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Conserved domains on  [gi|125656171|ref|NP_033842|]
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arylsulfatase B precursor [Mus musculus]

Protein Classification

arylsulfatase( domain architecture ID 10888118)

arylsulfatase catalyzes the hydrolysis of sulfate ester bonds of a wide variety of aromatic substrates, similar to N-acetylgalactosamine 4-sulfatase (arylsulftase B) that hydolyzes the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
46-489 0e+00

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: 628.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSCVP 124
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSdQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 125 LDEKLLPQLLKEAGYATHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNgtrcaLDLRDGEEPA 204
Cdd:cd16029   81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGN-----DDLRDNEEPA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 205 KEYNNIYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPY----GFIQDKHRRIYAGMVSLMDEAVGN 280
Cdd:cd16029  156 WDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYedkfAHIKDEDRRTYAAMVSALDESVGN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 281 VTKALKSHGLWNNTVFIFSTDNGGQTRSG--GNNWPLRGRKGTLWEGGIRGTGFVASPLLK-QKGVKSRELMHITDWLPT 357
Cdd:cd16029  236 VVDALKAKGMLDNTLIVFTSDNGGPTGGGdgGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPpKRGTVSDGLMHVTDWLPT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 358 LVDLAGGSTNGTKPLDGFNMWKTISEGHPSPRVELLHNIDQDffdglpcpgknmtpakddsfplehsaFNTSIHAGIRYK 437
Cdd:cd16029  316 LLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDI--------------------------TRTTGGAAIRVG 369
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 125656171 438 NWKLLTGHPgcgywfpppsqsnvseippvdpptktlwLFDINQDPEERHDVS 489
Cdd:cd16029  370 DWKLIVGKP----------------------------LFNIENDPCERNDLA 393
 
Name Accession Description Interval E-value
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
46-489 0e+00

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: 628.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSCVP 124
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSdQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 125 LDEKLLPQLLKEAGYATHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNgtrcaLDLRDGEEPA 204
Cdd:cd16029   81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGN-----DDLRDNEEPA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 205 KEYNNIYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPY----GFIQDKHRRIYAGMVSLMDEAVGN 280
Cdd:cd16029  156 WDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYedkfAHIKDEDRRTYAAMVSALDESVGN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 281 VTKALKSHGLWNNTVFIFSTDNGGQTRSG--GNNWPLRGRKGTLWEGGIRGTGFVASPLLK-QKGVKSRELMHITDWLPT 357
Cdd:cd16029  236 VVDALKAKGMLDNTLIVFTSDNGGPTGGGdgGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPpKRGTVSDGLMHVTDWLPT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 358 LVDLAGGSTNGTKPLDGFNMWKTISEGHPSPRVELLHNIDQDffdglpcpgknmtpakddsfplehsaFNTSIHAGIRYK 437
Cdd:cd16029  316 LLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDI--------------------------TRTTGGAAIRVG 369
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 125656171 438 NWKLLTGHPgcgywfpppsqsnvseippvdpptktlwLFDINQDPEERHDVS 489
Cdd:cd16029  370 DWKLIVGKP----------------------------LFNIENDPCERNDLA 393
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
35-508 1.41e-101

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 311.43  E-value: 1.41e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  35 SPARASGATQPPHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGLQH 112
Cdd:COG3119   13 AAAAAAAAAKRPNILFILADDLGYGDLGCYGNpLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHRTGVTD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 113 YLIMTCQPscVPLDEKLLPQLLKEAGYATHMVGKWHLgmyrkeclptrrgfdtyfgyllgsedyytheacapieslngtr 192
Cdd:COG3119   93 NGEGYNGG--LPPDEPTLAELLKEAGYRTALFGKWHL------------------------------------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 193 caldlrdgeepakeynniYSTNIFTKRATTVIANH-PPEKPLFLYLAFQSVHDPLQVPEEYMEPYG-------------- 257
Cdd:COG3119  128 ------------------YLTDLLTDKAIDFLERQaDKDKPFFLYLAFNAPHAPYQAPEEYLDKYDgkdiplppnlaprd 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 258 ---FIQDKHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGGnnwpLRGRKGTLWEGGIRGTGFVA 334
Cdd:COG3119  190 lteEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHG----LRGGKGTLYEGGIRVPLIVR 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 335 SPLLKQKGVKSRELMHITDWLPTLVDLAGGSTNgtKPLDGFNMWKTISEGHPSPRvellhnidqdffdglpcpgknmtpa 414
Cdd:COG3119  266 WPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIP--EDLDGRSLLPLLTGEKAEWR------------------------- 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 415 kdDSFPLEHSAFNTsiHAGIRYKNWKLLTGHPGCGYWfpppsqsnvseippvdpptktlWLFDINQDPEERHDVSREHPH 494
Cdd:COG3119  319 --DYLYWEYPRGGG--NRAIRTGRWKLIRYYDDDGPW----------------------ELYDLKNDPGETNNLAADYPE 372
                        490
                 ....*....|....
gi 125656171 495 IVQNLLSRLQYYHE 508
Cdd:COG3119  373 VVAELRALLEAWLK 386
Sulfatase pfam00884
Sulfatase;
46-363 1.25e-72

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 233.08  E-value: 1.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171   46 PHVVFVLADDLGWNDLGFHGSVIR-TPHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGLQhylimTCQPSCV 123
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPtTPFLDRLAEEGLLFSNFYSgGTLTAPSRFALLTGLPPHNFGSY-----VSTPVGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  124 PLDEKLLPQLLKEAGYATHMVGKWHLGMYRKEClPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNGtrcaldlrdgeep 203
Cdd:pfam00884  76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS-PCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGG------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  204 akeynniYSTNIFTKRATTVIANhpPEKPLFLYLAFQSVHDPLQVPEEYMEPYGF------IQDKHRRIYAGMVSLMDEA 277
Cdd:pfam00884 142 -------VSDEALLDEALEFLDN--NDKPFFLVLHTLGSHGPPYYPDRYPEKYATfkpsscSEEQLLNSYDNTLLYTDDA 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  278 VGNVTKALKSHGLWNNTVFIFSTDNGGQTrSGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPT 357
Cdd:pfam00884 213 IGRVLDKLEENGLLDNTLVVYTSDHGESL-GEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPT 291

                  ....*.
gi 125656171  358 LVDLAG 363
Cdd:pfam00884 292 ILDLAG 297
PRK13759 PRK13759
arylsulfatase; Provisional
42-489 9.22e-35

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 136.72  E-value: 9.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  42 ATQPPHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDN-YYVQPLCTPSRSQLLTGRYQIHLGLQHYlimtcq 119
Cdd:PRK13759   3 QTKKPNIILIMVDQMRGDCLGCNGNkAVETPNLDMLASEGYNFENaYSAVPSCTPARAALLTGLSQWHHGRVGY------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 120 PSCVPLDEK-LLPQLLKEAGYATHMVGKWHLGMYRKEClptrrGFDtyfGYLLgsEDYYTHEAcapiesLNGTRCALDLR 198
Cdd:PRK13759  77 GDVVPWNYKnTLPQEFRDAGYYTQCIGKMHVFPQRNLL-----GFH---NVLL--HDGYLHSG------RNEDKSQFDFV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 199 D-----------GEEP-------------AKEYN---NIYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHDPLQVPEE 251
Cdd:PRK13759 141 SdylawlrekapGKDPdltdigwdcnswvARPWDleeRLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKR 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 252 YME------------------------------PYGFIQDKH----RRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFI 297
Cdd:PRK13759 221 YFDmykdadipdphigdweyaedqdpeggsidaLRGNLGEEYarraRAAYYGLITHIDHQIGRFLQALKEFGLLDNTIIL 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 298 FSTDNGGQTrsGGNNWplrGRKGTLWEGGIRGTGFVASP---LLKQKGVKSRELMHITDWLPTLVDLAGGSTngTKPLDG 374
Cdd:PRK13759 301 FVSDHGDML--GDHYL---FRKGYPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGTI--PDDVDG 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 375 FNMWKTISEGHPSPRvellhnidqDFFDGlpcpgknmtpakddsfplEHSAFNTSIHAgIRYKNWKLLtghpgcgyWFpp 454
Cdd:PRK13759 374 RSLKNLIFGQYEGWR---------PYLHG------------------EHALGYSSDNY-LTDGKWKYI--------WF-- 415
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 125656171 455 pSQSNVSEippvdpptktlwLFDINQDPEERHDVS 489
Cdd:PRK13759 416 -SQTGEEQ------------LFDLKKDPHELHNLS 437
 
Name Accession Description Interval E-value
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
46-489 0e+00

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: 628.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSCVP 124
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSdQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 125 LDEKLLPQLLKEAGYATHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNgtrcaLDLRDGEEPA 204
Cdd:cd16029   81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGN-----DDLRDNEEPA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 205 KEYNNIYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPY----GFIQDKHRRIYAGMVSLMDEAVGN 280
Cdd:cd16029  156 WDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYedkfAHIKDEDRRTYAAMVSALDESVGN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 281 VTKALKSHGLWNNTVFIFSTDNGGQTRSG--GNNWPLRGRKGTLWEGGIRGTGFVASPLLK-QKGVKSRELMHITDWLPT 357
Cdd:cd16029  236 VVDALKAKGMLDNTLIVFTSDNGGPTGGGdgGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPpKRGTVSDGLMHVTDWLPT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 358 LVDLAGGSTNGTKPLDGFNMWKTISEGHPSPRVELLHNIDQDffdglpcpgknmtpakddsfplehsaFNTSIHAGIRYK 437
Cdd:cd16029  316 LLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDI--------------------------TRTTGGAAIRVG 369
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 125656171 438 NWKLLTGHPgcgywfpppsqsnvseippvdpptktlwLFDINQDPEERHDVS 489
Cdd:cd16029  370 DWKLIVGKP----------------------------LFNIENDPCERNDLA 393
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
35-508 1.41e-101

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 311.43  E-value: 1.41e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  35 SPARASGATQPPHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGLQH 112
Cdd:COG3119   13 AAAAAAAAAKRPNILFILADDLGYGDLGCYGNpLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHRTGVTD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 113 YLIMTCQPscVPLDEKLLPQLLKEAGYATHMVGKWHLgmyrkeclptrrgfdtyfgyllgsedyytheacapieslngtr 192
Cdd:COG3119   93 NGEGYNGG--LPPDEPTLAELLKEAGYRTALFGKWHL------------------------------------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 193 caldlrdgeepakeynniYSTNIFTKRATTVIANH-PPEKPLFLYLAFQSVHDPLQVPEEYMEPYG-------------- 257
Cdd:COG3119  128 ------------------YLTDLLTDKAIDFLERQaDKDKPFFLYLAFNAPHAPYQAPEEYLDKYDgkdiplppnlaprd 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 258 ---FIQDKHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGGnnwpLRGRKGTLWEGGIRGTGFVA 334
Cdd:COG3119  190 lteEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHG----LRGGKGTLYEGGIRVPLIVR 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 335 SPLLKQKGVKSRELMHITDWLPTLVDLAGGSTNgtKPLDGFNMWKTISEGHPSPRvellhnidqdffdglpcpgknmtpa 414
Cdd:COG3119  266 WPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIP--EDLDGRSLLPLLTGEKAEWR------------------------- 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 415 kdDSFPLEHSAFNTsiHAGIRYKNWKLLTGHPGCGYWfpppsqsnvseippvdpptktlWLFDINQDPEERHDVSREHPH 494
Cdd:COG3119  319 --DYLYWEYPRGGG--NRAIRTGRWKLIRYYDDDGPW----------------------ELYDLKNDPGETNNLAADYPE 372
                        490
                 ....*....|....
gi 125656171 495 IVQNLLSRLQYYHE 508
Cdd:COG3119  373 VVAELRALLEAWLK 386
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
46-508 4.27e-101

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: 310.64  E-value: 4.27e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLQH-YL---IMTcqp 120
Cdd:cd16146    1 PNVILILTDDQGYGDLGFHGNpILKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHtILgreRMR--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 121 scvpLDEKLLPQLLKEAGYATHMVGKWHLGM---YRkeclPTRRGFDTYFGYLLG----SEDYYTHEACAPIESLNGTRc 193
Cdd:cd16146   78 ----LDETTLAEVFKDAGYRTGIFGKWHLGDnypYR----PQDRGFDEVLGHGGGgigqYPDYWGNDYFDDTYYHNGKF- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 194 aldlrdgeepaKEYNNiYSTNIFTKRATTVIANHpPEKPLFLYLAFQSVHDPLQVPEEYMEPY---GFIqDKHRRIYaGM 270
Cdd:cd16146  149 -----------VKTEG-YCTDVFFDEAIDFIEEN-KDKPFFAYLATNAPHGPLQVPDKYLDPYkdmGLD-DKLAAFY-GM 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 271 VSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTR-SGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELM 349
Cdd:cd16146  214 IENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLT 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 350 HITDWLPTLVDLAGGSTNGTKPLDGFNMWKTISEG--HPSPRVELLHNIDqdffdglpcpGKNMTPAKDdsfplehsafn 427
Cdd:cd16146  294 AHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGEsdPWPERTLFTHSGR----------WPPPPKKKR----------- 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 428 tsiHAGIRYKNWKLltghpgcgywfpppsqsnvseippVDPPTKTLWLFDINQDPEERHDVSREHPHIVQNLLSRLQYYH 507
Cdd:cd16146  353 ---NAAVRTGRWRL------------------------VSPKGFQPELYDIENDPGEENDVADEHPEVVKRLKAAYEAWW 405

                 .
gi 125656171 508 E 508
Cdd:cd16146  406 D 406
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
45-489 6.67e-99

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: 304.49  E-value: 6.67e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  45 PPHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSC 122
Cdd:cd16026    1 KPNIVVILADDLGYGDLGCYGSpLIKTPNIDRLAAEGVRFTDFYAaAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 VPLDEKLLPQLLKEAGYATHMVGKWHLGMyRKECLPTRRGFDTYFGyLLGSEDYYTHeacaPIESLNGTRCALDLRDGEE 202
Cdd:cd16026   81 LPPDEITIAEVLKKAGYRTALVGKWHLGH-QPEFLPTRHGFDEYFG-IPYSNDMWPF----PLYRNDPPGPLPPLMENEE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 203 pAKEYNNIYS--TNIFTKRATTVIANHPpEKPLFLYLAFQSVHDPLQVPEEYmepygfiQDKHRR-IYAGMVSLMDEAVG 279
Cdd:cd16026  155 -VIEQPADQSslTQRYTDEAVDFIERNK-DQPFFLYLAHTMPHVPLFASEKF-------KGRSGAgLYGDVVEELDWSVG 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 280 NVTKALKSHGLWNNTVFIFSTDNG---GQTRSGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLP 356
Cdd:cd16026  226 RILDALKELGLEENTLVIFTSDNGpwlEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 357 TLVDLAGGSTNGTKPLDGFNMWKTISEGHPSPRVELLHNidqdffdglpcpgknmtpakddsfplehsaFNTSIHAGIRY 436
Cdd:cd16026  306 TLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYY------------------------------YDGGDLQAVRS 355
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 125656171 437 KNWKLLtghpgcgywFPPPSQSNVSEIPPVDPPTKTLWLFDINQDPEERHDVS 489
Cdd:cd16026  356 GRWKLH---------LPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNVA 399
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
46-504 7.91e-93

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: 289.83  E-value: 7.91e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSC- 122
Cdd:cd16144    1 PNIVLILVDDLGWADLGCYGSkFYETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDn 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 -----------VPLDEKLLPQLLKEAGYATHMVGKWHLGMyRKECLPTRRGFDTYFGY-LLGSEDYYTHEACAPIESLNg 190
Cdd:cd16144   81 tklipppsttrLPLEEVTIAEALKDAGYATAHFGKWHLGG-EGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLE- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 191 trcalDLRDGEepakeynniYSTNIFTKRATTVIANHPpEKPLFLYLAFQSVHDPLQVPEEYMEPY-----GFIQDKHRR 265
Cdd:cd16144  159 -----DGPEGE---------YLTDRLTDEAIDFIEQNK-DKPFFLYLSHYAVHTPIQARPELIEKYekkkkGLRKGQKNP 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 266 IYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGGN---NWPLRGRKGTLWEGGIRGTGFVASPLLKQKG 342
Cdd:cd16144  224 VYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPptsNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPG 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 343 VKSRELMHITDWLPTLVDLAGGSTNGTKPLDGFNMwktiseghpsprVELLHnidqdffdglpcpGKNMTPAKDDSF--- 419
Cdd:cd16144  304 SVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSL------------VPLLK-------------GGEADLPRRALFwhf 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 420 PLEHSAFNTSiHAGIRYKNWKLLtghpgcgYWFpppsqsnvsEippvdppTKTLWLFDINQDPEERHDVSREHPHIVQNL 499
Cdd:cd16144  359 PHYHGQGGRP-ASAIRKGDWKLI-------EFY---------E-------DGRVELYNLKNDIGETNNLAAEMPEKAAEL 414

                 ....*
gi 125656171 500 LSRLQ 504
Cdd:cd16144  415 KKKLD 419
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
44-488 1.88e-84

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: 267.39  E-value: 1.88e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  44 QPPHVVFVLADDLGWNDLGFHGSVIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGL-QHYLIMTCQP-- 120
Cdd:cd16025    1 GRPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMgTMAELATGKPgy 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 121 -SCVPLDEKLLPQLLKEAGYATHMVGKWHLGMyrkeclptrrgfdtyfgyllgsEDYytheacapieslngtrcaldlrd 199
Cdd:cd16025   81 eGYLPDSAATIAEVLKDAGYHTYMSGKWHLGP----------------------DDY----------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 200 geepakeynniYSTNIFTKRATTVI-ANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPY---------------------- 256
Cdd:cd16025  116 -----------YSTDDLTDKAIEYIdEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYkgkydagwdalreerlerqkel 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 257 GFIQ-------------------DKHRR-------IYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGqtrSGG 310
Cdd:cd16025  185 GLIPadtkltprppgvpawdslsPEEKKlearrmeVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGA---SAE 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 311 NNW------PLRGRKGTLWEGGIRgTGFVASP--LLKQKGVKSRELMHITDWLPTLVDLAG----GSTNG--TKPLDGFN 376
Cdd:cd16025  262 PGWanasntPFRLYKQASHEGGIR-TPLIVSWpkGIKAKGGIRHQFAHVIDIAPTILELAGveypKTVNGvpQLPLDGVS 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 377 MwktiseghpsprvellhnidQDFFDGlpcpgkNMTPAKDDSFPLEHSAfntsiHAGIRYKNWKLLTGHPGcgywfppps 456
Cdd:cd16025  341 L--------------------LPTLDG------AAAPSRRRTQYFELFG-----NRAIRKGGWKAVALHPP--------- 380
                        490       500       510
                 ....*....|....*....|....*....|...
gi 125656171 457 qsnvseippvdPPTKTLW-LFDINQDPEERHDV 488
Cdd:cd16025  381 -----------PGWGDQWeLYDLAKDPSETHDL 402
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
46-376 4.77e-81

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: 252.74  E-value: 4.77e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPscv 123
Cdd:cd16022    1 PNILLIMTDDLGYDDLGCYGNpDIKTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRHGVRGNVGNGGGL--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 124 PLDEKLLPQLLKEAGYATHMVGKWHlgmyrkeclptrrgfdtyfgyllgsedyytheacapieslngtrcaldlrdgeep 203
Cdd:cd16022   78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 204 akeynniystniftKRATTVIANHPPEKPLFLYLAFQSVHDPLqvpeeymepygfiqdkhrrIYAGMVSLMDEAVGNVTK 283
Cdd:cd16022  103 --------------DEAIDFIERRDKDKPFFLYVSFNAPHPPF-------------------AYYAMVSAIDDQIGRILD 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 284 ALKSHGLWNNTVFIFSTDNGGQTRSGGnnwpLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPTLVDLAG 363
Cdd:cd16022  150 ALEELGLLDNTLIVFTSDHGDMLGDHG----LRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAG 225
                        330
                 ....*....|...
gi 125656171 364 GSTNgtKPLDGFN 376
Cdd:cd16022  226 IEPP--EGLDGRS 236
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
46-493 1.12e-79

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: 255.60  E-value: 1.12e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGL-QHYLIMTCQPsc 122
Cdd:cd16145    1 PNIIFILADDLGYGDLGCYGQkKIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLHTGHTRVrGNSEPGGQDP-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 VPLDEKLLPQLLKEAGYATHMVGKWHLGMYRKECLPTRRGFDTYFGYL--LGSEDYYtheacaPIESL-NGTRCALD--- 196
Cdd:cd16145   79 LPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLdqVHAHNYY------PEYLWrNGEKVPLPnnv 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 197 --LRDGEEPAKEYNNIYSTNIFTKRATTVIANHpPEKPLFLYLAFQSVHDPLQVPEEYMEPYGFIQDKH---------RR 265
Cdd:cd16145  153 ipPLDEGNNAGGGGGTYSHDLFTDEALDFIREN-KDKPFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGIyaylpwpqpEK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 266 IYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGGN--------NWPLRGRKGTLWEGGIRGTGFVASPL 337
Cdd:cd16145  232 AYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEhdpdffdsNGPLRGYKRSLYEGGIRVPFIARWPG 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 338 LKQKGVKSRELMHITDWLPTLVDLAGGSTngTKPLDGFNMWKTiseghpsprveLLhnidqdffdglpcpGKNmTPAKDD 417
Cdd:cd16145  312 KIPAGSVSDHPSAFWDFMPTLADLAGAEP--PEDIDGISLLPT-----------LL--------------GKP-QQQQHD 363
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125656171 418 SFPLEhsaFNTSIHA-GIRYKNWKLLtghpgcgywfpppsqsnvsEIPPVDPPTKtlwLFDINQDPEERHDVSREHP 493
Cdd:cd16145  364 YLYWE---FYEGGGAqAVRMGGWKAV-------------------RHGKKDGPFE---LYDLSTDPGETNNLAAQHP 415
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
46-488 4.82e-76

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: 244.75  E-value: 4.82e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS----VIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLqHYLIMTCQPS 121
Cdd:cd16142    1 PNILVILGDDIGWGDLGCYGGgigrGAPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGL-TTVGLPGSPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 122 CVPLDEKLLPQLLKEAGYATHMVGKWHLGMyRKECLPTRRGFDTYFGYLLGSEDYYTHEAcapieslngtrcALDlrdge 201
Cdd:cd16142   80 GLPPWEPTLAELLKDAGYATAQFGKWHLGD-EDGRLPTDHGFDEFYGNLYHTIDEEIVDK------------AID----- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 202 epakeynniystniFTKRattviaNHPPEKPLFLYLAFQSVHDPLQVPEEYMEpygfiQDKHRRIYAGMVSLMDEAVGNV 281
Cdd:cd16142  142 --------------FIKR------NAKADKPFFLYVNFTKMHFPTLPSPEFEG-----KSSGKGKYADSMVELDDHVGQI 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 282 TKALKSHGLWNNTVFIFSTDNGGQTRS--GGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPTLV 359
Cdd:cd16142  197 LDALDELGIADNTIVIFTTDNGPEQDVwpDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLA 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 360 DLAGgstnGTKPLDGFNMWKTISEGhpsprvellhnIDQ-DFFDGlpcpgknmtpaKDDSFPLEHSAFNTSIH-AGIRYK 437
Cdd:cd16142  277 ALAG----APDPKDKLLGKDRHIDG-----------VDQsPFLLG-----------KSEKSRRSEFFYFGEGElGAVRWK 330
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 125656171 438 NWKLLTghpgcgYWFPPPSQSNVSEIPPVDPPtktlWLFDINQDPEERHDV 488
Cdd:cd16142  331 NWKVHF------KAQEDTGGPTGEPFYVLTFP----LIFNLRRDPKERYDV 371
Sulfatase pfam00884
Sulfatase;
46-363 1.25e-72

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 233.08  E-value: 1.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171   46 PHVVFVLADDLGWNDLGFHGSVIR-TPHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGLQhylimTCQPSCV 123
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPtTPFLDRLAEEGLLFSNFYSgGTLTAPSRFALLTGLPPHNFGSY-----VSTPVGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  124 PLDEKLLPQLLKEAGYATHMVGKWHLGMYRKEClPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNGtrcaldlrdgeep 203
Cdd:pfam00884  76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS-PCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGG------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  204 akeynniYSTNIFTKRATTVIANhpPEKPLFLYLAFQSVHDPLQVPEEYMEPYGF------IQDKHRRIYAGMVSLMDEA 277
Cdd:pfam00884 142 -------VSDEALLDEALEFLDN--NDKPFFLVLHTLGSHGPPYYPDRYPEKYATfkpsscSEEQLLNSYDNTLLYTDDA 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  278 VGNVTKALKSHGLWNNTVFIFSTDNGGQTrSGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPT 357
Cdd:pfam00884 213 IGRVLDKLEENGLLDNTLVVYTSDHGESL-GEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPT 291

                  ....*.
gi 125656171  358 LVDLAG 363
Cdd:pfam00884 292 ILDLAG 297
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
46-489 4.80e-71

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: 232.48  E-value: 4.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHG--SVIRTPHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSC 122
Cdd:cd16143    1 PNIVIILADDLGYGDISCYNpdSKIPTPNIDRLAAEGMRFTDAHSpSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 VPLDEKLLPQLLKEAGYATHMVGKWHLGM--YRKECL-------------------PTRRGFDTYFGYllgsedyythea 181
Cdd:cd16143   81 IEPDRVTLAKMLKQAGYRTAMVGKWHLGLdwKKKDGKkaatgtgkdvdyskpikggPLDHGFDYYFGI------------ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 182 capieslngTRCALDLRdgeepakeynniystniFTKRATTVIANHP-PEKPLFLYLAFQSVHDPLQVPEEY-----MEP 255
Cdd:cd16143  149 ---------PASEVLPT-----------------LTDKAVEFIDQHAkKDKPFFLYFALPAPHTPIVPSPEFqgksgAGP 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 256 YG-FIQDkhrriyagmvslMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQT--------RSGGN-NWPLRGRKGTLWEG 325
Cdd:cd16143  203 YGdFVYE------------LDWVVGRILDALKELGLAENTLVIFTSDNGPSPyadykeleKFGHDpSGPLRGMKADIYEG 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 326 GIRgTGFVAS-PLLKQKGVKSRELMHITDWLPTLVDLAGGSTNGTKPLDGFNMWKT-ISEGHPSPRVELLHNidqdffdg 403
Cdd:cd16143  271 GHR-VPFIVRwPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPAlLGPKKQEVRESLVHH-------- 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 404 lpcpgknmtpAKDDSFplehsafntsihaGIRYKNWKLLTGHPGCGYWfpPPSQSNVSEIPPVDpptktlwLFDINQDPE 483
Cdd:cd16143  342 ----------SGNGSF-------------AIRKGDWKLIDGTGSGGFS--YPRGKEKLGLPPGQ-------LYNLSTDPG 389

                 ....*.
gi 125656171 484 ERHDVS 489
Cdd:cd16143  390 ESNNLY 395
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-487 7.08e-63

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: 210.15  E-value: 7.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGSV-IRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLQHYlimtcqpscvP 124
Cdd:cd16151    1 PNIILIMADDLGYECIGCYGGEsYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFG----------Y 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 125 LD--EKLLPQLLKEAGYATHMVGKWHLGMYR-KECLPTRRGFDTY--FGYLLGSEDYYTheacaPIESLNGtrcaldLRD 199
Cdd:cd16151   71 LDpkQKTFGHLLKDAGYATAIAGKWQLGGGRgDGDYPHEFGFDEYclWQLTETGEKYSR-----PATPTFN------IRN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 200 GEEPaKEYNNIYSTNIFTKRATTVIANHpPEKPLFLYLAFQSVHDPLQV--PEEYMEPYGFIQDKHRRIYAGMVSLMDEA 277
Cdd:cd16151  140 GKLL-ETTEGDYGPDLFADFLIDFIERN-KDQPFFAYYPMVLVHDPFVPtpDSPDWDPDDKRKKDDPEYFPDMVAYMDKL 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 278 VGNVTKALKSHGLWNNTVFIFSTDNG----GQTRSGGNNwpLRGRKGTLWEGGIRgTGFVAS-PLLKQKGVKSRELMHIT 352
Cdd:cd16151  218 VGKLVDKLEELGLRENTIIIFTGDNGthrpITSRTNGRE--VRGGKGKTTDAGTH-VPLIVNwPGLIPAGGVSDDLVDFS 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 353 DWLPTLVDLAGGSTNGTKPLDGFNMWKTISeghpsprvellhnidqdffdglpcpGKNMTPAKDDSFPLEHSAFNTSIHA 432
Cdd:cd16151  295 DFLPTLAELAGAPLPEDYPLDGRSFAPQLL-------------------------GKTGSPRREWIYWYYRNPHKKFGSR 349
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 125656171 433 GIRYKNWKLltghpgcgYWfpppsqsnvseippvdpPTKtlwLFDINQDPEERHD 487
Cdd:cd16151  350 FVRTKRYKL--------YA-----------------DGR---FFDLREDPLEKNP 376
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
45-395 1.44e-62

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: 209.63  E-value: 1.44e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  45 PPHVVFVLADDLGWNDLGFHG--SVIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGLQHYLIMTCQpS 121
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVGHNFLPTSV-G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 122 CVPLDEKLLPQLLKEAGYATHMVGKWHLGmYRKECLPTRRGFDTYFGYLlgsedyYTHEAcapieslngtrcaldlrdge 201
Cdd:cd16161   80 GLPLNETTLAEVLRQAGYATGMIGKWHLG-QREAYLPNSRGFDYYFGIP------FSHDS-------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 202 EPAKEYnniystnifTKRATTVIANHP-PEKPLFLYLAFQSVHDPLQVPEEYMEPygfiqDKHRRIYAGMVSLMDEAVGN 280
Cdd:cd16161  133 SLADRY---------AQFATDFIQRASaKDRPFFLYAALAHVHVPLANLPRFQSP-----TSGRGPYGDALQEMDDLVGQ 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 281 VTKALKSHGLWNNTVFIFSTDNGG---QTRSGGN--------NWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELM 349
Cdd:cd16161  199 IMDAVKHAGLKDNTLTWFTSDNGPwevKCELAVGpgtgdwqgNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALV 278
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 125656171 350 HITDWLPTLVDLAGGSTNGTKPLDGFNMWKTISEGHPSPRVELLHN 395
Cdd:cd16161  279 STLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHP 324
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
46-364 6.73e-58

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: 196.96  E-value: 6.73e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGSVIRTPHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGLQHyliMTCQPSCVP 124
Cdd:cd16027    1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTtAPVCSPSRSALLTGLYPHQNGAHG---LRSRGFPLP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 125 LDEKLLPQLLKEAGYATHMVGKWHLGmyrkeclptrRGFDTYFGYLLGSEDYYTHEAcapieslngtrcaldlRDGEEPA 204
Cdd:cd16027   78 DGVKTLPELLREAGYYTGLIGKTHYN----------PDAVFPFDDEMRGPDDGGRNA----------------WDYASNA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 205 KEYnniystniftkrattvIANHPPEKPLFLYLAFQSVH--------DPLQVPEEYMEPYGFIQD-----KHRRIYAGMV 271
Cdd:cd16027  132 ADF----------------LNRAKKGQPFFLWFGFHDPHrpyppgdgEEPGYDPEKVKVPPYLPDtpevrEDLADYYDEI 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 272 SLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQtrsggnnWPlRGrKGTLWEGGIRgTGFVAS-PLLKQKGVKSRELMH 350
Cdd:cd16027  196 ERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMP-------FP-RA-KGTLYDSGLR-VPLIVRwPGKIKPGSVSDALVS 265
                        330
                 ....*....|....
gi 125656171 351 ITDWLPTLVDLAGG 364
Cdd:cd16027  266 FIDLAPTLLDLAGI 279
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
45-527 2.44e-56

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: 195.74  E-value: 2.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  45 PPHVVFVLADDLGWNDLGFHG-SVIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSC 122
Cdd:cd16158    1 PPNIVLLFADDLGYGDLGCYGhPSSSTPNLDRLAANGLRFTDFYSSsPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 VPLDEKLLPQLLKEAGYATHMVGKWHLGM-YRKECLPTRRGFDTYFGYLlgsedyYTHEACaPIESLN----GTRCALDL 197
Cdd:cd16158   81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVgLNGTYLPTHQGFDHYLGIP------YSHDQG-PCQNLTcfppNIPCFGGC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 198 RDGEEPAKEYNN-------IYSTNI---FTKRATTVIANHPPE-KPLFLYLAFQSVHDPLQVPEEYMEPYGfiqdkhRRI 266
Cdd:cd16158  154 DQGEVPCPLFYNesivqqpVDLLTLeerYAKFAKDFIADNAKEgKPFFLYYASHHTHYPQFAGQKFAGRSS------RGP 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 267 YAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTR---SGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGV 343
Cdd:cd16158  228 FGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMrksRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGV 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 344 kSRELMHITDWLPTLVDLAGGSTNGTKpLDGFNMWKTISEGHPSPRvellhnidQDFFDGLPCPGKNmtpakddsfpleH 423
Cdd:cd16158  308 -THELASTLDILPTIAKLAGAPLPNVT-LDGVDMSPILFEQGKSPR--------QTFFYYPTSPDPD------------K 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 424 SAFNTSIHagiRYKNWKLLTGHPGCGYwFPPPSQSNVSEIPPVDPPTktlwLFDINQDPEERHDVSREhPHIVQ--NLLS 501
Cdd:cd16158  366 GVFAVRWG---KYKAHFYTQGAAHSGT-TPDKDCHPSAELTSHDPPL----LFDLSQDPSENYNLLGL-PEYNQvlKQIQ 436
                        490       500       510
                 ....*....|....*....|....*....|....
gi 125656171 502 RLQYYHEHSV---PSHF-----PPLDPRCDPKST 527
Cdd:cd16158  437 QVKERFEASMkfgESEInkgedPALEPCCKPGCT 470
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
44-504 9.02e-54

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: 187.74  E-value: 9.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  44 QPPHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGlqhylIMTCQPS 121
Cdd:cd16031    1 KRPNIIFILTDDHRYDALGCYGNpIVKTPNIDRLAKEGVRFDNAFVtTSICAPSRASILTGQYSHRHG-----VTDNNGP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 122 CVPLDEKLLPQLLKEAGYATHMVGKWHLGMYRKEClptRRGFDtYFGYLLGSEDYYTheacAPIESLNGtrcaldlRDGE 201
Cdd:cd16031   76 LFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLP---PPGFD-YWVSFPGQGSYYD----PEFIENGK-------RVGQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 202 EPakeynniYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPYG--------------------FIQD 261
Cdd:cd16031  141 KG-------YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEdvtipepetfddddyagrpeWARE 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 262 KHRRI--------------------YAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNG---GQtrsggnnwplRGR 318
Cdd:cd16031  214 QRNRIrgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGfflGE----------HGL 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 319 --KGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPTLVDLAGGSTngTKPLDGFNMWKTISEGHPSP-RVELLHN 395
Cdd:cd16031  284 fdKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPI--PEDMQGRSLLPLLEGEKPVDwRKEFYYE 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 396 idqdFFDGlpcPGKNMTPAkddsfplehsafntsiHAGIRYKNWKLLtghpgcgYWfpppsqsnvseipPVDPPTktlW- 474
Cdd:cd16031  362 ----YYEE---PNFHNVPT----------------HEGVRTERYKYI-------YY-------------YGVWDE---Ee 395
                        490       500       510
                 ....*....|....*....|....*....|..
gi 125656171 475 LFDINQDPEERHDV--SREHPHIVQNLLSRLQ 504
Cdd:cd16031  396 LYDLKKDPLELNNLanDPEYAEVLKELRKRLE 427
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
46-393 6.31e-52

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: 183.01  E-value: 6.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGSVIRTP-HLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHLGL--QHYLIMTCQPS 121
Cdd:cd16160    2 PNIVLFFADDMGYGDLASYGHPTQERgPIDDMAAEGIRFTQAYSaDSVCTPSRAALLTGRLPIRSGMygGTRVFLPWDIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 122 CVPLDEKLLPQLLKEAGYATHMVGKWHLGM--YRKE---CLPTRRGFDtYFGYLLgseDYYTHEACAP----IESLNGTR 192
Cdd:cd16160   82 GLPKTEVTMAEALKEAGYTTGMVGKWHLGIneNNHSdgaHLPSHHGFD-FVGTNL---PFTNSWACDDtgrhVDFPDRSA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 193 CALDLRDgEEPAKEYNNIYSTNIFTKRATTVIANHpPEKPLFLYLAFQSVHDPLQVPEEymepygFIQDKHRRIYAGMVS 272
Cdd:cd16160  158 CFLYYND-TIVEQPIQHEHLTETLVGDAKSFIEDN-QENPFFLYFSFPQTHTPLFASKR------FKGKSKRGRYGDNIN 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 273 LMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTR---SGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSrELM 349
Cdd:cd16160  230 EMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEyclEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVSH-EVV 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 125656171 350 HITDWLPTLVDLAGGSTNGTKPLDGFNMWKTISEGHPSPRVELL 393
Cdd:cd16160  309 STMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDIL 352
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-504 1.55e-51

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: 180.07  E-value: 1.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHG-SVIRTPHLDALAAGGVVLDNYYVQ-----PLCTPSRSQLLTGRYQIHLGLQHylimtcq 119
Cdd:cd16155    3 PNILFILADDQRADTIGALGnPEIQTPNLDRLARRGTSFTNAYNMggwsgAVCVPSRAMLMTGRTLFHAPEGG------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 120 PSCVPLDEKLLPQLLKEAGYATHMVGKWHlgmyrkeclptrrgfdtyfgyllgsedyytheacapieslngtrcaldlrd 199
Cdd:cd16155   76 KAAIPSDDKTWPETFKKAGYRTFATGKWH--------------------------------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 200 geepakeynniystNIFTKRATTVIANHP-PEKPLFLYLAFQSVHDPLQVPEEYMEPY---------------------G 257
Cdd:cd16155  105 --------------NGFADAAIEFLEEYKdGDKPFFMYVAFTAPHDPRQAPPEYLDMYppetiplpenflpqhpfdngeG 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 258 FIQD--------------KHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNG---GQtrSGgnnwpLRGrKG 320
Cdd:cd16155  171 TVRDeqlapfprtpeavrQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGlavGS--HG-----LMG-KQ 242
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 321 TLWEGGIRGTGFVASPLLKqKGVKSRELMHITDWLPTLVDLAGgsTNGTKPLDGFNMWKTISEGHPSPRVELLHnidqdf 400
Cdd:cd16155  243 NLYEHSMRVPLIISGPGIP-KGKRRDALVYLQDVFPTLCELAG--IEIPESVEGKSLLPVIRGEKKAVRDTLYG------ 313
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 401 fdglpcpgknmtpakddsfplehsAFNTSIHAGIRyKNWKLLtghpgcgywfpppsqsnvseipPVDPPTKTLWLFDINQ 480
Cdd:cd16155  314 ------------------------AYRDGQRAIRD-DRWKLI----------------------IYVPGVKRTQLFDLKK 346
                        490       500
                 ....*....|....*....|....*.
gi 125656171 481 DPEERHDVS--REHPHIVQNLLSRLQ 504
Cdd:cd16155  347 DPDELNNLAdePEYQERLKKLLAELK 372
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-377 5.61e-51

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: 179.30  E-value: 5.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHG-SVIRTPHLDALAAGGVVLDNYY-VQPLCTPSRSQLLTGRYQIHLGLQHylimtcqpSCV 123
Cdd:cd16034    2 PNILFIFADQHRAQALGCAGdDPVKTPNLDRLAKEGVVFTNAVsNYPVCSPYRASLLTGQYPLTNGVFG--------NDV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 124 PL--DEKLLPQLLKEAGYATHMVGKWHL-GMYRKECL-------PTRR-GFDTYFGYllGSEDYYTHeacaPIESLNgtr 192
Cdd:cd16034   74 PLppDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRaddytppPERRhGFDYWKGY--ECNHDHNN----PHYYDD--- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 193 caldlrdgeEPAKEYNNIYSTNIFTKRATTVIANH-PPEKPLFLYLAFQSVHDP-LQVPEEYMEPYGFIQDKHR------ 264
Cdd:cd16034  145 ---------DGKRIYIKGYSPDAETDLAIEYLENQaDKDKPFALVLSWNPPHDPyTTAPEEYLDMYDPKKLLLRpnvped 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 265 -----------RIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGGNNwplrgRKGTLWEGGIRGTGFV 333
Cdd:cd16034  216 kkeeaglredlRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-----NKQVPYEESIRVPFII 290
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 125656171 334 ASPLLKQKGVKSRELMHITDWLPTLVDLAGGSTNGTkpLDGFNM 377
Cdd:cd16034  291 RYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDL 332
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
45-385 9.77e-51

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: 180.36  E-value: 9.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  45 PPHVVFVLADDLGWNDLGFHGSVIR-TPHLDALAAGGVVLDNYY-VQPLCTPSRSQLLTGRYQIHLGL----QH----YL 114
Cdd:cd16157    1 KPNIILMLMDDMGWGDLGVFGEPSReTPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNGFyttnAHarnaYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 115 ---IMtcqpSCVPLDEKLLPQLLKEAGYATHMVGKWHLGmYRKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNGT 191
Cdd:cd16157   81 pqnIV----GGIPDSEILLPELLKKAGYRNKIVGKWHLG-HRPQYHPLKHGFDEWFGAPNCHFGPYDNKAYPNIPVYRDW 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 192 RCA--------LDLRDGEepakeyNNIysTNIFTKRATTVIAN-HPPEKPLFLYLAFQSVHDPLqvpeeYMEPyGFIQDK 262
Cdd:cd16157  156 EMIgryyeefkIDKKTGE------SNL--TQIYLQEALEFIEKqHDAQKPFFLYWAPDATHAPV-----YASK-PFLGTS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 263 HRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQT----RSGGNNWPLRGRKGTLWEGGIRGTGFVASPLL 338
Cdd:cd16157  222 QRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALisapEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGH 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 125656171 339 KQKGVKSRELMHITDWLPTLVDLAGGSTNGTKPLDGFNMWKTISEGH 385
Cdd:cd16157  302 IKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGK 348
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
45-485 3.20e-48

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: 174.78  E-value: 3.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  45 PPHVVFVLADDLGWNDLGFHG-SVIRTPHLDALAAGGVVLD-NYYVQPLCTPSRSQLLTGRYQIHLGLQH-----YLIMT 117
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGnDTIRTPNIDRLAKEGVKLThHLAAAPLCTPSRAAFLTGRYPIRSGMASshgmrVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 118 CQPSCVPLDEKLLPQLLKEAGYATHMVGKWHLGMYRKECL-----PTRRGFDTYFGYLL--------GSEDYYTHEACAP 184
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNdfchhPLNHGFDYFYGLPLtnlkdcgdGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 185 IESLNG----------------------------------------------TRCALdLRDG---EEPAkEYNNIysTNI 215
Cdd:cd16159  161 FPLLTAfvlitaltiflllylgavskrffvfllilsllfislfflllitnryFNCIL-MRNHevvEQPM-SLENL--TQR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 216 FTKRATTVIANHpPEKPLFLYLAFQSVHDPLqvpeeYMEPYGFIQDKHRRiYAGMVSLMDEAVGNVTKALKSHGLWNNTV 295
Cdd:cd16159  237 LTKEAISFLERN-KERPFLLVMSFLHVHTAL-----FTSKKFKGRSKHGR-YGDNVEEMDWSVGQILDALDELGLKDNTF 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 296 FIFSTDNGG--------QTRSGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPTLVDLAGGSTN 367
Cdd:cd16159  310 VYFTSDNGGhleeisvgGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLP 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 368 GTKPLDGFNMwktiseghpsprVELLhnidqdffdglpcpgKNMTPAKDDSFpLEHSAfNTSIHAgIRYKN------WKL 441
Cdd:cd16159  390 SDRIIDGRDL------------MPLL---------------TGQEKRSPHEF-LFHYC-GAELHA-VRYRPrdggavWKA 439
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 125656171 442 L--------TGHPGCGYWFPPPSQSNVSEIppvDPPTktlwLFDINQDPEER 485
Cdd:cd16159  440 HyftpnfypGTEGCCGTLLCRCFGDSVTHH---DPPL----LFDLSADPSES 484
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-366 7.59e-41

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


Pssm-ID: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 151.35  E-value: 7.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDL---GFHGSVIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLqhylimTCQPSC 122
Cdd:cd16154    1 PNILLIIADDQGLDSSaqySLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGV------LAVPDE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 VPLDEKLLPQLLKE----AGYATHMVGKWHLGmyrkECLPTRR---GFDTYFGYLLGS-EDYYTHEacapiESLNGTrca 194
Cdd:cd16154   75 LLLSEETLLQLLIKdattAGYSSAVIGKWHLG----GNDNSPNnpgGIPYYAGILGGGvQDYYNWN-----LTNNGQ--- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 195 ldlrdgeepaKEYNNIYSTNIFTKRATTVIANHppEKPLFLYLAFQSVHDPLQVPEEYMEPYGF------IQDKHRRIYA 268
Cdd:cd16154  143 ----------TTNSTEYATTKLTNLAIDWIDQQ--TKPWFLWLAYNAPHTPFHLPPAELHSRSLlgdsadIEANPRPYYL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 269 GMVSLMDEAVGNVTKALKSHGLwNNTVFIFSTDNG--GQTRsggNNWPLRGR-KGTLWEGGIRGTGFVASPLLKQKGVKS 345
Cdd:cd16154  211 AAIEAMDTEIGRLLASIDEEER-ENTIIIFIGDNGtpGQVV---DLPYTRNHaKGSLYEGGINVPLIVSGAGVERANERE 286
                        330       340
                 ....*....|....*....|.
gi 125656171 346 RELMHITDWLPTLVDLAGGST 366
Cdd:cd16154  287 SALVNATDLYATIAELAGVDA 307
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
45-363 2.79e-37

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: 141.21  E-value: 2.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  45 PPHVVFVLADDLGWNDLGFHGSVI-RTPHLDALAAGGVVLDN-YYVQPLCTPSRSQLLTGRYQIHLGLQHYLIMtcqpsc 122
Cdd:cd16152    1 KPNVIVFFTDQQRWDTLGCYGQPLdLTPNLDALAEEGVLFENaFTPQPVCGPARACLQTGLYPTETGCFRNGIP------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 VPLDEKLLPQLLKEAGYATHMVGKWHLGMYRKECLptrrgfdtyfgyllgsedyytheacapieslngtrcaldlrdgee 202
Cdd:cd16152   75 LPADEKTLAHYFRDAGYETGYVGKWHLAGYRVDAL--------------------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 203 pakeynniystnifTKRATTVIANHPPEKPLFLYLAF-----QSVHDPLQVPEEYMEPY----------GFIQDKHRRI- 266
Cdd:cd16152  110 --------------TDFAIDYLDNRQKDKPFFLFLSYlephhQNDRDRYVAPEGSAERFanfwvppdlaALPGDWAEELp 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 267 -YAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGG--QTRSggnnwplRGRKGTLWEGGIR------GTGFvaspl 337
Cdd:cd16152  176 dYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGChfRTRN-------AEYKRSCHESSIRvplviyGPGF----- 243
                        330       340
                 ....*....|....*....|....*.
gi 125656171 338 lkQKGVKSRELMHITDWLPTLVDLAG 363
Cdd:cd16152  244 --NGGGRVEELVSLIDLPPTLLDAAG 267
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-363 8.24e-36

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: 138.12  E-value: 8.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGSVI-RTPHLDALAAGGVVLDNYY-VQPLCTPSRSQLLTGRYQIHLGLQH-YLIMTCQPSC 122
Cdd:cd16033    1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNAYtPSPVCCPARASLLTGLYPHEHGVLNnVENAGAYSRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 VPLDEKLLPQLLKEAGYATHMVGKWHLGmyrKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNGTrcaldlrdgee 202
Cdd:cd16033   81 LPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFDEYLPVETTIEYFLADRAIEMLEELAAD----------- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 203 pakeynniystniftkrattvianhppEKPLFLYLAFQSVHDPLQVPEEY--------MEPYGFIQD-------KHRRI- 266
Cdd:cd16033  147 ---------------------------DKPFFLRVNFWGPHDPYIPPEPYldmydpedIPLPESFADdfedkpyIYRREr 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 267 -------------------YAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGGnnwplrgrkgtLWEGG- 326
Cdd:cd16033  200 krwgvdtedeedwkeiiahYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHR-----------LWDKGp 268
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 125656171 327 ------------IRGTGfvasplLKQKGVKSRELMHITDWLPTLVDLAG 363
Cdd:cd16033  269 fmyeetyripliIKWPG------VIAAGQVVDEFVSLLDLAPTILDLAG 311
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-365 2.01e-35

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: 133.13  E-value: 2.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHG-SVIRTPHLDALAAGGVVLDNYY-VQPLCTPSRSQLLTGRYQIHLGL-----QHYLIMTC 118
Cdd:cd16149    1 PNILFILTDDQGPWALGCYGnSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 119 QPSCVPLDEKLLPQLLKEAGYATHMVGKWHLGmyrkeclptrrgfdtyfgyllgsedyytheacapieslngtrcaldlr 198
Cdd:cd16149   81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 199 dgeepakeynniystnifTKRATTVIANHPPEKPLFLYLAFQSVHDPLQvpeeymepygfiqdkhrriYAGMVSLMDEAV 278
Cdd:cd16149  113 ------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------------YFAAVTGVDRNV 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 279 GNVTKALKSHGLWNNTVFIFSTDNG------GQTRSGGNNWPLrgrkgTLWEGGIRGTGFVASPLLKQKGVKSRELMHIT 352
Cdd:cd16149  156 GRLLDELEELGLTENTLVIFTSDNGfnmghhGIWGKGNGTFPL-----NMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAY 230
                        330
                 ....*....|...
gi 125656171 353 DWLPTLVDLAGGS 365
Cdd:cd16149  231 DFFPTLLELAGVD 243
PRK13759 PRK13759
arylsulfatase; Provisional
42-489 9.22e-35

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 136.72  E-value: 9.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  42 ATQPPHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDN-YYVQPLCTPSRSQLLTGRYQIHLGLQHYlimtcq 119
Cdd:PRK13759   3 QTKKPNIILIMVDQMRGDCLGCNGNkAVETPNLDMLASEGYNFENaYSAVPSCTPARAALLTGLSQWHHGRVGY------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 120 PSCVPLDEK-LLPQLLKEAGYATHMVGKWHLGMYRKEClptrrGFDtyfGYLLgsEDYYTHEAcapiesLNGTRCALDLR 198
Cdd:PRK13759  77 GDVVPWNYKnTLPQEFRDAGYYTQCIGKMHVFPQRNLL-----GFH---NVLL--HDGYLHSG------RNEDKSQFDFV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 199 D-----------GEEP-------------AKEYN---NIYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHDPLQVPEE 251
Cdd:PRK13759 141 SdylawlrekapGKDPdltdigwdcnswvARPWDleeRLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKR 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 252 YME------------------------------PYGFIQDKH----RRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFI 297
Cdd:PRK13759 221 YFDmykdadipdphigdweyaedqdpeggsidaLRGNLGEEYarraRAAYYGLITHIDHQIGRFLQALKEFGLLDNTIIL 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 298 FSTDNGGQTrsGGNNWplrGRKGTLWEGGIRGTGFVASP---LLKQKGVKSRELMHITDWLPTLVDLAGGSTngTKPLDG 374
Cdd:PRK13759 301 FVSDHGDML--GDHYL---FRKGYPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGTI--PDDVDG 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 375 FNMWKTISEGHPSPRvellhnidqDFFDGlpcpgknmtpakddsfplEHSAFNTSIHAgIRYKNWKLLtghpgcgyWFpp 454
Cdd:PRK13759 374 RSLKNLIFGQYEGWR---------PYLHG------------------EHALGYSSDNY-LTDGKWKYI--------WF-- 415
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 125656171 455 pSQSNVSEippvdpptktlwLFDINQDPEERHDVS 489
Cdd:PRK13759 416 -SQTGEEQ------------LFDLKKDPHELHNLS 437
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-390 9.01e-33

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 127.66  E-value: 9.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHG-SVIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGlqhylimtCQPSCV 123
Cdd:cd16037    1 PNILIIMSDEHNPDAMGCYGhPVVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETG--------VWDNAD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 124 PLDEKL--LPQLLKEAGYATHMVGKWHlgmYRKECLPTrrGFDTyfgyllgsEDYYTHEACAPIESlngtrcaldlrdge 201
Cdd:cd16037   73 PYDGDVpsWGHALRAAGYETVLIGKLH---FRGEDQRH--GFRY--------DRDVTEAAVDWLRE-------------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 202 epakeynniystniftkrattviaNHPPEKPLFLYLAFQSVHDPLQVPEEYMEPYgfiQDKHRRIYAGMVSLMDEAVGNV 281
Cdd:cd16037  126 ------------------------EAADDKPWFLFVGFVAPHFPLIAPQEFYDLY---VRRARAAYYGLVEFLDENIGRV 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 282 TKALKSHGLWNNTVFIFSTDNGGQTRSGGNNWplrgrKGTLWEGG------IRGTGFVAspllkqkGVKSRELMHITDWL 355
Cdd:cd16037  179 LDALEELGLLDNTLIIYTSDHGDMLGERGLWG-----KSTMYEESvrvpmiISGPGIPA-------GKRVKTPVSLVDLA 246
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 125656171 356 PTLVDLAGGSTNGTkpLDGFNMWKTISEGHPSPRV 390
Cdd:cd16037  247 PTILEAAGAPPPPD--LDGRSLLPLAEGPDDPDRV 279
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
44-363 1.34e-32

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: 129.62  E-value: 1.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  44 QPPHVVFVLADDLgwND-LGFHGS-VIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRY--QIHL-GLQHYLIMT 117
Cdd:cd16030    1 KKPNVLFIAVDDL--RPwLGCYGGhPAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRpdTTGVyDNNSYFRKV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 118 CQpscvplDEKLLPQLLKEAGYATHMVGK-WHlgMYRKECLPTRRGFDTYFgYLLGSEDYYTHEACAPIESLNGTRCALD 196
Cdd:cd16030   79 AP------DAVTLPQYFKENGYTTAGVGKiFH--PGIPDGDDDPASWDEPP-NPPGPEKYPPGKLCPGKKGGKGGGGGPA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 197 LRDGEEPAKEYNNIYSTNiftkRATTVIAN-HPPEKPLFLYLAFQSVHDPLQVPEEYMEPY------------------- 256
Cdd:cd16030  150 WEAADVPDEAYPDGKVAD----EAIEQLRKlKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYplesiplpnpfdpidlpev 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 257 -----------------------GFI----QDKHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNG---GQT 306
Cdd:cd16030  226 awndlddlpkygdipalnpgdpkGPLpdeqARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGwhlGEH 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 125656171 307 rsggNNWplrgRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPTLVDLAG 363
Cdd:cd16030  306 ----GHW----GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG 354
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
45-374 1.77e-32

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


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 128.44  E-value: 1.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  45 PPHVVFVLADDLGWNDlgfhGSVIRTPHLDA-LAAGGVVLDNYYV-QPLCTPSRSQLLTGRYqIHlglQHyLIMTCQPS- 121
Cdd:cd16147    1 RPNIVLILTDDQDVEL----GSMDPMPKTKKlLADQGTTFTNAFVtTPLCCPSRASILTGQY-AH---NH-GVTNNSPPg 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 122 -CVP------LDEKLLPQLLKEAGYATHMVGKwHLGMYRKECLPTR--RGFDTYFGYLLGSEDYYTHEAcapieslNGTR 192
Cdd:cd16147   72 gGYPkfwqngLERSTLPVWLQEAGYRTAYAGK-YLNGYGVPGGVSYvpPGWDEWDGLVGNSTYYNYTLS-------NGGN 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 193 caldlrdgEEPAKEYNNIYSTNIFTKRATTVIANHPPE-KPLFLYLAFQSVHDPLQVPEEYMEPYGFIQDKHRR------ 265
Cdd:cd16147  144 --------GKHGVSYPGDYLTDVIANKALDFLRRAAADdKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPppnnpd 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 266 ------------------------IYAG-MVSLM--DEAVGNVTKALKSHGLWNNTVFIFSTDNG---GQTRsggnnwpL 315
Cdd:cd16147  216 vsdkphwlrrlpplnptqiayideLYRKrLRTLQsvDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHR-------L 288
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 125656171 316 RGRKGTLWEGGIRGTGFVASPLLKqKGVKSRELMHITDWLPTLVDLAGGSTNgtKPLDG 374
Cdd:cd16147  289 PPGKRTPYEEDIRVPLLVRGPGIP-AGVTVDQLVSNIDLAPTILDLAGAPPP--SDMDG 344
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
46-374 7.36e-32

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: 125.00  E-value: 7.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHG-SVIRTPHLDALAAGGVVLDNYY-VQPLCTPSRSQLLTGRYQIHLGLqhYLIMTCQPSCV 123
Cdd:cd16032    1 PNILLIMADQLTAAALPAYGnTVVKTPNLDRLAARGVVFDNAYcNSPLCAPSRASMMTGRLPSRIGA--YDNAAEFPADI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 124 PLdeklLPQLLKEAGYATHMVGKWHLgmyrkeCLPTR-RGFDtyfgyllgsedyYTHEACApieslNGTRCALDLRDGEE 202
Cdd:cd16032   79 PT----FAHYLRAAGYRTALSGKMHF------VGPDQlHGFD------------YDEEVAF-----KAVQKLYDLARGED 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 203 pakeynniystniftkrattvianhppEKPLFLYLAFQSVHDPLQVPEEYMEPYgfIQdKHRRIYAGMVSLMDEAVGNVT 282
Cdd:cd16032  132 ---------------------------GRPFFLTVSFTHPHDPYVIPQEYWDLY--VR-RARRAYYGMVSYVDDKVGQLL 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 283 KALKSHGLWNNTVFIFSTDNG---GQtrsggnnwplRGR--KGTLWEGGIRGTGFVASPLLKQkGVKSRELMHITDWLPT 357
Cdd:cd16032  182 DTLERTGLADDTIVIFTSDHGdmlGE----------RGLwyKMSFFEGSARVPLIISAPGRFA-PRRVAEPVSLVDLLPT 250
                        330
                 ....*....|....*...
gi 125656171 358 LVDLAGGST-NGTKPLDG 374
Cdd:cd16032  251 LVDLAGGGTaPHVPPLDG 268
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-369 4.61e-31

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 121.50  E-value: 4.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGS-VIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGLQHYLImtcqpscv 123
Cdd:cd16148    1 MNVILIVIDSLRADHLGCYGYdRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGVWGGPL-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 124 PLDEKLLPQLLKEAGYATHMVGKWHLgmyrkecLPTRRGFDTYFgyllgseDYYtheacapieslngtrcalDLRDGEEP 203
Cdd:cd16148   73 EPDDPTLAEILRKAGYYTAAVSSNPH-------LFGGPGFDRGF-------DTF------------------EDFRGQEG 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 204 AKEYNNIYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHdplqvpeeymEPYGfiqdkhrriYAGMVSLMDEAVGNVTK 283
Cdd:cd16148  121 DPGEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPH----------EPYL---------YDAEVRYVDEQIGRLLD 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 284 ALKSHGLWNNTVFIFSTDNG------GQTrsGGNNWPlrgrkgtLWEGGIRgtgfVasPLL-----KQKGVKSRELMHIT 352
Cdd:cd16148  182 KLKELGLLEDTLVIVTSDHGeefgehGLY--WGHGSN-------LYDEQLH----V--PLIirwpgKEPGKRVDALVSHI 246
                        330
                 ....*....|....*..
gi 125656171 353 DWLPTLVDLAGGSTNGT 369
Cdd:cd16148  247 DIAPTLLDLLGVEPPDY 263
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
48-503 3.08e-28

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: 117.36  E-value: 3.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  48 VVFVLADDLGWNDLGFHG-SVIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGlqhyliMTCQPSCVPL 125
Cdd:cd16028    3 VLFITADQWRADCLSCLGhPLVKTPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRYLMNHR------SVWNGTPLDA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 126 DEKLLPQLLKEAGYATHMVGKWHL-----GMYRKEclPTRR-------GFDTYF---GYllGSED----YYTHEACApie 186
Cdd:cd16028   77 RHLTLALELRKAGYDPALFGYTDTspdprGLAPLD--PRLLsyelampGFDPVDrldEY--PAEDsdtaFLTDRAIE--- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 187 slngtrcALDLRDGEE----------------PAkEYNNIYSTNIFTK--RATTV---IANHPPEKPLF----LYLAFQS 241
Cdd:cd16028  150 -------YLDERQDEPwflhlsyirphppfvaPA-PYHALYDPADVPPpiRAESLaaeAAQHPLLAAFLerieSLSFSPG 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 242 VHDPLQVPEEYMepygfiqDKHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQtrsGGNNWpLRGrKGT 321
Cdd:cd16028  222 AANAADLDDEEV-------AQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ---LGDHW-LWG-KDG 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 322 LWEGGIRGTGFVASPLLKQKGVKSRELMHIT---DWLPTLVDLAGGSTngTKPLDGFNMWKTISEGHPSPRVELLHnIDQ 398
Cdd:cd16028  290 FFDQAYRVPLIVRDPRREADATRGQVVDAFTesvDVMPTILDWLGGEI--PHQCDGRSLLPLLAGAQPSDWRDAVH-YEY 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 399 DFFDGlpcpgknmtpakddSFPLEHSAFNTSIH----AGIRYKNWKLLTghpgcgywFPppsqsnvsEIPPVdpptktlw 474
Cdd:cd16028  367 DFRDV--------------STRRPQEALGLSPDecslAVIRDERWKYVH--------FA--------ALPPL-------- 408
                        490       500       510
                 ....*....|....*....|....*....|.
gi 125656171 475 LFDINQDPEERHDVSR--EHPHIVQNLLSRL 503
Cdd:cd16028  409 LFDLKNDPGELRDLAAdpAYAAVVLRYAQKL 439
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-379 2.94e-26

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


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 108.23  E-value: 2.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLGFHGSV-----------IRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYQIHLGLQHY 113
Cdd:cd16153    2 PNILWIITDDQRVDSLSCYNNAhtgksesrlgyVESPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGVYGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 114 LIMTCQPSCVPLdekLLPQLLKEAGYATHMVGKWHLGMYRKeclptrrgfdtyfgYLlgsedyytheacapieslngtrc 193
Cdd:cd16153   82 EAAHPALDHGLP---TFPEVLKKAGYQTASFGKSHLEAFQR--------------YL----------------------- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 194 aldlrdgEEPAKEYNNIYSTNIFTKRattvianhpPEKPLFLYLAFQSVHDPLQVPEEYMEpygfiqdkhRRIYAGMVSL 273
Cdd:cd16153  122 -------KNANQSYKSFWGKIAKGAD---------SDKPFFVRLSFLQPHTPVLPPKEFRD---------RFDYYAFCAY 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 274 MDEAVGNVTKALKSHGLWN---NTVFIFSTDNGgqtrsggnnWPLrGRKG-----TLWEGGIRGTGFVASPLLKQKGVKS 345
Cdd:cd16153  177 GDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHG---------WHL-GEQGilakfTFWPQSHRVPLIVVSSDKLKAPAGK 246
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 125656171 346 R--ELMHITDWLPTLVDLAGGSTNGTKPLDGFNMWK 379
Cdd:cd16153  247 VrhDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-363 2.51e-25

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 108.48  E-value: 2.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLG-FHGSVIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRY---QIHLGLQHYLimtcQP 120
Cdd:cd16150    1 PNIVIFVADQLRADSLGhLGNPAAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGWYphvNGHRTLHHLL----RP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 121 scvplDEKLLPQLLKEAGYATHMVGKWHlgmyrkeCLPTRRGFDTYfgyllgsedyytheacapieslngtrCALDlrdg 200
Cdd:cd16150   77 -----DEPNLLKTLKDAGYHVAWAGKND-------DLPGEFAAEAY--------------------------CDSD---- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 201 eepakeYNNIYStniftkrATTVIANHPPEKPLFLYLAFQSVHDPLQVPEEY---------------------------- 252
Cdd:cd16150  115 ------EACVRT-------AIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWfsmidreklpprrppglrakgkpsmleg 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 253 MEPYGF------IQDKHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGG--NNWPlrgrkgtlwe 324
Cdd:cd16150  182 IEKQGLdrwseeRWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGlvEKWP---------- 251
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 125656171 325 ggirgTGF----VASPLLKQ--KGVKSR---ELMHITDWLPTLVDLAG 363
Cdd:cd16150  252 -----NTFedclTRVPLIIKppGGPAGGvsdALVELVDIPPTLLDLAG 294
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
46-404 1.28e-23

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: 103.62  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLG-FHGSVIRTPHLDALAAGGVVLDN-YYVQPLCTPSRSQLLTGRYQiHlglqhylimTCQP--S 121
Cdd:cd16156    1 KQFIFIMTDTQRWDMVGcYGNKAMKTPNLDRLAAEGVRFDSaYTTQPVCGPARSGLFTGLYP-H---------TNGSwtN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 122 CVPLDE--KLLPQLLKEAGYATHMVGKWHLGmyrkeclptrrGFDtYFGYllG------SEDYYTHEAC----APIESLN 189
Cdd:cd16156   71 CMALGDnvKTIGQRLSDNGIHTAYIGKWHLD-----------GGD-YFGN--GicpqgwDPDYWYDMRNyldeLTEEERR 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 190 GTRCALDLRDGEEPAKEYNniYSTNIfTKRATTVIANHpPEKPLFLYLAFQSVHDPLQVPEEYMEPY-GFIQDK------ 262
Cdd:cd16156  137 KSRRGLTSLEAEGIKEEFT--YGHRC-TNRALDFIEKH-KDEDFFLVVSYDEPHHPFLCPKPYASMYkDFEFPKgenayd 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 263 -------HRRIYA-------------------GMVSLMDEAVGNVTKALKSHGlwNNTVFIFSTDNGGQTRSGG------ 310
Cdd:cd16156  213 dlenkplHQRLWAgakphedgdkgtikhplyfGCNSFVDYEIGRVLDAADEIA--EDAWVIYTSDHGDMLGAHKlwakgp 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 311 ------NNWPLRGRkgtlWEGGIRGTGFVASPllkqkgvksreLMHItDWLPTLVDLAGgsTNGTKPLDGFNMWKTISEG 384
Cdd:cd16156  291 avydeiTNIPLIIR----GKGGEKAGTVTDTP-----------VSHI-DLAPTILDYAG--IPQPKVLEGESILATIEDP 352
                        410       420
                 ....*....|....*....|....*
gi 125656171 385 HPSPRVELL-----HNIDQDFFDGL 404
Cdd:cd16156  353 EIPENRGVFvefgrYEVDHDGFGGF 377
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
71-365 9.03e-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: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 87.26  E-value: 9.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  71 PHLDALAAGGVVLDNYYV-QPLCTPSRSQLLTGRYQIHlglqHYLIMTCQPSCVPLDEKLLPQL---LKEAGYATHMVGK 146
Cdd:cd16035   27 PARERLAANGLSFENHYTaACMCSPSRSTLYTGLHPQQ----TGVTDTLGSPMQPLLSPDVPTLghmLRAAGYYTAYKGK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 147 WHLGmyrkeclptrrgfdtyfGYLLGSEDY---YTHEACAPieslngtrcaldLRDGEEPAKEynniystniftkrattv 223
Cdd:cd16035  103 WHLS-----------------GAAGGGYKRdpgIAAQAVEW------------LRERGAKNAD----------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 224 ianhppEKPLFLYLAFQSVHDPLQVPEEYMEPYgfiqdKHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNG 303
Cdd:cd16035  137 ------GKPWFLVVSLVNPHDIMFPPDDEERWR-----RFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG 205
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125656171 304 GQTRSGGnnwpLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELM-HItDWLPTLVDLAGGS 365
Cdd:cd16035  206 EMGGAHG----LRGKGFNAYEEALHVPLIISHPDLFGTGQTTDALTsHI-DLLPTLLGLAGVD 263
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
46-362 9.73e-15

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: 73.61  E-value: 9.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGWNDLG-FHGSVIRTPHLDALAAGGVVLDNYYVQPLC--TPSRSQLLTGRYQIHLGlqhyliMTCQPSC 122
Cdd:cd00016    1 KHVVLIVLDGLGADDLGkAGNPAPTTPNLKRLASEGATFNFRSVSPPTssAPNHAALLTGAYPTLHG------YTGNGSA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 123 VPLDEK----------LLPQLLKEAGYATHMVGkwhlgmyrkeclptrrgFDTYFGYLLgsedyytheacapieslngtr 192
Cdd:cd00016   75 DPELPSraagkdedgpTIPELLKQAGYRTGVIG-----------------LLKAIDETS--------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 193 caldlrdgeepakeynniystniftkrattvianhpPEKPLFLYLAFQSVHDPLQVPEEYMEPYGfiqdkhrriyaGMVS 272
Cdd:cd00016  117 ------------------------------------KEKPFVLFLHFDGPDGPGHAYGPNTPEYY-----------DAVE 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 273 LMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGqTRSGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHiT 352
Cdd:cd00016  150 EIDERIGKVLDALKKAGDADDTVIIVTADHGG-IDKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQ-Y 227
                        330
                 ....*....|
gi 125656171 353 DWLPTLVDLA 362
Cdd:cd00016  228 DIAPTLADLL 237
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
46-363 1.18e-14

Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.


Pssm-ID: 293739 [Multi-domain]  Cd Length: 283  Bit Score: 74.26  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLA---DDLGWNDLGFHGSVirTPHLDALAAGGVVLDNYYVQPLCTP-SRSQ--LLTGRYQIHLG--LQHYLIMT 117
Cdd:cd16015    1 PNVIVILLesfSDPYIDKDVGGEDL--TPNLNKLAKEGLYFGNFYSPGFGGGtANGEfeVLTGLPPLPLGsgSYTLYKLN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 118 CQPScvpldeklLPQLLKEAGYATHMVGKWHLGMYRkeclptRRGFDTYFGYllgsEDYYtheacapieslngtrcalDL 197
Cdd:cd16015   79 PLPS--------LPSILKEQGYETIFIHGGDASFYN------RDSVYPNLGF----DEFY------------------DL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 198 RDGEEPAKEYNNIY-STNIFTKRATTVIANHPpEKPLFLYLafQSV--HDPLQVPEEYMEPYGFIQDKHRRI--YAGMVS 272
Cdd:cd16015  123 EDFPDDEKETNGWGvSDESLFDQALEELEELK-KKPFFIFL--VTMsnHGPYDLPEEKKDEPLKVEEDKTELenYLNAIH 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 273 LMDEAVGNVTKALKSHGLWNNTVFIFSTD---NGGQTRSGGNNWPLRGRKGTLweggirgtgFVASPLLKQKGVKSRELM 349
Cdd:cd16015  200 YTDKALGEFIEKLKKSGLYENTIIVIYGDhlpSLGSDYDETDEDPLDLYRTPL---------LIYSPGLKKPKKIDRVGS 270
                        330
                 ....*....|....
gi 125656171 350 HItDWLPTLVDLAG 363
Cdd:cd16015  271 QI-DIAPTLLDLLG 283
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
35-367 3.85e-13

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 71.99  E-value: 3.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  35 SPARASGATQPPHVVFVLADDLGWNDLGFHG---SVirTPHLDALAAGGVVLDNYYVQplcTP--SRSQ--LLTGRYQIH 107
Cdd:COG1368  224 PTPNPFGPAKKPNVVVILLESFSDFFIGALGngkDV--TPFLDSLAKESLYFGNFYSQ---GGrtSRGEfaVLTGLPPLP 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 108 LG--LQHYLIMTcQPScvpldeklLPQLLKEAGYATHMV----GKWhlgMYRKECLPtRRGFDTYFGyllgsEDYYTHEA 181
Cdd:COG1368  299 GGspYKRPGQNN-FPS--------LPSILKKQGYETSFFhggdGSF---WNRDSFYK-NLGFDEFYD-----REDFDDPF 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 182 CAPieslngtrcaLDLRDGEepakeynniystniFTKRATTVIANHPpeKPLFLYLAFQSVHDPLQVPEEYMEPYGFIQD 261
Cdd:COG1368  361 DGG----------WGVSDED--------------LFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEEDKKIPDYGKT 414
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 262 KHRRiYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGqtRSGGNNWPLrgrkgtLWEGGIRGTGFVASPLLKQK 341
Cdd:COG1368  415 TLNN-YLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP--RSPGKTDYE------NPLERYRVPLLIYSPGLKKP 485
                        330       340
                 ....*....|....*....|....*.
gi 125656171 342 GVKSReLMHITDWLPTLVDLAGGSTN 367
Cdd:COG1368  486 KVIDT-VGSQIDIAPTLLDLLGIDYP 510
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
46-383 1.12e-08

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


Pssm-ID: 293781 [Multi-domain]  Cd Length: 366  Bit Score: 57.17  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  46 PHVVFVLADDLGwNDLGFHG--SVIRTPHLDALAAGGVVLDNYYVQ-PLCTPSRSQLLTGRYqIHL--GLQHYlimtcqp 120
Cdd:cd16171    1 PNVVMVMSDSFD-GRLTFRPgnQVVDLPYINFMKQHGSVFLNAYTNsPICCPSRAAMWSGLF-THLteSWNNY------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 121 SCVPLDEKLLPQLLKEAGYATHMVGKW------HLGMYRKECLpTRrgfDTYFgyLLGSEDyytheacAPIESLNGTRCA 194
Cdd:cd16171   72 KGLDPNYPTWMDRLEKHGYHTQKYGKLdytsghHSVSNRVEAW-TR---DVPF--LLRQEG-------RPTVNLVGDRST 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 195 LDLRdgeepAKEYNNiystnifTKRATTVIANHPP--EKPLFLYLAFQSVHdplQVPEEYM-EPYGFIQDKhRRIYAGMV 271
Cdd:cd16171  139 VRVM-----LKDWQN-------TDKAVHWIRKEAPnlTQPFALYLGLNLPH---PYPSPSMgENFGSIRNI-RAFYYAMC 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 272 SLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGgqtrsggnNWPLRGR---KGTLWEGGIRGTGFVASPLLKqKGVKSREL 348
Cdd:cd16171  203 AETDAMLGEIISALKDTGLLDKTYVFFTSDHG--------ELAMEHRqfyKMSMYEGSSHVPLLIMGPGIK-AGQQVSDV 273
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 125656171 349 MHITDWLPTLVDLAGGSTngTKPLDGFNMWKTISE 383
Cdd:cd16171  274 VSLVDIYPTMLDIAGVPQ--PQNLSGYSLLPLLSE 306
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
37-303 2.65e-06

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 49.75  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  37 ARASGATQPPHVVFVLADDLGWNDLGFHgsviRTPHLDALAAGGVVLDNYY-VQPLCT-PSRSQLLTGRY-QIHlGLQHY 113
Cdd:COG1524   15 AAAAAAPPAKKVVLILVDGLRADLLERA----HAPNLAALAARGVYARPLTsVFPSTTaPAHTTLLTGLYpGEH-GIVGN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 114 --------LIMTCQPSCVPLD--EKLLP-----QLLKEAGYATHMVGKWHLGMYrkeclptrRGFDTYFGYLLGSEDYYT 178
Cdd:COG1524   90 gwydpelgRVVNSLSWVEDGFgsNSLLPvptifERARAAGLTTAAVFWPSFEGS--------GLIDAARPYPYDGRKPLL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171 179 HEacaPIESLNGTRCALDLRDGEEPAkeynniystniftkrattvianhppekplFLYLAFQSV----HDplqvpeeyme 254
Cdd:COG1524  162 GN---PAADRWIAAAALELLREGRPD-----------------------------LLLVYLPDLdyagHR---------- 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 125656171 255 pYGFIQDKhrriYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNG 303
Cdd:COG1524  200 -YGPDSPE----YRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
427-499 9.60e-03

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 36.52  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125656171  427 NTSIHAgIRYKNWKL--LTGHpgcgyWFPPPSQSNVSEIPPV---DPPtktLwLFDINQDPEERHDV---SREHPHIVQN 498
Cdd:pfam14707  11 GAALHA-VRWGPYKAhfFTPS-----FDPPGAEGCYGSKVPVthhDPP---L-LFDLERDPSEKYPLspdSPEYPEVLAE 80

                  .
gi 125656171  499 L 499
Cdd:pfam14707  81 I 81
 
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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