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Conserved domains on  [gi|544063470|ref|NP_001269557|]
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arylsulfatase L isoform 1 [Homo sapiens]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
62-585 0e+00

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


The actual alignment was detected with superfamily member cd16159:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 521  Bit Score: 755.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQK 221
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 222 LNFLFQVLALVALTLVAGKLthLIPVSWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 301
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLY--LGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 302 QEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 381
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 382 SLENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQD 461
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 462 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDL 541
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 544063470 542 SRDPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 585
Cdd:cd16159  478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
62-585 0e+00

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: 755.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQK 221
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 222 LNFLFQVLALVALTLVAGKLthLIPVSWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 301
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLY--LGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 302 QEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 381
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 382 SLENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQD 461
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 462 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDL 541
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 544063470 542 SRDPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 585
Cdd:cd16159  478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
44-549 9.58e-96

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 298.72  E-value: 9.58e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 123
Cdd:COG3119    5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 124 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesasdhchhplhhgfdhfygmpfslm 203
Cdd:COG3119   85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 204 gdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 283
Cdd:COG3119      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 284 htiteqpmcfqrtTPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGK----------------------- 338
Cdd:COG3119  130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 339 SLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlG-----NTQY-GGwngiykggkgmggweggI 412
Cdd:COG3119  197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEH-GlrggkGTLYeGG-----------------I 258
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 413 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWH 492
Cdd:COG3119  259 RVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRT 336
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 544063470 493 QRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhhDPPLLFDLSRDPSETH 549
Cdd:COG3119  337 GR-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
Sulfatase pfam00884
Sulfatase;
63-448 3.91e-58

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 197.26  E-value: 3.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470   63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtg 142
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  143 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhchhPLHHGFDHFYGmpfslmgdcaRWELSEKRVNLEqkl 222
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG----------RNTGSDLYADPP--- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmRNHTITEQPMCF-QRTTPLIL 301
Cdd:pfam00884 132 -----------------------------------------------------------DVPYNCSGGGVSdEALLDEAL 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  302 QevasfLKRNKHGPFLLFVSFLHVHIPL------------ITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSN 369
Cdd:pfam00884 153 E-----FLDNNDKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544063470  370 STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 448
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
PRK13759 PRK13759
arylsulfatase; Provisional
61-556 1.72e-38

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 148.28  E-value: 1.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  61 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssiGYrvlq 139
Cdd:PRK13759   5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 140 wtgASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchHP--LHHGFDHfygmpfSLMGDcarWELSEKRVN 217
Cdd:PRK13759  77 ---GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 218 LEQKLNFLFQVLALVALTLVaGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcflmRNHTITEQpmcfQRTT 297
Cdd:PRK13759 133 DKSQFDFVSDYLAWLREKAP-GKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPT 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 298 PLILQEVASFLKR-NKHGPFLLFVSFLHVHIPLITMENFL-------------------------GKSLHGLYGD----- 346
Cdd:PRK13759 183 NWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeey 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 347 ----------NVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ-------YGGwngiykggkgmggwe 409
Cdd:PRK13759 263 arraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG--------------- 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 410 gGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-YCER 484
Cdd:PRK13759 324 -SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYS 400
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544063470 485 FLHaarWHQRDRGT-MWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSRDPSETHILTPASE 556
Cdd:PRK13759 401 SDN---YLTDGKWKyIW--FSQTGEEQ---------------------------LFDLKKDPHELHNLSPSEK 441
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
62-585 0e+00

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: 755.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQK 221
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 222 LNFLFQVLALVALTLVAGKLthLIPVSWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 301
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLY--LGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 302 QEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 381
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 382 SLENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQD 461
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 462 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDL 541
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 544063470 542 SRDPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 585
Cdd:cd16159  478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
62-549 3.90e-156

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: 453.94  E-value: 3.90e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRVLQWT 141
Cdd:cd16026    1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasDH-CHHPLHHGFDHFYGMPFSLMGDCARWELSEKRvnleq 220
Cdd:cd16026   76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP----- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 221 klnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivHADCFLMRNHTITEQPMcFQRT-TPL 299
Cdd:cd16026  144 ------------------------------------------------------GPLPPLMENEEVIEQPA-DQSSlTQR 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 300 ILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD- 378
Cdd:cd16026  169 YTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDn 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 379 --------HGGSleNQL-----GNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR 445
Cdd:cd16026  249 gpwleyggHGGS--AGPlrggkGTTWEGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAA 309
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 446 LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGacygrkvcpc 525
Cdd:cd16026  310 LAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG---------- 373
                        490       500
                 ....*....|....*....|....
gi 544063470 526 fGEKVVHHDPPLLFDLSRDPSETH 549
Cdd:cd16026  374 -GLDPTKLEPPLLYDLEEDPGETY 396
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
62-566 6.75e-133

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: 396.42  E-value: 6.75e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsiGYRV-LQW 140
Cdd:cd16160    1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 141 TgaSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDhFYG--MPFSLMGDCARWELSekrvnl 218
Cdd:cd16160   79 D--IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGtnLPFTNSWACDDTGRH------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 219 eqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalIVHAD---CFLMRNHTITEQPMCFQR 295
Cdd:cd16160  150 ------------------------------------------------------VDFPDrsaCFLYYNDTIVEQPIQHEH 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 296 TTPLILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYF 375
Cdd:cd16160  176 LTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFF 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 376 TSDHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTV 443
Cdd:cd16160  256 LSDHGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTF 317
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 444 VRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACYGR 520
Cdd:cd16160  318 VDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGGG 390
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 544063470 521 KVCP------CFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMERV 566
Cdd:cd16160  391 PLSDyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPSVYEHMLEAVEKL 442
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
63-607 3.67e-99

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: 310.53  E-value: 3.67e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqwTG 142
Cdd:cd16158    2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhcHHPLHHGFDHFYGMPFSL-MGDCArwelsekrvnleqk 221
Cdd:cd16158   77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHdQGPCQ-------------- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 222 lnflfqvlalvaltlvagKLTHLIPvswmpviwsalsavlllASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 301
Cdd:cd16158  139 ------------------NLTCFPP-----------------NIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 302 QEVASFL----KRNKhgPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTS 377
Cdd:cd16158  184 KFAKDFIadnaKEGK--PFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 378 DHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVR 445
Cdd:cd16158  262 DNGpstmrksrggnaGLLKCGKGTTYEGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAK 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 446 LAGGEVPqDRVIDGQDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACY 518
Cdd:cd16158  324 LAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCH 396
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 519 GRKvcpcfgeKVVHHDPPLLFDLSRDPSETHILTpaSEPVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNiwrPWLQPC 598
Cdd:cd16158  397 PSA-------ELTSHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPC 464
                        570
                 ....*....|...
gi 544063470 599 ----CGPFPLCWC 607
Cdd:cd16158  465 ckpgCTPKPSCCQ 477
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
44-549 9.58e-96

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 298.72  E-value: 9.58e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 123
Cdd:COG3119    5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 124 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesasdhchhplhhgfdhfygmpfslm 203
Cdd:COG3119   85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 204 gdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 283
Cdd:COG3119      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 284 htiteqpmcfqrtTPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGK----------------------- 338
Cdd:COG3119  130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 339 SLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlG-----NTQY-GGwngiykggkgmggweggI 412
Cdd:COG3119  197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEH-GlrggkGTLYeGG-----------------I 258
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 413 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWH 492
Cdd:COG3119  259 RVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRT 336
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 544063470 493 QRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhhDPPLLFDLSRDPSETH 549
Cdd:COG3119  337 GR-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-552 1.09e-95

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: 297.91  E-value: 1.09e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssigYRVlQ 139
Cdd:cd16142    1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-----TTV-G 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 140 WTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPFSLMGDcarwELSEKRVNle 219
Cdd:cd16142   74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG------RLPTDHGFDEFYGNLYHTIDE----EIVDKAID-- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 220 qklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcFLMRNHtiteqpmcfqrttpl 299
Cdd:cd16142  142 -----------------------------------------------------------FIKRNA--------------- 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 300 ilqevasflKRNKhgPFLLFVSFLHVHIPLITMENFLGKSL-HGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 378
Cdd:cd16142  148 ---------KADK--PFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTD 216
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 379 HG-----------GSLENQLGNTQYGGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLA 447
Cdd:cd16142  217 NGpeqdvwpdggyTPFRGEKGTTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALA 279
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 448 GGEVP------QDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVtpVFQPEGAGACYGRK 521
Cdd:cd16142  280 GAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFY 351
                        490       500       510
                 ....*....|....*....|....*....|.
gi 544063470 522 VCPCfgekvvhhdpPLLFDLSRDPSETHILT 552
Cdd:cd16142  352 VLTF----------PLIFNLRRDPKERYDVT 372
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
62-552 3.30e-90

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: 284.36  E-value: 3.30e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRvlqw 140
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 141 tgASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSlmGDCarwELSEKRVNLeq 220
Cdd:cd16161   77 --SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFS--HDS---SLADRYAQF-- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 221 klnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhADCFLMRNhtiteqpmcfqrttpli 300
Cdd:cd16161  142 -------------------------------------------------------ATDFIQRA----------------- 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 301 lqevasflkRNKHGPFLLFVSFLHVHIPLITMENFLGKSLH-GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 379
Cdd:cd16161  150 ---------SAKDRPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDN 220
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 380 G-----GSLENQLGNTQY---GGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEV 451
Cdd:cd16161  221 GpwevkCELAVGPGTGDWqgnLGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASL 295
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 452 PQDRVIDGQDLLPLLLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtmWKVHFVTpvfqpEGAGACygrkvCPCF 526
Cdd:cd16161  296 PPGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALAC-----CGST 358
                        490       500
                 ....*....|....*....|....*.
gi 544063470 527 GEKvVHHDPPLLFDLSRDPSETHILT 552
Cdd:cd16161  359 GPK-LYHDPPLLFDLEVDPAESFPLT 383
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-549 1.32e-89

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: 283.67  E-value: 1.32e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 142
Cdd:cd16144    1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 A-------SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDH------------FYGMPFSLM 203
Cdd:cd16144   81 TklipppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVniggtgnggppsYYFPPGKPN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 204 GDCARWELSEKRVNleqklnflfqvlalvALTlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 283
Cdd:cd16144  155 PDLEDGPEGEYLTD---------------RLT------------------------------------------------ 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 284 htiteqpmcfqrttplilQEVASFLKRNKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYGDN-------VEEMD 352
Cdd:cd16144  172 ------------------DEAIDFIEQNKDKPFFLYLSHYAVHTPIQarpeLIEKYEKKKKGLRKGQKnpvyaamIESLD 233
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 353 WMVGRILDTLDVEGLSNSTLIYFTSDHGG-SLENQLGNTQY-----------GGwngiykggkgmggweggIRVPGIFRW 420
Cdd:cd16144  234 ESVGRILDALEELGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRW 296
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 421 PGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYcerFLHAARWHQRDRGTM- 499
Cdd:cd16144  297 PGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWH---FPHYHGQGGRPASAIr 373
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 544063470 500 ---WK-VHFvtpvfqpegagacygrkvcpcfgekvvHHDPPL-LFDLSRDPSETH 549
Cdd:cd16144  374 kgdWKlIEF---------------------------YEDGRVeLYNLKNDIGETN 401
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-549 1.83e-88

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: 279.86  E-value: 1.83e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssiGYRVLQWT 141
Cdd:cd16143    1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRL----KGGVLGGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 GASGgLPTNETTFAKILKEKGYATGLIGKWHLGLN------CESASDHCHH----------PLHHGFDHFYGMPFSlmgd 205
Cdd:cd16143   77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwkkkdgKKAATGTGKDvdyskpikggPLDHGFDYYFGIPAS---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 206 carwelsekrvnleqklnflfQVLalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnht 285
Cdd:cd16143  152 ---------------------EVL-------------------------------------------------------- 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 286 iteqpmcfqrttPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLD 363
Cdd:cd16143  155 ------------PTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 364 VEGLSNSTLIYFTSDHGGSLENQLGNTQ-----------------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLP 425
Cdd:cd16143  223 ELGLAENTLVIFTSDNGPSPYADYKELEkfghdpsgplrgmkadiYeGG-----------------HRVPFIVRWPGKIP 285
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 426 AGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTMWKVhfv 505
Cdd:cd16143  286 AGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL--- 356
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 544063470 506 tpVFQPEGAGACYGRKvcpcfgeKVVHHDPP-LLFDLSRDPSETH 549
Cdd:cd16143  357 --IDGTGSGGFSYPRG-------KEKLGLPPgQLYNLSTDPGESN 392
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
62-585 2.33e-86

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: 277.04  E-value: 2.33e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16157    1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 GAS--GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPfslmgDCARWELSEKRvnle 219
Cdd:cd16157   81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGPYDNKA---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 220 qklnflfqvlalvaltlvagklTHLIPV--SWmpviwsalsavlLLASSYFVGALIvhadcflmrNHTITEQPMcfqrtT 297
Cdd:cd16157  146 ----------------------YPNIPVyrDW------------EMIGRYYEEFKI---------DKKTGESNL-----T 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 298 PLILQEVASFLKR--NKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYF 375
Cdd:cd16157  178 QIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFF 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 376 TSDHGGSLenqLGNTQYGGWNgIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDR 455
Cdd:cd16157  258 SSDNGAAL---ISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDR 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 456 VIDGQDLLPLLLgtAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVT----PVFQPEGAGACYGRKVCPCFGEKVV 531
Cdd:cd16157  334 AIDGIDLLPVLL--NGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQT 405
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 544063470 532 HH-DPPLLFDLSRDPSETHILTPASePVFYQVMERVQQAVWEHQRTLSPVPLQLD 585
Cdd:cd16157  406 DHtKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-549 3.45e-75

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: 245.97  E-value: 3.45e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyRVLQWTG 142
Cdd:cd16145    1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasDHCHHPLHHGFDHFYGmpfslmgdcarwelsekrvnleqkl 222
Cdd:cd16145   75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGP-----GTPGHPTKQGFDYFYG------------------------- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 223 nFLFQVLAlvaltlvagkltHlipvswmpviwsalsavlllasSYFVGALIVHADCFLMRNHTIT-------EQPMCFQR 295
Cdd:cd16145  125 -YLDQVHA------------H----------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTY 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 296 TTPLILQEVASFLKRNKHGPFLLFVSFLHVHIPLIT-------MENFLGKSLHGLYGDNVEE--------MDWMVGRILD 360
Cdd:cd16145  170 SHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVpddgpykYKPKDPGIYAYLPWPQPEKayaamvtrLDRDVGRILA 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 361 TLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQY--------------------GGwngiykggkgmggweggIRVPGIFRW 420
Cdd:cd16145  250 LLKELGIDENTLVVFTSDNGPHSE---GGSEHdpdffdsngplrgykrslyeGG-----------------IRVPFIARW 309
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 421 PGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdr 496
Cdd:cd16145  310 PGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG--- 382
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 544063470 497 gtmWKVhfvtpVFQPEGAGacygrkvcpcfgekvvhhdPPLLFDLSRDPSETH 549
Cdd:cd16145  383 ---WKA-----VRHGKKDG-------------------PFELYDLSTDPGETN 408
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
63-461 1.36e-74

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: 238.11  E-value: 1.36e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssigyrVLQWTG 142
Cdd:cd16022    1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqkl 222
Cdd:cd16022   73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplilQ 302
Cdd:cd16022  103 -------------------------------------------------------------------------------D 103
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 303 EVASFLKRNKHG-PFLLFVSFLHVHIPLItmenflgkslhglYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 381
Cdd:cd16022  104 EAIDFIERRDKDkPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 382 SLENqlGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQD 461
Cdd:cd16022  171 MLGD--HGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
63-572 6.51e-72

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: 237.06  E-value: 6.51e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSIGYRVLqwt 141
Cdd:cd16146    1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSLMGDCARWELSEkrvnleqk 221
Cdd:cd16146   76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND-------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 222 lnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassYFvgalivhaDCFLMRNHTiteqpmcFQRT----T 297
Cdd:cd16146  137 ---------------------------------------------YF--------DDTYYHNGK-------FVKTegycT 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 298 PLILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMEN----FLGKSLH----GLYGdNVEEMDWMVGRILDTLDVEGLSN 369
Cdd:cd16146  157 DVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKyldpYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEE 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 370 STLIYFTSDHGGSLENQLGN---------TQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDV 439
Cdd:cd16146  236 NTIVIFMSDNGPAGGVPKRFnagmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDL 298
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 440 FPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTMWKVHFVtpVFQPEgagacYg 519
Cdd:cd16146  299 LPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W- 361
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 544063470 520 RKVCPcfgekvvHHDPPLLFDLSRDPSETHILTpASEPVFYQVMERVQQAVWE 572
Cdd:cd16146  362 RLVSP-------KGFQPELYDIENDPGEENDVA-DEHPEVVKRLKAAYEAWWD 406
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-491 3.99e-66

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: 220.93  E-value: 3.99e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqwtg 142
Cdd:cd16151    1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 aSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESASDhchHPLHHGFDHFygmpfslmgdCArWELSEKRVNLEQKL 222
Cdd:cd16151   68 -FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEY----------CL-WQLTETGEKYSRPA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 223 NFLFQVLalvaltlvAGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcFLMRnhtiteqpmcfqrttplilq 302
Cdd:cd16151  132 TPTFNIR--------NGKLLETTEGDYGPDLFAD----------------------FLID-------------------- 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 303 evasFLKRNKHGPFLLFVSFLHVHIPL----------ITMENFLGKSLHglYGDNVEEMDWMVGRILDTLDVEGLSNSTL 372
Cdd:cd16151  162 ----FIERNKDQPFFAYYPMVLVHDPFvptpdspdwdPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 373 IYFTSDHG--GSLENQLGNTQY-GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGG 449
Cdd:cd16151  236 IIFTGDNGthRPITSRTNGREVrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGA 306
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 544063470 450 EVPQDRVIDGQDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 491
Cdd:cd16151  307 PLPEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
62-551 6.78e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 212.81  E-value: 6.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVsSIGYRvlqwt 141
Cdd:cd16034    1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHH----PLHHGFDHFYGMpfslmgdcarwelsekrvn 217
Cdd:cd16034   75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------------------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 218 leqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhaDCFLMRNHTI----TEQPMCF 293
Cdd:cd16034  131 -----------------------------------------------------------ECNHDHNNPHyyddDGKRIYI 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 294 QRTTPLILQEVA-SFLKRNKHG--PFLLFVSF------------------------LHVHIPLITMENF-LGKSLHGLYG 345
Cdd:cd16034  152 KGYSPDAETDLAiEYLENQADKdkPFALVLSWnpphdpyttapeeyldmydpkkllLRPNVPEDKKEEAgLREDLRGYYA 231
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 346 dNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQYGGwngiykggkgmggwegGIRVPGIFRWPG 422
Cdd:cd16034  232 -MITALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYPG 294
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 423 VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTM--- 499
Cdd:cd16034  295 KIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtd 372
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 544063470 500 -WKvhFVtpvfqpegagacygrkvcpcfgekVVHHDPPLLFDLSRDPSETHIL 551
Cdd:cd16034  373 rYT--YV------------------------RDKNGPWLLFDNEKDPYQLNNL 399
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
63-549 9.37e-63

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: 212.41  E-value: 9.37e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssiGYRVLqWTG 142
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVI-LAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasdHCHH---PLHHGFDHFYGMpFSLMGDcarwelsekrvnle 219
Cdd:cd16029   75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY-YGGAED-------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 220 qklnflfqvlalvaltlvagkltHLIPVSWMPVIWSalsavlllassyfvgalivhaDCFLMRNHTIT-EQPMCFqrTTP 298
Cdd:cd16029  132 -----------------------YYTHTSGGANDYG---------------------NDDLRDNEEPAwDYNGTY--STD 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 299 LILQEVASFLKR-NKHGPFLLFVSFLHVHIPL------ITMENFLGKSLHG----LYGDNVEEMDWMVGRILDTLDVEGL 367
Cdd:cd16029  166 LFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLqvppeyADPYEDKFAHIKDedrrTYAAMVSALDESVGNVVDALKAKGM 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 368 SNSTLIYFTSDHGGSLENQLG----------NTQY-GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIGEPT 434
Cdd:cd16029  246 LDNTLIVFTSDNGGPTGGGDGgsnyplrggkNTLWeGG-----------------VRVPA-FVWSPLLPpkRGTVSDGLM 307
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 435 SLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRgtmwkvhfvtPVFQPEGA 514
Cdd:cd16029  308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDD----------ITRTTGGA 364
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 544063470 515 GACYGRKvcpcfgeKVVHHDPplLFDLSRDPSETH 549
Cdd:cd16029  365 AIRVGDW-------KLIVGKP--LFNIENDPCERN 390
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
63-575 1.22e-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: 200.81  E-value: 1.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssIGYRVLQWTg 142
Cdd:cd16027    1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 asggLPTNETTFAKILKEKGYATGLIGKWHlgLNCESASDHCHHPLHHGFDHFYGMPFslMGDCARWelsEKRVNLEQkl 222
Cdd:cd16027   76 ----LPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWDY--ASNAADF---LNRAKKGQ-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 223 NFLFQvlalvaltlVAGKLTHlipVSWMPVIWSAL----SAVLLlaSSYFVgalivhaDcflmrnhtiteqpmcfqrtTP 298
Cdd:cd16027  143 PFFLW---------FGFHDPH---RPYPPGDGEEPgydpEKVKV--PPYLP-------D-------------------TP 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 299 LILQEVASFLkrnkhgpfllfvsflhvhiplitmenflgkslhglygDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 378
Cdd:cd16027  183 EVREDLADYY-------------------------------------DEIERLDQQVGEILDELEEDGLLDNTIVIFTSD 225
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 379 HGGSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvID 458
Cdd:cd16027  226 HGMPFPRAKGTLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQ 286
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 459 GQDLLPLLLG-TAQHSDHEFLMH-------YCERFLHAARWHqrdrgtmwkvhfvtpvfqpegagacYgrkvcpcfgekV 530
Cdd:cd16027  287 GRSFLPLLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK-------------------------Y-----------I 330
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 544063470 531 VHHDPPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 575
Cdd:cd16027  331 RNYMPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
Sulfatase pfam00884
Sulfatase;
63-448 3.91e-58

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 197.26  E-value: 3.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470   63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtg 142
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  143 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhchhPLHHGFDHFYGmpfslmgdcaRWELSEKRVNLEqkl 222
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG----------RNTGSDLYADPP--- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmRNHTITEQPMCF-QRTTPLIL 301
Cdd:pfam00884 132 -----------------------------------------------------------DVPYNCSGGGVSdEALLDEAL 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  302 QevasfLKRNKHGPFLLFVSFLHVHIPL------------ITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSN 369
Cdd:pfam00884 153 E-----FLDNNDKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544063470  370 STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 448
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
473-607 4.91e-58

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 190.60  E-value: 4.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  473 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 552
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 544063470  553 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 607
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
61-568 8.52e-56

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: 194.67  E-value: 8.52e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  61 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqw 140
Cdd:cd16031    1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 141 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDhchhplhhGFDHFYGMP---------FSLMGDCARWEL 211
Cdd:cd16031   71 DNNGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFPgqgsyydpeFIENGKRVGQKG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 212 SEKRVNLEQKLNFL--------FqvlalvALTlVAGKLTHLipvSWMPViwsalsavlllassyfvgalIVHADcfLMRN 283
Cdd:cd16031  143 YVTDIITDKALDFLkerdkdkpF------CLS-LSFKAPHR---PFTPA--------------------PRHRG--LYED 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 284 HTITE-----------QPMCFQRTTPLI-LQEVASFLKRNKHGpfllfvsflhvhiplITMENFLGkSLHGlygdnveeM 351
Cdd:cd16031  191 VTIPEpetfddddyagRPEWAREQRNRIrGVLDGRFDTPEKYQ---------------RYMKDYLR-TVTG--------V 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 352 DWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGG-WNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVI 430
Cdd:cd16031  247 DDNVGRILDYLEEQGLADNTIIIYTSDNG----FFLGEHGLFDkRL----------MYEESIRVPLIIRDPRLIKAGTVV 312
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 431 GEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHS-DHEFLMHYCE--RFLHAARWH--QRDRgtmWK-VHF 504
Cdd:cd16031  313 DALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNVPTHEgvRTER---YKyIYY 387
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544063470 505 vtpvfqpegagacygrkvcpcfgekvvHHDPPL--LFDLSRDPSETH--ILTPASEPVFYQVMERVQQ 568
Cdd:cd16031  388 ---------------------------YGVWDEeeLYDLKKDPLELNnlANDPEYAEVLKELRKRLEE 428
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
62-549 7.19e-54

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: 188.81  E-value: 7.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEDGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSIGYRVLQW 140
Cdd:cd16025    2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 141 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLN----CESASDH-----------------------CHHPLH---- 189
Cdd:cd16025   78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPDdyysTDDLTDKaieyideqkapdkpfflylafgaPHAPLQapke 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 190 -----HG-FDhfygmpfslMGdcarWE-LSEKRvnLE-QKlnflfqvlalvALTLVAG--KLTHLIPvsWMPViWSALSA 259
Cdd:cd16025  158 widkyKGkYD---------AG----WDaLREER--LErQK-----------ELGLIPAdtKLTPRPP--GVPA-WDSLSP 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 260 vlllassyfvgalivhadcflmrnhtitEQPMCFQRttpliLQEV-ASFlkrnkhgpfllfvsflhvhiplitmenflgk 338
Cdd:cd16025  209 ----------------------------EEKKLEAR-----RMEVyAAM------------------------------- 224
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 339 slhglygdnVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN---QLGNTQY---------GGwngiykggkgmg 406
Cdd:cd16025  225 ---------VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPgwaNASNTPFrlykqasheGG------------ 283
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 407 gweggIRVPGIFRWP-GVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV------IDGQDLLPLLLGTAQHSDHEFLm 479
Cdd:cd16025  284 -----IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ- 357
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544063470 480 hYCERFLHAARWHQRdrgtmWKVhfvtpvfqpegagacygrkvcpcfgekVVHHDPPL------LFDLSRDPSETH 549
Cdd:cd16025  358 -YFELFGNRAIRKGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-545 3.47e-49

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: 173.88  E-value: 3.47e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRsgmvssIGYrvlqWTG 142
Cdd:cd16037    1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WDN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASGgLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhchhplHHGFDHfygmpfslmgdcarwelsekrvnleqkl 222
Cdd:cd16037   71 ADP-YDGDVPSWGHALRAAGYETVLIGKLHFRGEDQ----------RHGFRY---------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhaDcflmRNhtiteqpmcfqrttplILQ 302
Cdd:cd16037  112 ------------------------------------------------------D----RD----------------VTE 117
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 303 EVASFLKRNKH--GPFLLFVSFLHVHIPLITMENFLGKSLHGL---YGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTS 377
Cdd:cd16037  118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 378 DHGgsleNQLG-------NTQYggwngiykggkgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGE 450
Cdd:cd16037  198 DHG----DMLGerglwgkSTMY----------------EESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAP 256
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 451 VPQDRviDGQDLLPLLLGTAQHSDHEFlmhyCErfLHAARwhQRDRGTM-----WK-VHFVtpvfqpegagacygrkvcp 524
Cdd:cd16037  257 PPPDL--DGRSLLPLAEGPDDPDRVVF----SE--YHAHG--SPSGAFMlrkgrWKyIYYV------------------- 307
                        490       500
                 ....*....|....*....|.
gi 544063470 525 cfgekvvhHDPPLLFDLSRDP 545
Cdd:cd16037  308 --------GYPPQLFDLENDP 320
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-572 2.72e-46

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: 168.55  E-value: 2.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqWTG 142
Cdd:cd16033    1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 A-SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHC--HHPLHHGFDHFYgmpfslmGDCARWELSEkrvnLE 219
Cdd:cd16033   76 AySRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEETPLDYGFdeYLPVETTIEYFL-------ADRAIEMLEE----LA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 220 QKlnflfqvlalvaltlvaGKlthliPvsWMpvIWSAlsavlllassyFVGAlivHADCFLmrnhtitEQPMcFQRTTPL 299
Cdd:cd16033  145 AD-----------------DK-----P--FF--LRVN-----------FWGP---HDPYIP-------PEPY-LDMYDPE 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 300 ILQEVASF---------LKRNKHGPFLLFVSFLHVHIPLITmeNFLGkslhglygdNVEEMDWMVGRILDTLDVEGLSNS 370
Cdd:cd16033  177 DIPLPESFaddfedkpyIYRRERKRWGVDTEDEEDWKEIIA--HYWG---------YITLIDDAIGRILDALEELGLADD 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 371 TLIYFTSDHGGSLENQlgntqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGE 450
Cdd:cd16033  246 TLVIFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVD 313
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 451 VPQDrvIDGQDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWHQrdrgtmwkvhfvtpVFQPEGagacygr 520
Cdd:cd16033  314 VPPK--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYKY--------------VFNGFD------- 368
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 544063470 521 kvcpcFGEkvvhhdpplLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWE 572
Cdd:cd16033  369 -----IDE---------LYDLESDPYELNNL--IDDPEYEEILREMRTRLYE 404
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
63-545 3.49e-43

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: 157.74  E-value: 3.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 142
Cdd:cd16032    1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASGgLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhCHHPLHHGFDHfygmpfslmgDcarwelsekrvnlEQkl 222
Cdd:cd16032   71 AAE-FPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFDY----------D-------------EE-- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 223 nflfqvlalvaltlvagklthlipvswmpVIWSALSAVLLLAssyfvgalivhadcflmRNHTiteqpmcfqrttplilq 302
Cdd:cd16032  115 -----------------------------VAFKAVQKLYDLA-----------------RGED----------------- 131
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 303 evasflKRnkhgPFLLFVSFLHVHIPLITMENFLG----KSLHGLYGdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 378
Cdd:cd16032  132 ------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 379 HGgsleNQLGntQYGGWngiykggKGMGGWEGGIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV-I 457
Cdd:cd16032  201 HG----DMLG--ERGLW-------YKMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpL 266
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 458 DGQDLLPLLLGTAQHSDHEFLMHYCErflhaarwhqrdrgtmwkvhfvtpvfqpEGAGAcygrkvcPCF-----GEKVVH 532
Cdd:cd16032  267 DGRSLLPLLEGGDSGGEDEVISEYLA----------------------------EGAVA-------PCVmirrgRWKFIY 311
                        490
                 ....*....|....*
gi 544063470 533 --HDPPLLFDLSRDP 545
Cdd:cd16032  312 cpGDPDQLFDLEADP 326
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-464 1.46e-42

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: 153.93  E-value: 1.46e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 142
Cdd:cd16149    1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqkl 222
Cdd:cd16149   81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgaliVHADCFLMRNHtiteqpmcfqrttplilq 302
Cdd:cd16149  113 ---------------------------------------------------DDAADFLRRRA------------------ 123
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 303 evasflKRNKhgPFLLFVSFLHVHIPlitmenflgkslHGlYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGS 382
Cdd:cd16149  124 ------EAEK--PFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFN 182
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 383 LenqlgnTQYGGW---------NgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQ 453
Cdd:cd16149  183 M------GHHGIWgkgngtfplN----------MYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPA 246
                        410
                 ....*....|.
gi 544063470 454 DRVIDGQDLLP 464
Cdd:cd16149  247 DPRLPGRSFAD 257
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-464 1.95e-42

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: 153.86  E-value: 1.95e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyrvLQWT 141
Cdd:cd16148    1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 GASGGLPTNETTFAKILKEKGYATGLIgkwhlglncesaSDHCHHPLHHGFDH--FYGMPFSLMGDCARWELSEkrvnle 219
Cdd:cd16148   67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDRgfDTFEDFRGQEGDPGEEGDE------ 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 220 qklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrTTPL 299
Cdd:cd16148  129 ----------------------------------------------------------------------------RAER 132
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 300 ILQEVASFLKRNKHG-PFLLFVSFLHVHIPLitmenflgkslhgLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 378
Cdd:cd16148  133 VTDRALEWLDRNADDdPFFLFLHYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 379 HGGSLeNQLGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVRLAGGEVPQDrvID 458
Cdd:cd16148  200 HGEEF-GEHGLYWGHGSN----------LYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SD 265

                 ....*.
gi 544063470 459 GQDLLP 464
Cdd:cd16148  266 GRSLLP 271
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
63-575 5.40e-40

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: 152.03  E-value: 5.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqWTG 142
Cdd:cd16028    1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASggLPTNETTFAKILKEKGYATGLIGKWHL-----GLNCESASDHCHHPLHHGFDHFYGMPFslmgdcARWELSEKRVN 217
Cdd:cd16028   72 TP--LDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFDPVDRLDE------YPAEDSDTAFL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 218 LEQKLNFL--------FQVLA-------LVAltlvagklthliPVSWMPVI-WSALSAVLllassyfvgalivhadcflm 281
Cdd:cd16028  144 TDRAIEYLderqdepwFLHLSyirphppFVA------------PAPYHALYdPADVPPPI-------------------- 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 282 RNHTITEQpmcfQRTTPLIlqevASFLKRNKHGpfllfvSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDT 361
Cdd:cd16028  192 RAESLAAE----AAQHPLL----AAFLERIESL------SFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDY 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 362 LDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGGwngiykggkGMGGWEGGIRVPGIFRWPGVL---PAGRVIGEPTSLMD 438
Cdd:cd16028  258 LKETGQWDDTLIVFTSDHG----EQLGDHWLWG---------KDGFFDQAYRVPLIVRDPRREadaTRGQVVDAFTESVD 324
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 439 VFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQRDRGTmwkvhfvtpvfQP 511
Cdd:cd16028  325 VMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALGL-----------SP 384
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544063470 512 EGAGACYGRkvcpcfGE--KVVHHD--PPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 575
Cdd:cd16028  385 DECSLAVIR------DErwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSWRM 444
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
61-475 1.09e-39

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: 150.80  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  61 SRPNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqW 140
Cdd:cd16030    1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----F 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 141 TGASGglptNETTFAKILKEKGYATGLIGKWHlglncesasdhchhplHHGFDHFYGMPFSlmgdcarWELSEKRVNLEQ 220
Cdd:cd16030   76 RKVAP----DAVTLPQYFKENGYTTAGVGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 221 KLNFLFQVLALVALTLVAGKLTHLIPV--SWMPVIWSALSAVLLLAS------SYFVGA--------LIVHADCFLMRNH 284
Cdd:cd16030  129 YPPGKLCPGKKGGKGGGGGPAWEAADVpdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 285 TITEQPMCFQRT-TPLI----LQEVasflkRNKHGPFLLFVSFLHVHIPlitmENFLGKSLHGLYGdNVEEMDWMVGRIL 359
Cdd:cd16030  209 ESIPLPNPFDPIdLPEVawndLDDL-----PKYGDIPALNPGDPKGPLP----DEQARELRQAYYA-SVSYVDAQVGRVL 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 360 DTLDVEGLSNSTLIYFTSDHGGslenQLGntQYGGW---------NgiykggkgmggweggiRVPGIFRWPGVLPAGRVI 430
Cdd:cd16030  279 DALEELGLADNTIVVLWSDHGW----HLG--EHGHWgkhtlfeeaT----------------RVPLIIRAPGVTKPGKVT 336
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 544063470 431 GEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLLLGTAQHSDH 475
Cdd:cd16030  337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKD 379
PRK13759 PRK13759
arylsulfatase; Provisional
61-556 1.72e-38

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 148.28  E-value: 1.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  61 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssiGYrvlq 139
Cdd:PRK13759   5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 140 wtgASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchHP--LHHGFDHfygmpfSLMGDcarWELSEKRVN 217
Cdd:PRK13759  77 ---GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 218 LEQKLNFLFQVLALVALTLVaGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcflmRNHTITEQpmcfQRTT 297
Cdd:PRK13759 133 DKSQFDFVSDYLAWLREKAP-GKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPT 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 298 PLILQEVASFLKR-NKHGPFLLFVSFLHVHIPLITMENFL-------------------------GKSLHGLYGD----- 346
Cdd:PRK13759 183 NWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeey 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 347 ----------NVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ-------YGGwngiykggkgmggwe 409
Cdd:PRK13759 263 arraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG--------------- 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 410 gGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-YCER 484
Cdd:PRK13759 324 -SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYS 400
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544063470 485 FLHaarWHQRDRGT-MWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSRDPSETHILTPASE 556
Cdd:PRK13759 401 SDN---YLTDGKWKyIW--FSQTGEEQ---------------------------LFDLKKDPHELHNLSPSEK 441
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
62-568 1.92e-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: 142.75  E-value: 1.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRvlqwt 141
Cdd:cd16152    1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 gASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqk 221
Cdd:cd16152   71 -NGIPLPADEKTLAHYFRDAGYETGYVGKWHL------------------------------------------------ 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 222 lnflfqvlalvaltlvAGklthlipvswmpviwsalsavlllassYFVGALIVHADCFLMrnhtiteqpmcfqrttplil 301
Cdd:cd16152  102 ----------------AG---------------------------YRVDALTDFAIDYLD-------------------- 118
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 302 qevasflKRNKHGPFLLFVSFLHVHiplitMEN------------------FLGKSLHGLYGDN----------VEEMDW 353
Cdd:cd16152  119 -------NRQKDKPFFLFLSYLEPH-----HQNdrdryvapegsaerfanfWVPPDLAALPGDWaeelpdylgcCERLDE 186
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 354 MVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlgNTQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEP 433
Cdd:cd16152  187 NVGRIRDALKELGLYDNTIIVFTSDHGCHFRTR--NAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEEL 252
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 434 TSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCE----RFLHAARW----HQRDRGtmWKVHFV 505
Cdd:cd16152  253 VSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISEsqvgRAIRTDRWkysvAAPDKD--GWKDSG 328
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544063470 506 TPVFQPEgagacygrkvcpcfgekvvhhdppLLFDLSRDPSETHILtpASEPVFYQVMERVQQ 568
Cdd:cd16152  329 SDVYVED------------------------YLYDLEADPYELVNL--IGRPEYREVAAELRE 365
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
61-565 1.47e-34

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: 134.61  E-value: 1.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  61 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssigy 135
Cdd:cd16155    1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 136 rvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLnCESASDHCHHP--------LHHGFDH---FYGMPFSLMg 204
Cdd:cd16155   74 ------GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF-ADAAIEFLEEYkdgdkpffMYVAFTAphdPRQAPPEYL- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 205 dcarwelseKRVNLEqklnflfqvlalvaltlvagklTHLIPVSWMPViwsalsavlllassY-FVGALIVHADcflmrn 283
Cdd:cd16155  146 ---------DMYPPE----------------------TIPLPENFLPQ--------------HpFDNGEGTVRD------ 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 284 htitEQPMCFQRTTplilQEVASFLKRNkhgpfllfvsflhvhiplitmenflgkslhglYGdNVEEMDWMVGRILDTLD 363
Cdd:cd16155  175 ----EQLAPFPRTP----EAVRQHLAEY--------------------------------YA-MITHLDAQIGRILDALE 213
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 364 VEGLSNSTLIYFTSDHG------GSLENQlgNTQYGGWngiykggkgmggweggiRVPGIFRWPGVlPAGRVIGEPTSLM 437
Cdd:cd16155  214 ASGELDNTIIVFTSDHGlavgshGLMGKQ--NLYEHSM-----------------RVPLIISGPGI-PKGKRRDALVYLQ 273
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 438 DVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMhycerFLHAARWHQRDRgtmWKVHFVTPvfqpegaga 516
Cdd:cd16155  274 DVFPTLCELAGIEIPES--VEGKSLLPVIRGeKKAVRDTLYGA-----YRDGQRAIRDDR---WKLIIYVP--------- 334
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 544063470 517 cygrkvcpcfGEKVVhhdppLLFDLSRDPSETHILtpASEPVFYQVMER 565
Cdd:cd16155  335 ----------GVKRT-----QLFDLKKDPDELNNL--ADEPEYQERLKK 366
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
63-447 8.19e-31

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: 120.60  E-value: 8.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQwT 141
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPEL-P 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnLEQK 221
Cdd:cd00016   80 SRAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------------------LLKA 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 222 LNFLfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplil 301
Cdd:cd00016  112 IDET---------------------------------------------------------------------------- 115
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 302 qevasflkrNKHGPFLLFVSFLHVHIPLitmenFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 381
Cdd:cd00016  116 ---------SKEKPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544063470 382 SLENqLGNTqyggwngiYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLA 447
Cdd:cd00016  182 IDKG-HGGD--------PKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-549 1.30e-30

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 124.65  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssiGYRVLQWT 141
Cdd:cd16150    1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 142 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHChhplhhgfdhfygmpfslmgdcarwelSEKRVNLEQK 221
Cdd:cd16150   74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC---------------------------DSDEACVRTA 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 222 LNFLFQvlalvaltlvagkltHLIPVSWmpviwsalsaVLLLASSY----FVgaliVHADCFLMrnhtITEQPMCFQRTT 297
Cdd:cd16150  122 IDWLRN---------------RRPDKPF----------CLYLPLIFphppYG----VEEPWFSM----IDREKLPPRRPP 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 298 PLILQEVASFLK-RNKHGpfllFVSflhvhiplITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFT 376
Cdd:cd16150  169 GLRAKGKPSMLEgIEKQG----LDR--------WSEERW--RELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFF 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 377 SDHG-------------GSLENQLgntqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTV 443
Cdd:cd16150  235 SDHGdytgdyglvekwpNTFEDCL------------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPPTL 289
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 444 VRLAGgeVPQDRVIDGQDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHqrdrgtMWKVHFVTPVFQPEG----AGAC 517
Cdd:cd16150  290 LDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQA------MEGGHGPYDLKWPRLlqqeEPPE 357
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 544063470 518 YGRKVcpcfgeKVVHHD---------PPLLFDLSRDPSETH 549
Cdd:cd16150  358 HTKAV------MIRTRRykyvyrlyePDELYDLEADPLELH 392
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
63-466 7.33e-29

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: 120.18  E-value: 7.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 142
Cdd:cd16156    1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 aSGGLPTNETTFAKILKEKGYATGLIGKWHL------GLN-CESASDHchhplhhgfDHFYGMPFSLMgdcarwELSEKR 215
Cdd:cd16156   71 -CMALGDNVKTIGQRLSDNGIHTAYIGKWHLdggdyfGNGiCPQGWDP---------DYWYDMRNYLD------ELTEEE 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 216 VnleqklnflfqvlalvaltlvagklthlipvswmpVIWSalsavLLLASSYfvgalivhadcflmrNHTITEQPMCFQR 295
Cdd:cd16156  135 R-----------------------------------RKSR-----RGLTSLE---------------AEGIKEEFTYGHR 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 296 TTPLILQevasFLKRNKHGPFLLFVSFLHVHIPLI------TM-------------ENFLGKSLH------GLYGDNVEE 350
Cdd:cd16156  160 CTNRALD----FIEKHKDEDFFLVVSYDEPHHPFLcpkpyaSMykdfefpkgenayDDLENKPLHqrlwagAKPHEDGDK 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 351 M--------------DWMVGRILDTLDvEGLSNSTLIYfTSDHGGSLENQL----GNTQYggwngiykggkgmggwEGGI 412
Cdd:cd16156  236 GtikhplyfgcnsfvDYEIGRVLDAAD-EIAEDAWVIY-TSDHGDMLGAHKlwakGPAVY----------------DEIT 297
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 544063470 413 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLL 466
Cdd:cd16156  298 NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
62-460 9.34e-29

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: 118.42  E-value: 9.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSIGYRV 137
Cdd:cd16147    1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 138 LQWTGAsgglptNETTFAKILKEKGYATGLIGKWhlgLN-CESASDHCHHPLhhGFDHFYGMPFslmgdcarwelsekrv 216
Cdd:cd16147   77 FWQNGL------ERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVG---------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 217 nleqklNFLFQVLALVALTLVAGklthliPVSWmpviwsalsavlllASSYFvgalivhadcflmrnhtiteqpmcfqrt 296
Cdd:cd16147  130 ------NSTYYNYTLSNGGNGKH------GVSY--------------PGDYL---------------------------- 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 297 TPLILQEVASFLKR--NKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYG---------------------DNVE 349
Cdd:cd16147  156 TDVIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTpaprYANLFPNVTAPPRPPpnnpdvsdkphwlrrlpplnpTQIA 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 350 EMDW--------------MVGRILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQ-YggwngiykggkgmggwEGG 411
Cdd:cd16147  236 YIDElyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHRLPPGKRTpY----------------EED 299
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 544063470 412 IRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQ 460
Cdd:cd16147  300 IRVPLLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
62-462 5.66e-28

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: 113.62  E-value: 5.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  62 RPNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVS 131
Cdd:cd16153    1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 132 SIGYrvlqWTGASGGLPtnetTFAKILKEKGYATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwel 211
Cdd:cd16153   81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH--------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 212 sekrvnLEQKLNFLFQvlALVALTLVAGKlthlipVSWMPviwsalsavlllassyfvgalivhadcflmrnhtiteqpm 291
Cdd:cd16153  114 ------LEAFQRYLKN--ANQSYKSFWGK------IAKGA---------------------------------------- 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 292 cfqrttplilqevasflKRNKhgPFLLFVSFLHVHIPLITMENFLGK-SLHGL--YGDNveemdwMVGRILDTLDVEGLS 368
Cdd:cd16153  140 -----------------DSDK--PFFVRLSFLQPHTPVLPPKEFRDRfDYYAFcaYGDA------QVGRAVEAFKAYSLK 194
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 369 N---STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmggweGGIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTV 443
Cdd:cd16153  195 QdrdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTL 261
                        410
                 ....*....|....*....
gi 544063470 444 VRLAGGEVPQDRVIDGQDL 462
Cdd:cd16153  262 LAAAGVDVDAPDYLDGRDL 280
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-481 5.73e-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: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 108.45  E-value: 5.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYR 136
Cdd:cd16035    1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 137 VlQWTgasggLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrv 216
Cdd:cd16035   75 M-QPL-----LSPDVPTLGHMLRAAGYYTAYKGKWHL------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 217 nleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllaSSYFVGALivhadcflMRNHTITEQPMCFqrt 296
Cdd:cd16035  106 ------------------------------------------------SGAAGGGY--------KRDPGIAAQAVEW--- 126
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 297 tpliLQEVASflKRNKHGPFLLFVSFL--H-VHIPLITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLI 373
Cdd:cd16035  127 ----LRERGA--KNADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIV 198
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 374 YFTSDHG------GSLENqlGNTQYGgwngiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLA 447
Cdd:cd16035  199 VFTSDHGemggahGLRGK--GFNAYE----------------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLA 260
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 544063470 448 GGEVPQDRVID----GQDLLPLLLGTAQHSDHE-FLMHY 481
Cdd:cd16035  261 GVDAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-473 6.62e-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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 109.75  E-value: 6.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSIGYRVLQw 140
Cdd:cd16154    1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 141 tgasgglpTNETTFAKILKE---KGYATGLIGKWHLGlNCESasdhcHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVN 217
Cdd:cd16154   78 --------SEETLLQLLIKDattAGYSSAVIGKWHLG-GNDN-----SPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 218 LEQKlnflfqvlalvalTLVAGKLTHLiPVSWmpviwsalsavlllassyfvgalivhadcflmrnhtITEQpmcfqrTT 297
Cdd:cd16154  144 TNST-------------EYATTKLTNL-AIDW------------------------------------IDQQ------TK 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 298 P--LILQEVASflkrnkHGPFllfvsflhvHIPLITMENflgKSLHGLY---GDN--------VEEMDWMVGRILDTLDV 364
Cdd:cd16154  168 PwfLWLAYNAP------HTPF---------HLPPAELHS---RSLLGDSadiEANprpyylaaIEAMDTEIGRLLASIDE 229
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 365 EGLSNsTLIYFTSDHG--GSLENQLGNTQY-------GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPTS 435
Cdd:cd16154  230 EEREN-TIIIFIGDNGtpGQVVDLPYTRNHakgslyeGG-----------------INVPLIVSGAGV---ERANERESA 288
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 544063470 436 LM---DVFPTVVRLAGGEVPQdrVIDGQDLLPLLLGTAQHS 473
Cdd:cd16154  289 LVnatDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNAST 327
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
63-546 4.53e-15

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: 77.20  E-value: 4.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyRVLQWTG 142
Cdd:cd16171    1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESWN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 143 ASGGLPTNETTFAKILKEKGYATGLIGKwhlgLNCESAsdhchhplHHgfdhfygmpfSLMGDCARWElsekrvnleQKL 222
Cdd:cd16171   70 NYKGLDPNYPTWMDRLEKHGYHTQKYGK----LDYTSG--------HH----------SVSNRVEAWT---------RDV 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 223 NFLFQVLALVALTLVAGKLTHLIpvswmpviwsalsavlllassyfvgalivhadcfLMRNHTITEqpmcfqRTTPLILQ 302
Cdd:cd16171  119 PFLLRQEGRPTVNLVGDRSTVRV----------------------------------MLKDWQNTD------KAVHWIRK 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 303 EVASFLKrnkhgPFLLFVSFLHVH-IPLITM-ENFLG-KSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 379
Cdd:cd16171  159 EAPNLTQ-----PFALYLGLNLPHpYPSPSMgENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDH 233
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 380 GgslENQLGNTQYggwngiykggKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDG 459
Cdd:cd16171  234 G---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSG 297
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 460 QDLLPLLLGTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTMWKvhFVTpvfqpegagacYGRkvcpcfGE 528
Cdd:cd16171  298 YSLLPLLSESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YAD------GN 352
                        490
                 ....*....|....*...
gi 544063470 529 KVvhhdPPLLFDLSRDPS 546
Cdd:cd16171  353 SV----PPQLFDLSKDPD 366
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
51-463 6.28e-09

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 58.90  E-value: 6.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  51 APSASSDISASRPNILLLM----ADDLgigdIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVR 126
Cdd:COG1368  223 RPTPNPFGPAKKPNVVVILlesfSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLP 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 127 SG-MVSSIGYRVLQwtgasgglptnetTFAKILKEKGYATgligkwhlglncesasdHCHHP------------LHHGFD 193
Cdd:COG1368  299 GGsPYKRPGQNNFP-------------SLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFD 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 194 HFYGMPfslmgdcarwELSEKRVNleqklnflfqvlalvaltlvagklthlipvSWmpviwsalsavlllassyfvGAli 273
Cdd:COG1368  349 EFYDRE----------DFDDPFDG------------------------------GW--------------------GV-- 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 274 vhADcflmrnhtiteQPMcfqrttpliLQEVASFLKRNKhGPFLLFVsflhvhiplITMEN---F-----------LGKS 339
Cdd:COG1368  367 --SD-----------EDL---------FDKALEELEKLK-KPFFAFL---------ITLSNhgpYtlpeedkkipdYGKT 414
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 340 LHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQYggwngiykggkgmGGWEGGIRVPGIFR 419
Cdd:COG1368  415 TLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSP---GKTDY-------------ENPLERYRVPLLIY 478
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 544063470 420 WPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIdGQDLL 463
Cdd:COG1368  479 SPG-LKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
281-463 1.90e-08

Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 57.22  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 281 MRNHTITEQPMCFQRTTpLILQEVASFL-KRNKHGPFLLFVSFLHVHI------------------PLITMENFLGKSLH 341
Cdd:COG3083  348 VSLPRLHTPGGPAQRDR-QITAQWLQWLdQRDSDRPWFSYLFLDAPHAysfpadypkpfqpsedcnYLALDNESDPTPFK 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 342 GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSL----ENQLG-NTQYGGWNgiykggkgmggweggIRVPG 416
Cdd:COG3083  427 NRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGhNSNFSRYQ---------------LQVPL 491
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544063470 417 IFRWPGVLPagRVIGEPTSLMDVFPTVV-RLAGGEVPqdrVID---GQDLL 463
Cdd:COG3083  492 VIHWPGTPP--QVISKLTSHLDIVPTLMqRLLGVQNP---ASDysqGEDLF 537
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
63-448 3.68e-08

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: 55.00  E-value: 3.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  63 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSIGYRvl 138
Cdd:cd16015    1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 139 qwtgasgglPTNETTFAKILKEKGYATGLIgkwhlglncesasdHCHHP---------LHHGFDHFYgmpfslmgDCARW 209
Cdd:cd16015   77 ---------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFY--------DLEDF 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 210 ELSEKRVNleqklnflfqvlalvaltlvagklthlipvSWMpviwsalsavlllassyfvgalivhadcflmrnhtITEQ 289
Cdd:cd16015  126 PDDEKETN------------------------------GWG-----------------------------------VSDE 140
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 290 PMcfqrttpliLQEVASFLKRNKHGPFLLFVsflhvhiplITMENflgkslHGLYGDN---------------------- 347
Cdd:cd16015  141 SL---------FDQALEELEELKKKPFFIFL---------VTMSN------HGPYDLPeekkdeplkveedktelenyln 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 348 -VEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPa 426
Cdd:cd16015  197 aIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK- 261
                        410       420
                 ....*....|....*....|..
gi 544063470 427 GRVIGEPTSLMDVFPTVVRLAG 448
Cdd:cd16015  262 PKKIDRVGSQIDIAPTLLDLLG 283
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
44-218 1.48e-07

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 53.98  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470  44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGR 122
Cdd:COG1524    5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063470 123 YPVRSGMVSSIGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIGKWHLGlncESASDHCHHPLHH-G 191
Cdd:COG1524   80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdG 156
                        170       180
                 ....*....|....*....|....*....
gi 544063470 192 FDHFYGMPFS--LMGDCARWELSEKRVNL 218
Cdd:COG1524  157 RKPLLGNPAAdrWIAAAALELLREGRPDL 185
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
87-131 3.49e-03

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 40.10  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 544063470   87 RTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVS 131
Cdd:pfam01663  19 LTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVG 64
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
346-380 8.82e-03

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 38.56  E-value: 8.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 544063470  346 DNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG 380
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
 
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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