NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767994113|ref|XP_011522848|]
View 

arylsulfatase G isoform X12 [Homo sapiens]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-247 3.67e-117

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: 342.14  E-value: 3.67e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   1 MHVPLPVTQLPAAP-RGRSLYGAGLWEMDSLVGQIKDKVDH-TVKENTFLWFTGDNGPWAQKCELAgsVGPFTGFWQTRQ 78
Cdd:cd16161  165 VHVPLANLPRFQSPtSGRGPYGDALQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  79 GGSPAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHReee 158
Cdd:cd16161  243 GGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHR--- 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 159 agggkeaegaqsplcnalqmhgflVLFHPNSGAAGeFGALQTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLED 238
Cdd:cd16161  320 ------------------------CLFHPNSGAAG-AGALSAVRCGDYKAHYATGGALACCGSTGPKLYHDPPLLFDLEV 374


                 ....*....
gi 767994113 239 DTAEAVPLE 247
Cdd:cd16161  375 DPAESFPLT 383
 
Name Accession Description Interval E-value
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 1-247 3.67e-117

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: 342.14  E-value: 3.67e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   1 MHVPLPVTQLPAAP-RGRSLYGAGLWEMDSLVGQIKDKVDH-TVKENTFLWFTGDNGPWAQKCELAgsVGPFTGFWQTRQ 78
Cdd:cd16161  165 VHVPLANLPRFQSPtSGRGPYGDALQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  79 GGSPAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHReee 158
Cdd:cd16161  243 GGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHR--- 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 159 agggkeaegaqsplcnalqmhgflVLFHPNSGAAGeFGALQTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLED 238
Cdd:cd16161  320 ------------------------CLFHPNSGAAG-AGALSAVRCGDYKAHYATGGALACCGSTGPKLYHDPPLLFDLEV 374


                 ....*....
gi 767994113 239 DTAEAVPLE 247
Cdd:cd16161  375 DPAESFPLT 383
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
183-300 3.63e-32

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 115.49  E-value: 3.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  183 VLFHpNSGAAgefgaLQTVRLERYKAFYITG-----GARACDGSTGPELQHKFPLIFNLEDDTAEAVPLERGGAEYQAVL 257
Cdd:pfam14707   5 FLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYPEVL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767994113  258 PEVRKVLADVLQDI--ANDNISSADYTQDPSVTPCCnPYQIACRC 300
Cdd:pfam14707  79 AEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
3-275 3.97e-28

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 111.89  E-value: 3.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   3 VPLPVTQLPAA------PRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvgpftGFWQ 75
Cdd:COG3119  179 IPLPPNLAPRDlteeelRRARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEHG 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  76 TRQGgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHR 155
Cdd:COG3119  246 LRGG----KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRD 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 156 EeeagggkeaegaqsplcnalqmhgflVLFHpnsgaAGEFGALQTVRLERYKAFYITGGARAcdgstgPELqhkfpliFN 235
Cdd:COG3119  320 Y--------------------------LYWE-----YPRGGGNRAIRTGRWKLIRYYDDDGP------WEL-------YD 355

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767994113 236 LEDDTAEAVPLergGAEYqavlPEVRKVLADVLQDIANDN 275
Cdd:COG3119  356 LKNDPGETNNL---AADY----PEVVAELRALLEAWLKEL 388
PRK13759 PRK13759
arylsulfatase; Provisional
 12-157 2.82e-04

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 42.35  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  12 AAPRGRSLYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrqggspaKQTTWEG 90
Cdd:PRK13759 262 YARRARAAYYGLITHIDHQIGRFLQALkEFGLLDNTIILFVSDHG------DMLGDHYLFR------------KGYPYEG 323

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  91 GHRVPALAYWPG---RVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGrSQPGHREE 157
Cdd:PRK13759 324 SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIP--DDVDGRSLKNLIFG-QYEGWRPY 390
 
Name Accession Description Interval E-value
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 1-247 3.67e-117

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: 342.14  E-value: 3.67e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   1 MHVPLPVTQLPAAP-RGRSLYGAGLWEMDSLVGQIKDKVDH-TVKENTFLWFTGDNGPWAQKCELAgsVGPFTGFWQTRQ 78
Cdd:cd16161  165 VHVPLANLPRFQSPtSGRGPYGDALQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  79 GGSPAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHReee 158
Cdd:cd16161  243 GGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHR--- 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 159 agggkeaegaqsplcnalqmhgflVLFHPNSGAAGeFGALQTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLED 238
Cdd:cd16161  320 ------------------------CLFHPNSGAAG-AGALSAVRCGDYKAHYATGGALACCGSTGPKLYHDPPLLFDLEV 374


                 ....*....
gi 767994113 239 DTAEAVPLE 247
Cdd:cd16161  375 DPAESFPLT 383
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 1-246 1.54e-68

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: 218.20  E-value: 1.54e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   1 MHVPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqg 79
Cdd:cd16026  194 PHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG------- 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  80 gspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHREeea 159
Cdd:cd16026  267 ---GKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHP--- 340

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 160 gggkeaegaqsplcnalqmhgflVLFHPNSgaagefGALQTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLEDD 239
Cdd:cd16026  341 -----------------------FFYYYDG------GDLQAVRSGRWKLHLPTTYRTGTDPGGLDPTKLEPPLLYDLEED 391


                 ....*..
gi 767994113 240 TAEAVPL 246
Cdd:cd16026  392 PGETYNV 398
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
 1-265 1.09e-40

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: 146.81  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   1 MHVPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDK-VDHTVKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqg 79
Cdd:cd16160  205 THTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG------- 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  80 gspAKQTTWEGGHRVPALAYWPGRVPVNVtSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHREeea 159
Cdd:cd16160  278 ---GKGNSWEGGIRVPFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDD--- 350

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 160 gggkeaegaqsplcnalqmhgflVLFHPNSgaagefgALQTVRLERYKAFYITG--------GARACDGSTGPEL----- 226
Cdd:cd16160  351 -----------------------ILYYCCS-------RLMAVRYGSYKIHFKTQplpsqeslDPNCDGGGPLSDYivcyd 400

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767994113 227 -------QHKFPLIFNLEDDTAEAVPLERGGAEYqaVLPEVRKVLA 265
Cdd:cd16160  401 cedecvtKHNPPLIFDVEKDPGEQYPLQPSVYEH--MLEAVEKLIA 444
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 1-248 5.29e-36

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: 132.66  E-value: 5.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   1 MHVP-LPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSvGPFTGfwqtrq 78
Cdd:cd16142  162 MHFPtLPSPEFEGKSSGKGKYADSMVELDDHVGQILDALDELgIADNTIVIFTTDNGPEQDVWPDGGY-TPFRG------ 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  79 ggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLP------QGRRFDGVDVSEVLFGRSQP 152
Cdd:cd16142  235 ----EKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEK 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 153 GHREEeagggkeaegaqsplcnalqmhgflVLFHPNsgaaGEFGAlqtVRLERYKA-FYITGGARAcdGSTGPELQHKFP 231
Cdd:cd16142  311 SRRSE-------------------------FFYFGE----GELGA---VRWKNWKVhFKAQEDTGG--PTGEPFYVLTFP 356

                        250
                 ....*....|....*..
gi 767994113 232 LIFNLEDDtaeavPLER 248
Cdd:cd16142  357 LIFNLRRD-----PKER 368
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
 12-300 6.00e-36

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: 134.49  E-value: 6.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  12 AAPRGRslYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQGgspaKQTTWEG 90
Cdd:cd16158  222 RSSRGP--FGDALAELDGSVGELLQTLKENgIDNNTLVFFTSDNGPSTMRKSRGGNAGLL------KCG----KGTTYEG 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  91 GHRVPALAYWPGRVPVNVTStALLSVLDIFPTVVALAQASLPQgRRFDGVDVSEVLFGrSQPGHREEeagggkeaegaqs 170
Cdd:cd16158  290 GVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN-VTLDGVDMSPILFE-QGKSPRQT------------- 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 171 plcnalqmhgflVLFHPNSgAAGEFGALqTVRLERYKAFYITGGA--------RACDGSTgPELQHKFPLIFNLEDDTAE 242
Cdd:cd16158  354 ------------FFYYPTS-PDPDKGVF-AVRWGKYKAHFYTQGAahsgttpdKDCHPSA-ELTSHDPPLLFDLSQDPSE 418

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767994113 243 AVPLErGGAEYQAVLPEVRKVLADVLQDIANDNiSSADYTQDPSVTPCCN----PYQIACRC 300
Cdd:cd16158  419 NYNLL-GLPEYNQVLKQIQQVKERFEASMKFGE-SEINKGEDPALEPCCKpgctPKPSCCQC 478
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
 8-272 6.01e-34

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: 129.72  E-value: 6.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   8 TQLPAAP--RGRS---LYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcELAGSVGPFTGFWQTRQGGS 81
Cdd:cd16159  264 TALFTSKkfKGRSkhgRYGDNVEEMDWSVGQILDALDELgLKDNTFVYFTSDNGGHL---EEISVGGEYGGGNGGIYGGK 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  82 paKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQpghreeeagg 161
Cdd:cd16159  341 --KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEK---------- 408

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 162 gkeaegaQSP------LCNAlQMHGflVLFHPNSGAAgefgalqtvrleRYKAFYIT-----GGARA-------CDGSTG 223
Cdd:cd16159  409 -------RSPheflfhYCGA-ELHA--VRYRPRDGGA------------VWKAHYFTpnfypGTEGCcgtllcrCFGDSV 466

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 767994113 224 peLQHKFPLIFNLEDDTAEAVPLERGGAEYQAVLPEVRKVLADVLQDIA 272
Cdd:cd16159  467 --THHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIE 513
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
183-300 3.63e-32

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 115.49  E-value: 3.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  183 VLFHpNSGAAgefgaLQTVRLERYKAFYITG-----GARACDGSTGPELQHKFPLIFNLEDDTAEAVPLERGGAEYQAVL 257
Cdd:pfam14707   5 FLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYPEVL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767994113  258 PEVRKVLADVLQDI--ANDNISSADYTQDPSVTPCCnPYQIACRC 300
Cdd:pfam14707  79 AEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 2-266 2.21e-31

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: 121.81  E-value: 2.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   2 HVPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNG-PWAQKCELAGSVGPFTGfwqtrqg 79
Cdd:cd16157  208 HAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLgIENNTFVFFSSDNGaALISAPEQGGSNGPFLC------- 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  80 gspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFgrsqpghreeea 159
Cdd:cd16157  281 ---GKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLL------------ 345

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 160 gGGKEAEGAqsplcnalqmhgflVLFHPNSgaagefgALQTVRLERYKAFYIT---------GGARACDG------STGP 224
Cdd:cd16157  346 -NGKEKDRP--------------IFYYRGD-------ELMAVRLGQYKAHFWTwsnsweefrKGINFCPGqnvpgvTTHN 403

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767994113 225 ELQH-KFPLIFNLEDDTAEAVPLERGGAEYQAVLPEVRKVLAD 266
Cdd:cd16157  404 QTDHtKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQ 446
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
3-275 3.97e-28

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 111.89  E-value: 3.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   3 VPLPVTQLPAA------PRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvgpftGFWQ 75
Cdd:COG3119  179 IPLPPNLAPRDlteeelRRARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEHG 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  76 TRQGgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHR 155
Cdd:COG3119  246 LRGG----KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRD 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 156 EeeagggkeaegaqsplcnalqmhgflVLFHpnsgaAGEFGALQTVRLERYKAFYITGGARAcdgstgPELqhkfpliFN 235
Cdd:COG3119  320 Y--------------------------LYWE-----YPRGGGNRAIRTGRWKLIRYYDDDGP------WEL-------YD 355

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767994113 236 LEDDTAEAVPLergGAEYqavlPEVRKVLADVLQDIANDN 275
Cdd:COG3119  356 LKNDPGETNNL---AADY----PEVVAELRALLEAWLKEL 388
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 20-156 3.23e-26

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


Pssm-ID: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 106.86  E-value: 3.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  20 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQGgspaKQTTWEGGHRVPALA 98
Cdd:cd16144  225 YAAMIESLDESVGRILDALEELgLADNTLVIFTSDNGGLSTRGGPPTSNAPL------RGG----KGSLYEGGIRVPLIV 294

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767994113  99 YWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRE 156
Cdd:cd16144  295 RWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRR 352
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 1-157 7.60e-26

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


Pssm-ID: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 105.36  E-value: 7.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   1 MHVPLPVTQLPAAP----RGRS---LYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPwaqkcelagsvGPFTG 72
Cdd:cd16143  177 LYFALPAPHTPIVPspefQGKSgagPYGDFVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP-----------SPYAD 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  73 FWQT-RQGGSPA------KQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEV 145
Cdd:cd16143  246 YKELeKFGHDPSgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPA 325

                        170
                 ....*....|..
gi 767994113 146 LFGRSQPGHREE 157
Cdd:cd16143  326 LLGPKKQEVRES 337
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 26-141 4.43e-22

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: 92.11  E-value: 4.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  26 EMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPwaqkcelagsvgpFTGFWQTRQGgspaKQTTWEGGHRVPALAYWPGRV 104
Cdd:cd16022  139 AIDDQIGRILDALEELgLLDNTLIVFTSDHGD-------------MLGDHGLRGK----KGSLYEGGIRVPFIVRWPGKI 201

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767994113 105 PVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVD 141
Cdd:cd16022  202 PAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 2-156 6.93e-22

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 94.20  E-value: 6.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   2 HVPLPVTQLPAAPRGRS-----LYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcelagSVGPFTGFW- 74
Cdd:cd16151  184 FVPTPDSPDWDPDDKRKkddpeYFPDMVAYMDKLVGKLVDKLEELgLRENTIIIFTGDNG----------THRPITSRTn 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  75 -QTRQGGspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPG 153
Cdd:cd16151  254 gREVRGG---KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSP 330


                 ...
gi 767994113 154 HRE 156
Cdd:cd16151  331 RRE 333
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 27-152 2.69e-20

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: 89.92  E-value: 2.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  27 MDSLVGQIKDKVD-HTVKENTFLWFTGDNGPWAqkcelaGSVGPFTGFWQtrqgGSpaKQTTWEGGHRVPALAYWPGRVP 105
Cdd:cd16146  217 IDDNVGRLLAKLKeLGLEENTIVIFMSDNGPAG------GVPKRFNAGMR----GK--KGSVYEGGHRVPFFIRWPGKIL 284

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767994113 106 VNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQP 152
Cdd:cd16146  285 AGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDP 331
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 27-242 2.99e-20

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: 89.96  E-value: 2.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  27 MDSLVGQIKDKV-DHTVKENTFLWFTGDNGP-----WAQKCELAGSVGPFTGFwqtrqggspaKQTTWEGGHRVPALAYW 100
Cdd:cd16145  240 LDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----------KRSLYEGGIRVPFIARW 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 101 PGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPghreeeagggkeaegaqsplcnalQMHG 180
Cdd:cd16145  310 PGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPE--DIDGISLLPTLLGKPQQ------------------------QQHD 363

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767994113 181 FLVL-FHpnsgaagEFGALQTVRLERYKAFYItggaracDGSTGP-ELqhkfpliFNLEDDTAE 242
Cdd:cd16145  364 YLYWeFY-------EGGGAQAVRMGGWKAVRH-------GKKDGPfEL-------YDLSTDPGE 406
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 26-156 8.37e-16

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: 76.78  E-value: 8.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  26 EMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcelagsvGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWPGRV 104
Cdd:cd16027  197 RLDQQVGEILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------AKGTLYDSGLRVPLIVRWPGKI 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767994113 105 PVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRE 156
Cdd:cd16027  255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDY 304
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
 1-157 2.70e-15

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: 75.28  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   1 MHVPLPVTQLPAAP----------RGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCElAGSVGP 69
Cdd:cd16029  193 VHAPLQVPPEYADPyedkfahikdEDRRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYP 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  70 FTGfwqtrqggspAKQTTWEGGHRVPALAYWPGRVPV-NVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFG 148
Cdd:cd16029  272 LRG----------GKNTLWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSG 341


                 ....*....
gi 767994113 149 RSqPGHREE 157
Cdd:cd16029  342 GA-PSPRTE 349
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
 27-157 2.79e-14

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: 72.48  E-value: 2.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  27 MDSLVGQIKDKVDHT-VKENTFLWFTGDNGP-----WAQkcelAGSvGPFTGFwqtrqggspaKQTTWEGGHRVPALAYW 100
Cdd:cd16025  228 MDQQIGRLIDYLKELgELDNTLIIFLSDNGAsaepgWAN----ASN-TPFRLY----------KQASHEGGIRTPLIVSW 292

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767994113 101 PGRV-PVNVTSTALLSVLDIFPTVVALAQASLPQGRR------FDGVDVSEVLFGRSQPGHREE 157
Cdd:cd16025  293 PKGIkAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRT 356
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 13-139 3.47e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 68.03  E-value: 3.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  13 APRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcelagsvgpFT----GFWQTRQGGSPakQTT 87
Cdd:cd16149  137 APHSPWGYFAAVTGVDRNVGRLLDELEELgLTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNM 200

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767994113  88 WEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDG 139
Cdd:cd16149  201 YDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
Sulfatase pfam00884
Sulfatase;
17-129 3.54e-13

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 68.60  E-value: 3.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   17 RSLYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGPwaqkcelagSVGPFTGFWQTRQGGspakqTTWEGGHRVP 95
Cdd:pfam00884 199 LNSYDNTLLYTDDAIGRVLDKLeENGLLDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGYRVP 264

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767994113   96 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQA 129
Cdd:pfam00884 265 LLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 17-173 6.59e-11

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: 62.21  E-value: 6.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  17 RSLYGAGLWeMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVP 95
Cdd:cd16032  164 RAYYGMVSY-VDDKVGQLLDTLERTgLADDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSARVP 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  96 ALAYWPGR-VPVNVTstALLSVLDIFPTVVALAQASLPQGR-RFDGVDVSEVLFGRSQPGHReeEAGGGKEAEGAQSPLC 173
Cdd:cd16032  225 LIISAPGRfAPRRVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGED--EVISEYLAEGAVAPCV 300
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 5-239 4.37e-10

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: 59.89  E-value: 4.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   5 LPVTQLPAAPRGRSL---YGA--GLwemDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGPFtgfwqtrq 78
Cdd:cd16034  212 VPEDKKEEAGLREDLrgyYAMitAL---DDNIGRLLDALKELgLLENTIVVFTSDHG------DMLGSHGLM-------- 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  79 ggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHREEe 158
Cdd:cd16034  275 ----NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSV- 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113 159 agggkeaegaqsplcnalqmhgFLVLFHPNSG-AAGEFGALQTVRLERYKafYitggarACDGSTGpelqhkfPLIFNLE 237
Cdd:cd16034  348 ----------------------LLQCFVPFGGgSARDGGEWRGVRTDRYT--Y------VRDKNGP-------WLLFDNE 390


                 ..
gi 767994113 238 DD 239
Cdd:cd16034  391 KD 392
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 20-127 4.58e-10

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: 58.59  E-value: 4.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  20 YGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGpwaqkcelAGSVGPftgfwqTRQGGSPAKQTTWEGGHRVPALA 98
Cdd:cd00016  144 YYDAVEEIDERIGKVLDALkKAGDADDTVIIVTADHG--------GIDKGH------GGDPKADGKADKSHTGMRVPFIA 209

                         90       100
                 ....*....|....*....|....*....
gi 767994113  99 YWPGrVPVNVTSTALLSVLDIFPTVVALA 127
Cdd:cd00016  210 YGPG-VKKGGVKHELISQYDIAPTLADLL 237
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 2-144 5.81e-10

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: 58.93  E-value: 5.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113   2 HVPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVD----HTVKENTFLWFTGDNGpwaqkcelagsvgpftgfWQTR 77
Cdd:cd16153  152 LQPHTPVLPPKEFRDRFDYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLG 213

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767994113  78 QGGSPAKQTTWEGGHRVPALAYWPGR--VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 144
Cdd:cd16153  214 EQGILAKFTFWPQSHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 17-155 7.16e-10

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: 59.29  E-value: 7.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  17 RSLYGAGLWEMDSLVGQIKDKVDHTVKENTFLWFTGDNG-PwaqkcelagsvGPFTGFWQTRQGgspAKQTTWEGGHRVP 95
Cdd:cd16154  206 RPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYTRNH---AKGSLYEGGINVP 271

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  96 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPGHR 155
Cdd:cd16154  272 LIVSGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQ 329
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 27-157 1.53e-09

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: 58.39  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  27 MDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrQGGSPAKQTtweggHRVPALAYWPGRVP 105
Cdd:cd16033  226 IDDAIGRILDALEELgLADDTLVIFTSDHG------DALGAHRLWD------KGPFMYEET-----YRIPLIIKWPGVIA 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767994113 106 VNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHREE 157
Cdd:cd16033  289 AGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGEQPEDWRDE 338
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 26-157 1.86e-09

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: 57.92  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  26 EMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGpFTGfwqtrqggspaKQTTWEGGHRVPALAYWPGRV 104
Cdd:cd16031  245 GVDDNVGRILDYLEEQgLADNTIIIYTSDNG------FFLGEHG-LFD-----------KRLMYEESIRVPLIIRDPRLI 306

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767994113 105 PVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHREE 157
Cdd:cd16031  307 KAGTVVDALVLNIDFAPTILDLAGVPIP--EDMQGRSLLPLLEGEKPVDWRKE 357
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 27-139 3.52e-09

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: 57.17  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  27 MDSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelagsvgpftGFW--QTRQGgsPAKQTTWEGGHRVPALAYWPGr 103
Cdd:cd16147  251 VDDLVERLVNTLEATgQLDNTYIIYTSDN-----------------GYHlgQHRLP--PGKRTPYEEDIRVPLLVRGPG- 310

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767994113 104 VPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDG 139
Cdd:cd16147  311 IPAGVTVDQLVSNIDLAPTILDLAGAPPP--SDMDG 344
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 26-141 9.79e-09

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: 55.63  E-value: 9.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  26 EMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVPALAYWPGRV 104
Cdd:cd16037  170 FLDENIGRVLDALEELgLLDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPGIP 231

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767994113 105 PVNVTSTAlLSVLDIFPTVVALAQASLPqgRRFDGVD 141
Cdd:cd16037  232 AGKRVKTP-VSLVDLAPTILEAAGAPPP--PDLDGRS 265
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 19-141 4.15e-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: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 53.32  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  19 LYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcELAGSVGPFTGFWQTrqggspakqtTWEGGHRVPAL 97
Cdd:cd16148  164 LYDAEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EEFGEHGLYWGHGSN----------LYDEQLHVPLI 227

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767994113  98 AYWPGRVPVNVTStALLSVLDIFPTVVALAQASLPqgRRFDGVD 141
Cdd:cd16148  228 IRWPGKEPGKRVD-ALVSHIDIAPTLLDLLGVEPP--DYSDGRS 268
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 15-159 5.98e-07

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: 49.90  E-value: 5.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  15 RGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGpftgfwQTRQGGSPAKQTTwegghR 93
Cdd:cd16035  164 RFRNFYYNLIRDVDRQIGRVLDALDASgLADNTIVVFTSDHG------EMGGAHG------LRGKGFNAYEEAL-----H 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  94 VPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQ----GRRFDGVDVSEVLfgRSQPGHREEEA 159
Cdd:cd16035  227 VPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEArateAPPLPGRDLSPLL--TDADADAVRDG 294
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 27-146 6.74e-07

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: 50.26  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  27 MDSLVGQIKDKVD-HTVKENTFLWFTGDNGpWA--QKcelagsvgpftGFWqtrqggspAKQTTWEGGHRVPALAYWPGR 103
Cdd:cd16030  270 VDAQVGRVLDALEeLGLADNTIVVLWSDHG-WHlgEH-----------GHW--------GKHTLFEEATRVPLIIRAPGV 329

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767994113 104 VPVNVTSTALLSVLDIFPTVVALAQasLPQGRRFDGVDVSEVL 146
Cdd:cd16030  330 TKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLL 370
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
 17-134 2.00e-06

arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293781 [Multi-domain]  Cd Length: 366  Bit Score: 48.69  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  17 RSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAgsvgpftgfWQTRQGgspAKQTTWEGGHRVP 95
Cdd:cd16171  195 RAFYYAMCAETDAMLGEIISALKDTgLLDKTYVFFTSDHG------ELA---------MEHRQF---YKMSMYEGSSHVP 256

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767994113  96 ALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQG 134
Cdd:cd16171  257 LLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 26-146 1.21e-05

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: 46.40  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  26 EMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGpwaqkceLAgsVGpftgfwqtrQGGSPAKQTTWEGGHRVPALAYWPGrV 104
Cdd:cd16155  200 HLDAQIGRILDALEASGElDNTIIVFTSDHG-------LA--VG---------SHGLMGKQNLYEHSMRVPLIISGPG-I 260

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767994113 105 PVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVL 146
Cdd:cd16155  261 PKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVI 300
PRK13759 PRK13759
arylsulfatase; Provisional
 12-157 2.82e-04

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 42.35  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  12 AAPRGRSLYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrqggspaKQTTWEG 90
Cdd:PRK13759 262 YARRARAAYYGLITHIDHQIGRFLQALkEFGLLDNTIILFVSDHG------DMLGDHYLFR------------KGYPYEG 323

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  91 GHRVPALAYWPG---RVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGrSQPGHREE 157
Cdd:PRK13759 324 SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIP--DDVDGRSLKNLIFG-QYEGWRPY 390
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 28-156 3.21e-04

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: 41.98  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  28 DSLVGQIKDKVDHTVkENTFLWFTGDNGpwaqkcELAGSvgpftgfwQTRQGGSPAkqtTWEGGHRVPALAYWPGRVPVN 107
Cdd:cd16156  251 DYEIGRVLDAADEIA-EDAWVIYTSDHG------DMLGA--------HKLWAKGPA---VYDEITNIPLIIRGKGGEKAG 312

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767994113 108 VTSTALLSVLDIFPTVVALAQasLPQGRRFDGVDVSEVLFGRSQPGHRE 156
Cdd:cd16156  313 TVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATIEDPEIPENRG 359
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 27-150 3.78e-04

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: 41.84  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994113  27 MDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvGPFtGFWQTRQGGSPAKQTtwegghRVPALAYWPGRVP 105
Cdd:cd16150  209 LDHQFGRLLEALKETgLYDDTAVFFFSDHGDYT---------GDY-GLVEKWPNTFEDCLT------RVPLIIKPPGGPA 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767994113 106 VNVTStALLSVLDIFPTVVALAqaslpqgrrfdGVDVSEVLFGRS 150
Cdd:cd16150  273 GGVSD-ALVELVDIPPTLLDLA-----------GIPLSHTHFGRS 305
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH