|
Name |
Accession |
Description |
Interval |
E-value |
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
22-371 |
0e+00 |
|
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: 664.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGG 101
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPI 181
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNLTCFPPNIPCFGGCDQGEVPC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 182 PLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVG 261
Cdd:cd16158 161 PLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 262 TLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPT 341
Cdd:cd16158 241 ELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPT 320
|
330 340 350
....*....|....*....|....*....|
gi 1370482277 342 LAALAGAPLPNVTLDGFDLSPLLLGTGKAL 371
Cdd:cd16158 321 IAKLAGAPLPNVTLDGVDMSPILFEQGKSP 350
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
22-372 |
1.96e-176 |
|
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: 496.70 E-value: 1.96e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGG 101
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPatpcdggcdqgLVPI 181
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPE--FLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP-----------GPLP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 182 PLLANLSVEAQPPWLPGLEARYMAFAHDLMADAqrQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVG 261
Cdd:cd16026 148 PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 262 TLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLP 340
Cdd:cd16026 226 RILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGtVSDELASTMDLLP 305
|
330 340 350
....*....|....*....|....*....|...
gi 1370482277 341 TLAALAGAPLPN-VTLDGFDLSPLLLGTGKALP 372
Cdd:cd16026 306 TLAALAGAPLPEdRVIDGKDISPLLLGGSKSPP 338
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
23-375 |
1.84e-113 |
|
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: 338.25 E-value: 1.84e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPG--VLVPSSRG 100
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGtrVFLPWDIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPE----GAFLPPHQGFHrFLG--IPYSHdqgpcqNLTCFPPATPCDGGc 174
Cdd:cd16160 82 GLPKTEVTMAEALKEAGYTTGMVGKWHLGINENnhsdGAHLPSHHGFD-FVGtnLPFTN------SWACDDTGRHVDFP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 175 DQGLVPipLLANLSVEAQPPWLPGLEARYMAFAHDLMADaqRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLM 254
Cdd:cd16160 154 DRSACF--LYYNDTIVEQPIQHEHLTETLVGDAKSFIED--NQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNIN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 255 ELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELAS 334
Cdd:cd16160 230 EMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVS 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1370482277 335 SLDLLPTLAALAGAPLPNVT-LDGFDLSPLLLGTGKALPTVI 375
Cdd:cd16160 310 TMDIFPTFVDLAGGTLPTDRiYDGLSITDLLLGEADSPHDDI 351
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
23-372 |
7.47e-109 |
|
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: 324.10 E-value: 7.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSST---TPNLDQLAAGGLRFTDFYVPVSlCTPSRAALLTGRLPVRMGMYPgVLVPSSR 99
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTT-VGLPGSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 100 GGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHdqgpcqnltcfppatpcdggcdqglv 179
Cdd:cd16142 79 GGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG--RLPTDHGFDEFYGNLYHT-------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 180 pipllanlsveaqppwlpgLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYP-----QFSGQSfaerSGRGPFGDSLM 254
Cdd:cd16142 131 -------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPtlpspEFEGKS----SGKGKYADSMV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 255 ELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGcSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELA 333
Cdd:cd16142 188 ELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVWPDGG-YTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGrVSNEIV 266
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1370482277 334 SSLDLLPTLAALAGAPLPN-------VTLDGFDLSPLLLGTGKALP 372
Cdd:cd16142 267 SHLDWFPTLAALAGAPDPKdkllgkdRHIDGVDQSPFLLGKSEKSR 312
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
22-366 |
3.22e-103 |
|
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: 310.17 E-value: 3.22e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYGDLGCYGHPSS-TTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMyPGVLVPSSRG 100
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAiLTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLGVgpEGAFLPPHQGFHRFLGIPYSHDQgpcqnltcfppatpcdggcdqglvp 180
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLGQ--REAYLPNSRGFDYYFGIPFSHDS------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 181 ipllanlsveaqppwlpGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSF-AERSGRGPFGDSLMELDAA 259
Cdd:cd16161 133 -----------------SLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFqSPTSGRGPYGDALQEMDDL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 260 VGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGL--------LRCGKGTTYEGGVREPALAFWPGHIAPGVTHE 331
Cdd:cd16161 196 VGQIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGPGTgdwqgnlgGSVAKASTWEGGHREPAIVYWPGRIPANSTSA 275
|
330 340 350
....*....|....*....|....*....|....*..
gi 1370482277 332 -LASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLG 366
Cdd:cd16161 276 aLVSTLDIFPTVVALAGASLPpGRIYDGKDLSPVLFG 312
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
21-375 |
7.45e-99 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 299.10 E-value: 7.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 21 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPgvLVPSSRG 100
Cdd:COG3119 22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD--NGEGYNG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipYSHDqgpcqnltcfppatpcdggcdqglvp 180
Cdd:COG3119 100 GLPPDEPTLAELLKEAGYRTALFGKWHL----------------------YLTD-------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 181 ipllanlsveaqppwlpgleaRYMAFAHDLMADAQRQDRPFFLYYASHHTHYP---------QFSGQSFAE--------- 242
Cdd:COG3119 132 ---------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldKYDGKDIPLppnlaprdl 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 243 -----RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPEtmrmsrGGCSGlLRCGKGTTYEGGVREPAL 317
Cdd:COG3119 191 teeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS------LGEHG-LRGGKGTLYEGGIRVPLI 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370482277 318 AFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKALPTVI 375
Cdd:COG3119 264 VRWPGKIKAGsVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPLLTGEKAEWRDYL 321
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
23-372 |
1.24e-98 |
|
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: 299.46 E-value: 1.24e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMY------------ 90
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITdvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 91 PGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLgvGPEGAFLPPHQGFHRflGIPYSHDQGPcqnltcfppatpc 170
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHL--GGEGGYGPEDQGFDV--NIGGTGNGGP------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 171 DGGCDQGLVPIPLLANLSveaQPPWLPglearymafahDLMADA------QRQDRPFFLYYASHHTHYPQFSGQSFAE-- 242
Cdd:cd16144 144 PSYYFPPGKPNPDLEDGP---EGEYLT-----------DRLTDEaidfieQNKDKPFFLYLSHYAVHTPIQARPELIEky 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 243 RSGRGPFGD--------SLME-LDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVR 313
Cdd:cd16144 210 EKKKKGLRKgqknpvyaAMIEsLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNAPLRGGKGSLYEGGIR 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370482277 314 EPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKALP 372
Cdd:cd16144 290 VPLIVRWPGVIKPGsVSDVPVIGTDLYPTFLELAGGPLPpPQHLDGVSLVPLLKGGEADLP 350
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
23-370 |
6.23e-97 |
|
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: 294.11 E-value: 6.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGhPSST--TPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRG 100
Cdd:cd16143 1 PNIVIILADDLGYGDISCYN-PDSKipTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLG-----VGPEGAFL---------------PPHQGFHRFLGIPYShdqgpcQN 160
Cdd:cd16143 80 LIEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkKDGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPAS------EV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 161 LtcfppatpcdggcdqglvpiPLLANLSVEaqppwlpglearymafahdLMADAQRQDRPFFLYYASHHTHYPQFSGQSF 240
Cdd:cd16143 154 L--------------------PTLTDKAVE-------------------FIDQHAKKDKPFFLYFALPAPHTPIVPSPEF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 241 AERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMR----MSRGG--CSGLLRCGKGTTYEGGVRE 314
Cdd:cd16143 195 QGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYAdykeLEKFGhdPSGPLRGMKADIYEGGHRV 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370482277 315 PALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKA 370
Cdd:cd16143 275 PFIVRWPGKIPAGsVSDQLVSLTDLFATLAAIVGQKLPdNAAEDSFSFLPALLGPKKQ 332
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
22-365 |
2.91e-91 |
|
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: 282.05 E-value: 2.91e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMY----------- 90
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYttnaharnayt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 91 PGVLVpssrGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHdqgpcqnltcFPPATpc 170
Cdd:cd16157 81 PQNIV----GGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ--YHPLKHGFDEWFGAPNCH----------FGPYD-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 171 dggcDQGLVPIPLLANLSVEAQ---------PPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFA 241
Cdd:cd16157 143 ----NKAYPNIPVYRDWEMIGRyyeefkidkKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 242 ERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETM-RMSRGGCSGLLRCGKGTTYEGGVREPALAFW 320
Cdd:cd16157 219 GTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALIsAPEQGGSNGPFLCGKQTTFEGGMREPAIAWW 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1370482277 321 PGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLL 365
Cdd:cd16157 299 PGHIKPGqVSHQLGSLMDLFTTSLALAGLPIPsDRAIDGIDLLPVLL 345
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
22-372 |
3.13e-90 |
|
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: 281.10 E-value: 3.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGM-----YPGVLVP 96
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMasshgMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 97 SSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPE----GAFLPPHQGFHRFLGIPYSH------DQGPCQNLTCFPP 166
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCEsrndFCHHPLNHGFDYFYGLPLTNlkdcgdGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 167 ATPCDGGCD--------------------------QGLVPIP--------------LLANLSVEAQPPWLPGLEARYMAF 206
Cdd:cd16159 161 FPLLTAFVLitaltiflllylgavskrffvfllilSLLFISLfflllitnryfnciLMRNHEVVEQPMSLENLTQRLTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 207 AHDLMADaqRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGP 286
Cdd:cd16159 241 AISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 287 ETMRMSR-----GGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPN-VTLDGFD 359
Cdd:cd16159 319 HLEEISVggeygGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGsVIDEPTSLMDIFPTVAALAGAPLPSdRIIDGRD 398
|
410
....*....|...
gi 1370482277 360 LSPLLLGTGKALP 372
Cdd:cd16159 399 LMPLLTGQEKRSP 411
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
23-368 |
3.81e-84 |
|
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: 262.15 E-value: 3.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTG----RLPVRMGmypgvlvPSS 98
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGlhtgHTRVRGN-------SEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 99 RGGLPL--EEVTVAEVLAARGYLTGMAGKWHLG-VGPEGAflPPHQGFHRFLGIpysHDQGPCQNLtcFPPATPCDGgcd 175
Cdd:cd16145 74 GGQDPLppDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGH--PTKQGFDYFYGY---LDQVHAHNY--YPEYLWRNG--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 176 qGLVPIPlLANLSVEAQPPWLPGLEARYmafAHDLMADA------QRQDRPFFLYYAS---H-HTHYPQFSG--QSFAER 243
Cdd:cd16145 144 -EKVPLP-NNVIPPLDEGNNAGGGGGTY---SHDLFTDEaldfirENKDKPFFLYLAYtlpHaPLQVPDDGPykYKPKDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 244 SGRGPFGDSLME---------LDAAVGTLMTAIGDLGLLEETLVIFTADNGPEtmrmSRGGC---------SGLLRCGKG 305
Cdd:cd16145 219 GIYAYLPWPQPEkayaamvtrLDRDVGRILALLKELGIDENTLVVFTSDNGPH----SEGGSehdpdffdsNGPLRGYKR 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370482277 306 TTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTG 368
Cdd:cd16145 295 SLYEGGIRVPFIARWPGKIPAGsVSDHPSAFWDFMPTLADLAGAEPPE-DIDGISLLPTLLGKP 357
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
23-373 |
2.82e-83 |
|
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: 259.79 E-value: 2.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYV-PVslCTPSRAALLTGRLPVRMGmypgvlVPSSRGG 101
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVsPV--CAPTRAALLTGRYPFRTG------VWHTILG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 ---LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPegAFLPPHQGFHRFLGIpyshdqgpcqnltcfppatpCDGGCDQgl 178
Cdd:cd16146 73 rerMRLDETTLAEVFKDAGYRTGIFGKWHLGDNY--PYRPQDRGFDEVLGH--------------------GGGGIGQ-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 179 vpIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADA------QRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDS 252
Cdd:cd16146 129 --YPDYWGNDYFDDTYYHNGKFVKTEGYCTDVFFDEaidfieENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 253 L-----M--ELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSR--GGcsglLRCGKGTTYEGGVREPALAFWPGH 323
Cdd:cd16146 207 LaafygMieNIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRfnAG----MRGKKGSVYEGGHRVPFFIRWPGK 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1370482277 324 IAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKALPT 373
Cdd:cd16146 283 ILAGkDVDTLTAHIDLLPTLLDLCGVKLPeGIKLDGRSLLPLLKGESDPWPE 334
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
23-359 |
1.35e-78 |
|
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: 241.57 E-value: 1.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvLVPSSRGGL 102
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVR---GNVGNGGGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 PLEEVTVAEVLAARGYLTGMAGKWHlgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvpip 182
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 183 llaNLSVEaqppWLpglearymafahdlmaDAQRQDRPFFLYYASHHTHYPqfsgqsFAersgrgpFGDSLMELDAAVGT 262
Cdd:cd16022 103 ---DEAID----FI----------------ERRDKDKPFFLYVSFNAPHPP------FA-------YYAMVSAIDDQIGR 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 263 LMTAIGDLGLLEETLVIFTADNGPetMRMSRGgcsglLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPT 341
Cdd:cd16022 147 ILDALEELGLLDNTLIVFTSDHGD--MLGDHG-----LRGKKGSLYEGGIRVPFIVRWPGKIPAGqVSDALVSLLDLLPT 219
|
330
....*....|....*...
gi 1370482277 342 LAALAGAPLPNvTLDGFD 359
Cdd:cd16022 220 LLDLAGIEPPE-GLDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
23-366 |
1.40e-73 |
|
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: 234.37 E-value: 1.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPvSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGL 102
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 PLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgAFLPPHQGFHRFLGiPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPip 182
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTW-EYTPTNRGFDSFYG-YYGGAEDYYTHTSGGANDYGNDDLRDNEEPA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 183 llanlsveaqppwlPGLEARYMAfahDLMAD-AQR------QDRPFFLYYASHHTHYP-QFSGQSFAERSGRGPFGDS-- 252
Cdd:cd16029 156 --------------WDYNGTYST---DLFTDrAVDiienhdPSKPLFLYLAFQAVHAPlQVPPEYADPYEDKFAHIKDed 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 253 -------LMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSrGGCSGLLRCGKGTTYEGGVREPALaFWPGHI- 324
Cdd:cd16029 219 rrtyaamVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRGGKNTLWEGGVRVPAF-VWSPLLp 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1370482277 325 --APGVTHELASSLDLLPTLAALAGA-PLPNVTLDGFDLSPLLLG 366
Cdd:cd16029 297 pkRGTVSDGLMHVTDWLPTLLSLAGGdPDDLPPLDGVDQWDALSG 341
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
23-348 |
1.37e-71 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 226.15 E-value: 1.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvPSSRGGL 102
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY-----VSTPVGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 PLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAflPPHQGFHRFLGIPYSHDQgpcQNLTCFPPATPCDGGCdqglvpip 182
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS--PCNLGFDKFFGRNTGSDL---YADPPDVPYNCSGGGV-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 183 llanlsveaqppwlpgLEARYMAFAHDLmadAQRQDRPFFLYYASHHTHYP------------QFSGQSFAERSGRGPFG 250
Cdd:pfam00884 143 ----------------SDEALLDEALEF---LDNNDKPFFLVLHTLGSHGPpyypdrypekyaTFKPSSCSEEQLLNSYD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 251 DSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetmrmSRGGCSGLLRCGKG-TTYEGGVREPALAFWPGHIAPG-V 328
Cdd:pfam00884 204 NTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGE-----SLGEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGqK 278
|
330 340
....*....|....*....|
gi 1370482277 329 THELASSLDLLPTLAALAGA 348
Cdd:pfam00884 279 SEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-366 |
7.79e-71 |
|
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: 226.71 E-value: 7.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPvSLCTPSRAALLTGRLPVRMGMYPGVLVPSsrggl 102
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNYVVFGYLDPK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 pleEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPcqnltCFPPATpcdggcdqglvPIP 182
Cdd:cd16151 75 ---QKTFGHLLKDAGYATAIAGKWQLGGGRGDGDYPHEFGFDEYCLWQLTETGEK-----YSRPAT-----------PTF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 183 LLANLSVeaqppwlpgLEARYMAFAHDLMAD------AQRQDRPFFLYYASHHTHYP----------QFSGQSFAERSGR 246
Cdd:cd16151 136 NIRNGKL---------LETTEGDYGPDLFADflidfiERNKDQPFFAYYPMVLVHDPfvptpdspdwDPDDKRKKDDPEY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 247 gpFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNG--PETMRMSRGgcsGLLRCGKGTTYEGGVREPALAFWPGHI 324
Cdd:cd16151 207 --FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNG---REVRGGKGKTTDAGTHVPLIVNWPGLI 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1370482277 325 APG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLG 366
Cdd:cd16151 282 PAGgVSDDLVDFSDFLPTLAELAGAPLPeDYPLDGRSFAPQLLG 325
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
23-370 |
2.45e-69 |
|
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: 222.77 E-value: 2.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYgDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPgvlVPSSRGGL 102
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHG---LRSRGFPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 PLEEVTVAEVLAARGYLTGMAGKWHlgVGPEGAFLPPHQGFHRFLGIPYSHDQgpcqnltcfppatpcdggcdqglvpip 182
Cdd:cd16027 77 PDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWDY--------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 183 llanlsVEAQPPWLpglearymafahdlmaDAQRQDRPFFLYYASHHTHYPQFSGQSFAE-------------------R 243
Cdd:cd16027 128 ------ASNAADFL----------------NRAKKGQPFFLWFGFHDPHRPYPPGDGEEPgydpekvkvppylpdtpevR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 244 SGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpetMRMSRggcsgllrcGKGTTYEGGVREPALAFWPGH 323
Cdd:cd16027 186 EDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG---MPFPR---------AKGTLYDSGLRVPLIVRWPGK 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1370482277 324 IAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKA 370
Cdd:cd16027 254 IKPGsVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLLKGEKDP 300
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
22-373 |
2.54e-65 |
|
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: 213.07 E-value: 2.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYGDLGCYGHPSStTPNLDQLAAGGLRFTDFYVpVSLCTPSRAALLTGRLP--VRMGMYPGVL--VPS 97
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEIP-TPNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHhqVGMGTMAELAtgKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 98 SRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGvgpegaflppHQGFHrflgipYSHDqgpcqnLTcfppatpcdggcDQG 177
Cdd:cd16025 80 YEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG----------PDDYY------STDD------LT------------DKA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 178 LvpipllanlsveaqppwlpglearymafahDLMADAQRQDRPFFLYYASHHTHYP---------QFSGQ---------- 238
Cdd:cd16025 126 I------------------------------EYIDEQKAPDKPFFLYLAFGAPHAPlqapkewidKYKGKydagwdalre 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 239 ----------------SFAERSGRGPFGDSL-----------ME--------LDAAVGTLMTAIGDLGLLEETLVIFTAD 283
Cdd:cd16025 176 erlerqkelglipadtKLTPRPPGVPAWDSLspeekklearrMEvyaamvehMDQQIGRLIDYLKELGELDNTLIIFLSD 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 284 NGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAP--GVTHELASSLDLLPTLAALAGAPLPNV-------T 354
Cdd:cd16025 256 NGASAEPGWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkgGIRHQFAHVIDIAPTILELAGVEYPKTvngvpqlP 335
|
410
....*....|....*....
gi 1370482277 355 LDGFDLSPLLlgTGKALPT 373
Cdd:cd16025 336 LDGVSLLPTL--DGAAAPS 352
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
21-370 |
7.03e-57 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 191.97 E-value: 7.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 21 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTgrlpvrmGMYP---GVlVPS 97
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILT-------GQYShrhGV-TDN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 98 SRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaflPPHQGFHRFLGIPYSHDQGPCQNLTcfppatpcdggcDQG 177
Cdd:cd16031 73 NGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGD----LPPPGFDYWVSFPGQGSYYDPEFIE------------NGK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 178 LVPIP-----LLANLSVEaqppWLpglearymafahdlmaDAQRQDRPFFLYY---ASH--------HTH--------YP 233
Cdd:cd16031 137 RVGQKgyvtdIITDKALD----FL----------------KERDKDKPFCLSLsfkAPHrpftpaprHRGlyedvtipEP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 234 Q------FSGQS-FAERSGRGPFGD--------------------SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGp 286
Cdd:cd16031 197 EtfddddYAGRPeWAREQRNRIRGVldgrfdtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 287 etmrmsrggcsglLRCG------KGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFD 359
Cdd:cd16031 276 -------------FFLGehglfdKRLMYEESIRVPLIIRDPRLIKAGtVVDALVLNIDFAPTILDLAGVPIPE-DMQGRS 341
|
410
....*....|.
gi 1370482277 360 LSPLLLGTGKA 370
Cdd:cd16031 342 LLPLLEGEKPV 352
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-372 |
2.30e-54 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 184.31 E-value: 2.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVpssrggL 102
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 PLEEVTVAEVLAARGYLTGMAGKWHLGVGPEG-----AFLPPH---QGF---------HRFLGIPYSHDQGPcqnltcfp 165
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLDGPERNdgradDYTPPPerrHGFdywkgyecnHDHNNPHYYDDDGK-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 166 paTPCDGGcdqglvpipllanlsveaqppWLPGLEARyMAFahDLMADAQRQDRPFFLY--YASHHTHY---PQ-----F 235
Cdd:cd16034 148 --RIYIKG---------------------YSPDAETD-LAI--EYLENQADKDKPFALVlsWNPPHDPYttaPEeyldmY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 236 SGQSFAERsGRGPFGDSLME---------------LDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLL 300
Cdd:cd16034 202 DPKKLLLR-PNVPEDKKEEAglredlrgyyamitaLDDNIGRLLDALKELGLLENTIVVFTSDHG-DML-----GSHGLM 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370482277 301 RcgKGTTYEGGVREPALAFWPGHI-APGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKALP 372
Cdd:cd16034 275 N--KQVPYEESIRVPFIIRYPGKIkAGRVVDLLINTVDIMPTLLGLCGLPIPD-TVEGRDLSPLLLGGKDDEP 344
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-362 |
4.06e-48 |
|
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: 163.95 E-value: 4.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMY---PGVLVPSSR 99
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHdwiVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 100 GGLPL--EEVTVAEVLAARGYLTGMAGKWHLGvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcDQG 177
Cdd:cd16149 81 KPEGYleGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------------DDA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 178 LvpipllanlsveaqppwlpglearymafahDLMADAQRQDRPFFL---YYASHHTHypqfsgQSFAERSGrgpfgdslm 254
Cdd:cd16149 116 A------------------------------DFLRRRAEAEKPFFLsvnYTAPHSPW------GYFAAVTG--------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 255 eLDAAVGTLMTAIGDLGLLEETLVIFTADNGpetMRMsrgGCSGLLRCGKGTT----YEGGVREPALAFWPGHIAPG-VT 329
Cdd:cd16149 151 -VDRNVGRLLDELEELGLTENTLVIFTSDNG---FNM---GHHGIWGKGNGTFplnmYDNSVKVPFIIRWPGVVPAGrVV 223
|
330 340 350
....*....|....*....|....*....|....
gi 1370482277 330 HELASSLDLLPTLAALAGAPLP-NVTLDGFDLSP 362
Cdd:cd16149 224 DSLVSAYDFFPTLLELAGVDPPaDPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-366 |
1.86e-47 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 166.63 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSS-RGG 101
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAySRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 LPLEEVTVAEVLAARGYLTGMAGKWHLGvgpegaflpphqgfhrflgipyshdqgpcqnltcfPPATPCDGGCDqGLVPi 181
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVG-----------------------------------PEETPLDYGFD-EYLP- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 182 pllanlsVEAQPpwlpglEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQ---------------SFAE---- 242
Cdd:cd16033 124 -------VETTI------EYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEpyldmydpediplpeSFADdfed 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 243 -----RSGRGPFGDSLME-----------------LDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLL 300
Cdd:cd16033 191 kpyiyRRERKRWGVDTEDeedwkeiiahywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHG-DAL-----GAHRLW 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370482277 301 RcgKGT-TYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNVTlDGFDLSPLLLG 366
Cdd:cd16033 265 D--KGPfMYEETYRIPLIIKWPGVIAAGqVVDEFVSLLDLAPTILDLAGVDVPPKV-DGRSLLPLLRG 329
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-366 |
7.30e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 146.53 E-value: 7.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvpSSRGGL 102
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVW------DNADPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 PLEEVTVAEVLAARGYLTGMAGKWHLgVGPEgaflPPHqGFHrflgipysHDqgpcQNLTcfppatpcDGGCDqglvpip 182
Cdd:cd16037 75 DGDVPSWGHALRAAGYETVLIGKLHF-RGED----QRH-GFR--------YD----RDVT--------EAAVD------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 183 llanlsveaqppWLpglearymafahdlmADAQRQDRPFFLYYASHHTHYPQFSGQSF----AERSGRGPFGdsLME-LD 257
Cdd:cd16037 122 ------------WL---------------REEAADDKPWFLFVGFVAPHFPLIAPQEFydlyVRRARAAYYG--LVEfLD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 258 AAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLrcGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLD 337
Cdd:cd16037 173 ENIGRVLDALEELGLLDNTLIIYTSDHG-DML-----GERGLW--GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVD 244
|
330 340
....*....|....*....|....*....
gi 1370482277 338 LLPTLAALAGAPLPNvTLDGFDLSPLLLG 366
Cdd:cd16037 245 LAPTILEAAGAPPPP-DLDGRSLLPLAEG 272
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-362 |
2.75e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 143.84 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPssrggl 102
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLEP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 plEEVTVAEVLAARGYLTGMAGkWHLGVGPEGAFlppHQGFHRFLGIPYSHDQGPcqnltcFPPATPCDGGCDQGLvpip 182
Cdd:cd16148 75 --DDPTLAEILRKAGYYTAAVS-SNPHLFGGPGF---DRGFDTFEDFRGQEGDPG------EEGDERAERVTDRAL---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 183 llanlsveaqpPWLpglearymafahdlmaDAQRQDRPFFL---YYASHHthypqfsgqsfaersgrgPFG--DSLMELD 257
Cdd:cd16148 139 -----------EWL----------------DRNADDDPFFLflhYFDPHE------------------PYLydAEVRYVD 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 258 AAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLD 337
Cdd:cd16148 174 EQIGRLLDKLKELGLLEDTLVIVTSDHG-EEF-----GEHGLYWGHGSNLYDEQLHVPLIIRWPGKEPGKRVDALVSHID 247
|
330 340
....*....|....*....|....*
gi 1370482277 338 LLPTLAALAGAPlPNVTLDGFDLSP 362
Cdd:cd16148 248 IAPTLLDLLGVE-PPDYSDGRSLLP 271
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
23-375 |
6.19e-40 |
|
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: 144.26 E-value: 6.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVlvpssrGGL 102
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA------AEF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 PLEEVTVAEVLAARGYLTGMAGKWHLgVGPEgaflpPHQGFhrflgipySHDQgpcqnltcfppatpcdggcdqglvpip 182
Cdd:cd16032 75 PADIPTFAHYLRAAGYRTALSGKMHF-VGPD-----QLHGF--------DYDE--------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 183 llanlsveaqppwlpglEARYMA--FAHDLmadAQRQD-RPFFLYYASHHTHYPQFSGQSF----AERSGRGPFGdSLME 255
Cdd:cd16032 114 -----------------EVAFKAvqKLYDL---ARGEDgRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 256 LDAAVGTLMTAIGDLGLLEETLVIFTADNGpeTMRMSRGgcsgllRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASS 335
Cdd:cd16032 173 VDDKVGQLLDTLERTGLADDTIVIFTSDHG--DMLGERG------LWYKMSFFEGSARVPLIISAPGRFAPRRVAEPVSL 244
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1370482277 336 LDLLPTLAALAGAPLPNV--TLDGFDLSPLLLGTGKALPTVI 375
Cdd:cd16032 245 VDLLPTLVDLAGGGTAPHvpPLDGRSLLPLLEGGDSGGEDEV 286
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-370 |
7.95e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 140.01 E-value: 7.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVS----LCTPSRAALLTGR----LPVRMGMypgvl 94
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTGRtlfhAPEGGKA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 95 vpssrgGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPE------------------GAFLPPH------QGFhrflgip 150
Cdd:cd16155 78 ------AIPSDDKTWPETFKKAGYRTFATGKWHNGFADAaiefleeykdgdkpffmyVAFTAPHdprqapPEY------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 151 ysHDQGPCQNLTC---FPPATPCDGGcdQGLVPIPLLAnlsveaqpPWlPGLEArymafahdlMADAQRQDrpfflYYA- 226
Cdd:cd16155 145 --LDMYPPETIPLpenFLPQHPFDNG--EGTVRDEQLA--------PF-PRTPE---------AVRQHLAE-----YYAm 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 227 -SHhthypqfsgqsfaersgrgpfgdslmeLDAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrMSRGGcSGLLrcGKG 305
Cdd:cd16155 198 iTH---------------------------LDAQIGRILDALEASGELDNTIIVFTSDHG-----LAVGS-HGLM--GKQ 242
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370482277 306 TTYEGGVREPALAFWPGhIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKA 370
Cdd:cd16155 243 NLYEHSMRVPLIISGPG-IPKGkRRDALVYLQDVFPTLCELAGIEIPE-SVEGKSLLPVIRGEKKA 306
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-378 |
1.34e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 136.59 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvpSSRGG 101
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF------RNGIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 LPLEEVTVAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvpi 181
Cdd:cd16152 75 LPADEKTLAHYFRDAGYETGYVGKWHL----------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 182 pllanlsveaqppwlpgleARYMA-----FAHDLMADAQrQDRPFFL---YYASHHT----HY--PQFSGQSFAERS--- 244
Cdd:cd16152 102 -------------------AGYRVdaltdFAIDYLDNRQ-KDKPFFLflsYLEPHHQndrdRYvaPEGSAERFANFWvpp 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 245 ---GRGpfGDSLME----------LDAAVGTLMTAIGDLGLLEETLVIFTADNgpetmrmsrgGCSGLLRCG--KGTTYE 309
Cdd:cd16152 162 dlaALP--GDWAEElpdylgccerLDENVGRIRDALKELGLYDNTIIVFTSDH----------GCHFRTRNAeyKRSCHE 229
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370482277 310 GGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKALPTVIPLQ 378
Cdd:cd16152 230 SSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPE-EMQGRSLLPLVDGKVEDWRNEVFIQ 297
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
23-346 |
8.95e-34 |
|
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: 125.61 E-value: 8.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDF-YVPVSLCTPSRAALLTGRLPVRMGMY----PGVLVPS 97
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRsVSPPTSSAPNHAALLTGAYPTLHGYTgngsADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 98 SRGGLPLEEVTVAEVLAARGYLTGMAGkwhlgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqg 177
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 178 lvpipllanlsveaqppwlpglearymafAHDlMADAQRQDRPFFLYYashhtHYPQFSGQSFAERSGRGPFGDSLMELD 257
Cdd:cd00016 108 -----------------------------LLK-AIDETSKEKPFVLFL-----HFDGPDGPGHAYGPNTPEYYDAVEEID 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 258 AAVGTLMTAIGDLGLLEETLVIFTADNGpetmrMSRGGCSGLLR-CGKGTTYEGGVREPALAFWPGHIAPGVTHELASSL 336
Cdd:cd00016 153 ERIGKVLDALKKAGDADDTVIIVTADHG-----GIDKGHGGDPKaDGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQY 227
|
330
....*....|
gi 1370482277 337 DLLPTLAALA 346
Cdd:cd00016 228 DIAPTLADLL 237
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
22-357 |
2.14e-33 |
|
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: 128.44 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYGDLGcyghPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpGVLVPSsrGG 101
Cdd:cd16147 1 RPNIVLILTDDQDVELGS----MDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVT-NNSPPG--GG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 LP------LEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGI--PYSHDqgpcqNLTcfppatpcdgg 173
Cdd:cd16147 74 YPkfwqngLERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPPGWDEWDGLvgNSTYY-----NYT----------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 174 cdqglvpiplLANLSVEAQPPWLPGlearymAFAHDLMAD--------AQRQDRPFFLYYASH--HTHY---PQFSGQSF 240
Cdd:cd16147 138 ----------LSNGGNGKHGVSYPG------DYLTDVIANkaldflrrAAADDKPFFLVVAPPapHGPFtpaPRYANLFP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 241 -AERSGRGPFGD---------------------------------SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGP 286
Cdd:cd16147 202 nVTAPPRPPPNNpdvsdkphwlrrlpplnptqiayidelyrkrlrTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGY 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370482277 287 ETmrmsrgGCSGLLRcGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDG 357
Cdd:cd16147 282 HL------GQHRLPP-GKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPS-DMDG 344
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
23-367 |
1.98e-32 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 127.09 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLgYGD-LGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMypgvlVPSSRGG 101
Cdd:PRK13759 7 PNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR-----VGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 LPLEEVTVAEVLAARGYLTGMAGKWHlgVGPEGAFLpphqGFHRFL---GIPYS-HDQGPCQN------LTCFPPATPcd 171
Cdd:PRK13759 81 PWNYKNTLPQEFRDAGYYTQCIGKMH--VFPQRNLL----GFHNVLlhdGYLHSgRNEDKSQFdfvsdyLAWLREKAP-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 172 gGCDQGLVPIPLLANlSVEAQpPWlpGLEARY------MAFAHDLMadaQRQDR--PFFLY--YASHHTHY--PQF---- 235
Cdd:PRK13759 153 -GKDPDLTDIGWDCN-SWVAR-PW--DLEERLhptnwvGSESIEFL---RRRDPtkPFFLKmsFARPHSPYdpPKRyfdm 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 236 -----------SGQSFAERSG---------RGPFGDSLME------------LDAAVGTLMTAIGDLGLLEETLVIFTAD 283
Cdd:PRK13759 225 ykdadipdphiGDWEYAEDQDpeggsidalRGNLGEEYARraraayyglithIDHQIGRFLQALKEFGLLDNTIILFVSD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 284 NGpETMrmsrgGCSGLLRcgKGTTYEGGVREPALAFWPGHIAPG----VTHELASSLDLLPTLAALAGAPLPNvTLDGFD 359
Cdd:PRK13759 305 HG-DML-----GDHYLFR--KGYPYEGSAHIPFIIYDPGGLLAGnrgtVIDQVVELRDIMPTLLDLAGGTIPD-DVDGRS 375
|
....*...
gi 1370482277 360 LSPLLLGT 367
Cdd:PRK13759 376 LKNLIFGQ 383
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
22-364 |
3.16e-31 |
|
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: 123.07 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 22 PPNIVLIFADDLGYgDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPgvLVPSSRGG 101
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYD--NNSYFRKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 LPlEEVTVAEVLAARGYLTGMAGKWHlgvgpegaflppHQGFHRFLGIPYSHDQGPCQNLTCFPPATPcdgGCDQGLVPI 181
Cdd:cd16030 79 AP-DAVTLPQYFKENGYTTAGVGKIF------------HPGIPDGDDDPASWDEPPNPPGPEKYPPGK---LCPGKKGGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 182 PLLANLSVEAqppwLPGLEARYM-----AFAHDLMADAQRQDRPFFL--------------------Y------------ 224
Cdd:cd16030 143 GGGGGPAWEA----ADVPDEAYPdgkvaDEAIEQLRKLKDSDKPFFLavgfykphlpfvapkkyfdlYplesiplpnpfd 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 225 ------YASHHTHYPQFSGQSFAERSGR--GPFGDSL-MEL-----------DAAVGTLMTAIGDLGLLEETLVIFTADN 284
Cdd:cd16030 219 pidlpeVAWNDLDDLPKYGDIPALNPGDpkGPLPDEQaRELrqayyasvsyvDAQVGRVLDALEELGLADNTIVVLWSDH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 285 GpetmrMSRG--GcsgllRCGKGTTYEGGVREPaLAFW-PGHIAPG-VTHELASSLDLLPTLAALAGAPLPNVtLDGFDL 360
Cdd:cd16030 299 G-----WHLGehG-----HWGKHTLFEEATRVP-LIIRaPGVTKPGkVTDALVELVDIYPTLAELAGLPAPPC-LEGKSL 366
|
....
gi 1370482277 361 SPLL 364
Cdd:cd16030 367 VPLL 370
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-366 |
1.78e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 115.77 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMY--PGvlvPSSRG 100
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTdtLG---SPMQP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAflpphqgfhrflgipYSHDQGPCQNLTCFppatpcdggcdqglvp 180
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWHLSGAAGGG---------------YKRDPGIAAQAVEW---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 181 iplLANL--SVEAQPPWL-------PglearymafaHDLMADAQRQDRpfflyYASHHTHYpqfsgqsfaersgrgpfGD 251
Cdd:cd16035 127 ---LRERgaKNADGKPWFlvvslvnP----------HDIMFPPDDEER-----WRRFRNFY-----------------YN 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 252 SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrmSRGGCSGLLRCGkGTTYEGGVREPAL----AFWPGhiaPG 327
Cdd:cd16035 172 LIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG------EMGGAHGLRGKG-FNAYEEALHVPLIishpDLFGT---GQ 241
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1370482277 328 VTHELASSLDLLPTLAALAGAPLPNV-----TLDGFDLSPLLLG 366
Cdd:cd16035 242 TTDALTSHIDLLPTLLGLAGVDAEARateapPLPGRDLSPLLTD 285
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-368 |
9.81e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 115.14 E-value: 9.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSS--TTPNLDQLAAGGLRFTDFYV-PVslCTPSRAALLTGRLPVRMgmypGVLVPSSR 99
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFDNLWAtPA--CSPTRATILTGKYGFRT----GVLAVPDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 100 GGLPLEEVTVAEVLAAR--GYLTGMAGKWHLGVGPEGafLPPHQGFHRFLGIPYSHDQGPCQ-NLTCFPPATPCDGGCDQ 176
Cdd:cd16154 75 LLLSEETLLQLLIKDATtaGYSSAVIGKWHLGGNDNS--PNNPGGIPYYAGILGGGVQDYYNwNLTNNGQTTNSTEYATT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 177 GLVpipllaNLSVEaqppWLpglearymafahdlmadaQRQDRPFFLYYA-----------SHHTHYPQFSGQSFAERSG 245
Cdd:cd16154 153 KLT------NLAID----WI------------------DQQTKPWFLWLAynaphtpfhlpPAELHSRSLLGDSADIEAN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 246 RGPFGDSLME-LDAAVGTLMTAIgDLGLLEETLVIFTADNG-PETMR---MSRGGcsgllrcGKGTTYEGGVREPALAFW 320
Cdd:cd16154 205 PRPYYLAAIEaMDTEIGRLLASI-DEEERENTIIIFIGDNGtPGQVVdlpYTRNH-------AKGSLYEGGINVPLIVSG 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1370482277 321 PGhIAPGVTHE--LASSLDLLPTLAALAGAPLPNVTlDGFDLSPLLLGTG 368
Cdd:cd16154 277 AG-VERANEREsaLVNATDLYATIAELAGVDAAEIH-DSVSFKPLLSDVN 324
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-360 |
2.27e-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: 112.08 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSST----------TPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYP- 91
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAHTGksesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 92 GVLVPSSRGGLPleevTVAEVLAARGYLTGMAGKWHlgvgpegaflppHQGFHRFLGIPYSHDQGPcqnltcfppatpcD 171
Cdd:cd16153 82 EAAHPALDHGLP----TFPEVLKKAGYQTASFGKSH------------LEAFQRYLKNANQSYKSF-------------W 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 172 GGCDQGLVPI-PLLANLSVEA-QPPWLPGLEARymafahdlmadaqrqDRpfFLYYAshhthypqFSGqsfaersgrgpF 249
Cdd:cd16153 133 GKIAKGADSDkPFFVRLSFLQpHTPVLPPKEFR---------------DR--FDYYA--------FCA-----------Y 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 250 GDSLmeldaaVGTLMTAIGDLGLL---EETLVIFTADNGpetmrmSRGGCSGLLrcGKGTTYEGGVREPALAFWPGHI-- 324
Cdd:cd16153 177 GDAQ------VGRAVEAFKAYSLKqdrDYTIVYVTGDHG------WHLGEQGIL--AKFTFWPQSHRVPLIVVSSDKLka 242
|
330 340 350
....*....|....*....|....*....|....*...
gi 1370482277 325 -APGVTHELASSLDLLPTLAALAGAPLPNVT-LDGFDL 360
Cdd:cd16153 243 pAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDyLDGRDL 280
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
23-367 |
4.96e-26 |
|
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: 108.50 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvpssRGGL 102
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV--------WNGT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 PL--EEVTVAEVLAARGYLTGMAGKWHLGVGPEG---------AFLPPHQGFH---RFLGIPYSHdqGPCQNLTcfppat 168
Cdd:cd16028 73 PLdaRHLTLALELRKAGYDPALFGYTDTSPDPRGlapldprllSYELAMPGFDpvdRLDEYPAED--SDTAFLT------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 169 pcDGGCD--QGLVPIPLLANLS-VEAQPPWLpgLEARYMAF-----------AHDLMADAqrQDRPFflyYASHHTHYPQ 234
Cdd:cd16028 145 --DRAIEylDERQDEPWFLHLSyIRPHPPFV--APAPYHALydpadvpppirAESLAAEA--AQHPL---LAAFLERIES 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 235 --FSGQSFAERSGRGPFGDSLM--------ELDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLrcGK 304
Cdd:cd16028 216 lsFSPGAANAADLDDEEVAQMRatylgliaEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG-EQL-----GDHWLW--GK 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482277 305 GTTYEGGVREPALAFWPG----HIAPGVTHELASSLDLLPTLAALAGAPLPNVtLDGFDLSPLLLGT 367
Cdd:cd16028 288 DGFFDQAYRVPLIVRDPRreadATRGQVVDAFTESVDVMPTILDWLGGEIPHQ-CDGRSLLPLLAGA 353
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
23-364 |
1.98e-21 |
|
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: 95.53 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSrggl 102
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 103 plEEVTVAEVLAARGYLTGMAGKWHL--------GVGPEGaflpphqgfhrflgipyshdqgpcqnltcFPPATPCDGGC 174
Cdd:cd16156 77 --NVKTIGQRLSDNGIHTAYIGKWHLdggdyfgnGICPQG-----------------------------WDPDYWYDMRN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 175 dqglvpipLLANLSVEAQPPW---LPGLEARYMA----FAHDLMADA-----QRQDRPFFLYYASHHTHYPQFSGQSFAE 242
Cdd:cd16156 126 --------YLDELTEEERRKSrrgLTSLEAEGIKeeftYGHRCTNRAldfieKHKDEDFFLVVSYDEPHHPFLCPKPYAS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 243 ----------------------------RSGRGPFGDSL---MEL--------DAAVGTLMTAIGDlgLLEETLVIFTAD 283
Cdd:cd16156 198 mykdfefpkgenayddlenkplhqrlwaGAKPHEDGDKGtikHPLyfgcnsfvDYEIGRVLDAADE--IAEDAWVIYTSD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 284 NGpETMrmsrgGCSGLLrcGKG-TTYEGGVREPALAFWPGHI-APGVTHELASSLDLLPTLAALAGAPLPNVtLDGFDLS 361
Cdd:cd16156 276 HG-DML-----GAHKLW--AKGpAVYDEITNIPLIIRGKGGEkAGTVTDTPVSHIDLAPTILDYAGIPQPKV-LEGESIL 346
|
...
gi 1370482277 362 PLL 364
Cdd:cd16156 347 ATI 349
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-371 |
4.03e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 94.22 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRlpvrmgmYPGVlvpssRGG- 101
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGW-------YPHV-----NGHr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 102 -----LPLEEVTVAEVLAARGYLTGMAGKWHLGVGP--------------EGA--FL---PPHQGFHRFLGIPYSHdqgp 157
Cdd:cd16150 69 tlhhlLRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEfaaeaycdsdeacvRTAidWLrnrRPDKPFCLYLPLIFPH---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 158 cqnltcfPPAT---PCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMafahdlmadaQRQDRPFFlyYASHHTHYPQ 234
Cdd:cd16150 145 -------PPYGveePWFSMIDREKLPPRRPPGLRAKGKPSMLEGIEKQGL----------DRWSEERW--RELRATYLGM 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 235 FSgqsfaersgrgpfgdslmELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETmrmsrgGCSGLLRCGKGTTYEGGVRE 314
Cdd:cd16150 206 VS------------------RLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT------GDYGLVEKWPNTFEDCLTRV 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482277 315 PALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLdGFDLSPLLLGTGKAL 371
Cdd:cd16150 262 PLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGETEEH 317
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
21-360 |
1.37e-18 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 87.40 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 21 RPPNIVLI----FADDLgygdLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPV--SlctpSRA--ALLTGRLPVRMGmypG 92
Cdd:COG1368 233 KKPNVVVIllesFSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGgrT----SRGefAVLTGLPPLPGG---S 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 93 VLVPSSRGGLPleevTVAEVLAARGYLT-----GMAGKWHLgvgpeGAFLpPHQGFHRFLGIPYshdqgpcqnltcFPPa 167
Cdd:COG1368 302 PYKRPGQNNFP----SLPSILKKQGYETsffhgGDGSFWNR-----DSFY-KNLGFDEFYDRED------------FDD- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 168 tPCDGG---CDQglvpipllanlsveaqppwlpglearymAFAHDLMADAQRQDRPFFLYY--ASHHTHYPQFSGQSFAE 242
Cdd:COG1368 359 -PFDGGwgvSDE----------------------------DLFDKALEELEKLKKPFFAFLitLSNHGPYTLPEEDKKIP 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 243 RSGRGPFGD---SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetmrMSRGGCSGLLRCGKGTTyeggvrePALaF 319
Cdd:COG1368 410 DYGKTTLNNylnAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP----RSPGKTDYENPLERYRV-------PLL-I 477
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1370482277 320 W-PGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDL 360
Cdd:COG1368 478 YsPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDL 519
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
23-347 |
2.07e-16 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 78.88 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLI----FADDLgygdLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRA--ALLTGRLPVRMGmyPGVLVP 96
Cdd:cd16015 1 PNVIVIllesFSDPY----IDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLG--SGSYTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 97 SSRGGLPleevTVAEVLAARGYLT-----GMAGKWHLgvgpeGAFLpPHQGFHRFLGIPYshdqgpcqnltcFPPATPCD 171
Cdd:cd16015 75 YKLNPLP----SLPSILKEQGYETifihgGDASFYNR-----DSVY-PNLGFDEFYDLED------------FPDDEKET 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 172 GG---CDQGLvpipllanlsveaqppwlpglearyMAFAHDLMADAQRQdrPFFLY---YASHH-----THYPQFSGQSF 240
Cdd:cd16015 133 NGwgvSDESL-------------------------FDQALEELEELKKK--PFFIFlvtMSNHGpydlpEEKKDEPLKVE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 241 AERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetmrmsrggcsGLLRCGKGTTYEGGVRE--PALA 318
Cdd:cd16015 186 EDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLP-----------SLGSDYDETDEDPLDLYrtPLLI 254
|
330 340
....*....|....*....|....*....
gi 1370482277 319 FWPGHIAPGVTHELASSLDLLPTLAALAG 347
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
23-369 |
2.30e-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: 76.81 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 23 PNIVLIFADDLgygDLGCYGHPSSTT---PNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvpSSR 99
Cdd:cd16171 1 PNVVMVMSDSF---DGRLTFRPGNQVvdlPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW------NNY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 100 GGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPegaflppHQGFHRFLG----IPYSHDQG--PCQNLTCfppatpcdgg 173
Cdd:cd16171 72 KGLDPNYPTWMDRLEKHGYHTQKYGKLDYTSGH-------HSVSNRVEAwtrdVPFLLRQEgrPTVNLVG---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 174 cDQGLVPIPLLANLSVEAQPPWLpglearymafahdlMADAQRQDRPFFLYYASHHTH-YP-QFSGQSFAE-RSGRGPFG 250
Cdd:cd16171 135 -DRSTVRVMLKDWQNTDKAVHWI--------------RKEAPNLTQPFALYLGLNLPHpYPsPSMGENFGSiRNIRAFYY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 251 DSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSrggcsgllRCGKGTTYEGGVREPALAFWPGhIAPGVTH 330
Cdd:cd16171 200 AMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHR--------QFYKMSMYEGSSHVPLLIMGPG-IKAGQQV 270
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1370482277 331 ELASSL-DLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGK 369
Cdd:cd16171 271 SDVVSLvDIYPTMLDIAGVPQPQ-NLSGYSLLPLLSESSI 309
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
21-285 |
1.33e-06 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 49.75 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 21 RPPNIVLIFADDLGYGDLGcyghpSSTTPNLDQLAAGGLRFTDFYVPV-SLCTPSRAALLTGRLPVRMGM---------Y 90
Cdd:COG1524 22 PAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIvgngwydpeL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 91 PGVLVPSSRGGLP------LEEVTVAEVLAARGYLTGMAGKWHLGVGP--EGAFLPPHQGFHRFLGIPYShdqgpcqnlt 162
Cdd:COG1524 97 GRVVNSLSWVEDGfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGliDAARPYPYDGRKPLLGNPAA---------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 163 cfppatpcdggcDQGLVpipllanlsveaqppwlpglearymafahDLMADAQRQDRPFFLY-------YASHHThypqf 235
Cdd:COG1524 167 ------------DRWIA-----------------------------AAALELLREGRPDLLLvylpdldYAGHRY----- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1370482277 236 sgqsfaersgrGPFG----DSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNG 285
Cdd:COG1524 201 -----------GPDSpeyrAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
189-285 |
2.44e-04 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 42.57 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 189 VEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYashHTHYPQFSGQSFaersgrGPFG----DSLMELDAAVGTLM 264
Cdd:cd16018 126 IPLGGYWQPYNDSFPFEERVDTILEWLDLERPDLILL---YFEEPDSAGHKY------GPDSpevnEALKRVDRRLGYLI 196
|
90 100
....*....|....*....|.
gi 1370482277 265 TAIGDLGLLEETLVIFTADNG 285
Cdd:cd16018 197 EALKERGLLDDTNIIVVSDHG 217
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
209-293 |
2.06e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 39.71 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482277 209 DLMADAQRQDRPFFLYYASHHTHYpqfSGQSFAERSGRgpFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPET 288
Cdd:pfam01663 152 DLPFADVAAERPDLLLVYLEEPDY---AGHRYGPDSPE--VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTP 226
|
....*
gi 1370482277 289 MRMSR 293
Cdd:pfam01663 227 VSDDK 231
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
21-65 |
4.35e-03 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 38.76 E-value: 4.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1370482277 21 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFY 65
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVI 45
|
|
| |
