ppqafsnlgpnrwhneritlstgksiwLFNITADPYERVDLS 507
Cdd:cd16029 379 ---------------------------LFNIENDPCERNDLA 393
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
73-507 |
7.35e-94 |
|
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: 293.70 E-value: 7.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTGLQHSIIRPTQPNC 150
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPlIKTPNIDRLAAEGVRFTDFYAaAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 151 LPLDNATLPQKLKEVGYSTHMVGKWHLGFyRKDCMPTKRGFDTFFGsLLGSGD--YYTHYKCDSPGvCGYDLYENDNA-A 227
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGH-QPEFLPTRHGFDEYFG-IPYSNDmwPFPLYRNDPPG-PLPPLMENEEViE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 228 WDYDngiYS--TQMYTQRVQQILATHDPtKPLFLYVAYQAVHSPLQAPGRYFEHYRsiininRRRYAAMLSCLDEAIHNV 305
Cdd:cd16026 158 QPAD---QSslTQRYTDEAVDFIERNKD-QPFFLYLAHTMPHVPLFASEKFKGRSG------AGLYGDVVEELDWSVGRI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 306 TLALKRYGFYNNSIIIYSSDNG---GQPTAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTL 382
Cdd:cd16026 228 LDALKELGLEENTLVIFTSDNGpwlEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 383 ISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHNIDpiytkakngswaagygiwNTAIQsAIRVQHWKLLtgnpgys 462
Cdd:cd16026 308 AALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYD------------------GGDLQ-AVRSGRWKLH------- 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 77416378 463 dwVPPQAFSNLGPNRWHNeritlSTGKSIWLFNITADPYERVDLS 507
Cdd:cd16026 362 --LPTTYRTGTDPGGLDP-----TKLEPPLLYDLEEDPGETYNVA 399
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
64-527 |
6.19e-93 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 291.01 E-value: 6.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 64 PEAGTAGTSQPHLIFILADDQGFRDVGYHGS-EIKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQIHTGLQHs 141
Cdd:COG3119 14 AAAAAAAAKRPNILFILADDLGYGDLGCYGNpLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHRTGVTD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 142 iIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLgfyrkdcmptkrgfdtffgsllgsgdyythykcdspgvcgydly 221
Cdd:COG3119 93 -NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 222 endnaawdydngiYSTQMYTQRVQQILATH-DPTKPLFLYVAYQAVHSPLQAPGRYFEHYR-----------------SI 283
Cdd:COG3119 128 -------------YLTDLLTDKAIDFLERQaDKDKPFFLYLAFNAPHAPYQAPEEYLDKYDgkdiplppnlaprdlteEE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 284 ININRRRYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQPTAGGsnwpLRGSKGTYWEGGIRAVGFVHSPLLK 363
Cdd:COG3119 195 LRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHG----LRGGKGTLYEGGIRVPLIVRWPGKI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 364 NKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDGYDIWETISEGLRSPRvdilhniDPIYTkakngSWAAGYGiwntai 443
Cdd:COG3119 271 KAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWR-------DYLYW-----EYPRGGG------ 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 444 QSAIRVQHWKLLtgnpgysdwvppqafsnlgpnRWHNEritlstGKSIWLFNITADPYERVDLSSRYPGIVKKLLRRLSQ 523
Cdd:COG3119 331 NRAIRTGRWKLI---------------------RYYDD------DGPWELYDLKNDPGETNNLAADYPEVVAELRALLEA 383
|
....
gi 77416378 524 FNKT 527
Cdd:COG3119 384 WLKE 387
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
74-524 |
3.12e-92 |
|
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: 290.21 E-value: 3.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTGLQHSI--------- 142
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKfYETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 143 ---IRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFyRKDCMPTKRGFD-TFFGSLLGSGDYYThykcDSPGVCGY 218
Cdd:cd16144 81 tklIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGG-EGGYGPEDQGFDvNIGGTGNGGPPSYY----FPPGKPNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 219 DLYendnaawDYDNGIYSTQMYTQRVQQILATHDpTKPLFLYVAYQAVHSPLQAPGRYFEHYRSIININRRR-----YAA 293
Cdd:cd16144 156 DLE-------DGPEGEYLTDRLTDEAIDFIEQNK-DKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRKGqknpvYAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 294 MLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQPTAGG---SNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCK 370
Cdd:cd16144 228 MIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGpptSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 371 ELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETIS-EGLRSPRvdilhniDPIYtkakngsW-AAGYGIWNTAIQSAIR 448
Cdd:cd16144 308 VPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKgGEADLPR-------RALF-------WhFPHYHGQGGRPASAIR 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77416378 449 VQHWKLLtgnpgysdwvppqafsnlgpnRWHNeritlstGKSIWLFNITADPYERVDLSSRYPGIVKKLLRRLSQF 524
Cdd:cd16144 374 KGDWKLI---------------------EFYE-------DGRVELYNLKNDIGETNNLAAEMPEKAAELKKKLDAW 421
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
74-524 |
1.03e-89 |
|
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: 283.29 E-value: 1.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLENYYVQPICTPSRSQFITGKYQIHTGLQHSII-RptqpNCL 151
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPiLKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTILgR----ERM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 PLDNATLPQKLKEVGYSTHMVGKWHLGF---YRkdcmPTKRGFDTFFGSLLGS-GDYYTHYKCDSPgvcgYDLYENdNAA 227
Cdd:cd16146 77 RLDETTLAEVFKDAGYRTGIFGKWHLGDnypYR----PQDRGFDEVLGHGGGGiGQYPDYWGNDYF----DDTYYH-NGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 228 WDYDNGiYSTQMYTQRVQQILATHDpTKPLFLYVAYQAVHSPLQAPGRYFEHYRSI-ININRRRYAAMLSCLDEAIHNVT 306
Cdd:cd16146 148 FVKTEG-YCTDVFFDEAIDFIEENK-DKPFFAYLATNAPHGPLQVPDKYLDPYKDMgLDDKLAAFYGMIENIDDNVGRLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 307 LALKRYGFYNNSIIIYSSDNGGQP-TAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISL 385
Cdd:cd16146 226 AKLKELGLEENTIVIFMSDNGPAGgVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 386 AEGQIDEDIQLDGYDIWETISEGLRS--PRVDILHNIDPIYTKAKNGswaagygiwntaiQSAIRVQHWKLltgnpgysd 463
Cdd:cd16146 306 CGVKLPEGIKLDGRSLLPLLKGESDPwpERTLFTHSGRWPPPPKKKR-------------NAAVRTGRWRL--------- 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77416378 464 wvppqafsnLGPNRWHNEritlstgksiwLFNITADPYERVDLSSRYPGIVKKLLRRLSQF 524
Cdd:cd16146 364 ---------VSPKGFQPE-----------LYDIENDPGEENDVADEHPEVVKRLKAAYEAW 404
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
74-511 |
7.98e-74 |
|
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: 242.11 E-value: 7.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKyqiHTGlqHSIIR----PTQ 147
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKkIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGL---HTG--HTRVRgnsePGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 148 PNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKDCMPTKRGFDTFFGSL--LGSGDYYTHY------KCDSPGVCGYD 219
Cdd:cd16145 76 QDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLdqVHAHNYYPEYlwrngeKVPLPNNVIPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 220 LYENDNAawDYDNGIYSTQMYTQRVQQILATHDpTKPLFLYVAYQAVHSPLQAPGRYFEHYRSII---------NINRRR 290
Cdd:cd16145 156 LDEGNNA--GGGGGTYSHDLFTDEALDFIRENK-DKPFFLYLAYTLPHAPLQVPDDGPYKYKPKDpgiyaylpwPQPEKA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 291 YAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQPTAGG--------SNWPLRGSKGTYWEGGIRAVGFVHSPLL 362
Cdd:cd16145 233 YAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSehdpdffdSNGPLRGYKRSLYEGGIRVPFIARWPGK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 363 KNKGTVCKELVHITDWYPTLISLAEGQIDEDIqlDGYDIWETisegLRSPRVDILHniDPIYtkakngswaagYGIWNTA 442
Cdd:cd16145 313 IPAGSVSDHPSAFWDFMPTLADLAGAEPPEDI--DGISLLPT----LLGKPQQQQH--DYLY-----------WEFYEGG 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 77416378 443 IQSAIRVQHWKLLtgnpgysdwvppqafsnlgpnrwhneRITLSTGKsIWLFNITADPYERVDLSSRYP 511
Cdd:cd16145 374 GAQAVRMGGWKAV--------------------------RHGKKDGP-FELYDLSTDPGETNNLAAQHP 415
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
74-400 |
7.80e-71 |
|
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: 228.09 E-value: 7.80e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGS-EIKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQIHTGLQHSIIRPTQpncL 151
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNpDIKTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRHGVRGNVGNGGG---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 PLDNATLPQKLKEVGYSTHMVGKWHlgfyrkdcmptkrgfdtffgsllgsgdyythykcdspgvcgydlyendnaawdyd 231
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 232 ngiystqmytQRVQQILATHDPTKPLFLYVAYQAVHSPLqapgryfehyrsiininrrRYAAMLSCLDEAIHNVTLALKR 311
Cdd:cd16022 103 ----------DEAIDFIERRDKDKPFFLYVSFNAPHPPF-------------------AYYAMVSAIDDQIGRILDALEE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 312 YGFYNNSIIIYSSDNGGQPTAGGsnwpLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAegQID 391
Cdd:cd16022 154 LGLLDNTLIVFTSDHGDMLGDHG----LRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLA--GIE 227
|
....*....
gi 77416378 392 EDIQLDGYD 400
Cdd:cd16022 228 PPEGLDGRS 236
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
73-506 |
1.26e-66 |
|
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: 222.70 E-value: 1.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHGSEIKTPTLDKLAAEGVKLENYYVQPICTPSRSQFITGKYQIHTGL-QHSIIRPTQPNC- 150
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMgTMAELATGKPGYe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 151 --LPLDNATLPQKLKEVGYSTHMVGKWHLGFyrkdcmptkrgfdtffgsllgsgdyythykcdspgvcgydlyendnaaw 228
Cdd:cd16025 82 gyLPDSAATIAEVLKDAGYHTYMSGKWHLGP------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 229 dydNGIYSTQMYTQR-VQQILATHDPTKPLFLYVAYQAVHSPLQAP--------GRY---FEHYRS----------II-- 284
Cdd:cd16025 113 ---DDYYSTDDLTDKaIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPkewidkykGKYdagWDALREerlerqkelgLIpa 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 285 -----------------NINRRR--------YAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQPTAG---GSN 336
Cdd:cd16025 190 dtkltprppgvpawdslSPEEKKlearrmevYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPGwanASN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 337 WPLRGSKGTYWEGGIRAVGFVHSP-LLKNKGTVCKELVHITDWYPTLISLAEGQIDEDI------QLDGYDIWETIS-EG 408
Cdd:cd16025 270 TPFRLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVngvpqlPLDGVSLLPTLDgAA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 409 LRSPRvdilhniDPIYtkakngswaagygiWNTAIQSAIRVQHWKLLTGNPGYSDwvppqafsnlgPNRWHneritlstg 488
Cdd:cd16025 350 APSRR-------RTQY--------------FELFGNRAIRKGGWKAVALHPPPGW-----------GDQWE--------- 388
|
490
....*....|....*...
gi 77416378 489 ksiwLFNITADPYERVDL 506
Cdd:cd16025 389 ----LYDLAKDPSETHDL 402
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
74-506 |
7.95e-65 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 217.02 E-value: 7.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVG-YHGSEI---KTPTLDKLAAEGVKLENYYVQPICTPSRSQFITGKYQIHTGLqHSIIRPTQPN 149
Cdd:cd16142 1 PNILVILGDDIGWGDLGcYGGGIGrgaPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGL-TTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 150 CLPLDNATLPQKLKEVGYSTHMVGKWHLGfYRKDCMPTKRGFDTFFGSLlgsgdYYThykCDspgvcgydlyendnaawd 229
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLG-DEDGRLPTDHGFDEFYGNL-----YHT---ID------------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 230 ydngiystQMYTQRVQQILATHDPT-KPLFLYVAYQAVHSP-LQAPGryFEHYRSIINinrrRYAAMLSCLDEAIHNVTL 307
Cdd:cd16142 133 --------EEIVDKAIDFIKRNAKAdKPFFLYVNFTKMHFPtLPSPE--FEGKSSGKG----KYADSMVELDDHVGQILD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 308 ALKRYGFYNNSIIIYSSDNGGQPTA--GGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISL 385
Cdd:cd16142 199 ALDELGIADNTIVIFTTDNGPEQDVwpDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAAL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 386 AEGQIDE------DIQLDGYDIwetiseglrSPrvdilhnidpiYTKAKNGSWAAGYGIWNTAIQ-SAIRVQHWKLltgn 458
Cdd:cd16142 279 AGAPDPKdkllgkDRHIDGVDQ---------SP-----------FLLGKSEKSRRSEFFYFGEGElGAVRWKNWKV---- 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 77416378 459 pgYSDWVPPQAFSNLGPnrwhneritLSTGKSIWLFNITADPYERVDL 506
Cdd:cd16142 335 --HFKAQEDTGGPTGEP---------FYVLTFPLIFNLRRDPKERYDV 371
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
74-507 |
8.72e-62 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 209.36 E-value: 8.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSE--IKTPTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTGLQHSIIRPTQPNC 150
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDskIPTPNIDRLAAEGMRFTDAHSpSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 151 LPLDNATLPQKLKEVGYSTHMVGKWHLG--FYRKDCMPTKRGFDTFFgsllgsgDYYTHYKcDSPGVCGYDlyendnaaw 228
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKWHLGldWKKKDGKKAATGTGKDV-------DYSKPIK-GGPLDHGFD--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 229 dYDNGIYSTQM---YTQRVQQILATH-DPTKPLFLYVAYQAVHSPLQAPGRYfeHYRSIINinrrRYAAMLSCLDEAIHN 304
Cdd:cd16143 144 -YYFGIPASEVlptLTDKAVEFIDQHaKKDKPFFLYFALPAPHTPIVPSPEF--QGKSGAG----PYGDFVYELDWVVGR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 305 VTLALKRYGFYNNSIIIYSSDNGGQPTAGG---------SNWPLRGSKGTYWEGGIRaVGF-VHSPLLKNKGTVCKELVH 374
Cdd:cd16143 217 ILDALKELGLAENTLVIFTSDNGPSPYADYkelekfghdPSGPLRGMKADIYEGGHR-VPFiVRWPGKIPAGSVSDQLVS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 375 ITDWYPTLISLAEGQIDEDIQLDGYDI---WetISEGLRSPRVDILHNidpiytkAKNGSwaagygiwntaiqSAIRVQH 451
Cdd:cd16143 296 LTDLFATLAAIVGQKLPDNAAEDSFSFlpaL--LGPKKQEVRESLVHH-------SGNGS-------------FAIRKGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 77416378 452 WKLLTGNPGYSDWVPPQAfsnlgpnrwhneriTLSTGKSIWLFNITADPYERVDLS 507
Cdd:cd16143 354 WKLIDGTGSGGFSYPRGK--------------EKLGLPPGQLYNLSTDPGESNNLY 395
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
74-386 |
3.97e-59 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 199.57 E-value: 3.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSEIK-TPTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTGLQHSIirptqPNCL 151
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPtTPFLDRLAEEGLLFSNFYSgGTLTAPSRFALLTGLPPHNFGSYVST-----PVGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 PLDNATLPQKLKEVGYSTHMVGKWHLGFYRKDCmPTKRGFDTFFGSLLGSGDYYTHYKCDspgvcgydlyendnaaWDYD 231
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS-PCNLGFDKFFGRNTGSDLYADPPDVP----------------YNCS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 232 NGIYSTQMYTQRVQQILATHDptKPLFLYVAYQAVHSPLQAPGRY------FEHYRSIININRRRYAAMLSCLDEAIHNV 305
Cdd:pfam00884 139 GGGVSDEALLDEALEFLDNND--KPFFLVLHTLGSHGPPYYPDRYpekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 306 TLALKRYGFYNNSIIIYSSDNGgqPTAGGSNWPLRGSKG-TYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLIS 384
Cdd:pfam00884 217 LDKLEENGLLDNTLVVYTSDHG--ESLGEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILD 294
|
..
gi 77416378 385 LA 386
Cdd:pfam00884 295 LA 296
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
73-422 |
4.80e-57 |
|
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: 196.54 E-value: 4.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHGSE--IKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQIHTGLQHSIIrPTQPN 149
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPnaILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVGHNFL-PTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 150 CLPLDNATLPQKLKEVGYSTHMVGKWHLGfYRKDCMPTKRGFDTFFGsllgsgdyyTHYKCDSpgvcgydlyendnaawd 229
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLG-QREAYLPNSRGFDYYFG---------IPFSHDS----------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 230 ydngiYSTQMYTQRVQQILATH-DPTKPLFLYVAYQAVHSPLQAPGRYfeHYRSIIninRRRYAAMLSCLDEAIHNVTLA 308
Cdd:cd16161 133 -----SLADRYAQFATDFIQRAsAKDRPFFLYAALAHVHVPLANLPRF--QSPTSG---RGPYGDALQEMDDLVGQIMDA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 309 LKRYGFYNNSIIIYSSDNG---------GQPTAGG--SNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITD 377
Cdd:cd16161 203 VKHAGLKDNTLTWFTSDNGpwevkcelaVGPGTGDwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLD 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 77416378 378 WYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHNIDP 422
Cdd:cd16161 283 IFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSG 327
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
73-417 |
6.73e-55 |
|
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: 192.64 E-value: 6.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHGSEIKTPT-LDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTGLqHSIIRPTQPNC 150
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGpIDDMAAEGIRFTQAYSaDSVCTPSRAALLTGRLPIRSGM-YGGTRVFLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 151 ---LPLDNATLPQKLKEVGYSTHMVGKWHLGF--YRKD---CMPTKRGFDtFFGSLLgsgDYYTHYKCDS---------P 213
Cdd:cd16160 80 iggLPKTEVTMAEALKEAGYTTGMVGKWHLGIneNNHSdgaHLPSHHGFD-FVGTNL---PFTNSWACDDtgrhvdfpdR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 214 GVCGydLYENDNAAWDYDNGIYSTQMYTQRVQQILAThDPTKPLFLYVAYQAVHSPLQAPGRYFEHYRsiininRRRYAA 293
Cdd:cd16160 156 SACF--LYYNDTIVEQPIQHEHLTETLVGDAKSFIED-NQENPFFLYFSFPQTHTPLFASKRFKGKSK------RGRYGD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 294 MLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQPT---AGGSNWPLRGSKGTYWEGGIRAVGFVHSPllknkGT--- 367
Cdd:cd16160 227 NINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEyclEGGSTGGLKGGKGNSWEGGIRVPFIAYWP-----GTikp 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 77416378 368 -VCKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDIL 417
Cdd:cd16160 302 rVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDIL 352
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
72-521 |
1.60e-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: 191.20 E-value: 1.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 72 SQPHLIFILADDQGFRDVGYHGSEI-KTPTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTG---LQHSIIRPT 146
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIvKTPNIDRLAKEGVRFDNAFVtTSICAPSRASILTGQYSHRHGvtdNNGPLFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 147 QPnclpldnaTLPQKLKEVGYSTHMVGKWHLGFYRKDCmptKRGFDtFFGSLLGSGDYYThykcdspgvcgydlYENDNA 226
Cdd:cd16031 81 QP--------TYPKLLRKAGYQTAFIGKWHLGSGGDLP---PPGFD-YWVSFPGQGSYYD--------------PEFIEN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 227 AWDYDNGIYSTQMYTQRVQQILATHDPTKPLFLYVAYQAVHSPLQAPGRYFEHYRSI----------------------- 283
Cdd:cd16031 135 GKRVGQKGYVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVtipepetfddddyagrpewareq 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 284 ININR-----------------RRYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQptAGGSNWplrGSKGTY 346
Cdd:cd16031 215 RNRIRgvldgrfdtpekyqrymKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFF--LGEHGL---FDKRLM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 347 WEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQldGYDIWETIS-EGLRSPRVDILHNidpiYt 425
Cdd:cd16031 290 YEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQ--GRSLLPLLEgEKPVDWRKEFYYE----Y- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 426 kakngswaagYGIWN---TAIQSAIRVQHWKLLtgnpgysdwvppqafsnlgpnRWHNERITlstgksiW-LFNITADPY 501
Cdd:cd16031 363 ----------YEEPNfhnVPTHEGVRTERYKYI---------------------YYYGVWDE-------EeLYDLKKDPL 404
|
490 500
....*....|....*....|..
gi 77416378 502 ERVDL--SSRYPGIVKKLLRRL 521
Cdd:cd16031 405 ELNNLanDPEYAEVLKELRKRL 426
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
74-395 |
2.37e-51 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 180.78 E-value: 2.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSEIKTPTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTGLQHsiIRPTQPNcLP 152
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTtAPVCSPSRSALLTGLYPHQNGAHG--LRSRGFP-LP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 153 LDNATLPQKLKEVGYSTHMVGKWHLGFyrkdcmPTKRGFDTFFGSLLGSGDYythykcdspgvcgydlyendnaAWDYDn 232
Cdd:cd16027 78 DGVKTLPELLREAGYYTGLIGKTHYNP------DAVFPFDDEMRGPDDGGRN----------------------AWDYA- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 233 giystqmytQRVQQILATHDPTKPLFLYVAYQAVHSPLQAPGRYFEHYR-SIINI---------NRR---RYAAMLSCLD 299
Cdd:cd16027 129 ---------SNAADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDpEKVKVppylpdtpeVREdlaDYYDEIERLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 300 EAIHNVTLALKRYGFYNNSIIIYSSDNGgqptaggsnWPLRGSKGTYWEGGIRaVGF-VHSPLLKNKGTVCKELVHITDW 378
Cdd:cd16027 200 QQVGEILDELEEDGLLDNTIVIFTSDHG---------MPFPRAKGTLYDSGLR-VPLiVRWPGKIKPGSVSDALVSFIDL 269
|
330
....*....|....*..
gi 77416378 379 YPTLISLAEGQIDEDIQ 395
Cdd:cd16027 270 APTLLDLAGIEPPEYLQ 286
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
73-506 |
9.74e-51 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 180.07 E-value: 9.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLENYY-VQPICTPSRSQFITGKYQIHTGLQHsiirptqpNC 150
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDpVKTPNLDRLAKEGVVFTNAVsNYPVCSPYRASLLTGQYPLTNGVFG--------ND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 151 LPLDNA--TLPQKLKEVGYSTHMVGKWHL-GFYRKDCM-------PTKR-GFDTFFGsLLGSGDYYTHYkcdspgvcgyd 219
Cdd:cd16034 73 VPLPPDapTIADVLKDAGYRTGYIGKWHLdGPERNDGRaddytppPERRhGFDYWKG-YECNHDHNNPH----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 220 lYENDNAAWDYDNGiYSTQMYTQRVQQILATH-DPTKPLFLYVAYQAVHSP-LQAPGRYFEHYRSIININR--------- 288
Cdd:cd16034 141 -YYDDDGKRIYIKG-YSPDAETDLAIEYLENQaDKDKPFALVLSWNPPHDPyTTAPEEYLDMYDPKKLLLRpnvpedkke 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 289 --------RRYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQptaGGSNWPLRgsKGTYWEGGIRAVGFVHSP 360
Cdd:cd16034 219 eaglredlRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM---LGSHGLMN--KQVPYEESIRVPFIIRYP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 361 LLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQldGYDiwetISEGLRSPRvDILHNIDPIYTKAKNGSWAAGYGIWn 440
Cdd:cd16034 294 GKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVE--GRD----LSPLLLGGK-DDEPDSVLLQCFVPFGGGSARDGGE- 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77416378 441 taiQSAIRVQHWKLLtgnpgYSDWVPPqafsnlgpnrwhneritlstgksiWLFNITADPYERVDL 506
Cdd:cd16034 366 ---WRGVRTDRYTYV-----RDKNGPW------------------------LLFDNEKDPYQLNNL 399
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
73-533 |
2.74e-50 |
|
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: 181.72 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHG-SEIKTPTLDKLAAEGVKLE-NYYVQPICTPSRSQFITGKYQIHTGLQHS-----IIRP 145
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGnDTIRTPNIDRLAKEGVKLThHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrvILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 146 TQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKD----CM-PTKRGFDTFFG------------------------ 196
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESrndfCHhPLNHGFDYFYGlpltnlkdcgdgsngeydlsfdpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 197 -----------SLLGSGDYYTHYKCDSPGVC-------------GYD---------LYENDNAA---WDYDNgiySTQMY 240
Cdd:cd16159 161 fplltafvlitALTIFLLLYLGAVSKRFFVFllilsllfislffLLLitnryfnciLMRNHEVVeqpMSLEN---LTQRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 241 TQRVQQILATHDpTKPLFLYVAYQAVHSPLQAPGRYFEHYRsiininRRRYAAMLSCLDEAIHNVTLALKRYGFYNNSII 320
Cdd:cd16159 238 TKEAISFLERNK-ERPFLLVMSFLHVHTALFTSKKFKGRSK------HGRYGDNVEEMDWSVGQILDALDELGLKDNTFV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 321 IYSSDNGGQPT--------AGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDE 392
Cdd:cd16159 311 YFTSDNGGHLEeisvggeyGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 393 DIQLDGYDIWETIS-EGLRSPRVDILH----NIDPIYTKAKNGswaagygiwnTAIqsairvqhWKLLTGNPgysDWVPp 467
Cdd:cd16159 391 DRIIDGRDLMPLLTgQEKRSPHEFLFHycgaELHAVRYRPRDG----------GAV--------WKAHYFTP---NFYP- 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77416378 468 qafsnlGPNRWHNERITLSTGKSI------WLFNITADPYERVDLSS---RYPGIVKKLLRRLSQFNKTAVPVRY 533
Cdd:cd16159 449 ------GTEGCCGTLLCRCFGDSVthhdppLLFDLSADPSESNPLDPtdePYQEIIKKILEAVAEHQSSIEPVES 517
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-506 |
3.67e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 177.79 E-value: 3.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVG-YHGSEIKTPTLDKLAAEGVKLENYYVQPICTPSRSQFITGKYQIHTGLQHSIIRPTQPnclp 152
Cdd:cd16151 1 PNIILIMADDLGYECIGcYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 153 ldnaTLPQKLKEVGYSTHMVGKWHLGFYRKDCM-PTKRGFDTF--FGsLLGSGDYYTHYKCDSPgvcgydlYENDNAAWD 229
Cdd:cd16151 77 ----TFGHLLKDAGYATAIAGKWQLGGGRGDGDyPHEFGFDEYclWQ-LTETGEKYSRPATPTF-------NIRNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 230 YDNGIYSTQMYTQRVQQILATH-DptKPLFLYVAYQAVHSPLQ----------APGRYFEHYrsiininrRRYAAMLSCL 298
Cdd:cd16151 145 TTEGDYGPDLFADFLIDFIERNkD--QPFFAYYPMVLVHDPFVptpdspdwdpDDKRKKDDP--------EYFPDMVAYM 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 299 DEAIHNVTLALKRYGFYNNSIIIYSSDNGGQPT----AGGSNwpLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVH 374
Cdd:cd16151 215 DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrTNGRE--VRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 375 ITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHnidpIYTKAKNGSWAAGygiwntaiqsAIRVQHWKL 454
Cdd:cd16151 293 FSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIY----WYYRNPHKKFGSR----------FVRTKRYKL 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 77416378 455 ltgnpgYSDwvppqafsnlgpnrwhneritlstGKsiwLFNITADPYERVDL 506
Cdd:cd16151 359 ------YAD------------------------GR---FFDLREDPLEKNPL 377
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
74-542 |
1.43e-49 |
|
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: 178.79 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSEIK-TPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQIHTGLQHSIIRPTQPNCL 151
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSsTPNLDRLAANGLRFTDFYSSsPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 PLDNATLPQKLKEVGYSTHMVGKWHLGF-YRKDCMPTKRGFDTFFGsLLGSGD---------YYTHYKCDS---PGVCGY 218
Cdd:cd16158 82 PLNETTIAEVLKTVGYQTAMVGKWHLGVgLNGTYLPTHQGFDHYLG-IPYSHDqgpcqnltcFPPNIPCFGgcdQGEVPC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 219 DLYENDNAAWDYDNGIYSTQMYTQRVQQILA-THDPTKPLFLYVAYQAVHSPLQAPGRYFEhyRSIininRRRYAAMLSC 297
Cdd:cd16158 161 PLFYNESIVQQPVDLLTLEERYAKFAKDFIAdNAKEGKPFFLYYASHHTHYPQFAGQKFAG--RSS----RGPFGDALAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 298 LDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQ---PTAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGtVCKELVH 374
Cdd:cd16158 235 LDGSVGELLQTLKENGIDNNTLVFFTSDNGPStmrKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPG-VTHELAS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 375 ITDWYPTLISLAeGQIDEDIQLDGYDIWETISEGLRSPRVDILHNidPIYTKAKNGSWAAGYGIWNTaiqsairvqHWkl 454
Cdd:cd16158 314 TLDILPTIAKLA-GAPLPNVTLDGVDMSPILFEQGKSPRQTFFYY--PTSPDPDKGVFAVRWGKYKA---------HF-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 455 LTGNPGYSDWVPPQAFSNLGPNRWHNERItlstgksiwLFNITADPYERVDL--SSRYPGIVKKLLRRLSQFNKTavpVR 532
Cdd:cd16158 380 YTQGAAHSGTTPDKDCHPSAELTSHDPPL---------LFDLSQDPSENYNLlgLPEYNQVLKQIQQVKERFEAS---MK 447
|
490
....*....|....*.
gi 77416378 533 YPP------KDPRSNP 542
Cdd:cd16158 448 FGEseinkgEDPALEP 463
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
73-530 |
3.31e-49 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 177.66 E-value: 3.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHGSEIK-TPTLDKLAAEGVKLENYY-VQPICTPSRSQFITGKYQIHTGL----QHSIIRPT 146
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSReTPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNGFyttnAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 147 QPNC---LPLDNATLPQKLKEVGYSTHMVGKWHLGfYRKDCMPTKRGFDTFFGSLlgsgdyYTHYKC-DSPGVCGYDLYE 222
Cdd:cd16157 81 PQNIvggIPDSEILLPELLKKAGYRNKIVGKWHLG-HRPQYHPLKHGFDEWFGAP------NCHFGPyDNKAYPNIPVYR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 223 NDNAAWDY--------DNGIYS-TQMYTQR-VQQILATHDPTKPLFLYVAYQAVHSPLQAPgryfEHYRSiiNINRRRYA 292
Cdd:cd16157 154 DWEMIGRYyeefkidkKTGESNlTQIYLQEaLEFIEKQHDAQKPFFLYWAPDATHAPVYAS----KPFLG--TSQRGLYG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 293 AMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNG----GQPTAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTV 368
Cdd:cd16157 228 DAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaaliSAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 369 CKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHNIDPIYtKAKNGSWAAGYGIWNTAIQSAIR 448
Cdd:cd16157 308 SHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGDELM-AVRLGQYKAHFWTWSNSWEEFRK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 449 VQHwklltgnpgysdWVPPQAFSNLGPnrwHNEriTLSTGKSIwLFNITADPYERVDLSSR---YPGIVKKLLRRLSQFN 525
Cdd:cd16157 387 GIN------------FCPGQNVPGVTT---HNQ--TDHTKLPL-LFHLGRDPGEKYPISFKsaeYKQAMPRISKVVQQHQ 448
|
....*
gi 77416378 526 KTAVP 530
Cdd:cd16157 449 KTLVP 453
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
72-521 |
6.81e-47 |
|
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: 168.90 E-value: 6.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 72 SQPHLIFILADDQGFRDVGYHG-SEIKTPTLDKLAAEGVKLENYYVQ-----PICTPSRSQFITGKYQIHTGLQHsiirp 145
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGnPEIQTPNLDRLARRGTSFTNAYNMggwsgAVCVPSRAMLMTGRTLFHAPEGG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 146 tqPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYrkdcmptkrgfdtffgsllgsgdyythykcdspgvcgydlyendN 225
Cdd:cd16155 76 --KAAIPSDDKTWPETFKKAGYRTFATGKWHNGFA--------------------------------------------D 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 226 AAWDYdngiystqmytqrvqqILATHDPTKPLFLYVAYQAVHSPLQAPGRYFEHY------------------------- 280
Cdd:cd16155 110 AAIEF----------------LEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYppetiplpenflpqhpfdngegtvr 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 281 ----------RSIININRRRYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGgqpTAGGSNwPLRGsKGTYWEGG 350
Cdd:cd16155 174 deqlapfprtPEAVRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG---LAVGSH-GLMG-KQNLYEHS 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 351 IRAVGFVHSPLLKnKGTVCKELVHITDWYPTLISLAEGQIDEDIqlDGYDIWETISEGLRSPRvdilhniDPIYTKAKNG 430
Cdd:cd16155 249 MRVPLIISGPGIP-KGKRRDALVYLQDVFPTLCELAGIEIPESV--EGKSLLPVIRGEKKAVR-------DTLYGAYRDG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 431 swaagygiwntaiQSAIRVQHWKLltgnpgysDWVPPQAfsnlgpnrwhneRITLstgksiwLFNITADPYERVDLSS-- 508
Cdd:cd16155 319 -------------QRAIRDDRWKL--------IIYVPGV------------KRTQ-------LFDLKKDPDELNNLADep 358
|
490
....*....|...
gi 77416378 509 RYPGIVKKLLRRL 521
Cdd:cd16155 359 EYQERLKKLLAEL 371
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-433 |
1.33e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 151.73 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGfRDV----GYHGSEIKTPTLDKLAAEGVKLENYYVQPICTPSRSQFITGKYQIHTGlqhsIIRPtqPN 149
Cdd:cd16154 1 PNILLIIADDQG-LDSsaqySLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTG----VLAV--PD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 150 CLPLDNATLPQKLKE----VGYSTHMVGKWHLGfyrkDCMPTKR---GFDTFFGSLLGSG-DYYThykcdspgvcgYDLY 221
Cdd:cd16154 74 ELLLSEETLLQLLIKdattAGYSSAVIGKWHLG----GNDNSPNnpgGIPYYAGILGGGVqDYYN-----------WNLT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 222 ENDNAAwdyDNGIYSTQMYTQrvQQILATHDPTKPLFLYVAYQAVHSPLQAP-----GRYFEHYRSIININRRR-YAAML 295
Cdd:cd16154 139 NNGQTT---NSTEYATTKLTN--LAIDWIDQQTKPWFLWLAYNAPHTPFHLPpaelhSRSLLGDSADIEANPRPyYLAAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 296 SCLDEAI----HNVTLALKrygfyNNSIIIYSSDNGGQPTAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKE 371
Cdd:cd16154 214 EAMDTEIgrllASIDEEER-----ENTIIIFIGDNGTPGQVVDLPYTRNHAKGSLYEGGINVPLIVSGAGVERANERESA 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77416378 372 LVHITDWYPTLISLAEGQIDEdiQLDGYDIWETISEGLRSPRvdilhniDPIYTKAKNGSWA 433
Cdd:cd16154 289 LVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTR-------QYNYTEYESPTTT 341
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
71-418 |
2.73e-38 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 147.51 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 71 TSQPHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLEN-YYVQPICTPSRSQFITGKYQIHTGlqhsiiRPTQP 148
Cdd:PRK13759 4 TKKPNIILIMVDQMRGDCLGCNGNKaVETPNLDMLASEGYNFENaYSAVPSCTPARAALLTGLSQWHHG------RVGYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 149 NCLPLD-NATLPQKLKEVGYSTHMVGKWHLGFYRKDCmptkrGFDtffGSLLGSG-----------------DYYTHYKC 210
Cdd:PRK13759 78 DVVPWNyKNTLPQEFRDAGYYTQCIGKMHVFPQRNLL-----GFH---NVLLHDGylhsgrnedksqfdfvsDYLAWLRE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 211 DSPG--VCGYDLYENDNAA----WDYDNGIYSTQMYTQRVQQILATHDPTKPLFLYVAYQAVHSPLQAPGRYFEHY---- 280
Cdd:PRK13759 150 KAPGkdPDLTDIGWDCNSWvarpWDLEERLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYkdad 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 281 ----------------RSIININ--------------RRRYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQp 330
Cdd:PRK13759 230 ipdphigdweyaedqdPEGGSIDalrgnlgeeyarraRAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 331 tAGGSNWpLRgsKGTYWEGGIRAVGFVHSP---LLKNKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDGYDIWETISE 407
Cdd:PRK13759 309 -LGDHYL-FR--KGYPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFG 382
|
410
....*....|.
gi 77416378 408 GLRSPRvDILH 418
Cdd:PRK13759 383 QYEGWR-PYLH 392
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-398 |
4.93e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 135.44 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHG-SEIKTPTLDKLAAEGVKLENYY-VQPICTPSRSQFITGKYQ----IHTGL-QHSIIRPT 146
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGnSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRMPsqhgIHDWIvEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 147 QPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGfyrkdcmptkrgfdtffgsllgsgdyythykcdspgvcgydlyendna 226
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 227 awdydngiystqmyTQRVQQILATHDPTKPLFLYVAYQAVHSPLQapgryfehyrsiininrrrYAAMLSCLDEAIHNVT 306
Cdd:cd16149 113 --------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------------YFAAVTGVDRNVGRLL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 307 LALKRYGFYNNSIIIYSSDNG------GQPTAGGSNWPLrgskgTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYP 380
Cdd:cd16149 160 DELEELGLTENTLVIFTSDNGfnmghhGIWGKGNGTFPL-----NMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFP 234
|
330
....*....|....*...
gi 77416378 381 TLISLAEGQIDEDIQLDG 398
Cdd:cd16149 235 TLLELAGVDPPADPRLPG 252
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-414 |
1.41e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 133.44 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQIHTGlqhsiirpTQPNCL 151
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPvVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETG--------VWDNAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 PLDN--ATLPQKLKEVGYSTHMVGKwhlgfyrkdcmptkrgfdtffgsllgsgdyyTHYkcdspgvcgydLYENDNAAWD 229
Cdd:cd16037 73 PYDGdvPSWGHALRAAGYETVLIGK-------------------------------LHF-----------RGEDQRHGFR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 230 YDngiystQMYTQRVQQILATHDP-TKPLFLYVAYQAVHSPLQAPGRYFEHYRSIIninRRRYAAMLSCLDEAIHNVTLA 308
Cdd:cd16037 111 YD------RDVTEAAVDWLREEAAdDKPWFLFVGFVAPHFPLIAPQEFYDLYVRRA---RAAYYGLVEFLDENIGRVLDA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 309 LKRYGFYNNSIIIYSSDNGGQPTAGGSNWplrgsKGTYWEGGiravgfVHSPLL-----KNKGTVCKELVHITDWYPTLI 383
Cdd:cd16037 182 LEELGLLDNTLIIYTSDHGDMLGERGLWG-----KSTMYEES------VRVPMIisgpgIPAGKRVKTPVSLVDLAPTIL 250
|
330 340 350
....*....|....*....|....*....|.
gi 77416378 384 SLAEGQIDEDiqLDGYDIWETISEGLRSPRV 414
Cdd:cd16037 251 EAAGAPPPPD--LDGRSLLPLAEGPDDPDRV 279
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
73-521 |
5.34e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 133.12 E-value: 5.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHGSEIK-TPTLDKLAAEGVKLEN-YYVQPICTPSRSQFITGKYQIHTGLQHSIIRptqpnc 150
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDlTPNLDALAEEGVLFENaFTPQPVCGPARACLQTGLYPTETGCFRNGIP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 151 LPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKDCMptkrgfdtffgsllgsgdyythykcdspgvcgydlyendnaawdy 230
Cdd:cd16152 75 LPADEKTLAHYFRDAGYETGYVGKWHLAGYRVDAL--------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 231 dngiystqmyTQRVQQILATHDPTKPLFLYVAYQAVH---------SP---------------LQA-PGRYFEHYRSiin 285
Cdd:cd16152 110 ----------TDFAIDYLDNRQKDKPFFLFLSYLEPHhqndrdryvAPegsaerfanfwvppdLAAlPGDWAEELPD--- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 286 inrrrYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNggqptagGSNWPLRGS--KGTYWEGGIravgfvHSPLLK 363
Cdd:cd16152 177 -----YLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH-------GCHFRTRNAeyKRSCHESSI------RVPLVI 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 364 -----NKGTVCKELVHITDWYPTLISLAegQIDEDIQLDGYDIWETISEGLRSPRVDILHNIdpiytkakNGSWaagygi 438
Cdd:cd16152 239 ygpgfNGGGRVEELVSLIDLPPTLLDAA--GIDVPEEMQGRSLLPLVDGKVEDWRNEVFIQI--------SESQ------ 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 439 wntaIQSAIRVQHWKLLTGNPGYSDWVPPqafsnlGPNRWHNEritlstgksiWLFNITADPYERVDL--SSRYPGIVKK 516
Cdd:cd16152 303 ----VGRAIRTDRWKYSVAAPDKDGWKDS------GSDVYVED----------YLYDLEADPYELVNLigRPEYREVAAE 362
|
....*
gi 77416378 517 LLRRL 521
Cdd:cd16152 363 LRERL 367
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-524 |
4.04e-33 |
|
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: 131.19 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSEI-KTPTLDKLAAEGVKLENYY-VQPICTPSRSQFITGKYQIHTGLQHSIIRPTQPNC- 150
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNAYtPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 151 LPLDNATLPQKLKEVGYSTHMVGKWHLGfyrKDCMPTKRGFDTFFGsllgsgdyythykcdspgvcgydlyenDNAAWDY 230
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFDEYLP---------------------------VETTIEY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 231 DngiystqmYTQRVQQILATH-DPTKPLFLYVAYQAVHSPLQAPGRYF----------------------EHYRSIINI- 286
Cdd:cd16033 131 F--------LADRAIEMLEELaADDKPFFLRVNFWGPHDPYIPPEPYLdmydpediplpesfaddfedkpYIYRRERKRw 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 287 ------------NRRRYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGgqpTAGGSNwplRG-SKGTY-WEGGIR 352
Cdd:cd16033 203 gvdtedeedwkeIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHG---DALGAH---RLwDKGPFmYEETYR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 353 AVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAegQIDEDIQLDGydiwetiseglRSpRVDILHNIDPiyTKAKNGSW 432
Cdd:cd16033 277 IPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLA--GVDVPPKVDG-----------RS-LLPLLRGEQP--EDWRDEVV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 433 AAGYGIWNTAIQSAIRVQHWKLLTGNPGYsdwvppqafsnlgpnrwhNEritlstgksiwLFNITADPYERVDL--SSRY 510
Cdd:cd16033 341 TEYNGHEFYLPQRMVRTDRYKYVFNGFDI------------------DE-----------LYDLESDPYELNNLidDPEY 391
|
490
....*....|....
gi 77416378 511 PGIVKKLLRRLSQF 524
Cdd:cd16033 392 EEILREMRTRLYEW 405
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
73-398 |
1.45e-31 |
|
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: 126.51 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQgfrDVGYHGSEIKTPTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTGLQHsIIRPtqPNCL 151
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMPKTKKLLADQGTTFTNAFVtTPLCCPSRASILTGQYAHNHGVTN-NSPP--GGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 P------LDNATLPQKLKEVGYSTHMVGK----WHLGFYRKDCMPtkrGFDTFFGSLLGSGDYYTHYKCDSPGVcGYDLY 221
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVPP---GWDEWDGLVGNSTYYNYTLSNGGNGK-HGVSY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 222 ENDnaawdydngiYSTQMYTQRVQQILATHDPT-KPLFLYVAYQAVHSPLQAPGRYFEHY-------------------- 280
Cdd:cd16147 151 PGD----------YLTDVIANKALDFLRRAAADdKPFFLVVAPPAPHGPFTPAPRYANLFpnvtapprpppnnpdvsdkp 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 281 --------------RSIININRRRYAAMLScLDEAIHNVTLALKRYGFYNNSIIIYSSDNG---GQPTaggsnwpLRGSK 343
Cdd:cd16147 221 hwlrrlpplnptqiAYIDELYRKRLRTLQS-VDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHR-------LPPGK 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 77416378 344 GTYWEGGIRAVGFVHSPLLKnKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDG 398
Cdd:cd16147 293 RTPYEEDIRVPLLVRGPGIP-AGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDG 344
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
73-403 |
3.54e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 114.01 E-value: 3.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 73 QPHLIFILADDQGFRDVGYHGS-----------EIKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQIHTGLQH 140
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlgYVESPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 141 SiiRPTQPNcLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKdcmptkrgfdtffgsllgsgdyYThykcdspgvcgydl 220
Cdd:cd16153 81 F--EAAHPA-LDHGLPTFPEVLKKAGYQTASFGKSHLEAFQR----------------------YL-------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 221 yENDNaawdydngiystQMYTQRVQQILATHDPTKPLFLYVAYQAVHSPLQAPGRYFEHYrsiininrrRYAAMLSCLDE 300
Cdd:cd16153 122 -KNAN------------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEFRDRF---------DYYAFCAYGDA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 301 AIHNVTLALKRYGFYN---NSIIIYSSDNGgqptaggsnWPL--RG--SKGTYWEGGIR-AVGFVHS-PLLKNKGTVCKE 371
Cdd:cd16153 180 QVGRAVEAFKAYSLKQdrdYTIVYVTGDHG---------WHLgeQGilAKFTFWPQSHRvPLIVVSSdKLKAPAGKVRHD 250
|
330 340 350
....*....|....*....|....*....|..
gi 77416378 372 LVHITDWYPTLISLAEGQIDEDIQLDGYDIWE 403
Cdd:cd16153 251 FVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
72-398 |
8.05e-28 |
|
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: 116.52 E-value: 8.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 72 SQPHLIFILADDqgFRDV--GYHGSEIKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQIHTGLQ--HSIIRPT 146
Cdd:cd16030 1 KKPNVLFIAVDD--LRPWlgCYGGHPAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTGVYdnNSYFRKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 147 QPnclplDNATLPQKLKEVGYSTHMVGK-WHLGFYRKDCMPtkRGFDTFFGSlLGSGDYYTHYKCDSPGVCGYDLYENDN 225
Cdd:cd16030 79 AP-----DAVTLPQYFKENGYTTAGVGKiFHPGIPDGDDDP--ASWDEPPNP-PGPEKYPPGKLCPGKKGGKGGGGGPAW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 226 AAWDYDNGIYSTQMYTQRVQQILAT-HDPTKPLFLYVAYQAVHSPLQAPGRYFEHY-RSIININ---------------- 287
Cdd:cd16030 151 EAADVPDEAYPDGKVADEAIEQLRKlKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYpLESIPLPnpfdpidlpevawndl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 288 -----------------------------RRRYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGgqptaggsnWP 338
Cdd:cd16030 231 ddlpkygdipalnpgdpkgplpdeqarelRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG---------WH 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77416378 339 LrGSKGTY-----WEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAEgqIDEDIQLDG 398
Cdd:cd16030 302 L-GEHGHWgkhtlFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEG 363
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
74-398 |
1.15e-24 |
|
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: 104.97 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADD---QGFRDvgYHGSEIKTPTLDKLAAEGVKLENYY-VQPICTPSRSQFITGKYqihtglqhsiirPTQPN 149
Cdd:cd16032 1 PNILLIMADQltaAALPA--YGNTVVKTPNLDRLAARGVVFDNAYcNSPLCAPSRASMMTGRL------------PSRIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 150 CLplDNA--------TLPQKLKEVGYSTHMVGKWHLgfyrkdCMPTK-RGFDtffgsllgsgdyythykcdspgvcgYDl 220
Cdd:cd16032 67 AY--DNAaefpadipTFAHYLRAAGYRTALSGKMHF------VGPDQlHGFD-------------------------YD- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 221 yenDNAAWdydngiystqmytQRVQQI--LATHDPTKPLFLYVAYQAVHSPLQAPGRYFEHYrsIINInRRRYAAMLSCL 298
Cdd:cd16032 113 ---EEVAF-------------KAVQKLydLARGEDGRPFFLTVSFTHPHDPYVIPQEYWDLY--VRRA-RRAYYGMVSYV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 299 DEAIHNVTLALKRYGFYNNSIIIYSSDNG---GQptaggsnwplRG--SKGTYWEGGIRAVGFVHSPLLKnKGTVCKELV 373
Cdd:cd16032 174 DDKVGQLLDTLERTGLADDTIVIFTSDHGdmlGE----------RGlwYKMSFFEGSARVPLIISAPGRF-APRRVAEPV 242
|
330 340
....*....|....*....|....*.
gi 77416378 374 HITDWYPTLISLAEGQIDEDI-QLDG 398
Cdd:cd16032 243 SLVDLLPTLVDLAGGGTAPHVpPLDG 268
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-395 |
8.20e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 101.47 E-value: 8.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVG-YHGSEIKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQIHTGLQHSIIRPTQPncl 151
Cdd:cd16148 1 MNVILIVIDSLRADHLGcYGYDRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGVWGGPLEPDDP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 pldnaTLPQKLKEVGYSTHMVGKWHLGFYRkdcMPTKRGFDTFFGSLLGSGDyythykcdspgvcgydlyendnaawDYD 231
Cdd:cd16148 78 -----TLAEILRKAGYYTAAVSSNPHLFGG---PGFDRGFDTFEDFRGQEGD-------------------------PGE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 232 NGIYSTQMYTQRVQQILATHDPTKPLFLYVAYQAVHSPlqapgrYfehyrsiininrrRYAAMLSCLDEAIHNVTLALKR 311
Cdd:cd16148 125 EGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEP------Y-------------LYDAEVRYVDEQIGRLLDKLKE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 312 YGFYNNSIIIYSSDNG---GQptaGGSNWplrGSKGTYWEGGIRAVGFVHSPLLKnKGTVCKELVHITDWYPTLISLAEG 388
Cdd:cd16148 186 LGLLEDTLVIVTSDHGeefGE---HGLYW---GHGSNLYDEQLHVPLIIRWPGKE-PGKRVDALVSHIDIAPTLLDLLGV 258
|
....*..
gi 77416378 389 QIDEDIQ 395
Cdd:cd16148 259 EPPDYSD 265
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-387 |
9.18e-22 |
|
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: 98.08 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDqgFR-D-VGYHGSE-IKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKY---QIHTGLQHsIIRPT 146
Cdd:cd16150 1 PNIVIFVADQ--LRaDsLGHLGNPaAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGWYphvNGHRTLHH-LLRPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 147 QPNCLpldnatlpQKLKEVGYSTHMVGKwhlgfyrKDCMPTKRGFdtffgsllgsGDYythykCDSpgvcgyDlYENDNA 226
Cdd:cd16150 78 EPNLL--------KTLKDAGYHVAWAGK-------NDDLPGEFAA----------EAY-----CDS------D-EACVRT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 227 AWDYdngiystqmytqrvqqiLATHDPTKPLFLYVAYQAVHSPLQAPGRYFEHY-----------------RSIININRR 289
Cdd:cd16150 121 AIDW-----------------LRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIdreklpprrppglrakgKPSMLEGIE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 290 R-----------------YAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQptaggsnwplrgsKGTY-----W 347
Cdd:cd16150 184 KqgldrwseerwrelratYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDY-------------TGDYglvekW 250
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 77416378 348 EGGIRAVgFVHSPLLKN-----KGTVCKELVHITDWYPTLISLAE 387
Cdd:cd16150 251 PNTFEDC-LTRVPLIIKppggpAGGVSDALVELVDIPPTLLDLAG 294
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
74-327 |
9.67e-22 |
|
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: 98.61 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVG-YHGSEIKTPTLDKLAAEGVKLEN-YYVQPICTPSRSQFITGKYQIHTGlqhsiirpTQPNCL 151
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcYGNKAMKTPNLDRLAAEGVRFDSaYTTQPVCGPARSGLFTGLYPHTNG--------SWTNCM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 PL-DNA-TLPQKLKEVGYSTHMVGKWHLGfyrkdcmptkrgfdtffgsllgSGDYYTHykcdspGVC--GYD-------- 219
Cdd:cd16156 73 ALgDNVkTIGQRLSDNGIHTAYIGKWHLD----------------------GGDYFGN------GICpqGWDpdywydmr 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 220 -----LYENDNAAW------DYDNGIYSTQMY----TQRVQQILATHDpTKPLFLYVAYQAVHSPLQAPGRYFEHY---- 280
Cdd:cd16156 125 nyldeLTEEERRKSrrgltsLEAEGIKEEFTYghrcTNRALDFIEKHK-DEDFFLVVSYDEPHHPFLCPKPYASMYkdfe 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77416378 281 -----------------------------RSIININRRRYAAMLSCLDEAIHNVTLALKRYgfYNNSIIIYSSDNG 327
Cdd:cd16156 204 fpkgenayddlenkplhqrlwagakphedGDKGTIKHPLYFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHG 277
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-386 |
2.93e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 88.80 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVgYHGSEIKT--PTLDKLAAEGVKLENYYV-QPICTPSRSQFITGKYQIHTGLQHSIIRPTQPNc 150
Cdd:cd16035 1 PNILLILTDQERYPPP-WPAGWAALnlPARERLAANGLSFENHYTaACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 151 LPLDNATLPQKLKEVGYSTHMVGKWHLgfyrkdcmptkrgfdtffgSLLGSGdyythykcdspgvcgydlyendnaAWDY 230
Cdd:cd16035 79 LSPDVPTLGHMLRAAGYYTAYKGKWHL-------------------SGAAGG------------------------GYKR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 231 DngiystQMYTQRVQQILATHDP----TKPLFLYVAY---QAVHSPLQAPGRYFEHyrsiininRRRYAAMLSCLDEAIH 303
Cdd:cd16035 116 D------PGIAAQAVEWLRERGAknadGKPWFLVVSLvnpHDIMFPPDDEERWRRF--------RNFYYNLIRDVDRQIG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 304 NVTLALKRYGFYNNSIIIYSSDNGGQPTAGGsnwpLRGSKGTYWEGGIRaVGFVHS-PLLKNKGTVCKELV-HItDWYPT 381
Cdd:cd16035 182 RVLDALDASGLADNTIVVFTSDHGEMGGAHG----LRGKGFNAYEEALH-VPLIIShPDLFGTGQTTDALTsHI-DLLPT 255
|
....*
gi 77416378 382 LISLA 386
Cdd:cd16035 256 LLGLA 260
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
78-521 |
4.35e-18 |
|
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: 86.93 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 78 FILADDQGFRDVGYHG-SEIKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGKYQihtgLQHSIIRPTQPncLPLDN 155
Cdd:cd16028 5 FITADQWRADCLSCLGhPLVKTPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRYL----MNHRSVWNGTP--LDARH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 156 ATLPQKLKEVGYSTHMVGKWHlgfYRKDCMPTKRGFDTFFGSLLGSgdyythykcdspgvCGYDLYENDNaawDYDNGIY 235
Cdd:cd16028 79 LTLALELRKAGYDPALFGYTD---TSPDPRGLAPLDPRLLSYELAM--------------PGFDPVDRLD---EYPAEDS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 236 STQMYTQRVQQILATHDpTKPLFLYVAYQAVHSPLQAPGRY---------------------------FEHYRSII---- 284
Cdd:cd16028 139 DTAFLTDRAIEYLDERQ-DEPWFLHLSYIRPHPPFVAPAPYhalydpadvpppiraeslaaeaaqhplLAAFLERIesls 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 285 --------------NINRRR--YAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQptaGGSNWpLRGsKGTYWE 348
Cdd:cd16028 218 fspgaanaadlddeEVAQMRatYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ---LGDHW-LWG-KDGFFD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 349 GGiravgfVHSPLL---------KNKGTVCKELVHITDWYPTLISLAEGQIDEdiQLDGydiwetiseglRS--PrvdIL 417
Cdd:cd16028 293 QA------YRVPLIvrdprreadATRGQVVDAFTESVDVMPTILDWLGGEIPH--QCDG-----------RSllP---LL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 418 HNIDPiytkakngswaagyGIWNTAIqsairvqHWKLLTGNPGYSDwvpPQAFSNLGPNR-----WHNERITLS--TGKS 490
Cdd:cd16028 351 AGAQP--------------SDWRDAV-------HYEYDFRDVSTRR---PQEALGLSPDEcslavIRDERWKYVhfAALP 406
|
490 500 510
....*....|....*....|....*....|...
gi 77416378 491 IWLFNITADPYERVDLSSR--YPGIVKKLLRRL 521
Cdd:cd16028 407 PLLFDLKNDPGELRDLAADpaYAAVVLRYAQKL 439
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
74-325 |
2.14e-13 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 70.79 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADdqGFRD---VGYHGSEIKTPTLDKLAAEGVKLENYYVQPICTP-SRSQFitgkyQIHTGLQHSIIRPTQPN 149
Cdd:cd16015 1 PNVIVILLE--SFSDpyiDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGtANGEF-----EVLTGLPPLPLGSGSYT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 150 CLPLDNA-TLPQKLKEVGYSTHMVGKWHLGFYRKDCMPTKRGFDTFFGSllgsgDYYTH--YKCDSPGVCGYDLYEndna 226
Cdd:cd16015 74 LYKLNPLpSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDL-----EDFPDdeKETNGWGVSDESLFD---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 227 awdydngiystqmytqRVQQILATHDPtKPLFLY-VAYQAvHSPLQAPGRYFEHYRSIININR--RRYAAMLSCLDEAIH 303
Cdd:cd16015 145 ----------------QALEELEELKK-KPFFIFlVTMSN-HGPYDLPEEKKDEPLKVEEDKTelENYLNAIHYTDKALG 206
|
250 260
....*....|....*....|..
gi 77416378 304 NVTLALKRYGFYNNSIIIYSSD 325
Cdd:cd16015 207 EFIEKLKKSGLYENTIIVIYGD 228
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
74-386 |
3.03e-12 |
|
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: 66.68 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSEIK-TPTLDKLAAEGVKLENYYVQPIC--TPSRSQFITGKYQIHTGL-QHSIIRPTQPN 149
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPtTPNLKRLASEGATFNFRSVSPPTssAPNHAALLTGAYPTLHGYtGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 150 C---LPLDNATLPQKLKEVGYSTHMVGkwhlgfyrkdcmptkrgFDTFfgsllgsgdyythykcdspgvcgydLYENDNA 226
Cdd:cd00016 81 RaagKDEDGPTIPELLKQAGYRTGVIG-----------------LLKA-------------------------IDETSKE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 227 awdydngiystqmytqrvqqilathdptKPLFLYVAYQAVHSPLQAPGRYFEhyrsiininrrRYAAMLSCLDEAIHNVT 306
Cdd:cd00016 119 ----------------------------KPFVLFLHFDGPDGPGHAYGPNTP-----------EYYDAVEEIDERIGKVL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 307 LALKRYGFYNNSIIIYSSDNGGQPtAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKnKGTVCKELVHITDWYPTLISLA 386
Cdd:cd00016 160 DALKKAGDADDTVIIVTADHGGID-KGHGGDPKADGKADKSHTGMRVPFIAYGPGVK-KGGVKHELISQYDIAPTLADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
61-401 |
1.41e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 67.37 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 61 DERPEAGTAGTSQ-PHLIFILADdqGFRD--VGYHGSEIK-TPTLDKLAAEGVKLENYYVQPICTpSRSQFItgkyqIHT 136
Cdd:COG1368 221 SNRPTPNPFGPAKkPNVVVILLE--SFSDffIGALGNGKDvTPFLDSLAKESLYFGNFYSQGGRT-SRGEFA-----VLT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 137 GL----QHSIIRPTQPNCLPldnaTLPQKLKEVGYSTHMvgkWH---LGFYRKDCMPTKRGFDTFFGsllgsGDYYTHYK 209
Cdd:COG1368 293 GLpplpGGSPYKRPGQNNFP----SLPSILKKQGYETSF---FHggdGSFWNRDSFYKNLGFDEFYD-----REDFDDPF 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 210 CDSPGVCGYDLYendnaawdydngiystqmytQRVQQILATHDptKPLFLYVayQAV--HSPLQAPgryfEHYRSIININ 287
Cdd:COG1368 361 DGGWGVSDEDLF--------------------DKALEELEKLK--KPFFAFL--ITLsnHGPYTLP----EEDKKIPDYG 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 288 RRRYAAMLSCL---DEAIHNVTLALKRYGFYNNSIIIYSSDNGGqptaggsnwPLRGSKGTYWEGGIRAV-GFVHSPLLK 363
Cdd:COG1368 413 KTTLNNYLNAVryaDQALGEFIEKLKKSGWYDNTIFVIYGDHGP---------RSPGKTDYENPLERYRVpLLIYSPGLK 483
|
330 340 350
....*....|....*....|....*....|....*...
gi 77416378 364 NKGTVcKELVHITDWYPTLISLAEGQIDEDIQLdGYDI 401
Cdd:COG1368 484 KPKVI-DTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
74-470 |
4.10e-08 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 55.63 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 74 PHLIFILADDQGFRDVGYHGSE-IKTPTLDKLAAEGVKLENYYVQ-PICTPSRSQFITGkyqIHTGLQHSIirpTQPNCL 151
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQvVDLPYINFMKQHGSVFLNAYTNsPICCPSRAAMWSG---LFTHLTESW---NNYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 152 PLDNATLPQKLKEVGYSTHMVGKWhlgfyrkdcmptkrgfdtffgsllgsgDYythykcdspgVCGYDLYENDNAAWDYD 231
Cdd:cd16171 75 DPNYPTWMDRLEKHGYHTQKYGKL---------------------------DY----------TSGHHSVSNRVEAWTRD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 232 NGIYSTQ-----------MYTQRVQQI------LATH-------DPTKPLFLYVAYQAVHS-PLQAPGryfEHYRSIINI 286
Cdd:cd16171 118 VPFLLRQegrptvnlvgdRSTVRVMLKdwqntdKAVHwirkeapNLTQPFALYLGLNLPHPyPSPSMG---ENFGSIRNI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 287 nRRRYAAMLSCLDEAIHNVTLALKRYGFYNNSIIIYSSDNGGQPTAGGSNWplrgsKGTYWEGGiravgfVHSPLLK--- 363
Cdd:cd16171 195 -RAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFY-----KMSMYEGS------SHVPLLImgp 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 364 --NKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDGYDIWETISEGlrsprvdilhNIDPIYTKAKNGSWAAG--YGIW 439
Cdd:cd16171 263 giKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSES----------SIKESPSRVPHPDWVLSefHGCN 330
|
410 420 430
....*....|....*....|....*....|.
gi 77416378 440 NTAIQSAIRVQHWKLLTGNPGYSdwVPPQAF 470
Cdd:cd16171 331 VNASTYMLRTNSWKYIAYADGNS--VPPQLF 359
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
446-531 |
4.95e-04 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 40.37 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77416378 446 AIRVQHWKL--LTGNpgysdWVPPQA---FSNLGPNRWHNERItlstgksiwLFNITADPYERVDL---SSRYPGIVKKL 517
Cdd:pfam14707 16 AVRWGPYKAhfFTPS-----FDPPGAegcYGSKVPVTHHDPPL---------LFDLERDPSEKYPLspdSPEYPEVLAEI 81
|
90
....*....|....
gi 77416378 518 LRRLSQFNKTAVPV 531
Cdd:pfam14707 82 KAAVEEHKATLVPV 95
|
|
| |
