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Conserved domains on  [gi|1372261824|ref|NP_001348906|]
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arylsulfatase G isoform 3 [Mus musculus]

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 ...
 1-336 2.29e-144

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 cd16161:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 383  Bit Score: 414.94  E-value: 2.29e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqp 80
Cdd:cd16161   101 MIGKWHLGQREAYLPNSRGFDYYFGIPFSHD------------------------------------------------- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 vnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQS-LYRASLREMDSLVGQIKDKVDHV-A 158
Cdd:cd16161   132 ---SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDALQEMDDLVGQIMDAVKHAgL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 159 RENTLLWFTGDNGPWAQKCELAgsVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPT 238
Cdd:cd16161   209 KDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPT 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 239 VIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGeYGALQTVRLNHYKAFYITGGAKACDGSVGPEQHHV 318
Cdd:cd16161   287 VVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAHYATGGALACCGSTGPKLYHD 365

                         330
                  ....*....|....*...
gi 1372261824 319 APLIFNLEDAADEGMPLQ 336
Cdd:cd16161   366 PPLLFDLEVDPAESFPLT 383
 
Name Accession Description Interval E-value
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 1-336 2.29e-144

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: 414.94  E-value: 2.29e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqp 80
Cdd:cd16161   101 MIGKWHLGQREAYLPNSRGFDYYFGIPFSHD------------------------------------------------- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 vnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQS-LYRASLREMDSLVGQIKDKVDHV-A 158
Cdd:cd16161   132 ---SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDALQEMDDLVGQIMDAVKHAgL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 159 RENTLLWFTGDNGPWAQKCELAgsVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPT 238
Cdd:cd16161   209 KDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPT 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 239 VIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGeYGALQTVRLNHYKAFYITGGAKACDGSVGPEQHHV 318
Cdd:cd16161   287 VVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAHYATGGALACCGSTGPKLYHD 365

                         330
                  ....*....|....*...
gi 1372261824 319 APLIFNLEDAADEGMPLQ 336
Cdd:cd16161   366 PPLLFDLEVDPAESFPLT 383
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
86-299 3.97e-43

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 154.65  E-value: 3.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  86 LAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHP-----------------------QRQSLYRASLRE 142
Cdd:COG3119   129 LTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEE 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 143 MDSLVGQIkdkVDHVAR----ENTLLWFTGDNGPWaqkcelagsvgpfFGLWqTHQGGsptKQTTWEGGHRVPALAYWPG 218
Cdd:COG3119   209 VDDQVGRL---LDALEElglaDNTIVVFTSDNGPS-------------LGEH-GLRGG---KGTLYEGGIRVPLIVRWPG 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 219 RVPANVTSTALLSLLDIFPTVIALAGASLPPnrKFDGRDVSEVLFGKSQMGHRVLFHpnsgAAGEYGALQTVRLNHYKAF 298
Cdd:COG3119   269 KIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--DLDGRSLLPLLTGEKAEWRDYLYW----EYPRGGGNRAIRTGRWKLI 342


                  .
gi 1372261824 299 Y 299
Cdd:COG3119   343 R 343
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
269-389 1.93e-32

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 118.57  E-value: 1.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 269 GHRVLFHpNSGAAgeygaLQTVRLNHYKAFYITG-----GAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQKGSPEYQ 343
Cdd:pfam14707   2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1372261824 344 EVLQQVTRALADVLQDI--ADDNSSRADYTQDPSVIPCCnPYQTTCRC 389
Cdd:pfam14707  76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
PRK13759 PRK13759
arylsulfatase; Provisional
 59-359 9.08e-12

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 66.23  E-value: 9.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  59 GRDCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLLYVGLAHMHVPLSvtPPLA-------- 128
Cdd:PRK13759  162 GWDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFLKMSFARPHSPYD--PPKRyfdmykda 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 129 ----------------HPQRQSL------------------YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpw 173
Cdd:PRK13759  229 dipdphigdweyaedqDPEGGSIdalrgnlgeeyarraraaYYGLITHIDHQIGRFLQALKEFGlLDNTIILFVSDHG-- 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 174 aqkcELAGSvgpfFGLWQthqggsptKQTTWEGGHRVPALAYWPG---RVPANVTSTALLSLLDIFPTVIALAGASLPPN 250
Cdd:PRK13759  307 ----DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 251 rkFDGRDVSEVLFGKSQmGHRVLFHpnsgaaGEYGalqtvrlNHYKAF-YITGGA-KACDGSV-GPEQhhvaplIFNLED 327
Cdd:PRK13759  371 --VDGRSLKNLIFGQYE-GWRPYLH------GEHA-------LGYSSDnYLTDGKwKYIWFSQtGEEQ------LFDLKK 428

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1372261824 328 AADEGMPLQkGSPEYQEVLQQVTRALADVLQD 359
Cdd:PRK13759  429 DPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
 
Name Accession Description Interval E-value
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 1-336 2.29e-144

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: 414.94  E-value: 2.29e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqp 80
Cdd:cd16161   101 MIGKWHLGQREAYLPNSRGFDYYFGIPFSHD------------------------------------------------- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 vnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQS-LYRASLREMDSLVGQIKDKVDHV-A 158
Cdd:cd16161   132 ---SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDALQEMDDLVGQIMDAVKHAgL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 159 RENTLLWFTGDNGPWAQKCELAgsVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPT 238
Cdd:cd16161   209 KDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPT 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 239 VIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGeYGALQTVRLNHYKAFYITGGAKACDGSVGPEQHHV 318
Cdd:cd16161   287 VVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAHYATGGALACCGSTGPKLYHD 365

                         330
                  ....*....|....*...
gi 1372261824 319 APLIFNLEDAADEGMPLQ 336
Cdd:cd16161   366 PPLLFDLEVDPAESFPLT 383
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 1-332 9.08e-111

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: 329.91  E-value: 9.08e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDMGCTDAPGYNYPPCPAcpqrdglwrnpgrdcytdvalPLYENLNIVEQP 80
Cdd:cd16026   101 LVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP---------------------PLMENEEVIEQP 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 VNLSGLAQKYAERAVEFIEQAStsGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVDHV-AR 159
Cdd:cd16026   160 ADQSSLTQRYTDEAVDFIERNK--DQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELgLE 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 160 ENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQGGsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTV 239
Cdd:cd16026   238 ENTLVIFTSDNGPWLEYGGHGGSAGPL-------RGG---KGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTL 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 240 IALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGaageyGALQTVRLNHYKAFYITGGAKACDGSVGPEQHHVA 319
Cdd:cd16026   308 AALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDG-----GDLQAVRSGRWKLHLPTTYRTGTDPGGLDPTKLEP 382

                         330
                  ....*....|...
gi 1372261824 320 PLIFNLEDaaDEG 332
Cdd:cd16026   383 PLLYDLEE--DPG 393
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
 1-389 5.06e-67

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: 220.01  E-value: 5.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLG--HHGSYHPNFRGFDYYFGIPYSNDMGctdaPGYN---YPPCPACpqrDGLWRnPGrdcytDVALPLYENLN 75
Cdd:cd16158   101 MVGKWHLGvgLNGTYLPTHQGFDHYLGIPYSHDQG----PCQNltcFPPNIPC---FGGCD-QG-----EVPCPLFYNES 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  76 IVEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVD 155
Cdd:cd16158   168 IVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLK 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 156 HVA-RENTLLWFTGDNGPWAQKCELAGSVgpffGLWQTHQGgsptkqTTWEGGHRVPALAYWPGRVPANVTStALLSLLD 234
Cdd:cd16158   248 ENGiDNNTLVFFTSDNGPSTMRKSRGGNA----GLLKCGKG------TTYEGGVREPAIAYWPGRIKPGVTH-ELASTLD 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 235 IFPTVIALAGASLpPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGEYGALqTVRLNHYKAFYITGGA--------KA 306
Cdd:cd16158   317 ILPTIAKLAGAPL-PNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWGKYKAHFYTQGAahsgttpdKD 394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 307 CDGSvGPEQHHVAPLIFNLEDAADEGMPLQKGsPEYQEVLQQVtRALADVLQDIADDNSSRADYTQDPSVIPCCN----P 382
Cdd:cd16158   395 CHPS-AELTSHDPPLLFDLSQDPSENYNLLGL-PEYNQVLKQI-QQVKERFEASMKFGESEINKGEDPALEPCCKpgctP 471


                  ....*..
gi 1372261824 383 YQTTCRC 389
Cdd:cd16158   472 KPSCCQC 478
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
 1-354 1.73e-66

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: 217.68  E-value: 1.73e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLG-----HHGSYH-PNFRGFDYY-FGIPYSNDMGCtDAPGYNYPpcpacpqrdglWRNPGRdCYtdvalpLYEN 73
Cdd:cd16160   103 MVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWAC-DDTGRHVD-----------FPDRSA-CF------LYYN 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  74 LNIVEQPVNLSGLAQKYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDK 153
Cdd:cd16160   164 DTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDT 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 154 -VDHVARENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQGGsptKQTTWEGGHRVPALAYWPGRVPANVtSTALLSL 232
Cdd:cd16160   242 lVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGL-------KGG---KGNSWEGGIRVPFIAYWPGTIKPRV-SHEVVST 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 233 LDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR-VLFHPNSgaageygALQTVRLNHYKAFYITG--------G 303
Cdd:cd16160   311 MDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDdILYYCCS-------RLMAVRYGSYKIHFKTQplpsqeslD 383

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1372261824 304 AKACDG---------SVGPEQH---HVAPLIFNLEDAADEGMPLQkgSPEYQEVLQQVTRALA 354
Cdd:cd16160   384 PNCDGGgplsdyivcYDCEDECvtkHNPPLIFDVEKDPGEQYPLQ--PSVYEHMLEAVEKLIA 444
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
 2-361 7.40e-64

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: 212.53  E-value: 7.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   2 IGKWHLGHH------GSYHPNFRGFDYYFGIPYSNDMGCTDAPG--YNYPPCPACPQRDGL------------------W 55
Cdd:cd16159   107 IGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeYDLSFDPLFPLLTAFvlitaltiflllylgavsK 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  56 RnPGRDCYTDVALP-----------------LYENLNIVEQPVNLSGLAQKYAERAVEFIEQasTSGRPFLLYVGLAHMH 118
Cdd:cd16159   187 R-FFVFLLILSLLFislfflllitnryfnciLMRNHEVVEQPMSLENLTQRLTKEAISFLER--NKERPFLLVMSFLHVH 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 119 VPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPWAqkcELAGSVGPFFGLWQTHQGGS 197
Cdd:cd16159   264 TALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYFTSDNGGHL---EEISVGGEYGGGNGGIYGGK 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 198 ptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMG-HRVLFH- 275
Cdd:cd16159   341 --KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSpHEFLFHy 418

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 276 -----------PNSGAAgeygalqtvrlnHYKAFYIT-----GGAKACDGSVGP-----EQHHVAPLIFNLEDAADEGMP 334
Cdd:cd16159   419 cgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEGCCGTLLCRcfgdsVTHHDPPLLFDLSADPSESNP 486

                         410       420
                  ....*....|....*....|....*..
gi 1372261824 335 LQKGSPEYQEVLQQVTRALADVLQDIA 361
Cdd:cd16159   487 LDPTDEPYQEIIKKILEAVAEHQSSIE 513
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 1-355 1.85e-59

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: 199.62  E-value: 1.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGIPysndmGCTDAPGYN--YPPCPAcpQRDglWRNPGRdcytdvalpLYENLNIvE 78
Cdd:cd16157   108 IVGKWHLGHRPQYHPLKHGFDEWFGAP-----NCHFGPYDNkaYPNIPV--YRD--WEMIGR---------YYEEFKI-D 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  79 QPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVDHVA 158
Cdd:cd16157   169 KKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 159 -RENTLLWFTGDNG-PWAQKCELAGSVGPFFGlwqthqggspTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIF 236
Cdd:cd16157   249 iENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLF 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 237 PTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSgaageygALQTVRLNHYKAFYIT---------GGAKAC 307
Cdd:cd16157   319 TTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMAVRLGQYKAHFWTwsnsweefrKGINFC 391

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1372261824 308 DGSVGP-------EQHHVAPLIFNLEDAADEGMPLQKGSPEYQEVLQQVTRALAD 355
Cdd:cd16157   392 PGQNVPgvtthnqTDHTKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQ 446
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 1-326 7.69e-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: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 179.65  E-value: 7.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGIPYSNdmgctdapgynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqp 80
Cdd:cd16142   101 QFGKWHLGDEDGRLPTDHGFDEFYGNLYHT-------------------------------------------------- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 vnlsgLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAH-PQRQSLYRASLREMDSLVGQIKDKVDHVA- 158
Cdd:cd16142   131 -----IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGkSSGKGKYADSMVELDDHVGQILDALDELGi 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 159 RENTLLWFTGDNGPWAQKCELAGSvGPFFGlwqthqggspTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPT 238
Cdd:cd16142   206 ADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPT 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 239 VIALAGASLPP------NRKFDGRDVSEVLFGKS-QMGHRVLFHpnsGAAGEYGAlqtVRLNHYKAFYITGGAKACDGSV 311
Cdd:cd16142   275 LAALAGAPDPKdkllgkDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---VRWKNWKVHFKAQEDTGGPTGE 348

                         330
                  ....*....|....*
gi 1372261824 312 GPEQHHVaPLIFNLE 326
Cdd:cd16142   349 PFYVLTF-PLIFNLR 362
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
86-299 3.97e-43

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 154.65  E-value: 3.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  86 LAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHP-----------------------QRQSLYRASLRE 142
Cdd:COG3119   129 LTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEE 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 143 MDSLVGQIkdkVDHVAR----ENTLLWFTGDNGPWaqkcelagsvgpfFGLWqTHQGGsptKQTTWEGGHRVPALAYWPG 218
Cdd:COG3119   209 VDDQVGRL---LDALEElglaDNTIVVFTSDNGPS-------------LGEH-GLRGG---KGTLYEGGIRVPLIVRWPG 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 219 RVPANVTSTALLSLLDIFPTVIALAGASLPPnrKFDGRDVSEVLFGKSQMGHRVLFHpnsgAAGEYGALQTVRLNHYKAF 298
Cdd:COG3119   269 KIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--DLDGRSLLPLLTGEKAEWRDYLYW----EYPRGGGNRAIRTGRWKLI 342


                  .
gi 1372261824 299 Y 299
Cdd:COG3119   343 R 343
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 1-296 7.71e-43

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: 154.62  E-value: 7.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGipysndMGCTDAPGYNYPPCPACPqrdGLWRNPGRDCYtdvalplyenlniveqp 80
Cdd:cd16144   112 HFGKWHLGGEGGYGPEDQGFDVNIG------GTGNGGPPSYYFPPGKPN---PDLEDGPEGEY----------------- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 vnlsgLAQKYAERAVEFIEQAStsGRPFLLYvgLAH--MHVPLSVTP-----------PLAHPQRQSLYRASLREMDSLV 147
Cdd:cd16144   166 -----LTDRLTDEAIDFIEQNK--DKPFFLY--LSHyaVHTPIQARPeliekyekkkkGLRKGQKNPVYAAMIESLDESV 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 148 GQIKDKVDHVA-RENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQGGsptKQTTWEGGHRVPALAYWPGRVPANVTS 226
Cdd:cd16144   237 GRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPL-------RGG---KGSLYEGGIRVPLIVRWPGVIKPGSVS 306

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372261824 227 TALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR--VLFH-PN-SGAAGEYGAlqTVRLNHYK 296
Cdd:cd16144   307 DVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraLFWHfPHyHGQGGRPAS--AIRKGDWK 378
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 1-305 2.63e-39

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: 145.04  E-value: 2.63e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSY-HPNFRGFDYYFGIpysndMGCTDAPGYnYPPCpacpqrdgLWRNPGRdcytdvaLPLYENLNIVEQ 79
Cdd:cd16145    99 AFGKWGLGGPGTPgHPTKQGFDYFYGY-----LDQVHAHNY-YPEY--------LWRNGEK-------VPLPNNVIPPLD 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  80 PVNLSGLAQK-YAE-----RAVEFIEQAStsGRPFLLYVGL----AHMHVP-----------LSVTPPLAHPQRQSLYRA 138
Cdd:cd16145   158 EGNNAGGGGGtYSHdlftdEALDFIRENK--DKPFFLYLAYtlphAPLQVPddgpykykpkdPGIYAYLPWPQPEKAYAA 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 139 SLREMDSLVGQIKDKV-DHVARENTLLWFTGDNGP-----WAQKCELAGSVGPFFGLwqthqggsptKQTTWEGGHRVPA 212
Cdd:cd16145   236 MVTRLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----------KRSLYEGGIRVPF 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 213 LAYWPGRVPANVTSTALLSLLDIFPTVIALAGASlPPNRKfDGRDVSEVLFGKS-QMGHRVLFHpnsgAAGEYGALQTVR 291
Cdd:cd16145   306 IARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAE-PPEDI-DGISLLPTLLGKPqQQQHDYLYW----EFYEGGGAQAVR 379

                         330
                  ....*....|....
gi 1372261824 292 LNHYKAFYITGGAK 305
Cdd:cd16145   380 MGGWKAVRHGKKDG 393
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 1-327 4.07e-39

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: 143.88  E-value: 4.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLG-----------HHGSYH-----------PNFRGFDYYFGIPYSNdmgctdapgynyppcpacpqrdglwrnp 58
Cdd:cd16143   101 MVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPASE---------------------------- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  59 grdcytdvALPLyenlniveqpvnlsgLAQKyaerAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRA 138
Cdd:cd16143   153 --------VLPT---------------LTDK----AVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGD 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 139 SLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGPwaqkcelagSVGPFFGLWQtHQGGSPT------KQTTWEGGHRVP 211
Cdd:cd16143   206 FVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP---------SPYADYKELE-KFGHDPSgplrgmKADIYEGGHRVP 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 212 ALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGeygalQTVR 291
Cdd:cd16143   276 FIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGS-----FAIR 350

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1372261824 292 LNHYKafYITGGAKacDGSVGPEQHHVAPL----IFNLED 327
Cdd:cd16143   351 KGDWK--LIDGTGS--GGFSYPRGKEKLGLppgqLYNLST 386
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 1-296 3.33e-37

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: 139.22  E-value: 3.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGIpysndmgctdapgynyppcpacpqRDGLWRNPGRDCYTDVALPLYENLNIVEQp 80
Cdd:cd16146    96 IFGKWHLGDNYPYRPQDRGFDEVLGH------------------------GGGGIGQYPDYWGNDYFDDTYYHNGKFVK- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 vnlsglAQKYA-----ERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLRE-------MDSLVG 148
Cdd:cd16146   151 ------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAfygmienIDDNVG 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 149 QIKDKVDHV-ARENTLLWFTGDNGPWaqkcelagsvGPFFGLWQTHQGGspTKQTTWEGGHRVPALAYWPGRVPANVTST 227
Cdd:cd16146   223 RLLAKLKELgLEENTIVIFMSDNGPA----------GGVPKRFNAGMRG--KKGSVYEGGHRVPFFIRWPGKILAGKDVD 290

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372261824 228 ALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQM-GHRVLF--HPNSGAAGEYGALQTVRLNHYK 296
Cdd:cd16146   291 TLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwPERTLFthSGRWPPPPKKKRNAAVRTGRWR 362
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 42-257 6.93e-35

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: 128.32  E-value: 6.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  42 YPPCPAC-PQRDGLW--RNPGRdcyTDVALPLYENLNIVEQPVNLSGLAQK--YA--------ERAVEFIEQASTSgRPF 108
Cdd:cd16022    43 YVASPVCsPSRASLLtgRYPHR---HGVRGNVGNGGGLPPDEPTLAELLKEagYRtaligkwhDEAIDFIERRDKD-KPF 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 109 LLYVGLAHMHvplsvtPPLAhpqrqslYRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpwaqkcelaGSVGPFF 187
Cdd:cd16022   119 FLYVSFNAPH------PPFA-------YYAMVSAIDDQIGRILDALEeLGLLDNTLIVFTSDHG---------DMLGDHG 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 188 GLWQthqggsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPpnRKFDGRD 257
Cdd:cd16022   177 LRGK--------KGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
269-389 1.93e-32

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 118.57  E-value: 1.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 269 GHRVLFHpNSGAAgeygaLQTVRLNHYKAFYITG-----GAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQKGSPEYQ 343
Cdd:pfam14707   2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1372261824 344 EVLQQVTRALADVLQDI--ADDNSSRADYTQDPSVIPCCnPYQTTCRC 389
Cdd:pfam14707  76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 90-302 1.53e-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: 123.09  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  90 YAERAVEFIEQAStsGRPFLLYVGLAHMHVPLSVTPPLAHP--------QRQSLYRASLREMDSLVGQIKDKVDHVA-RE 160
Cdd:cd16151   155 FADFLIDFIERNK--DQPFFAYYPMVLVHDPFVPTPDSPDWdpddkrkkDDPEYFPDMVAYMDKLVGKLVDKLEELGlRE 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 161 NTLLWFTGDNGpwaqkcelagSVGPFFGLW--QTHQGGsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPT 238
Cdd:cd16151   233 NTIIIFTGDNG----------THRPITSRTngREVRGG---KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPT 299

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372261824 239 VIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGEYGALQTVRLNHYKaFYITG 302
Cdd:cd16151   300 LAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRFVRTKRYK-LYADG 362
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
 1-302 1.45e-30

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: 120.73  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYH-PNFRGFDYYFGiPYSndmGCTDapGYNYPPCPACP-QRDGLWRN-----PGRDCY-TDValplye 72
Cdd:cd16029    99 LVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDyGNDDLRDNeepawDYNGTYsTDL------ 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  73 nlniveqpvnlsglaqkYAERAVEFIEQASTSgRPFLLYVGLAHMHVPLSVTPPLA-----------HPQRQsLYRASLR 141
Cdd:cd16029   167 -----------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYAdpyedkfahikDEDRR-TYAAMVS 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 142 EMDSLVGQIKDKVDHVAR-ENTLLWFTGDNGPWAQKCElAGSVGPFFGlwqthqggspTKQTTWEGGHRVPALAYWPGRV 220
Cdd:cd16029   228 ALDESVGNVVDALKAKGMlDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNTLWEGGVRVPAFVWSPLLP 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 221 P-ANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR-VLFHPNSGAAGEYGAlqTVRLNHYKaf 298
Cdd:cd16029   297 PkRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDITRTTGGA--AIRVGDWK-- 372


                  ....
gi 1372261824 299 YITG 302
Cdd:cd16029   373 LIVG 376
Sulfatase pfam00884
Sulfatase;
1-245 1.23e-23

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 99.42  E-value: 1.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFG-IPYSNDMGctdapgynyppcpACPQRDGLWRNPGrdCYTDValplyenlniveq 79
Cdd:pfam00884  95 AIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYA-------------DPPDVPYNCSGGG--VSDEA------------- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  80 pvnlsglaqkYAERAVEFIEQAStsgRPFLLYVGLAHMHVPLSVTP----------PLAHPQRQSL--YRASLREMDSLV 147
Cdd:pfam00884 147 ----------LLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDrypekyatfkPSSCSEEQLLnsYDNTLLYTDDAI 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 148 GQIKDKVDHVA-RENTLLWFTGDNGPwaqkcelagSVGPFfglwQTHQGGSPTKQTtWEGGHRVPALAYWPGRVPANVTS 226
Cdd:pfam00884 214 GRVLDKLEENGlLDNTLVVYTSDHGE---------SLGEG----GGYLHGGKYDNA-PEGGYRVPLLIWSPGGKAKGQKS 279

                         250
                  ....*....|....*....
gi 1372261824 227 TALLSLLDIFPTVIALAGA 245
Cdd:pfam00884 280 EALVSHVDLFPTILDLAGI 298
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 89-274 1.54e-23

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: 100.66  E-value: 1.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  89 KYAERAVEFIEQAStSGRPFLLYVGLAHMHV-------------PLSVTPPLAHPQ----RQSL--YRASLREMDSLVGQ 149
Cdd:cd16027   126 DYASNAADFLNRAK-KGQPFFLWFGFHDPHRpyppgdgeepgydPEKVKVPPYLPDtpevREDLadYYDEIERLDQQVGE 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 150 IKDKVD-HVARENTLLWFTGDNGpwaqkcelagsvGPFFGlwqthqggspTKQTTWEGGHRVPALAYWPGRVPANVTSTA 228
Cdd:cd16027   205 ILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------AKGTLYDSGLRVPLIVRWPGKIKPGSVSDA 262

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1372261824 229 LLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKSQMGHRVLF 274
Cdd:cd16027   263 LVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVF 306
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 91-327 1.19e-21

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 94.53  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  91 AERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAhpqrqSLYRASLR--------EMDSLVGQIKDKVDHVA-REN 161
Cdd:cd16037   116 TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFY-----DLYVRRARaayyglveFLDENIGRVLDALEELGlLDN 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 162 TLLWFTGDNGpwaqkcELAGSvgpfFGLWQthqggsptKQTTWEGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIA 241
Cdd:cd16037   191 TLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILE 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 242 LAGASLPPNRkfDGRDVSEVLFGKSQMGHRVL--FHpnsgAAGEYGALQTVRLNHYKafYItggakacdgsvgpeqHHV- 318
Cdd:cd16037   252 AAGAPPPPDL--DGRSLLPLAEGPDDPDRVVFseYH----AHGSPSGAFMLRKGRWK--YI---------------YYVg 308

                         250
                  ....*....|
gi 1372261824 319 -APLIFNLED 327
Cdd:cd16037   309 yPPQLFDLEN 318
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 2-291 2.08e-20

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: 91.86  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   2 IGKWHL-GHHGSYH--------PNFR-GFDYYFGipysndMGCTDapGYNYPPcpacpqrdgLWRNPGRDCYTDVALPLY 71
Cdd:cd16034    96 IGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNPH---------YYDDDGKRIYIKGYSPDA 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  72 EnlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYV--GLAH------------MHVPLSVT----PPLAHPQRQ 133
Cdd:cd16034   159 E------------------TDLAIEYLENQADKDKPFALVLswNPPHdpyttapeeyldMYDPKKLLlrpnVPEDKKEEA 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 134 SL------YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpffglwqtHqgGSPTKQTTWEG 206
Cdd:cd16034   221 GLredlrgYYAMITALDDNIGRLLDALKELGlLENTIVVFTSDHG------DMLGS----------H--GLMNKQVPYEE 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 207 GHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGasLPPNRKFDGRDVSEVLFGKSQMGHR----VLFHPNSGAA- 281
Cdd:cd16034   283 SIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDsvllQCFVPFGGGSa 360

                         330
                  ....*....|...
gi 1372261824 282 ---GEYGALQTVR 291
Cdd:cd16034   361 rdgGEWRGVRTDR 373
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 42-260 7.83e-20

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: 88.06  E-value: 7.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  42 YPPCPAC-PQRDGL-------------WRNPGRDCYTDVALPLYENL----NIVEQPVNLSGLAQKY--AERAVEFIEQA 101
Cdd:cd16149    43 FCTSPVCsPARASLltgrmpsqhgihdWIVEGSHGKTKKPEGYLEGQttlpEVLQDAGYRCGLSGKWhlGDDAADFLRRR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 102 STSGRPFLLYVGLAHMHVPLSvtpplahpqrqslYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcela 180
Cdd:cd16149   123 AEAEKPFFLSVNYTAPHSPWG-------------YFAAVTGVDRNVGRLLDELEELGlTENTLVIFTSDNG--------- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 181 gsvgpfF-----GLWqtHQGGSPTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDG 255
Cdd:cd16149   181 ------FnmghhGIW--GKGNGTFPLNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252


                  ....*
gi 1372261824 256 RDVSE 260
Cdd:cd16149   253 RSFAD 257
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 1-274 1.68e-18

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: 86.43  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGsYHPNfRGFDYYFGIPysndmgctdAPGYNYPPcpacpqrdglwrnpgrdcytdvalPLYENLNIVEQP 80
Cdd:cd16031    97 FIGKWHLGSGG-DLPP-PGFDYWVSFP---------GQGSYYDP------------------------EFIENGKRVGQK 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 VNLSGLaqkYAERAVEFIEQAStSGRPFLLYVG--LAH---------------MHVPLSVT---------PPLAHPQRQS 134
Cdd:cd16031   142 GYVTDI---ITDKALDFLKERD-KDKPFCLSLSfkAPHrpftpaprhrglyedVTIPEPETfddddyagrPEWAREQRNR 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 135 L--------------------YRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpwaqkcelagsvgpFF----GL 189
Cdd:cd16031   218 IrgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEeQGLADNTIIIYTSDNG--------------FFlgehGL 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 190 wqthqGGsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKSQMG 269
Cdd:cd16031   284 -----FD---KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVD 353


                  ....*
gi 1372261824 270 HRVLF 274
Cdd:cd16031   354 WRKEF 358
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
 90-275 4.13e-17

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: 82.11  E-value: 4.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  90 YAERAVEFIEQASTSGRPFLLYV--GLAH--MHVP-------------------------------------LSVTPPLA 128
Cdd:cd16025   121 LTDKAIEYIDEQKAPDKPFFLYLafGAPHapLQAPkewidkykgkydagwdalreerlerqkelglipadtkLTPRPPGV 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 129 HP-------------QRQSLYRASLREMDSLVGQIkdkVDHVAR----ENTLLWFTGDNGP-----WAQkcelAGSvGPF 186
Cdd:cd16025   201 PAwdslspeekkleaRRMEVYAAMVEHMDQQIGRL---IDYLKElgelDNTLIIFLSDNGAsaepgWAN----ASN-TPF 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 187 FGlwqthqggspTKQTTWEGGHRVPALAYWPGRVPA-NVTSTALLSLLDIFPTVIALAGASLP------PNRKFDGRDVS 259
Cdd:cd16025   273 RL----------YKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYPktvngvPQLPLDGVSLL 342

                         250       260
                  ....*....|....*....|....*..
gi 1372261824 260 EVLFGKSQ-----------MGHRVLFH 275
Cdd:cd16025   343 PTLDGAAApsrrrtqyfelFGNRAIRK 369
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 90-353 5.25e-17

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: 81.46  E-value: 5.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  90 YAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPL-----------------AHP---------------------- 130
Cdd:cd16155   107 FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYldmyppetiplpenflpQHPfdngegtvrdeqlapfprtpea 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 131 --QRQSLYRASLREMDSLVGQIKDKVDHVAR-ENTLLWFTGDNGpwaqkceLA-GSvgpfFGLwqthQGgsptKQTTWEG 206
Cdd:cd16155   187 vrQHLAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG-------LAvGS----HGL----MG----KQNLYEH 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 207 GHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPnrKFDGRDVSEVLFGKSQMGHRVLFhpnsgaaGEYGA 286
Cdd:cd16155   248 SMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE--SVEGKSLLPVIRGEKKAVRDTLY-------GAYRD 317

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372261824 287 LQ-TVRLNHYKAFYITGGAKacdgsvgpeqhhvAPLIFNLEDAADEGMPLQkGSPEYQEVLQQVTRAL 353
Cdd:cd16155   318 GQrAIRDDRWKLIIYVPGVK-------------RTQLFDLKKDPDELNNLA-DEPEYQERLKKLLAEL 371
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 105-327 3.28e-16

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: 78.77  E-value: 3.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 105 GRPFLLYVGLAHMHVPLSVTPPL----AHPQRQSLYrASLREMDSLVGQIKDKVDHV-ARENTLLWFTGDNGpwaqkcEL 179
Cdd:cd16032   132 GRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYY-GMVSYVDDKVGQLLDTLERTgLADDTIVIFTSDHG------DM 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 180 AGSVGpffgLWQthqggsptKQTTWEGGHRVPALAYWPG-----RVPANVtstallSLLDIFPTVIALAGASLPPNR-KF 253
Cdd:cd16032   205 LGERG----LWY--------KMSFFEGSARVPLIISAPGrfaprRVAEPV------SLVDLLPTLVDLAGGGTAPHVpPL 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 254 DGRDVSEVLFGKSQMGHRVLFhpnsgaaGEYGA------LQTVRLNHYKAFYItggakacdgsvgpeqHHVAPLIFNLED 327
Cdd:cd16032   267 DGRSLLPLLEGGDSGGEDEVI-------SEYLAegavapCVMIRRGRWKFIYC---------------PGDPDQLFDLEA 324
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 87-257 3.34e-16

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: 77.97  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  87 AQKYAERAVEFIEQASTSgRPFLLYVglaHM---HVPlsvtpplahpqrqSLYRASLREMDSLVGQIKDKVD-HVARENT 162
Cdd:cd16148   130 AERVTDRALEWLDRNADD-DPFFLFL---HYfdpHEP-------------YLYDAEVRYVDEQIGRLLDKLKeLGLLEDT 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 163 LLWFTGDNGpwaqkcELagsvgpFF--GLWQTHqGGSPTKQTTwegghRVPALAYWPGRVPANVTStALLSLLDIFPTVI 240
Cdd:cd16148   193 LVIVTSDHG------EE------FGehGLYWGH-GSNLYDEQL-----HVPLIIRWPGKEPGKRVD-ALVSHIDIAPTLL 253

                         170
                  ....*....|....*..
gi 1372261824 241 ALAGasLPPNRKFDGRD 257
Cdd:cd16148   254 DLLG--VEPPDYSDGRS 268
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 1-256 3.38e-16

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: 79.52  E-value: 3.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGK----WHLGHHGSYHPnfRGFDYYFGI-------PYSNDMGCTDAPGYNYPpcpacpqrdglwrnpgRDCYTDValp 69
Cdd:cd16147   100 YAGKylngYGVPGGVSYVP--PGWDEWDGLvgnstyyNYTLSNGGNGKHGVSYP----------------GDYLTDV--- 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  70 lyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVG---------LAHMHVPLSVTPPLAHP---------- 130
Cdd:cd16147   159 --------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftPAPRYANLFPNVTAPPRpppnnpdvsd 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 131 -----------------QRQSLYRA---SLREMDSLVGQIKDKVDHVAR-ENTLLWFTGDNG-PWAQkcelagsvgpfFG 188
Cdd:cd16147   219 kphwlrrlpplnptqiaYIDELYRKrlrTLQSVDDLVERLVNTLEATGQlDNTYIIYTSDNGyHLGQ-----------HR 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372261824 189 LWqthqggsPTKQTTWEGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPNrkFDGR 256
Cdd:cd16147   288 LP-------PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 77-260 2.76e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 72.41  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  77 VEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPlsVTPPLAHPQRqSLYRASLREMDSLVGQIKDKVD- 155
Cdd:cd16153   114 LEAFQRYLKNANQSYKSFWGKIAKGADSDKPFFVRLSFLQPHTP--VLPPKEFRDR-FDYYAFCAYGDAQVGRAVEAFKa 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 156 ---HVARENTLLWFTGDNGpwaqkcelagsvgpffglWQTHQGGSPTKQTTWEGGHRVPALAYWPGR--VPANVTSTALL 230
Cdd:cd16153   191 yslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQSHRVPLIVVSSDKlkAPAGKVRHDFV 252

                         170       180       190
                  ....*....|....*....|....*....|
gi 1372261824 231 SLLDIFPTVIALAGASLPPNRKFDGRDVSE 260
Cdd:cd16153   253 EFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 1-248 2.92e-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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 73.54  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   1 MIGKWHLGHHGSYHPNFRGFDYYFGIpysndmgctdapgynyppcpacpqrdglwrNPGrdcytdvALPLYENLNIVEQP 80
Cdd:cd16154    99 VIGKWHLGGNDNSPNNPGGIPYYAGI------------------------------LGG-------GVQDYYNWNLTNNG 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  81 VNLSglAQKYA-----ERAVEFIEQASTsgrPFLLYVGLAHMHVPLSVTPPLAHPQRQS------------LYRASLREM 143
Cdd:cd16154   142 QTTN--STEYAttkltNLAIDWIDQQTK---PWFLWLAYNAPHTPFHLPPAELHSRSLLgdsadieanprpYYLAAIEAM 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 144 DSLVGQIKDKVDHVARENTLLWFTGDNG-PwaqkcelaGSVGPffgLWQTHQGgspTKQTTWEGGHRVPALAYWPGRVPA 222
Cdd:cd16154   217 DTEIGRLLASIDEEERENTIIIFIGDNGtP--------GQVVD---LPYTRNH---AKGSLYEGGINVPLIVSGAGVERA 282

                         250       260
                  ....*....|....*....|....*.
gi 1372261824 223 NVTSTALLSLLDIFPTVIALAGASLP 248
Cdd:cd16154   283 NERESALVNATDLYATIAELAGVDAA 308
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 90-256 4.96e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 73.02  E-value: 4.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  90 YAERAVEFIEQASTSGRPFLLYVGL-------------AHMHVPLSVTPP--LAHP-------QRQSLYRASLRE----- 142
Cdd:cd16033   132 LADRAIEMLEELAADDKPFFLRVNFwgphdpyippepyLDMYDPEDIPLPesFADDfedkpyiYRRERKRWGVDTedeed 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 143 --------------MDSLVGQIKDKVDHV-ARENTLLWFTGDNGpwaqkcELAGSvgpfFGLWQThqgGSPTKQTTwegg 207
Cdd:cd16033   212 wkeiiahywgyitlIDDAIGRILDALEELgLADDTLVIFTSDHG------DALGA----HRLWDK---GPFMYEET---- 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1372261824 208 HRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGAslPPNRKFDGR 256
Cdd:cd16033   275 YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGV--DVPPKVDGR 321
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 94-243 8.92e-14

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: 70.14  E-value: 8.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  94 AVEFIEQaSTSGRPFLLYVGLAHMHVPLSvtpplAHPQRQSLYRASLREMDSLVGQIKDKVD--HVArENTLLWFTGDNG 171
Cdd:cd00016   108 LLKAIDE-TSKEKPFVLFLHFDGPDGPGH-----AYGPNTPEYYDAVEEIDERIGKVLDALKkaGDA-DDTVIIVTADHG 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372261824 172 pwaqkcelagsvGPFFGLwqTHQGGSPTKQTTWEGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALA 243
Cdd:cd00016   181 ------------GIDKGH--GGDPKADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELISQYDIAPTLADLL 237
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 91-262 4.02e-13

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: 70.29  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  91 AERAVEFIEQASTSGRPFLLYVGLAHMHVPLSV----------------------------------------------- 123
Cdd:cd16030   166 ADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVApkkyfdlyplesiplpnpfdpidlpevawndlddlpkygdipalnpg 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 124 --TPPLAHPQRQSL---YRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpWA--QKcelagsvgpffGLWQthqg 195
Cdd:cd16030   246 dpKGPLPDEQARELrqaYYASVSYVDAQVGRVLDALEeLGLADNTIVVLWSDHG-WHlgEH-----------GHWG---- 309

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372261824 196 gsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGasLPPNRKFDGRDVSEVL 262
Cdd:cd16030   310 ----KHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLL 370
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 83-275 9.46e-13

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: 68.39  E-value: 9.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  83 LSGLAQ-------KYAERAVEFIEQASTS---GRPFLLYVGLAHMH-VPLSVTPPLAHPQRQSLYRASLREMDSLVGQIK 151
Cdd:cd16035   105 LSGAAGggykrdpGIAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYYNLIRDVDRQIGRVL 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 152 DKVDHVA-RENTLLWFTGDNGpwaqkcELAGSVGpffGLwqtHQGGSPTKQTTwegghRVPALAYWPGRVPANVTSTALL 230
Cdd:cd16035   185 DALDASGlADNTIVVFTSDHG------EMGGAHG---LR---GKGFNAYEEAL-----HVPLIISHPDLFGTGQTTDALT 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1372261824 231 SLLDIFPTVIALAGASLPPNRK----FDGRDVSEVLFGKS--QMGHRVLFH 275
Cdd:cd16035   248 SHIDLLPTLLGLAGVDAEARATeappLPGRDLSPLLTDADadAVRDGILFT 298
PRK13759 PRK13759
arylsulfatase; Provisional
 59-359 9.08e-12

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 66.23  E-value: 9.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  59 GRDCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLLYVGLAHMHVPLSvtPPLA-------- 128
Cdd:PRK13759  162 GWDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFLKMSFARPHSPYD--PPKRyfdmykda 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 129 ----------------HPQRQSL------------------YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpw 173
Cdd:PRK13759  229 dipdphigdweyaedqDPEGGSIdalrgnlgeeyarraraaYYGLITHIDHQIGRFLQALKEFGlLDNTIILFVSDHG-- 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 174 aqkcELAGSvgpfFGLWQthqggsptKQTTWEGGHRVPALAYWPG---RVPANVTSTALLSLLDIFPTVIALAGASLPPN 250
Cdd:PRK13759  307 ----DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 251 rkFDGRDVSEVLFGKSQmGHRVLFHpnsgaaGEYGalqtvrlNHYKAF-YITGGA-KACDGSV-GPEQhhvaplIFNLED 327
Cdd:PRK13759  371 --VDGRSLKNLIFGQYE-GWRPYLH------GEHA-------LGYSSDnYLTDGKwKYIWFSQtGEEQ------LFDLKK 428

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1372261824 328 AADEGMPLQkGSPEYQEVLQQVTRALADVLQD 359
Cdd:PRK13759  429 DPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
 92-330 1.39e-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: 59.09  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  92 ERAVEFIEQASTS-GRPFLLYVGLAhmhvplsvtppLAHPQR--------------QSLYRASLREMDSLVGQIKDKV-D 155
Cdd:cd16171   150 DKAVHWIRKEAPNlTQPFALYLGLN-----------LPHPYPspsmgenfgsirniRAFYYAMCAETDAMLGEIISALkD 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 156 HVARENTLLWFTGDNGpwaqkcELAGSVGPFFglwqthqggsptKQTTWEGGHRVPALAYWPGrVPANVTSTALLSLLDI 235
Cdd:cd16171   219 TGLLDKTYVFFTSDHG------ELAMEHRQFY------------KMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDI 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 236 FPTVIALAGASLPPNrkFDGRDVSEVLFGKS-QMGHRVLFHPNSGAAGEYG-----ALQTVRLNHYKafYITGGakacDG 309
Cdd:cd16171   280 YPTMLDIAGVPQPQN--LSGYSLLPLLSESSiKESPSRVPHPDWVLSEFHGcnvnaSTYMLRTNSWK--YIAYA----DG 351

                         250       260
                  ....*....|....*....|.
gi 1372261824 310 SvgpeqhHVAPLIFNLEDAAD 330
Cdd:cd16171   352 N------SVPPQLFDLSKDPD 366
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 89-266 1.43e-08

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: 56.09  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  89 KYAERAVEFIEQASTsGRPFLLYVGLAHMHVPLSVTPP--------------------------LAHPQRQSLYRAS--- 139
Cdd:cd16150   116 ACVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPYGVEEPwfsmidreklpprrppglrakgkpsmLEGIEKQGLDRWSeer 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 140 LREM-----------DSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpfFGLWQTHQGGSPTKQTtwegg 207
Cdd:cd16150   195 WRELratylgmvsrlDHQFGRLLEALKETGlYDDTAVFFFSDHG------DYTGD----YGLVEKWPNTFEDCLT----- 259

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1372261824 208 hRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPNRkfdgrdvsevlFGKS 266
Cdd:cd16150   260 -RVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAGIPLSHTH-----------FGRS 305
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 2-291 7.05e-07

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: 50.84  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824   2 IGKWHLGhhgsyhpnfrGFDYY-FGI-P------YSNDMGC-----TDapgynyppcpacpQRDGLWRNPgrdcytdvaL 68
Cdd:cd16156    95 IGKWHLD----------GGDYFgNGIcPqgwdpdYWYDMRNyldelTE-------------EERRKSRRG---------L 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  69 PLYENLNIVEQPVnlsgLAQKYAERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLA-------------------- 128
Cdd:cd16156   143 TSLEAEGIKEEFT----YGHRCTNRALDFIEKHKD--EDFFLVVSYDEPHHPFLCPKPYAsmykdfefpkgenayddlen 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 129 -------------HPQRQS------LYRASLREMDSLVGQIKDKVDHVArENTLLWFTGDNGpwaqkcELAGSvgpfFGL 189
Cdd:cd16156   217 kplhqrlwagakpHEDGDKgtikhpLYFGCNSFVDYEIGRVLDAADEIA-EDAWVIYTSDHG------DMLGA----HKL 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 190 WQthQGGSPTKQTTwegghRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPnrKFDGRDVSEVLFGKSQMG 269
Cdd:cd16156   286 WA--KGPAVYDEIT-----NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPK--VLEGESILATIEDPEIPE 356

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1372261824 270 HRVLF---------HPNsgaageYGALQTVR 291
Cdd:cd16156   357 NRGVFvefgryevdHDG------FGGFQPVR 381
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 96-258 1.80e-05

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 46.57  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  96 EFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAH-----PQRQSLYRASLREMDSLVGQIKDKVDHVAR-ENTLLWFTGD 169
Cdd:COG1368   374 KALEELEKLKKPFFAFLITLSNHGPYTLPEEDKKipdygKTTLNNYLNAVRYADQALGEFIEKLKKSGWyDNTIFVIYGD 453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 170 ngpwaqkcelagsvgpffglwqtHQGGSPTKQTTWE--GGHRVPALAYWPGRVPANVTSTaLLSLLDIFPTVIALAGASL 247
Cdd:COG1368   454 -----------------------HGPRSPGKTDYENplERYRVPLLIYSPGLKKPKVIDT-VGSQIDIAPTLLDLLGIDY 509

                         170
                  ....*....|.
gi 1372261824 248 PPNRKFdGRDV 258
Cdd:COG1368   510 PSYYAF-GRDL 519
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 91-256 8.79e-04

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: 41.09  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824  91 AERAVEFIEqaSTSGRPFLLYVGLAHMHVPL-------------SVTPPLAHPQRQS------LYRASLREMDSL----- 146
Cdd:cd16028   144 TDRAIEYLD--ERQDEPWFLHLSYIRPHPPFvapapyhalydpaDVPPPIRAESLAAeaaqhpLLAAFLERIESLsfspg 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 147 -------------------VGQIKDKVDHVAR-----------ENTLLWFTGDNGpwaqkcELAGsvgpffglwQTHQGG 196
Cdd:cd16028   222 aanaadlddeevaqmratyLGLIAEVDDHLGRlfdylketgqwDDTLIVFTSDHG------EQLG---------DHWLWG 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372261824 197 sptKQTTWEGGHRVPALAYWPGRvPANVTS----TALLSLLDIFPTVIALAGASLPPnrKFDGR 256
Cdd:cd16028   287 ---KDGFFDQAYRVPLIVRDPRR-EADATRgqvvDAFTESVDVMPTILDWLGGEIPH--QCDGR 344
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 136-244 7.49e-03

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: 38.05  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372261824 136 YRASLREMDSLVGQIKDKVDHV-ARENTLLWFTGDngpwaqkcelagsvgpffglwqtHQGGSPTKQTTWEGG----HRV 210
Cdd:cd16015   194 YLNAIHYTDKALGEFIEKLKKSgLYENTIIVIYGD-----------------------HLPSLGSDYDETDEDpldlYRT 250

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1372261824 211 PALAYWPGRVPANVTSTaLLSLLDIFPTVIALAG 244
Cdd:cd16015   251 PLLIYSPGLKKPKKIDR-VGSQIDIAPTLLDLLG 283
 
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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