NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568976097|ref|XP_006534413|]
View 

arylsulfatase G isoform X1 [Mus musculus]

Protein Classification

ARSG domain-containing protein( domain architecture ID 10888435)

ARSG domain-containing protein

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: 598.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgr 193
Cdd:cd16161   81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQS-LYRAS 272
Cdd:cd16161  132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 273 LREMDSLVGQIKDKVDHV-ARENTLLWFTGDNGPWAQKCELAgsVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161  189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 352 RVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGeYGALQTVRLNHYKAF 431
Cdd:cd16161  267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 568976097 432 YITGGAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQ 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: 598.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgr 193
Cdd:cd16161   81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQS-LYRAS 272
Cdd:cd16161  132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 273 LREMDSLVGQIKDKVDHV-ARENTLLWFTGDNGPWAQKCELAgsVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161  189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 352 RVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGeYGALQTVRLNHYKAF 431
Cdd:cd16161  267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 568976097 432 YITGGAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQ 469
Cdd:cd16161  346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
13-432 2.46e-91

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 284.46  E-value: 2.46e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  13 MAFSGFFYPLVDFSISGKTRAPQPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLL 92
Cdd:COG3119    1 MKRLLLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  93 TGRLGLRNGVTHNFAvTSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLghhgsyhpnfrgfdyyfgipYSNDmgctdapg 172
Cdd:COG3119   81 TGRYPHRTGVTDNGE-GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD-------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 173 ynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqpvnlsglaqKYAERAVEFIEQASTSGRPFLLYVGLAHMHV 252
Cdd:COG3119  132 -------------------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHA 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 253 PLSVTPPLAHP-----------------------QRQSLYRASLREMDSLVGQIkdkVDHVAR----ENTLLWFTGDNGP 305
Cdd:COG3119  163 PYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRL---LDALEElglaDNTIVVFTSDNGP 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 306 WaqkcelagsvgpfFGLWqTHQGGsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPnrK 385
Cdd:COG3119  240 S-------------LGEH-GLRGG---KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--D 300
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 568976097 386 FDGRDVSEVLFGKSQMGHRVLFHpnsgAAGEYGALQTVRLNHYKAFY 432
Cdd:COG3119  301 LDGRSLLPLLTGEKAEWRDYLYW----EYPRGGGNRAIRTGRWKLIR 343
Sulfatase pfam00884
Sulfatase;
36-378 1.27e-56

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 191.10  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097   36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  116 VNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFG-IPYSNDMGctdapgynyppcpACPQRDGLWRNPGrd 194
Cdd:pfam00884  77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYA-------------DPPDVPYNCSGGG-- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  195 CYTDValplyenlniveqpvnlsglaqkYAERAVEFIEQAStsgRPFLLYVGLAHMHVPLSVTP----------PLAHPQ 264
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDrypekyatfkPSSCSE 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  265 RQSL--YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPwaqkcelagSVGPFfglwQTHQGGSPTKQTtWEGGH 341
Cdd:pfam00884 196 EQLLnsYDNTLLYTDDAIGRVLDKLEENGlLDNTLVVYTSDHGE---------SLGEG----GGYLHGGKYDNA-PEGGY 261
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568976097  342 RVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
35-492 2.94e-36

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 140.57  E-value: 2.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGwGD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGVTHNF 106
Cdd:PRK13759   6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVVPWNY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 107 avtsvgglpvnETTLAEVLRQEGYVTAMIGKWHlghhgsYHP--NFRGFDYYF---GIPYSN--------DMgCTD---- 169
Cdd:PRK13759  85 -----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVLlhdGYLHSGrnedksqfDF-VSDylaw 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 170 ----APGYNyppcpacPQRDGLwrnpGRDCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLL 243
Cdd:PRK13759 147 lrekAPGKD-------PDLTDI----GWDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 244 YVGLAHMHVPLSvtPPLA------------------------HPQRQSL------------------YRASLREMDSLVG 281
Cdd:PRK13759 205 KMSFARPHSPYD--PPKRyfdmykdadipdphigdweyaedqDPEGGSIdalrgnlgeeyarraraaYYGLITHIDHQIG 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 282 QIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpfFGLWQthqggsptKQTTWEGGHRVPALAYWPG---RVPANV 357
Cdd:PRK13759 283 RFLQALKEFGlLDNTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGT 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 358 TSTALLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKSQmGHRVLFHpnsgaaGEYGalqtvrlNHYKAF-YITGG 436
Cdd:PRK13759 345 VIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYE-GWRPYLH------GEHA-------LGYSSDnYLTDG 408
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568976097 437 A-KACDGSV-GPEQhhvaplIFNLEDAADEGMPLQkGSPEYQEVLQQVTRALADVLQD 492
Cdd:PRK13759 409 KwKYIWFSQtGEEQ------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: 598.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgr 193
Cdd:cd16161   81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQS-LYRAS 272
Cdd:cd16161  132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 273 LREMDSLVGQIKDKVDHV-ARENTLLWFTGDNGPWAQKCELAgsVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161  189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 352 RVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGeYGALQTVRLNHYKAF 431
Cdd:cd16161  267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 568976097 432 YITGGAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQ 469
Cdd:cd16161  346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
35-465 6.95e-173

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: 493.23  E-value: 6.95e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16026    1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDMGCTDAPGYNYPPCPAcpqrdglwrnpgr 193
Cdd:cd16026   81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 dcytdvalPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQAstSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASL 273
Cdd:cd16026  148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 274 REMDSLVGQIKDKVDHV-ARENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQGGsptKQTTWEGGHRVPALAYWPGR 352
Cdd:cd16026  218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPL-------RGG---KGTTWEGGVRVPFIAWWPGV 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 353 VPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGaageyGALQTVRLNHYKAFY 432
Cdd:cd16026  288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDG-----GDLQAVRSGRWKLHL 362
                        410       420       430
                 ....*....|....*....|....*....|...
gi 568976097 433 ITGGAKACDGSVGPEQHHVAPLIFNLEDaaDEG 465
Cdd:cd16026  363 PTTYRTGTDPGGLDPTKLEPPLLYDLEE--DPG 393
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
36-522 1.14e-114

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: 347.90  E-value: 1.14e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGGL 114
Cdd:cd16158    2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 115 PVNETTLAEVLRQEGYVTAMIGKWHL--GHHGSYHPNFRGFDYYFGIPYSNDMGctdaPGYN---YPPCPACpqrDGLWR 189
Cdd:cd16158   82 PLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQG----PCQNltcFPPNIPC---FGGCD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 190 nPGrdcytDVALPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLY 269
Cdd:cd16158  155 -QG-----EVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPF 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 270 RASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPWAQKCELAGSVgpffGLWQTHQGgsptkqTTWEGGHRVPALAY 348
Cdd:cd16158  229 GDALAELDGSVGELLQTLKENGiDNNTLVFFTSDNGPSTMRKSRGGNA----GLLKCGKG------TTYEGGVREPAIAY 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 349 WPGRVPANVTStALLSLLDIFPTVIALAGASLpPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGEYGALqTVRLNHY 428
Cdd:cd16158  299 WPGRIKPGVTH-ELASTLDILPTIAKLAGAPL-PNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWGKY 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 429 KAFYITGGA--------KACDGSvGPEQHHVAPLIFNLEDAADEGMPLQKGsPEYQEVLQQVtRALADVLQDIADDNSSR 500
Cdd:cd16158  376 KAHFYTQGAahsgttpdKDCHPS-AELTSHDPPLLFDLSQDPSENYNLLGL-PEYNQVLKQI-QQVKERFEASMKFGESE 452
                        490       500
                 ....*....|....*....|....*.
gi 568976097 501 ADYTQDPSVIPCCN----PYQTTCRC 522
Cdd:cd16158  453 INKGEDPALEPCCKpgctPKPSCCQC 478
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
35-487 1.69e-110

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: 335.94  E-value: 1.69e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---THNFAVTSV 111
Cdd:cd16160    1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 112 GGLPVNETTLAEVLRQEGYVTAMIGKWHLG-----HHGSYH-PNFRGFDYY-FGIPYSNDMGCtDAPGYNYPpcpacpqr 184
Cdd:cd16160   81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWAC-DDTGRHVD-------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 185 dglWRNPGRdCYtdvalpLYENLNIVEQPVNLSGLAQKYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPLSVTPPLAHPQ 264
Cdd:cd16160  152 ---FPDRSA-CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKS 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 265 RQSLYRASLREMDSLVGQIKDK-VDHVARENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQGGsptKQTTWEGGHRV 343
Cdd:cd16160  220 KRGRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGL-------KGG---KGNSWEGGIRV 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 344 PALAYWPGRVPANVtSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR-VLFHPNSgaageygALQT 422
Cdd:cd16160  290 PFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDdILYYCCS-------RLMA 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 423 VRLNHYKAFYITG--------GAKACDG---------SVGPEQH---HVAPLIFNLEDAADEGMPLQkgSPEYQEVLQQV 482
Cdd:cd16160  362 VRYGSYKIHFKTQplpsqeslDPNCDGGgplsdyivcYDCEDECvtkHNPPLIFDVEKDPGEQYPLQ--PSVYEHMLEAV 439

                 ....*
gi 568976097 483 TRALA 487
Cdd:cd16160  440 EKLIA 444
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
35-488 1.68e-105

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: 323.65  E-value: 1.68e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTHNFAVTS-- 110
Cdd:cd16157    1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 111 ----VGGLPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPysndmGCTDAPGYN--YPPCPAcpQR 184
Cdd:cd16157   81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAP-----NCHFGPYDNkaYPNIPV--YR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 185 DglWRNPGRdcytdvalpLYENLNIvEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQ 264
Cdd:cd16157  154 D--WEMIGR---------YYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 265 RQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNG-PWAQKCELAGSVGPFFGlwqthqggspTKQTTWEGGHR 342
Cdd:cd16157  222 QRGLYGDAVMELDSSVGKILESLKSLGiENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMR 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 343 VPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSgaageygALQT 422
Cdd:cd16157  292 EPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMA 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 423 VRLNHYKAFYIT---------GGAKACDGSVGP-------EQHHVAPLIFNLEDAADEGMPLQKGSPEYQEVLQQVTRAL 486
Cdd:cd16157  365 VRLGQYKAHFWTwsnsweefrKGINFCPGQNVPgvtthnqTDHTKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVV 444

                 ..
gi 568976097 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 4.83e-104

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: 321.54  E-value: 4.83e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN------FAV 108
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 109 TSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLGHH------GSYHPNFRGFDYYFGIPYSNDMGCTDAPG--YNYPPCPA 180
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 181 CPQRDGL------------------WRnPGRDCYTDVALP-----------------LYENLNIVEQPVNLSGLAQKYAE 225
Cdd:cd16159  161 FPLLTAFvlitaltiflllylgavsKR-FFVFLLILSLLFislfflllitnryfnciLMRNHEVVEQPMSLENLTQRLTK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 226 RAVEFIEQasTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNG 304
Cdd:cd16159  240 EAISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYFTSDNG 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 305 PWAqkcELAGSVGPFFGLWQTHQGGSptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNR 384
Cdd:cd16159  318 GHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDR 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 385 KFDGRDVSEVLFGKSQMG-HRVLFH------------PNSGAAgeygalqtvrlnHYKAFYIT-----GGAKACDGSVGP 446
Cdd:cd16159  393 IIDGRDLMPLLTGQEKRSpHEFLFHycgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEGCCGTLLCR 460
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568976097 447 -----EQHHVAPLIFNLEDAADEGMPLQKGSPEYQEVLQQVTRALADVLQDIA 494
Cdd:cd16159  461 cfgdsVTHHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIE 513
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
36-459 6.38e-93

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


Pssm-ID: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 287.89  E-value: 6.38e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGAN---WAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHNFAVTSVG 112
Cdd:cd16142    1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 113 GLPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNdmgctdapgynyppcpacpqrdglwrnpg 192
Cdd:cd16142   80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHT----------------------------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 193 rdcytdvalplyenlniveqpvnlsgLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAH-PQRQSLYRA 271
Cdd:cd16142  131 --------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGkSSGKGKYAD 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 272 SLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPWAQKCELAGSvGPFFGlwqthqggspTKQTTWEGGHRVPALAYWP 350
Cdd:cd16142  185 SMVELDDHVGQILDALDELGiADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 351 GRVPANVTSTALLSLLDIFPTVIALAGASLPP------NRKFDGRDVSEVLFGKS-QMGHRVLFHpnsGAAGEYGAlqtV 423
Cdd:cd16142  254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPKdkllgkDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 568976097 424 RLNHYKAFYITGGAKACDGSVGPEQHHVaPLIFNLE 459
Cdd:cd16142  328 RWKNWKVHFKAQEDTGGPTGEPFYVLTF-PLIFNLR 362
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
13-432 2.46e-91

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 284.46  E-value: 2.46e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  13 MAFSGFFYPLVDFSISGKTRAPQPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLL 92
Cdd:COG3119    1 MKRLLLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  93 TGRLGLRNGVTHNFAvTSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLghhgsyhpnfrgfdyyfgipYSNDmgctdapg 172
Cdd:COG3119   81 TGRYPHRTGVTDNGE-GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD-------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 173 ynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqpvnlsglaqKYAERAVEFIEQASTSGRPFLLYVGLAHMHV 252
Cdd:COG3119  132 -------------------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHA 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 253 PLSVTPPLAHP-----------------------QRQSLYRASLREMDSLVGQIkdkVDHVAR----ENTLLWFTGDNGP 305
Cdd:COG3119  163 PYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRL---LDALEElglaDNTIVVFTSDNGP 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 306 WaqkcelagsvgpfFGLWqTHQGGsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPnrK 385
Cdd:COG3119  240 S-------------LGEH-GLRGG---KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--D 300
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 568976097 386 FDGRDVSEVLFGKSQMGHRVLFHpnsgAAGEYGALQTVRLNHYKAFY 432
Cdd:COG3119  301 LDGRSLLPLLTGEKAEWRDYLYW----EYPRGGGNRAIRTGRWKLIR 343
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
36-429 7.80e-88

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


Pssm-ID: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 276.35  E-value: 7.80e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--------- 106
Cdd:cd16144    1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 107 ----AVTSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGipysndMGCTDAPGYNYPPCPACP 182
Cdd:cd16144   81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG------GTGNGGPPSYYFPPGKPN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 183 qrdGLWRNPGRDCYtdvalplyenlniveqpvnlsgLAQKYAERAVEFIEQAstSGRPFLLYvgLAH--MHVPLSVTP-- 258
Cdd:cd16144  155 ---PDLEDGPEGEY----------------------LTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPel 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 259 ---------PLAHPQRQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQG 328
Cdd:cd16144  206 iekyekkkkGLRKGQKNPVYAAMIESLDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPL-------RG 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 329 GsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR--VL 406
Cdd:cd16144  279 G---KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraLF 355
                        410       420
                 ....*....|....*....|....*
gi 568976097 407 FH-PN-SGAAGEYGAlqTVRLNHYK 429
Cdd:cd16144  356 WHfPHyHGQGGRPAS--AIRKGDWK 378
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
36-460 8.33e-85

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: 267.91  E-value: 8.33e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETK-DTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGLRNGVTHNFAvTS 110
Cdd:cd16143    1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwRSRLKGGVLGGFS-PP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 111 VggLPVNETTLAEVLRQEGYVTAMIGKWHLG-----------HHGSYH-----------PNFRGFDYYFGIPYSNdmgct 168
Cdd:cd16143   80 L--IEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPASE----- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 169 dapgynyppcpacpqrdglwrnpgrdcytdvALPLyenlniveqpvnlsgLAQKyaerAVEFIEQASTSGRPFLLYVGLA 248
Cdd:cd16143  153 -------------------------------VLPT---------------LTDK----AVEFIDQHAKKDKPFFLYFALP 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 249 HMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGPwaqkcelagSVGPFFGLWQtHQ 327
Cdd:cd16143  183 APHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP---------SPYADYKELE-KF 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 328 GGSPT------KQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQM 401
Cdd:cd16143  253 GHDPSgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQ 332
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568976097 402 GHRVLFHPNSGAAGeygalQTVRLNHYKafYITGGAKacDGSVGPEQHHVAPL----IFNLED 460
Cdd:cd16143  333 EVRESLVHHSGNGS-----FAIRKGDWK--LIDGTGS--GGFSYPRGKEKLGLppgqLYNLST 386
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
36-438 2.99e-84

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: 267.15  E-value: 2.99e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLP 115
Cdd:cd16145    1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 116 VNETTLAEVLRQEGYVTAMIGKWHLGHHGSY-HPNFRGFDYYFGIpysndMGCTDAPGYnYPPCpacpqrdgLWRNPGRd 194
Cdd:cd16145   81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGY-----LDQVHAHNY-YPEY--------LWRNGEK- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 195 cytdvaLPLYENLNIVEQPVNLSGLAQK-YAE-----RAVEFIEQAstSGRPFLLYVGL----AHMHVP----------- 253
Cdd:cd16145  146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYtlphAPLQVPddgpykykpkd 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 254 LSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKV-DHVARENTLLWFTGDNGP-----WAQKCELAGSVGPFFGLwqthq 327
Cdd:cd16145  218 PGIYAYLPWPQPEKAYAAMVTRLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 328 ggsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASlPPNRKfDGRDVSEVLFGKS-QMGHRVL 406
Cdd:cd16145  293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAE-PPEDI-DGISLLPTLLGKPqQQQHDYL 365
                        410       420       430
                 ....*....|....*....|....*....|..
gi 568976097 407 FHpnsgAAGEYGALQTVRLNHYKAFYITGGAK 438
Cdd:cd16145  366 YW----EFYEGGGAQAVRMGGWKAVRHGKKDG 393
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
36-429 2.57e-81

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: 259.40  E-value: 2.57e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTHnfavTSVGG-- 113
Cdd:cd16146    1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIpysndmgctdapgynyppcpacpqRDGLWRNPGR 193
Cdd:cd16146   76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGH------------------------GGGGIGQYPD 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 DCYTDVALPLYENLNIVEQpvnlsglAQKYA-----ERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLAHPQRQSL 268
Cdd:cd16146  132 YWGNDYFDDTYYHNGKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPYKDMG 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 269 YRASLRE-------MDSLVGQIKDKVDHV-ARENTLLWFTGDNGPWaqkcelagsvGPFFGLWQTHQGGspTKQTTWEGG 340
Cdd:cd16146  203 LDDKLAAfygmienIDDNVGRLLAKLKELgLEENTIVIFMSDNGPA----------GGVPKRFNAGMRG--KKGSVYEGG 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 341 HRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQM-GHRVLF--HPNSGAAGEY 417
Cdd:cd16146  271 HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwPERTLFthSGRWPPPPKK 350
                        410
                 ....*....|..
gi 568976097 418 GALQTVRLNHYK 429
Cdd:cd16146  351 KRNAAVRTGRWR 362
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
36-390 3.24e-74

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


Pssm-ID: 293746 [Multi-domain]  Cd Length: 236  Bit Score: 234.64  E-value: 3.24e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGLP 115
Cdd:cd16022    1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 116 VNETTLAEVLRQEGYVTAMIGKWHlghhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacpqrdglwrnpgrdc 195
Cdd:cd16022   79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 196 ytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSgRPFLLYVGLAHMHvplsvtPPLAhpqrqslYRASLRE 275
Cdd:cd16022  103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPH------PPFA-------YYAMVSA 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 276 MDSLVGQIKDKVD-HVARENTLLWFTGDNGpwaqkcelaGSVGPFFGLWQthqggsptKQTTWEGGHRVPALAYWPGRVP 354
Cdd:cd16022  140 IDDQIGRILDALEeLGLLDNTLIVFTSDHG---------DMLGDHGLRGK--------KGSLYEGGIRVPFIVRWPGKIP 202
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 568976097 355 ANVTSTALLSLLDIFPTVIALAGASLPpnRKFDGRD 390
Cdd:cd16022  203 AGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
36-435 1.00e-68

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: 225.89  E-value: 1.00e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSV-GGL 114
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 115 PVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYH-PNFRGFDYYFGiPYSndmGCTDapGYNYPPCPACP-QRDGLWRN-- 190
Cdd:cd16029   80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDyGNDDLRDNee 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 191 ---PGRDCY-TDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSgRPFLLYVGLAHMHVPLSVTPPLA----- 261
Cdd:cd16029  154 pawDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYAdpyed 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 262 ------HPQRQsLYRASLREMDSLVGQIKDKVDHVAR-ENTLLWFTGDNGPWAQKCElAGSVGPFFGlwqthqggspTKQ 334
Cdd:cd16029  210 kfahikDEDRR-TYAAMVSALDESVGNVVDALKAKGMlDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKN 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 335 TTWEGGHRVPALAYWPGRVP-ANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR-VLFHPNSG 412
Cdd:cd16029  278 TLWEGGVRVPAFVWSPLLPPkRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDI 357
                        410       420
                 ....*....|....*....|...
gi 568976097 413 AAGEYGAlqTVRLNHYKafYITG 435
Cdd:cd16029  358 TRTTGGA--AIRVGDWK--LIVG 376
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-435 5.04e-66

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 218.24  E-value: 5.04e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHnfavtsvGGLP 115
Cdd:cd16151    1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 116 VNETTLAEVLRQEGYVTAMIGKWHLG---HHGSYHPNFrGFDYY--FGIPYSNDmgctDAPGYNYPpCPACPQRDGLWRN 190
Cdd:cd16151   73 PKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDEYclWQLTETGE----KYSRPATP-TFNIRNGKLLETT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 191 PGR---DCYTDVALplyenlniveqpvnlsglaqkyaeravEFIEQAStsGRPFLLYVGLAHMHVPLSVTPPLAHP---- 263
Cdd:cd16151  147 EGDygpDLFADFLI---------------------------DFIERNK--DQPFFAYYPMVLVHDPFVPTPDSPDWdpdd 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 264 ----QRQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcelagSVGPFFGLW--QTHQGGsptKQTT 336
Cdd:cd16151  198 krkkDDPEYFPDMVAYMDKLVGKLVDKLEELGlRENTIIIFTGDNG----------THRPITSRTngREVRGG---KGKT 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 337 WEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGE 416
Cdd:cd16151  265 TDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHK 344
                        410
                 ....*....|....*....
gi 568976097 417 YGALQTVRLNHYKaFYITG 435
Cdd:cd16151  345 KFGSRFVRTKRYK-LYADG 362
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
36-407 1.15e-57

N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.


Pssm-ID: 293751 [Multi-domain]  Cd Length: 373  Bit Score: 196.19  E-value: 1.15e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGA--NWAETkdtTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFavTSVGG 113
Cdd:cd16027    1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgr 193
Cdd:cd16027   76 LPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWD----------------------------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 dcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQAStSGRPFLLYVGLAHMHV-------------PLSVTPPL 260
Cdd:cd16027  127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHRpyppgdgeepgydPEKVKVPP 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 261 AHPQ----RQSL--YRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpwaqkcelagsvGPFFGlwqthqggspTK 333
Cdd:cd16027  177 YLPDtpevREDLadYYDEIERLDQQVGEILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------AK 234
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568976097 334 QTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKSQMGHRVLF 407
Cdd:cd16027  235 GTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVF 306
Sulfatase pfam00884
Sulfatase;
36-378 1.27e-56

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 191.10  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097   36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  116 VNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFG-IPYSNDMGctdapgynyppcpACPQRDGLWRNPGrd 194
Cdd:pfam00884  77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYA-------------DPPDVPYNCSGGG-- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  195 CYTDValplyenlniveqpvnlsglaqkYAERAVEFIEQAStsgRPFLLYVGLAHMHVPLSVTP----------PLAHPQ 264
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDrypekyatfkPSSCSE 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  265 RQSL--YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPwaqkcelagSVGPFfglwQTHQGGSPTKQTtWEGGH 341
Cdd:pfam00884 196 EQLLnsYDNTLLYTDDAIGRVLDKLEENGlLDNTLVVYTSDHGE---------SLGEG----GGYLHGGKYDNA-PEGGY 261
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568976097  342 RVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
35-408 6.55e-55

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: 189.58  E-value: 6.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETkDTTNLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGV-THNFAVTSVGG 113
Cdd:cd16025    2 RPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGMgTMAELATGKPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 114 ----LPVNETTLAEVLRQEGYVTAMIGKWHLGHHgsyhpnfrgfDYYFgipysndmgcTDApgynyppcpacpqrdglwr 189
Cdd:cd16025   80 yegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----------TDD------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 190 npgrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYV--GLAH--MHVP------------ 253
Cdd:cd16025  121 ---------------------------------LTDKAIEYIDEQKAPDKPFFLYLafGAPHapLQAPkewidkykgkyd 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 254 -------------------------LSVTPPLAHP-------------QRQSLYRASLREMDSLVGQIkdkVDHVAR--- 292
Cdd:cd16025  168 agwdalreerlerqkelglipadtkLTPRPPGVPAwdslspeekkleaRRMEVYAAMVEHMDQQIGRL---IDYLKElge 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 293 -ENTLLWFTGDNGP-----WAQkcelAGSvGPFFGlwqthqggspTKQTTWEGGHRVPALAYWPGRVPA-NVTSTALLSL 365
Cdd:cd16025  245 lDNTLIIFLSDNGAsaepgWAN----ASN-TPFRL----------YKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHV 309
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 366 LDIFPTVIALAGASLP------PNRKFDGRDVSEVLFGKSQ-----------MGHRVLFH 408
Cdd:cd16025  310 IDIAPTILELAGVEYPktvngvPQLPLDGVSLLPTLDGAAApsrrrtqyfelFGNRAIRK 369
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
35-424 7.27e-51

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


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 178.92  E-value: 7.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggL 114
Cdd:cd16034    1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 115 PVNETTLAEVLRQEGYVTAMIGKWHL-GHHGSYH--------PNFR-GFDYYFGipysndMGCTDapGYNYPPcpacpqr 184
Cdd:cd16034   76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNPH------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 185 dgLWRNPGRDCYTDVALPLYEnlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYV--GLAH------------M 250
Cdd:cd16034  141 --YYDDDGKRIYIKGYSPDAE------------------TDLAIEYLENQADKDKPFALVLswNPPHdpyttapeeyldM 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 251 HVPLSVT----PPLAHPQRQSL------YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpf 319
Cdd:cd16034  201 YDPKKLLlrpnVPEDKKEEAGLredlrgYYAMITALDDNIGRLLDALKELGlLENTIVVFTSDHG------DMLGS---- 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 320 fglwqtHqgGSPTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGasLPPNRKFDGRDVSEVLFGKS 399
Cdd:cd16034  271 ------H--GLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGK 340
                        410       420       430
                 ....*....|....*....|....*....|...
gi 568976097 400 QMGHR----VLFHPNSGAA----GEYGALQTVR 424
Cdd:cd16034  341 DDEPDsvllQCFVPFGGGSardgGEWRGVRTDR 373
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
35-486 6.40e-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: 171.56  E-value: 6.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvGGL 114
Cdd:cd16031    2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PLF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 115 PVNETTLAEVLRQEGYVTAMIGKWHLGHHGsYHPNfRGFDYYFGIPysndmgctdAPGYNYPPcpacpqrdglwrnpgrd 194
Cdd:cd16031   78 DASQPTYPKLLRKAGYQTAFIGKWHLGSGG-DLPP-PGFDYWVSFP---------GQGSYYDP----------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 195 cytdvalPLYENLNIVEQPVNLSGLaqkYAERAVEFIEQAStSGRPFLLYVG--LAH---------------MHVPLSVT 257
Cdd:cd16031  130 -------EFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLSfkAPHrpftpaprhrglyedVTIPEPET 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 258 ---------PPLAHPQRQSL--------------------YRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpwa 307
Cdd:cd16031  199 fddddyagrPEWAREQRNRIrgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEeQGLADNTIIIYTSDNG--- 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 308 qkcelagsvgpFF----GLwqthqGGsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPN 383
Cdd:cd16031  276 -----------FFlgehGL-----FD---KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 384 rkFDGRDVSEVLFGKSQMGHR------VLFHPNSGAAGEYGALQTVRlnhYKAFYITGGAKAcdgsvgpEQhhvaplIFN 457
Cdd:cd16031  337 --MQGRSLLPLLEGEKPVDWRkefyyeYYEEPNFHNVPTHEGVRTER---YKYIYYYGVWDE-------EE------LYD 398
                        490       500       510
                 ....*....|....*....|....*....|...
gi 568976097 458 LEdaADegmPLQK----GSPEYQEVLQQVTRAL 486
Cdd:cd16031  399 LK--KD---PLELnnlaNDPEYAEVLKELRKRL 426
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-393 2.50e-46

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 162.41  E-value: 2.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----THNFAVTS 110
Cdd:cd16149    1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 111 VG-GLPVNETTLAEVLRQEGYVTAMIGKWHLGhhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacpqrdglwr 189
Cdd:cd16149   81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 190 npgrdcytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSGRPFLLYVGLAHMHVPLSvtpplahpqrqslY 269
Cdd:cd16149  113 -----------------------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------Y 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 270 RASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcelagsvgpfF-----GLWqtHQGGSPTKQTTWEGGHRV 343
Cdd:cd16149  145 FAAVTGVDRNVGRLLDELEELGlTENTLVIFTSDNG---------------FnmghhGIW--GKGNGTFPLNMYDNSVKV 207
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 568976097 344 PALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSE 393
Cdd:cd16149  208 PFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
35-389 8.69e-40

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: 148.85  E-value: 8.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWgDLGANWAETKdTTNLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtSVGGL 114
Cdd:cd16147    1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 115 PV------NETTLAEVLRQEGYVTAMIGK----WHLGHHGSYHPnfRGFDYYFGI-------PYSNDMGCTDAPGYNYPp 177
Cdd:cd16147   75 PKfwqnglERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgnstyyNYTLSNGGNGKHGVSYP- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 178 cpacpqrdglwrnpgRDCYTDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVG---------LA 248
Cdd:cd16147  152 ---------------GDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftPA 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 249 HMHVPLSVTPPLAHP---------------------------QRQSLYRA---SLREMDSLVGQIKDKVDHVAR-ENTLL 297
Cdd:cd16147  194 PRYANLFPNVTAPPRpppnnpdvsdkphwlrrlpplnptqiaYIDELYRKrlrTLQSVDDLVERLVNTLEATGQlDNTYI 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 298 WFTGDNG-PWAQkcelagsvgpfFGLWqthqggsPTKQTTWEGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALA 376
Cdd:cd16147  274 IYTSDNGyHLGQ-----------HRLP-------PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLA 334
                        410
                 ....*....|...
gi 568976097 377 GASLPPNrkFDGR 389
Cdd:cd16147  335 GAPPPSD--MDGR 345
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-389 1.05e-39

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: 148.91  E-value: 1.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--AVTSVGG 113
Cdd:cd16033    1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSyhPNFRGFDYYFGIpysndmgctdapgynyppcpacpqrdglwrNPGR 193
Cdd:cd16033   81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYLPV------------------------------ETTI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 DCYTdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGL-------------AHMHVPLSVTPP- 259
Cdd:cd16033  129 EYFL--------------------------ADRAIEMLEELAADDKPFFLRVNFwgphdpyippepyLDMYDPEDIPLPe 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 260 -LAHP-------QRQSLYRASLRE-------------------MDSLVGQIKDKVDHV-ARENTLLWFTGDNGpwaqkcE 311
Cdd:cd16033  183 sFADDfedkpyiYRRERKRWGVDTedeedwkeiiahywgyitlIDDAIGRILDALEELgLADDTLVIFTSDHG------D 256
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976097 312 LAGSvgpfFGLWQThqgGSPTKQTTweggHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGAslPPNRKFDGR 389
Cdd:cd16033  257 ALGA----HRLWDK---GPFMYEET----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGV--DVPPKVDGR 321
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-381 1.14e-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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 145.19  E-value: 1.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWgDLGANWAETKD---TTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVThnfavtSVG 112
Cdd:cd16154    1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 113 G-LPVNETTLAEVLRQE----GYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIpysndmgctdapgynyppcpacpqrdgl 187
Cdd:cd16154   73 DeLLLSEETLLQLLIKDattaGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI---------------------------- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 188 wrNPGrdcytdvALPLYENLNIVEQPVNLSglAQKYA-----ERAVEFIEQASTsgrPFLLYVGLAHMHVPLSVTPPLAH 262
Cdd:cd16154  125 --LGG-------GVQDYYNWNLTNNGQTTN--STEYAttkltNLAIDWIDQQTK---PWFLWLAYNAPHTPFHLPPAELH 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 263 PQRQS------------LYRASLREMDSLVGQIKDKVDHVARENTLLWFTGDNG-PwaqkcelaGSVGPffgLWQTHQGg 329
Cdd:cd16154  191 SRSLLgdsadieanprpYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP--------GQVVD---LPYTRNH- 258
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568976097 330 spTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLP 381
Cdd:cd16154  259 --AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAA 308
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-460 2.34e-37

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 139.99  E-value: 2.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggLP 115
Cdd:cd16037    1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 116 VNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHpnfrGFDYyfgipysndmgctdapgynyppcpacpqrdglwrnpgrdc 195
Cdd:cd16037   76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY---------------------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 196 ytdvalplyenlnivEQPVnlsglaqkyAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAhpqrqSLYRASLR- 274
Cdd:cd16037  112 ---------------DRDV---------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFY-----DLYVRRARa 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 275 -------EMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpfFGLWQthqggsptKQTTWEGGHRVPAL 346
Cdd:cd16037  163 ayyglveFLDENIGRVLDALEELGlLDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMI 224
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 347 AYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPNRkfDGRDVSEVLFGKSQMGHRVL--FHpnsgAAGEYGALQTVR 424
Cdd:cd16037  225 ISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVFseYH----AHGSPSGAFMLR 297
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 568976097 425 LNHYKafYItggakacdgsvgpeqHHV--APLIFNLED 460
Cdd:cd16037  298 KGRWK--YI---------------YYVgyPPQLFDLEN 318
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-390 3.17e-37

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 138.45  E-value: 3.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILAD----DMgwgdLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHnfavtsv 111
Cdd:cd16148    1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 112 GGLPVNETTLAEVLRQEGYVTAMIGKWhlgHHGSYHPNF-RGFDYYFgipysndmgctdapgynyppcpacPQRDGLWRN 190
Cdd:cd16148   70 GPLEPDDPTLAEILRKAGYYTAAVSSN---PHLFGGPGFdRGFDTFE------------------------DFRGQEGDP 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 191 PGRDCYTdvalplyenlniveqpvnlsglAQKYAERAVEFIEQASTSgRPFLLYVglaHM---HVPlsvtpplahpqrqS 267
Cdd:cd16148  123 GEEGDER----------------------AERVTDRALEWLDRNADD-DPFFLFL---HYfdpHEP-------------Y 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 268 LYRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpwaqkcELagsvgpFF--GLWQTHqGGSPTKQTTwegghRVP 344
Cdd:cd16148  164 LYDAEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EE------FGehGLYWGH-GSNLYDEQL-----HVP 225
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 568976097 345 ALAYWPGRVPANVTStALLSLLDIFPTVIALAGasLPPNRKFDGRD 390
Cdd:cd16148  226 LIIRWPGKEPGKRVD-ALVSHIDIAPTLLDLLG--VEPPDYSDGRS 268
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
35-486 1.31e-36

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 139.24  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRlglrngvtHNFAVTS 110
Cdd:cd16155    2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR--------TLFHAPE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 111 VGG--LPVNETTLAEVLRQEGYVTAMIGKWHLGhhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacpqrdglw 188
Cdd:cd16155   74 GGKaaIPSDDKTWPETFKKAGYRTFATGKWHNG----------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 189 rnpgrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPL-------- 260
Cdd:cd16155  107 ----------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYldmyppet 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 261 ---------AHP------------------------QRQSLYRASLREMDSLVGQIKDKVDHVAR-ENTLLWFTGDNGpw 306
Cdd:cd16155  153 iplpenflpQHPfdngegtvrdeqlapfprtpeavrQHLAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG-- 230
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 307 aqkceLA-GSvgpfFGLwqthQGgsptKQTTWEGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPnrK 385
Cdd:cd16155  231 -----LAvGS----HGL----MG----KQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE--S 290
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 386 FDGRDVSEVLFGKSQMGHRVLFhpnsgaaGEYGALQ-TVRLNHYKAFYITGGAKacdgsvgpeqhhvAPLIFNLEDAADE 464
Cdd:cd16155  291 VEGKSLLPVIRGEKKAVRDTLY-------GAYRDGQrAIRDDRWKLIIYVPGVK-------------RTQLFDLKKDPDE 350
                        490       500
                 ....*....|....*....|..
gi 568976097 465 GMPLQkGSPEYQEVLQQVTRAL 486
Cdd:cd16155  351 LNNLA-DEPEYQERLKKLLAEL 371
PRK13759 PRK13759
arylsulfatase; Provisional
35-492 2.94e-36

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 140.57  E-value: 2.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGwGD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGVTHNF 106
Cdd:PRK13759   6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVVPWNY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 107 avtsvgglpvnETTLAEVLRQEGYVTAMIGKWHlghhgsYHP--NFRGFDYYF---GIPYSN--------DMgCTD---- 169
Cdd:PRK13759  85 -----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVLlhdGYLHSGrnedksqfDF-VSDylaw 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 170 ----APGYNyppcpacPQRDGLwrnpGRDCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLL 243
Cdd:PRK13759 147 lrekAPGKD-------PDLTDI----GWDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 244 YVGLAHMHVPLSvtPPLA------------------------HPQRQSL------------------YRASLREMDSLVG 281
Cdd:PRK13759 205 KMSFARPHSPYD--PPKRyfdmykdadipdphigdweyaedqDPEGGSIdalrgnlgeeyarraraaYYGLITHIDHQIG 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 282 QIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpfFGLWQthqggsptKQTTWEGGHRVPALAYWPG---RVPANV 357
Cdd:PRK13759 283 RFLQALKEFGlLDNTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGT 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 358 TSTALLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKSQmGHRVLFHpnsgaaGEYGalqtvrlNHYKAF-YITGG 436
Cdd:PRK13759 345 VIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYE-GWRPYLH------GEHA-------LGYSSDnYLTDG 408
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568976097 437 A-KACDGSV-GPEQhhvaplIFNLEDAADEGMPLQkGSPEYQEVLQQVTRALADVLQD 492
Cdd:PRK13759 409 KwKYIWFSQtGEEQ------LFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
35-395 2.95e-34

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: 134.24  E-value: 2.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDM----GWgdLGANWAETKdttNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtHNFAVTS 110
Cdd:cd16030    2 KPNVLFIAVDDLrpwlGC--YGGHPAKTP---NIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV-YDNNSYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 111 VGGLPvNETTLAEVLRQEGYVTAMIGK-WHlGHHGSYHPNFRGFDYYFGIPysndmgctdAPGYNYPPCPACPQRDGLWR 189
Cdd:cd16030   76 RKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPP---------GPEKYPPGKLCPGKKGGKGG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 190 NPGRDC---------YTDvalplyenlniveqpvnlsglaQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSV---- 256
Cdd:cd16030  145 GGGPAWeaadvpdeaYPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVApkky 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 257 ---------------------------------------------TPPLAHPQRQSL---YRASLREMDSLVGQIKDKVD 288
Cdd:cd16030  203 fdlyplesiplpnpfdpidlpevawndlddlpkygdipalnpgdpKGPLPDEQARELrqaYYASVSYVDAQVGRVLDALE 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 289 -HVARENTLLWFTGDNGpWA--QKcelagsvgpffGLWQthqggsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSL 365
Cdd:cd16030  283 eLGLADNTIVVLWSDHG-WHlgEH-----------GHWG--------KHTLFEEATRVPLIIRAPGVTKPGKVTDALVEL 342
                        410       420       430
                 ....*....|....*....|....*....|
gi 568976097 366 LDIFPTVIALAGasLPPNRKFDGRDVSEVL 395
Cdd:cd16030  343 VDIYPTLAELAG--LPAPPCLEGKSLVPLL 370
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
402-522 5.24e-33

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 122.04  E-value: 5.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  402 GHRVLFHpNSGAAgeygaLQTVRLNHYKAFYITG-----GAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQKGSPEYQ 476
Cdd:pfam14707   2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568976097  477 EVLQQVTRALADVLQDI--ADDNSSRADYTQDPSVIPCCnPYQTTCRC 522
Cdd:pfam14707  76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-408 1.33e-30

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


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 121.16  E-value: 1.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDM-GWGDLGANWAETKdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGL 114
Cdd:cd16035    1 PNILLILTDQErYPPPWPAGWAALN-LPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 115 PVNETTLAEVLRQEGYVTAMIGKWHLGHHGsyhpnfrgfdyyfgipysndmgctdapgynyppcPACPQRDGLwrnpgrd 194
Cdd:cd16035   80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA----------------------------------GGGYKRDPG------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 195 cytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTS---GRPFLLYVGLAHMH-VPLSVTPPLAHPQRQSLYR 270
Cdd:cd16035  119 ----------------------------IAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYY 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 271 ASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSVGpffGLwqtHQGGSPTKQTTwegghRVPALAYW 349
Cdd:cd16035  171 NLIRDVDRQIGRVLDALDASGlADNTIVVFTSDHG------EMGGAHG---LR---GKGFNAYEEAL-----HVPLIISH 233
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568976097 350 PGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRK----FDGRDVSEVLFGKS--QMGHRVLFH 408
Cdd:cd16035  234 PDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATeappLPGRDLSPLLTDADadAVRDGILFT 298
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
35-393 1.09e-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: 117.86  E-value: 1.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGA-NWAETKD---------TTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:cd16153    1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 105 NFAVTSVG--GLPvnetTLAEVLRQEGYVTAMIGKWHLghhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacp 182
Cdd:cd16153   81 FEAAHPALdhGLP----TFPEVLKKAGYQTASFGKSHL------------------------------------------ 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 183 qrdglwrnpgrdcytdvalplyenlnivEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPlsVTPPLAH 262
Cdd:cd16153  115 ----------------------------EAFQRYLKNANQSYKSFWGKIAKGADSDKPFFVRLSFLQPHTP--VLPPKEF 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 263 PQRqSLYRASLREMDSLVGQIKDKVD----HVARENTLLWFTGDNGpwaqkcelagsvgpffglWQTHQGGSPTKQTTWE 338
Cdd:cd16153  165 RDR-FDYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWP 225
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568976097 339 GGHRVPALAYWPGR--VPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSE 393
Cdd:cd16153  226 QSHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
36-460 1.92e-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: 118.45  E-value: 1.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16032    1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 116 VNETTLAEVLRQEGYVTAMIGKWHL-G---HHGsyhpnfrgFDYyfgipysNDmgctdapgynyppcpacpqrdglwrnp 191
Cdd:cd16032   76 ADIPTFAHYLRAAGYRTALSGKMHFvGpdqLHG--------FDY-------DE--------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 192 grdcytDVALplyenlniveqpvnlsglaqkyaeRAVEFIEQASTS--GRPFLLYVGLAHMHVPLSVTPPL----AHPQR 265
Cdd:cd16032  114 ------EVAF------------------------KAVQKLYDLARGedGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRAR 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 266 QSLYrASLREMDSLVGQIKDKVDHV-ARENTLLWFTGDNGpwaqkcELAGSVGpffgLWQthqggsptKQTTWEGGHRVP 344
Cdd:cd16032  164 RAYY-GMVSYVDDKVGQLLDTLERTgLADDTIVIFTSDHG------DMLGERG----LWY--------KMSFFEGSARVP 224
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 345 ALAYWPG-----RVPANVtstallSLLDIFPTVIALAGASLPPNR-KFDGRDVSEVLFGKSQMGHRVLFhpnsgaaGEYG 418
Cdd:cd16032  225 LIISAPGrfaprRVAEPV------SLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVI-------SEYL 291
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 568976097 419 A------LQTVRLNHYKAFYItggakacdgsvgpeqHHVAPLIFNLED 460
Cdd:cd16032  292 AegavapCVMIRRGRWKFIYC---------------PGDPDQLFDLEA 324
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
36-376 1.18e-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: 105.20  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTHNFAVT----- 109
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 110 SVGGLPVNETTLAEVLRQEGYVTAMIGkwhlghhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacpqrdglwr 189
Cdd:cd00016   81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 190 npgrdcytdvalplyenlniveqpvnlsglaqkyaerAVEFIEQaSTSGRPFLLYVGLAHMHVPLSvtpplAHPQRQSLY 269
Cdd:cd00016  108 -------------------------------------LLKAIDE-TSKEKPFVLFLHFDGPDGPGH-----AYGPNTPEY 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 270 RASLREMDSLVGQIKDKVD--HVArENTLLWFTGDNGpwaqkcelagsvGPFFGLwqTHQGGSPTKQTTWEGGHRVPALA 347
Cdd:cd00016  145 YDAVEEIDERIGKVLDALKkaGDA-DDTVIIVTADHG------------GIDKGH--GGDPKADGKADKSHTGMRVPFIA 209
                        330       340
                 ....*....|....*....|....*....
gi 568976097 348 YWPGrVPANVTSTALLSLLDIFPTVIALA 376
Cdd:cd00016  210 YGPG-VKKGGVKHELISQYDIAPTLADLL 237
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
36-424 1.27e-23

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


Pssm-ID: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 103.62  E-value: 1.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG-VTHNFAVTSvggl 114
Cdd:cd16156    1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGsWTNCMALGD---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 115 pvNETTLAEVLRQEGYVTAMIGKWHLGhhgsyhpnfrGFDYY-FGI-P------YSNDMGC-----TDapgynyppcpac 181
Cdd:cd16156   77 --NVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGIcPqgwdpdYWYDMRNyldelTE------------ 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 182 pQRDGLWRNPgrdcytdvaLPLYENLNIVEQPVnlsgLAQKYAERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLA 261
Cdd:cd16156  133 -EERRKSRRG---------LTSLEAEGIKEEFT----YGHRCTNRALDFIEKHKD--EDFFLVVSYDEPHHPFLCPKPYA 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 262 ---------------------------------HPQRQS------LYRASLREMDSLVGQIKDKVDHVArENTLLWFTGD 302
Cdd:cd16156  197 smykdfefpkgenayddlenkplhqrlwagakpHEDGDKgtikhpLYFGCNSFVDYEIGRVLDAADEIA-EDAWVIYTSD 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 303 NGpwaqkcELAGSvgpfFGLWQthQGGSPTKQTTwegghRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPP 382
Cdd:cd16156  276 HG------DMLGA----HKLWA--KGPAVYDEIT-----NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPK 338
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568976097 383 nrKFDGRDVSEVLFGKSQMGHRVLF---------HPNsgaageYGALQTVR 424
Cdd:cd16156  339 --VLEGESILATIEDPEIPENRGVFvefgryevdHDG------FGGFQPVR 381
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
35-398 8.45e-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: 94.22  E-value: 8.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtsVGGL 114
Cdd:cd16152    1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 115 PVNETTLAEVLRQEGYVTAMIGKWHLGhhgsyhpnfrgfdyyfgipysndmgctdapGYnyppcpacpqrdglwrnpgR- 193
Cdd:cd16152   76 PADEKTLAHYFRDAGYETGYVGKWHLA------------------------------GY-------------------Rv 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 DCYTDvalplyenlniveqpvnlsglaqkyaeRAVEFIEQASTSgRPFLLYVGLAHMH---------VPLS--------V 256
Cdd:cd16152  107 DALTD---------------------------FAIDYLDNRQKD-KPFFLFLSYLEPHhqndrdryvAPEGsaerfanfW 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 257 TPPLAHPQ----RQSL--YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkCelagsvgpffglwqtHQGG 329
Cdd:cd16152  159 VPPDLAALpgdwAEELpdYLGCCERLDENVGRIRDALKELGlYDNTIIVFTSDHG-----C---------------HFRT 218
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568976097 330 SPT--KQTTWEGGHRVPALAYWPG-----RVPANVtstallSLLDIFPTVIALAGASLPPnrKFDGRDVSEVLFGK 398
Cdd:cd16152  219 RNAeyKRSCHESSIRVPLVIYGPGfngggRVEELV------SLIDLPPTLLDAAGIDVPE--EMQGRSLLPLVDGK 286
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
36-389 8.65e-20

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: 91.94  E-value: 8.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16028    1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 116 VNETTLAEVLRQEGYVTAMIGKWHlghhgsYHPNFRGFDyyfgipySND----MGCTDAPGYNyPPCPACPQRDGLwrnp 191
Cdd:cd16028   76 ARHLTLALELRKAGYDPALFGYTD------TSPDPRGLA-------PLDprllSYELAMPGFD-PVDRLDEYPAED---- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 192 grdcyTDVALplyenlniveqpvnlsglaqkYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPL-------------SVTP 258
Cdd:cd16028  138 -----SDTAF---------------------LTDRAIEYLD--ERQDEPWFLHLSYIRPHPPFvapapyhalydpaDVPP 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 259 PLAHPQRQS------LYRASLREMDSL------------------------VGQIKDKVDHVAR-----------ENTLL 297
Cdd:cd16028  190 PIRAESLAAeaaqhpLLAAFLERIESLsfspgaanaadlddeevaqmratyLGLIAEVDDHLGRlfdylketgqwDDTLI 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 298 WFTGDNGpwaqkcELAGsvgpffglwQTHQGGsptKQTTWEGGHRVPALAYWPGRvPANVTS----TALLSLLDIFPTVI 373
Cdd:cd16028  270 VFTSDHG------EQLG---------DHWLWG---KDGFFDQAYRVPLIVRDPRR-EADATRgqvvDAFTESVDVMPTIL 330
                        410
                 ....*....|....*.
gi 568976097 374 ALAGASLPPnrKFDGR 389
Cdd:cd16028  331 DWLGGEIPH--QCDGR 344
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
36-399 2.75e-19

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 89.99  E-value: 2.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRNgvTHNFavtsv 111
Cdd:cd16150    1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHRT--LHHL----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 112 ggLPVNETTLAEVLRQEGYVTAMIGKwhlghhgsyhpnfrgfdyyfgipysNDmgCTDAPgynyppcpacpqrdglwRNP 191
Cdd:cd16150   74 --LRPDEPNLLKTLKDAGYHVAWAGK-------------------------ND--DLPGE-----------------FAA 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 192 GRDCYTDVAlplyenlniveqpvnlsglaqkYAERAVEFIEQASTsGRPFLLYVGLAHMHVPLSVTPP------------ 259
Cdd:cd16150  108 EAYCDSDEA----------------------CVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPYGVEEPwfsmidreklpp 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 260 --------------LAHPQRQSLYRAS---LREM-----------DSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkc 310
Cdd:cd16150  165 rrppglrakgkpsmLEGIEKQGLDRWSeerWRELratylgmvsrlDHQFGRLLEALKETGlYDDTAVFFFSDHG------ 238
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 311 ELAGSvgpfFGLWQTHQGGSPTKQTtwegghRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPNRkfdgrd 390
Cdd:cd16150  239 DYTGD----YGLVEKWPNTFEDCLT------RVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAGIPLSHTH------ 301

                 ....*....
gi 568976097 391 vsevlFGKS 399
Cdd:cd16150  302 -----FGRS 305
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
36-463 1.06e-15

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


Pssm-ID: 293781 [Multi-domain]  Cd Length: 366  Bit Score: 78.74  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTHNFavTSVGGLP 115
Cdd:cd16171    1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 116 VNETTLAEVLRQEGYVTAMIGK--WHLGHHGsyhpnfrgfdyyfgipYSNDMgctDAPGYNYPpcpacpqrdGLWRNPGR 193
Cdd:cd16171   76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHS----------------VSNRV---EAWTRDVP---------FLLRQEGR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 194 DCytdvalplyENLNIVEQPVNLSGLAQKYAERAVEFIEQASTS-GRPFLLYVGLAhmhvplsvtppLAHPQR------- 265
Cdd:cd16171  128 PT---------VNLVGDRSTVRVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLN-----------LPHPYPspsmgen 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 266 -------QSLYRASLREMDSLVGQIKDKV-DHVARENTLLWFTGDNGpwaqkcELAGSVGPFFglwqthqggsptKQTTW 337
Cdd:cd16171  188 fgsirniRAFYYAMCAETDAMLGEIISALkDTGLLDKTYVFFTSDHG------ELAMEHRQFY------------KMSMY 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 338 EGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKS-QMGHRVLFHPNSGAAGE 416
Cdd:cd16171  250 EGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSiKESPSRVPHPDWVLSEF 326
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568976097 417 YG-----ALQTVRLNHYKafYITGGakacDGSvgpeqhHVAPLIFNLEDAAD 463
Cdd:cd16171  327 HGcnvnaSTYMLRTNSWK--YIAYA----DGN------SVPPQLFDLSKDPD 366
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
28-391 1.45e-13

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 73.15  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  28 SGKTRAPQPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVthnfA 107
Cdd:COG1368  227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 108 VTSVGGLPVNetTLAEVLRQEGYVTAMIgkwHlGHHGS------YHPNFrGFDYYFGIpysNDMGctdapgynyppcpac 181
Cdd:COG1368  303 YKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDR---EDFD--------------- 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 182 PQRDGLWRnpgrdcYTDvaLPLYEnlniveqpvnlsglaqkyaeravEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLA 261
Cdd:COG1368  358 DPFDGGWG------VSD--EDLFD-----------------------KALEELEKLKKPFFAFLITLSNHGPYTLPEEDK 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 262 H-----PQRQSLYRASLREMDSLVGQIKDKVDHVAR-ENTLLWFTGDngpwaqkcelagsvgpffglwqtHQGGSPTKQT 335
Cdd:COG1368  407 KipdygKTTLNNYLNAVRYADQALGEFIEKLKKSGWyDNTIFVIYGD-----------------------HGPRSPGKTD 463
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568976097 336 TWE--GGHRVPALAYWPGRVPANVTSTaLLSLLDIFPTVIALAGASLPPNRKFdGRDV 391
Cdd:COG1368  464 YENplERYRVPLLIYSPGLKKPKVIDT-VGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
13-304 6.33e-08

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 54.75  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  13 MAFSGFFYPLVDFSISGKTRAPQPNIVIILADDMGWGDLGANwaetkDTTNLDKMASEGMRFVDFHAA--ASTCsPSRAS 90
Cdd:COG1524    1 MKRGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  91 LLTGRLGLRNGVTHNFAVTSVGGLPVNE----------------TTLAEVLRQEGYVTAMIGKWHLGHHGSYHPN----F 150
Cdd:COG1524   75 LLTGLYPGEHGIVGNGWYDPELGRVVNSlswvedgfgsnsllpvPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 151 RGFDYYFGIPYSNdmgctdapgynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqpvnlsglaqkyaERAVEF 230
Cdd:COG1524  155 DGRKPLLGNPAAD-------------------------------------------------------------RWIAAA 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 231 IEQASTSGRPFLLYVGL------AHMHVPLSvtpplahPQrqslYRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDN 303
Cdd:COG1524  174 ALELLREGRPDLLLVYLpdldyaGHRYGPDS-------PE----YRAALREVDAALGRLLDALKaRGLYEGTLVIVTADH 242

                 .
gi 568976097 304 G 304
Cdd:COG1524  243 G 243
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
36-377 1.48e-07

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


Pssm-ID: 293739 [Multi-domain]  Cd Length: 283  Bit Score: 53.07  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097  36 PNIVIILADdmGWGDLGANW-AETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRA--SLLTGRLGLRNGvthnfAVTSV 111
Cdd:cd16015    1 PNVIVILLE--SFSDPYIDKdVGGEDLTpNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLG-----SGSYT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 112 GGLPVNETTLAEVLRQEGYVTAMIgkwHlGHHGS------YHPNFrGFDYYFGIpysNDMGCTDapgynyppcpacPQRD 185
Cdd:cd16015   74 LYKLNPLPSLPSILKEQGYETIFI---H-GGDASfynrdsVYPNL-GFDEFYDL---EDFPDDE------------KETN 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 186 GLWrnpgrdcYTDVALplyenlniveqpvnlsglaqkyAERAVEFIEqaSTSGRPFLLYVGLAHMHVPLSV--------T 257
Cdd:cd16015  134 GWG-------VSDESL----------------------FDQALEELE--ELKKKPFFIFLVTMSNHGPYDLpeekkdepL 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976097 258 PPLAHPQRQSLYRASLREMDSLVGQIKDKVDHV-ARENTLLWFTGDngpwaqkcelagsvgpffglwqtHQGGSPTKQTT 336
Cdd:cd16015  183 KVEEDKTELENYLNAIHYTDKALGEFIEKLKKSgLYENTIIVIYGD-----------------------HLPSLGSDYDE 239
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 568976097 337 WEGG----HRVPALAYWPGRVPANVTSTaLLSLLDIFPTVIALAG 377
Cdd:cd16015  240 TDEDpldlYRTPLLIYSPGLKKPKKIDR-VGSQIDIAPTLLDLLG 283
 
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