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Conserved domains on  [gi|767995604|ref|XP_011523428|]
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N-sulphoglucosamine sulphohydrolase isoform X1 [Homo sapiens]

Protein Classification

sulfatase( domain architecture ID 10888093)

sulfatase catalyzes the hydrolysis of sulfate ester bonds of a wide variety of substrates, similar to N-sulphoglucosamine sulphohydrolase that catalyzes the cleavage of N-linked sulfate groups from the glycosaminoglycans heparin sulfate and heparin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
24-316 5.65e-116

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: 340.25  E-value: 5.65e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16027    2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRS--RGFPLPDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 104 VRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENgsvlQVGRNITRIKLLVRKFLQTQD-DRPFFLYVAFHDPHR 182
Cdd:cd16027   80 VKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPD----DGGRNAWDYASNAADFLNRAKkGQPFFLWFGFHDPHR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 183 CGHSQPQYGTFcekfgngesgmgripdwtpqaYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGV 262
Cdd:cd16027  156 PYPPGDGEEPG---------------------YDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELEEDGL 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767995604 263 LNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16027  215 LDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPGKIKP-GSVSDALVSFI 267
 
Name Accession Description Interval E-value
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
24-316 5.65e-116

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: 340.25  E-value: 5.65e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16027    2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRS--RGFPLPDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 104 VRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENgsvlQVGRNITRIKLLVRKFLQTQD-DRPFFLYVAFHDPHR 182
Cdd:cd16027   80 VKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPD----DGGRNAWDYASNAADFLNRAKkGQPFFLWFGFHDPHR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 183 CGHSQPQYGTFcekfgngesgmgripdwtpqaYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGV 262
Cdd:cd16027  156 PYPPGDGEEPG---------------------YDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELEEDGL 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767995604 263 LNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16027  215 LDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPGKIKP-GSVSDALVSFI 267
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
21-316 2.88e-61

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 200.49  E-value: 2.88e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFN 99
Cdd:COG3119   23 RP-NILFILADDlGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 SFDKVrSLPLLLSQAGVRTGIIGKKHvgpetVYpFDFAYTEEngsvlqvgrnitrikllVRKFLQTQ--DDRPFFLYVAF 177
Cdd:COG3119  102 PPDEP-TLAELLKEAGYRTALFGKWH-----LY-LTDLLTDK-----------------AIDFLERQadKDKPFFLYLAF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 178 HDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYDPLDVLVP-YFVP---NTPAARADLAAQYTTVGRMDQGVGLV 253
Cdd:COG3119  158 NAPHAPYQAPEEY---------------------LDKYDGKDIPLPpNLAPrdlTEEELRRARAAYAAMIEEVDDQVGRL 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767995604 254 LQELRDAGVLNDTLVIFTSDNGIPFPS-----GRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:COG3119  217 LDALEELGLADNTIVVFTSDNGPSLGEhglrgGKGTLYEGGIRVPLIVRWPGKIKA-GSVSDALVSLI 283
Sulfatase pfam00884
Sulfatase;
23-314 3.17e-50

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 169.14  E-value: 3.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604   23 RNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhfNSF 101
Cdd:pfam00884   1 PNVVLVLGESLRAPDlGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV----GLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  102 DKVRSLPLLLSQAGVRTGIIGKKHVGP-----ETVYPFDFAYTEENGSVLQVGRNITRI---------KLLVRKFLQ--T 165
Cdd:pfam00884  77 RTEPSLPDLLKRAGYNTGAIGKWHLGWynnqsPCNLGFDKFFGRNTGSDLYADPPDVPYncsgggvsdEALLDEALEflD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  166 QDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYdpldvlvPYFVPNTPAARADLAAQYTTVGR 245
Cdd:pfam00884 157 NNDKPFFLVLHTLGSHGPPYYPDRY---------------------PEKY-------ATFKPSSCSEEQLLNSYDNTLLY 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995604  246 MDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPF--------PSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVS 314
Cdd:pfam00884 209 TDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLgegggylhGGKYDNAPEGGYRVPLLIWSPGGKAK-GQKSEALVS 284
PRK13759 PRK13759
arylsulfatase; Provisional
21-275 2.31e-27

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 111.68  E-value: 2.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlHQDVhhfN 99
Cdd:PRK13759   6 KP-NIILIMVDQMRGDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG-YGDV---V 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 SFDKVRSLPLLLSQAGVRTGIIGKKHVGPETV--------------------YPFDFAYTEENGSVLQ---VGRNITRIK 156
Cdd:PRK13759  81 PWNYKNTLPQEFRDAGYYTQCIGKMHVFPQRNllgfhnvllhdgylhsgrneDKSQFDFVSDYLAWLRekaPGKDPDLTD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 157 LLVR--------------------------KFLQTQD-DRPFFLYVAFHDPHRcGHSQPQYgtFCEKFGNGESGMGRIPD 209
Cdd:PRK13759 161 IGWDcnswvarpwdleerlhptnwvgsesiEFLRRRDpTKPFFLKMSFARPHS-PYDPPKR--YFDMYKDADIPDPHIGD 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995604 210 WT------PQAYDPlDVLVPYFvPNTPAARAdLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:PRK13759 238 WEyaedqdPEGGSI-DALRGNL-GEEYARRA-RAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG 306
 
Name Accession Description Interval E-value
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
24-316 5.65e-116

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: 340.25  E-value: 5.65e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16027    2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRS--RGFPLPDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 104 VRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENgsvlQVGRNITRIKLLVRKFLQTQD-DRPFFLYVAFHDPHR 182
Cdd:cd16027   80 VKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPD----DGGRNAWDYASNAADFLNRAKkGQPFFLWFGFHDPHR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 183 CGHSQPQYGTFcekfgngesgmgripdwtpqaYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGV 262
Cdd:cd16027  156 PYPPGDGEEPG---------------------YDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELEEDGL 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767995604 263 LNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16027  215 LDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPGKIKP-GSVSDALVSFI 267
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
21-316 2.88e-61

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 200.49  E-value: 2.88e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFN 99
Cdd:COG3119   23 RP-NILFILADDlGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 SFDKVrSLPLLLSQAGVRTGIIGKKHvgpetVYpFDFAYTEEngsvlqvgrnitrikllVRKFLQTQ--DDRPFFLYVAF 177
Cdd:COG3119  102 PPDEP-TLAELLKEAGYRTALFGKWH-----LY-LTDLLTDK-----------------AIDFLERQadKDKPFFLYLAF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 178 HDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYDPLDVLVP-YFVP---NTPAARADLAAQYTTVGRMDQGVGLV 253
Cdd:COG3119  158 NAPHAPYQAPEEY---------------------LDKYDGKDIPLPpNLAPrdlTEEELRRARAAYAAMIEEVDDQVGRL 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767995604 254 LQELRDAGVLNDTLVIFTSDNGIPFPS-----GRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:COG3119  217 LDALEELGLADNTIVVFTSDNGPSLGEhglrgGKGTLYEGGIRVPLIVRWPGKIKA-GSVSDALVSLI 283
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
24-316 1.34e-56

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: 183.41  E-value: 1.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNsfD 102
Cdd:cd16022    2 NILLIMTDDLGYDDlGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLP--P 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 103 KVRSLPLLLSQAGVRTGIIGKKHvgpetvypfDFAyteengsvlqvgrnitrikllvRKFLQTQD-DRPFFLYVAFHDPH 181
Cdd:cd16022   80 DEPTLAELLKEAGYRTALIGKWH---------DEA----------------------IDFIERRDkDKPFFLYVSFNAPH 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 182 rcghsqpqygtfcekfgngesgmgripdwTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVLQELRDAG 261
Cdd:cd16022  129 -----------------------------PPFAY------------------------YAMVSAIDDQIGRILDALEELG 155
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 262 VLNDTLVIFTSDNGIPFPSGR-----TNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16022  156 LLDNTLIVFTSDHGDMLGDHGlrgkkGSLYEGGIRVPFIVRWPGKIPA-GQVSDALVSLL 214
Sulfatase pfam00884
Sulfatase;
23-314 3.17e-50

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 169.14  E-value: 3.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604   23 RNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhfNSF 101
Cdd:pfam00884   1 PNVVLVLGESLRAPDlGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV----GLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  102 DKVRSLPLLLSQAGVRTGIIGKKHVGP-----ETVYPFDFAYTEENGSVLQVGRNITRI---------KLLVRKFLQ--T 165
Cdd:pfam00884  77 RTEPSLPDLLKRAGYNTGAIGKWHLGWynnqsPCNLGFDKFFGRNTGSDLYADPPDVPYncsgggvsdEALLDEALEflD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  166 QDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYdpldvlvPYFVPNTPAARADLAAQYTTVGR 245
Cdd:pfam00884 157 NNDKPFFLVLHTLGSHGPPYYPDRY---------------------PEKY-------ATFKPSSCSEEQLLNSYDNTLLY 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995604  246 MDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPF--------PSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVS 314
Cdd:pfam00884 209 TDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLgegggylhGGKYDNAPEGGYRVPLLIWSPGGKAK-GQKSEALVS 284
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
21-313 1.60e-48

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: 168.09  E-value: 1.60e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPRNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVhhFN 99
Cdd:cd16031    1 KRPNIIFILTDDHRYDAlGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPL--FD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 SFDKvrSLPLLLSQAGVRTGIIGKKHVGPETVYP---FDF------------AYTEENGSVLQVGRNITRIKL-LVRKFL 163
Cdd:cd16031   79 ASQP--TYPKLLRKAGYQTAFIGKWHLGSGGDLPppgFDYwvsfpgqgsyydPEFIENGKRVGQKGYVTDIITdKALDFL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 164 QTQD-DRPFFLYVAFHDPHRCGHSQPQYGtfcEKFGNGEsgMGRIPDWTPQAYDPLdvlvPYFVPNTPAARADLA----- 237
Cdd:cd16031  157 KERDkDKPFCLSLSFKAPHRPFTPAPRHR---GLYEDVT--IPEPETFDDDDYAGR----PEWAREQRNRIRGVLdgrfd 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 238 ----------AQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipFPSG-------RTnLYWPGTAEPLLVSSPE 300
Cdd:cd16031  228 tpekyqrymkDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG--FFLGehglfdkRL-MYEESIRVPLIIRDPR 304
                        330
                 ....*....|...
gi 767995604 301 HPKRwGQVSEAYV 313
Cdd:cd16031  305 LIKA-GTVVDALV 316
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
21-315 3.29e-47

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: 164.15  E-value: 3.29e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADDGGF-ESGAYNnSAIATPHLDALARRSLLFRNaFTSVSSCSPSRASLLTGLPQHQNG---MYGLHQDVH 96
Cdd:cd16025    2 RP-NILLILADDLGFsDLGCFG-GEIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHHQVGmgtMAELATGKP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  97 HFNSF--DKVRSLPLLLSQAGVRTGIIGKKHVGPETVYpFDFAYTEengsvlqvgrnitriKLLvrKFLQTQ--DDRPFF 172
Cdd:cd16025   79 GYEGYlpDSAATIAEVLKDAGYHTYMSGKWHLGPDDYY-STDDLTD---------------KAI--EYIDEQkaPDKPFF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 173 LYVAF---HDPHrcgHSQPQY-----GTFcekfgngESG--------------MGRIPDWTPQAYDPLDvlvpyfVPN-- 228
Cdd:cd16025  141 LYLAFgapHAPL---QAPKEWidkykGKY-------DAGwdalreerlerqkeLGLIPADTKLTPRPPG------VPAwd 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 229 --TPAARADL-------AAQyttVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IPFPSGRTNLYW 287
Cdd:cd16025  205 slSPEEKKLEarrmevyAAM---VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaepgwanasnTPFRLYKQASHE 281
                        330       340
                 ....*....|....*....|....*...
gi 767995604 288 PGTAEPLLVSSPEHPKRWGQVSEAYVSL 315
Cdd:cd16025  282 GGIRTPLIVSWPKGIKAKGGIRHQFAHV 309
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-316 9.51e-45

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: 156.96  E-value: 9.51e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAF----TSVSSCSPSRASLLTglpqhqnGMYGLH-QD 94
Cdd:cd16155    2 KP-NILFILADDQRADTiGALGNPEIQTPNLDRLARRGTSFTNAYnmggWSGAVCVPSRAMLMT-------GRTLFHaPE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  95 VHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVgpetvypfDFAyteeNGSVlqvgrnitrikllvrKFL--QTQDDRPFF 172
Cdd:cd16155   74 GGKAAIPSDDKTWPETFKKAGYRTFATGKWHN--------GFA----DAAI---------------EFLeeYKDGDKPFF 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 173 LYVAFHDPHrcghsQPQYGT--FCEKFGNGEsgmgrIPDwtPQAYDPL------------DVLVPYfvPNTPAA-RADLA 237
Cdd:cd16155  127 MYVAFTAPH-----DPRQAPpeYLDMYPPET-----IPL--PENFLPQhpfdngegtvrdEQLAPF--PRTPEAvRQHLA 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 238 AQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYV 313
Cdd:cd16155  193 EYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGShglmGKQNLYEHSMRVPLIISGPGIPK--GKRRDALV 270

                 ...
gi 767995604 314 SLL 316
Cdd:cd16155  271 YLQ 273
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
24-310 2.00e-38

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: 141.19  E-value: 2.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:cd16145    2 NIIFILADDlGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLPP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 103 KVRSLPLLLSQAGVRTGIIGKKHVGPETV--YP----FDF---------------AYTEENG------SVLQVGRNITRI 155
Cdd:cd16145   82 DDVTLAEVLKKAGYATAAFGKWGLGGPGTpgHPtkqgFDYfygyldqvhahnyypEYLWRNGekvplpNNVIPPLDEGNN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 156 KLLVR-------------KFLQTQDDRPFFLYVAFHDPHrcGHSQpqygtfcekfgngesgmgrIPDWTPQAYDPLDvLV 222
Cdd:cd16145  162 AGGGGgtyshdlftdealDFIRENKDKPFFLYLAYTLPH--APLQ-------------------VPDDGPYKYKPKD-PG 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 223 PYFVPNTPAARADLAAQyttVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI-----------------PFPSGRTNL 285
Cdd:cd16145  220 IYAYLPWPQPEKAYAAM---VTRLDRDVGRILALLKELGIDENTLVVFTSDNGPhseggsehdpdffdsngPLRGYKRSL 296
                        330       340
                 ....*....|....*....|....*
gi 767995604 286 YWPGTAEPLLVSSPEHPKRwGQVSE 310
Cdd:cd16145  297 YEGGIRVPFIARWPGKIPA-GSVSD 320
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
22-275 4.49e-38

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: 139.62  E-value: 4.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  22 PRNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTG-LPQ---------HQNGMYG 90
Cdd:cd16026    1 KPNIVVILADDLGYGDlGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGrYPVrvglpgvvgPPGSKGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  91 LHQDVHhfnsfdkvrSLPLLLSQAGVRTGIIGKKHVG--PETvYP----FDFAY---------------TEENGSVLQVG 149
Cdd:cd16026   81 LPPDEI---------TIAEVLKKAGYRTALVGKWHLGhqPEF-LPtrhgFDEYFgipysndmwpfplyrNDPPGPLPPLM 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 150 RNITRI----------KLLVRK---FLQTQDDRPFFLYVAFHDPHrcghsQPQYGTfcEKFgNGESGMGRIPDwtpqayd 216
Cdd:cd16026  151 ENEEVIeqpadqssltQRYTDEavdFIERNKDQPFFLYLAHTMPH-----VPLFAS--EKF-KGRSGAGLYGD------- 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767995604 217 pldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16026  216 -------------------------VVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
24-314 1.03e-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: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 139.22  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGL--PQHQNGMYGLHQDVHHFNS 100
Cdd:cd16144    2 NIVLILVDDlGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQypARLGITDVIPGRRGPPDNT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 101 F-----------DKVRSLPLLLSQAGVRTGIIGKKHVGPE-TVYP----FD---------------FAYTEENGSVLQVG 149
Cdd:cd16144   82 KlipppsttrlpLEEVTIAEALKDAGYATAHFGKWHLGGEgGYGPedqgFDvniggtgnggppsyyFPPGKPNPDLEDGP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 150 RNITRIKLLVR---KFLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQaydpldvlvpyfv 226
Cdd:cd16144  162 EGEYLTDRLTDeaiDFIEQNKDKPFFLYLSHYAVH-----------------------------TPI------------- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 227 pntpAARADLAAQYTTVGR-----------------MDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IP 277
Cdd:cd16144  200 ----QARPELIEKYEKKKKglrkgqknpvyaamiesLDESVGRILDALEELGLADNTLVIFTSDNGglstrggpptsnAP 275
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 767995604 278 FPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVS 314
Cdd:cd16144  276 LRGGKGSLYEGGIRVPLIVRWPGVIKP-GSVSDVPVI 311
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-316 2.99e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 127.66  E-value: 2.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  23 RNALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNS- 100
Cdd:cd16037    1 PNILIIMSDEhNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWD--------NAd 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 101 --FDKVRSLPLLLSQAGVRTGIIGKKHVGPETVYPFdFAYTeengsvlqvgRNITRiklLVRKFLQTQ--DDRPFFLYVA 176
Cdd:cd16037   73 pyDGDVPSWGHALRAAGYETVLIGKLHFRGEDQRHG-FRYD----------RDVTE---AAVDWLREEaaDDKPWFLFVG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 177 FHDPHrcghsqpqygtFcekfgngesgmgriPDWTPQA-YDpldvlvpYFVpntpaaRADLAAQYTTVGRMDQGVGLVLQ 255
Cdd:cd16037  139 FVAPH-----------F--------------PLIAPQEfYD-------LYV------RRARAAYYGLVEFLDENIGRVLD 180
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767995604 256 ELRDAGVLNDTLVIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLL 316
Cdd:cd16037  181 ALEELGLLDNTLIIYTSDHGDMLGErglwGKSTMYEESVRVPMIISGPGIPA--GKRVKTPVSLV 243
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
24-289 5.80e-34

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: 128.82  E-value: 5.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSfd 102
Cdd:cd16146    2 NVILILTDDQGYgDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWHTILGRERMRL-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 103 KVRSLPLLLSQAGVRTGIIGKKHVGpeTVYP-------FDFAYTEENGSVLQVG-------------RNITRIK------ 156
Cdd:cd16146   79 DETTLAEVFKDAGYRTGIFGKWHLG--DNYPyrpqdrgFDEVLGHGGGGIGQYPdywgndyfddtyyHNGKFVKtegyct 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 157 -LLVR---KFLQTQDDRPFFLYVAFHDPHRcghsqpqygtfcekfgngesgmgripdwtpqaydpldvlvPYFVPNTPAA 232
Cdd:cd16146  157 dVFFDeaiDFIEENKDKPFFAYLATNAPHG----------------------------------------PLQVPDKYLD 196
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995604 233 R-------ADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipfPSGRTNLYWPG 289
Cdd:cd16146  197 PykdmgldDKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG---PAGGVPKRFNA 257
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
24-317 7.44e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 125.80  E-value: 7.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhQDVHHFNSF- 101
Cdd:cd16033    2 NILFIMTDQQRYDTlGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVL---NNVENAGAYs 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 102 ----DKVRSLPLLLSQAGVRTGIIGKKHVGPETVyPFDFAYtEENGSVLQ------VGRNITRIkllvRKFLqtQDDRPF 171
Cdd:cd16033   79 rglpPGVETFSEDLREAGYRNGYVGKWHVGPEET-PLDYGF-DEYLPVETtieyflADRAIEML----EELA--ADDKPF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 172 FLYVAFHDPHrcghsQPqYgtfcekfgngesgmgRIPDWTPQAYDPLDVLVP--YFVP--NTPAA--------------- 232
Cdd:cd16033  151 FLRVNFWGPH-----DP-Y---------------IPPEPYLDMYDPEDIPLPesFADDfeDKPYIyrrerkrwgvdtede 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 233 ---RADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG---------------------IPFPSGrtnlyWP 288
Cdd:cd16033  210 edwKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGdalgahrlwdkgpfmyeetyrIPLIIK-----WP 284
                        330       340
                 ....*....|....*....|....*....
gi 767995604 289 GTAEPllvsspehpkrwGQVSEAYVSLLE 317
Cdd:cd16033  285 GVIAA------------GQVVDEFVSLLD 301
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
24-275 1.37e-32

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: 125.01  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGF-ESGAYN-NSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTG-------LPQHQNGMYGLHQd 94
Cdd:cd16143    2 NIVIILADDLGYgDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwrsrLKGGVLGGFSPPL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  95 vhhfnsFDKVR-SLPLLLSQAGVRTGIIGKKHVG----------PETVYPFDFAYTE-------ENG-------SVLQVG 149
Cdd:cd16143   81 ------IEPDRvTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkAATGTGKDVDYSKpikggplDHGfdyyfgiPASEVL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 150 RNITRiKllVRKFLQTQ--DDRPFFLYVAFHDPHrcGHSQPqygtfCEKFgNGESGMGripdwtpqaydpldvlvpyfvp 227
Cdd:cd16143  155 PTLTD-K--AVEFIDQHakKDKPFFLYFALPAPH--TPIVP-----SPEF-QGKSGAG---------------------- 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 767995604 228 ntpaARADLAAQyttvgrMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16143  202 ----PYGDFVYE------LDWVVGRILDALKELGLAENTLVIFTSDNG 239
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-275 4.73e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 123.45  E-value: 4.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDV 95
Cdd:cd16034    1 KP-NILFIFADQHRAQAlGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGndvpLPPDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  96 HhfnSFDKVrslpllLSQAGVRTGIIGKKHV-GPETVYP--------------FDF------------AYTEENGSVLQV 148
Cdd:cd16034   80 P---TIADV------LKDAGYRTGYIGKWHLdGPERNDGraddytppperrhgFDYwkgyecnhdhnnPHYYDDDGKRIY 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 149 GRNITRIKL--LVRKFL--QTQDDRPFFLYVAFHDPHrcghsqPQYGTFCEKFGNGesgmgripdwtpqaYDPLDVLVPY 224
Cdd:cd16034  151 IKGYSPDAEtdLAIEYLenQADKDKPFALVLSWNPPH------DPYTTAPEEYLDM--------------YDPKKLLLRP 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767995604 225 FVPNTPAARADLAAQ----YTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16034  211 NVPEDKKEEAGLREDlrgyYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHG 265
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
21-314 6.27e-32

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 123.04  E-value: 6.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADDGGFESGAYNnsaiATPHLDA-LARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhFN 99
Cdd:cd16147    1 RP-NIVLILTDDQDVELGSMD----PMPKTKKlLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPP---GG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 SFDKV-------RSLPLLLSQAGVRTGIIGK------KHVGPETVYP-FDFAYTEENGSV-----LQVGRNITRIK---- 156
Cdd:cd16147   73 GYPKFwqnglerSTLPVWLQEAGYRTAYAGKylngygVPGGVSYVPPgWDEWDGLVGNSTyynytLSNGGNGKHGVsypg 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 157 -----LLVRK---FLQT--QDDRPFFLYVAFHDPHRCGHSQPQYGtfcekfgNGESGMGRIPDWTPQAYDPLDVlvPYFV 226
Cdd:cd16147  153 dyltdVIANKaldFLRRaaADDKPFFLVVAPPAPHGPFTPAPRYA-------NLFPNVTAPPRPPPNNPDVSDK--PHWL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 227 PNTPAARADLAAQYTTVGR--------MDQGVGLVLQELRDAGVLNDTLVIFTSDNGipF-------PSGRTNLYWPGTA 291
Cdd:cd16147  224 RRLPPLNPTQIAYIDELYRkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNG--YhlgqhrlPPGKRTPYEEDIR 301
                        330       340
                 ....*....|....*....|...
gi 767995604 292 EPLLVSSPEHPKrwGQVSEAYVS 314
Cdd:cd16147  302 VPLLVRGPGIPA--GVTVDQLVS 322
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
24-313 1.99e-31

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: 121.55  E-value: 1.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGmyglhqdVHHFNSFD 102
Cdd:cd16151    2 NIILIMADDLGYECiGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNY-------VVFGYLDP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 103 KVRSLPLLLSQAGVRTGIIGKKHVGPETVYP-------FD-------------------FAYTEENGSVLQVGRNITRIK 156
Cdd:cd16151   74 KQKTFGHLLKDAGYATAIAGKWQLGGGRGDGdyphefgFDeyclwqltetgekysrpatPTFNIRNGKLLETTEGDYGPD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 157 LLVRK---FLQTQDDRPFFLY---VAFHDPHrcghsqpqYGTfcekfgngesgmgriPD---WTPQAYDPLDVLvPYFvp 227
Cdd:cd16151  154 LFADFlidFIERNKDQPFFAYypmVLVHDPF--------VPT---------------PDspdWDPDDKRKKDDP-EYF-- 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 228 ntpaarADLAAqYttvgrMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFP-SGRTN----------LYWPGTAEPLLV 296
Cdd:cd16151  208 ------PDMVA-Y-----MDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPiTSRTNgrevrggkgkTTDAGTHVPLIV 275
                        330
                 ....*....|....*..
gi 767995604 297 SSPEHPKRwGQVSEAYV 313
Cdd:cd16151  276 NWPGLIPA-GGVSDDLV 291
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
24-298 2.07e-31

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: 118.50  E-value: 2.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGM-----YGLHQDVHH 97
Cdd:cd16149    2 NILFILTDDQGPWAlGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTKK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  98 FNSFDKVR-SLPLLLSQAGVRTGIIGKKHVGPETVypfDFayteengsvlqvgrnitriklLVRkflQTQDDRPFFLYVA 176
Cdd:cd16149   82 PEGYLEGQtTLPEVLQDAGYRCGLSGKWHLGDDAA---DF---------------------LRR---RAEAEKPFFLSVN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 177 FHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVLQE 256
Cdd:cd16149  135 YTAPH-----------------------------SPWGY------------------------FAAVTGVDRNVGRLLDE 161
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767995604 257 LRDAGVLNDTLVIFTSDNGipFPSG------------RTNLY-----------WPGTAEPLLVSS 298
Cdd:cd16149  162 LEELGLTENTLVIFTSDNG--FNMGhhgiwgkgngtfPLNMYdnsvkvpfiirWPGVVPAGRVVD 224
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-316 3.77e-28

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 113.10  E-value: 3.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGmyglHQDVHHFNSFDKvrslPLLLS---QA 114
Cdd:cd16150   17 GHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG----HRTLHHLLRPDE----PNLLKtlkDA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 115 GVRTGIIGKKHVGPETVYPFDFAYTEEngsvLQVGRNITRIKllvrkflQTQDDRPFFLYVAFHDPHrcghsqPQYGtfC 194
Cdd:cd16150   89 GYHVAWAGKNDDLPGEFAAEAYCDSDE----ACVRTAIDWLR-------NRRPDKPFCLYLPLIFPH------PPYG--V 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 195 EKfgngesgmgriPDWTpqAYDPLDVLVPyfVPNTPAARADL-----------------------AAQYTTVGRMDQGVG 251
Cdd:cd16150  150 EE-----------PWFS--MIDREKLPPR--RPPGLRAKGKPsmlegiekqgldrwseerwrelrATYLGMVSRLDHQFG 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767995604 252 LVLQELRDAGVLNDTLVIFTSDNGipfpsGRTNLY-----WPGTAE------PLLVSSPEHPKrwGQVSEAYVSLL 316
Cdd:cd16150  215 RLLEALKETGLYDDTAVFFFSDHG-----DYTGDYglvekWPNTFEdcltrvPLIIKPPGGPA--GGVSDALVELV 283
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
22-317 5.81e-28

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: 113.33  E-value: 5.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  22 PRNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNS 100
Cdd:cd16157    1 KPNIILMLMDDMGWgDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA--HARNA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 101 F----------DKVRSLPLLLSQAGVRTGIIGKKHVGPETVY-P----FDFAYTEENGSV-----------------LQV 148
Cdd:cd16157   79 YtpqnivggipDSEILLPELLKKAGYRNKIVGKWHLGHRPQYhPlkhgFDEWFGAPNCHFgpydnkaypnipvyrdwEMI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 149 GR--------------NITRIkLLVR--KFLQTQ--DDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGnGESGMGRIPDw 210
Cdd:cd16157  159 GRyyeefkidkktgesNLTQI-YLQEalEFIEKQhdAQKPFFLYWAPDATH-----APVYAS--KPFL-GTSQRGLYGD- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 211 tpqaydpldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI-------------P 277
Cdd:cd16157  229 -------------------------------AVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAalisapeqggsngP 277
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 767995604 278 FPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLE 317
Cdd:cd16157  278 FLCGKQTTFEGGMREPAIAWWPGHIKP-GQVSHQLGSLMD 316
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
24-313 6.13e-28

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: 112.26  E-value: 6.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFESGAYNNSA-IATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGMYglHQDVHHfnsfD 102
Cdd:cd16029    2 HIVFILADDLGWNDVGFHGSDqIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQ--HGVILA----G 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 103 KVRSLPL-------LLSQAGVRTGIIGKKHVG--------------------------------PETVYPFDFAYTEENG 143
Cdd:cd16029   75 EPYGLPLnetllpqYLKELGYATHLVGKWHLGfytweytptnrgfdsfygyyggaedyythtsgGANDYGNDDLRDNEEP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 144 SVLQVGRNITriKLLVR---KFLQTQD-DRPFFLYVAFHDPHrcghsqpqygtfcekFGNGEsgmgripdwtPQAYDPLD 219
Cdd:cd16029  155 AWDYNGTYST--DLFTDravDIIENHDpSKPLFLYLAFQAVH---------------APLQV----------PPEYADPY 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 220 VLVPYFVPNTpaARADLAAqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRT--N---------LYWP 288
Cdd:cd16029  208 EDKFAHIKDE--DRRTYAA---MVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsNyplrggkntLWEG 282
                        330       340
                 ....*....|....*....|....*
gi 767995604 289 GTAEPLLVSSPEHPKRWGQVSEAYV 313
Cdd:cd16029  283 GVRVPAFVWSPLLPPKRGTVSDGLM 307
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-316 6.30e-28

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 109.56  E-value: 6.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLpqhqngmYGLHQDVHHFNSFDKVRSLPLLLSQAGVR 117
Cdd:cd16148   17 GCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGL-------YPFYHGVWGGPLEPDDPTLAEILRKAGYY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 118 TGIIGkKHVGPETVYPFDFAYTEENGSVLQVGRNI----TRIKLLVRKFL----QTQDDRPFFLYVAFHDPHrcghsqpq 189
Cdd:cd16148   90 TAAVS-SNPHLFGGPGFDRGFDTFEDFRGQEGDPGeegdERAERVTDRALewldRNADDDPFFLFLHYFDPH-------- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 190 ygtfcekfgngesgmgripdwTPQAYDpldvlvpyfvpntpaarADLAaqyttvgRMDQGVGLVLQELRDAGVLNDTLVI 269
Cdd:cd16148  161 ---------------------EPYLYD-----------------AEVR-------YVDEQIGRLLDKLKELGLLEDTLVI 195
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767995604 270 FTSDNGIPFpsGRTNLYW----PGTAE----PLLVSSPEHPKrwGQVSEAYVSLL 316
Cdd:cd16148  196 VTSDHGEEF--GEHGLYWghgsNLYDEqlhvPLIIRWPGKEP--GKRVDALVSHI 246
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
22-316 2.06e-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: 111.13  E-value: 2.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  22 PRNALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSF 101
Cdd:cd16030    2 KPNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNS--YFRKVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 102 DKVRSLPLLLSQAGVRTGIIGK---KHVGPE-------TVYPFDFAYTEENGSVLQVGRNITR----------------- 154
Cdd:cd16030   80 PDAVTLPQYFKENGYTTAGVGKifhPGIPDGdddpaswDEPPNPPGPEKYPPGKLCPGKKGGKgggggpaweaadvpdea 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 155 ----------IKLLVRKFlqtQDDRPFFLYVAFHDPHRcghsqP---------QYGTFCEKFGNGESGMG----RIPDWT 211
Cdd:cd16030  160 ypdgkvadeaIEQLRKLK---DSDKPFFLAVGFYKPHL-----PfvapkkyfdLYPLESIPLPNPFDPIDlpevAWNDLD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 212 --PQAYDPLDVLVPYFVPNTPAARADLAAQ--YTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipFPSG------ 281
Cdd:cd16030  232 dlPKYGDIPALNPGDPKGPLPDEQARELRQayYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG--WHLGehghwg 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 767995604 282 -RTNlyWpgtaE-----PLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16030  310 kHTL--F----EeatrvPLIIRAPGVTKP-GKVTDALVELV 343
PRK13759 PRK13759
arylsulfatase; Provisional
21-275 2.31e-27

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 111.68  E-value: 2.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlHQDVhhfN 99
Cdd:PRK13759   6 KP-NIILIMVDQMRGDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG-YGDV---V 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 SFDKVRSLPLLLSQAGVRTGIIGKKHVGPETV--------------------YPFDFAYTEENGSVLQ---VGRNITRIK 156
Cdd:PRK13759  81 PWNYKNTLPQEFRDAGYYTQCIGKMHVFPQRNllgfhnvllhdgylhsgrneDKSQFDFVSDYLAWLRekaPGKDPDLTD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 157 LLVR--------------------------KFLQTQD-DRPFFLYVAFHDPHRcGHSQPQYgtFCEKFGNGESGMGRIPD 209
Cdd:PRK13759 161 IGWDcnswvarpwdleerlhptnwvgsesiEFLRRRDpTKPFFLKMSFARPHS-PYDPPKR--YFDMYKDADIPDPHIGD 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995604 210 WT------PQAYDPlDVLVPYFvPNTPAARAdLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:PRK13759 238 WEyaedqdPEGGSI-DALRGNL-GEEYARRA-RAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG 306
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
24-316 5.70e-27

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: 108.43  E-value: 5.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDV--- 95
Cdd:cd16032    2 NILLIMADQlTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDnaaeFPADIptf 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  96 -HHfnsfdkvrslpllLSQAGVRTGIIGKKH-VGPETVYPFDfaYTEEngsvlqVGRNITRiKL--LVRKflqtQDDRPF 171
Cdd:cd16032   82 aHY-------------LRAAGYRTALSGKMHfVGPDQLHGFD--YDEE------VAFKAVQ-KLydLARG----EDGRPF 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 172 FLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwtpqayDPLDVLVPYFVPNTPAARadlAAQYTTVGRMDQGVG 251
Cdd:cd16032  136 FLTVSFTHPH----------------------------------DPYVIPQEYWDLYVRRAR---RAYYGMVSYVDDKVG 178
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995604 252 LVLQELRDAGVLNDTLVIFTSDN-------GIPFpsgRTNLYWPGTAEPLLVSSPE--HPKRwgqVSEAyVSLL 316
Cdd:cd16032  179 QLLDTLERTGLADDTIVIFTSDHgdmlgerGLWY---KMSFFEGSARVPLIISAPGrfAPRR---VAEP-VSLV 245
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
24-275 1.04e-26

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: 108.39  E-value: 1.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGF-ESGAYNNSAI---ATPHLDALARRSLLFRNaFTSVSSCSPSRASLLTG---------LPQHQNGMYG 90
Cdd:cd16142    2 NILVILGDDIGWgDLGCYGGGIGrgaPTPNIDRLAKEGLRFTS-FYVEPSCTPGRAAFITGrhpirtgltTVGLPGSPGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  91 LHqdvhhfnsfDKVRSLPLLLSQAGVRTGIIGKKHVG--PE---TVYPFD----FAYT---EEngsvlQVGRNITRIKll 158
Cdd:cd16142   81 LP---------PWEPTLAELLKDAGYATAQFGKWHLGdeDGrlpTDHGFDefygNLYHtidEE-----IVDKAIDFIK-- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 159 vRkflQTQDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgMGRIPDWTPQAydplDVLVpyfvpntpaaradlaa 238
Cdd:cd16142  145 -R---NAKADKPFFLYVNFTKMHFPTLPSPEF-------------EGKSSGKGKYA----DSMV---------------- 187
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767995604 239 qyttvgRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16142  188 ------ELDDHVGQILDALDELGIADNTIVIFTTDNG 218
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
22-275 2.09e-25

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: 105.99  E-value: 2.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  22 PRNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhQDVHHFNS 100
Cdd:cd16158    1 PPNIVLLFADDLGYgDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVY---PGVFYPGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 101 FDkvrSLPL-------LLSQAGVRTGIIGKKH--VGPETVY-P----FDF----AYTEENG------------------- 143
Cdd:cd16158   78 RG---GLPLnettiaeVLKTVGYQTAMVGKWHlgVGLNGTYlPthqgFDHylgiPYSHDQGpcqnltcfppnipcfggcd 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 144 ------------SVLQVGRNITRIKLLVRKFLQ------TQDDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGnGESGMG 205
Cdd:cd16158  155 qgevpcplfyneSIVQQPVDLLTLEERYAKFAKdfiadnAKEGKPFFLYYASHHTH-----YPQFAG--QKFA-GRSSRG 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 206 RIPDwtpqaydpldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16158  227 PFGD--------------------------------ALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG 264
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
22-317 3.55e-25

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: 104.47  E-value: 3.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  22 PRNALLLLADDGGFESGAYNN--SAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHFN 99
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMT-------GRLGLRNGVGHNF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 SFDKVRSLPL-------LLSQAGVRTGIIGKKHVGPETVY-P----FDFAY--TEENGSVLQvgrniTRIKLLVRKFLQ- 164
Cdd:cd16161   74 LPTSVGGLPLnettlaeVLRQAGYATGMIGKWHLGQREAYlPnsrgFDYYFgiPFSHDSSLA-----DRYAQFATDFIQr 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 165 -TQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYDPLdvlvpyfVPNTPAARADLAAqytTV 243
Cdd:cd16161  149 aSAKDRPFFLYAALAHVH-----------------------------VPLANLPR-------FQSPTSGRGPYGD---AL 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 244 GRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG--------IPFPSG---RTNLYWP---------GTAEPLLVSSPEHPK 303
Cdd:cd16161  190 QEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelAVGPGTgdwQGNLGGSvakastwegGHREPAIVYWPGRIP 269
                        330
                 ....*....|....
gi 767995604 304 RwGQVSEAYVSLLE 317
Cdd:cd16161  270 A-NSTSAALVSTLD 282
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-316 3.44e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 101.54  E-value: 3.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMY----GLHQDvhhfnsfdkVRSLPLLLSQ 113
Cdd:cd16152   18 GCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFrngiPLPAD---------EKTLAHYFRD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 114 AGVRTGIIGKKHVGpetVYPFDFayteengsvlqvgrnITRIKLlvrKFLQT-QDDRPFFLYVAFHDPHrcgHsQPQYGT 192
Cdd:cd16152   89 AGYETGYVGKWHLA---GYRVDA---------------LTDFAI---DYLDNrQKDKPFFLFLSYLEPH---H-QNDRDR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 193 F------CEKFGNGesgmgripdWTPQAYDPLdvlvpyfvPNTpaARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDT 266
Cdd:cd16152  144 YvapegsAERFANF---------WVPPDLAAL--------PGD--WAEELPDYLGCCERLDENVGRIRDALKELGLYDNT 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767995604 267 LVIFTSDNGIPFPSgRTNLYWPGTAE-----PLLVSSPehPKRWGQVSEAYVSLL 316
Cdd:cd16152  205 IIVFTSDHGCHFRT-RNAEYKRSCHEssirvPLVIYGP--GFNGGGRVEELVSLI 256
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
24-275 7.81e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 95.91  E-value: 7.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFESGAYNNSAIA-----------TPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGL- 91
Cdd:cd16153    3 NILWIITDDQRVDSLSCYNNAHTgksesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFe 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  92 --HQDVHHFNsfdkvRSLPLLLSQAGVRTGIIGKKHVGPETVYpfdfayteengsvlqVGRNITRIKLLVRKFLQTQD-D 168
Cdd:cd16153   83 aaHPALDHGL-----PTFPEVLKKAGYQTASFGKSHLEAFQRY---------------LKNANQSYKSFWGKIAKGADsD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 169 RPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPqaydpldVLVpyfvpntPAARADLAAQYTTVGRMDQ 248
Cdd:cd16153  143 KPFFVRLSFLQPH-----------------------------TP-------VLP-------PKEFRDRFDYYAFCAYGDA 179
                        250       260       270
                 ....*....|....*....|....*....|
gi 767995604 249 GVGLVLQELRDAGVLND---TLVIFTSDNG 275
Cdd:cd16153  180 QVGRAVEAFKAYSLKQDrdyTIVYVTGDHG 209
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
23-275 2.98e-22

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: 96.94  E-value: 2.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  23 RNALLLLADDGGFE-SGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMY--GLHQDVHHfn 99
Cdd:cd16028    1 RNVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVwnGTPLDARH-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 sfdkvRSLPLLLSQAGVRTGIIGKKHVGP----------------------ETVYPFDFaYTEENGSVlqvgRNITRiKL 157
Cdd:cd16028   79 -----LTLALELRKAGYDPALFGYTDTSPdprglapldprllsyelampgfDPVDRLDE-YPAEDSDT----AFLTD-RA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 158 LvrKFLQTQDDRPFFLYVAFHDPH----------------------RCGHSQ------PQYGTFCEKFGNGESGMGRIPD 209
Cdd:cd16028  148 I--EYLDERQDEPWFLHLSYIRPHppfvapapyhalydpadvpppiRAESLAaeaaqhPLLAAFLERIESLSFSPGAANA 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995604 210 WTPqaydpldvlvpyfvpnTPAARADLAAQYT-TVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16028  226 ADL----------------DDEEVAQMRATYLgLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG 276
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
24-317 4.20e-21

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: 93.26  E-value: 4.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:cd16160    3 NIVLFFADDMGYgDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDIGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 103 KVRS---LPLLLSQAGVRTGIIGKKHVG------------PE--------TVYPFDFAY----TEE-------NGSVLQV 148
Cdd:cd16160   83 LPKTevtMAEALKEAGYTTGMVGKWHLGinennhsdgahlPShhgfdfvgTNLPFTNSWacddTGRhvdfpdrSACFLYY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 149 GRNIT-----------RIKLLVRKFLQTQDDRPFFLYVAFhdphrcghSQPQYGTFCEKFGNGESGMGRIPDwtpqaydp 217
Cdd:cd16160  163 NDTIVeqpiqhehlteTLVGDAKSFIEDNQENPFFLYFSF--------PQTHTPLFASKRFKGKSKRGRYGD-------- 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 218 ldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI------------PFPSGRTN- 284
Cdd:cd16160  227 ------------------------NINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPhveycleggstgGLKGGKGNs 282
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767995604 285 ----------LYWPGTAEPllvsspehpkrwgQVSEAYVSLLE 317
Cdd:cd16160  283 weggirvpfiAYWPGTIKP-------------RVSHEVVSTMD 312
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
24-297 2.02e-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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 87.79  E-value: 2.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  24 NALLLLADDGGFESGA---YNNSAIATPHLDALARRSLLFRNAFtSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHF-- 98
Cdd:cd16154    2 NILLIIADDQGLDSSAqysLSSDLPVTPTLDSLANSGIVFDNLW-ATPACSPTRATILT-------GKYGFRTGVLAVpd 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  99 NSFDKVRSLPLLL----SQAGVRTGIIGKKHVG------PETVYPFDFA---------YTE----ENGSVLQVGR-NITR 154
Cdd:cd16154   74 ELLLSEETLLQLLikdaTTAGYSSAVIGKWHLGgndnspNNPGGIPYYAgilgggvqdYYNwnltNNGQTTNSTEyATTK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 155 IKLLVRKFLQTQdDRPFFLYVAFHDPHRCGHSQPqygtfcekfgNGESGMGRIPDWTPQAYDPLdvlvPYFvpntpaara 234
Cdd:cd16154  154 LTNLAIDWIDQQ-TKPWFLWLAYNAPHTPFHLPP----------AELHSRSLLGDSADIEANPR----PYY--------- 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995604 235 dLAAqyttVGRMDQGVGLVLQELrDAGVLNDTLVIFTSDNGIP-------FPSGRT--NLYWPGTAEPLLVS 297
Cdd:cd16154  210 -LAA----IEAMDTEIGRLLASI-DEEERENTIIIFIGDNGTPgqvvdlpYTRNHAkgSLYEGGINVPLIVS 275
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-275 5.74e-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: 85.72  E-value: 5.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  48 PHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhqDVHHFNSF----DKVRSLPLLLSQAGVRTGIIGK 123
Cdd:cd16035   27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT----DTLGSPMQpllsPDVPTLGHMLRAAGYYTAYKGK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 124 KHV--GPETVYPFDFAYTEEngsvlqvgrnitRIKLLVRKFLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgnge 201
Cdd:cd16035  103 WHLsgAAGGGYKRDPGIAAQ------------AVEWLRERGAKNADGKPWFLVVSLVNPH-------------------- 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995604 202 sgmgripdwtpqaydplDVLvpYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16035  151 -----------------DIM--FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG 205
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
38-309 8.48e-19

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: 86.67  E-value: 8.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNSF---DKVRSLPLLLSQA 114
Cdd:cd16156   17 GCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWT--------NCMalgDNVKTIGQRLSDN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 115 GVRTGIIGKKHV-------------GPETVYPFDFA-YTEE----------NGSVLQVGRNIT-------RIKLLVRKFL 163
Cdd:cd16156   89 GIHTAYIGKWHLdggdyfgngicpqGWDPDYWYDMRnYLDElteeerrksrRGLTSLEAEGIKeeftyghRCTNRALDFI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 164 QTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFgngesgmgRIPDwTPQAYDPLDvlvpyfvpNTPA-ARADLAAQYTT 242
Cdd:cd16156  169 EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDF--------EFPK-GENAYDDLE--------NKPLhQRLWAGAKPHE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 243 VGR---------------MDQGVGLVLQELRDagVLNDTLVIFTSDNGIPFpsGRTNLYWPGTAE-------PLLVSSPE 300
Cdd:cd16156  232 DGDkgtikhplyfgcnsfVDYEIGRVLDAADE--IAEDAWVIYTSDHGDML--GAHKLWAKGPAVydeitniPLIIRGKG 307

                 ....*....
gi 767995604 301 HPKRWGQVS 309
Cdd:cd16156  308 GEKAGTVTD 316
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
23-314 2.36e-16

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: 77.08  E-value: 2.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  23 RNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFR-NAFTSVSSCSPSRASLLTGLPQHQNGMYG--------LH 92
Cdd:cd00016    1 KHVVLIVLDGLGAdDLGKAGNPAPTTPNLKRLASEGATFNfRSVSPPTSSAPNHAALLTGAYPTLHGYTGngsadpelPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  93 QDVHHFNSFDkvrSLPLLLSQAGVRTGIIGkkhvgpetvypfdfayteengsvlqvgrnitrikllVRKFL-QTQDDRPF 171
Cdd:cd00016   81 RAAGKDEDGP---TIPELLKQAGYRTGVIG------------------------------------LLKAIdETSKEKPF 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 172 FLYVAFHDPHRCGHSqpqygtfcekfgngesgmgriPDWTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVG 251
Cdd:cd00016  122 VLFLHFDGPDGPGHA---------------------YGPNTPEY------------------------YDAVEEIDERIG 156
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767995604 252 LVLQELRDAGVLNDTLVIFTSDNG-IPFPSGRT--NLYWPGTAE-----PLLVSSPEHPKrwGQVSEAYVS 314
Cdd:cd00016  157 KVLDALKKAGDADDTVIIVTADHGgIDKGHGGDpkADGKADKSHtgmrvPFIAYGPGVKK--GGVKHELIS 225
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
21-275 2.33e-14

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: 73.48  E-value: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  21 RPrNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMyGLHQDVHHFN 99
Cdd:cd16159    1 KP-NIVLFMADDLGIgDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGM-ASSHGMRVIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 100 SFDKVRSLP-------LLLSQAGVRTGIIGKKHVG--PETV---------YPFDFAY-----------TEENGSVLQVGR 150
Cdd:cd16159   79 FTASSGGLPpnettfaEVLKQQGYSTALIGKWHLGlhCESRndfchhplnHGFDYFYglpltnlkdcgDGSNGEYDLSFD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 151 N-----------------------------------------------ITRIK----LLVR------------------- 160
Cdd:cd16159  159 PlfplltafvlitaltiflllylgavskrffvfllilsllfislffllLITNRyfncILMRnhevveqpmslenltqrlt 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 161 ----KFLQTQDDRPFFLYVAFHDPHRCGHSQPqygtfceKFgNGESGMGRIPDwtpqaydpldvlvpyfvpntpaaradl 236
Cdd:cd16159  239 keaiSFLERNKERPFLLVMSFLHVHTALFTSK-------KF-KGRSKHGRYGD--------------------------- 283
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 767995604 237 aaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16159  284 -----NVEEMDWSVGQILDALDELGLKDNTFVYFTSDNG 317
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
10-276 9.22e-12

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 65.15  E-value: 9.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  10 ALLLVLGLCRARPRNALLLLADdgGFesGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCS-PSRASLLTGLP--QHQ- 85
Cdd:COG1524   11 SLLAAAAAAAPPAKKVVLILVD--GL--RADLLERAHAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGLYpgEHGi 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  86 --NGMY-----------GLHQDVHHFNSFDKVRSLPLLLSQAGVRTGIIG-KKHVGPETV-YPFDFAYteeNGSVLQVGR 150
Cdd:COG1524   87 vgNGWYdpelgrvvnslSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFwPSFEGSGLIdAARPYPY---DGRKPLLGN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 151 NITRiKLLVRKFLQT-QDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNT 229
Cdd:COG1524  164 PAAD-RWIAAAALELlREGRPDLLLVYLPDLDYAGH---RYG-----------------------------------PDS 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 767995604 230 PAARADLAaqyttvgRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI 276
Cdd:COG1524  205 PEYRAALR-------EVDAALGRLLDALKARGLYEGTLVIVTADHGM 244
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
26-276 2.66e-09

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: 57.21  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  26 LLLLADdgGFESgAYNNSAIATPHLDALARRSLLF---RNAFTSVSScsPSRASLLTGLP--QHQ---NGMY-------G 90
Cdd:cd16018    4 IVISID--GFRW-DYLDRAGLTPNLKRLAEEGVRAkyvKPVFPTLTF--PNHYSIVTGLYpeSHGivgNYFYdpktneeF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  91 LHQDVHHFNSFDKVRSLPLLLSQAGVRTGII------GKKHVGPETVYPFDFAYTEENGSVLqvgrNITRIKLLVRKFlq 164
Cdd:cd16018   79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYfwpgseVAIIGYNPTPIPLGGYWQPYNDSFP----FEERVDTILEWL-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 165 tQDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNTPAARADLAaqyttvg 244
Cdd:cd16018  153 -DLERPDLILLYFEEPDSAGH---KYG-----------------------------------PDSPEVNEALK------- 186
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767995604 245 RMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI 276
Cdd:cd16018  187 RVDRRLGYLIEALKERGLLDDTNIIVVSDHGM 218
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
47-276 4.74e-09

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: 57.05  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604   47 TPHLDALARRSLLFRNAFTSV-SSCSPSRASLLTGLPQHQNGMYG-----------LHQDVHHFNSFDKVRSLPLL--LS 112
Cdd:pfam01663  20 TPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGntfydpktgeyLVFVISDPEDPRWWQGEPIWdtAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  113 QAGVRTGII----GKKHVGPETVYPFDFAYTEENGSVLQVGR--NITRIKLLVRKFLQTQDDRPFFLYVAFHDPHRCGHs 186
Cdd:pfam01663 100 KAGVRAAALfwpgSEVDYSTYYGTPPRYLKDDYNNSVPFEDRvdTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGH- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  187 qpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNTPAARADLAaqyttvgRMDQGVGLVLQELRDAGVLNDT 266
Cdd:pfam01663 179 --RYG-----------------------------------PDSPEVEDALR-------RVDRAIGDLLEALDERGLFEDT 214
                         250
                  ....*....|
gi 767995604  267 LVIFTSDNGI 276
Cdd:pfam01663 215 NVIVVSDHGM 224
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
33-314 1.25e-08

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 56.20  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  33 GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLP-QHQNGMYGLHQDVHHFnsfdkvrSLPLLL 111
Cdd:COG1368  246 SDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKRPGQNNFP-------SLPSIL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 112 SQAGVRTGIIgkkHVGPET------VYP---FDFAYTEENgsvLQVGRNIT-RI--KLLVRKFLQT--QDDRPFFLYV-- 175
Cdd:COG1368  319 KKQGYETSFF---HGGDGSfwnrdsFYKnlgFDEFYDRED---FDDPFDGGwGVsdEDLFDKALEEleKLKKPFFAFLit 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 176 -AFHDPhrcghsqpqYgtfceKFGNGESGMGRIPDWTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVL 254
Cdd:COG1368  393 lSNHGP---------Y-----TLPEEDKKIPDYGKTTLNNY------------------------LNAVRYADQALGEFI 434
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995604 255 QELRDAGVLNDTLVIFTSDNGIPFPsGRTNLYWPGTAE--PLLVSSPEHPKrwGQVSEAYVS 314
Cdd:COG1368  435 EKLKKSGWYDNTIFVIYGDHGPRSP-GKTDYENPLERYrvPLLIYSPGLKK--PKVIDTVGS 493
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
42-317 3.76e-08

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: 54.47  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  42 NSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHqngmygLHQDVHHFNSFDK-VRSLPLLLSQAGVRTGI 120
Cdd:cd16171   21 NQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTH------LTESWNNYKGLDPnYPTWMDRLEKHGYHTQK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 121 IGKKHV--GPETVYPFDFAYTEENGSVL-QVGR---NITRIKLLVRKFL---QTQD-------------DRPFFLYVAFH 178
Cdd:cd16171   95 YGKLDYtsGHHSVSNRVEAWTRDVPFLLrQEGRptvNLVGDRSTVRVMLkdwQNTDkavhwirkeapnlTQPFALYLGLN 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 179 DPHrcghsqpQYGTfcekfgngesgmgripdwtpqaydpldvlvPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELR 258
Cdd:cd16171  175 LPH-------PYPS------------------------------PSMGENFGSIRNIRAFYYAMCAETDAMLGEIISALK 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767995604 259 DAGVLNDTLVIFTSDNGIPFPSGR----TNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLLE 317
Cdd:cd16171  218 DTGLLDKTYVFFTSDHGELAMEHRqfykMSMYEGSSHVPLLIMGPGIKA--GQQVSDVVSLVD 278
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
38-280 3.25e-07

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: 51.14  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604  38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRA--SLLTGLPQHQNGMYGLHQDVHHfnsfdKVRSLPLLLSQAG 115
Cdd:cd16015   17 DKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLN-----PLPSLPSILKEQG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 116 VRTGIIgkkHVGP------ETVYP---FDFAYTEENGSVLQVGRNITRI--KLLVRKF---LQTQDDRPFFLYV---AFH 178
Cdd:cd16015   92 YETIFI---HGGDasfynrDSVYPnlgFDEFYDLEDFPDDEKETNGWGVsdESLFDQAleeLEELKKKPFFIFLvtmSNH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995604 179 DPhrcghsqpqYGTFCEKFgngesgmgripdwtpqaydpldvlvpYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELR 258
Cdd:cd16015  169 GP---------YDLPEEKK--------------------------DEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLK 213
                        250       260
                 ....*....|....*....|..
gi 767995604 259 DAGVLNDTLVIFTSDNGIPFPS 280
Cdd:cd16015  214 KSGLYENTIIVIYGDHLPSLGS 235
 
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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