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Conserved domains on  [gi|157266309|ref|NP_000038|]
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arylsulfatase L isoform 2 precursor [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 ...
37-560 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: 752.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 116
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQK 196
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 LNFLFQVLALVALTLVAGKLthLIPVSWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 276
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLY--LGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 QEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 356
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 357 SLENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQD 436
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 437 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDL 516
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 157266309 517 SRDPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 560
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 ...
37-560 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: 752.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 116
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQK 196
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 LNFLFQVLALVALTLVAGKLthLIPVSWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 276
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLY--LGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 QEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 356
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 357 SLENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQD 436
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 437 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDL 516
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 157266309 517 SRDPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 560
Cdd:cd16159  478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
19-524 1.34e-95

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 297.56  E-value: 1.34e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  19 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 98
Cdd:COG3119    5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  99 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesasdhchhplhhgfdhfygmpfslm 178
Cdd:COG3119   85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 179 gdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 258
Cdd:COG3119      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 htiteqpmcfqrtTPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGK----------------------- 313
Cdd:COG3119  130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 314 SLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlG-----NTQY-GGwngiykggkgmggweggI 387
Cdd:COG3119  197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEH-GlrggkGTLYeGG-----------------I 258
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 388 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWH 467
Cdd:COG3119  259 RVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRT 336
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157266309 468 QRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhhDPPLLFDLSRDPSETH 524
Cdd:COG3119  337 GR-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
Sulfatase pfam00884
Sulfatase;
38-423 5.08e-58

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 196.49  E-value: 5.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309   38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtg 117
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  118 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhchhPLHHGFDHFYGmpfslmgdcaRWELSEKRVNLEqkl 197
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG----------RNTGSDLYADPP--- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmRNHTITEQPMCF-QRTTPLIL 276
Cdd:pfam00884 132 -----------------------------------------------------------DVPYNCSGGGVSdEALLDEAL 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  277 QevasfLKRNKHGPFLLFVSFLHVHIPL------------ITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSN 344
Cdd:pfam00884 153 E-----FLDNNDKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157266309  345 STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 423
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
PRK13759 PRK13759
arylsulfatase; Provisional
36-531 3.18e-38

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 147.12  E-value: 3.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  36 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssiGYrvlq 114
Cdd:PRK13759   5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 115 wtgASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchHP--LHHGFDHfygmpfSLMGDcarWELSEKRVN 192
Cdd:PRK13759  77 ---GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 LEQKLNFLFQVLALVALTLVaGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcflmRNHTITEQpmcfQRTT 272
Cdd:PRK13759 133 DKSQFDFVSDYLAWLREKAP-GKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPT 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 PLILQEVASFLKR-NKHGPFLLFVSFLHVHIPLITMENFL-------------------------GKSLHGLYGD----- 321
Cdd:PRK13759 183 NWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeey 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 322 ----------NVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ-------YGGwngiykggkgmggwe 384
Cdd:PRK13759 263 arraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG--------------- 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 385 gGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-YCER 459
Cdd:PRK13759 324 -SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYS 400
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157266309 460 FLHaarWHQRDR-GTMWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSRDPSETHILTPASE 531
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 ...
37-560 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: 752.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 116
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQK 196
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 LNFLFQVLALVALTLVAGKLthLIPVSWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 276
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLY--LGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 QEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 356
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 357 SLENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQD 436
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 437 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDL 516
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 157266309 517 SRDPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 560
Cdd:cd16159  478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
37-524 3.76e-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: 453.17  E-value: 3.76e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRVLQWT 116
Cdd:cd16026    1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasDH-CHHPLHHGFDHFYGMPFSLMGDCARWELSEKRvnleq 195
Cdd:cd16026   76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP----- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 196 klnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivHADCFLMRNHTITEQPMcFQRT-TPL 274
Cdd:cd16026  144 ------------------------------------------------------GPLPPLMENEEVIEQPA-DQSSlTQR 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 275 ILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD- 353
Cdd:cd16026  169 YTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDn 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 --------HGGSleNQL-----GNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR 420
Cdd:cd16026  249 gpwleyggHGGS--AGPlrggkGTTWEGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAA 309
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 421 LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGacygrkvcpc 500
Cdd:cd16026  310 LAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG---------- 373
                        490       500
                 ....*....|....*....|....
gi 157266309 501 fGEKVVHHDPPLLFDLSRDPSETH 524
Cdd:cd16026  374 -GLDPTKLEPPLLYDLEEDPGETY 396
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
37-541 1.70e-132

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: 394.49  E-value: 1.70e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsiGYRV-LQW 115
Cdd:cd16160    1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 TgaSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDhFYG--MPFSLMGDCARWELSekrvnl 193
Cdd:cd16160   79 D--IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGtnLPFTNSWACDDTGRH------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 194 eqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalIVHAD---CFLMRNHTITEQPMCFQR 270
Cdd:cd16160  150 ------------------------------------------------------VDFPDrsaCFLYYNDTIVEQPIQHEH 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 271 TTPLILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYF 350
Cdd:cd16160  176 LTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFF 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 351 TSDHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTV 418
Cdd:cd16160  256 LSDHGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTF 317
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 419 VRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACYGR 495
Cdd:cd16160  318 VDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGGG 390
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157266309 496 KVCP------CFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMERV 541
Cdd:cd16160  391 PLSDyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPSVYEHMLEAVEKL 442
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
38-582 2.69e-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: 310.15  E-value: 2.69e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqwTG 117
Cdd:cd16158    2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhcHHPLHHGFDHFYGMPFSL-MGDCArwelsekrvnleqk 196
Cdd:cd16158   77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHdQGPCQ-------------- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 lnflfqvlalvaltlvagKLTHLIPvswmpviwsalsavlllASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 276
Cdd:cd16158  139 ------------------NLTCFPP-----------------NIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 QEVASFL----KRNKhgPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTS 352
Cdd:cd16158  184 KFAKDFIadnaKEGK--PFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 353 DHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVR 420
Cdd:cd16158  262 DNGpstmrksrggnaGLLKCGKGTTYEGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAK 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 421 LAGGEVPqDRVIDGQDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACY 493
Cdd:cd16158  324 LAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCH 396
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 494 GRKvcpcfgeKVVHHDPPLLFDLSRDPSETHILTpaSEPVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNiwrPWLQPC 573
Cdd:cd16158  397 PSA-------ELTSHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPC 464
                        570
                 ....*....|...
gi 157266309 574 ----CGPFPLCWC 582
Cdd:cd16158  465 ckpgCTPKPSCCQ 477
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
38-527 9.35e-96

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: 297.52  E-value: 9.35e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssigYRVlQ 114
Cdd:cd16142    1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-----TTV-G 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 115 WTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPFSLMGDcarwELSEKRVNle 194
Cdd:cd16142   74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG------RLPTDHGFDEFYGNLYHTIDE----EIVDKAID-- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 qklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcFLMRNHtiteqpmcfqrttpl 274
Cdd:cd16142  142 -----------------------------------------------------------FIKRNA--------------- 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 275 ilqevasflKRNKhgPFLLFVSFLHVHIPLITMENFLGKSL-HGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 353
Cdd:cd16142  148 ---------KADK--PFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTD 216
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 HG-----------GSLENQLGNTQYGGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLA 422
Cdd:cd16142  217 NGpeqdvwpdggyTPFRGEKGTTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALA 279
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 423 GGEVP------QDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVtpVFQPEGAGACYGRK 496
Cdd:cd16142  280 GAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFY 351
                        490       500       510
                 ....*....|....*....|....*....|.
gi 157266309 497 VCPCfgekvvhhdpPLLFDLSRDPSETHILT 527
Cdd:cd16142  352 VLTF----------PLIFNLRRDPKERYDVT 372
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
19-524 1.34e-95

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 297.56  E-value: 1.34e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  19 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 98
Cdd:COG3119    5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  99 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesasdhchhplhhgfdhfygmpfslm 178
Cdd:COG3119   85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 179 gdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 258
Cdd:COG3119      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 htiteqpmcfqrtTPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGK----------------------- 313
Cdd:COG3119  130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 314 SLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlG-----NTQY-GGwngiykggkgmggweggI 387
Cdd:COG3119  197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEH-GlrggkGTLYeGG-----------------I 258
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 388 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWH 467
Cdd:COG3119  259 RVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRT 336
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157266309 468 QRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhhDPPLLFDLSRDPSETH 524
Cdd:COG3119  337 GR-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
37-527 2.67e-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: 283.59  E-value: 2.67e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRvlqw 115
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 tgASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSlmGDCarwELSEKRVNLeq 195
Cdd:cd16161   77 --SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFS--HDS---SLADRYAQF-- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 196 klnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhADCFLMRNhtiteqpmcfqrttpli 275
Cdd:cd16161  142 -------------------------------------------------------ATDFIQRA----------------- 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 276 lqevasflkRNKHGPFLLFVSFLHVHIPLITMENFLGKSLH-GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 354
Cdd:cd16161  150 ---------SAKDRPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDN 220
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 355 G-----GSLENQLGNTQY---GGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEV 426
Cdd:cd16161  221 GpwevkCELAVGPGTGDWqgnLGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASL 295
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 427 PQDRVIDGQDLLPLLLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtmWKVHFVTpvfqpEGAGACygrkvCPCF 501
Cdd:cd16161  296 PPGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALAC-----CGST 358
                        490       500
                 ....*....|....*....|....*.
gi 157266309 502 GEKvVHHDPPLLFDLSRDPSETHILT 527
Cdd:cd16161  359 GPK-LYHDPPLLFDLEVDPAESFPLT 383
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
38-524 1.19e-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: 283.28  E-value: 1.19e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 117
Cdd:cd16144    1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 A-------SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDH------------FYGMPFSLM 178
Cdd:cd16144   81 TklipppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVniggtgnggppsYYFPPGKPN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 179 GDCARWELSEKRVNleqklnflfqvlalvALTlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 258
Cdd:cd16144  155 PDLEDGPEGEYLTD---------------RLT------------------------------------------------ 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 htiteqpmcfqrttplilQEVASFLKRNKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYGDN-------VEEMD 327
Cdd:cd16144  172 ------------------DEAIDFIEQNKDKPFFLYLSHYAVHTPIQarpeLIEKYEKKKKGLRKGQKnpvyaamIESLD 233
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 328 WMVGRILDTLDVEGLSNSTLIYFTSDHGG-SLENQLGNTQY-----------GGwngiykggkgmggweggIRVPGIFRW 395
Cdd:cd16144  234 ESVGRILDALEELGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRW 296
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 396 PGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYcerFLHAARWHQRDRGTM- 474
Cdd:cd16144  297 PGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWH---FPHYHGQGGRPASAIr 373
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157266309 475 ---WK-VHFvtpvfqpegagacygrkvcpcfgekvvHHDPPL-LFDLSRDPSETH 524
Cdd:cd16144  374 kgdWKlIEF---------------------------YEDGRVeLYNLKNDIGETN 401
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
38-524 1.61e-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: 279.47  E-value: 1.61e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssiGYRVLQWT 116
Cdd:cd16143    1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRL----KGGVLGGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGgLPTNETTFAKILKEKGYATGLIGKWHLGLN------CESASDHCHH----------PLHHGFDHFYGMPFSlmgd 180
Cdd:cd16143   77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwkkkdgKKAATGTGKDvdyskpikggPLDHGFDYYFGIPAS---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 181 carwelsekrvnleqklnflfQVLalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnht 260
Cdd:cd16143  152 ---------------------EVL-------------------------------------------------------- 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 261 iteqpmcfqrttPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLD 338
Cdd:cd16143  155 ------------PTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 339 VEGLSNSTLIYFTSDHGGSLENQLGNTQ-----------------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLP 400
Cdd:cd16143  223 ELGLAENTLVIFTSDNGPSPYADYKELEkfghdpsgplrgmkadiYeGG-----------------HRVPFIVRWPGKIP 285
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 401 AGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTMWKVhfv 480
Cdd:cd16143  286 AGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL--- 356
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 157266309 481 tpVFQPEGAGACYGRKvcpcfgeKVVHHDPP-LLFDLSRDPSETH 524
Cdd:cd16143  357 --IDGTGSGGFSYPRG-------KEKLGLPPgQLYNLSTDPGESN 392
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
37-560 1.58e-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: 276.66  E-value: 1.58e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 116
Cdd:cd16157    1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GAS--GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPfslmgDCARWELSEKRvnle 194
Cdd:cd16157   81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGPYDNKA---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 qklnflfqvlalvaltlvagklTHLIPV--SWmpviwsalsavlLLASSYFVGALIvhadcflmrNHTITEQPMcfqrtT 272
Cdd:cd16157  146 ----------------------YPNIPVyrDW------------EMIGRYYEEFKI---------DKKTGESNL-----T 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 PLILQEVASFLKR--NKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYF 350
Cdd:cd16157  178 QIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFF 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 351 TSDHGGSLenqLGNTQYGGWNgIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDR 430
Cdd:cd16157  258 SSDNGAAL---ISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDR 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 431 VIDGQDLLPLLLgtAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVT----PVFQPEGAGACYGRKVCPCFGEKVV 506
Cdd:cd16157  334 AIDGIDLLPVLL--NGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQT 405
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157266309 507 HH-DPPLLFDLSRDPSETHILTPASePVFYQVMERVQQAVWEHQRTLSPVPLQLD 560
Cdd:cd16157  406 DHtKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
38-524 5.12e-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: 244.81  E-value: 5.12e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyRVLQWTG 117
Cdd:cd16145    1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasDHCHHPLHHGFDHFYGmpfslmgdcarwelsekrvnleqkl 197
Cdd:cd16145   75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGP-----GTPGHPTKQGFDYFYG------------------------- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nFLFQVLAlvaltlvagkltHlipvswmpviwsalsavlllasSYFVGALIVHADCFLMRNHTIT-------EQPMCFQR 270
Cdd:cd16145  125 -YLDQVHA------------H----------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTY 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 271 TTPLILQEVASFLKRNKHGPFLLFVSFLHVHIPLIT-------MENFLGKSLHGLYGDNVEE--------MDWMVGRILD 335
Cdd:cd16145  170 SHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVpddgpykYKPKDPGIYAYLPWPQPEKayaamvtrLDRDVGRILA 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 336 TLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQY--------------------GGwngiykggkgmggweggIRVPGIFRW 395
Cdd:cd16145  250 LLKELGIDENTLVVFTSDNGPHSE---GGSEHdpdffdsngplrgykrslyeGG-----------------IRVPFIARW 309
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 396 PGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdr 471
Cdd:cd16145  310 PGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG--- 382
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157266309 472 gtmWKVhfvtpVFQPEGAGacygrkvcpcfgekvvhhdPPLLFDLSRDPSETH 524
Cdd:cd16145  383 ---WKA-----VRHGKKDG-------------------PFELYDLSTDPGETN 408
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
38-436 1.35e-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: 237.72  E-value: 1.35e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssigyrVLQWTG 117
Cdd:cd16022    1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqkl 197
Cdd:cd16022   73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplilQ 277
Cdd:cd16022  103 -------------------------------------------------------------------------------D 103
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 EVASFLKRNKHG-PFLLFVSFLHVHIPLItmenflgkslhglYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 356
Cdd:cd16022  104 EAIDFIERRDKDkPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 357 SLENqlGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQD 436
Cdd:cd16022  171 MLGD--HGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
38-547 1.05e-71

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: 235.91  E-value: 1.05e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSIGYRVLqwt 116
Cdd:cd16146    1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSLMGDCARWELSEkrvnleqk 196
Cdd:cd16146   76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND-------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 lnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassYFvgalivhaDCFLMRNHTITE-QPMCfqrtTPLI 275
Cdd:cd16146  137 ---------------------------------------------YF--------DDTYYHNGKFVKtEGYC----TDVF 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 276 LQEVASFLKRNKHGPFLLFVSFLHVHIPLITMEN----FLGKSLH----GLYGdNVEEMDWMVGRILDTLDVEGLSNSTL 347
Cdd:cd16146  160 FDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKyldpYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEENTI 238
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 348 IYFTSDHGGSLENQLGN---------TQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPT 417
Cdd:cd16146  239 VIFMSDNGPAGGVPKRFnagmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLPT 301
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 418 VVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTMWKVHFVtpVFQPEgagacYgRKV 497
Cdd:cd16146  302 LLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W-RLV 364
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 157266309 498 CPcfgekvvHHDPPLLFDLSRDPSETHILTpASEPVFYQVMERVQQAVWE 547
Cdd:cd16146  365 SP-------KGFQPELYDIENDPGEENDVA-DEHPEVVKRLKAAYEAWWD 406
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-466 2.35e-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: 2.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqwtg 117
Cdd:cd16151    1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 aSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESASDhchHPLHHGFDHFygmpfslmgdCArWELSEKRVNLEQKL 197
Cdd:cd16151   68 -FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEY----------CL-WQLTETGEKYSRPA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 NFLFQVLalvaltlvAGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcFLMRnhtiteqpmcfqrttplilq 277
Cdd:cd16151  132 TPTFNIR--------NGKLLETTEGDYGPDLFAD----------------------FLID-------------------- 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 evasFLKRNKHGPFLLFVSFLHVHIPL----------ITMENFLGKSLHglYGDNVEEMDWMVGRILDTLDVEGLSNSTL 347
Cdd:cd16151  162 ----FIERNKDQPFFAYYPMVLVHDPFvptpdspdwdPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 348 IYFTSDHG--GSLENQLGNTQY-GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGG 424
Cdd:cd16151  236 IIFTGDNGthRPITSRTNGREVrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGA 306
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 157266309 425 EVPQDRVIDGQDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 466
Cdd:cd16151  307 PLPEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
37-526 1.14e-62

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: 211.66  E-value: 1.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVsSIGYRvlqwt 116
Cdd:cd16034    1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHH----PLHHGFDHFYGMpfslmgdcarwelsekrvn 192
Cdd:cd16034   75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------------------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 leqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhaDCFLMRNHTI----TEQPMCF 268
Cdd:cd16034  131 -----------------------------------------------------------ECNHDHNNPHyyddDGKRIYI 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 269 QRTTPLILQEVA-SFLKRNKHG--PFLLFVSF------------------------LHVHIPLITMENF-LGKSLHGLYG 320
Cdd:cd16034  152 KGYSPDAETDLAiEYLENQADKdkPFALVLSWnpphdpyttapeeyldmydpkkllLRPNVPEDKKEEAgLREDLRGYYA 231
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 321 dNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQYGGwngiykggkgmggwegGIRVPGIFRWPG 397
Cdd:cd16034  232 -MITALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYPG 294
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 398 VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTM--- 474
Cdd:cd16034  295 KIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtd 372
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157266309 475 -WKvhFVtpvfqpegagacygrkvcpcfgekVVHHDPPLLFDLSRDPSETHIL 526
Cdd:cd16034  373 rYT--YV------------------------RDKNGPWLLFDNEKDPYQLNNL 399
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
38-524 1.94e-62

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: 210.87  E-value: 1.94e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssiGYRVLqWTG 117
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVI-LAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasdHCHH---PLHHGFDHFYGMpFSLMGDcarwelsekrvnle 194
Cdd:cd16029   75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY-YGGAED-------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 qklnflfqvlalvaltlvagkltHLIPVSWMPVIWSalsavlllassyfvgalivhaDCFLMRNHTIT-EQPMCFqrTTP 273
Cdd:cd16029  132 -----------------------YYTHTSGGANDYG---------------------NDDLRDNEEPAwDYNGTY--STD 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 274 LILQEVASFLKR-NKHGPFLLFVSFLHVHIPL------ITMENFLGKSLHG----LYGDNVEEMDWMVGRILDTLDVEGL 342
Cdd:cd16029  166 LFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLqvppeyADPYEDKFAHIKDedrrTYAAMVSALDESVGNVVDALKAKGM 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 343 SNSTLIYFTSDHGGSLENQLG----------NTQY-GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIGEPT 409
Cdd:cd16029  246 LDNTLIVFTSDNGGPTGGGDGgsnyplrggkNTLWeGG-----------------VRVPA-FVWSPLLPpkRGTVSDGLM 307
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 410 SLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRgtmwkvhfvtPVFQPEGA 489
Cdd:cd16029  308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDD----------ITRTTGGA 364
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 157266309 490 GACYGRKvcpcfgeKVVHHDPplLFDLSRDPSETH 524
Cdd:cd16029  365 AIRVGDW-------KLIVGKP--LFNIENDPCERN 390
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
38-550 1.74e-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: 200.04  E-value: 1.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssIGYRVLQWTg 117
Cdd:cd16027    1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 asggLPTNETTFAKILKEKGYATGLIGKWHlgLNCESASDHCHHPLHHGFDHFYGMPFslMGDCARWelsEKRVNLEQkl 197
Cdd:cd16027   76 ----LPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWDY--ASNAADF---LNRAKKGQ-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 NFLFQvlalvaltlVAGKLTHlipVSWMPVIWSAL----SAVLLlaSSYFVgalivhaDcflmrnhtiteqpmcfqrtTP 273
Cdd:cd16027  143 PFFLW---------FGFHDPH---RPYPPGDGEEPgydpEKVKV--PPYLP-------D-------------------TP 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 274 LILQEVASFLkrnkhgpfllfvsflhvhiplitmenflgkslhglygDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 353
Cdd:cd16027  183 EVREDLADYY-------------------------------------DEIERLDQQVGEILDELEEDGLLDNTIVIFTSD 225
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 HGGSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvID 433
Cdd:cd16027  226 HGMPFPRAKGTLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQ 286
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 434 GQDLLPLLLG-TAQHSDHEFLMH-------YCERFLHAARWHqrdrgtmwkvhfvtpvfqpegagacYgrkvcpcfgekV 505
Cdd:cd16027  287 GRSFLPLLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK-------------------------Y-----------I 330
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 157266309 506 VHHDPPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 550
Cdd:cd16027  331 RNYMPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
Sulfatase pfam00884
Sulfatase;
38-423 5.08e-58

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 196.49  E-value: 5.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309   38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtg 117
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  118 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhchhPLHHGFDHFYGmpfslmgdcaRWELSEKRVNLEqkl 197
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG----------RNTGSDLYADPP--- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmRNHTITEQPMCF-QRTTPLIL 276
Cdd:pfam00884 132 -----------------------------------------------------------DVPYNCSGGGVSdEALLDEAL 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  277 QevasfLKRNKHGPFLLFVSFLHVHIPL------------ITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSN 344
Cdd:pfam00884 153 E-----FLDNNDKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157266309  345 STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 423
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
448-582 1.05e-57

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 189.06  E-value: 1.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  448 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 527
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157266309  528 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 582
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
36-543 5.30e-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: 5.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  36 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqw 115
Cdd:cd16031    1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDhchhplhhGFDHFYGMP---------FSLMGDCARWEL 186
Cdd:cd16031   71 DNNGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFPgqgsyydpeFIENGKRVGQKG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 187 SEKRVNLEQKLNFL--------FqvlalvALTlVAGKLTHLipvSWMPViwsalsavlllassyfvgalIVHADcfLMRN 258
Cdd:cd16031  143 YVTDIITDKALDFLkerdkdkpF------CLS-LSFKAPHR---PFTPA--------------------PRHRG--LYED 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 HTITE-----------QPMCFQRTTPLI-LQEVASFLKRNKHGpfllfvsflhvhiplITMENFLGkSLHGlygdnveeM 326
Cdd:cd16031  191 VTIPEpetfddddyagRPEWAREQRNRIrGVLDGRFDTPEKYQ---------------RYMKDYLR-TVTG--------V 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 327 DWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGG-WNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVI 405
Cdd:cd16031  247 DDNVGRILDYLEEQGLADNTIIIYTSDNG----FFLGEHGLFDkRL----------MYEESIRVPLIIRDPRLIKAGTVV 312
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 406 GEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHS-DHEFLMHYCE--RFLHAARWH--QRDRgtmWK-VHF 479
Cdd:cd16031  313 DALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNVPTHEgvRTER---YKyIYY 387
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157266309 480 vtpvfqpegagacygrkvcpcfgekvvHHDPPL--LFDLSRDPSETH--ILTPASEPVFYQVMERVQQ 543
Cdd:cd16031  388 ---------------------------YGVWDEeeLYDLKKDPLELNnlANDPEYAEVLKELRKRLEE 428
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
37-524 8.55e-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: 188.04  E-value: 8.55e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEDGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSIGYRVLQW 115
Cdd:cd16025    2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLN----CESASDH-----------------------CHHPLH---- 164
Cdd:cd16025   78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPDdyysTDDLTDKaieyideqkapdkpfflylafgaPHAPLQapke 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 165 -----HG-FDhfygmpfslMGdcarWE-LSEKRvnLE-QKlnflfqvlalvALTLVAG--KLTHLIPvsWMPViWSALSA 234
Cdd:cd16025  158 widkyKGkYD---------AG----WDaLREER--LErQK-----------ELGLIPAdtKLTPRPP--GVPA-WDSLSP 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 235 vlllassyfvgalivhadcflmrnhtitEQPMCFQRttpliLQEV-ASFlkrnkhgpfllfvsflhvhiplitmenflgk 313
Cdd:cd16025  209 ----------------------------EEKKLEAR-----RMEVyAAM------------------------------- 224
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 314 slhglygdnVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN---QLGNTQY---------GGwngiykggkgmg 381
Cdd:cd16025  225 ---------VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPgwaNASNTPFrlykqasheGG------------ 283
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 382 gweggIRVPGIFRWP-GVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV------IDGQDLLPLLLGTAQHSDHEFLm 454
Cdd:cd16025  284 -----IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ- 357
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157266309 455 hYCERFLHAARWHQRdrgtmWKVhfvtpvfqpegagacygrkvcpcfgekVVHHDPPL------LFDLSRDPSETH 524
Cdd:cd16025  358 -YFELFGNRAIRKGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-520 6.11e-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: 172.73  E-value: 6.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRsgmvssIGYrvlqWTG 117
Cdd:cd16037    1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WDN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGgLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhchhplHHGFDHfygmpfslmgdcarwelsekrvnleqkl 197
Cdd:cd16037   71 ADP-YDGDVPSWGHALRAAGYETVLIGKLHFRGEDQ----------RHGFRY---------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhaDcflmRNhtiteqpmcfqrttplILQ 277
Cdd:cd16037  112 ------------------------------------------------------D----RD----------------VTE 117
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 EVASFLKRNKH--GPFLLFVSFLHVHIPLITMENFLGKSLHGL---YGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTS 352
Cdd:cd16037  118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 353 DHGgsleNQLG-------NTQYggwngiykggkgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGE 425
Cdd:cd16037  198 DHG----DMLGerglwgkSTMY----------------EESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAP 256
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 426 VPQDRviDGQDLLPLLLGTAQHSDHEFlmhyCErfLHAARwhQRDRGTM-----WK-VHFVtpvfqpegagacygrkvcp 499
Cdd:cd16037  257 PPPDL--DGRSLLPLAEGPDDPDRVVF----SE--YHAHG--SPSGAFMlrkgrWKyIYYV------------------- 307
                        490       500
                 ....*....|....*....|.
gi 157266309 500 cfgekvvhHDPPLLFDLSRDP 520
Cdd:cd16037  308 --------GYPPQLFDLENDP 320
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-547 6.20e-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: 167.01  E-value: 6.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqWTG 117
Cdd:cd16033    1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 A-SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHC--HHPLHHGFDHFYgmpfslmGDCARWELSEkrvnLE 194
Cdd:cd16033   76 AySRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEETPLDYGFdeYLPVETTIEYFL-------ADRAIEMLEE----LA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 QKlnflfqvlalvaltlvaGKlthliPvsWMpvIWSAlsavlllassyFVGAlivHADCFLmrnhtitEQPMcFQRTTPL 274
Cdd:cd16033  145 AD-----------------DK-----P--FF--LRVN-----------FWGP---HDPYIP-------PEPY-LDMYDPE 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 275 ILQEVASF---------LKRNKHGPFLLFVSFLHVHIPLITmeNFLGkslhglygdNVEEMDWMVGRILDTLDVEGLSNS 345
Cdd:cd16033  177 DIPLPESFaddfedkpyIYRRERKRWGVDTEDEEDWKEIIA--HYWG---------YITLIDDAIGRILDALEELGLADD 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 346 TLIYFTSDHGGSLENQlgntqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGE 425
Cdd:cd16033  246 TLVIFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVD 313
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 426 VPQDrvIDGQDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWHQrdrgtmwkvhfvtpVFQPEGagacygr 495
Cdd:cd16033  314 VPPK--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYKY--------------VFNGFD------- 368
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157266309 496 kvcpcFGEkvvhhdpplLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWE 547
Cdd:cd16033  369 -----IDE---------LYDLESDPYELNNL--IDDPEYEEILREMRTRLYE 404
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
38-520 4.15e-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: 156.97  E-value: 4.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 117
Cdd:cd16032    1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGgLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhCHHPLHHGFDHfygmpfslmgDcarwelsekrvnlEQkl 197
Cdd:cd16032   71 AAE-FPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFDY----------D-------------EE-- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpVIWSALSAVLLLAssyfvgalivhadcflmRNHTiteqpmcfqrttplilq 277
Cdd:cd16032  115 -----------------------------VAFKAVQKLYDLA-----------------RGED----------------- 131
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 evasflKRnkhgPFLLFVSFLHVHIPLITMENFLG----KSLHGLYGdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 353
Cdd:cd16032  132 ------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 HGgsleNQLGntQYGGWngiykggKGMGGWEGGIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV-I 432
Cdd:cd16032  201 HG----DMLG--ERGLW-------YKMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpL 266
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 433 DGQDLLPLLLGTAQHSDHEFLMHYCErflhaarwhqrdrgtmwkvhfvtpvfqpEGAGAcygrkvcPCF-----GEKVVH 507
Cdd:cd16032  267 DGRSLLPLLEGGDSGGEDEVISEYLA----------------------------EGAVA-------PCVmirrgRWKFIY 311
                        490
                 ....*....|....*
gi 157266309 508 --HDPPLLFDLSRDP 520
Cdd:cd16032  312 cpGDPDQLFDLEADP 326
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-439 2.21e-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: 152.78  E-value: 2.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 117
Cdd:cd16149    1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqkl 197
Cdd:cd16149   81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgaliVHADCFLMRNHtiteqpmcfqrttplilq 277
Cdd:cd16149  113 ---------------------------------------------------DDAADFLRRRA------------------ 123
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 evasflKRNKhgPFLLFVSFLHVHIPlitmenflgkslHGlYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGS 357
Cdd:cd16149  124 ------EAEK--PFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFN 182
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 358 LenqlgnTQYGGW---------NgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQ 428
Cdd:cd16149  183 M------GHHGIWgkgngtfplN----------MYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPA 246
                        410
                 ....*....|.
gi 157266309 429 DRVIDGQDLLP 439
Cdd:cd16149  247 DPRLPGRSFAD 257
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-439 6.45e-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: 151.93  E-value: 6.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyrvLQWT 116
Cdd:cd16148    1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIgkwhlglncesaSDHCHHPLHHGFDH--FYGMPFSLMGDCARWELSEkrvnle 194
Cdd:cd16148   67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDRgfDTFEDFRGQEGDPGEEGDE------ 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 qklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrTTPL 274
Cdd:cd16148  129 ----------------------------------------------------------------------------RAER 132
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 275 ILQEVASFLKRNKHG-PFLLFVSFLHVHIPLitmenflgkslhgLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 353
Cdd:cd16148  133 VTDRALEWLDRNADDdPFFLFLHYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 HGGSLeNQLGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVRLAGGEVPQDrvID 433
Cdd:cd16148  200 HGEEF-GEHGLYWGHGSN----------LYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SD 265

                 ....*.
gi 157266309 434 GQDLLP 439
Cdd:cd16148  266 GRSLLP 271
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
38-550 1.08e-39

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: 150.87  E-value: 1.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqWTG 117
Cdd:cd16028    1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASggLPTNETTFAKILKEKGYATGLIGKWHL-----GLNCESASDHCHHPLHHGFDHFYGMPFslmgdcARWELSEKRVN 192
Cdd:cd16028   72 TP--LDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFDPVDRLDE------YPAEDSDTAFL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 LEQKLNFL--------FQVLA-------LVAltlvagklthliPVSWMPVI-WSALSAVLllassyfvgalivhadcflm 256
Cdd:cd16028  144 TDRAIEYLderqdepwFLHLSyirphppFVA------------PAPYHALYdPADVPPPI-------------------- 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 257 RNHTITEQpmcfQRTTPLIlqevASFLKRNKHGpfllfvSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDT 336
Cdd:cd16028  192 RAESLAAE----AAQHPLL----AAFLERIESL------SFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDY 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 337 LDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGGwngiykggkGMGGWEGGIRVPGIFRWPGVL---PAGRVIGEPTSLMD 413
Cdd:cd16028  258 LKETGQWDDTLIVFTSDHG----EQLGDHWLWG---------KDGFFDQAYRVPLIVRDPRREadaTRGQVVDAFTESVD 324
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 414 VFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQRDRGTmwkvhfvtpvfQP 486
Cdd:cd16028  325 VMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALGL-----------SP 384
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157266309 487 EGAGACYGRkvcpcfGE--KVVHHD--PPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 550
Cdd:cd16028  385 DECSLAVIR------DErwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSWRM 444
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
36-450 1.53e-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: 150.03  E-value: 1.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  36 SRPNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqW 115
Cdd:cd16030    1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----F 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 TGASGglptNETTFAKILKEKGYATGLIGKWHlglncesasdhchhplHHGFDHFYGMPFSlmgdcarWELSEKRVNLEQ 195
Cdd:cd16030   76 RKVAP----DAVTLPQYFKENGYTTAGVGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 196 KLNFLFQVLALVALTLVAGKLTHLIPV--SWMPVIWSALSAVLLLAS------SYFVGA--------LIVHADCFLMRNH 259
Cdd:cd16030  129 YPPGKLCPGKKGGKGGGGGPAWEAADVpdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 260 TITEQPMCFQRT-TPLI----LQEVasflkRNKHGPFLLFVSFLHVHIPlitmENFLGKSLHGLYGdNVEEMDWMVGRIL 334
Cdd:cd16030  209 ESIPLPNPFDPIdLPEVawndLDDL-----PKYGDIPALNPGDPKGPLP----DEQARELRQAYYA-SVSYVDAQVGRVL 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 335 DTLDVEGLSNSTLIYFTSDHGGslenQLGntQYGGW---------NgiykggkgmggweggiRVPGIFRWPGVLPAGRVI 405
Cdd:cd16030  279 DALEELGLADNTIVVLWSDHGW----HLG--EHGHWgkhtlfeeaT----------------RVPLIIRAPGVTKPGKVT 336
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 157266309 406 GEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLLLGTAQHSDH 450
Cdd:cd16030  337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKD 379
PRK13759 PRK13759
arylsulfatase; Provisional
36-531 3.18e-38

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 147.12  E-value: 3.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  36 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssiGYrvlq 114
Cdd:PRK13759   5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 115 wtgASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchHP--LHHGFDHfygmpfSLMGDcarWELSEKRVN 192
Cdd:PRK13759  77 ---GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 LEQKLNFLFQVLALVALTLVaGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcflmRNHTITEQpmcfQRTT 272
Cdd:PRK13759 133 DKSQFDFVSDYLAWLREKAP-GKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPT 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 PLILQEVASFLKR-NKHGPFLLFVSFLHVHIPLITMENFL-------------------------GKSLHGLYGD----- 321
Cdd:PRK13759 183 NWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeey 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 322 ----------NVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ-------YGGwngiykggkgmggwe 384
Cdd:PRK13759 263 arraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG--------------- 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 385 gGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-YCER 459
Cdd:PRK13759 324 -SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYS 400
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157266309 460 FLHaarWHQRDR-GTMWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSRDPSETHILTPASE 531
Cdd:PRK13759 401 SDN---YLTDGKwKYIW--FSQTGEEQ---------------------------LFDLKKDPHELHNLSPSEK 441
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
37-543 2.34e-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: 142.37  E-value: 2.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRvlqwt 116
Cdd:cd16152    1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 gASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqk 196
Cdd:cd16152   71 -NGIPLPADEKTLAHYFRDAGYETGYVGKWHL------------------------------------------------ 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 lnflfqvlalvaltlvAGklthlipvswmpviwsalsavlllassYFVGALIVHADCFLMrnhtiteqpmcfqrttplil 276
Cdd:cd16152  102 ----------------AG---------------------------YRVDALTDFAIDYLD-------------------- 118
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 qevasflKRNKHGPFLLFVSFLHVHiplitMEN------------------FLGKSLHGLYGDN----------VEEMDW 328
Cdd:cd16152  119 -------NRQKDKPFFLFLSYLEPH-----HQNdrdryvapegsaerfanfWVPPDLAALPGDWaeelpdylgcCERLDE 186
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 329 MVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlgNTQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEP 408
Cdd:cd16152  187 NVGRIRDALKELGLYDNTIIVFTSDHGCHFRTR--NAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEEL 252
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 409 TSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCE----RFLHAARW----HQRDRGtmWKVHFV 480
Cdd:cd16152  253 VSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISEsqvgRAIRTDRWkysvAAPDKD--GWKDSG 328
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157266309 481 TPVFQPEgagacygrkvcpcfgekvvhhdppLLFDLSRDPSETHILtpASEPVFYQVMERVQQ 543
Cdd:cd16152  329 SDVYVED------------------------YLYDLEADPYELVNL--IGRPEYREVAAELRE 365
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-540 1.79e-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: 134.23  E-value: 1.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  36 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssigy 110
Cdd:cd16155    1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 111 rvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLnCESASDHCHHP--------LHHGFDH---FYGMPFSLMg 179
Cdd:cd16155   74 ------GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF-ADAAIEFLEEYkdgdkpffMYVAFTAphdPRQAPPEYL- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 180 dcarwelseKRVNLEqklnflfqvlalvaltlvagklTHLIPVSWMPViwsalsavlllassY-FVGALIVHADcflmrn 258
Cdd:cd16155  146 ---------DMYPPE----------------------TIPLPENFLPQ--------------HpFDNGEGTVRD------ 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 htitEQPMCFQRTTplilQEVASFLKRNkhgpfllfvsflhvhiplitmenflgkslhglYGdNVEEMDWMVGRILDTLD 338
Cdd:cd16155  175 ----EQLAPFPRTP----EAVRQHLAEY--------------------------------YA-MITHLDAQIGRILDALE 213
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 339 VEGLSNSTLIYFTSDHG------GSLENQlgNTQYGGWngiykggkgmggweggiRVPGIFRWPGVlPAGRVIGEPTSLM 412
Cdd:cd16155  214 ASGELDNTIIVFTSDHGlavgshGLMGKQ--NLYEHSM-----------------RVPLIISGPGI-PKGKRRDALVYLQ 273
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 413 DVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMhycerFLHAARWHQRDRgtmWKVHFVTPvfqpegaga 491
Cdd:cd16155  274 DVFPTLCELAGIEIPES--VEGKSLLPVIRGeKKAVRDTLYGA-----YRDGQRAIRDDR---WKLIIYVP--------- 334
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 157266309 492 cygrkvcpcfGEKVVhhdppLLFDLSRDPSETHILtpASEPVFYQVMER 540
Cdd:cd16155  335 ----------GVKRT-----QLFDLKKDPDELNNL--ADEPEYQERLKK 366
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
38-422 1.22e-30

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: 119.83  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQwT 116
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPEL-P 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnLEQK 196
Cdd:cd00016   80 SRAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------------------LLKA 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 LNFLfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplil 276
Cdd:cd00016  112 IDET---------------------------------------------------------------------------- 115
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 qevasflkrNKHGPFLLFVSFLHVHIPLitmenFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 356
Cdd:cd00016  116 ---------SKEKPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157266309 357 SLENqLGNTqyggwngiYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLA 422
Cdd:cd00016  182 IDKG-HGGD--------PKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-524 2.07e-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: 123.50  E-value: 2.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssiGYRVLQWT 116
Cdd:cd16150    1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHChhplhhgfdhfygmpfslmgdcarwelSEKRVNLEQK 196
Cdd:cd16150   74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC---------------------------DSDEACVRTA 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 LNFLFQvlalvaltlvagkltHLIPVSWmpviwsalsaVLLLASSY----FVgaliVHADCFLMrnhtITEQPMCFQRTT 272
Cdd:cd16150  122 IDWLRN---------------RRPDKPF----------CLYLPLIFphppYG----VEEPWFSM----IDREKLPPRRPP 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 PLILQEVASFLK-RNKHGpfllFVSflhvhiplITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFT 351
Cdd:cd16150  169 GLRAKGKPSMLEgIEKQG----LDR--------WSEERW--RELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFF 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 352 SDHG-------------GSLENQLgntqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTV 418
Cdd:cd16150  235 SDHGdytgdyglvekwpNTFEDCL------------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPPTL 289
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 419 VRLAGgeVPQDRVIDGQDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHqrdrgtMWKVHFVTPVFQPEG----AGAC 492
Cdd:cd16150  290 LDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQA------MEGGHGPYDLKWPRLlqqeEPPE 357
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 157266309 493 YGRKVcpcfgeKVVHHD---------PPLLFDLSRDPSETH 524
Cdd:cd16150  358 HTKAV------MIRTRRykyvyrlyePDELYDLEADPLELH 392
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
38-441 6.33e-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: 6.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 117
Cdd:cd16156    1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 aSGGLPTNETTFAKILKEKGYATGLIGKWHL------GLN-CESASDHchhplhhgfDHFYGMPFSLMgdcarwELSEKR 190
Cdd:cd16156   71 -CMALGDNVKTIGQRLSDNGIHTAYIGKWHLdggdyfGNGiCPQGWDP---------DYWYDMRNYLD------ELTEEE 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 191 VnleqklnflfqvlalvaltlvagklthlipvswmpVIWSalsavLLLASSYfvgalivhadcflmrNHTITEQPMCFQR 270
Cdd:cd16156  135 R-----------------------------------RKSR-----RGLTSLE---------------AEGIKEEFTYGHR 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 271 TTPLILQevasFLKRNKHGPFLLFVSFLHVHIPLI------TM-------------ENFLGKSLH------GLYGDNVEE 325
Cdd:cd16156  160 CTNRALD----FIEKHKDEDFFLVVSYDEPHHPFLcpkpyaSMykdfefpkgenayDDLENKPLHqrlwagAKPHEDGDK 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 326 M--------------DWMVGRILDTLDvEGLSNSTLIYfTSDHGGSLENQL----GNTQYggwngiykggkgmggwEGGI 387
Cdd:cd16156  236 GtikhplyfgcnsfvDYEIGRVLDAAD-EIAEDAWVIY-TSDHGDMLGAHKlwakGPAVY----------------DEIT 297
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157266309 388 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLL 441
Cdd:cd16156  298 NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
37-435 1.44e-28

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: 117.65  E-value: 1.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSIGYRV 112
Cdd:cd16147    1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 113 LQWTGAsgglptNETTFAKILKEKGYATGLIGKWhlgLN-CESASDHCHHPLhhGFDHFYGMPFslmgdcarwelsekrv 191
Cdd:cd16147   77 FWQNGL------ERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVG---------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 192 nleqklNFLFQVLALVALTLVAGklthliPVSWmpviwsalsavlllASSYFvgalivhadcflmrnhtiteqpmcfqrt 271
Cdd:cd16147  130 ------NSTYYNYTLSNGGNGKH------GVSY--------------PGDYL---------------------------- 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 272 TPLILQEVASFLKR--NKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYG---------------------DNVE 324
Cdd:cd16147  156 TDVIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTpaprYANLFPNVTAPPRPPpnnpdvsdkphwlrrlpplnpTQIA 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 325 EMDW--------------MVGRILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQ-YggwngiykggkgmggwEGG 386
Cdd:cd16147  236 YIDElyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHRLPPGKRTpY----------------EED 299
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 157266309 387 IRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQ 435
Cdd:cd16147  300 IRVPLLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
37-437 6.53e-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: 113.24  E-value: 6.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  37 RPNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVS 106
Cdd:cd16153    1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 107 SIGYrvlqWTGASGGLPtnetTFAKILKEKGYATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwel 186
Cdd:cd16153   81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH--------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 187 sekrvnLEQKLNFLFQvlALVALTLVAGKlthlipVSWMPviwsalsavlllassyfvgalivhadcflmrnhtiteqpm 266
Cdd:cd16153  114 ------LEAFQRYLKN--ANQSYKSFWGK------IAKGA---------------------------------------- 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 267 cfqrttplilqevasflKRNKhgPFLLFVSFLHVHIPLITMENFLGK-SLHGL--YGDNveemdwMVGRILDTLDVEGLS 343
Cdd:cd16153  140 -----------------DSDK--PFFVRLSFLQPHTPVLPPKEFRDRfDYYAFcaYGDA------QVGRAVEAFKAYSLK 194
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 344 N---STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmggweGGIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTV 418
Cdd:cd16153  195 QdrdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTL 261
                        410
                 ....*....|....*....
gi 157266309 419 VRLAGGEVPQDRVIDGQDL 437
Cdd:cd16153  262 LAAAGVDVDAPDYLDGRDL 280
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-448 5.92e-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: 5.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSIGYRVLQw 115
Cdd:cd16154    1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 tgasgglpTNETTFAKILKE---KGYATGLIGKWHLGlNCESasdhcHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVN 192
Cdd:cd16154   78 --------SEETLLQLLIKDattAGYSSAVIGKWHLG-GNDN-----SPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 LEQKlnflfqvlalvalTLVAGKLTHLiPVSWmpviwsalsavlllassyfvgalivhadcflmrnhtITEQpmcfqrTT 272
Cdd:cd16154  144 TNST-------------EYATTKLTNL-AIDW------------------------------------IDQQ------TK 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 P--LILQEVASflkrnkHGPFllfvsflhvHIPLITMENflgKSLHGLY---GDN--------VEEMDWMVGRILDTLDV 339
Cdd:cd16154  168 PwfLWLAYNAP------HTPF---------HLPPAELHS---RSLLGDSadiEANprpyylaaIEAMDTEIGRLLASIDE 229
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 340 EGLSNsTLIYFTSDHG--GSLENQLGNTQY-------GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPTS 410
Cdd:cd16154  230 EEREN-TIIIFIGDNGtpGQVVDLPYTRNHakgslyeGG-----------------INVPLIVSGAGV---ERANERESA 288
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 157266309 411 LM---DVFPTVVRLAGGEVPQdrVIDGQDLLPLLLGTAQHS 448
Cdd:cd16154  289 LVnatDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNAST 327
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-456 8.56e-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: 108.06  E-value: 8.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYR 111
Cdd:cd16035    1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 112 VlQWTgasggLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrv 191
Cdd:cd16035   75 M-QPL-----LSPDVPTLGHMLRAAGYYTAYKGKWHL------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 192 nleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllaSSYFVGALivhadcflMRNHTITEQPMCFqrt 271
Cdd:cd16035  106 ------------------------------------------------SGAAGGGY--------KRDPGIAAQAVEW--- 126
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 272 tpliLQEVASflKRNKHGPFLLFVSFL--H-VHIPLITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLI 348
Cdd:cd16035  127 ----LRERGA--KNADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIV 198
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 349 YFTSDHG------GSLENqlGNTQYGgwngiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLA 422
Cdd:cd16035  199 VFTSDHGemggahGLRGK--GFNAYE----------------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLA 260
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 157266309 423 GGEVPQDRVID----GQDLLPLLLGTAQHSDHE-FLMHY 456
Cdd:cd16035  261 GVDAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
38-521 5.20e-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: 76.81  E-value: 5.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyRVLQWTG 117
Cdd:cd16171    1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESWN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKwhlgLNCESAsdhchhplHHgfdhfygmpfSLMGDCARWElsekrvnleQKL 197
Cdd:cd16171   70 NYKGLDPNYPTWMDRLEKHGYHTQKYGK----LDYTSG--------HH----------SVSNRVEAWT---------RDV 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 NFLFQVLALVALTLVAGKLTHLIpvswmpviwsalsavlllassyfvgalivhadcfLMRNHTITEqpmcfqRTTPLILQ 277
Cdd:cd16171  119 PFLLRQEGRPTVNLVGDRSTVRV----------------------------------MLKDWQNTD------KAVHWIRK 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 EVASFLKrnkhgPFLLFVSFLHVH-IPLITM-ENFLG-KSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 354
Cdd:cd16171  159 EAPNLTQ-----PFALYLGLNLPHpYPSPSMgENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDH 233
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 355 GgslENQLGNTQYggwngiykggKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDG 434
Cdd:cd16171  234 G---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSG 297
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 435 QDLLPLLLGTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTMWKvhFVTpvfqpegagacYGRkvcpcfGE 503
Cdd:cd16171  298 YSLLPLLSESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YAD------GN 352
                        490
                 ....*....|....*...
gi 157266309 504 KVvhhdPPLLFDLSRDPS 521
Cdd:cd16171  353 SV----PPQLFDLSKDPD 366
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
26-438 6.52e-09

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 58.51  E-value: 6.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  26 APSASSDISASRPNILLLM----ADDLgigdIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVR 101
Cdd:COG1368  223 RPTPNPFGPAKKPNVVVILlesfSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLP 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 102 SG-MVSSIGYRVLQwtgasgglptnetTFAKILKEKGYATgligkwhlglncesasdHCHHP------------LHHGFD 168
Cdd:COG1368  299 GGsPYKRPGQNNFP-------------SLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFD 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 169 HFYGMPfslmgdcarwELSEKRVNleqklnflfqvlalvaltlvagklthlipvSWmpviwsalsavlllassyfvGAli 248
Cdd:COG1368  349 EFYDRE----------DFDDPFDG------------------------------GW--------------------GV-- 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 249 vhADcflmrnhtiteQPMcfqrttpliLQEVASFLKRNKhGPFLLFVsflhvhiplITMEN---F-----------LGKS 314
Cdd:COG1368  367 --SD-----------EDL---------FDKALEELEKLK-KPFFAFL---------ITLSNhgpYtlpeedkkipdYGKT 414
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 315 LHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQYggwngiykggkgmGGWEGGIRVPGIFR 394
Cdd:COG1368  415 TLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSP---GKTDY-------------ENPLERYRVPLLIY 478
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 157266309 395 WPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIdGQDLL 438
Cdd:COG1368  479 SPG-LKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
256-438 1.84e-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: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 256 MRNHTITEQPMCFQRTTpLILQEVASFL-KRNKHGPFLLFVSFLHVHI------------------PLITMENFLGKSLH 316
Cdd:COG3083  348 VSLPRLHTPGGPAQRDR-QITAQWLQWLdQRDSDRPWFSYLFLDAPHAysfpadypkpfqpsedcnYLALDNESDPTPFK 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 317 GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSL----ENQLG-NTQYGGWNgiykggkgmggweggIRVPG 391
Cdd:COG3083  427 NRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGhNSNFSRYQ---------------LQVPL 491
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157266309 392 IFRWPGVLPagRVIGEPTSLMDVFPTVV-RLAGGEVPqdrVID---GQDLL 438
Cdd:COG3083  492 VIHWPGTPP--QVISKLTSHLDIVPTLMqRLLGVQNP---ASDysqGEDLF 537
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
38-423 3.41e-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: 3.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  38 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSIGYRvl 113
Cdd:cd16015    1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 114 qwtgasgglPTNETTFAKILKEKGYATGLIgkwhlglncesasdHCHHP---------LHHGFDHFYgmpfslmgDCARW 184
Cdd:cd16015   77 ---------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFY--------DLEDF 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 185 ELSEKRVNleqklnflfqvlalvaltlvagklthlipvSWMpviwsalsavlllassyfvgalivhadcflmrnhtITEQ 264
Cdd:cd16015  126 PDDEKETN------------------------------GWG-----------------------------------VSDE 140
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 265 PMcfqrttpliLQEVASFLKRNKHGPFLLFVsflhvhiplITMENflgkslHGLYGDN---------------------- 322
Cdd:cd16015  141 SL---------FDQALEELEELKKKPFFIFL---------VTMSN------HGPYDLPeekkdeplkveedktelenyln 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 323 -VEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPa 401
Cdd:cd16015  197 aIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK- 261
                        410       420
                 ....*....|....*....|..
gi 157266309 402 GRVIGEPTSLMDVFPTVVRLAG 423
Cdd:cd16015  262 PKKIDRVGSQIDIAPTLLDLLG 283
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
19-193 1.67e-07

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 53.60  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  19 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGR 97
Cdd:COG1524    5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309  98 YPVRSGMVSSIGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIGKWHLGlncESASDHCHHPLHH-G 166
Cdd:COG1524   80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdG 156
                        170       180
                 ....*....|....*....|....*....
gi 157266309 167 FDHFYGMPFS--LMGDCARWELSEKRVNL 193
Cdd:COG1524  157 RKPLLGNPAAdrWIAAAALELLREGRPDL 185
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
62-106 3.94e-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: 39.71  E-value: 3.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 157266309   62 RTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVS 106
Cdd:pfam01663  19 LTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVG 64
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
321-355 9.53e-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: 9.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 157266309  321 DNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG 355
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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