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Conserved domains on  [gi|71852586|ref|NP_033667|]
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arylsulfatase D isoform beta precursor [Homo sapiens]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
40-333 6.37e-163

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


The actual alignment was detected with superfamily member cd16159:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 521  Bit Score: 466.76  E-value: 6.37e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWN 119
Cdd:cd16159   1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAQ 199
Cdd:cd16159  81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 200 LWGYTQFLALGILTLAAGQTCGFfsVSARAVTGMAGVGCLFFISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLML 279
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71852586 280 KEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI 333
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSV 292
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
40-333 6.37e-163

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: 466.76  E-value: 6.37e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWN 119
Cdd:cd16159   1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAQ 199
Cdd:cd16159  81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 200 LWGYTQFLALGILTLAAGQTCGFfsVSARAVTGMAGVGCLFFISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLML 279
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71852586 280 KEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI 333
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSV 292
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
40-150 3.28e-52

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 178.53  E-value: 3.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYralqwn 119
Cdd:COG3119  23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGV-TDNGE------ 95
                        90       100       110
                ....*....|....*....|....*....|.
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIGKWH 150
Cdd:COG3119  96 GYNGGLPPDEPTLAELLKEAGYRTALFGKWH 126
Sulfatase pfam00884
Sulfatase;
41-335 2.82e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 133.70  E-value: 2.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586    41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGyralqwna 120
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586   121 gsGGLPENETTFARILQQHGYATGLIGKWHQGVNCASrgdhchHPLNHGFDYFYGMPFTLTNDCDPGRPPevdaalraql 200
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ------SPCNLGFDKFFGRNTGSDLYADPPDVP---------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586   201 wgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrWNCILMRNHDVteqpmvlektasLMLK 280
Cdd:pfam00884 135 -----------------------------------------------------YNCSGGGVSDE------------ALLD 149
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71852586   281 EAVSYIERHkHGPFLLFLSLLHVHIPL------------VTTSAFLGKSQHGLYGDNVEEMDWLIAS 335
Cdd:pfam00884 150 EALEFLDNN-DKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGR 215
PRK13759 PRK13759
arylsulfatase; Provisional
40-150 4.03e-22

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 97.43  E-value: 4.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586   40 KPNILLIMADDLgTGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasNGYralqw 118
Cdd:PRK13759   6 KPNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR---VGY----- 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 71852586  119 naGSGGLPENETTFARILQQHGYATGLIGKWH 150
Cdd:PRK13759  77 --GDVVPWNYKNTLPQEFRDAGYYTQCIGKMH 106
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
40-333 6.37e-163

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: 466.76  E-value: 6.37e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWN 119
Cdd:cd16159   1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAQ 199
Cdd:cd16159  81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 200 LWGYTQFLALGILTLAAGQTCGFfsVSARAVTGMAGVGCLFFISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLML 279
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71852586 280 KEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI 333
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSV 292
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
40-333 5.97e-89

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: 273.67  E-value: 5.97e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWN 119
Cdd:cd16026   1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQgvncasrGDH-CHHPLNHGFDYFYGMPFtlTNDCDPGRPPEVDAALRa 198
Cdd:cd16026  76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHL-------GHQpEFLPTRHGFDEYFGIPY--SNDMWPFPLYRNDPPGP- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 199 qlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwNCILMRNHDVTEQPMVLEKTASLM 278
Cdd:cd16026 146 --------------------------------------------------------LPPLMENEEVIEQPADQSSLTQRY 169
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71852586 279 LKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI 333
Cdd:cd16026 170 TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSV 224
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
40-333 2.49e-70

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: 227.31  E-value: 2.49e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYrALQWn 119
Cdd:cd16160   1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRV-FLPW- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 aGSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDyFYG--MPFTLTNDCDPgrppevdaalr 197
Cdd:cd16160  79 -DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGtnLPFTNSWACDD----------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 198 aqlWGYTQflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfGFVRRWNCILMRNHDVTEQPMVLEKTASL 277
Cdd:cd16160 146 ---TGRHV-------------------------------------------DFPDRSACFLYYNDTIVEQPIQHEHLTET 179
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71852586 278 MLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI 333
Cdd:cd16160 180 LVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAV 235
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
41-333 7.36e-53

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: 180.09  E-value: 7.36e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYG-NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM--DASNGYRALQ 117
Cdd:cd16143   1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkgGVLGGFSPPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 118 wnagsggLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHH----------------PLNHGFDYFYGMPftlT 181
Cdd:cd16143  81 -------IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP---A 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 182 NDCDPgrppevdaalraqlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrn 261
Cdd:cd16143 151 SEVLP--------------------------------------------------------------------------- 155
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71852586 262 hdvteqpmvlektasLMLKEAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI 333
Cdd:cd16143 156 ---------------TLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVV 214
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
40-150 3.28e-52

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 178.53  E-value: 3.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYralqwn 119
Cdd:COG3119  23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGV-TDNGE------ 95
                        90       100       110
                ....*....|....*....|....*....|.
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIGKWH 150
Cdd:COG3119  96 GYNGGLPPDEPTLAELLKEAGYRTALFGKWH 126
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
40-333 4.97e-52

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: 180.33  E-value: 4.97e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWN 119
Cdd:cd16158   1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGV-----YPGVFYP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGVNcasrGDHCHHPLNHGFDYFYGMPFTltndcdpgrppevdaalraQ 199
Cdd:cd16158  76 GSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPYS-------------------H 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 200 LWGYTQFLalgiltlaagqTCgffsvsaravtgmagvgclfFISWYSSFGFVRRW--NCILMRNHDVTEQPMVLEKTASL 277
Cdd:cd16158 133 DQGPCQNL-----------TC--------------------FPPNIPCFGGCDQGevPCPLFYNESIVQQPVDLLTLEER 181
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71852586 278 MLKEAVSYIER--HKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI 333
Cdd:cd16158 182 YAKFAKDFIADnaKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSV 239
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
41-316 5.53e-52

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


Pssm-ID: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 178.51  E-value: 5.53e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM-DASNGYRALQWN 119
Cdd:cd16144   1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItDVIPGRRGPPDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 A------GSGGLPENETTFARILQQHGYATGLIGKWHQGvncasrGDHCHHPLNHGFDYFYGmpftltnDCDPGRPPevd 193
Cdd:cd16144  81 TklipppSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG-------GTGNGGPP--- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 194 aalraqlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiSWYSSFGFvrrwncilmrNHDVTEQPMVLEK 273
Cdd:cd16144 145 -------------------------------------------------SYYFPPGK----------PNPDLEDGPEGEY 165
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71852586 274 TASLMLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGK 316
Cdd:cd16144 166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIEK 208
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
41-175 1.17e-51

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: 177.40  E-value: 1.17e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyRALQWNA 120
Cdd:cd16145   1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71852586 121 GSGGLPENETTFARILQQHGYATGLIGKWHqgvncasRGDHCH--HPLNHGFDYFYG 175
Cdd:cd16145  75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWG-------LGGPGTpgHPTKQGFDYFYG 124
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
41-151 1.68e-50

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: 169.15  E-value: 1.68e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyraLQWNA 120
Cdd:cd16022   1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGV--------RGNVG 72
                        90       100       110
                ....*....|....*....|....*....|.
gi 71852586 121 GSGGLPENETTFARILQQHGYATGLIGKWHQ 151
Cdd:cd16022  73 NGGGLPPDEPTLAELLKEAGYRTALIGKWHD 103
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
40-335 3.54e-48

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: 167.65  E-value: 3.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGN-NTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALqw 118
Cdd:cd16161   1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSV-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 119 nagsGGLPENETTFARILQQHGYATGLIGKWHQGVNCAsrgdhcHHPLNHGFDYFYGMPFTltndcdpgrppevdaalra 198
Cdd:cd16161  79 ----GGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA------YLPNSRGFDYYFGIPFS------------------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 199 qlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnHDVTEQPMVLEKtaslm 278
Cdd:cd16161 130 ---------------------------------------------------------------HDSSLADRYAQF----- 141
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 279 lkeAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGKSQH-GLYGDNVEEMDWLIAS 335
Cdd:cd16161 142 ---ATDFIQRASAKdrPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQ 198
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
40-335 4.21e-47

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: 166.87  E-value: 4.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRAlqwN 119
Cdd:cd16157   1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHAR---N 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 AGS-----GGLPENETTFARILQQHGYATGLIGKWHQGvncasrgdH--CHHPLNHGFDYFYGMPftltnDCDPGRPPEV 192
Cdd:cd16157  78 AYTpqnivGGIPDSEILLPELLKKAGYRNKIVGKWHLG--------HrpQYHPLKHGFDEWFGAP-----NCHFGPYDNK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 193 DaalRAQLWGYTQFLalgiltlaagqtcgffsvsaravtgMAGvgclffiSWYSSFGFvrrwncilmrNHDVTEQPMvle 272
Cdd:cd16157 145 A---YPNIPVYRDWE-------------------------MIG-------RYYEEFKI----------DKKTGESNL--- 176
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71852586 273 ktASLMLKEAVSYIERH--KHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIAS 335
Cdd:cd16157 177 --TQIYLQEALEFIEKQhdAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGK 239
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
41-177 1.52e-46

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: 163.09  E-value: 1.52e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLR---TPNIDQLAEEGVRLTQHLAAaPLCTPSRAAFLTGRHSFRSGMdasngyRALQ 117
Cdd:cd16142   1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTGL------TTVG 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 118 WNAGSGGLPENETTFARILQQHGYATGLIGKWHQGvncASRGdhcHHPLNHGFDYFYGMP 177
Cdd:cd16142  74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDG---RLPTDHGFDEFYGNL 127
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
41-175 9.22e-46

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: 161.95  E-value: 9.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQ-HlaAAPLCTPSRAAFLTGRHSFRSGMdasngyralqWN 119
Cdd:cd16146   1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTGV----------WH 68
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71852586 120 AGSGG--LPENETTFARILQQHGYATGLIGKWHQGVNCAsrgdhcHHPLNHGFDYFYG 175
Cdd:cd16146  69 TILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLG 120
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
41-176 1.69e-43

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: 155.40  E-value: 1.69e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLaAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWNA 120
Cdd:cd16029   1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGM-----QHGVILAG 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71852586 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGvncasrgdHCHH---PLNHGFDYFYGM 176
Cdd:cd16029  75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY 125
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
41-174 4.47e-41

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 148.52  E-value: 4.47e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTqHLAAAPLCTPSRAAFLTGRHSFRSGmdasngyralqwnA 120
Cdd:cd16151   1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY-------------V 66
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71852586 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASrGDHCHHplnHGFDYFY 174
Cdd:cd16151  67 VFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGD-GDYPHE---FGFDEYC 116
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-176 9.70e-41

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


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 148.10  E-value: 9.70e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRalqwn 119
Cdd:cd16034   1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV-FGNDVP----- 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71852586 120 agsggLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHH----PLNHGFDYFYGM 176
Cdd:cd16034  75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY 130
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
40-177 1.61e-40

unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.


Pssm-ID: 293755 [Multi-domain]  Cd Length: 429  Bit Score: 148.06  E-value: 1.61e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGyralqwn 119
Cdd:cd16031   2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG------- 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71852586 120 agsGGLPENETTFARILQQHGYATGLIGKWHQGVNcasrgdhcHHPLNHGFDYFYGMP 177
Cdd:cd16031  75 ---PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSFP 121
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
40-152 1.12e-37

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


Pssm-ID: 293749 [Multi-domain]  Cd Length: 402  Bit Score: 139.89  E-value: 1.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNtLRTPNIDQLAEEGVRLTQ-HlaAAPLCTPSRAAFLTGRHSFRSGMdASNGYRALQW 118
Cdd:cd16025   2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
                        90       100       110
                ....*....|....*....|....*....|....
gi 71852586 119 NAGSGGLPENETTFARILQQHGYATGLIGKWHQG 152
Cdd:cd16025  78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG 111
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
41-150 1.46e-37

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: 139.18  E-value: 1.46e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTgDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyralQWNA 120
Cdd:cd16027   1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---------HGLR 70
                        90       100       110
                ....*....|....*....|....*....|.
gi 71852586 121 GSGG-LPENETTFARILQQHGYATGLIGKWH 150
Cdd:cd16027  71 SRGFpLPDGVKTLPELLREAGYYTGLIGKTH 101
Sulfatase pfam00884
Sulfatase;
41-335 2.82e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 133.70  E-value: 2.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586    41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGyralqwna 120
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586   121 gsGGLPENETTFARILQQHGYATGLIGKWHQGVNCASrgdhchHPLNHGFDYFYGMPFTLTNDCDPGRPPevdaalraql 200
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ------SPCNLGFDKFFGRNTGSDLYADPPDVP---------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586   201 wgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrWNCILMRNHDVteqpmvlektasLMLK 280
Cdd:pfam00884 135 -----------------------------------------------------YNCSGGGVSDE------------ALLD 149
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71852586   281 EAVSYIERHkHGPFLLFLSLLHVHIPL------------VTTSAFLGKSQHGLYGDNVEEMDWLIAS 335
Cdd:pfam00884 150 EALEFLDNN-DKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGR 215
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
41-154 6.96e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 123.50  E-value: 6.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGR-------HSFRSGMDASNGY 113
Cdd:cd16149   1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRmpsqhgiHDWIVEGSHGKTK 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71852586 114 RALQWnagsgglPENETTFARILQQHGYATGLIGKWHQGVN 154
Cdd:cd16149  81 KPEGY-------LEGQTTLPEVLQDAGYRCGLSGKWHLGDD 114
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
41-191 1.50e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 126.18  E-value: 1.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRAlqwNA 120
Cdd:cd16033   1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGV-LNNVENA---GA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGVNC--ASRGDHCHHPLNHGFDYFY--------------GMPFTLTNDC 184
Cdd:cd16033  77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEEtpLDYGFDEYLPVETTIEYFLadraiemleelaadDKPFFLRVNF 156
                       170
                ....*....|.
gi 71852586 185 ----DPGRPPE 191
Cdd:cd16033 157 wgphDPYIPPE 167
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
40-153 3.32e-28

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: 114.59  E-value: 3.32e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTgDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSG-MDASNGYRALQW 118
Cdd:cd16030   2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGvYDNNSYFRKVAP 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71852586 119 NAgsgglpeneTTFARILQQHGYATGLIGK-WHQGV 153
Cdd:cd16030  81 DA---------VTLPQYFKENGYTTAGVGKiFHPGI 107
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-153 4.69e-27

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 110.35  E-value: 4.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQ-HLAAA---PLCTPSRAAFLTGRHSFRSGMDasngyra 115
Cdd:cd16155   2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMGGwsgAVCVPSRAMLMTGRTLFHAPEG------- 74
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 71852586 116 lqwnaGSGGLPENETTFARILQQHGYATGLIGKWHQGV 153
Cdd:cd16155  75 -----GKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF 107
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-150 1.24e-26

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


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 109.24  E-value: 1.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRalqwN 119
Cdd:cd16152   1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----N 71
                        90       100       110
                ....*....|....*....|....*....|.
gi 71852586 120 AGSggLPENETTFARILQQHGYATGLIGKWH 150
Cdd:cd16152  72 GIP--LPADEKTLAHYFRDAGYETGYVGKWH 100
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
41-197 5.59e-26

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 105.32  E-value: 5.59e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLgTGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRsgmdasngyralqWN 119
Cdd:cd16148   1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY-------------HG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIgkwhqgvncasrGDHCHHPLNHGFD--YFYGMPFTLTNDCDPGRPPE-----V 192
Cdd:cd16148  67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDrgFDTFEDFRGQEGDPGEEGDEraervT 134

                ....*
gi 71852586 193 DAALR 197
Cdd:cd16148 135 DRALE 139
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
41-172 1.77e-25

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 104.93  E-value: 1.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRsgmdasNGYralqWNa 120
Cdd:cd16037   1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WD- 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 71852586 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGvncaSRGDhchhplNHGFDY 172
Cdd:cd16037  70 NADPYDGDVPSWGHALRAAGYETVLIGKLHFR----GEDQ------RHGFRY 111
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-150 4.36e-25

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


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 103.22  E-value: 4.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLGTGDLGCYGN----------NTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDA 109
Cdd:cd16153   1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71852586 110 SNGYralqWNAGSGGLPenetTFARILQQHGYATGLIGKWH 150
Cdd:cd16153  81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH 113
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
41-175 2.59e-24

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


Pssm-ID: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 102.81  E-value: 2.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTL--RTPNIDQLAEEGVRLTqHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRAlqw 118
Cdd:cd16154   1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGVLAVPDELL--- 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71852586 119 nagsggLPENETTFARILQQ--HGYATGLIGKWHQGvncasrGDHCHHPLNHGFDYFYG 175
Cdd:cd16154  77 ------LSEETLLQLLIKDAttAGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAG 123
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
41-178 4.05e-24

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: 103.11  E-value: 4.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLgTGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFrsgmdasnGYRALqWN 119
Cdd:cd16028   1 RNVLFITADQW-RADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSV-WN 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71852586 120 AGSggLPENETTFARILQQHGYATGLIGKWHQGVNcaSRGDHCHHPLNH-------GFDYFYGMPF 178
Cdd:cd16028  71 GTP--LDARHLTLALELRKAGYDPALFGYTDTSPD--PRGLAPLDPRLLsyelampGFDPVDRLDE 132
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
41-172 6.71e-24

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: 100.73  E-value: 6.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM-DasngyralqwN 119
Cdd:cd16032   1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAyD----------N 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71852586 120 AGSggLPENETTFARILQQHGYATGLIGKWH-----QgvncasrgdhchhplNHGFDY 172
Cdd:cd16032  71 AAE--FPADIPTFAHYLRAAGYRTALSGKMHfvgpdQ---------------LHGFDY 111
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
41-162 2.36e-22

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 97.69  E-value: 2.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGR--HsfrsgmdaSNGYRALqw 118
Cdd:cd16150   1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWypH--------VNGHRTL-- 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71852586 119 nagSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHC 162
Cdd:cd16150  71 ---HHLLRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC 111
PRK13759 PRK13759
arylsulfatase; Provisional
40-150 4.03e-22

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 97.43  E-value: 4.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586   40 KPNILLIMADDLgTGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasNGYralqw 118
Cdd:PRK13759   6 KPNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR---VGY----- 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 71852586  119 naGSGGLPENETTFARILQQHGYATGLIGKWH 150
Cdd:PRK13759  77 --GDVVPWNYKNTLPQEFRDAGYYTQCIGKMH 106
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
41-150 4.30e-22

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


Pssm-ID: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 97.45  E-value: 4.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyralqWnA 120
Cdd:cd16156   1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------W-T 69
                        90       100       110
                ....*....|....*....|....*....|
gi 71852586 121 GSGGLPENETTFARILQQHGYATGLIGKWH 150
Cdd:cd16156  70 NCMALGDNVKTIGQRLSDNGIHTAYIGKWH 99
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
40-176 1.47e-20

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: 92.23  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  40 KPNILLIMADDLgtgDLGCYGNNTLRtPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM----DASNGYRA 115
Cdd:cd16147   1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVtnnsPPGGGYPK 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71852586 116 lQWNAGsgglpENETTFARILQQHGYATGLIGKWHQGVNcaSRGDHCHHPLnhGFDYFYGM 176
Cdd:cd16147  77 -FWQNG-----LERSTLPVWLQEAGYRTAYAGKYLNGYG--VPGGVSYVPP--GWDEWDGL 127
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
41-147 3.96e-17

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: 79.77  E-value: 3.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRL-TQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRALQWN 119
Cdd:cd00016   1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGY-TGNGSADPELP 79
                        90       100
                ....*....|....*....|....*...
gi 71852586 120 AGSGGLPENETTFARILQQHGYATGLIG 147
Cdd:cd00016  80 SRAAGKDEDGPTIPELLKQAGYRTGVIG 107
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
41-150 3.44e-14

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: 72.63  E-value: 3.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMAD------DLGTGDLGcygnntLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDaSNGYR 114
Cdd:cd16035   1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT-DTLGS 73
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71852586 115 ALQWNAgSGGLPenetTFARILQQHGYATGLIGKWH 150
Cdd:cd16035  74 PMQPLL-SPDVP----TLGHMLRAAGYYTAYKGKWH 104
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
41-148 1.92e-09

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: 58.71  E-value: 1.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSfrsgmdasngYRALQWNa 120
Cdd:cd16171   1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT----------HLTESWN- 69
                        90       100
                ....*....|....*....|....*...
gi 71852586 121 GSGGLPENETTFARILQQHGYATGLIGK 148
Cdd:cd16171  70 NYKGLDPNYPTWMDRLEKHGYHTQKYGK 97
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
33-176 2.70e-04

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 43.10  E-value: 2.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  33 PKTANAFKPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAaaplctpsraaflTGRHSFRS------G 106
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYS-------------QGGRTSRGefavltG 293
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586 107 MDASNGYRALQwnagsggLPENET--TFARILQQHGYATgligkwhqgvncasrgdHCHHP------------LNHGFDY 172
Cdd:COG1368 294 LPPLPGGSPYK-------RPGQNNfpSLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFDE 349

                ....
gi 71852586 173 FYGM 176
Cdd:COG1368 350 FYDR 353
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
41-176 6.87e-04

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: 41.13  E-value: 6.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71852586  41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRA--AFLTGRHSFRSGMDASNGYRalqw 118
Cdd:cd16015   1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK---- 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71852586 119 nagsgglPENETTFARILQQHGYATGLIgkwhqgvncasrgdHCHHP---------LNHGFDYFYGM 176
Cdd:cd16015  77 -------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFYDL 122
 
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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