NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564374894|ref|XP_006247666|]
View 

arylsulfatase G isoform X1 [Rattus norvegicus]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 10888435)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
35-469 0e+00

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: 615.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDmgctdnpgynyppcpacpqsdgrwrnpdr 193
Cdd:cd16161   81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQR-LYRAS 272
Cdd:cd16161  132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 273 LQEMDSLVGQIKDKVDHV-AKENTLLWFAGDNGPWAQKCELAGsmGPFSGLWQTHQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161  189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELAV--GPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 352 RVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGAAGeYGALQTVRLDRYKAF 431
Cdd:cd16161  267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 564374894 432 YITGGAKACDGGVGPEQHHVSPLIFNLEDDAAESSPLQ 469
Cdd:cd16161  346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
 
Name Accession Description Interval E-value
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
35-469 0e+00

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: 615.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDmgctdnpgynyppcpacpqsdgrwrnpdr 193
Cdd:cd16161   81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQR-LYRAS 272
Cdd:cd16161  132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 273 LQEMDSLVGQIKDKVDHV-AKENTLLWFAGDNGPWAQKCELAGsmGPFSGLWQTHQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161  189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELAV--GPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 352 RVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGAAGeYGALQTVRLDRYKAF 431
Cdd:cd16161  267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 564374894 432 YITGGAKACDGGVGPEQHHVSPLIFNLEDDAAESSPLQ 469
Cdd:cd16161  346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
25-474 5.49e-94

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 291.40  E-value: 5.49e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  25 FSISGETRAPRPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:COG3119   13 AAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 105 NFAvTSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyfgipYSNDmgctdnpgynyppcpacpqs 184
Cdd:COG3119   93 NGE-GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD-------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 185 dgrwrnpdrdcytdvalplyenlniveqpvnlsglaqKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANP- 263
Cdd:COG3119  132 -------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKy 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 264 ----------------------QSQRLYRASLQEMDSLVGQIkdkVDHVAK----ENTLLWFAGDNGPWaqkcelAGSMG 317
Cdd:COG3119  175 dgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRL---LDALEElglaDNTIVVFTSDNGPS------LGEHG 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 318 pFSGlwqthqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPnrKFDGVDVSEVLFG 397
Cdd:COG3119  246 -LRG----------GKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--DLDGRSLLPLLTG 312
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564374894 398 KSQTGHRVLFHpnsgAAGEYGALQTVRLDRYKAFYitggakaCDGGVGPEQhhvsplIFNLEDDAAESSPLQKGSPE 474
Cdd:COG3119  313 EKAEWRDYLYW----EYPRGGGNRAIRTGRWKLIR-------YYDDDGPWE------LYDLKNDPGETNNLAADYPE 372
Sulfatase pfam00884
Sulfatase;
36-378 8.16e-57

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 191.48  E-value: 8.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894   36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFG-IPYSNDMgctDNPGYNYPPCPACPQSDgrwrnpdrd 194
Cdd:pfam00884  77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLY---ADPPDVPYNCSGGGVSD--------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  195 cytdvalplyenlniveqpvnlsglaQKYAERAVEFIEQAStsgRPFLLYVGLAHMHVPLSVTPPLANP----------- 263
Cdd:pfam00884 145 --------------------------EALLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscse 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  264 -QSQRLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGPwaqkcelagSMGPFSGLWQTHQGGspakqTTWEGGH 341
Cdd:pfam00884 196 eQLLNSYDNTLLYTDDAIGRVLDKLEENGLlDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGY 261
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 564374894  342 RVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
35-492 1.27e-36

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 141.73  E-value: 1.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGwGD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGVTHNF 106
Cdd:PRK13759   6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVVPWNY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 107 avtsvgglplnETTLAEVLQQAGYVTAMIGKWHlghhgsYHP--SFRGFDYYF---GIPYSndmgctdnpGYNYPPCPAC 181
Cdd:PRK13759  85 -----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVLlhdGYLHS---------GRNEDKSQFD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 182 PQSDGR-W-------RNPDR-----DCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLLYVG 246
Cdd:PRK13759 139 FVSDYLaWlrekapgKDPDLtdigwDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFLKMS 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 247 LAHMHVPLSvtPP-----------------------------LANPQ-------------SQRLYRASLQEMDSLVGQI- 283
Cdd:PRK13759 208 FARPHSPYD--PPkryfdmykdadipdphigdweyaedqdpeGGSIDalrgnlgeeyarrARAAYYGLITHIDHQIGRFl 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 284 ---KDKVDHvakENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQthqggspaKQTTWEGGHRVPALAYWPG---RVPVNV 357
Cdd:PRK13759 286 qalKEFGLL---DNTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGT 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 358 TSTALLSLLDIFPTVIALAGASLPPNrkFDGVDVSEVLFGKsQTGHRVLFHpnsgaaGE----YGALQTVRLDRYKafYI 433
Cdd:PRK13759 345 VIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ-YEGWRPYLH------GEhalgYSSDNYLTDGKWK--YI 413
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564374894 434 TGgakacdGGVGPEQhhvsplIFNLEDDAAESSPLQkGSPEYQELLPKVTRVLADVLQD 492
Cdd:PRK13759 414 WF------SQTGEEQ------LFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
 
Name Accession Description Interval E-value
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
35-469 0e+00

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: 615.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDmgctdnpgynyppcpacpqsdgrwrnpdr 193
Cdd:cd16161   81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQR-LYRAS 272
Cdd:cd16161  132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 273 LQEMDSLVGQIKDKVDHV-AKENTLLWFAGDNGPWAQKCELAGsmGPFSGLWQTHQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161  189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELAV--GPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 352 RVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGAAGeYGALQTVRLDRYKAF 431
Cdd:cd16161  267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 564374894 432 YITGGAKACDGGVGPEQHHVSPLIFNLEDDAAESSPLQ 469
Cdd:cd16161  346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
35-468 5.16e-178

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: 506.33  E-value: 5.16e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16026    1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDMGCTDNPGYNYPPCPAcpqsdgrwrnpdr 193
Cdd:cd16026   81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 194 dcytdvalPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQAstSGRPFLLYVGLAHMHVPLSVTPPLANPqSQR-LYRAS 272
Cdd:cd16026  148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGR-SGAgLYGDV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 273 LQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGPWAQKCELAGSMGPFSGlwqthqggspAKQTTWEGGHRVPALAYWP 350
Cdd:cd16026  217 VEELDWSVGRILDALKelGLE-ENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 351 GRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGaageyGALQTVRLDRYKA 430
Cdd:cd16026  286 GVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDG-----GDLQAVRSGRWKL 360
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 564374894 431 FYITGGAKACDGGVGPEQHHVSPLIFNLEDDAAESSPL 468
Cdd:cd16026  361 HLPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
36-522 1.70e-118

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: 357.53  E-value: 1.70e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGGL 114
Cdd:cd16158    2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 115 PLNETTLAEVLQQAGYVTAMIGKWHL--GHHGSYHPSFRGFDYYFGIPYSNDMGctdnPGYNYPPCPacpqsdgrwrnPD 192
Cdd:cd16158   82 PLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQG----PCQNLTCFP-----------PN 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 193 RDCY-----TDVALPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQR 267
Cdd:cd16158  147 IPCFggcdqGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 268 LYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWAQKCELAGSmgpfSGLWQTHQGgspakqTTWEGGHRVPAL 346
Cdd:cd16158  227 PFGDALAELDGSVGELLQTLKENGiDNNTLVFFTSDNGPSTMRKSRGGN----AGLLKCGKG------TTYEGGVREPAI 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 347 AYWPGRVPVNVTStALLSLLDIFPTVIALAGASLpPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGAAGEYGALqTVRLD 426
Cdd:cd16158  297 AYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPL-PNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWG 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 427 RYKAFYITGGA--------KACDgGVGPEQHHVSPLIFNLEDDAAESSPLQKGsPEYQELLPKVTRVLADVLQDIAdDNS 498
Cdd:cd16158  374 KYKAHFYTQGAahsgttpdKDCH-PSAELTSHDPPLLFDLSQDPSENYNLLGL-PEYNQVLKQIQQVKERFEASMK-FGE 450
                        490       500
                 ....*....|....*....|....*...
gi 564374894 499 SQADYTQDPSVTPCCN----PYQITCRC 522
Cdd:cd16158  451 SEINKGEDPALEPCCKpgctPKPSCCQC 478
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
35-487 8.85e-114

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: 344.41  E-value: 8.85e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---THNFAVTSV 111
Cdd:cd16160    1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 112 GGLPLNETTLAEVLQQAGYVTAMIGKWHLG-----HHGSYH-PSFRGFDYY-FGIPYSNDMGCtDNPGYNYPpcpacpqs 184
Cdd:cd16160   81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWAC-DDTGRHVD-------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 185 dgrwrNPDRD-CYtdvalpLYENLNIVEQPVNLSGLAQKYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPLSVTPPLANp 263
Cdd:cd16160  152 -----FPDRSaCF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKG- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 264 QSQR-LYRASLQEMDSLVGQIKDK-VDHVAKENTLLWFAGDNGPWAQKCELAGSMGPFSGlwqthqggspAKQTTWEGGH 341
Cdd:cd16160  218 KSKRgRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGI 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 342 RVPALAYWPGRVPVNVtSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHR-VLFHPNSgaageygAL 420
Cdd:cd16160  288 RVPFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDdILYYCCS-------RL 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 421 QTVRLDRYKAFYITG--------GAKACDGGVGPE------------QHHVSPLIFNLEDDAAESSPLQkgSPEYQELLP 480
Cdd:cd16160  360 MAVRYGSYKIHFKTQplpsqeslDPNCDGGGPLSDyivcydcedecvTKHNPPLIFDVEKDPGEQYPLQ--PSVYEHMLE 437

                 ....*..
gi 564374894 481 KVTRVLA 487
Cdd:cd16160  438 AVEKLIA 444
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
35-488 1.62e-106

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: 326.35  E-value: 1.62e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTHNFAVTS-- 110
Cdd:cd16157    1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 111 ----VGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNdMGCTDNPgyNYPPCPACPQSD- 185
Cdd:cd16157   81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNK--AYPNIPVYRDWEm 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 186 -GRWrnpdrdcytdvalplYENLNIvEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQ 264
Cdd:cd16157  158 iGRY---------------YEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 265 SQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNG-PWAQKCELAGSMGPFSGlwqthqggspAKQTTWEGGHR 342
Cdd:cd16157  222 QRGLYGDAVMELDSSVGKILESLKSLGiENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMR 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 343 VPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSgaageygALQT 422
Cdd:cd16157  292 EPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMA 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 423 VRLDRYKAFYIT---------GGAKACDG----GVGP---EQHHVSPLIFNLEDDAAESSPLQKGSPEYQELLPKVTRVL 486
Cdd:cd16157  365 VRLGQYKAHFWTwsnsweefrKGINFCPGqnvpGVTThnqTDHTKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVV 444

                 ..
gi 564374894 487 AD 488
Cdd:cd16157  445 QQ 446
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
35-494 3.45e-106

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: 327.32  E-value: 3.45e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN------FAV 108
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 109 TSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHH------GSYHPSFRGFDYYFGIPYSN--DMGCTDNPGYNYPPCPA 180
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNlkDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 181 CPQSDG------------------RWR----------------------NPDRDCYtdvalpLYENLNIVEQPVNLSGLA 220
Cdd:cd16159  161 FPLLTAfvlitaltiflllylgavSKRffvfllilsllfislfflllitNRYFNCI------LMRNHEVVEQPMSLENLT 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 221 QKYAERAVEFIEQasTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWF 299
Cdd:cd16159  235 QRLTKEAISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYF 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 300 AGDNGPWAQKCELAGSMGpfsGLWQTHQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGAS 379
Cdd:cd16159  313 TSDNGGHLEEISVGGEYG---GGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAP 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 380 LPPNRKFDGVDVSEVLFGKSQ-TGHRVLFH------------PNSGAAgeygalqtvrldRYKAFYIT-----GGAKACD 441
Cdd:cd16159  388 LPSDRIIDGRDLMPLLTGQEKrSPHEFLFHycgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEGCCG 455
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564374894 442 GGVGP-----EQHHVSPLIFNLEDDAAESSPLQKGSPEYQELLPKVTRVLADVLQDIA 494
Cdd:cd16159  456 TLLCRcfgdsVTHHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIE 513
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
36-468 8.89e-95

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


Pssm-ID: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 292.90  E-value: 8.89e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGAN---WAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHNFAVTSVG 112
Cdd:cd16142    1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 113 GLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDmgctdnpgynyppcpacpqsDGRWrnpd 192
Cdd:cd16142   80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHTI--------------------DEEI---- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 193 rdcytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQS-QRLYRA 271
Cdd:cd16142  136 -------------------------------VDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYAD 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 272 SLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWaQKCELAGSMGPFSGlwqthqggspAKQTTWEGGHRVPALAYWP 350
Cdd:cd16142  185 SMVELDDHVGQILDALDELGiADNTIVIFTTDNGPE-QDVWPDGGYTPFRG----------EKGTTWEGGVRVPAIVRWP 253
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 351 GRVPVNVTSTALLSLLDIFPTVIALAGASLPP------NRKFDGVDVSEVLFGKS-QTGHRVLFHpnsGAAGEYGAlqtV 423
Cdd:cd16142  254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPKdkllgkDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 564374894 424 RLDRYKAFYITGGAKACDGGVGPEQHHVsPLIFNLEDDAAESSPL 468
Cdd:cd16142  328 RWKNWKVHFKAQEDTGGPTGEPFYVLTF-PLIFNLRRDPKERYDV 371
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
25-474 5.49e-94

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 291.40  E-value: 5.49e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  25 FSISGETRAPRPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:COG3119   13 AAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 105 NFAvTSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyfgipYSNDmgctdnpgynyppcpacpqs 184
Cdd:COG3119   93 NGE-GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD-------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 185 dgrwrnpdrdcytdvalplyenlniveqpvnlsglaqKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANP- 263
Cdd:COG3119  132 -------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKy 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 264 ----------------------QSQRLYRASLQEMDSLVGQIkdkVDHVAK----ENTLLWFAGDNGPWaqkcelAGSMG 317
Cdd:COG3119  175 dgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRL---LDALEElglaDNTIVVFTSDNGPS------LGEHG 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 318 pFSGlwqthqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPnrKFDGVDVSEVLFG 397
Cdd:COG3119  246 -LRG----------GKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--DLDGRSLLPLLTG 312
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564374894 398 KSQTGHRVLFHpnsgAAGEYGALQTVRLDRYKAFYitggakaCDGGVGPEQhhvsplIFNLEDDAAESSPLQKGSPE 474
Cdd:COG3119  313 EKAEWRDYLYW----EYPRGGGNRAIRTGRWKLIR-------YYDDDGPWE------LYDLKNDPGETNNLAADYPE 372
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
36-474 8.24e-92

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: 286.75  E-value: 8.24e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--------- 106
Cdd:cd16144    1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 107 ----AVTSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGipysndMGCTDNPGYNYPPCPACP 182
Cdd:cd16144   81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG------GTGNGGPPSYYFPPGKPN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 183 qsdGRWRNPDRDCYtdvalplyenlniveqpvnlsgLAQKYAERAVEFIEQAstSGRPFLLYvgLAH--MHVPLSVTP-- 258
Cdd:cd16144  155 ---PDLEDGPEGEY----------------------LTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPel 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 259 ---------PLANPQSQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWAQKCELAGSMGPFSGlwqthqg 328
Cdd:cd16144  206 iekyekkkkGLRKGQKNPVYAAMIESLDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPLRG------- 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 329 gspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHR--VL 406
Cdd:cd16144  279 ---GKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraLF 355
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564374894 407 FH-PN-SGAAGEYGAlqTVRLDRYK--AFYITGgakacdggvgpeqhhvSPLIFNLEDDAAESSPLQKGSPE 474
Cdd:cd16144  356 WHfPHyHGQGGRPAS--AIRKGDWKliEFYEDG----------------RVELYNLKNDIGETNNLAAEMPE 409
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
36-465 1.34e-86

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: 272.54  E-value: 1.34e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETK-DTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGL 114
Cdd:cd16143    1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGG--VLGGFSP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 115 PL---NETTLAEVLQQAGYVTAMIGKWHLG-----------HHGSYH-----------PSFRGFDYYFGIPYSNdmgctd 169
Cdd:cd16143   79 PLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPASE------ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 170 npgynyppcpacpqsdgrwrnpdrdcytdvALPLyenlniveqpvnlsgLAQKyaerAVEFIEQASTSGRPFLLYVGLAH 249
Cdd:cd16143  153 ------------------------------VLPT---------------LTDK----AVEFIDQHAKKDKPFFLYFALPA 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 250 MHVPLSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGP----WAQKCELAG--SMGPFSG 321
Cdd:cd16143  184 PHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKelGLA-ENTLVIFTSDNGPspyaDYKELEKFGhdPSGPLRG 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 322 LwqthqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQT 401
Cdd:cd16143  263 M----------KADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQ 332
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564374894 402 GHRVLFHPNSGAAGeygalQTVRLDRYKAFYITGGAKACDGGVGPEQHHVSPLIFNLEDDAAES 465
Cdd:cd16143  333 EVRESLVHHSGNGS-----FAIRKGDWKLIDGTGSGGFSYPRGKEKLGLPPGQLYNLSTDPGES 391
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
36-465 7.10e-83

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: 263.69  E-value: 7.10e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLP 115
Cdd:cd16145    1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSY-HPSFRGFDYYFGipYSNDMGCTdnpGYnYPPCpacpqsdgRWRNPDRd 194
Cdd:cd16145   81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYG--YLDQVHAH---NY-YPEY--------LWRNGEK- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 195 cytdvaLPLYENLNIVEQPVNLSGLAQK-YAE-----RAVEFIEQAstSGRPFLLYVGL----AHMHVP----------- 253
Cdd:cd16145  146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYtlphAPLQVPddgpykykpkd 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 254 LSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKV-DHVAKENTLLWFAGDNGP-----WAQKCELAGSMGPFSGLwqthq 327
Cdd:cd16145  218 PGIYAYLPWPQPEKAYAAMVTRLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 328 ggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASlPPNRKfDGVDVSEVLFGKS-QTGHRVL 406
Cdd:cd16145  293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAE-PPEDI-DGISLLPTLLGKPqQQQHDYL 365
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564374894 407 FHpnsgAAGEYGALQTVRLDRYKAFYITGGAKacdggvgpeqhhvSPLIFNLEDDAAES 465
Cdd:cd16145  366 YW----EFYEGGGAQAVRMGGWKAVRHGKKDG-------------PFELYDLSTDPGET 407
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
36-478 7.57e-82

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: 260.56  E-value: 7.57e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTHnfavTSVGG-- 113
Cdd:cd16146    1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPysndmgctdnpgynyppcpacpqsDGRWRNPDR 193
Cdd:cd16146   76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHG------------------------GGGIGQYPD 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 194 DCYTDVALPLYENLNIVEQpvnlsglAQKYA-----ERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLANP----- 263
Cdd:cd16146  132 YWGNDYFDDTYYHNGKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPykdmg 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 264 --QSQRLYRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGPWaqkcelagsmGPFSGLWQTHQGGSpaKQTTWEG 339
Cdd:cd16146  203 ldDKLAAFYGMIENIDDNVGRLLAKLKelGLE-ENTIVIFMSDNGPA----------GGVPKRFNAGMRGK--KGSVYEG 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 340 GHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQ-TGHRVLF--HPNSGAAGE 416
Cdd:cd16146  270 GHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDpWPERTLFthSGRWPPPPK 349
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564374894 417 YGALQTVRLDRYKAfyitggakacdggVGPeqHHVSPLIFNLEDDAAESSPLQKGSPE-YQEL 478
Cdd:cd16146  350 KKRNAAVRTGRWRL-------------VSP--KGFQPELYDIENDPGEENDVADEHPEvVKRL 397
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
36-390 1.25e-73

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: 233.48  E-value: 1.25e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGLP 115
Cdd:cd16022    1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 116 LNETTLAEVLQQAGYVTAMIGKWHlghhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrwrnpdrdc 195
Cdd:cd16022   79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 196 ytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSgRPFLLYVGLAHMHvplsvtPPLAnpqsqrlYRASLQE 275
Cdd:cd16022  103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPH------PPFA-------YYAMVSA 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 276 MDSLVGQIkdkVDHVAK----ENTLLWFAGDNGpwaqkcelaGSMGPFSGLWQthqggspaKQTTWEGGHRVPALAYWPG 351
Cdd:cd16022  140 IDDQIGRI---LDALEElgllDNTLIVFTSDHG---------DMLGDHGLRGK--------KGSLYEGGIRVPFIVRWPG 199
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 564374894 352 RVPVNVTSTALLSLLDIFPTVIALAGASLPpnRKFDGVD 390
Cdd:cd16022  200 KIPAGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
36-468 2.52e-71

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: 232.83  E-value: 2.52e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSV-GGL 114
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYH-PSFRGFDYYFGiPYSndmGCTDNpgYNYPPCPACPQSDGRWR---- 189
Cdd:cd16029   80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAEDY--YTHTSGGANDYGNDDLRdnee 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 190 --NPDRDCY-TDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSgRPFLLYVGLAHMHVPLSVTPPLANPQSQ 266
Cdd:cd16029  154 paWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYED 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 267 ----------RLYRASLQEMDSLVGQIKDKVDHV-AKENTLLWFAGDNGPWAQKCElAGSMGPFSGlwqthqggspAKQT 335
Cdd:cd16029  210 kfahikdedrRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNT 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 336 TWEGGHRVPALAYWPGRVPV-NVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHR-VLFHPNSGA 413
Cdd:cd16029  279 LWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDIT 358
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564374894 414 AGEYGAlqTVRLDRYKafYITGGakacdggvgpeqhhvsPLiFNLEDDAAESSPL 468
Cdd:cd16029  359 RTTGGA--AIRVGDWK--LIVGK----------------PL-FNIENDPCERNDL 392
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-468 1.60e-68

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: 224.79  E-value: 1.60e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHnfavtsvGGLP 115
Cdd:cd16151    1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 116 LNETTLAEVLQQAGYVTAMIGKWHLG--HHGSYHPSFRGFDYY--FGIPYsndmgcTDNPGynyppcpacpqsdGRWRNP 191
Cdd:cd16151   73 PKQKTFGHLLKDAGYATAIAGKWQLGggRGDGDYPHEFGFDEYclWQLTE------TGEKY-------------SRPATP 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 192 DRDCYTDVALPLYENlniveqpvnlsglaqKY-----AERAVEFIEQAStsGRPFLLYVGLAHMHVPLSVTP--PLANPQ 264
Cdd:cd16151  134 TFNIRNGKLLETTEG---------------DYgpdlfADFLIDFIERNK--DQPFFAYYPMVLVHDPFVPTPdsPDWDPD 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 265 SQRL------YRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGpwaqkcelagSMGPFSGLW--QTHQGGspaKQ 334
Cdd:cd16151  197 DKRKkddpeyFPDMVAYMDKLVGKLVDKLEelGLR-ENTIIIFTGDNG----------THRPITSRTngREVRGG---KG 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 335 TTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGAA 414
Cdd:cd16151  263 KTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNP 342
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564374894 415 GEYGALQTVRLDRYKaFYITGGakacdggvgpeqhhvsplIFNLEDDAAESSPL 468
Cdd:cd16151  343 HKKFGSRFVRTKRYK-LYADGR------------------FFDLREDPLEKNPL 377
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
35-465 4.04e-57

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: 195.74  E-value: 4.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETkDTTNLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGV-THNFAVTSVGG 113
Cdd:cd16025    2 RPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGMgTMAELATGKPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 114 ----LPLNETTLAEVLQQAGYVTAMIGKWHLGHHgsyhpsfrgfDYYFgipySNDmgctdnpgynyppcpacpqsdgrwr 189
Cdd:cd16025   80 yegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 190 npdrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYV--GLAH--MHVP------------ 253
Cdd:cd16025  121 ---------------------------------LTDKAIEYIDEQKAPDKPFFLYLafGAPHapLQAPkewidkykgkyd 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 254 -------------------------LSVTPPLA------NPQSQRLYrASLQE--------MDSLVGQIkdkVDHVAK-- 292
Cdd:cd16025  168 agwdalreerlerqkelglipadtkLTPRPPGVpawdslSPEEKKLE-ARRMEvyaamvehMDQQIGRL---IDYLKElg 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 293 --ENTLLWFAGDNGP-----WAQkcelAGSmGPFSGlwqthqggspAKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLS 364
Cdd:cd16025  244 elDNTLIIFLSDNGAsaepgWAN----ASN-TPFRL----------YKQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAH 308
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 365 LLDIFPTVIALAGASLP------PNRKFDGVDVSEVLFGKSQ-TGHRVLFHPNSGAAGeygalqtVRLDRYKAFYITGGa 437
Cdd:cd16025  309 VIDIAPTILELAGVEYPktvngvPQLPLDGVSLLPTLDGAAApSRRRTQYFELFGNRA-------IRKGGWKAVALHPP- 380
                        490       500
                 ....*....|....*....|....*...
gi 564374894 438 kacdGGVGPEQHhvsplIFNLEDDAAES 465
Cdd:cd16025  381 ----PGWGDQWE-----LYDLAKDPSET 399
Sulfatase pfam00884
Sulfatase;
36-378 8.16e-57

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 191.48  E-value: 8.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894   36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFG-IPYSNDMgctDNPGYNYPPCPACPQSDgrwrnpdrd 194
Cdd:pfam00884  77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLY---ADPPDVPYNCSGGGVSD--------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  195 cytdvalplyenlniveqpvnlsglaQKYAERAVEFIEQAStsgRPFLLYVGLAHMHVPLSVTPPLANP----------- 263
Cdd:pfam00884 145 --------------------------EALLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscse 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  264 -QSQRLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGPwaqkcelagSMGPFSGLWQTHQGGspakqTTWEGGH 341
Cdd:pfam00884 196 eQLLNSYDNTLLYTDDAIGRVLDKLEENGLlDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGY 261
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 564374894  342 RVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
36-433 1.61e-55

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: 190.41  E-value: 1.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGA--NWAETkdtTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFavTSVGG 113
Cdd:cd16027    1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 114 LPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyfgipysndmgctdNPGYNYPPCPACPQSDGRWRNPDR 193
Cdd:cd16027   76 LPDGVKTLPELLREAGYYTGLIGKTHY-----------------------------NPDAVFPFDDEMRGPDDGGRNAWD 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 194 dcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQAStSGRPFLLYVGLAHMHVP---LSVTPPLANPQSQRL-- 268
Cdd:cd16027  127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHRPyppGDGEEPGYDPEKVKVpp 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 269 --------------YRASLQEMDSLVGQIkdkVDHVAK----ENTLLWFAGDNGpwaqkcelagsmGPFSGlwqthqggs 330
Cdd:cd16027  177 ylpdtpevredladYYDEIERLDQQVGEI---LDELEEdgllDNTIVIFTSDHG------------MPFPR--------- 232
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 331 pAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNrkFDGVDVSEVLFGKSQTGHRVLFHPN 410
Cdd:cd16027  233 -AKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVFAER 309
                        410       420
                 ....*....|....*....|...
gi 564374894 411 SGAAGEYGALQTVRLDRYKafYI 433
Cdd:cd16027  310 DRHDETYDPIRSVRTGRYK--YI 330
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
35-469 4.52e-54

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: 187.39  E-value: 4.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggL 114
Cdd:cd16034    1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 115 PLNETTLAEVLQQAGYVTAMIGKWHL-GHHGSYHPSFR---------GFDYYFGipysndMGCTD---NPGYnyppcpac 181
Cdd:cd16034   76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRADDytppperrhGFDYWKG------YECNHdhnNPHY-------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 182 pqsdgrWRNPDRDCYTDVALPLYEnlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYvglahmhvpLSVTPP-- 259
Cdd:cd16034  142 ------YDDDGKRIYIKGYSPDAE------------------TDLAIEYLENQADKDKPFALV---------LSWNPPhd 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 260 ---LANPQSQRLYRASLQEM----------------------------DSLVGQIkdkVDHVAK----ENTLLWFAGDNG 304
Cdd:cd16034  189 pytTAPEEYLDMYDPKKLLLrpnvpedkkeeaglredlrgyyamitalDDNIGRL---LDALKElgllENTIVVFTSDHG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 305 pwaqkcELAGSmgpfsglwqtHqgGSPAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGasLPPNR 384
Cdd:cd16034  266 ------DMLGS----------H--GLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPD 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 385 KFDGVDVSEVLFGKSQTGHR----VLFHPNSG-AAGEYGALQTVRLDRYKafYitggakACDGGVGpeqhhvsPLIFNLE 459
Cdd:cd16034  326 TVEGRDLSPLLLGGKDDEPDsvllQCFVPFGGgSARDGGEWRGVRTDRYT--Y------VRDKNGP-------WLLFDNE 390
                        490
                 ....*....|
gi 564374894 460 DDaaessPLQ 469
Cdd:cd16034  391 KD-----PYQ 395
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
35-479 2.32e-48

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: 172.71  E-value: 2.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvGGL 114
Cdd:cd16031    2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PLF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGsyHPSFRGFDYYFGIPysndmgctdNPGYNYPPcpacpqsdgrwrnpdrd 194
Cdd:cd16031   78 DASQPTYPKLLRKAGYQTAFIGKWHLGSGG--DLPPPGFDYWVSFP---------GQGSYYDP----------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 195 cytdvalPLYENLNIVEQPVNLSGLaqkYAERAVEFIEQAStSGRPFLLYVGL-----------AHMHVPLSVT---PPL 260
Cdd:cd16031  130 -------EFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLSFkaphrpftpapRHRGLYEDVTipePET 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 261 ANPQS-----------------------------QRLYR---ASLQEMDSLVGQIKDKVDH--VAkENTLLWFAGDNGpw 306
Cdd:cd16031  199 FDDDDyagrpewareqrnrirgvldgrfdtpekyQRYMKdylRTVTGVDDNVGRILDYLEEqgLA-DNTIIIYTSDNG-- 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 307 aqkcELAGSMGPFSglwqthqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNrkF 386
Cdd:cd16031  276 ----FFLGEHGLFD------------KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--M 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 387 DGVDVSEVLFGKSQTGHR------VLFHPNS-GAAGEYGalqtVRLDRYKAFYITGGAKAcdggvgpEQhhvsplIFNLE 459
Cdd:cd16031  338 QGRSLLPLLEGEKPVDWRkefyyeYYEEPNFhNVPTHEG----VRTERYKYIYYYGVWDE-------EE------LYDLK 400
                        490       500
                 ....*....|....*....|....
gi 564374894 460 DDaaessPLQK----GSPEYQELL 479
Cdd:cd16031  401 KD-----PLELnnlaNDPEYAEVL 419
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-388 8.83e-44

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: 155.86  E-value: 8.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----THNFAVTS 110
Cdd:cd16149    1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 111 VG-GLPLNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrwr 189
Cdd:cd16149   81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 190 npdrdcytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSGRPFLLYVGLAHMHVPLSvtpplanpqsqrlY 269
Cdd:cd16149  113 -----------------------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------Y 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 270 RASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGpwaqkcelaGSMGpFSGLWQTHQGGSPakQTTWEGGHRVPALAY 348
Cdd:cd16149  145 FAAVTGVDRNVGRLLDELEELGlTENTLVIFTSDNG---------FNMG-HHGIWGKGNGTFP--LNMYDNSVKVPFIIR 212
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 564374894 349 WPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDG 388
Cdd:cd16149  213 WPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
35-388 9.35e-42

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: 154.25  E-value: 9.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWgDLGANWAETKdTTNLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtSVGGL 114
Cdd:cd16147    1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 115 P------LNETTLAEVLQQAGYVTAMIGK----WHLGHHGSYHPsfRGFDYYFGI--PYSNDMGCTDNPGYNYPPcpacp 182
Cdd:cd16147   75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgNSTYYNYTLSNGGNGKHG----- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 183 qsdgrwRNPDRDCYTDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVG-------------LAH 249
Cdd:cd16147  148 ------VSYPGDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftpaprYAN 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 250 MHVPLSVTPPLANP-----------------------QSQRLYRA---SLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGD 302
Cdd:cd16147  199 LFPNVTAPPRPPPNnpdvsdkphwlrrlpplnptqiaYIDELYRKrlrTLQSVDDLVERLVNTLEATGQlDNTYIIYTSD 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 303 NGPWaqkcelagsMGPFsGLWqthqggsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSLLDIFPTVIALAGASLPP 382
Cdd:cd16147  279 NGYH---------LGQH-RLP-------PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPS 340

                 ....*.
gi 564374894 383 NrkFDG 388
Cdd:cd16147  341 D--MDG 344
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
35-479 4.20e-41

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 151.56  E-value: 4.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRlglrngvtHNFAVTS 110
Cdd:cd16155    2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR--------TLFHAPE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 111 VGG--LPLNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrw 188
Cdd:cd16155   74 GGKaaIPSDDKTWPETFKKAGYRTFATGKWHNG----------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 189 rnpdrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPL-------- 260
Cdd:cd16155  107 ----------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYldmyppet 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 261 ----ANPQSQ-----------------------------RLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpw 306
Cdd:cd16155  153 iplpENFLPQhpfdngegtvrdeqlapfprtpeavrqhlAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG-- 230
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 307 aqkceLA----GSMGpfsglwqthqggspaKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSLLDIFPTVIALAGASLPP 382
Cdd:cd16155  231 -----LAvgshGLMG---------------KQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE 289
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 383 nrKFDGVDVSEVLFGKSQTGHRVLFhpnsgaaGEYGALQ-TVRLDRYKAFYITGGAKAcdggvgpeqhhvsPLIFNLEDD 461
Cdd:cd16155  290 --SVEGKSLLPVIRGEKKAVRDTLY-------GAYRDGQrAIRDDRWKLIIYVPGVKR-------------TQLFDLKKD 347
                        490
                 ....*....|....*...
gi 564374894 462 AAESSPLQkGSPEYQELL 479
Cdd:cd16155  348 PDELNNLA-DEPEYQERL 364
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-436 5.31e-40

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: 148.65  E-value: 5.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWgDLGANWAETKD---TTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVThnfavtSVG 112
Cdd:cd16154    1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 113 G-LPLNETTL--AEVLQQ--AGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNdmgctdnpgynyppcpacPQSDGR 187
Cdd:cd16154   73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILGGG------------------VQDYYN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 188 WrnpdrdcytdvalplyeNLNIVEQPVNLSGLA-QKYAERAVEFIEQASTsgrPFLLYVGLAHMHVPLSVtPP------- 259
Cdd:cd16154  135 W-----------------NLTNNGQTTNSTEYAtTKLTNLAIDWIDQQTK---PWFLWLAYNAPHTPFHL-PPaelhsrs 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 260 --------LANPQSqrLYRASLQEMDSLVGQIKDKVDHVAKENTLLWFAGDNG-PwaqkcelagsmGPFSGLWQTHQGgs 330
Cdd:cd16154  194 llgdsadiEANPRP--YYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYTRNH-- 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 331 pAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPpnRKFDGVDVSEVLFGKSQTGHRVLFHPN 410
Cdd:cd16154  259 -AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAA--EIHDSVSFKPLLSDVNASTRQYNYTEY 335
                        410       420
                 ....*....|....*....|....*.
gi 564374894 411 SGAAgeyGALQTVRLDRYKAFYITGG 436
Cdd:cd16154  336 ESPT---TTGWATRNQYYKLIESENG 358
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-432 6.40e-40

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: 149.29  E-value: 6.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--AVTSVGG 113
Cdd:cd16033    1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSyhPSFRGFDYYFGIpysndmgctdnpgynyppcpacpqsdgrwrNPDR 193
Cdd:cd16033   81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYLPV------------------------------ETTI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 194 DCYTdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGL-------------AHMHVPLSVTPP- 259
Cdd:cd16033  129 EYFL--------------------------ADRAIEMLEELAADDKPFFLRVNFwgphdpyippepyLDMYDPEDIPLPe 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 260 -----LAN-PQSQRLYRASLQ---------------------EMDSLVGQIKDKVDHV-AKENTLLWFAGDNGpwaqkcE 311
Cdd:cd16033  183 sfaddFEDkPYIYRRERKRWGvdtedeedwkeiiahywgyitLIDDAIGRILDALEELgLADDTLVIFTSDHG------D 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 312 LAGSmgpfSGLWQthQGGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGAslPPNRKFDGVDV 391
Cdd:cd16033  257 ALGA----HRLWD--KGPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGV--DVPPKVDGRSL 323
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 564374894 392 SEVLFGKSQTGHR--VL--FHPNsgaaGEYGALQTVRLDRYKAFY 432
Cdd:cd16033  324 LPLLRGEQPEDWRdeVVteYNGH----EFYLPQRMVRTDRYKYVF 364
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-461 2.75e-38

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: 142.68  E-value: 2.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggLP 115
Cdd:cd16037    1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHpsfrGFDYyfgipysndmgctdnpgynyppcpacpqsdgrwrnpDRDC 195
Cdd:cd16037   76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY------------------------------------DRDV 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 196 ytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAnpqsqRLYR----- 270
Cdd:cd16037  116 ----------------------------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFY-----DLYVrrara 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 271 ---ASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQthqggspaKQTTWEGGHRVPAL 346
Cdd:cd16037  163 ayyGLVEFLDENIGRVLDALEELGLlDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMI 224
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 347 AYWPGRVPVNVTSTALlSLLDIFPTVIALAGASLPPNRkfDGVDVSEVLFGKSQTGHRVL--FHpnsgAAGEYGALQTVR 424
Cdd:cd16037  225 ISGPGIPAGKRVKTPV-SLVDLAPTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVFseYH----AHGSPSGAFMLR 297
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 564374894 425 LDRYKafYItggakacdggvgpeqHHVS--PLIFNLEDD 461
Cdd:cd16037  298 KGRWK--YI---------------YYVGypPQLFDLEND 319
PRK13759 PRK13759
arylsulfatase; Provisional
35-492 1.27e-36

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 141.73  E-value: 1.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGwGD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGVTHNF 106
Cdd:PRK13759   6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVVPWNY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 107 avtsvgglplnETTLAEVLQQAGYVTAMIGKWHlghhgsYHP--SFRGFDYYF---GIPYSndmgctdnpGYNYPPCPAC 181
Cdd:PRK13759  85 -----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVLlhdGYLHS---------GRNEDKSQFD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 182 PQSDGR-W-------RNPDR-----DCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLLYVG 246
Cdd:PRK13759 139 FVSDYLaWlrekapgKDPDLtdigwDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFLKMS 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 247 LAHMHVPLSvtPP-----------------------------LANPQ-------------SQRLYRASLQEMDSLVGQI- 283
Cdd:PRK13759 208 FARPHSPYD--PPkryfdmykdadipdphigdweyaedqdpeGGSIDalrgnlgeeyarrARAAYYGLITHIDHQIGRFl 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 284 ---KDKVDHvakENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQthqggspaKQTTWEGGHRVPALAYWPG---RVPVNV 357
Cdd:PRK13759 286 qalKEFGLL---DNTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGT 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 358 TSTALLSLLDIFPTVIALAGASLPPNrkFDGVDVSEVLFGKsQTGHRVLFHpnsgaaGE----YGALQTVRLDRYKafYI 433
Cdd:PRK13759 345 VIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ-YEGWRPYLH------GEhalgYSSDNYLTDGKWK--YI 413
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564374894 434 TGgakacdGGVGPEQhhvsplIFNLEDDAAESSPLQkGSPEYQELLPKVTRVLADVLQD 492
Cdd:PRK13759 414 WF------SQTGEEQ------LFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
35-428 1.40e-33

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: 132.31  E-value: 1.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDM----GWgdLGANWAETKdttNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtHNFAVTS 110
Cdd:cd16030    2 KPNVLFIAVDDLrpwlGC--YGGHPAKTP---NIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV-YDNNSYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 111 VGGLPlNETTLAEVLQQAGYVTAMIGK-WHlGHHGSYHPSFRGFDYYFGIP--------YSNDMGCTDNPGYNYPPCPAC 181
Cdd:cd16030   76 RKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPPgpekyppgKLCPGKKGGKGGGGGPAWEAA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 182 PQSDGRwrnpdrdcYTDvalplyenlniveqpvnlsglaQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSV----- 256
Cdd:cd16030  154 DVPDEA--------YPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVApkkyf 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 257 --------------------------------------------TPPLANPQSQRL---YRASLQEMDSLVGQIKDKVD- 288
Cdd:cd16030  204 dlyplesiplpnpfdpidlpevawndlddlpkygdipalnpgdpKGPLPDEQARELrqaYYASVSYVDAQVGRVLDALEe 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 289 HVAKENTLLWFAGDNGpwaqkcelagsmgpFS----GLWqthqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLS 364
Cdd:cd16030  284 LGLADNTIVVLWSDHG--------------WHlgehGHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVE 341
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564374894 365 LLDIFPTVIALAGasLPPNRKFDGVDVSEVLFGKSQTGHRVLF--HPNSGAAGEygalqTVRLDRY 428
Cdd:cd16030  342 LVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKDAAFsqYPRPSIMGY-----SIRTERY 400
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-390 1.57e-33

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 128.05  E-value: 1.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILAD----DMgwgdLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHnfavtsv 111
Cdd:cd16148    1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 112 GGLPLNETTLAEVLQQAGYVTAMIGKWhlGHHGSYHPSFRGFDYYFGIPYsndmgctdnpgynyppcpacpQSDGRWRNP 191
Cdd:cd16148   70 GPLEPDDPTLAEILRKAGYYTAAVSSN--PHLFGGPGFDRGFDTFEDFRG---------------------QEGDPGEEG 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 192 DRDcytdvalplyenlniveqpvnlsglAQKYAERAVEFIEQASTSgRPFLLYVglaHM---HVPLsvtpplanpqsqrL 268
Cdd:cd16148  127 DER-------------------------AERVTDRALEWLDRNADD-DPFFLFL---HYfdpHEPY-------------L 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 269 YRASLQEMDSLVGQIKDKVD-HVAKENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQTHQggspakQTTWEGGHRVPALA 347
Cdd:cd16148  165 YDAEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EEFGE----HGLYWGHG------SNLYDEQLHVPLII 228
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 564374894 348 YWPGRVPVNVTStALLSLLDIFPTVIALAGasLPPNRKFDGVD 390
Cdd:cd16148  229 RWPGKEPGKRVD-ALVSHIDIAPTLLDLLG--VEPPDYSDGRS 268
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
402-522 4.34e-32

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 119.34  E-value: 4.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  402 GHRVLFHpNSGAAgeygaLQTVRLDRYKAFYITG-----GAKACDGGVGPEQHHVSPLIFNLEDDAAESSPLQKGSPEYQ 476
Cdd:pfam14707   2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 564374894  477 ELLPKVTRVLADVLQDI--ADDNSSQADYTQDPSVTPCCnPYQITCRC 522
Cdd:pfam14707  76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-408 1.63e-29

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


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 118.08  E-value: 1.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDM-GWGDLGANWAETKdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGL 114
Cdd:cd16035    1 PNILLILTDQErYPPPWPAGWAALN-LPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGsyhpsfrgfdyyfgipysndmgctdNPGYNYppcpacpqsDGRwrnpdrd 194
Cdd:cd16035   80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA-------------------------GGGYKR---------DPG------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 195 cytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTS---GRPFLLYVGLAHMH-VplsVTPPLANPQSQRL-- 268
Cdd:cd16035  119 ----------------------------IAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdI---MFPPDDEERWRRFrn 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 269 -YRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGpwaqkcELAGSMGpfsGLwqtHQGGSPAKQTTwegghRVPAL 346
Cdd:cd16035  168 fYYNLIRDVDRQIGRVLDALDASGlADNTIVVFTSDHG------EMGGAHG---LR---GKGFNAYEEAL-----HVPLI 230
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564374894 347 AYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRK----FDGVDVSEVLFGKSQTGHR--VLFH 408
Cdd:cd16035  231 ISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATeappLPGRDLSPLLTDADADAVRdgILFT 298
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
36-461 2.71e-29

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: 117.68  E-value: 2.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16032    1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 116 LNETTLAEVLQQAGYVTAMIGKWHL-G---HHGsyhpsfrgFDYyfgipysndmgctDNpgynyppcpacpqsdgrwrnp 191
Cdd:cd16032   76 ADIPTFAHYLRAAGYRTALSGKMHFvGpdqLHG--------FDY-------------DE--------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 192 drdcytDVALplyenlniveqpvnlsglaqkyaeRAVEFIEQASTS--GRPFLLYVGLAHMHVPLSVTPPLAN---PQSQ 266
Cdd:cd16032  114 ------EVAF------------------------KAVQKLYDLARGedGRPFFLTVSFTHPHDPYVIPQEYWDlyvRRAR 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 267 RLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQthqggspaKQTTWEGGHRVPA 345
Cdd:cd16032  164 RAYYGMVSYVDDKVGQLLDTLERTGLaDDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSARVPL 225
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 346 LAYWPGR-VPVNVTstALLSLLDIFPTVIALAGASLPPNR-KFDGVDVSEVLFGKSQTGHRVLFhpnsgaaGEYGA---- 419
Cdd:cd16032  226 IISAPGRfAPRRVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVI-------SEYLAegav 296
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 564374894 420 --LQTVRLDRYKAFYITGgakacDGgvgpeqhhvsPLIFNLEDD 461
Cdd:cd16032  297 apCVMIRRGRWKFIYCPG-----DP----------DQLFDLEAD 325
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
35-393 3.38e-29

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


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 116.32  E-value: 3.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGA-NWAETKD---------TTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:cd16153    1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTAMIGKWHLGHHGSYhpsfrgfdyyfgipysndmgcTDNPGYNYppcpacpqs 184
Cdd:cd16153   81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHLEAFQRY---------------------LKNANQSY--------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 185 dgrwrnpdrdcytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSGRPFLLYVGLAHMHVPlsVTPPlaNPQ 264
Cdd:cd16153  129 ----------------------------------------KSFWGKIAKGADSDKPFFVRLSFLQPHTP--VLPP--KEF 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 265 SQRL-YRASLQEMDSLVGQIKDKVD----HVAKENTLLWFAGDNGpwaqkcelagsmgpfsglWQTHQGGSPAKQTTWEG 339
Cdd:cd16153  165 RDRFdYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQ 226
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564374894 340 GHRVPALAYWPGR--VPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSE 393
Cdd:cd16153  227 SHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
36-376 1.96e-25

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: 104.81  E-value: 1.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTHNFAVT----- 109
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 110 SVGGLPLNETTLAEVLQQAGYVTAMIGkwhlghhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrwr 189
Cdd:cd00016   81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 190 npdrdcytdvalplyenlniveqpvnlsglaqkyaerAVEFIEQaSTSGRPFLLYVGLAHMHVPLsvTPPLANPQSqrlY 269
Cdd:cd00016  108 -------------------------------------LLKAIDE-TSKEKPFVLFLHFDGPDGPG--HAYGPNTPE---Y 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 270 RASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpwaqkcelagsmGPFSGLwqTHQGGSPAKQTTWEGGHRVPALAY 348
Cdd:cd00016  145 YDAVEEIDERIGKVLDALKKAGDaDDTVIIVTADHG------------GIDKGH--GGDPKADGKADKSHTGMRVPFIAY 210
                        330       340       350
                 ....*....|....*....|....*....|..
gi 564374894 349 WPG----RVPVNVTSTAllsllDIFPTVIALA 376
Cdd:cd00016  211 GPGvkkgGVKHELISQY-----DIAPTLADLL 237
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
36-429 6.12e-24

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: 104.77  E-value: 6.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG-VTHNFAVTSvggl 114
Cdd:cd16156    1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGsWTNCMALGD---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 115 plNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrGFDYY-FGIpysndmgCTD--NPGYNYppcpacpqsDGR---- 187
Cdd:cd16156   77 --NVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGI-------CPQgwDPDYWY---------DMRnyld 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 188 ---------WRNPdrdcytdvaLPLYENLNIVEQPVnlsgLAQKYAERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTP 258
Cdd:cd16156  129 elteeerrkSRRG---------LTSLEAEGIKEEFT----YGHRCTNRALDFIEKHKD--EDFFLVVSYDEPHHPFLCPK 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 259 PLAN--------------------PQSQRL-------------------YRASLQEMDSLVGQIKDKVDHVAkENTLLWF 299
Cdd:cd16156  194 PYASmykdfefpkgenayddlenkPLHQRLwagakphedgdkgtikhplYFGCNSFVDYEIGRVLDAADEIA-EDAWVIY 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 300 AGDNGpwaqkcELAGSmgpfSGLWqthqGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGAS 379
Cdd:cd16156  273 TSDHG------DMLGA----HKLW----AKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIP 335
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564374894 380 LPPnrKFDGVDVSEVLFGKSQTGHRVLF---------HPNsgaageYGALQTVRL---DRYK 429
Cdd:cd16156  336 QPK--VLEGESILATIEDPEIPENRGVFvefgryevdHDG------FGGFQPVRCvvdGRYK 389
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
35-140 2.46e-21

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: 95.76  E-value: 2.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtsVGGL 114
Cdd:cd16152    1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
                         90       100
                 ....*....|....*....|....*.
gi 564374894 115 PLNETTLAEVLQQAGYVTAMIGKWHL 140
Cdd:cd16152   76 PADEKTLAHYFRDAGYETGYVGKWHL 101
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-399 4.13e-20

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 92.68  E-value: 4.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRNgvTHNFavtsv 111
Cdd:cd16150    1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHRT--LHHL----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 112 ggLPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyFGIPYSNDMGCTdnpgynyppcpacpqsdgrwrnP 191
Cdd:cd16150   74 --LRPDEPNLLKTLKDAGYHVAWAGKNDD----------------LPGEFAAEAYCD----------------------S 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 192 DRDCytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTsGRPFLLYVGLAHMHVPLSVTPP------------ 259
Cdd:cd16150  114 DEAC----------------------------VRTAIDWLRNRRP-DKPFCLYLPLIFPHPPYGVEEPwfsmidreklpp 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 260 --------------LANPQSQRLYRAS---LQEM-----------DSLVGQIKDKVDHVA-KENTLLWFAGDNGPWAqkc 310
Cdd:cd16150  165 rrppglrakgkpsmLEGIEKQGLDRWSeerWRELratylgmvsrlDHQFGRLLEALKETGlYDDTAVFFFSDHGDYT--- 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 311 elagsmGPFsGLWQTHQGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSLLDIFPTVIALAgaslppnrkfdGVD 390
Cdd:cd16150  242 ------GDY-GLVEKWPNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLA-----------GIP 296

                 ....*....
gi 564374894 391 VSEVLFGKS 399
Cdd:cd16150  297 LSHTHFGRS 305
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
36-382 1.29e-16

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: 82.31  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16028    1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 116 LNETTLAEVLQQAGYVTAMIGKWHL-----GHH------GSYHPSFRGFDYYFGIPYsndmgctdnpgynYPPcpacPQS 184
Cdd:cd16028   76 ARHLTLALELRKAGYDPALFGYTDTspdprGLApldprlLSYELAMPGFDPVDRLDE-------------YPA----EDS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 185 DGRWrnpdrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPL---------- 254
Cdd:cd16028  139 DTAF----------------------------------LTDRAIEYLD--ERQDEPWFLHLSYIRPHPPFvapapyhaly 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 255 ---SVTPPLANPQSQR------LYRASLQEMDS---------------------------LVGQIKDKVDHVAK------ 292
Cdd:cd16028  183 dpaDVPPPIRAESLAAeaaqhpLLAAFLERIESlsfspgaanaadlddeevaqmratylgLIAEVDDHLGRLFDylketg 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 293 --ENTLLWFAGDNGpwaqkcELAGsmgpfsglwQTHQGGspaKQTTWEGGHRVPALAYWPGRvPVNVTS----TALLSLL 366
Cdd:cd16028  263 qwDDTLIVFTSDHG------EQLG---------DHWLWG---KDGFFDQAYRVPLIVRDPRR-EADATRgqvvDAFTESV 323
                        410
                 ....*....|....*.
gi 564374894 367 DIFPTVIALAGASLPP 382
Cdd:cd16028  324 DVMPTILDWLGGEIPH 339
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
36-383 6.38e-12

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: 67.18  E-value: 6.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTHNFavTSVGGLP 115
Cdd:cd16171    1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 116 LNETTLAEVLQQAGYVTAMIGK--WHLGHHGSyhpSFRGFDYYFGIPYSndmgctdnpgynyppcpacpqsdgrWRNPDR 193
Cdd:cd16171   76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHSV---SNRVEAWTRDVPFL-------------------------LRQEGR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 194 DCytdvalplyENLNIVEQPVNLSGLAQKYAERAVEFIEQASTS-GRPFLLYVGL--AHMHVPLSVTPPLANPQSQR-LY 269
Cdd:cd16171  128 PT---------VNLVGDRSTVRVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLnlPHPYPSPSMGENFGSIRNIRaFY 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 270 RASLQEMDSLVGQIKDKV-DHVAKENTLLWFAGDNGpwaqkcELAGSMGPFSglwqthqggspaKQTTWEGGHRVPALAY 348
Cdd:cd16171  199 YAMCAETDAMLGEIISALkDTGLLDKTYVFFTSDHG------ELAMEHRQFY------------KMSMYEGSSHVPLLIM 260
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 564374894 349 WPGrVPVNVTSTALLSLLDIFPTVIALAGASLPPN 383
Cdd:cd16171  261 GPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
28-391 6.47e-12

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 67.76  E-value: 6.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  28 SGETRAPRPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVthnfA 107
Cdd:COG1368  227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 108 VTSVGGLPLNetTLAEVLQQAGYVTAMIgkwHlGHHGS------YHPSFrGFDYYFGIpysNDMGctdnpgynyppcpac 181
Cdd:COG1368  303 YKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDR---EDFD--------------- 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 182 PQSDGRWRNPDRDcytdvalpLYEnlniveqpvnlsglaqkyaeravEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLA 261
Cdd:COG1368  358 DPFDGGWGVSDED--------LFD-----------------------KALEELEKLKKPFFAFLITLSNHGPYTLPEEDK 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 262 -----NPQSQRLYRASLQEMDSLVGQIKDKvdhvAK-----ENTLLWFAGDngpwaqkcelagsmgpfsglwqtHQGGSP 331
Cdd:COG1368  407 kipdyGKTTLNNYLNAVRYADQALGEFIEK----LKksgwyDNTIFVIYGD-----------------------HGPRSP 459
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564374894 332 AKQTTWE--GGHRVPALAYWPGRVPVNVTSTaLLSLLDIFPTVIALAGASLPPNRKFdGVDV 391
Cdd:COG1368  460 GKTDYENplERYRVPLLIYSPGLKKPKVIDT-VGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
13-304 2.62e-07

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 52.83  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  13 MVFSGLLYPFVDFSISGETRAPRPNIVIILADDMGWGDLGANwaetkDTTNLDKMASEGMRFVDFHAA--ASTCsPSRAS 90
Cdd:COG1524    1 MKRGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  91 LLTGRLGLRNGVTHNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPS----F 150
Cdd:COG1524   75 LLTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 151 RGFDYYFGIPYSNdmgctdnpgynyppcpacpqsdgrwrnpdrdcytdvalplyenlniveqpvnlsglaqkyaERAVEF 230
Cdd:COG1524  155 DGRKPLLGNPAAD-------------------------------------------------------------RWIAAA 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 231 IEQASTSGRPFLLYVGL------AHMHVPLSvtpplanPQsqrlYRASLQEMDSLVGQIKDKVD-HVAKENTLLWFAGDN 303
Cdd:COG1524  174 ALELLREGRPDLLLVYLpdldyaGHRYGPDS-------PE----YRAALREVDAALGRLLDALKaRGLYEGTLVIVTADH 242

                 .
gi 564374894 304 G 304
Cdd:COG1524  243 G 243
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
16-371 6.29e-04

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: 42.58  E-value: 6.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  16 SGLLYPFVDFSISgeTRAPRPNIVIILADDMGWGDLGAnwaetKDTTNLDKMASEGMRFVDfHAAASTCSPsrasllTGR 95
Cdd:COG3083  227 SSLNYPLHPLQFS--DPAKPPNILLIVVDSLRADMLDP-----EVMPNLYAFAQRSLRFTN-HYSSGNSTR------AGL 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894  96 LGLRNGVTHNFAvTSVgglpLNETT---LAEVLQQAGYVtamigkwhlghhgsyhpsfrgfdyyFGIPYSNdmgctdnpG 172
Cdd:COG3083  293 FGLFYGLPGNYW-DSI----LAERTppvLIDALQQQGYQ-------------------------FGLFSSA--------G 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 173 YNYPPCpacpqsdgrwrnpDRDCYTDVALPLYENLNIVEQPvnlsglAQKYAERAVEFIEQAStSGRPFLLYVGLAHMH- 251
Cdd:COG3083  335 FNSPLF-------------RQTIFSDVSLPRLHTPGGPAQR------DRQITAQWLQWLDQRD-SDRPWFSYLFLDAPHa 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374894 252 -----------------VPLSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGP-------- 305
Cdd:COG3083  395 ysfpadypkpfqpsedcNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLlENTIVIITADHGEefnengqn 474
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564374894 306 -WaqkcelaGSMGPFSgLWQTHqggspakqttwegghrVPALAYWPGRVPVNVTStaLLSLLDIFPT 371
Cdd:COG3083  475 yW-------GHNSNFS-RYQLQ----------------VPLVIHWPGTPPQVISK--LTSHLDIVPT 515
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH