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Conserved domains on  [gi|17559078|ref|NP_505102|]
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Sulfatase N-terminal domain-containing protein [Caenorhabditis elegans]

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 ...
32-388 0e+00

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 cd16160:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 445  Bit Score: 550.11  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  32 HPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVFVPYDI 111
Cdd:cd16160   1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 GGLPKSETTMAEMLQEAGYATGMVGKWHLGINENNATDGAHLPSKRGFEYVGVNLPFTNVWQCDTTREFYDkGPDPSLCF 191
Cdd:cd16160  81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVGTNLPFTNSWACDDTGRHVD-FPDRSACF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 192 LYDGDDIVQQPMKFEHMTENLVGDWKRFLMTRLaqdqhERPFFFYFSFPQVHSTQFASKRFRGSSK-------------- 257
Cdd:cd16160 160 LYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQ-----ENPFFLYFSFPQTHTPLFASKRFKGKSKrgrygdninemswa 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078     --------------------------------------------------------------------------------
Cdd:cd16160 235 vgevldtlvdtgldqntlvfflsdhgphveycleggstgglkggkgnsweggirvpfiaywpgtikprvshevvstmdif 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 258 ------------EALRSDGIDISDELRGESEDvegslgKARPIIYYCNTHLMAIRMGDYKVHYKTSPIFFNNSVDPNLDY 325
Cdd:cd16160 315 ptfvdlaggtlpTDRIYDGLSITDLLLGEADS------PHDDILYYCCSRLMAVRYGSYKIHFKTQPLPSQESLDPNCDG 388
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559078 326 FCpngkPKSDWYVSQVCPDEHLQKHYPPLVFDLIRDPYEQYPLQNTVksQEIRFQAMQRLSEH 388
Cdd:cd16160 389 GG----PLSDYIVCYDCEDECVTKHNPPLIFDVEKDPGEQYPLQPSV--YEHMLEAVEKLIAH 445
 
Name Accession Description Interval E-value
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
32-388 0e+00

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: 550.11  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  32 HPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVFVPYDI 111
Cdd:cd16160   1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 GGLPKSETTMAEMLQEAGYATGMVGKWHLGINENNATDGAHLPSKRGFEYVGVNLPFTNVWQCDTTREFYDkGPDPSLCF 191
Cdd:cd16160  81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVGTNLPFTNSWACDDTGRHVD-FPDRSACF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 192 LYDGDDIVQQPMKFEHMTENLVGDWKRFLMTRLaqdqhERPFFFYFSFPQVHSTQFASKRFRGSSK-------------- 257
Cdd:cd16160 160 LYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQ-----ENPFFLYFSFPQTHTPLFASKRFKGKSKrgrygdninemswa 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078     --------------------------------------------------------------------------------
Cdd:cd16160 235 vgevldtlvdtgldqntlvfflsdhgphveycleggstgglkggkgnsweggirvpfiaywpgtikprvshevvstmdif 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 258 ------------EALRSDGIDISDELRGESEDvegslgKARPIIYYCNTHLMAIRMGDYKVHYKTSPIFFNNSVDPNLDY 325
Cdd:cd16160 315 ptfvdlaggtlpTDRIYDGLSITDLLLGEADS------PHDDILYYCCSRLMAVRYGSYKIHFKTQPLPSQESLDPNCDG 388
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559078 326 FCpngkPKSDWYVSQVCPDEHLQKHYPPLVFDLIRDPYEQYPLQNTVksQEIRFQAMQRLSEH 388
Cdd:cd16160 389 GG----PLSDYIVCYDCEDECVTKHNPPLIFDVEKDPGEQYPLQPSV--YEHMLEAVEKLIAH 445
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
28-140 1.00e-44

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 160.43  E-value: 1.00e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  28 PSPRHPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGgrrvFV 107
Cdd:COG3119  19 AAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD----NG 94
                        90       100       110
                ....*....|....*....|....*....|...
gi 17559078 108 PYDIGGLPKSETTMAEMLQEAGYATGMVGKWHL 140
Cdd:COG3119  95 EGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL 127
Sulfatase pfam00884
Sulfatase;
33-252 1.35e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 136.01  E-value: 1.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078    33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGivggrrvFVPYDIG 112
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFG-------SYVSTPV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078   113 GLPKSETTMAEMLQEAGYATGMVGKWHLGINENNAtdgahlPSKRGFEYV-GVNLPFTNVWQCDtTREFYDKGPDPSlcf 191
Cdd:pfam00884  74 GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFfGRNTGSDLYADPP-DVPYNCSGGGVS--- 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559078   192 lydgDDIvqqpmkfehMTENLVGdwkrflmtrlAQDQHERPFFFYFSFPQVHSTQFASKRF 252
Cdd:pfam00884 144 ----DEA---------LLDEALE----------FLDNNDKPFFLVLHTLGSHGPPYYPDRY 181
PRK13759 PRK13759
arylsulfatase; Provisional
30-244 1.95e-20

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 93.58  E-value: 1.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078   30 PRHPNIVILMIDDLgYGD-IASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVfVP 108
Cdd:PRK13759   4 TKKPNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDV-VP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  109 YDIgglpksETTMAEMLQEAGYATGMVGKWH-------LGInENNATDGAHLPSKRgfeyvgvNLPFTNVWQCDTTREFY 181
Cdd:PRK13759  82 WNY------KNTLPQEFRDAGYYTQCIGKMHvfpqrnlLGF-HNVLLHDGYLHSGR-------NEDKSQFDFVSDYLAWL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  182 ---DKGPDPSLCFL-YDGDDIVQQPMKFE---HMTENLVGDWKRFLMTRlaqdQHERPFFFYFSFPQVHS 244
Cdd:PRK13759 148 rekAPGKDPDLTDIgWDCNSWVARPWDLEerlHPTNWVGSESIEFLRRR----DPTKPFFLKMSFARPHS 213
 
Name Accession Description Interval E-value
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
32-388 0e+00

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: 550.11  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  32 HPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVFVPYDI 111
Cdd:cd16160   1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 GGLPKSETTMAEMLQEAGYATGMVGKWHLGINENNATDGAHLPSKRGFEYVGVNLPFTNVWQCDTTREFYDkGPDPSLCF 191
Cdd:cd16160  81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVGTNLPFTNSWACDDTGRHVD-FPDRSACF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 192 LYDGDDIVQQPMKFEHMTENLVGDWKRFLMTRLaqdqhERPFFFYFSFPQVHSTQFASKRFRGSSK-------------- 257
Cdd:cd16160 160 LYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQ-----ENPFFLYFSFPQTHTPLFASKRFKGKSKrgrygdninemswa 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078     --------------------------------------------------------------------------------
Cdd:cd16160 235 vgevldtlvdtgldqntlvfflsdhgphveycleggstgglkggkgnsweggirvpfiaywpgtikprvshevvstmdif 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 258 ------------EALRSDGIDISDELRGESEDvegslgKARPIIYYCNTHLMAIRMGDYKVHYKTSPIFFNNSVDPNLDY 325
Cdd:cd16160 315 ptfvdlaggtlpTDRIYDGLSITDLLLGEADS------PHDDILYYCCSRLMAVRYGSYKIHFKTQPLPSQESLDPNCDG 388
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559078 326 FCpngkPKSDWYVSQVCPDEHLQKHYPPLVFDLIRDPYEQYPLQNTVksQEIRFQAMQRLSEH 388
Cdd:cd16160 389 GG----PLSDYIVCYDCEDECVTKHNPPLIFDVEKDPGEQYPLQPSV--YEHMLEAVEKLIAH 445
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
32-368 1.51e-82

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: 259.80  E-value: 1.51e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  32 HPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGrrVFVPYDI 111
Cdd:cd16026   1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGV--VGPPGSK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 GGLPKSETTMAEMLQEAGYATGMVGKWHLGINEnnatdgAHLPSKRGF-EYVGVnlPFTNvwqcDTTREFYDKGPDP-SL 189
Cdd:cd16026  79 GGLPPDEITIAEVLKKAGYRTALVGKWHLGHQP------EFLPTRHGFdEYFGI--PYSN----DMWPFPLYRNDPPgPL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 190 CFLYDGDDIVQQPMKFEHMTENLVGDWKRFLmtrlaQDQHERPFFFYFSFPQVHSTQFASKRFRGSSK------------ 257
Cdd:cd16026 147 PPLMENEEVIEQPADQSSLTQRYTDEAVDFI-----ERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGaglygdvveeld 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 258 -------EALRS-------------------------------------------------------------------- 262
Cdd:cd16026 222 wsvgrilDALKElgleentlviftsdngpwleygghggsagplrggkgttweggvrvpfiawwpgvipagtvsdelastm 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 263 --------------------DGIDISDELRGESEdvegslGKARPIIYY-CNTHLMAIRMGDYKVHYKTSpiffnnsvdp 321
Cdd:cd16026 302 dllptlaalagaplpedrviDGKDISPLLLGGSK------SPPHPFFYYyDGGDLQAVRSGRWKLHLPTT---------- 365
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 17559078 322 nldYFCPNGKPKSDWyvsqvcpdehlQKHYPPLVFDLIRDPYEQYPL 368
Cdd:cd16026 366 ---YRTGTDPGGLDP-----------TKLEPPLLYDLEEDPGETYNV 398
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
33-395 3.14e-70

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: 231.41  E-value: 3.14e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVFVPYDI- 111
Cdd:cd16159   2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTa 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 --GGLPKSETTMAEMLQEAGYATGMVGKWHLGINENNATDGAHLPSKRGFEYVgVNLPFTNVWQC-DTTREFYDKGPDPS 188
Cdd:cd16159  82 ssGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYF-YGLPLTNLKDCgDGSNGEYDLSFDPL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 189 L-----------------------------------------------------CFLYDGDDIVQQPMKFEHMTENLVGD 215
Cdd:cd16159 161 FplltafvlitaltiflllylgavskrffvfllilsllfislfflllitnryfnCILMRNHEVVEQPMSLENLTQRLTKE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 216 WKRFLmtrlaQDQHERPFFFYFSFPQVHSTQFASKRFRGSSKEALRSDGID--------------------------ISD 269
Cdd:cd16159 241 AISFL-----ERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEemdwsvgqildaldelglkdntfvyfTSD 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 270 -----ELRGESEDVEG-------------------------------------------------------SLGKARPI- 288
Cdd:cd16159 316 ngghlEEISVGGEYGGgnggiyggkkmggweggirvptivrwpgvippgsvideptslmdifptvaalagaPLPSDRIId 395
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 289 --------------------IYYCNTHLMAIRMGD------YKVHYKTspiffnnsvdpnldyfcPNGKPKSD-WYVSQV 341
Cdd:cd16159 396 grdlmplltgqekrspheflFHYCGAELHAVRYRPrdggavWKAHYFT-----------------PNFYPGTEgCCGTLL 458
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17559078 342 CP--DEHLQKHYPPLVFDLIRDPYEQYPLQNTVKS-QEIRFQAMQRLSEHKSSLVKV 395
Cdd:cd16159 459 CRcfGDSVTHHDPPLLFDLSADPSESNPLDPTDEPyQEIIKKILEAVAEHQSSIEPV 515
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
33-417 2.37e-65

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: 217.31  E-value: 2.37e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGrrVFVPYDIG 112
Cdd:cd16158   2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPG--VFYPGSRG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 113 GLPKSETTMAEMLQEAGYATGMVGKWHLGINENnatdGAHLPSKRGFE-YVGVnlPFTNVW-QCDTTREFY-----DKGP 185
Cdd:cd16158  80 GLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLN----GTYLPTHQGFDhYLGI--PYSHDQgPCQNLTCFPpnipcFGGC 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 186 DP--SLCFLYDGDDIVQQPMKFEHMtENLVGDWKRFLMTRLAQDqhERPFFFYFSFPQVHSTQFASKRFRGSSK------ 257
Cdd:cd16158 154 DQgeVPCPLFYNESIVQQPVDLLTL-EERYAKFAKDFIADNAKE--GKPFFLYYASHHTHYPQFAGQKFAGRSSrgpfgd 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 258 -------------EALRSDGID-------ISDE---------------LR-GESEDVEGslGKARPIIYYCN-------T 294
Cdd:cd16158 231 alaeldgsvgellQTLKENGIDnntlvffTSDNgpstmrksrggnaglLKcGKGTTYEG--GVREPAIAYWPgrikpgvT 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 295 HLMAIRMGDYKV---------------HYKTSPIFFNNSVDPNLDYF----CPN----------GKPKSDWY-----VSQ 340
Cdd:cd16158 309 HELASTLDILPTiaklagaplpnvtldGVDMSPILFEQGKSPRQTFFyyptSPDpdkgvfavrwGKYKAHFYtqgaaHSG 388
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 341 VCPDE------HLQKHYPPLVFDLIRDPYEQYPLQNTVKSQEIRFQAMQRLSEHKSSLVKVKNVLGSY-NKTLIPCCNP- 412
Cdd:cd16158 389 TTPDKdchpsaELTSHDPPLLFDLSQDPSENYNLLGLPEYNQVLKQIQQVKERFEASMKFGESEINKGeDPALEPCCKPg 468

                ....*....
gi 17559078 413 ----PSCKC 417
Cdd:cd16158 469 ctpkPSCCQ 477
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
33-369 4.61e-53

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: 182.28  E-value: 4.61e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYT-QVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGrrvFVPYDI 111
Cdd:cd16161   2 PNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHN---FLPTSV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 GGLPKSETTMAEMLQEAGYATGMVGKWHLGINEnnatdgAHLPSKRGFEYVgVNLPFTnvwqCDTT--REFYDKGPD--- 186
Cdd:cd16161  79 GGLPLNETTLAEVLRQAGYATGMIGKWHLGQRE------AYLPNSRGFDYY-FGIPFS----HDSSlaDRYAQFATDfiq 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 187 -------PSLCF-----------------------------LYDGDDIVQQPM-------------------------KF 205
Cdd:cd16161 148 rasakdrPFFLYaalahvhvplanlprfqsptsgrgpygdaLQEMDDLVGQIMdavkhaglkdntltwftsdngpwevKC 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 206 EHMTENLVGDWKRFLMTRLAQDQ-----HERPFFFYFSF---PQVHSTQFASK--------RFRGSSKEALRS-DGIDIS 268
Cdd:cd16161 228 ELAVGPGTGDWQGNLGGSVAKAStweggHREPAIVYWPGripANSTSAALVSTldifptvvALAGASLPPGRIyDGKDLS 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 269 DELRGESEDvegslgkARPIIYYCNT------HLMAIRMGDYKVHYKTSPiffnnsvdpnlDYFCPNGKpksdwyvsqvC 342
Cdd:cd16161 308 PVLFGGSKT-------GHRCLFHPNSgaagagALSAVRCGDYKAHYATGG-----------ALACCGST----------G 359
                       410       420
                ....*....|....*....|....*..
gi 17559078 343 PDEHlqkHYPPLVFDLIRDPYEQYPLQ 369
Cdd:cd16161 360 PKLY---HDPPLLFDLEVDPAESFPLT 383
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
33-393 6.05e-49

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: 173.81  E-value: 6.05e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVG----GRRVFVP 108
Cdd:cd16157   2 PNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTtnahARNAYTP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 109 YDI-GGLPKSETTMAEMLQEAGYATGMVGKWHLGINENnatdgaHLPSKRGF-EYVGV-NLPFTNvwqcdttrefYDKGP 185
Cdd:cd16157  82 QNIvGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFdEWFGApNCHFGP----------YDNKA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 186 DPSLCfLYDGDDIV---QQPMKFEHMT--ENLVgdwKRFLMTRLA----QDQHERPFFFYFSFPQVHSTQFASKRFRGSS 256
Cdd:cd16157 146 YPNIP-VYRDWEMIgryYEEFKIDKKTgeSNLT---QIYLQEALEfiekQHDAQKPFFLYWAPDATHAPVYASKPFLGTS 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 257 K-------------------EALRSDGID-------ISDE-----------------LRGESEDVEG------------- 280
Cdd:cd16157 222 QrglygdavmeldssvgkilESLKSLGIEnntfvffSSDNgaalisapeqggsngpfLCGKQTTFEGgmrepaiawwpgh 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 281 --------SLG-------------------------------------KARPIIYYCNTHLMAIRMGDYKVHYKTspifF 315
Cdd:cd16157 302 ikpgqvshQLGslmdlfttslalaglpipsdraidgidllpvllngkeKDRPIFYYRGDELMAVRLGQYKAHFWT----W 377
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 316 NNSVDPNLD--YFCPnGKpksdwYVSQVCpdEHLQKHYP--PLVFDLIRDPYEQYPLqnTVKSQEIRfQAMQRLS----E 387
Cdd:cd16157 378 SNSWEEFRKgiNFCP-GQ-----NVPGVT--THNQTDHTklPLLFHLGRDPGEKYPI--SFKSAEYK-QAMPRISkvvqQ 446

                ....*.
gi 17559078 388 HKSSLV 393
Cdd:cd16157 447 HQKTLV 452
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
33-368 9.66e-49

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: 170.79  E-value: 9.66e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGH------PTQEytqVDRMAAEGTRFTQAYSADSmCSPSRAGFITGRLPIRLGIvggRRVF 106
Cdd:cd16142   1 PNILVILGDDIGWGDLGCYGGgigrgaPTPN---IDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL---TTVG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 107 VPYDIGGLPKSETTMAEMLQEAGYATGMVGKWHLGinennATDGaHLPSKRGFEyvgvnlpftnvwqcdttrEFYDkgpd 186
Cdd:cd16142  74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG-----DEDG-RLPTDHGFD------------------EFYG---- 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 187 pslcFLYDGDD--IVQQPMKFehmtenlvgdwkrflMTRLAQDqhERPFFFYFSFPQVHSTQFASKRFRGSSK------- 257
Cdd:cd16142 126 ----NLYHTIDeeIVDKAIDF---------------IKRNAKA--DKPFFLYVNFTKMHFPTLPSPEFEGKSSgkgkyad 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 258 -------------EALRSDGID------------------------------------------------------ISDE 270
Cdd:cd16142 185 smvelddhvgqilDALDELGIAdntivifttdngpeqdvwpdggytpfrgekgttweggvrvpaivrwpgkikpgrVSNE 264
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 271 -------------LRGESEDVEGSLGKARPI---------------------IYYCNTHLMAIRMGDYKVHYKTSPiffn 316
Cdd:cd16142 265 ivshldwfptlaaLAGAPDPKDKLLGKDRHIdgvdqspfllgkseksrrsefFYFGEGELGAVRWKNWKVHFKAQE---- 340
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 17559078 317 nsvdpnldyfcPNGKPKSDWYVSQVCpdehlqkhypPLVFDLIRDPYEQYPL 368
Cdd:cd16142 341 -----------DTGGPTGEPFYVLTF----------PLIFNLRRDPKERYDV 371
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
33-244 7.36e-48

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


Pssm-ID: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 169.65  E-value: 7.36e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGI----------VGG 102
Cdd:cd16144   1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdvipgrrgpPDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 103 RRVFVPYDIGGLPKSETTMAEMLQEAGYATGMVGKWHLGINennatdGAHLPSKRGFEYV----GVNLPFTNvwqcdtTR 178
Cdd:cd16144  81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVNiggtGNGGPPSY------YF 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559078 179 EFYDKGPDPSlcflYDGDDivqqpmkfEHMTENLVGDWKRFLmtrlaQDQHERPFFFYFSFPQVHS 244
Cdd:cd16144 149 PPGKPNPDLE----DGPEG--------EYLTDRLTDEAIDFI-----EQNKDKPFFLYLSHYAVHT 197
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
28-140 1.00e-44

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 160.43  E-value: 1.00e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  28 PSPRHPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGgrrvFV 107
Cdd:COG3119  19 AAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD----NG 94
                        90       100       110
                ....*....|....*....|....*....|...
gi 17559078 108 PYDIGGLPKSETTMAEMLQEAGYATGMVGKWHL 140
Cdd:COG3119  95 EGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL 127
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
33-139 2.63e-43

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: 152.21  E-value: 2.63e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGgrrvfVPYDIG 112
Cdd:cd16022   1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRG-----NVGNGG 75
                        90       100
                ....*....|....*....|....*..
gi 17559078 113 GLPKSETTMAEMLQEAGYATGMVGKWH 139
Cdd:cd16022  76 GLPPDEPTLAELLKEAGYRTALIGKWH 102
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
33-265 4.37e-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: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 156.21  E-value: 4.37e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYT-QVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGrrVFVPYDI 111
Cdd:cd16143   1 PNIVIILADDLGYGDISCYNPDSKIPTpNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGG--VLGGFSP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 GGLPKSETTMAEMLQEAGYATGMVGKWHLGINeNNATDGAHLPSKRGfeyvgvnlpftnvWQCDTTREFYDkGP-----D 186
Cdd:cd16143  79 PLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLD-WKKKDGKKAATGTG-------------KDVDYSKPIKG-GPldhgfD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 187 PSlcFLYDGDDIVQqpmkfeHMTENLVGdwkrFLmtrlaqDQH---ERPFFFYFSFPQVHSTQFASKRFRGSSKEALRSD 263
Cdd:cd16143 144 YY--FGIPASEVLP------TLTDKAVE----FI------DQHakkDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGD 205

                ..
gi 17559078 264 GI 265
Cdd:cd16143 206 FV 207
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
33-244 9.30e-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: 9.30e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRvfvPYDIG 112
Cdd:cd16145   1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSE---PGGQD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 113 GLPKSETTMAEMLQEAGYATGMVGKWHLGinenNATDGAHlPSKRGFEYV-GVNlpftnvwqcDTTR--EFYdkgPDpsl 189
Cdd:cd16145  78 PLPPDDVTLAEVLKKAGYATAAFGKWGLG----GPGTPGH-PTKQGFDYFyGYL---------DQVHahNYY---PE--- 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559078 190 cFLYDGDDIVQQP-MKFEHMTENLVGDWKRF-----LMTRLA----QDQHERPFFFYFSFPQVHS 244
Cdd:cd16145 138 -YLWRNGEKVPLPnNVIPPLDEGNNAGGGGGtyshdLFTDEAldfiRENKDKPFFLYLAYTLPHA 201
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
33-244 2.43e-38

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: 143.07  E-value: 2.43e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIaSYGHPTQEYT-QVDRMAAEGTRFTQAYSAdSMCSPSRAGFITGRLPIRLGIVGGrrVFVPYDI 111
Cdd:cd16029   1 PHIVFILADDLGWNDV-GFHGSDQIKTpNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHG--VILAGEP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 GGLPKSETTMAEMLQEAGYATGMVGKWHLGinennATDGAHLPSKRGFEYvgvnlpFTNVWQCDTTreFYDKgpdpSLCF 191
Cdd:cd16029  77 YGLPLNETLLPQYLKELGYATHLVGKWHLG-----FYTWEYTPTNRGFDS------FYGYYGGAED--YYTH----TSGG 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559078 192 LYDGDDIVqqpmkFEHMTENLVGDWKR---FLMTRLAQD---QH--ERPFFFYFSFPQVHS 244
Cdd:cd16029 140 ANDYGNDD-----LRDNEEPAWDYNGTystDLFTDRAVDiieNHdpSKPLFLYLAFQAVHA 195
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
33-239 4.95e-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: 139.99  E-value: 4.95e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYsADSMCSPSRAGFITGRLPIRLGIV---GGRRVfvpy 109
Cdd:cd16146   1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWhtiLGRER---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 110 diggLPKSETTMAEMLQEAGYATGMVGKWHLGINEnnatdgAHLPSKRGFEYV------GVNLPFtNVWQCDTTREFYDK 183
Cdd:cd16146  76 ----MRLDETTLAEVFKDAGYRTGIFGKWHLGDNY------PYRPQDRGFDEVlghgggGIGQYP-DYWGNDYFDDTYYH 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559078 184 GPDPslcFLYDG---DDIVQQPMKFehmtenlvgdwkrflmtrlAQDQHERPFFFYFSF 239
Cdd:cd16146 145 NGKF---VKTEGyctDVFFDEAIDF-------------------IEENKDKPFFAYLAT 181
Sulfatase pfam00884
Sulfatase;
33-252 1.35e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 136.01  E-value: 1.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078    33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGivggrrvFVPYDIG 112
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFG-------SYVSTPV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078   113 GLPKSETTMAEMLQEAGYATGMVGKWHLGINENNAtdgahlPSKRGFEYV-GVNLPFTNVWQCDtTREFYDKGPDPSlcf 191
Cdd:pfam00884  74 GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFfGRNTGSDLYADPP-DVPYNCSGGGVS--- 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559078   192 lydgDDIvqqpmkfehMTENLVGdwkrflmtrlAQDQHERPFFFYFSFPQVHSTQFASKRF 252
Cdd:pfam00884 144 ----DEA---------LLDEALE----------FLDNNDKPFFLVLHTLGSHGPPYYPDRY 181
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
33-141 2.69e-33

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: 129.49  E-value: 2.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGH----PTqeytqVDRMAAEGTRFTQAYSAdSMCSPSRAGFITGRLPIR--LGIVGGRRVF 106
Cdd:cd16025   3 PNILLILADDLGFSDLGCFGGeiptPN-----LDALAAEGLRFTNFHTT-ALCSPTRAALLTGRNHHQvgMGTMAELATG 76
                        90       100       110
                ....*....|....*....|....*....|....*
gi 17559078 107 VPYDIGGLPKSETTMAEMLQEAGYATGMVGKWHLG 141
Cdd:cd16025  77 KPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG 111
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
286-417 1.04e-32

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 120.11  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078   286 RPIIYYCNTHLMAIRMGDYKVHYKTspiffnNSVDPNLDYFCPNGKPksdwyvsqvcpdeHLQKHYPPLVFDLIRDPYEQ 365
Cdd:pfam14707   4 EFLFHYCGAALHAVRWGPYKAHFFT------PSFDPPGAEGCYGSKV-------------PVTHHDPPLLFDLERDPSEK 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17559078   366 YPLQ-NTVKSQEIRFQAMQRLSEHKSSLVKVKNVLGSYNKT----LIPCC-NPPSCKC 417
Cdd:pfam14707  65 YPLSpDSPEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLwdpwLQPCCpTFPACTC 122
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-141 3.89e-30

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 117.34  E-value: 3.89e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGhPTQEYT-QVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGI---VGGRRVFVP 108
Cdd:cd16149   1 PNILFILTDDQGPWALGCYG-NSEAVTpNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwIVEGSHGKT 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 17559078 109 YDIGGLPKSETTMAEMLQEAGYATGMVGKWHLG 141
Cdd:cd16149  80 KKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG 112
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-244 1.20e-29

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 118.86  E-value: 1.20e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGhPTQEYT-QVDRMAAEGTRFTQAYsADSMCSPSRAGFITGRLPIRLGIVGGRrvfvpydi 111
Cdd:cd16151   1 PNIILIMADDLGYECIGCYG-GESYKTpNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGY-------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 ggLPKSETTMAEMLQEAGYATGMVGKWHLGinenNATDGAHLPSKRGF-EYVgvnlpftnVWQCDTTREFYdKGPDPSLC 190
Cdd:cd16151  71 --LDPKQKTFGHLLKDAGYATAIAGKWQLG----GGRGDGDYPHEFGFdEYC--------LWQLTETGEKY-SRPATPTF 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559078 191 FLYDGddivqqpmKFEHMTENLVG--DWKRFL---MTRlaqdQHERPFFFYFSFPQVHS 244
Cdd:cd16151 136 NIRNG--------KLLETTEGDYGpdLFADFLidfIER----NKDQPFFAYYPMVLVHD 182
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
33-243 8.18e-28

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: 113.76  E-value: 8.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQeyT-QVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVFVPydi 111
Cdd:cd16027   1 PNILWIIADDLSPDLGGYGGNVVK--TpNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFP--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 ggLPKSETTMAEMLQEAGYATGMVGKWHLGInennatdgahlPSKRGFEYVGVNLPFTNVWQCDTTREFYdkgpdpslcf 191
Cdd:cd16027  76 --LPDGVKTLPELLREAGYYTGLIGKTHYNP-----------DAVFPFDDEMRGPDDGGRNAWDYASNAA---------- 132
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17559078 192 lydgddivqqpmkfehmtenlvgDWkrflmtrLAQDQHERPFFFYFSFPQVH 243
Cdd:cd16027 133 -----------------------DF-------LNRAKKGQPFFLWFGFHDPH 154
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
33-254 4.94e-25

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: 106.46  E-value: 4.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRvfvpydiG 112
Cdd:cd16031   3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG-------P 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 113 GLPKSETTMAEMLQEAGYATGMVGKWHLGINENNAtdgahlpsKRGFEYvgvnlpftnvWqcdttREFYDKG--PDPSlc 190
Cdd:cd16031  76 LFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLP--------PPGFDY----------W-----VSFPGQGsyYDPE-- 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559078 191 FLYDGDDIVQQPmkfeHMTEnLVGDW-KRFLMTRLAQdqheRPFFFYFSFPQVHSTQFASKRFRG 254
Cdd:cd16031 131 FIENGKRVGQKG----YVTD-IITDKaLDFLKERDKD----KPFCLSLSFKAPHRPFTPAPRHRG 186
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
32-244 3.05e-24

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


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 103.80  E-value: 3.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  32 HPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVfvpydi 111
Cdd:cd16034   1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 112 ggLPKSETTMAEMLQEAGYATGMVGKWHL-GINENNATDGAHLPSKR---GFEYvgvnlpftnvWQcdttreFYDKGPDP 187
Cdd:cd16034  75 --LPPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRADDYTPPPErrhGFDY----------WK------GYECNHDH 136
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559078 188 SLCFLYDGDDIVQQPMKF--EHMTENLVgdwkRFLMTRLAQDQherPFFFYFSFPQVHS 244
Cdd:cd16034 137 NNPHYYDDDGKRIYIKGYspDAETDLAI----EYLENQADKDK---PFALVLSWNPPHD 188
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-252 1.44e-23

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


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 101.91  E-value: 1.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVFVPYDiG 112
Cdd:cd16033   1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYS-R 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 113 GLPKSETTMAEMLQEAGYATGMVGKWHLGiNENNATDgahlpskRGF-EYVGVnlpftnvwqcDTTREFYdkgpdpslcf 191
Cdd:cd16033  80 GLPPGVETFSEDLREAGYRNGYVGKWHVG-PEETPLD-------YGFdEYLPV----------ETTIEYF---------- 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559078 192 lydgddIVQQPMKFehmtenlvgdwkrflMTRLAQDqhERPFFFYFSFPQVHSTQFASKRF 252
Cdd:cd16033 132 ------LADRAIEM---------------LEELAAD--DKPFFLRVNFWGPHDPYIPPEPY 169
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
31-141 3.57e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 97.64  E-value: 3.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  31 RHPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSM----CSPSRAGFITGRlpirlgivggrRVF 106
Cdd:cd16155   1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR-----------TLF 69
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17559078 107 VPYDIGG--LPKSETTMAEMLQEAGYATGMVGKWHLG 141
Cdd:cd16155  70 HAPEGGKaaIPSDDKTWPETFKKAGYRTFATGKWHNG 106
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
32-140 1.02e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 93.45  E-value: 1.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  32 HPNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGivggrrVFVpyDI 111
Cdd:cd16152   1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG------CFR--NG 72
                        90       100
                ....*....|....*....|....*....
gi 17559078 112 GGLPKSETTMAEMLQEAGYATGMVGKWHL 140
Cdd:cd16152  73 IPLPADEKTLAHYFRDAGYETGYVGKWHL 101
PRK13759 PRK13759
arylsulfatase; Provisional
30-244 1.95e-20

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 93.58  E-value: 1.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078   30 PRHPNIVILMIDDLgYGD-IASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRRVfVP 108
Cdd:PRK13759   4 TKKPNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDV-VP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  109 YDIgglpksETTMAEMLQEAGYATGMVGKWH-------LGInENNATDGAHLPSKRgfeyvgvNLPFTNVWQCDTTREFY 181
Cdd:PRK13759  82 WNY------KNTLPQEFRDAGYYTQCIGKMHvfpqrnlLGF-HNVLLHDGYLHSGR-------NEDKSQFDFVSDYLAWL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  182 ---DKGPDPSLCFL-YDGDDIVQQPMKFE---HMTENLVGDWKRFLMTRlaqdQHERPFFFYFSFPQVHS 244
Cdd:PRK13759 148 rekAPGKDPDLTDIgWDCNSWVARPWDLEerlHPTNWVGSESIEFLRRR----DPTKPFFLKMSFARPHS 213
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-238 4.03e-19

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 86.83  E-value: 4.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGGRrvfvpydig 112
Cdd:cd16148   1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGP--------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 113 gLPKSETTMAEMLQEAGYATGMVgkwhlginennaTDGAHLPSKRGFeyvgvnlpftnvwqcdttrefyDKGPDPSLCFL 192
Cdd:cd16148  72 -LEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGF----------------------DRGFDTFEDFR 116
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17559078 193 YDGDDIVQQPMKFEHMTENLVGDWkrflmtrLAQDQHERPFF---FYFS 238
Cdd:cd16148 117 GQEGDPGEEGDERAERVTDRALEW-------LDRNADDDPFFlflHYFD 158
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
33-139 3.53e-18

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: 84.94  E-value: 3.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIvggrrvfvpYDIG 112
Cdd:cd16032   1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA---------YDNA 71
                        90       100
                ....*....|....*....|....*...
gi 17559078 113 G-LPKSETTMAEMLQEAGYATGMVGKWH 139
Cdd:cd16032  72 AeFPADIPTFAHYLRAAGYRTALSGKMH 99
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
33-244 1.12e-17

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: 84.52  E-value: 1.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLgygDIASYGHPTQEYTQvDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGgrrVFVPYdiG 112
Cdd:cd16147   2 PNIVLILTDDQ---DVELGSMDPMPKTK-KLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTN---NSPPG--G 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 113 GLPKS------ETTMAEMLQEAGYATGMVGKWhlgINENNATDG-AHLPskRGF-EYVGVNLPFTNVWqcdTTREFYDKG 184
Cdd:cd16147  73 GYPKFwqngleRSTLPVWLQEAGYRTAYAGKY---LNGYGVPGGvSYVP--PGWdEWDGLVGNSTYYN---YTLSNGGNG 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559078 185 PDPslcFLYDGDdivqqpmkfeHMTeNLVGDwK--RFLMTRLAQDqheRPFFFYFSFPQVHS 244
Cdd:cd16147 145 KHG---VSYPGD----------YLT-DVIAN-KalDFLRRAAADD---KPFFLVVAPPAPHG 188
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-161 2.42e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 82.59  E-value: 2.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIvggrrvfvpYDIG 112
Cdd:cd16037   1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGV---------WDNA 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17559078 113 G-LPKSETTMAEMLQEAGYATGMVGKWH-LGINENNatdgahlpskrGFEY 161
Cdd:cd16037  72 DpYDGDVPSWGHALRAAGYETVLIGKLHfRGEDQRH-----------GFRY 111
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-171 7.69e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 77.42  E-value: 7.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYG--HPTQEYTQ--------VDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGG 102
Cdd:cd16153   2 PNILWIITDDQRVDSLSCYNnaHTGKSESRlgyvespnIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 103 RRVFVPYDIGGLpksetTMAEMLQEAGYATGMVGKWHLG------INENNATDGAHLPSKRG-------FEYVGVNLPFT 169
Cdd:cd16153  82 EAAHPALDHGLP-----TFPEVLKKAGYQTASFGKSHLEafqrylKNANQSYKSFWGKIAKGadsdkpfFVRLSFLQPHT 156

                ..
gi 17559078 170 NV 171
Cdd:cd16153 157 PV 158
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
33-137 2.19e-15

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: 77.61  E-value: 2.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYgDIASYGHPtqeYTQ---VDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGgrrvFVPY 109
Cdd:cd16030   3 PNVLFIAVDDLRP-WLGCYGGH---PAKtpnIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYD----NNSY 74
                        90       100
                ....*....|....*....|....*...
gi 17559078 110 DIGGLPKSeTTMAEMLQEAGYATGMVGK 137
Cdd:cd16030  75 FRKVAPDA-VTLPQYFKENGYTTAGVGK 101
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-165 2.80e-15

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: 77.00  E-value: 2.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGH-------PTqeytqVDRMAAEGTRFTQAYsADSMCSPSRAGFITGRLPIRLGIVggrrv 105
Cdd:cd16154   1 PNILLIIADDQGLDSSAQYSLssdlpvtPT-----LDSLANSGIVFDNLW-ATPACSPTRATILTGKYGFRTGVL----- 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559078 106 FVPydiGGLPKSETTMAEML----QEAGYATGMVGKWHLGINENNATDGAHLPSkrgfeYVGVN 165
Cdd:cd16154  70 AVP---DELLLSEETLLQLLikdaTTAGYSSAVIGKWHLGGNDNSPNNPGGIPY-----YAGIL 125
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-140 2.39e-14

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


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 73.40  E-value: 2.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGY-----GDIASYGHPTQEytqvdRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGivggrrVFV 107
Cdd:cd16035   1 PNILLILTDQERYpppwpAGWAALNLPARE-----RLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTG------VTD 69
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17559078 108 ---PYDIGGLPKSETTMAEMLQEAGYATGMVGKWHL 140
Cdd:cd16035  70 tlgSPMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHL 105
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
33-140 5.76e-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: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 73.42  E-value: 5.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPirlgIVGGRRvfvpyDIG 112
Cdd:cd16150   1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYP----HVNGHR-----TLH 71
                        90       100
                ....*....|....*....|....*....
gi 17559078 113 GL-PKSETTMAEMLQEAGYATGMVGKWHL 140
Cdd:cd16150  72 HLlRPDEPNLLKTLKDAGYHVAWAGKNDD 100
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
33-136 7.24e-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: 70.91  E-value: 7.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRF-TQAYSADSMCSPSRAGFITGRLPIRLGIVG--GRRVFVPY 109
Cdd:cd00016   1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGngSADPELPS 80
                        90       100
                ....*....|....*....|....*..
gi 17559078 110 DIGGLPKSETTMAEMLQEAGYATGMVG 136
Cdd:cd00016  81 RAAGKDEDGPTIPELLKQAGYRTGVIG 107
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
33-140 1.16e-13

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: 72.80  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVGgrrvfvpyDIG 112
Cdd:cd16156   1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWT--------NCM 72
                        90       100
                ....*....|....*....|....*...
gi 17559078 113 GLPKSETTMAEMLQEAGYATGMVGKWHL 140
Cdd:cd16156  73 ALGDNVKTIGQRLSDNGIHTAYIGKWHL 100
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
33-139 9.53e-13

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: 69.60  E-value: 9.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  33 PNIVILMIDDLGYGDIASYGHPTQEYTQVDRMAAEGTRFTQAYSADSMCSPSRAGFITGRLPIRLGIVggrRVFVPydig 112
Cdd:cd16028   1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---WNGTP---- 73
                        90       100
                ....*....|....*....|....*..
gi 17559078 113 gLPKSETTMAEMLQEAGYATGMVGKWH 139
Cdd:cd16028  74 -LDARHLTLALELRKAGYDPALFGYTD 99
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
26-193 2.00e-08

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 55.91  E-value: 2.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078  26 QPPSPRHPNIVILMIDDLGYGDIASYGHPTqeytqVDRMAAEGTRFTQAYSA-DSMCSPSRAGFITGRLPIRLGIVG--- 101
Cdd:COG1524  17 AAAAPPAKKVVLILVDGLRADLLERAHAPN-----LAALAARGVYARPLTSVfPSTTAPAHTTLLTGLYPGEHGIVGngw 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559078 102 -----GRRVFVPYDIGGLPKSE-----TTMAEMLQEAGYATGMVGKWHLginENNATDGAHLPSKRGFEYVGVNLPFTNV 171
Cdd:COG1524  92 ydpelGRVVNSLSWVEDGFGSNsllpvPTIFERARAAGLTTAAVFWPSF---EGSGLIDAARPYPYDGRKPLLGNPAADR 168
                       170       180
                ....*....|....*....|..
gi 17559078 172 WQCDTTREfYDKGPDPSLCFLY 193
Cdd:COG1524 169 WIAAAALE-LLREGRPDLLLVY 189
 
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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