|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-453 |
0e+00 |
|
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: 594.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 114 LPLNETTLAEVLQQAGYVTGMIG----------------FDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 177
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGkwhlgqreaylpnsrgFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 178 dcytdvalplyenlniveqpvnlSSLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQLPAAPW-GRRLYGAG 256
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTsGRGPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 257 LREMDGLVGQIKDKVDR-TAKENTFLWFTGDNGPWAQKCELAgsVGPFTGLWQTRQGGSPAKQTTWEGGHRVPALAYWPG 335
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 336 RVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGeFGALQTVRLERYKAF 415
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
|
410 420 430
....*....|....*....|....*....|....*...
gi 1864488359 416 YITGGARACDGSTGPEMQHKFPLIFNLEDDIAEAMPLE 453
Cdd:cd16161 346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-452 |
1.85e-163 |
|
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: 468.58 E-value: 1.85e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 114 LPLNETTLAEVLQQAGYVTGMI----------------GFDYYFGIPYSHDMGCTDTPGYNHPPCPAcpqgdgpsrnlqr 177
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVgkwhlghqpeflptrhGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 178 dcytdvalPLYENLNIVEQPVNLSSLAQKYAEKATQFIQQAstSGRPFLLYVGLAHMHVPLPVTQLPAAPWGRRLYGAGL 257
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 258 REMDGLVGQIKDKVDRT-AKENTFLWFTGDNGPWAQKCELAGSVGPFTGlwqtrqggspAKQTTWEGGHRVPALAYWPGR 336
Cdd:cd16026 218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 337 VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefGALQTVRLERYKAF 415
Cdd:cd16026 288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKsPPHPFFYYYDG------GDLQAVRSGRWKLH 361
|
410 420 430
....*....|....*....|....*....|....*..
gi 1864488359 416 YITGGARACDGSTGPEMQHKFPLIFNLEDDIAEAMPL 452
Cdd:cd16026 362 LPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-499 |
9.58e-109 |
|
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: 332.10 E-value: 9.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 114 LPLNETTLAEVLQQAGYVTGMI------------------GFDYYFGIPYSHDMG-CTD-TPGYNHPPC-PACPQGDGPs 172
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVgkwhlgvglngtylpthqGFDHYLGIPYSHDQGpCQNlTCFPPNIPCfGGCDQGEVP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 173 rnlqrdcytdvaLPLYENLNIVEQPVNLSSLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQLPAAPWGRRL 252
Cdd:cd16158 160 ------------CPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 253 YGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSvgpfTGLWQTRQGgspakqTTWEGGHRVPALA 331
Cdd:cd16158 228 FGDALAELDGSVGELLQTLKENGiDNNTLVFFTSDNGPSTMRKSRGGN----AGLLKCGKG------TTYEGGVREPAIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 332 YWPGRVPVNVTStALLSVLDIFPTVVALAQASLPQgRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGALqTVRLER 411
Cdd:cd16158 298 YWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN-VTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWGK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 412 YKAFYITGGA--------RACDGSTgPEMQHKFPLIFNLEDDIAEAMPLErGGTEYRAVLPKVRKVLADILQDI--ANDS 481
Cdd:cd16158 375 YKAHFYTQGAahsgttpdKDCHPSA-ELTSHDPPLLFDLSQDPSENYNLL-GLPEYNQVLKQIQQVKERFEASMkfGESE 452
|
490
....*....|....*...
gi 1864488359 482 ISRADytlDPSVTPCCNP 499
Cdd:cd16158 453 INKGE---DPALEPCCKP 467
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-471 |
2.42e-101 |
|
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: 311.67 E-value: 2.42e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---THNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 112 GGLPLNETTLAEVLQQAGYVTGMIGfDYYFGI-PYSHDMGC------------TDTPGYNHPPC-PACPQGDGPSRNLqr 177
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVG-KWHLGInENNHSDGAhlpshhgfdfvgTNLPFTNSWACdDTGRHVDFPDRSA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 178 dCYtdvalpLYENLNIVEQPVNLSSLAQKYAEKATQFIQqaSTSGRPFLLYVGLAHMHVPLPVTQLPAAPWGRRLYGAGL 257
Cdd:cd16160 158 -CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 258 REMDGLVGQIKDK-VDRTAKENTFLWFTGDNGPWAQKCELAGSVGPFTGlwqtrqggspAKQTTWEGGHRVPALAYWPGR 336
Cdd:cd16160 229 NEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGIRVPFIAYWPGT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 337 VPVNVtSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefgALQTVRLERYKAF 415
Cdd:cd16160 299 IKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADsPHDDILYYCCS-------RLMAVRYGSYKIH 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864488359 416 YITG--------GARACDGSTGPE------------MQHKFPLIFNLEDDIAEAMPLErgGTEYRAVLPKVRKVLA 471
Cdd:cd16160 371 FKTQplpsqeslDPNCDGGGPLSDyivcydcedecvTKHNPPLIFDVEKDPGEQYPLQ--PSVYEHMLEAVEKLIA 444
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-472 |
7.07e-87 |
|
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: 275.11 E-value: 7.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTHNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 111 ----VGGLPLNETTLAEVLQQAGYVTGMIG----------------FDYYFGIPYSHdMGCTDTPGYNHPPcpacpqgdg 170
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGkwhlghrpqyhplkhgFDEWFGAPNCH-FGPYDNKAYPNIP--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 171 psrnLQRDcyTDVALPLYENLNIvEQPVNLSSLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQLPAAPWGR 250
Cdd:cd16157 151 ----VYRD--WEMIGRYYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 251 RLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNG-PWAQKCELAGSVGPFTGlwqtrqggspAKQTTWEGGHRVP 328
Cdd:cd16157 224 GLYGDAVMELDSSVGKILESLKSLGiENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMREP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 329 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSgaagefgALQTVR 408
Cdd:cd16157 294 AIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMAVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 409 LERYKAFYIT---------GGARACDG------STGPEMQH-KFPLIFNLEDDIAEAMPLERGGTEYRAVLPKVRKVLAD 472
Cdd:cd16157 367 LGQYKAHFWTwsnsweefrKGINFCPGqnvpgvTTHNQTDHtKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQ 446
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
28-448 |
1.26e-85 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 269.44 E-value: 1.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 28 SGKARGQKPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFA 107
Cdd:COG3119 16 AAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 108 vTSVGGLPLNETTLAEVLQQAGYVTGMIgfdyyfgipyshdmgctdtpGYNHppcpacpqgdgpsrnlqrdcytdvalpL 187
Cdd:COG3119 96 -GYNGGLPPDEPTLAELLKEAGYRTALF--------------------GKWH---------------------------L 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 188 YenlniveqpvnlssLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVP-----------------LPVTQLPAAPW-- 248
Cdd:COG3119 128 Y--------------LTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldkydgkdipLPPNLAPRDLTee 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 249 ----GRRLYGAGLREMDGLVGQIKDKVDRT-AKENTFLWFTGDNGPWAqkcelagsvgpftGLWQTRQGgspaKQTTWEG 323
Cdd:COG3119 194 elrrARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEHGLRGG----KGTLYEG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 324 GHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLFHpnsgAAGEFGA 403
Cdd:COG3119 257 GIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYW----EYPRGGG 330
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1864488359 404 LQTVRLERYKAFYitggaraCDGSTGPEMqhkfplIFNLEDDIAE 448
Cdd:COG3119 331 NRAIRTGRWKLIR-------YYDDDGPWE------LYDLKNDPGE 362
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-491 |
1.71e-85 |
|
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: 273.01 E-value: 1.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN------FAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 109 TSVGGLPLNETTLAEVLQQAGYVTGMIG----------------------FDYYFGIPYSHDMGCTDTPG--YNHPPCPA 164
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGkwhlglhcesrndfchhplnhgFDYFYGLPLTNLKDCGDGSNgeYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 165 CPQgdgpSRNLQRDCYTDVALPLY--------------------------------------ENLNIVEQPVNLSSLAQK 206
Cdd:cd16159 161 FPL----LTAFVLITALTIFLLLYlgavskrffvfllilsllfislfflllitnryfncilmRNHEVVEQPMSLENLTQR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 207 YAEKATQFIQQasTSGRPFLLYVGLAHMHVPLPVTQLPAAPWGRRLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTG 285
Cdd:cd16159 237 LTKEAISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYFTS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 286 DNGPWAqkcELAGSVGPFTGLWQTRQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLP 365
Cdd:cd16159 315 DNGGHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 366 QGRRFDGVDVSEVLFGRSQ-PGHRVLFH------------PNSGAAgefgalqtvrleRYKAFYIT-----GGARA---- 423
Cdd:cd16159 390 SDRIIDGRDLMPLLTGQEKrSPHEFLFHycgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEGCcgtl 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864488359 424 ---CDGSTGpeMQHKFPLIFNLEDDIAEAMPLERGGTEYRAVLPKVRKVLADilqdiANDSISRADYTLDP 491
Cdd:cd16159 458 lcrCFGDSV--THHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAE-----HQSSIEPVESQLSF 521
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-452 |
4.26e-81 |
|
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: 257.08 E-value: 4.26e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGAN---WAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 113 GLPLNETTLAEVLQQAGYVTGMIG----------------FDYYFGIPYSHdmgctdtpgynhppcpacpqgdgpsrnlq 176
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGkwhlgdedgrlptdhgFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 177 rdcytdvalplyenlniveqpvnlssLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVP-LPVTQLPAAPWGRRLYGA 255
Cdd:cd16142 131 --------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPtLPSPEFEGKSSGKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 256 GLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSvGPFTGlwqtrqggspAKQTTWEGGHRVPALAYWP 334
Cdd:cd16142 185 SMVELDDHVGQILDALDELGiADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 335 GRVPVNVTSTALLSVLDIFPTVVALAQASLP------QGRRFDGVDVSEVLFGRS-QPGHRVLFHpnsGAAGEFGAlqtV 407
Cdd:cd16142 254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1864488359 408 RLERYKA-FYITGGARAcdGSTGPEMQHKFPLIFNLEDDIAEAMPL 452
Cdd:cd16142 328 RWKNWKVhFKAQEDTGG--PTGEPFYVLTFPLIFNLRRDPKERYDV 371
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-448 |
1.11e-73 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 238.25 E-value: 1.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETK-DTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGL 114
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGG--VLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 115 PL---NETTLAEVLQQAGYVTGMIG-----FDYYFGIPYSHDMGCTDTPGYNHPPcpacpqGDGPsrnLQR--D-CYTDV 183
Cdd:cd16143 79 PLiepDRVTLAKMLKQAGYRTAMVGkwhlgLDWKKKDGKKAATGTGKDVDYSKPI------KGGP---LDHgfDyYFGIP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 184 AlplyenlniveqpvnlSSLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLpvtqLPAAPW-GRrlYGAGLR---- 258
Cdd:cd16143 150 A----------------SEVLPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPI----VPSPEFqGK--SGAGPYgdfv 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 259 -EMDGLVGQIKDKVDRTA-KENTFLWFTGDNGP----WAQKCELAG--SVGPFTGLwqtrqggspaKQTTWEGGHRVPAL 330
Cdd:cd16143 208 yELDWVVGRILDALKELGlAENTLVIFTSDNGPspyaDYKELEKFGhdPSGPLRGM----------KADIYEGGHRVPFI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 331 AYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRV-LFHpnSGAAGEFgalqTVR- 408
Cdd:cd16143 278 VRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVREsLVH--HSGNGSF----AIRk 351
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1864488359 409 ----LERYKAFYITGGARACDGSTGPEMQhkfplIFNLEDDIAE 448
Cdd:cd16143 352 gdwkLIDGTGSGGFSYPRGKEKLGLPPGQ-----LYNLSTDPGE 390
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-449 |
1.68e-70 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 230.89 E-value: 1.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--------- 106
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 107 ----AVTSVGGLPLNETTLAEVLQQAGYVTGMIG----------------FDYYFGI-PYSHDMGCTDTPGYNHPPCPAC 165
Cdd:cd16144 81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGkwhlggeggygpedqgFDVNIGGtGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 166 PQGDgpsrnlqrdcytdvalplyenlniveqpvnlsSLAQKYAEKATQFIQQAstSGRPFLLYvgLAH--MHVPLPVTQ- 242
Cdd:cd16144 161 PEGE--------------------------------YLTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPe 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 243 -------LPAAPWGRR---LYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSVGPFtglwqtRQ 311
Cdd:cd16144 205 liekyekKKKGLRKGQknpVYAAMIESLDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPL------RG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 312 GgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR--V 389
Cdd:cd16144 279 G----KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraL 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864488359 390 LFH-PN-SGAAGEFGAlqTVRLERYK--AFYITGgaracdgstgpemqhKFPLiFNLEDDIAEA 449
Cdd:cd16144 355 FWHfPHyHGQGGRPAS--AIRKGDWKliEFYEDG---------------RVEL-YNLKNDIGET 400
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-448 |
6.35e-68 |
|
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: 224.01 E-value: 6.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 116 LNETTLAEVLQQAGYVTGMI-----------------GFDYYFGIpYSHdmgctdTPGYNHPPcpacPQGDgpsRNLQRd 178
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFgkwglggpgtpghptkqGFDYFYGY-LDQ------VHAHNYYP----EYLW---RNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 179 cytdvaLPLYENLNIVEQPVNLSSLAQK-YAE-----KATQFIQQAstSGRPFLLYVGLAHMHVPLPVTQLPAA------ 246
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYTLPHAPLQVPDDGPYkykpkd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 247 -------PW--GRRLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGP-----WAQKCELAGSVGPFTGLwqtrq 311
Cdd:cd16145 218 pgiyaylPWpqPEKAYAAMVTRLDRDVGRILALLKELGiDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 312 ggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPG-HRVL 390
Cdd:cd16145 293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPE--DIDGISLLPTLLGKPQQQqHDYL 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1864488359 391 FHpnsgAAGEFGALQTVRLERYKAFYItggaracDGSTGPEMqhkfplIFNLEDDIAE 448
Cdd:cd16145 366 YW----EFYEGGGAQAVRMGGWKAVRH-------GKKDGPFE------LYDLSTDPGE 406
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-374 |
3.88e-66 |
|
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: 213.45 E-value: 3.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 116 LNETTLAEVLQQAGYVTGMIGfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdcytdvalplyenlnive 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIG----------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 196 qpvnlsslaqKYAEKATQFIQQASTSgRPFLLYVGLAHMHVPLpvtqlpaapwgrrLYGAGLREMDGLVGQIKDKVDRTA 275
Cdd:cd16022 100 ----------KWHDEAIDFIERRDKD-KPFFLYVSFNAPHPPF-------------AYYAMVSAIDDQIGRILDALEELG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 276 K-ENTFLWFTGDNGpwaqkcelaGSVGPFTGLWQtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFP 354
Cdd:cd16022 156 LlDNTLIVFTSDHG---------DMLGDHGLRGK--------KGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLP 218
|
330 340
....*....|....*....|
gi 1864488359 355 TVVALAQASLPQGrrFDGVD 374
Cdd:cd16022 219 TLLDLAGIEPPEG--LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-391 |
4.31e-63 |
|
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: 211.25 E-value: 4.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTHnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 114 LPLNETTLAEVLQQAGYVTGMI----------------GFDYYFGIPYSHDmgcTDTPGYnhppcpacpqgdgpsrnLQR 177
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFgkwhlgdnypyrpqdrGFDEVLGHGGGGI---GQYPDY-----------------WGN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 178 DCYTDValpLYENlNIVEQpvnlsslAQKYA-----EKATQFIQQASTsgRPFLLYVGLAHMHVPLpvtQLPAAPWGrRL 252
Cdd:cd16146 136 DYFDDT---YYHN-GKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPL---QVPDKYLD-PY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 253 YGAGLRE-----------MDGLVGQIKDKVDRT-AKENTFLWFTGDNGPWaqkcelAGSVGPFTGLWQtrqgGSpaKQTT 320
Cdd:cd16146 199 KDMGLDDklaafygmienIDDNVGRLLAKLKELgLEENTIVIFMSDNGPA------GGVPKRFNAGMR----GK--KGSV 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864488359 321 WEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQP-GHRVLF 391
Cdd:cd16146 267 YEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwPERTLF 338
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-454 |
1.42e-56 |
|
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: 193.54 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 115 PLNETTLAEVLQQAGYVTGMI-----------------GFDYYFGiPYShdmGCTDtpGYNHPPCPACP------QGDGP 171
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVgkwhlgfytweytptnrGFDSFYG-YYG---GAED--YYTHTSGGANDygnddlRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 172 SRNLQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQQASTSgRPFLLYVGLAHMHVPLPVTQLPAAPW-- 248
Cdd:cd16029 154 PAWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYed 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 249 --------GRRLYGAGLREMDGLVGQIKDK-VDRTAKENTFLWFTGDNGPWAQKCElAGSVGPFTGlwqtrqggspAKQT 319
Cdd:cd16029 210 kfahikdeDRRTYAAMVSALDESVGNVVDAlKAKGMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 320 TWEGGHRVPALAYWPGRVPV-NVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR-VLFHPNSGA 397
Cdd:cd16029 279 LWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDIT 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1864488359 398 AGEFGAlqTVRLERYKafYITGgaracdgstgpemqhkFPLiFNLEDDiaeamPLER 454
Cdd:cd16029 359 RTTGGA--AIRVGDWK--LIVG----------------KPL-FNIEND-----PCER 389
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-452 |
1.57e-56 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 192.81 E-value: 1.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 116 LNETTLAEVLQQAGYVTGMIG----FDYYFGIPYSHDMG---------CTDTPGYNHPPCPACPQGDGPSRNLQRDCY-T 181
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGkwqlGGGRGDGDYPHEFGfdeyclwqlTETGEKYSRPATPTFNIRNGKLLETTEGDYgP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 182 DValplyenlniveqpvnlsslaqkYAEKATQFIQQAStsGRPFLLY--VGLAH-MHVPLPVTQLPAAPWGR-----RLY 253
Cdd:cd16151 153 DL-----------------------FADFLIDFIERNK--DQPFFAYypMVLVHdPFVPTPDSPDWDPDDKRkkddpEYF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 254 GAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGpwaqkcelagSVGPFTGLW--QTRQGGspaKQTTWEGGHRVPAL 330
Cdd:cd16151 208 PDMVAYMDKLVGKLVDKLEELGlRENTIIIFTGDNG----------THRPITSRTngREVRGG---KGKTTDAGTHVPLI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 331 AYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGALQTVRLE 410
Cdd:cd16151 275 VNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRFVRTK 354
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1864488359 411 RYKaFYITGgaracdgstgpemqhKFpliFNLEDDIAEAMPL 452
Cdd:cd16151 355 RYK-LYADG---------------RF---FDLREDPLEKNPL 377
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-417 |
1.86e-50 |
|
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: 176.54 E-value: 1.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGA--NWAETkdtTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 114 LPLNETTLAEVLQQAGYVTGMIGF-DYYFGIPYSHDMGCTDTPGYNHPpcpacpqgdgpsrnlqrdcytdvalplyenln 192
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKtHYNPDAVFPFDDEMRGPDDGGRN-------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 193 iveqpvnlsslAQKYAEKATQFIQQAStSGRPFLLYVGLAHMH-----------------VPLPvTQLPAAPWGRR---L 252
Cdd:cd16027 124 -----------AWDYASNAADFLNRAK-KGQPFFLWFGFHDPHrpyppgdgeepgydpekVKVP-PYLPDTPEVREdlaD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 253 YGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcelagsvGPFTGlwqtrqggspAKQTTWEGGHRVPALA 331
Cdd:cd16027 191 YYDEIERLDQQVGEILDELEEDGLlDNTIVIFTSDHG------------MPFPR----------AKGTLYDSGLRVPLIV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 332 YWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLF-----HpnsgaaGEFGALQ- 405
Cdd:cd16027 249 RWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVFaerdrH------DETYDPIr 320
|
410
....*....|..
gi 1864488359 406 TVRLERYKafYI 417
Cdd:cd16027 321 SVRTGRYK--YI 330
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-362 |
4.89e-50 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 173.38 E-value: 4.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 116 LNETTLAEVLQQAGYVTGMIGfdYYFGIPYSHDMGCTDtpGYNHPPcpacpqGDGPSRNLQRDCYtdvalplyenlNIVE 195
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIG--KWHLGWYNNQSPCNL--GFDKFF------GRNTGSDLYADPP-----------DVPY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 196 QPVNLSSLAQKYAEKATQFIQQAStsgRPFLLYVGLAHMHVPLPVTQLPAAPWG------------RRLYGAGLREMDGL 263
Cdd:pfam00884 136 NCSGGGVSDEALLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 264 VGQIKDKVDRTAK-ENTFLWFTGDNGPwaqkcelagSVGPFTGLWQTRQGGspakqTTWEGGHRVPALAYWPGRVPVNVT 342
Cdd:pfam00884 213 IGRVLDKLEENGLlDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGYRVPLLIWSPGGKAKGQK 278
|
330 340
....*....|....*....|
gi 1864488359 343 STALLSVLDIFPTVVALAQA 362
Cdd:pfam00884 279 SEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-449 |
2.56e-48 |
|
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: 171.86 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 34 QKPNFVIILADDIGWGDLGANWAETkDTTNLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGV-THNFAVTSVG 112
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGMgTMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 113 G----LPLNETTLAEVLQQAGYVTGMIG------FDYYFgipySHDmgctdtpgynhppcpacpqgdgpsrnlqrdcytd 182
Cdd:cd16025 79 GyegyLPDSAATIAEVLKDAGYHTYMSGkwhlgpDDYYS----TDD---------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 183 valplyenlniveqpvnlsslaqkYAEKATQFIQQASTSGRPFLLYvgLAH--MHVPL---------------------- 238
Cdd:cd16025 121 ------------------------LTDKAIEYIDEQKAPDKPFFLY--LAFgaPHAPLqapkewidkykgkydagwdalr 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 239 --------------PVTQLPA-----APW-----------GRR--LYGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTG 285
Cdd:cd16025 175 eerlerqkelglipADTKLTPrppgvPAWdslspeekkleARRmeVYAAMVEHMDQQIGRLIDYLKELGElDNTLIIFLS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 286 DNGP-----WAQkcelAGSvGPFTGlwqtrqggspAKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLSVLDIFPTVVAL 359
Cdd:cd16025 255 DNGAsaepgWAN----ASN-TPFRL----------YKQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVIDIAPTILEL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 360 AQASLPQGRR------FDGVDVSEVLFGRSQPG-HRVLFHPNSGAAGefgalqtVRLERYKAFYITGGaracdGSTGPEM 432
Cdd:cd16025 320 AGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSrRRTQYFELFGNRA-------IRKGGWKAVALHPP-----PGWGDQW 387
|
490
....*....|....*..
gi 1864488359 433 QhkfplIFNLEDDIAEA 449
Cdd:cd16025 388 E-----LYDLAKDPSET 399
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-372 |
3.17e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 145.84 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----THNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 111 VG-GLPLNETTLAEVLQQAGYVTGMIGfDYYFGipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdcytdvalplye 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSG-KWHLG----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 190 nlniveqpvnlsslaqkyaEKATQFIQQASTSGRPFLLYVGlahmhvplpvTQLPAAPWGrrlYGAGLREMDGLVGQIKD 269
Cdd:cd16149 113 -------------------DDAADFLRRRAEAEKPFFLSVN----------YTAPHSPWG---YFAAVTGVDRNVGRLLD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 270 KVDRTA-KENTFLWFTGDNGpwaqkcelagsvgpFT----GLWQTRQGGSPakQTTWEGGHRVPALAYWPGRVPVNVTST 344
Cdd:cd16149 161 ELEELGlTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNMYDNSVKVPFIIRWPGVVPAGRVVD 224
|
330 340
....*....|....*....|....*...
gi 1864488359 345 ALLSVLDIFPTVVALAQASLPQGRRFDG 372
Cdd:cd16149 225 SLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-445 |
2.29e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 147.33 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 115 PLNETTLAEVLQQAGYVTGMIG--------------------------FDYYFGipyshdMGCTDtpGYNHPPCpacpQG 168
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGkwhldgperndgraddytppperrhgFDYWKG------YECNH--DHNNPHY----YD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 169 DGPSRNlQRDCYTDVALplyenlniveqpvnlsslaqkyAEKATQFIQQASTSGRPFLLYV--GLAHM---HVP------ 237
Cdd:cd16034 144 DDGKRI-YIKGYSPDAE----------------------TDLAIEYLENQADKDKPFALVLswNPPHDpytTAPeeyldm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 238 -----------LPVTQLPAAPWGR--RLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGpwaqkcELAGSVGPF 303
Cdd:cd16034 201 ydpkklllrpnVPEDKKEEAGLREdlRGYYAMITALDDNIGRLLDALKELGlLENTIVVFTSDHG------DMLGSHGLM 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 304 tglwqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRS 383
Cdd:cd16034 275 ------------NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGK 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864488359 384 QPGHR----VLFHPNSG-AAGEFGALQTVRLERYKafYitggarACDGSTGpemqhkfPLIFNLEDD 445
Cdd:cd16034 341 DDEPDsvllQCFVPFGGgSARDGGEWRGVRTDRYT--Y------VRDKNGP-------WLLFDNEKD 392
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-417 |
1.52e-34 |
|
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: 134.58 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 34 QKPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvGG 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 114 LPLNETTLAEVLQQAGYVTGMIG--------------FDYYFGIPyshdmgctdtpgynhppcpacPQGDgpsrnlqrdc 179
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGkwhlgsggdlpppgFDYWVSFP---------------------GQGS---------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 180 YTDvaLPLYENLNIVEQPVNLSSLaqkYAEKATQFIQQAStSGRPFLLYVG--LAH---------------MHVPLPVTQ 242
Cdd:cd16031 126 YYD--PEFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLSfkAPHrpftpaprhrglyedVTIPEPETF 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 243 LPA-----APWGR------------------------RLYGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaq 292
Cdd:cd16031 200 DDDdyagrPEWAReqrnrirgvldgrfdtpekyqrymKDYLRTVTGVDDNVGRILDYLEEQGLaDNTIIIYTSDNG---- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 293 kcelagsvgpFT----GLwqtrqGGspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgR 368
Cdd:cd16031 276 ----------FFlgehGL-----FD---KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP--E 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1864488359 369 RFDGVDVSEVLFGRSQPGHR------VLFHPNS-GAAGEFGalqtVRLERYKafYI 417
Cdd:cd16031 336 DMQGRSLLPLLEGEKPVDWRkefyyeYYEEPNFhNVPTHEG----VRTERYK--YI 385
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-372 |
5.87e-32 |
|
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: 5.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWgDLGANWAETKdTTNLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 115 P------LNETTLAEVLQQAGYVTGMIGfDYYFGipYSHDMGCTDTP-GYNHPpcpacpqgDGPSRNLQRDCYTdvalpl 187
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAG-KYLNG--YGVPGGVSYVPpGWDEW--------DGLVGNSTYYNYT------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 188 YENLNIVEQPVN-----LSSLaqkYAEKATQFIQQASTSGRPFLLYVG-------------LAHMHVPLPVTQLPA---- 245
Cdd:cd16147 138 LSNGGNGKHGVSypgdyLTDV---IANKALDFLRRAAADDKPFFLVVAppaphgpftpaprYANLFPNVTAPPRPPpnnp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 246 -----APWGRRLYGAG-----------------LREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGPWaqkcelagsvgp 302
Cdd:cd16147 215 dvsdkPHWLRRLPPLNptqiayidelyrkrlrtLQSVDDLVERLVNTLEATGQlDNTYIIYTSDNGYH------------ 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 303 ftgLWQTRQGgsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDG 372
Cdd:cd16147 283 ---LGQHRLP--PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPP--SDMDG 344
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
386-506 |
8.46e-31 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 115.87 E-value: 8.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 386 GHRVLFHpNSGAAgefgaLQTVRLERYKAFYITG-----GARACDGSTGPEMQHKFPLIFNLEDDIAEAMPLERGGTEYR 460
Cdd:pfam14707 2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1864488359 461 AVLPKVRKVLADILQDI--ANDSISRADYTLDPSVTPCCnPYHIACRC 506
Cdd:pfam14707 76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-453 |
1.05e-30 |
|
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: 122.67 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 34 QKPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRlglrngvtHNFAVT 109
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR--------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 110 SVGG--LPLNETTLAEVLQQAGYVTGMIgfdyyfgipyshdmgctdtpGYNHPPcpacpqgdgpsrnlqrdcytdvalpl 187
Cdd:cd16155 73 EGGKaaIPSDDKTWPETFKKAGYRTFAT--------------------GKWHNG-------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 188 yenlniveqpvnlsslaqkYAEKATQFIQQASTSGRPFLLYVGLAHMH-----------------VPLPVTQLPA----- 245
Cdd:cd16155 107 -------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHdprqappeyldmyppetIPLPENFLPQhpfdn 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 246 ----------APWGRRL---------YGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkceLA-GSvgpfT 304
Cdd:cd16155 168 gegtvrdeqlAPFPRTPeavrqhlaeYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG-------LAvGS----H 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 305 GLwqtrQGgspaKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQ 384
Cdd:cd16155 237 GL----MG----KQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKK 305
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 385 PGHRVLFhpnsgaaGEFGALQ-TVRLERYKAFYITGGAracdgstgpemqhKFPLIFNLEDDiaeamPLE 453
Cdd:cd16155 306 AVRDTLY-------GAYRDGQrAIRDDRWKLIIYVPGV-------------KRTQLFDLKKD-----PDE 350
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-360 |
1.15e-28 |
|
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: 113.67 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTHNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 110 SVGGLPLNETTLAEVLQQAGYVTGMIGFDyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdcytdvalplye 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIGLL--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 190 nlniveqpvnlsslaqkyaekatQFIQQaSTSGRPFLLYVGLAHMHVPL--PVTQLPaapwgrrLYGAGLREMDGLVGQI 267
Cdd:cd00016 110 -----------------------KAIDE-TSKEKPFVLFLHFDGPDGPGhaYGPNTP-------EYYDAVEEIDERIGKV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 268 KDKVDRTAK-ENTFLWFTGDNGpwaqkcelagsvGPFTGLwqTRQGGSPAKQTTWEGGHRVPALAYWPGrVPVNVTSTAL 346
Cdd:cd00016 159 LDALKKAGDaDDTVIIVTADHG------------GIDKGH--GGDPKADGKADKSHTGMRVPFIAYGPG-VKKGGVKHEL 223
|
330
....*....|....
gi 1864488359 347 LSVLDIFPTVVALA 360
Cdd:cd00016 224 ISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-377 |
2.31e-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: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGA-NWAETKD---------TTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTGMIGFDYYfgipyshdmgctdtpgynhppcpacpqgdgpsRNLQRdcYTDVA 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHL--------------------------------EAFQR--YLKNA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 185 LPLYENLNIVEqpvnlsslaqkyaekatqfIQQASTSGrPFLLYVGLAHMHVPLpvtqLPAAPWGRRL-YGAGLREMDGL 263
Cdd:cd16153 125 NQSYKSFWGKI-------------------AKGADSDK-PFFVRLSFLQPHTPV----LPPKEFRDRFdYYAFCAYGDAQ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 264 VGQIKDKVDR----TAKENTFLWFTGDNGpwaqkcelagsvgpftglWQTRQGGSPAKQTTWEGGHRVPALAYWPGR--V 337
Cdd:cd16153 181 VGRAVEAFKAyslkQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQSHRVPLIVVSSDKlkA 242
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1864488359 338 PVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 377
Cdd:cd16153 243 PAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-448 |
2.58e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 115.91 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWgDLGANWAETKD---TTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGvthnfaVTSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTG------VLAVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 113 G-LPLNETTL--AEVLQQ--AGYVTGMIGfDYYFGipyshdmGCTDTPgyNHPpcpacpqGDGPSrnlqrdcYTDV---A 184
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIG-KWHLG-------GNDNSP--NNP-------GGIPY-------YAGIlggG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 185 LPLYENLNIVEQPVNLSS---LAQKYAEKATQFIQQASTsgrPFLLYVGLAHMHVP--LPVTQL------------PAAP 247
Cdd:cd16154 129 VQDYYNWNLTNNGQTTNSteyATTKLTNLAIDWIDQQTK---PWFLWLAYNAPHTPfhLPPAELhsrsllgdsadiEANP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 248 wgRRLYGAGLREMDGLVGQIKDKVDRTAKENTFLWFTGDNG-PwaqkcelagsvGPFTGLWQTRQGgspAKQTTWEGGHR 326
Cdd:cd16154 206 --RPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYTRNH---AKGSLYEGGIN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 327 VPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGAlqt 406
Cdd:cd16154 270 VPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQYNYTEYESPTTTGWA--- 344
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1864488359 407 VRLERYKAFYITGGARAcdgstgpemqhkfplIFNLEDDIAE 448
Cdd:cd16154 345 TRNQYYKLIESENGQEE---------------LYDLINDPSE 371
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-412 |
1.46e-27 |
|
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: 114.59 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 34 QKPNFVIILADD----IGWgdLGANWAETKdttNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtHNFAVT 109
Cdd:cd16030 1 KKPNVLFIAVDDlrpwLGC--YGGHPAKTP---NIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV-YDNNSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 110 SVGGLPlNETTLAEVLQQAGYVTGMIGFDYYFGIPYSHDMGCTDTPGYNHPPCPACPQGDGPSRNLQRDCytDVALPLYE 189
Cdd:cd16030 75 FRKVAP-DAVTLPQYFKENGYTTAGVGKIFHPGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKG--GGGGPAWE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 190 NLNIVEqpvnlSSLA-QKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQ---------------------LPAAP 247
Cdd:cd16030 152 AADVPD-----EAYPdGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKkyfdlyplesiplpnpfdpidLPEVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 248 WG-------------------------------RRLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGpWA--QK 293
Cdd:cd16030 227 WNdlddlpkygdipalnpgdpkgplpdeqarelRQAYYASVSYVDAQVGRVLDALEELGlADNTIVVLWSDHG-WHlgEH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 294 celagsvgpftGLWqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQasLPQGRRFDGV 373
Cdd:cd16030 306 -----------GHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGK 364
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1864488359 374 DVSEVLFGRSQPGHRVLF--HPNSGAAGEfgalqTVRLERY 412
Cdd:cd16030 365 SLVPLLKNPSAKWKDAAFsqYPRPSIMGY-----SIRTERY 400
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-416 |
4.29e-27 |
|
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: 113.08 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 114 LPLNETTLAEVLQQAGYvtgmigfdyyfgipyshDMGCTdtpGYNHppcpaCPQGDGPSrnlqrDCYtdvalplYENLNI 193
Cdd:cd16033 81 LPPGVETFSEDLREAGY-----------------RNGYV---GKWH-----VGPEETPL-----DYG-------FDEYLP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 194 VEqpvnlSSLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMH-----------------VPLP------------VTQLP 244
Cdd:cd16033 124 VE-----TTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHdpyippepyldmydpedIPLPesfaddfedkpyIYRRE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 245 AAPWG------------RRLYGAGLREMDGLVGQIKDKVDRT-AKENTFLWFTGDNGpwaqkcELAGSvgpfTGLWqtRQ 311
Cdd:cd16033 199 RKRWGvdtedeedwkeiIAHYWGYITLIDDAIGRILDALEELgLADDTLVIFTSDHG------DALGA----HRLW--DK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 312 GGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHR--V 389
Cdd:cd16033 267 GPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGEQPEDWRdeV 339
|
410 420 430
....*....|....*....|....*....|
gi 1864488359 390 L--FHPNsgaagEFGALQT-VRLERYKAFY 416
Cdd:cd16033 340 VteYNGH-----EFYLPQRmVRTDRYKYVF 364
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-374 |
1.09e-26 |
|
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: 108.79 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILAD----DIgwgdLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHnfavtsv 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 112 GGLPLNETTLAEVLQQAGYVTGMIgfdyyfgipyshdmgcTDTPGYnhppcpacpqgdGPSRNLQRDCYTDVALPLYENL 191
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAV----------------SSNPHL------------FGGPGFDRGFDTFEDFRGQEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 192 NIVEQPVNlsslAQKYAEKATQFIQQASTSgRPFLLYVglaHM---HvplpvtqlpaAPWgrrLYGAGLREMDGLVGQIK 268
Cdd:cd16148 122 PGEEGDER----AERVTDRALEWLDRNADD-DPFFLFL---HYfdpH----------EPY---LYDAEVRYVDEQIGRLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 269 DKVDRT-AKENTFLWFTGDNGpwaqkcELAGSVGPFTGlwqtrqGGSPAkqttWEGGHRVPALAYWPGRVPVNVTStALL 347
Cdd:cd16148 181 DKLKELgLLEDTLVIVTSDHG------EEFGEHGLYWG------HGSNL----YDEQLHVPLIIRWPGKEPGKRVD-ALV 243
|
330 340
....*....|....*....|....*..
gi 1864488359 348 SVLDIFPTVVALAQASLPqgRRFDGVD 374
Cdd:cd16148 244 SHIDIAPTLLDLLGVEPP--DYSDGRS 268
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
31-476 |
1.24e-25 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 109.76 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 31 ARGQKPNFVIILADDigW-GD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNG 101
Cdd:PRK13759 2 VQTKKPNIILIMVDQ--MrGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 102 VTHNFavtsvgglplnETTLAEVLQQAGYVTGMIGFDYYFgiPYSHDMGCTDT---PGY------NHPPCPACP------ 166
Cdd:PRK13759 80 VPWNY-----------KNTLPQEFRDAGYYTQCIGKMHVF--PQRNLLGFHNVllhDGYlhsgrnEDKSQFDFVsdylaw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 167 -QGDGPSRN-----LQRDCYTDVALP--LYENLNiveqPVNLSslaqkyAEKATQFIQQAStSGRPFLLYVGLAHMHVPL 238
Cdd:PRK13759 147 lREKAPGKDpdltdIGWDCNSWVARPwdLEERLH----PTNWV------GSESIEFLRRRD-PTKPFFLKMSFARPHSPY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 239 ------------------------------PVTQLPAAPWG----------RRLYGAGLREMDGLVGQIKDKV-DRTAKE 277
Cdd:PRK13759 216 dppkryfdmykdadipdphigdweyaedqdPEGGSIDALRGnlgeeyarraRAAYYGLITHIDHQIGRFLQALkEFGLLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 278 NTFLWFTGDNGpwaqkcELAGSvgpfTGLWQtrqggspaKQTTWEGGHRVPALAYWPG---RVPVNVTSTALLSVLDIFP 354
Cdd:PRK13759 296 NTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 355 TVVALAQASLPqgRRFDGVDVSEVLFGrSQPGHRVLFHpnsgaaGEFGALqtvrlerYKAF-YITGGaracdgstgpemQ 433
Cdd:PRK13759 358 TLLDLAGGTIP--DDVDGRSLKNLIFG-QYEGWRPYLH------GEHALG-------YSSDnYLTDG------------K 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1864488359 434 HKF--------PLIFNLEDDIAEAMPLErGGTEYRAVLPKVRKVLADILQD 476
Cdd:PRK13759 410 WKYiwfsqtgeEQLFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-445 |
2.76e-25 |
|
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: 106.12 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 116 LNETTLAEVLQQAGYVTGM------IGFDYYFGipYSHDmgctdtpgynhppcpacpqgdgpsrnlqrdcyTDVALplye 189
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALsgkmhfVGPDQLHG--FDYD--------------------------------EEVAF---- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 190 nlniveqpvnlsslaqkyaeKATQFIQQASTS--GRPFLLYVGLAHMHVPLPVTQ------LPAApwgRRLYGAGLREMD 261
Cdd:cd16032 118 --------------------KAVQKLYDLARGedGRPFFLTVSFTHPHDPYVIPQeywdlyVRRA---RRAYYGMVSYVD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 262 GLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQtrqggspaKQTTWEGGHRVPALAYWPGR-VPV 339
Cdd:cd16032 175 DKVGQLLDTLERTGLaDDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSARVPLIISAPGRfAPR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 340 NVTstALLSVLDIFPTVVALAQASLPQGR-RFDGVDVSEVLFGRSQPGHRVLFHPNSGaAGEFGALQTVRLERYKAFYIT 418
Cdd:cd16032 237 RVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVISEYLA-EGAVAPCVMIRRGRWKFIYCP 313
|
410 420
....*....|....*....|....*..
gi 1864488359 419 GgaracDGstgpemqhkfPLIFNLEDD 445
Cdd:cd16032 314 G-----DP----------DQLFDLEAD 325
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-445 |
5.92e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 105.32 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 116 LNETTLAEVLQQAGYVTGMIGFDYYFGIPYSHdmgctdtpGYNHppcpacpqgdgpsrnlqrdcytdvalplyenlnivE 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH--------GFRY-----------------------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 196 QPVnlsslaqkyAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQ-------LPAapwgRRLYGAGLREMDGLVGQIK 268
Cdd:cd16037 113 RDV---------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQefydlyvRRA----RAAYYGLVEFLDENIGRVL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 269 DKVDRTAK-ENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTAlL 347
Cdd:cd16037 180 DALEELGLlDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPGIPAGKRVKTP-V 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 348 SVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHRVL--FHPNSGAAGEFgalqTVRLERYKAFYITGGAracd 425
Cdd:cd16037 241 SLVDLAPTILEAAGAPPP--PDLDGRSLLPLAEGPDDPDRVVFseYHAHGSPSGAF----MLRKGRWKYIYYVGYP---- 310
|
410 420
....*....|....*....|
gi 1864488359 426 gstgpemqhkfPLIFNLEDD 445
Cdd:cd16037 311 -----------PQLFDLEND 319
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-392 |
1.62e-23 |
|
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: 100.74 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILAD-DIGWGDLGANWAETKdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDqERYPPPWPAGWAALN-LPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 115 PLNETTLAEVLQQAGYVTgmigfdYYFGipYSHdmgCTDTP--GYNHppcpacpqgDGpsrnlqrdcytdvalplyenln 192
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYT------AYKG--KWH---LSGAAggGYKR---------DP---------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 193 iveqpvnlsslaqKYAEKATQFIQQASTS---GRPFLLYVGLAHMH-VPLPVTQLPAAPWGRRLYGAGLREMDGLVGQIK 268
Cdd:cd16035 118 -------------GIAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYYNLIRDVDRQIGRVL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 269 DKVDRTA-KENTFLWFTGDNGpwaqkcELAGSVGpftGLwqtRQGGSPAKQTTwegghRVPALAYWPGRVPVNVTSTALL 347
Cdd:cd16035 185 DALDASGlADNTIVVFTSDHG------EMGGAHG---LR---GKGFNAYEEAL-----HVPLIISHPDLFGTGQTTDALT 247
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1864488359 348 SVLDIFPTVVALAQASLPQ----GRRFDGVDVSEVLfgRSQPGHRV----LFH 392
Cdd:cd16035 248 SHIDLLPTLLGLAGVDAEArateAPPLPGRDLSPLL--TDADADAVrdgiLFT 298
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-383 |
1.16e-16 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 81.90 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRNgvTHNFavtsv 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHRT--LHHL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 112 ggLPLNETTLAEVLQQAGYVTGMIGFDYYFGIPYSHDMGCTDtpgynhppcpacpqgdgpsrnlqrdcytDVAlplyenl 191
Cdd:cd16150 74 --LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYCDS----------------------------DEA------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 192 niveqpvnlsslaqkYAEKATQFIQQASTsGRPFLLYVGLAHMHVP---------------LPVTQLPAAPWGRRLYGAG 256
Cdd:cd16150 117 ---------------CVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPygveepwfsmidrekLPPRRPPGLRAKGKPSMLE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 257 LRE-------------------------MDGLVGQIKDKVDRTA-KENTFLWFTGDNGPWAqkcelagsvGPFtGLWQTR 310
Cdd:cd16150 181 GIEkqgldrwseerwrelratylgmvsrLDHQFGRLLEALKETGlYDDTAVFFFSDHGDYT---------GDY-GLVEKW 250
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864488359 311 QGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSVLDIFPTVVALAqaslpqgrrfdGVDVSEVLFGRS 383
Cdd:cd16150 251 PNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLA-----------GIPLSHTHFGRS 305
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-136 |
1.01e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 78.81 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|..
gi 1864488359 115 PLNETTLAEVLQQAGYVTGMIG 136
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVG 97
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-413 |
1.38e-15 |
|
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: 78.96 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG-VTHNFAVTSvggl 114
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGsWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 115 plNETTLAEVLQQAGYVTGMI------GFDYY-FGIpyshdmgctdtpgynhppcpaCPQGDGPSRNLQRDCYTD----- 182
Cdd:cd16156 77 --NVKTIGQRLSDNGIHTAYIgkwhldGGDYFgNGI---------------------CPQGWDPDYWYDMRNYLDeltee 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 183 ------VALPLYENLNIVEQpvnlSSLAQKYAEKATQFIQQASTsgRPFLLYVGLAHMHVP---------------LPVT 241
Cdd:cd16156 134 errksrRGLTSLEAEGIKEE----FTYGHRCTNRALDFIEKHKD--EDFFLVVSYDEPHHPflcpkpyasmykdfeFPKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 242 Q-----LPAAPWGRRLYGAGLREMDG-------------------LVGQIKDKVDRTAkENTFLWFTGDNGpwaqkcELA 297
Cdd:cd16156 208 EnayddLENKPLHQRLWAGAKPHEDGdkgtikhplyfgcnsfvdyEIGRVLDAADEIA-EDAWVIYTSDHG------DML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 298 GSvgpfTGLWqtrqGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQasLPQGRRFDGVDVSE 377
Cdd:cd16156 281 GA----HKLW----AKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILA 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1864488359 378 VLFGRSQPGHRVLF---------HPNsgaageFGALQTVRL---ERYK 413
Cdd:cd16156 348 TIEDPEIPENRGVFvefgryevdHDG------FGGFQPVRCvvdGRYK 389
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-367 |
5.69e-15 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 76.43 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTHNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 116 LNETTLAEVLQQAGYVTgmigfdyyfgipysHDMGCTDTPGYNHppcpacpqgdgpSRNLQRDCYT-DVALPLYE----- 189
Cdd:cd16171 76 PNYPTWMDRLEKHGYHT--------------QKYGKLDYTSGHH------------SVSNRVEAWTrDVPFLLRQegrpt 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 190 -NLNIVEQPVNLSSLAQKYAEKATQFIQQASTS-GRPFLLYVGLAHMHvPLPVTQLPAAPWG----RRLYGAGLREMDGL 263
Cdd:cd16171 130 vNLVGDRSTVRVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLNLPH-PYPSPSMGENFGSirniRAFYYAMCAETDAM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 264 VGQIKDKVDRTAKEN-TFLWFTGDNGpwaqkcELAgsvgpftglWQTRQGgspAKQTTWEGGHRVPALAYWPGrVPVNVT 342
Cdd:cd16171 209 LGEIISALKDTGLLDkTYVFFTSDHG------ELA---------MEHRQF---YKMSMYEGSSHVPLLIMGPG-IKAGQQ 269
|
330 340
....*....|....*....|....*
gi 1864488359 343 STALLSVLDIFPTVVALAQASLPQG 367
Cdd:cd16171 270 VSDVVSLVDIYPTMLDIAGVPQPQN 294
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-372 |
9.83e-15 |
|
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: 76.14 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 116 LNETTLAEVLQQAGYVTGMIGFdyyfgipyshdmgcTDTPgynhppcpacPQGDGPSRNLQRDCYTDVALPLY-ENLNIV 194
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGY--------------TDTS----------PDPRGLAPLDPRLLSYELAMPGFdPVDRLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 195 EQPVNLSSLAqkY-AEKATQFIQqaSTSGRPFLLYVGLAHMH-----------------VPLPVTQLPAA------PW-- 248
Cdd:cd16028 132 EYPAEDSDTA--FlTDRAIEYLD--ERQDEPWFLHLSYIRPHppfvapapyhalydpadVPPPIRAESLAaeaaqhPLla 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 249 -----------------GRRLYGAGLREMD----GLVGQIKDKVDRTAK--------ENTFLWFTGDNGpwaqkcELAGS 299
Cdd:cd16028 208 aflerieslsfspgaanAADLDDEEVAQMRatylGLIAEVDDHLGRLFDylketgqwDDTLIVFTSDHG------EQLGD 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864488359 300 vgpfTGLWqtrqggspAKQTTWEGGHRVPALAYWPGRvPVNVTS----TALLSVLDIFPTVvaLAQASLPQGRRFDG 372
Cdd:cd16028 282 ----HWLW--------GKDGFFDQAYRVPLIVRDPRR-EADATRgqvvDAFTESVDVMPTI--LDWLGGEIPHQCDG 343
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
14-288 |
3.03e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 43.20 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 14 SFSGFLYPLVDFCFSGKARGQKPnFVIILADdigwGdLGANWAETKDTTNLDKMASEGMRFVDFHAA--ASTCsPSRASL 91
Cdd:COG1524 3 RGLSLLLASLLAAAAAAAPPAKK-VVLILVD----G-LRADLLERAHAPNLAALAARGVYARPLTSVfpSTTA-PAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 92 LTGRLGLRNGVTHNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTGMIGFdyyfgipyshdmgctdtP 155
Cdd:COG1524 76 LTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFW-----------------P 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 156 GYNHPPcpacpqgdgpsrnlqrdcYTDVALPLYENLNIVEQPVNLSSLAQkyAEKATQFIQQastsGRPFLLYVGL---- 231
Cdd:COG1524 139 SFEGSG------------------LIDAARPYPYDGRKPLLGNPAADRWI--AAAALELLRE----GRPDLLLVYLpdld 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 232 --AHMHvplpvtqlpaaPWGRRLYGAGLREMDGLVGQIKDKVD-RTAKENTFLWFTGDNG 288
Cdd:COG1524 195 yaGHRY-----------GPDSPEYRAALREVDAALGRLLDALKaRGLYEGTLVIVTADHG 243
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-145 |
3.29e-04 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 43.10 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 28 SGKARGQKPNFVIIL-----ADDIGWGDLGANWaetkdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV 102
Cdd:COG1368 227 NPFGPAKKPNVVVILlesfsDFFIGALGNGKDV-----TPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS 301
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488359 103 thnfAVTSVGGLPLNetTLAEVLQQAGYVTGMI-----------------GFDYYFGIPY 145
Cdd:COG1368 302 ----PYKRPGQNNFP--SLPSILKKQGYETSFFhggdgsfwnrdsfyknlGFDEFYDRED 355
|
|
| |
