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Conserved domains on  [gi|768032438|ref|XP_011543826|]
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arylsulfatase F isoform X3 [Homo sapiens]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

alkaline phosphatase (ALP) family protein may catalyze the hydrolysis of substrates; the ALP superfamily includes alkaline phosphatases and sulfatases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 46-425 2.38e-175

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.


The actual alignment was detected with superfamily member cd16159:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 521  Bit Score: 501.82  E-value: 2.38e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNL 125
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 126 AVPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYYYGMPFTLVDSCWPDPSRNTELAFESQ 205
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 206 LWLCVQLVAIAILTLTFGKLSGWVSvpWLLIFSMILFIFLLGYAWFSSHTSPLYWDCLLMRGHEITEQPMKAERAGSIMV 285
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 286 KEAISFLE------------------------------------------------------------------------ 293
Cdd:cd16159  239 KEAISFLErnkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvgqildaldelglkdntfvyftsdngg 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 294 -------------------------------------------------------------------------RVIDGRD 300
Cdd:cd16159  319 hleeisvggeygggnggiyggkkmggweggirvptivrwpgvippgsvideptslmdifptvaalagaplpsdRIIDGRD 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 301 LMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPKdDSGSVWKAHYVTPVFQpPASGGCYVTSLCRCFGEQVTYHNPPLLFD 380
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPR-DGGAVWKAHYFTPNFY-PGTEGCCGTLLCRCFGDSVTHHDPPLLFD 476

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 768032438 381 LSRDPSESTPLTPATEPlHDFVIKKVANALKEHQETIVPVTYQLS 425
Cdd:cd16159  477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
 46-425 2.38e-175

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: 501.82  E-value: 2.38e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNL 125
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 126 AVPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYYYGMPFTLVDSCWPDPSRNTELAFESQ 205
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 206 LWLCVQLVAIAILTLTFGKLSGWVSvpWLLIFSMILFIFLLGYAWFSSHTSPLYWDCLLMRGHEITEQPMKAERAGSIMV 285
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 286 KEAISFLE------------------------------------------------------------------------ 293
Cdd:cd16159  239 KEAISFLErnkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvgqildaldelglkdntfvyftsdngg 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 294 -------------------------------------------------------------------------RVIDGRD 300
Cdd:cd16159  319 hleeisvggeygggnggiyggkkmggweggirvptivrwpgvippgsvideptslmdifptvaalagaplpsdRIIDGRD 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 301 LMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPKdDSGSVWKAHYVTPVFQpPASGGCYVTSLCRCFGEQVTYHNPPLLFD 380
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPR-DGGAVWKAHYFTPNFY-PGTEGCCGTLLCRCFGDSVTHHDPPLLFD 476

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 768032438 381 LSRDPSESTPLTPATEPlHDFVIKKVANALKEHQETIVPVTYQLS 425
Cdd:cd16159  477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
312-446 2.07e-54

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 177.51  E-value: 2.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  312 SEHEFLFHYCGSYLHAVRWIPkddsgsvWKAHYVTPVFQPPASGGCYVTslcrcfGEQVTYHNPPLLFDLSRDPSESTPL 391
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP-------YKAHFFTPSFDPPGAEGCYGS------KVPVTHHDPPLLFDLERDPSEKYPL 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032438  392 TPATePLHDFVIKKVANALKEHQETIVPVTYQLSELNQG-RTWLKPCCGVFPFCLC 446
Cdd:pfam14707  68 SPDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLwDPWLQPCCPTFPACTC 122
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
18-156 4.33e-52

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 180.46  E-value: 4.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  18 MRpRRPLVFMSLVCALLNTCQAhrvhdDKPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSP 97
Cdd:COG3119    1 MK-RLLLLLLALLAAAAAAAAA-----KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSP 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032438  98 SRSAFLTGRYPIRSGMVSSGNRRviqnlavPAGLPLNETTLAALLKKQGYSTGLIGKWH 156
Cdd:COG3119   75 SRASLLTGRYPHRTGVTDNGEGY-------NGGLPPDEPTLAELLKEAGYRTALFGKWH 126
PRK13759 PRK13759
arylsulfatase; Provisional
 46-156 1.83e-22

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 99.74  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGiGD-LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrviqn 124
Cdd:PRK13759   6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGD------ 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 768032438 125 lavpaGLPLN-ETTLAALLKKQGYSTGLIGKWH 156
Cdd:PRK13759  79 -----VVPWNyKNTLPQEFRDAGYYTQCIGKMH 106
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
 46-425 2.38e-175

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: 501.82  E-value: 2.38e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNL 125
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 126 AVPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYYYGMPFTLVDSCWPDPSRNTELAFESQ 205
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 206 LWLCVQLVAIAILTLTFGKLSGWVSvpWLLIFSMILFIFLLGYAWFSSHTSPLYWDCLLMRGHEITEQPMKAERAGSIMV 285
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 286 KEAISFLE------------------------------------------------------------------------ 293
Cdd:cd16159  239 KEAISFLErnkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvgqildaldelglkdntfvyftsdngg 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 294 -------------------------------------------------------------------------RVIDGRD 300
Cdd:cd16159  319 hleeisvggeygggnggiyggkkmggweggirvptivrwpgvippgsvideptslmdifptvaalagaplpsdRIIDGRD 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 301 LMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPKdDSGSVWKAHYVTPVFQpPASGGCYVTSLCRCFGEQVTYHNPPLLFD 380
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPR-DGGAVWKAHYFTPNFY-PGTEGCCGTLLCRCFGDSVTHHDPPLLFD 476

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 768032438 381 LSRDPSESTPLTPATEPlHDFVIKKVANALKEHQETIVPVTYQLS 425
Cdd:cd16159  477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 46-392 5.67e-75

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: 240.54  E-value: 5.67e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNl 125
Cdd:cd16026    1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 126 avpaGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrsDQ-CHHPYNYGFDYYYGMPFTLvDSCWPDPSRNTELAFES 204
Cdd:cd16026   80 ----GLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSN-DMWPFPLYRNDPPGPLP 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 205 QLWLCVQLVA----IAILTLTFGKLSgwvsvpwllifsmILFI-------FLLGYAwfssHTSP---------------- 257
Cdd:cd16026  148 PLMENEEVIEqpadQSSLTQRYTDEA-------------VDFIernkdqpFFLYLA----HTMPhvplfasekfkgrsga 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 258 -LYWDCLlmrgHEI---TEQPMKA-------------------------ERAGS--------------------IM---- 284
Cdd:cd16026  211 gLYGDVV----EELdwsVGRILDAlkelgleentlviftsdngpwleygGHGGSagplrggkgttweggvrvpfIAwwpg 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 285 -------VKEAISFL----------------ERVIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPkddsgsvWK 341
Cdd:cd16026  287 vipagtvSDELASTMdllptlaalagaplpeDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR-------WK 359

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032438 342 AHYVTPVFQPPASGGCYVTSlcrcfgeqvtyHNPPLLFDLSRDPSESTPLT 392
Cdd:cd16026  360 LHLPTTYRTGTDPGGLDPTK-----------LEPPLLYDLEEDPGETYNVA 399
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
 46-412 2.69e-65

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: 216.53  E-value: 2.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVsSGNRRVIQNL 125
Cdd:cd16160    1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY-GGTRVFLPWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 126 AVpaGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYY-YGMPFTLVDSC------WPDPSRNt 198
Cdd:cd16160   80 IG--GLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNSWACddtgrhVDFPDRS- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 199 eLAFesqLWLCVQLVA--IAILTLTFGKLSGWVSV-------PWLLIFSmilfifllgyawFSSHTSPLY----WDCLLM 265
Cdd:cd16160  157 -ACF---LYYNDTIVEqpIQHEHLTETLVGDAKSFiednqenPFFLYFS------------FPQTHTPLFaskrFKGKSK 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 266 RGH-------------EITEQ--------------------------------PMKAERA----GSIMV----------- 285
Cdd:cd16160  221 RGRygdninemswavgEVLDTlvdtgldqntlvfflsdhgphveycleggstgGLKGGKGnsweGGIRVpfiaywpgtik 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 286 ----KEAISFLE----------------RVIDGRDLMPLLQGNVRHSEHEFLFHYCgSYLHAVRwipkddSGSvWKAHYV 345
Cdd:cd16160  301 prvsHEVVSTMDifptfvdlaggtlptdRIYDGLSITDLLLGEADSPHDDILYYCC-SRLMAVR------YGS-YKIHFK 372

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032438 346 TPVFQ------PPASGGCYVTS--LCR-CFGEQVTYHNPPLLFDLSRDPSESTPLTPAtepLHDFVIKKVANALKE 412
Cdd:cd16160  373 TQPLPsqesldPNCDGGGPLSDyiVCYdCEDECVTKHNPPLIFDVEKDPGEQYPLQPS---VYEHMLEAVEKLIAH 445
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
312-446 2.07e-54

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 177.51  E-value: 2.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  312 SEHEFLFHYCGSYLHAVRWIPkddsgsvWKAHYVTPVFQPPASGGCYVTslcrcfGEQVTYHNPPLLFDLSRDPSESTPL 391
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP-------YKAHFFTPSFDPPGAEGCYGS------KVPVTHHDPPLLFDLERDPSEKYPL 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032438  392 TPATePLHDFVIKKVANALKEHQETIVPVTYQLSELNQG-RTWLKPCCGVFPFCLC 446
Cdd:pfam14707  68 SPDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLwDPWLQPCCPTFPACTC 122
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 47-392 4.15e-52

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: 179.65  E-value: 4.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDT---MRTPHIDRLAREGVRLTQHISAASlCSPSRSAFLTGRYPIRSGMVSSGnrrvIQ 123
Cdd:cd16142    1 PNILVILGDDIGWGDLGCYGGGIgrgAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVG----LP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 124 NLavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsRSDQcHHPYNYGFDYYYGMPFTLVDSCWPDPSrnteLAF- 202
Cdd:cd16142   76 GS--PGGLPPWEPTLAELLKDAGYATAQFGKWHLG-----DEDG-RLPTDHGFDEFYGNLYHTIDEEIVDKA----IDFi 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 203 ESQ--------LWLCVQLVAI-AILTLTF-GKLSGWVSVPWLLI-----FSMIL------------FIFLL--------- 246
Cdd:cd16142  144 KRNakadkpffLYVNFTKMHFpTLPSPEFeGKSSGKGKYADSMVelddhVGQILdaldelgiadntIVIFTtdngpeqdv 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 247 ----GYAWFSS--HTS-------PL--YW-----------------DCLlmrgheiteqPMKAERAGSIMVKEAISFLER 294
Cdd:cd16142  224 wpdgGYTPFRGekGTTweggvrvPAivRWpgkikpgrvsneivshlDWF----------PTLAALAGAPDPKDKLLGKDR 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 295 VIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVRWipKDdsgsvWKAHY-VTPVFQPPASGGCYVTSLcrcfgeqvtyh 373
Cdd:cd16142  294 HIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRW--KN-----WKVHFkAQEDTGGPTGEPFYVLTF----------- 355

                        410
                 ....*....|....*....
gi 768032438 374 npPLLFDLSRDPSESTPLT 392
Cdd:cd16142  356 --PLIFNLRRDPKERYDVT 372
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
18-156 4.33e-52

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 180.46  E-value: 4.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  18 MRpRRPLVFMSLVCALLNTCQAhrvhdDKPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSP 97
Cdd:COG3119    1 MK-RLLLLLLALLAAAAAAAAA-----KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSP 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032438  98 SRSAFLTGRYPIRSGMVSSGNRRviqnlavPAGLPLNETTLAALLKKQGYSTGLIGKWH 156
Cdd:COG3119   75 SRASLLTGRYPHRTGVTDNGEGY-------NGGLPPDEPTLAELLKEAGYRTALFGKWH 126
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 47-182 2.36e-51

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: 173.78  E-value: 2.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSsgnrrviqNLA 126
Cdd:cd16022    1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRG--------NVG 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032438 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWH-QGLNCDSRSDQC------------HHPYNygfdyYYGM 182
Cdd:cd16022   73 NGGGLPPDEPTLAELLKEAGYRTALIGKWHdEAIDFIERRDKDkpfflyvsfnapHPPFA-----YYAM 136
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 46-392 1.38e-50

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: 176.12  E-value: 1.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMR-TPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIqn 124
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSV-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 125 lavpAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdsrsdQCHHPYNYGFDYYYGMPFT------------------- 185
Cdd:cd16161   79 ----GGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFShdssladryaqfatdfiqr 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 186 ------------------LVDSCWPDPSRNTEL------AFESQLWLCVQLVAIAILTLTFGKLSGWVSV---PWLLIFS 238
Cdd:cd16161  149 asakdrpfflyaalahvhVPLANLPRFQSPTSGrgpygdALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSdngPWEVKCE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 239 MILFIFLLGY------------AWFSSHTSP--LYWdcllmRGHeITEQPMKAERAGSIMVKEAISFL-------ERVID 297
Cdd:cd16161  229 LAVGPGTGDWqgnlggsvakasTWEGGHREPaiVYW-----PGR-IPANSTSAALVSTLDIFPTVVALagaslppGRIYD 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 298 GRDLMPLLQGNVRhSEHEFLFHYCGSY-----LHAVRWIPkddsgsvWKAHYVTpvfqppasGGCYVTslCRCFGEQVtY 372
Cdd:cd16161  303 GKDLSPVLFGGSK-TGHRCLFHPNSGAagagaLSAVRCGD-------YKAHYAT--------GGALAC--CGSTGPKL-Y 363

                        410       420
                 ....*....|....*....|
gi 768032438 373 HNPPLLFDLSRDPSESTPLT 392
Cdd:cd16161  364 HDPPLLFDLEVDPAESFPLT 383
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 47-181 1.67e-50

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: 176.97  E-value: 1.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM--VSSGNRRVIQN 124
Cdd:cd16144    1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032438 125 LAVPA-----GLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqcHHPYNYGFDYYYG 181
Cdd:cd16144   81 TKLIPppsttRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGG------YGPEDQGFDVNIG 136
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
 46-446 1.35e-49

Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.


Pssm-ID: 293777 [Multi-domain]  Cd Length: 479  Bit Score: 176.10  E-value: 1.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMV-------SSGn 118
Cdd:cd16158    1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpgvfypgSRG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 119 rrviqnlavpaGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdsrSDQCHHPYNYGFDYYYGMPFT------LVDSC-W 191
Cdd:cd16158   80 -----------GLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPYShdqgpcQNLTCfP 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 192 PD--------------PSRNTELAFESQLWLCVQLVAIAILTLTFGKLSGWVSVPWLLIF-------------------- 237
Cdd:cd16158  145 PNipcfggcdqgevpcPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYashhthypqfagqkfagrss 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 238 ------SMILFIFLLG---------------YAWFSSHTSP-------------------------------LYWDCLLM 265
Cdd:cd16158  225 rgpfgdALAELDGSVGellqtlkengidnntLVFFTSDNGPstmrksrggnagllkcgkgttyeggvrepaiAYWPGRIK 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 266 RG--HEITEQ----PMKAERAGSIMVkeaisflERVIDGRDLMPLLQGNVRHSEHEFLFHYCGSY----LHAVRWipkdd 335
Cdd:cd16158  305 PGvtHELASTldilPTIAKLAGAPLP-------NVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDpdkgVFAVRW----- 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 336 sgSVWKAHYVT---PVFQPPASGGCYVTSLcrcfgeqVTYHNPPLLFDLSRDPSESTPLTPATEplHDFVIKKVaNALKE 412
Cdd:cd16158  373 --GKYKAHFYTqgaAHSGTTPDKDCHPSAE-------LTSHDPPLLFDLSQDPSENYNLLGLPE--YNQVLKQI-QQVKE 440

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 768032438 413 HQETivPVTYQLSELNQGR-TWLKPCC--GVFPF---CLC 446
Cdd:cd16158  441 RFEA--SMKFGESEINKGEdPALEPCCkpGCTPKpscCQC 478
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
 47-203 3.36e-48

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: 170.04  E-value: 3.36e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASlCSPSRSAFLTGRYPIRSGMvssgNRRVIQNlA 126
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVILA-G 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrsdQCHHPY---NYGFDYYYGM-----------PFTLVDSCWP 192
Cdd:cd16029   75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWEYtptNRGFDSFYGYyggaedyythtSGGANDYGND 146

                        170
                 ....*....|.
gi 768032438 193 DPSRNTELAFE 203
Cdd:cd16029  147 DLRDNEEPAWD 157
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 47-181 4.09e-48

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: 170.47  E-value: 4.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYpirsgmvsSGNRRVIQNLA 126
Cdd:cd16145    1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLH--------TGHTRVRGNSE 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768032438 127 VPAGLPL--NETTLAALLKKQGYSTGLIGKWhqGLNCDSRSDqchHPYNYGFDYYYG 181
Cdd:cd16145   73 PGGQDPLppDDVTLAEVLKKAGYATAAFGKW--GLGGPGTPG---HPTKQGFDYFYG 124
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 47-183 9.67e-48

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: 168.92  E-value: 9.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDT-MRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM---VSSGNRrvi 122
Cdd:cd16143    1 PNIVIILADDLGYGDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkggVLGGFS--- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032438 123 qnlavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHH----------------PYNYGFDYYYGMP 183
Cdd:cd16143   78 -----PPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP 149
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 47-181 9.41e-43

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: 155.79  E-value: 9.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQ-HISaaSLCSPSRSAFLTGRYPIRSGMVSSGNRRVIqnl 125
Cdd:cd16146    1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032438 126 avpagLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqcHHPYNYGFDYYYG 181
Cdd:cd16146   76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLG 120
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 46-182 4.70e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 153.49  E-value: 4.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrviqnl 125
Cdd:cd16034    1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------ 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032438 126 avpagLPLNETTLAALLKKQGYSTGLIGKWH----QGLNCDSRSDQCHHPYNYGFDYYYGM 182
Cdd:cd16034   75 -----LPPDAPTIADVLKDAGYRTGYIGKWHldgpERNDGRADDYTPPPERRHGFDYWKGY 130
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 46-424 4.72e-40

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: 149.54  E-value: 4.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSG----NRRV 121
Cdd:cd16157    1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNaharNAYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 122 IQNLAvpAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrSDQCHHPYNYGFDYYYGMPftlvdSCWPDPSRNTEL- 200
Cdd:cd16157   81 PQNIV--GGIPDSEILLPELLKKAGYRNKIVGKWHLG------HRPQYHPLKHGFDEWFGAP-----NCHFGPYDNKAYp 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 201 ---AFESQLWLCVQLVAIAIltltfGKLSGWVSVPWLLIFSMILFI---------FLLGYAWFSSHT----SP------- 257
Cdd:cd16157  148 nipVYRDWEMIGRYYEEFKI-----DKKTGESNLTQIYLQEALEFIekqhdaqkpFFLYWAPDATHApvyaSKpflgtsq 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 258 --LYWDCLL----------------------------------------------------------MRGHEITEQPMKA 277
Cdd:cd16157  223 rgLYGDAVMeldssvgkileslkslgienntfvffssdngaalisapeqggsngpflcgkqttfeggMREPAIAWWPGHI 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 278 E------RAGSIM--VKEAISFLE------RVIDGRDLMPLLQGNvrHSEHEFLFHYCGSYLHAVRWipkddsgSVWKAH 343
Cdd:cd16157  303 KpgqvshQLGSLMdlFTTSLALAGlpipsdRAIDGIDLLPVLLNG--KEKDRPIFYYRGDELMAVRL-------GQYKAH 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 344 YVTpvFQPPASGGCYVTSLCRcfGEQ---VTYHN------PPLLFDLSRDPSESTPLTPATePLHDFVIKKVANALKEHQ 414
Cdd:cd16157  374 FWT--WSNSWEEFRKGINFCP--GQNvpgVTTHNqtdhtkLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQ 448

                        490
                 ....*....|
gi 768032438 415 ETIVPVTYQL 424
Cdd:cd16157  449 KTLVPGEPQL 458
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 47-196 4.52e-38

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: 142.26  E-value: 4.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIgDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvsSGNRRVIQNLa 126
Cdd:cd16027    1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA--HGLRSRGFPL- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438 127 vPAGLPlnetTLAALLKKQGYSTGLIGKWHQGlncdsrsdqchHPYNYGFDYYYGMPFTLVDSCWPDPSR 196
Cdd:cd16027   77 -PDGVK----TLPELLREAGYYTGLIGKTHYN-----------PDAVFPFDDEMRGPDDGGRNAWDYASN 130
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
 45-158 2.06e-37

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: 141.04  E-value: 2.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  45 DKPNIVLIMVDDLGIGDLGCYGNDtMRTPHIDRLAREGVRLTQ-HisAASLCSPSRSAFLTGRYPIRSGMvssGNrrvIQ 123
Cdd:cd16025    1 GRPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM---GT---MA 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 768032438 124 NLAVPAG-----LPLNETTLAALLKKQGYSTGLIGKWHQG 158
Cdd:cd16025   72 ELATGKPgyegyLPDSAATIAEVLKDAGYHTYMSGKWHLG 111
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 45-183 6.11e-37

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: 140.36  E-value: 6.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  45 DKPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGnrrviqn 124
Cdd:cd16031    1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNN------- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032438 125 lavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDqchhpynyGFDYYYGMP 183
Cdd:cd16031   74 ---GPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFP 121
Sulfatase pfam00884
Sulfatase;
47-181 1.77e-35

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 133.32  E-value: 1.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438   47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrviqnla 126
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS---------- 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768032438  127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdSRSDqchhPYNYGFDYYYG 181
Cdd:pfam00884  71 TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWY--NNQS----PCNLGFDKFFG 119
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-180 7.97e-34

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 130.80  E-value: 7.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTqHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrviqnlA 126
Cdd:cd16151    1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY-------------V 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032438 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSdqchHPYNYGFDYYY 180
Cdd:cd16151   67 VFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYC 116
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-158 1.34e-30

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 118.88  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM---VSSGNrrvIQ 123
Cdd:cd16149    1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwIVEGS---HG 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 768032438 124 NLAVPAGLPLNETTLAALLKKQGYSTGLIGKWHQG 158
Cdd:cd16149   78 KTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG 112
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-179 1.27e-29

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 119.63  E-value: 1.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrviqNLA 126
Cdd:cd16033    1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVEN----AGA 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032438 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqchhPYNYGFDYY 179
Cdd:cd16033   77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEET--------PLDYGFDEY 121
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 45-158 5.93e-27

iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.


Pssm-ID: 293754 [Multi-domain]  Cd Length: 435  Bit Score: 112.28  E-value: 5.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  45 DKPNIVLIMVDDLGiGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVIQN 124
Cdd:cd16030    1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTG--------VYDN 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 768032438 125 LAVPAGLPLNETTLAALLKKQGYSTGLIGK-WHQG 158
Cdd:cd16030   72 NSYFRKVAPDAVTLPQYFKENGYTTAGVGKiFHPG 106
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 46-156 1.49e-25

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 107.31  E-value: 1.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVIQNl 125
Cdd:cd16152    1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG--------CFRN- 71

                         90       100       110
                 ....*....|....*....|....*....|.
gi 768032438 126 AVPagLPLNETTLAALLKKQGYSTGLIGKWH 156
Cdd:cd16152   72 GIP--LPADEKTLAHYFRDAGYETGYVGKWH 100
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 47-184 3.58e-25

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: 107.34  E-value: 3.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIrsgmvssgNRRVIQNlA 126
Cdd:cd16028    1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSVWN-G 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032438 127 VPagLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQchHPYN-------YGFDYYYGMPF 184
Cdd:cd16028   72 TP--LDARHLTLALELRKAGYDPALFGYTDTSPDPRGLAPL--DPRLlsyelamPGFDPVDRLDE 132
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-180 7.04e-25

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 103.40  E-value: 7.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLgIGD-LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrviqnl 125
Cdd:cd16148    1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG------------- 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032438 126 AVPAGLPLNETTLAALLKKQGYSTGLIgkwhqglncdsrSDQCHHPYNYGFDYYY 180
Cdd:cd16148   67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDRGF 109
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-181 1.78e-24

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 104.35  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCY--GNDTMRTPHIDRLAREGVRLTqHISAASLCSPSRSAFLTGRYPIRSGMvssgnrrviqn 124
Cdd:cd16154    1 PNILLIIADDQGLDSSAQYslSSDLPVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV----------- 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032438 125 LAVPAGLPLNETTLAALLKKQ----GYSTGLIGKWHQGlNCDSrsdqchHPYNYG-FDYYYG 181
Cdd:cd16154   69 LAVPDELLLSEETLLQLLIKDattaGYSSAVIGKWHLG-GNDN------SPNNPGgIPYYAG 123
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 47-178 5.61e-23

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: 99.19  E-value: 5.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvssgnrrvIQNLA 126
Cdd:cd16032    1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA--------YDNAA 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032438 127 -VPAGLPlnetTLAALLKKQGYSTGLIGKWH-QGlncdsrSDQCHhpynyGFDY 178
Cdd:cd16032   73 eFPADIP----TFAHYLRAAGYRTALSGKMHfVG------PDQLH-----GFDY 111
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 46-158 6.61e-23

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 99.56  E-value: 6.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQ-HI----SAAsLCSPSRSAFLTGRYPIRSGMvssgnrr 120
Cdd:cd16155    2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------- 73

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 768032438 121 viqnlAVPAGLPLNETTLAALLKKQGYSTGLIGKWHQG 158
Cdd:cd16155   74 -----GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNG 106
PRK13759 PRK13759
arylsulfatase; Provisional
 46-156 1.83e-22

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 99.74  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGiGD-LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrviqn 124
Cdd:PRK13759   6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGD------ 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 768032438 125 lavpaGLPLN-ETTLAALLKKQGYSTGLIGKWH 156
Cdd:PRK13759  79 -----VVPWNyKNTLPQEFRDAGYYTQCIGKMH 106
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 46-156 2.87e-22

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 96.29  E-value: 2.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGN----------DTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVs 115
Cdd:cd16153    1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 768032438 116 sGNRRVIQNLavPAGLPlnetTLAALLKKQGYSTGLIGKWH 156
Cdd:cd16153   80 -GFEAAHPAL--DHGLP----TFPEVLKKAGYQTASFGKSH 113
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 47-156 4.27e-22

uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 98.61  E-value: 4.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrviqNLA 126
Cdd:cd16156    1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN-------CMA 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 768032438 127 vpagLPLNETTLAALLKKQGYSTGLIGKWH 156
Cdd:cd16156   74 ----LGDNVKTIGQRLSDNGIHTAYIGKWH 99
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 46-182 6.04e-22

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: 97.24  E-value: 6.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLgigDLGCYGNDTMRtPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPirsgmvssGNRRVIQNL 125
Cdd:cd16147    1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYA--------HNHGVTNNS 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032438 126 AVPAGLP------LNETTLAALLKKQGYSTGLIGKWhqgLN-CDSRSDQCHHPynYGFDYYYGM 182
Cdd:cd16147   69 PPGGGYPkfwqngLERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVP--PGWDEWDGL 127
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-178 5.29e-21

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 93.38  E-value: 5.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrvIQNLA 126
Cdd:cd16037    1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETG---------VWDNA 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032438 127 VPagLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsRSDQCHhpynyGFDY 178
Cdd:cd16037   72 DP--YDGDVPSWGHALRAAGYETVLIGKLHFR-----GEDQRH-----GFRY 111
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-154 5.61e-21

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 94.61  E-value: 5.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnRRVIQNLa 126
Cdd:cd16150    1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG------HRTLHHL- 73

                         90       100
                 ....*....|....*....|....*...
gi 768032438 127 vpagLPLNETTLAALLKKQGYSTGLIGK 154
Cdd:cd16150   74 ----LRPDEPNLLKTLKDAGYHVAWAGK 97
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-156 5.86e-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: 87.26  E-value: 5.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDD--------LGIGDLGCygndtmrtPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvssgn 118
Cdd:cd16035    1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGV----- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 768032438 119 rrvIQNLAVPAGLPLNET--TLAALLKKQGYSTGLIGKWH 156
Cdd:cd16035   68 ---TDTLGSPMQPLLSPDvpTLGHMLRAAGYYTAYKGKWH 104
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 47-153 1.04e-18

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: 85.16  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRL-TQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNl 125
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELP- 79

                         90       100
                 ....*....|....*....|....*...
gi 768032438 126 AVPAGLPLNETTLAALLKKQGYSTGLIG 153
Cdd:cd00016   80 SRAAGKDEDGPTIPELLKQAGYRTGVIG 107
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 18-185 7.73e-10

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 60.53  E-value: 7.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  18 MRPRRPLVFMSLVCALLNTCQAHRvhddkpNIVLIMVDDLGIGDLgcygnDTMRTPHIDRLAREGVRLTQHISAA-SLCS 96
Cdd:COG1524    1 MKRGLSLLLASLLAAAAAAAPPAK------KVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  97 PSRSAFLTGRYPIRSGMVSSG-----NRRVIQNLAVPAGLP-----LNETTLAALLKKQGYSTGLIGKWHQGlncDSRSD 166
Cdd:COG1524   70 PAHTTLLTGLYPGEHGIVGNGwydpeLGRVVNSLSWVEDGFgsnslLPVPTIFERARAAGLTTAAVFWPSFE---GSGLI 146

                        170       180
                 ....*....|....*....|
gi 768032438 167 QCHHPYNY-GFDYYYGMPFT 185
Cdd:COG1524  147 DAARPYPYdGRKPLLGNPAA 166
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 46-182 1.39e-07

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 53.89  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSG--MVSSGNRRViq 123
Cdd:COG1368  234 KPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGspYKRPGQNNF-- 311

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032438 124 nlavpaglplneTTLAALLKKQGYSTgligkwhqglncdsrsdQCHHPYNY------------GFDYYYGM 182
Cdd:COG1368  312 ------------PSLPSILKKQGYET-----------------SFFHGGDGsfwnrdsfyknlGFDEFYDR 353
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
 47-154 9.69e-06

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: 47.54  E-value: 9.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDDLGiGDLGCY-GNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPirsgmvssgnrRVIQNL 125
Cdd:cd16171    1 PNVVMVMSDSFD-GRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESW 68

                         90       100
                 ....*....|....*....|....*....
gi 768032438 126 AVPAGLPLNETTLAALLKKQGYSTGLIGK 154
Cdd:cd16171   69 NNYKGLDPNYPTWMDRLEKHGYHTQKYGK 97
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 47-182 1.39e-05

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: 46.52  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032438  47 PNIVLIMVDdlGIGD--LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRS--AFLTGRYPIRSGMVSsgNRRVI 122
Cdd:cd16015    1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGS--YTLYK 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032438 123 QNLAvpaglplneTTLAALLKKQGYSTGLIgkwhqglncdsrsdqchHPY------------NYGFDYYYGM 182
Cdd:cd16015   77 LNPL---------PSLPSILKEQGYETIFI-----------------HGGdasfynrdsvypNLGFDEFYDL 122
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 50-115 6.08e-05

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: 45.10  E-value: 6.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032438   50 VLIMVDDLGIGDLgcygNDTMRTPHIDRLAREGVRLTQHISAA-SLCSPSRSAFLTGRYPIRSGMVS 115
Cdd:pfam01663   2 LVISLDGFRADYL----DRFELTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVG 64
 
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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