|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
38-337 |
9.34e-162 |
|
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: 458.96 E-value: 9.34e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16030 4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 118 TIPQYFKENGYVTMSVGKVFHPGISsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLP 197
Cdd:cd16030 84 TLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 198 DKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPEVPDGLPPVAYNPWMDIRQREDVQ 277
Cdd:cd16030 162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 278 ALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGF 337
Cdd:cd16030 241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGW 300
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
22-339 |
3.74e-66 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 213.59 E-value: 3.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 22 VALGSETQANSTTDALNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT 100
Cdd:COG3119 9 LALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 101 RLYDFNSYWRVH-AGNFSTIPQYFKENGYVTMSVGKVFHpgissnHTDDspyswsfppyhpssekyentktcrgpdgELh 179
Cdd:COG3119 89 GVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTD----------------------------LL- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 180 anllcpvdvldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlapdpEVPDGL 259
Cdd:COG3119 134 ----------------------TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI------PLPPNL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 260 PPVAYNPWmdirqredvqalnisvpygpipvdFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFLM 339
Cdd:COG3119 186 APRDLTEE------------------------ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL 241
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
38-336 |
6.26e-49 |
|
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: 168.07 E-value: 6.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 118 TIPQYFKENGYVTMSVGKVFHPGissnhtdDSPYSWSFPPYHPSSEKYENTKTCRGPDgelhanllcpvDVLDVPEgtlP 197
Cdd:cd16027 82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAA-----------DFLNRAK---K 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 198 DKqsteqaiqllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAP----DPEVpdglppvaynpwmdirqR 273
Cdd:cd16027 141 GQ------------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPylpdTPEV-----------------R 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5360208 274 EDVQAlnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16027 186 EDLAD---------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG 227
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-336 |
2.44e-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: 164.70 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY----DFNSYWRVH 112
Cdd:cd16033 2 NILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 113 AGNFSTIPQYFKENGYVTMSVGKvFHPGissnhTDDSPYSWSFPPYHPssekYENTKtcrgpdgelhanllcpvdvldvp 192
Cdd:cd16033 82 PPGVETFSEDLREAGYRNGYVGK-WHVG-----PEETPLDYGFDEYLP----VETTI----------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 193 EGTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVP-DGLPPVAYNpwmdIR 271
Cdd:cd16033 129 EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDfEDKPYIYRR----ER 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5360208 272 QREDVQALNISVpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16033 200 KRWGVDTEDEED---------WKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHG 255
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-339 |
1.52e-46 |
|
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: 162.35 E-value: 1.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLydFNSYWRVHAgNF 116
Cdd:cd16034 3 NILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV--FGNDVPLPP-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 STIPQYFKENGYVTMSVGKvFHpgISSNHTDDSPYSWSFPP-----------------YHPSSEKYENTktcrgpdgelh 179
Cdd:cd16034 80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDDD----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 180 anllcpvDVLDVPEGTLPDKQsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDpevpdg 258
Cdd:cd16034 146 -------GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 259 lppvaynpwMDIRQREDVQAlnisvpygpipvdfQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFL 338
Cdd:cd16034 212 ---------VPEDKKEEAGL--------------REDLRG-YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM 267
|
.
gi 5360208 339 M 339
Cdd:cd16034 268 L 268
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-343 |
2.35e-45 |
|
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: 160.02 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16144 2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 S---------------TIPQYFKENGYVTMSVGKvFHPGISSNHT--------DDSPYSWSFPPYHPSSEKYENTKTCRG 173
Cdd:cd16144 82 KlipppsttrlpleevTIAEALKDAGYATAHFGK-WHLGGEGGYGpedqgfdvNIGGTGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 174 PDGElHanllcPVDVLdvpegtlpdkqsTEQAIQLLEkmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdP 253
Cdd:cd16144 161 PEGE-Y-----LTDRL------------TDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKY----------E 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 254 EVPDGLPPVAYNPwmdirqredvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTS 333
Cdd:cd16144 211 KKKKGLRKGQKNP--------------------------------VYAAMIESLDESVGRILDALEELGLADNTLVIFTS 258
|
330
....*....|
gi 5360208 334 DHGFLMRTNT 343
Cdd:cd16144 259 DNGGLSTRGG 268
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
38-339 |
6.12e-44 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 157.52 E-value: 6.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHAGN 115
Cdd:PRK13759 8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 116 FS-TIPQYFKENGYVTMSVGKV-FHPGIS----SNHTDDSPYSWSFPPYHPSseKYENTKTCR--------GPDGEL--- 178
Cdd:PRK13759 84 YKnTLPQEFRDAGYYTQCIGKMhVFPQRNllgfHNVLLHDGYLHSGRNEDKS--QFDFVSDYLawlrekapGKDPDLtdi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 179 ----HANLLCPvdvLDVPEGTLPDKQSTEQAIQLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPE 254
Cdd:PRK13759 162 gwdcNSWVARP---WDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 255 VPDglppvaynpWmDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSD 334
Cdd:PRK13759 235 IGD---------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSD 304
|
....*
gi 5360208 335 HGFLM 339
Cdd:PRK13759 305 HGDML 309
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-336 |
1.22e-43 |
|
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: 154.26 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQ----QAVCAPSRVSFLTGRrpdttrlydfnSYWRVH 112
Cdd:cd16155 4 NILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR-----------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 113 AGNFS-------TIPQYFKENGYVTMSVGKvfhpgissNHTDdspyswsfppyhpssekyentktcrgpdgelHANllcp 185
Cdd:cd16155 73 EGGKAaipsddkTWPETFKKAGYRTFATGK--------WHNG-------------------------------FAD---- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 186 vdvldvpegtlpdkqsteQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdPEVPDGLPPVAyN 265
Cdd:cd16155 110 ------------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL---PENFLPQHPFD-N 167
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5360208 266 PWMDIRqreDVQalnisvpYGPIPVDFQ--RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16155 168 GEGTVR---DEQ-------LAPFPRTPEavRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG 230
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
38-339 |
1.29e-42 |
|
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: 147.58 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16022 2 NILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 STIPQYFKENGYVTMSVGKvfhpgissNHtddspyswsfppyhpssekyentktcrgpdgelhanllcpvdvldvpegtl 196
Cdd:cd16022 82 PTLAELLKEAGYRTALIGK--------WH--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 197 pdkqstEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRypkefqklyplenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:cd16022 103 ------DEAIDFIERRDKDK-PFFLYVSFNAPHPPFA------------------------------------------- 132
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5360208 277 qalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFLM 339
Cdd:cd16022 133 -----------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDML 172
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-336 |
2.27e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 149.62 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhAGNF 116
Cdd:cd16037 2 NILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPY---DGDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 STIPQYFKENGYVTMSVGKvfhpgissnhtddspyswsfppyhpssekyentktcrgpdgeLHANllcpvdVLDVPEGTL 196
Cdd:cd16037 79 PSWGHALRAAGYETVLIGK------------------------------------------LHFR------GEDQRHGFR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 197 PDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:cd16037 111 YDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY---------------------------------- 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 277 qalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16037 157 ----------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHG 200
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
38-339 |
3.65e-41 |
|
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: 148.83 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRvhAGNF 116
Cdd:cd16031 4 NIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLF--DASQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 STIPQYFKENGYVTMSVGKvFHPGISSNHTDDS--------PYSWSFPPYHPSSEKYentktcRGPDGelHANLLCpvdv 188
Cdd:cd16031 82 PTYPKLLRKAGYQTAFIGK-WHLGSGGDLPPPGfdywvsfpGQGSYYDPEFIENGKR------VGQKG--YVTDII---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 189 ldvpegtlpdkqsTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAP--DPEVPDGLPPVAYNP 266
Cdd:cd16031 149 -------------TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPEtfDDDDYAGRPEWAREQ 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5360208 267 WMDIRQREDVQALNisvpygpiPVDFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFLM 339
Cdd:cd16031 215 RNRIRGVLDGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL 278
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-336 |
6.78e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 136.74 E-value: 6.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRP-SLGCYGDKL----------VRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFN 106
Cdd:cd16153 3 NILWIITDDQRVdSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 107 SYWRVHAGNFSTIPQYFKENGYVTMSVGKvfhpgissnhtddspyswsfppyhpssEKYENtktcrgpdgelhanllcPV 186
Cdd:cd16153 83 AAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA-----------------FQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 187 DVLDVPEgtlpdkQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdpevpdglppvaynp 266
Cdd:cd16153 119 RYLKNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---------------------------- 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5360208 267 wmdiRQREDvqalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLAN---STIIAFTSDHG 336
Cdd:cd16153 165 ----RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHG 209
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-339 |
2.33e-37 |
|
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: 134.98 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 37 LNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPdttrlydfnSYWRVHAG- 114
Cdd:cd16148 1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP---------FYHGVWGGp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 115 ---NFSTIPQYFKENGYVTMSVGkvfhpgissnhtdDSPYSWSFPPYHPSSEKYENTktcRGPDGElhanllcpvdvlDV 191
Cdd:cd16148 72 lepDDPTLAEILRKAGYYTAAVS-------------SNPHLFGGPGFDRGFDTFEDF---RGQEGD------------PG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 192 PEGTLPDKQSTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapDpevpdglppvaynpwmdir 271
Cdd:cd16148 124 EEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-----------------D------------------- 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5360208 272 qredvqalnisvpygpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFLM 339
Cdd:cd16148 167 ------------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEF 204
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-336 |
4.56e-37 |
|
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: 137.73 E-value: 4.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY---WRVHA 113
Cdd:cd16145 2 NIIFILADDLGYGdLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPggqDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 114 GNfSTIPQYFKENGYVTMSVGKVfhpGISSNHTDDSPYS----------------WSFPPYhpsseKYENTKTcrgpdgE 177
Cdd:cd16145 82 DD-VTLAEVLKKAGYATAAFGKW---GLGGPGTPGHPTKqgfdyfygyldqvhahNYYPEY-----LWRNGEK------V 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 178 LHANLLCPVDVLDVPEGTLPDKQS----TEQAIQLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDP 253
Cdd:cd16145 147 PLPNNVIPPLDEGNNAGGGGGTYShdlfTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 254 EVPDGLPPVAYNPWMDIRQRedvqalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTS 333
Cdd:cd16145 213 YKPKDPGIYAYLPWPQPEKA--------------------------YAAMVTRLDRDVGRILALLKELGIDENTLVVFTS 266
|
...
gi 5360208 334 DHG 336
Cdd:cd16145 267 DNG 269
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
38-336 |
3.91e-35 |
|
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: 133.15 E-value: 3.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFN--SYWR---V 111
Cdd:cd16028 2 NVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR-------YLMNhrSVWNgtpL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 112 HAGnFSTIPQYFKENGYVTMSVGKvfhpgissnhTDDSPYSWSFPPYHPSSEKYEntktcrgpdgelhaNLLCPVDVLDV 191
Cdd:cd16028 75 DAR-HLTLALELRKAGYDPALFGY----------TDTSPDPRGLAPLDPRLLSYE--------------LAMPGFDPVDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 192 PEGtLPDKQS-----TEQAIQLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDPEVPDGLPPVa 263
Cdd:cd16028 130 LDE-YPAEDSdtaflTDRAIEYLDERQD--EPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQHPL- 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5360208 264 YNPWMDIRQREDVQALNISVPYGPIPVdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16028 206 LAAFLERIESLSFSPGAANAADLDDEE--VAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG 276
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
37-336 |
3.11e-34 |
|
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: 128.08 E-value: 3.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 37 LNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfnsywrvHAGN 115
Cdd:cd16032 1 PNILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYD-------NAAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 116 FS----TIPQYFKENGYVTMSVGKVfHpgissnhtddspyswsFPpyhpssekyentktcrGPDgELHanllcpvdvldv 191
Cdd:cd16032 74 FPadipTFAHYLRAAGYRTALSGKM-H----------------FV----------------GPD-QLH------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 192 peGTLPDKQSTEQAIQLLEKMKTSAS--PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdpevpdglppvaynpwmd 269
Cdd:cd16032 108 --GFDYDEEVAFKAVQKLYDLARGEDgrPFFLTVSFTHPHDPYVIPQEYWDLY--------------------------- 158
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5360208 270 irqredvqalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16032 159 -----------------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHG 202
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-336 |
2.34e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 127.74 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16150 2 NIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 StipQYFKENGYVTMSVGKvfhpgissNHTDDSPYSWsfppyhpssEKYEntktcrgpdgelhanllcpvdvldvpegtL 196
Cdd:cd16150 82 L---KTLKDAGYHVAWAGK--------NDDLPGEFAA---------EAYC-----------------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 197 PDKQSTEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPdPEVPDGLPpvAYNPWMDIRQREDv 276
Cdd:cd16150 113 SDEACVRTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLR--AKGKPSMLEGIEK- 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 277 QALNisvpygPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16150 185 QGLD------RWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHG 238
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-336 |
6.93e-33 |
|
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: 125.75 E-value: 6.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16026 3 NIVVILADDLGYGdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 115 -NFSTIPQYFKENGYVTMSVGKvFHPGISSNH--TD---DS----PYS---WSFPPYHPSSEKYEntktcrgpdgelhAN 181
Cdd:cd16026 83 pDEITIAEVLKKAGYRTALVGK-WHLGHQPEFlpTRhgfDEyfgiPYSndmWPFPLYRNDPPGPL-------------PP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 182 LLCPVDVLDVPegtlPD-----KQSTEQAIQLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFqklyplENITLApdpevp 256
Cdd:cd16026 149 LMENEEVIEQP----ADqssltQRYTDEAVDFIERNKD--QPFFLYLAHTMPHVPLFASEKF------KGRSGA------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 257 dGLppvaynpwmdirqredvqalnisvpYGpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16026 211 -GL-------------------------YG---------------DVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
38-336 |
7.19e-33 |
|
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: 125.74 E-value: 7.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLrpslGcYGD------KLVRSPNIDQLASHSLLFQNAFAQQaVCAPSRVSFLTGRRPDTTRLYDFNSYWRV 111
Cdd:cd16029 2 HIVFILADDL----G-WNDvgfhgsDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILAGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 112 HAG---NFSTIPQYFKENGYVTMSVGKvFHPGISS-NHTD-----DSPYSwsfppYHPSSEKYENTKTCRGPDgelhanl 182
Cdd:cd16029 76 PYGlplNETLLPQYLKELGYATHLVGK-WHLGFYTwEYTPtnrgfDSFYG-----YYGGAEDYYTHTSGGAND------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 183 lCPVDVLDVPEGTLPDKQS-------TEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpev 255
Cdd:cd16029 143 -YGNDDLRDNEEPAWDYNGtystdlfTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE------------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 256 pdglppvaynpwmdirqredVQALNISvpygpipvDFQRKIrqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDH 335
Cdd:cd16029 209 --------------------DKFAHIK--------DEDRRT---YAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDN 257
|
.
gi 5360208 336 G 336
Cdd:cd16029 258 G 258
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
38-336 |
8.43e-33 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 123.69 E-value: 8.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVhAGNF 116
Cdd:pfam00884 2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYV-STPVGL-PRTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 STIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelhanllcpvdvldvPEGTL 196
Cdd:pfam00884 80 PSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------SGGGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 197 PDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:pfam00884 143 SDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA--------------------------------- 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 277 qalnISVPYGpipvDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:pfam00884 187 ----TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHG 238
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-339 |
5.35e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 120.42 E-value: 5.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRV----- 111
Cdd:cd16149 2 NILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHgktkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 112 ---HAGNFSTIPQYFKENGYVTMSVGKvFHPGissnhtddspyswsfppyhpssekyentktcrgpdgelhanllcpvdv 188
Cdd:cd16149 82 pegYLEGQTTLPEVLQDAGYRCGLSGK-WHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 189 ldvpegtlpdkqstEQAIQLLEKMKTSASPFFLAVGYHKPHipfrypkefqklyplenitlapdpevpdglppvayNPWm 268
Cdd:cd16149 113 --------------DDAADFLRRRAEAEKPFFLSVNYTAPH-----------------------------------SPW- 142
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5360208 269 dirqredvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFLM 339
Cdd:cd16149 143 ------------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNM 183
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-336 |
3.84e-30 |
|
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: 118.46 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRP-SLGCYGDK-LVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFNSY--WRVhA 113
Cdd:cd16143 2 NIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGR-------YPWRSRlkGGV-L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 114 GNFS---------TIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelHANLLC 184
Cdd:cd16143 74 GGFSppliepdrvTLAKMLKQAGYRTAMVGK-WHLGLDWKKKDGKKAATGTGKDVDYSKPIKGGPLDHGFD---YYFGIP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 185 PVDVLDvpegTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapdpevpdglppvay 264
Cdd:cd16143 150 ASEVLP----TL-----TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQG------------------------ 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5360208 265 npwmdirqredVQALNisvPYGpipvDFqrkIRQsyfasvsyLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16143 197 -----------KSGAG---PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNG 239
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
38-339 |
2.87e-29 |
|
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: 117.10 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTtrlydfNSYWR---VHA 113
Cdd:cd16156 2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT------NGSWTncmALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 114 GNFSTIPQYFKENGYVTMSVGK-------VFHPGISSNHTDdSPYSWSFPPYHPSSEKYENTKTCRGPDgELHANllcpv 186
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKwhldggdYFGNGICPQGWD-PDYWYDMRNYLDELTEEERRKSRRGLT-SLEAE----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 187 dvlDVPEGTLPDKQSTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplENITLAPDPEVPDGLP--PVAY 264
Cdd:cd16156 149 ---GIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLHQ 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5360208 265 NPWMDIRQREDVQALNISVPYgpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLqLANSTIIaFTSDHGFLM 339
Cdd:cd16156 222 RLWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI-AEDAWVI-YTSDHGDML 280
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
38-336 |
5.14e-29 |
|
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: 115.34 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNaFAQQAVCAPSRVSFLTGRRPDTTRLydfnsyWRVHAG-- 114
Cdd:cd16146 2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGV------WHTILGre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 115 ----NFSTIPQYFKENGYVTMSVGKvFHPGissnhtDDSPY----------------SWSFPPYHPSSEKYENTKTCRGP 174
Cdd:cd16146 75 rmrlDETTLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 175 ----DGelhanlLCPvDVLdvpegtlpdkqsTEQAIQLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFQKLYplenitla 250
Cdd:cd16146 148 fvktEG------YCT-DVF------------FDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPY-------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 251 PDPEVPDGlppvaynpwmdirqredvqalnisvpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIA 330
Cdd:cd16146 199 KDMGLDDK--------------------------------------LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVI 240
|
....*.
gi 5360208 331 FTSDHG 336
Cdd:cd16146 241 FMSDNG 246
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
38-336 |
3.04e-28 |
|
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: 113.31 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDkLVRSPNIDQLASHSLLFQNaFAQQAVCAPSRVSFLTGRRP-------DTTRLYDFNSYW 109
Cdd:cd16025 4 NILLILADDLGFSdLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHhqvgmgtMAELATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 110 RVHAGNFSTIPQYFKENGYVTMSVGKvfhpgissnhtddspysW--SFPPYHpSSEKYentktcrgpdgelhanllcpvd 187
Cdd:cd16025 82 GYLPDSAATIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL---------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 188 vldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LY 242
Cdd:cd16025 122 --------------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 243 PlENITLAP-DPEVPdglppvaynPWMDIRQRE-DVQALNISVpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDD 320
Cdd:cd16025 188 P-ADTKLTPrPPGVP---------AWDSLSPEEkKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKE 241
|
330
....*....|....*.
gi 5360208 321 LQLANSTIIAFTSDHG 336
Cdd:cd16025 242 LGELDNTLIIFLSDNG 257
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-336 |
4.45e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 109.61 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAqQAVCAPSRVSFLTGRRPDTTrlYDFNSYWrvHAGNf 116
Cdd:cd16151 2 NIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRN--YVVFGYL--DPKQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 STIPQYFKENGYVTMSVGKvfhPGISSNhTDDSPYS-------WSFPPYHPSSEKYENTKTcrgPDGELHANllcpvDVL 189
Cdd:cd16151 76 KTFGHLLKDAGYATAIAGK---WQLGGG-RGDGDYPhefgfdeYCLWQLTETGEKYSRPAT---PTFNIRNG-----KLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 190 DVPEGTL-PDkQSTEQAIQLLEKMKtsASPFFLavgY------HKPHIPFrypkefqklyplenitlaPDPEvpdglppv 262
Cdd:cd16151 144 ETTEGDYgPD-LFADFLIDFIERNK--DQPFFA---YypmvlvHDPFVPT------------------PDSP-------- 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5360208 263 aynPWMDIRQRedvqalnisvpygpipvdfqRKIRQSYF-ASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16151 192 ---DWDPDDKR--------------------KKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNG 243
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-341 |
3.77e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 106.93 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHAGNF 116
Cdd:cd16152 3 NVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFR-NG--IPLPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 STIPQYFKENGYVTMSVGKvfhpgissnhtddspysWSFPPYHpssekyentktcrgpdgelhanllcpVDVLdvpegtl 196
Cdd:cd16152 80 KTLAHYFRDAGYETGYVGK-----------------WHLAGYR--------------------------VDAL------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 197 pdkqsTEQAIQLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYplenitlaPDPEVPdglppvaynpwmdir 271
Cdd:cd16152 110 -----TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERF--------ANFWVP--------------- 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 272 qrEDVQALnisvpygpiPVDFQRKIrQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFLMRT 341
Cdd:cd16152 161 --PDLAAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRT 218
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-336 |
5.58e-25 |
|
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: 103.77 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDKLVR---SPNIDQLASHSLLFQNAFAQQAvCAPSRVSFLTGRRPdttrlydfnsywrVHA 113
Cdd:cd16142 2 NILVILGDDIGWGdLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP-------------IRT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 114 GNFS---------------TIPQYFKENGYVTMSVGKvfhpgissNHTDDSPYSWsfPpyhpssekyentkTCRGPDgEL 178
Cdd:cd16142 68 GLTTvglpgspgglppwepTLAELLKDAGYATAQFGK--------WHLGDEDGRL--P-------------TDHGFD-EF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 179 HANLLcpvdvldvpegTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdg 258
Cdd:cd16142 124 YGNLY-----------HTIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS--------------- 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5360208 259 lppvAYNPWMDirqredvqalnisvpygpipvdfqrkirqsyfaSVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16142 178 ----GKGKYAD---------------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNG 218
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
38-339 |
5.65e-24 |
|
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: 101.09 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPSLGCYGD--KLVRspnidQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSY----WRV 111
Cdd:cd16147 3 NIVLILTDDQDVELGSMDPmpKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTN-NSPpgggYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 112 HAGNF---STIPQYFKENGYVTMSVGKVFHpGISSNHTDDSP---YSWSFPPYHPSseKYENTKTCRGPDGELHANllCP 185
Cdd:cd16147 77 FWQNGlerSTLPVWLQEAGYRTAYAGKYLN-GYGVPGGVSYVppgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVS--YP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 186 V----DVLdvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAP-----DPEVP 256
Cdd:cd16147 152 GdyltDVI------------ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPrpppnNPDVS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 257 DG--------LPPVAYNPWMDIRQREDVQALnisvpygpipvdfqrkirqsyfASVsylDTQVGRLLSALDDLQLANSTI 328
Cdd:cd16147 218 DKphwlrrlpPLNPTQIAYIDELYRKRLRTL----------------------QSV---DDLVERLVNTLEATGQLDNTY 272
|
330
....*....|.
gi 5360208 329 IAFTSDHGFLM 339
Cdd:cd16147 273 IIYTSDNGYHL 283
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-336 |
2.54e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 86.88 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYD-FNSYWRVHAGN 115
Cdd:cd16035 2 NILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLLSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 116 -FSTIPQYFKENGYVTMSVGKvfhpgissnhtddspysWsfppyHPSSekyentktcrgpdgelHANllcpvdvldvpEG 194
Cdd:cd16035 82 dVPTLGHMLRAAGYYTAYKGK-----------------W-----HLSG----------------AAG-----------GG 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 195 TLPDKQSTEQAIQLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdpevpdglppvaynpwmdir 271
Cdd:cd16035 113 YKRDPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH------------------------------------------ 150
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5360208 272 qreDVQalnisvpYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16035 151 ---DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG 205
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
38-336 |
6.85e-18 |
|
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: 84.26 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYwRV----- 111
Cdd:cd16159 3 NIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGM-RVilfta 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 112 -HAG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHTDDSpyswsfpPYHPSSEKYE--------NTKTCRGPDGElh 179
Cdd:cd16159 82 sSGGlppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDF-------CHHPLNHGFDyfyglpltNLKDCGDGSNG-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 180 ANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKL--------------YPLE 245
Cdd:cd16159 152 EYDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRYFncilmrnhevveqpMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 246 NITLAPDPEVPDGL------PPVAYNPWmdirqredvqaLNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALD 319
Cdd:cd16159 232 NLTQRLTKEAISFLernkerPFLLVMSF-----------LHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALD 300
|
330
....*....|....*..
gi 5360208 320 DLQLANSTIIAFTSDHG 336
Cdd:cd16159 301 ELGLKDNTFVYFTSDNG 317
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
38-336 |
8.97e-18 |
|
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: 84.03 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16158 3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 115 -NFSTIPQYFKENGYVTMSVGKvFHPGISSN-----------HTDDSPYSWSFPPYHPSSEKYENTK---TCRgpDGELH 179
Cdd:cd16158 83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNgtylpthqgfdHYLGIPYSHDQGPCQNLTCFPPNIPcfgGCD--QGEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 180 ANLLC-------PVDVLDVpegtlpDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapd 252
Cdd:cd16158 160 CPLFYnesivqqPVDLLTL------EERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFA------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 253 pevpdglppvaynpwmdirqredvqalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFT 332
Cdd:cd16158 221 ----------------------------------------GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFT 260
|
....
gi 5360208 333 SDHG 336
Cdd:cd16158 261 SDNG 264
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-336 |
1.27e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 77.00 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDL-RPSLGCY--GDKLVRSPNIDQLASHSLLFQNAFAqQAVCAPSRVSFLTGRrpdttrlYDFN----SYWR 110
Cdd:cd16154 2 NILLIIADDQgLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGK-------YGFRtgvlAVPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 111 VHAGNFSTIPQYFKEN----GYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPS--SEKYENTKTCRGPDGELHanllc 184
Cdd:cd16154 74 ELLLSEETLLQLLIKDattaGYSSAVIGK-WHLGGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 185 pvdvldvpegTLPDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDpevpdgLPPV 262
Cdd:cd16154 148 ----------EYATTKLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGD------SADI 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5360208 263 AYNPwmdirqredvqalnisvpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIaFTSDHG 336
Cdd:cd16154 202 EANP------------------------------RPYYLAAIEAMDTEIGRLLASIDEEERENTIII-FIGDNG 244
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-336 |
4.65e-15 |
|
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: 75.58 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSywrvHAGNF 116
Cdd:cd16157 3 NIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA----HARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 ST--------------IPQYFKENGYVTMSVGK-------VFHPgisSNHTDD----SPySWSFPPY----HPSSEKYEN 167
Cdd:cd16157 79 YTpqnivggipdseilLPELLKKAGYRNKIVGKwhlghrpQYHP---LKHGFDewfgAP-NCHFGPYdnkaYPNIPVYRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 168 TKTCrgpdGELHANLlcPVDvLDVPEGTLpDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPfrypkefqkLYpleni 247
Cdd:cd16157 155 WEMI----GRYYEEF--KID-KKTGESNL-TQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAP---------VY----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 248 tlapdpevpdglppvAYNPWMDIRQREdvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANST 327
Cdd:cd16157 213 ---------------ASKPFLGTSQRG------------------------LYGDAVMELDSSVGKILESLKSLGIENNT 253
|
....*....
gi 5360208 328 IIAFTSDHG 336
Cdd:cd16157 254 FVFFSSDNG 262
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
38-338 |
2.31e-14 |
|
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: 73.34 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPSLGCY-GDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRlyDFNSYWRVHAgNF 116
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE--SWNNYKGLDP-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 117 STIPQYFKENGYVTMSVGKVFHpgiSSNHtddspyswsfppyHPSSEKYE----NTKTCRGPDGELHANLLCPVDVLDVp 192
Cdd:cd16171 79 PTWMDRLEKHGYHTQKYGKLDY---TSGH-------------HSVSNRVEawtrDVPFLLRQEGRPTVNLVGDRSTVRV- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 193 egTLPDKQSTEQAIQLLEKMKTSAS-PFFLAVGYHKPHiPFRYPkefqklypleniTLAPDpevpdglppvaynpwmdir 271
Cdd:cd16171 142 --MLKDWQNTDKAVHWIRKEAPNLTqPFALYLGLNLPH-PYPSP------------SMGEN------------------- 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5360208 272 qredvqalnisvpYGPIpvdfqRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFL 338
Cdd:cd16171 188 -------------FGSI-----RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGEL 236
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
38-336 |
2.86e-14 |
|
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: 73.23 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRpslgcYGDKLV-------RSPnIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY--DFNSY 108
Cdd:cd16160 3 NIVLFFADDMG-----YGDLASyghptqeRGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 109 WRVHAG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYswsFPPYH---------PssekYENTKTCrgPDG 176
Cdd:cd16160 77 PWDIGGlpkTEVTMAEALKEAGYTTGMVGK-WHLGINENNHSDGAH---LPSHHgfdfvgtnlP----FTNSWAC--DDT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 177 ELHanllcpVDVLDVPEGTLPDK-QSTEQAIQ---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyp 243
Cdd:cd16160 147 GRH------VDFPDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 244 lenitlapdpevpdglppvaynpwmdirqredvqalNISVpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQL 323
Cdd:cd16160 217 ------------------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGL 247
|
330
....*....|...
gi 5360208 324 ANSTIIAFTSDHG 336
Cdd:cd16160 248 DQNTLVFFLSDHG 260
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
38-336 |
3.10e-14 |
|
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: 72.89 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLR-PSLGCYGDKLVR-SPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVHAG- 114
Cdd:cd16161 3 NFLLLFADDLGwGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH-NFLPTSVGGl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 115 --NFSTIPQYFKENGYVTMSVGKvFHPGissnHTDdspyswsfpPYHPSSekyentktcRGPDgelhanllcpvDVLDVP 192
Cdd:cd16161 82 plNETTLAEVLRQAGYATGMIGK-WHLG----QRE---------AYLPNS---------RGFD-----------YYFGIP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 193 ---EGTLPDKQStEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdpevpdglppvaynpwmd 269
Cdd:cd16161 128 fshDSSLADRYA-QFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQ------------------------------ 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5360208 270 irqredvQALNISVPYGpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16161 177 -------SPTSGRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNG 221
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
26-336 |
4.62e-13 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 70.07 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 26 SETQANSTTDALNVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGrrpdttrLYD 104
Cdd:COG1368 224 PTPNPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-------LPP 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 105 FNS---YWRVHAGNFSTIPQYFKENGYVTMsvgkVFHPGissnhtddSPYSWSFPPYHP--------SSEKYENTKTcrG 173
Cdd:COG1368 297 LPGgspYKRPGQNNFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYKnlgfdefyDREDFDDPFD--G 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 174 PDGelhanllcpvdvldvpegtLPDKQSTEQAIQLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITL 249
Cdd:COG1368 363 GWG-------------------VSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 250 apdpevpdglppvaynpwmdirqredvqalnisvpygpipvdfqrkirQSYFASVSYLDTQVGRLLSALDDLQLANSTII 329
Cdd:COG1368 417 ------------------------------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIF 448
|
....*..
gi 5360208 330 AFTSDHG 336
Cdd:COG1368 449 VIYGDHG 455
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
38-336 |
1.36e-11 |
|
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: 64.24 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVC--APSRVSFLTGRRPDTTRLYDFNSYwrvHAG 114
Cdd:cd16015 2 NVIVILLESFsDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPPLPLGSGSYTLY---KLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 115 NFSTIPQYFKENGYVTMSvgkvFHPGissnhtddSPYSWSFPPYHP--------SSEKYENTKTCRGPDGelhanllcpv 186
Cdd:cd16015 79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPnlgfdefyDLEDFPDDEKETNGWG---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 187 dvldvpegtLPDKQSTEQAIQLLEKMKtsASPFFLAV----GyhkpHIPFRYPKEFQKLyplenitlapdpevpdglppv 262
Cdd:cd16015 137 ---------VSDESLFDQALEELEELK--KKPFFIFLvtmsN----HGPYDLPEEKKDE--------------------- 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5360208 263 aynpwmdirqredvqalnisvpygPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16015 181 ------------------------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHL 230
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
38-336 |
9.61e-09 |
|
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: 55.12 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQnAFAQQAVC--APSRVSFLTGRRPDttrlydfnsywrvhag 114
Cdd:cd00016 2 HVVLIVLDGLGADdLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTssAPNHAALLTGAYPT---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 115 nfstipqyfkENGYVTMSVGKVFHPGISSNHTDDSPyswSFPpyhpssekyentktcrgpdgelhanllcpvdvldvpeG 194
Cdd:cd00016 65 ----------LHGYTGNGSADPELPSRAAGKDEDGP---TIP-------------------------------------E 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 195 TLPDKQSTEQAIQLLE--KMKTSASPFFLAVGYHKPHIPFRypkefqklyplenitlAPDPEVPdglppvaynpwmdirq 272
Cdd:cd00016 95 LLKQAGYRTGVIGLLKaiDETSKEKPFVLFLHFDGPDGPGH----------------AYGPNTP---------------- 142
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5360208 273 redvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd00016 143 --------------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-337 |
1.98e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 45.89 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 13 LGLVLSSVCVALGSETQANSttdalNVLLIIVDDLRPslgcygDKLVR--SPNIDQLASHSLLFQNAfaqQAVC----AP 86
Cdd:COG1524 5 LSLLLASLLAAAAAAAPPAK-----KVVLILVDGLRA------DLLERahAPNLAALAARGVYARPL---TSVFpsttAP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 87 SRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS------------------TIPQYFKENGyvtMSVGKVFHPGissnhTDD 148
Cdd:COG1524 71 AHTTLLTGLYPGEHGIVGNGWYDPELGRVVNslswvedgfgsnsllpvpTIFERARAAG---LTTAAVFWPS-----FEG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 149 SPYSWSFPPYHPSSEKYentktcrgpdgelhanllcpvdVLDVPEGtlpDKQSTEQAIQLLEKmktsaspfflavgyHKP 228
Cdd:COG1524 143 SGLIDAARPYPYDGRKP----------------------LLGNPAA---DRWIAAAALELLRE--------------GRP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5360208 229 HIpfrypkefqkLYplenitlapdpevpdglppvAYNPWMD-IRQRedvqalnisvpYGPipvdfqrkirQS--YFASVS 305
Cdd:COG1524 184 DL----------LL--------------------VYLPDLDyAGHR-----------YGP----------DSpeYRAALR 212
|
330 340 350
....*....|....*....|....*....|..
gi 5360208 306 YLDTQVGRLLSALDDLQLANSTIIAFTSDHGF 337
Cdd:COG1524 213 EVDAALGRLLDALKARGLYEGTLVIVTADHGM 244
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
302-338 |
3.59e-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: 41.80 E-value: 3.59e-04
10 20 30
....*....|....*....|....*....|....*..
gi 5360208 302 ASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGFL 338
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMT 219
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
301-337 |
2.49e-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: 39.33 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|....*..
gi 5360208 301 FASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGF 337
Cdd:pfam01663 188 EDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGM 224
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
39-108 |
7.68e-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: 37.79 E-value: 7.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5360208 39 VLLIIVDDLRPSlgcYGDKLVRSPNIDQLASHSLLFQNAFAQ-QAVCAPSRVSFLTGRRPDTTRLYDFNSY 108
Cdd:pfam01663 1 LLVISLDGFRAD---YLDRFELTPNLAALAKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGSHGIVGNTFY 68
|
|
| |
