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Conserved domains on  [gi|5360208|ref|NP_006114|]
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iduronate 2-sulfatase isoform b precursor [Homo sapiens]

Protein Classification

sulfatase( domain architecture ID 10888136)

sulfatase catalyzes the hydrolysis of sulfate ester bonds of a wide variety of substrates, similar to iduronate 2-sulfatase that hydrolyzes the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate, and heparin

Graphical summary

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List of domain hits

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
 
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
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 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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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