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Conserved domains on  [gi|1444497654|ref|XP_025925092|]
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steryl-sulfatase isoform X1 [Apteryx rowi]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 10888433)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
25-548 0e+00

Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.


:

Pssm-ID: 293778 [Multi-domain]  Cd Length: 521  Bit Score: 856.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFSA 104
Cdd:cd16159     2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHHPLSHGFDYFYGLTMTNLRDCKLGQGSVFLKGTEKSI 184
Cdd:cd16159    82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPLF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 VTSIQIFGITLLSLATVHFIGFlkVPFQALGYCLLITAILLVVLLFFFYNFRYLNCFLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16159   162 PLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 344
Cdd:cd16159   240 EAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 345 VEEISSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRIIDGHDL 424
Cdd:cd16159   320 LEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 425 MPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPRNSESIWKVFFFTPNFNPEdSNGCHDSHVCFCYGSFITRHDPPLLFDLS 504
Cdd:cd16159   400 MPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPG-TEGCCGTLLCRCFGDSVTHHDPPLLFDLS 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1444497654 505 RDPEEKVPLTPETEsRFYEVLHVILRAVDNHTKSLHAVPDQLSW 548
Cdd:cd16159   479 ADPSESNPLDPTDE-PYQEIIKKILEAVAEHQSSIEPVESQLSF 521
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
25-548 0e+00

Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.


Pssm-ID: 293778 [Multi-domain]  Cd Length: 521  Bit Score: 856.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFSA 104
Cdd:cd16159     2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHHPLSHGFDYFYGLTMTNLRDCKLGQGSVFLKGTEKSI 184
Cdd:cd16159    82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPLF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 VTSIQIFGITLLSLATVHFIGFlkVPFQALGYCLLITAILLVVLLFFFYNFRYLNCFLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16159   162 PLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 344
Cdd:cd16159   240 EAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 345 VEEISSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRIIDGHDL 424
Cdd:cd16159   320 LEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 425 MPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPRNSESIWKVFFFTPNFNPEdSNGCHDSHVCFCYGSFITRHDPPLLFDLS 504
Cdd:cd16159   400 MPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPG-TEGCCGTLLCRCFGDSVTHHDPPLLFDLS 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1444497654 505 RDPEEKVPLTPETEsRFYEVLHVILRAVDNHTKSLHAVPDQLSW 548
Cdd:cd16159   479 ADPSESNPLDPTDE-PYQEIIKKILEAVAEHQSSIEPVESQLSF 521
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
1-533 3.41e-105

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 322.21  E-value: 3.41e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654   1 MRLLSFLIICqCAIKSLSSHSASNPNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAF 80
Cdd:COG3119     1 MKRLLLLLLA-LLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  81 LTGRYPIRSGMAaysrvgvFLFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLgmncessndfchhplshgfdyfygl 160
Cdd:COG3119    80 LTGRYPHRTGVT-------DNGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 161 tmtnlrdcklgqgsvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylnc 240
Cdd:COG3119       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 241 flmrnhqiiqqplsyeNLTQRLTKEAVQFIGRNT--DAPFLLILSYLHVHTALYASKNFIGK------------------ 300
Cdd:COG3119   128 ----------------YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlt 191
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 301 -----SKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVEEisssgevHGgyngiYKGGKSMNWEGGIR 375
Cdd:COG3119   192 eeelrRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGE-------HG-----LRGGKGTLYEGGIR 259
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 376 VPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLN-AVRWH 454
Cdd:COG3119   260 VPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNrAIRTG 337
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 455 PrnsesiWK-VFFFTPNfnpedsngchdshvcfcygsfitrhDPPLLFDLSRDPEEKVPL---TPETESRFYEVLHVILR 530
Cdd:COG3119   338 R------WKlIRYYDDD-------------------------GPWELYDLKNDPGETNNLaadYPEVVAELRALLEAWLK 386

                  ...
gi 1444497654 531 AVD 533
Cdd:COG3119   387 ELG 389
Sulfatase pfam00884
Sulfatase;
25-411 1.31e-66

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 218.83  E-value: 1.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVgvflfsa 104
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 ssgGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSndfchhPLSHGFDYFYGL--TMTNLRDCKlgqgsvflkgtek 182
Cdd:pfam00884  74 ---GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFGRntGSDLYADPP------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 183 sivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRYLNCflmrnhqiiqqplsyenLTQRL 262
Cdd:pfam00884 132 -----------------------------------------------DVPYNCSGGGV-----------------SDEAL 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 263 TKEAVQFIGRNTDaPFLLILSYLHVHTALYASKNFIGKSK------------HGLYGDAVEEMDWSVGRILDVLEKSNLN 330
Cdd:pfam00884 148 LDEALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLL 226
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 331 NKTLVYFTSDQGAHVEEisssgevhggYNGIYKGGKSMN-WEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLA 409
Cdd:pfam00884 227 DNTLVVYTSDHGESLGE----------GGGYLHGGKYDNaPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLA 296

                  ..
gi 1444497654 410 GA 411
Cdd:pfam00884 297 GI 298
PRK13759 PRK13759
arylsulfatase; Provisional
25-509 1.72e-35

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 139.42  E-value: 1.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGiGD-LGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFs 103
Cdd:PRK13759    7 PNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPWNY- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 104 assgglpseEITFSKLLKQRGYSTALIGKWHLgmncessndfchHP--LSHGFDYfygltmTNLRDCKLGQGSVFLKGTE 181
Cdd:PRK13759   85 ---------KNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHDGYLHSGRNEDKSQF 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 182 KSIVTSIQIFGItllslatvhfigflkvpfQALGYCLLITAIllvvllfffynfrYLNCflmrnHQIIQQPLSY-ENL-- 258
Cdd:PRK13759  138 DFVSDYLAWLRE------------------KAPGKDPDLTDI-------------GWDC-----NSWVARPWDLeERLhp 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 259 TQRLTKEAVQFI-GRNTDAPFLLILSYLHVH------------------------------------TALYASKNFIGK- 300
Cdd:PRK13759  182 TNWVGSESIEFLrRRDPTKPFFLKMSFARPHspydppkryfdmykdadipdphigdweyaedqdpegGSIDALRGNLGEe 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 301 ----SKHGLYGDaVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDqgaHveeisssGEVHGGYngiYKGGKSMNWEGGIRV 376
Cdd:PRK13759  262 yarrARAAYYGL-ITHIDHQIGRFLQALKEFGLLDNTIILFVSD---H-------GDMLGDH---YLFRKGYPYEGSAHI 327
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 377 PGLLLWPG---VIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKiiqskheflfhycnaylnavrw 453
Cdd:PRK13759  328 PFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ---------------------- 383
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1444497654 454 hprnsESIWKVFFFTPNFNPEDSNgcH---DSHVCFCYGSFITRHDpplLFDLSRDPEE 509
Cdd:PRK13759  384 -----YEGWRPYLHGEHALGYSSD--NyltDGKWKYIWFSQTGEEQ---LFDLKKDPHE 432
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
25-548 0e+00

Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.


Pssm-ID: 293778 [Multi-domain]  Cd Length: 521  Bit Score: 856.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFSA 104
Cdd:cd16159     2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHHPLSHGFDYFYGLTMTNLRDCKLGQGSVFLKGTEKSI 184
Cdd:cd16159    82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPLF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 VTSIQIFGITLLSLATVHFIGFlkVPFQALGYCLLITAILLVVLLFFFYNFRYLNCFLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16159   162 PLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 344
Cdd:cd16159   240 EAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 345 VEEISSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRIIDGHDL 424
Cdd:cd16159   320 LEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 425 MPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPRNSESIWKVFFFTPNFNPEdSNGCHDSHVCFCYGSFITRHDPPLLFDLS 504
Cdd:cd16159   400 MPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPG-TEGCCGTLLCRCFGDSVTHHDPPLLFDLS 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1444497654 505 RDPEEKVPLTPETEsRFYEVLHVILRAVDNHTKSLHAVPDQLSW 548
Cdd:cd16159   479 ADPSESNPLDPTDE-PYQEIIKKILEAVAEHQSSIEPVESQLSF 521
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
25-514 0e+00

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: 526.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAaysrvGVFLFSA 104
Cdd:cd16026     2 PNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLP-----GVVGPPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGLTMTNLRDCKLGQGsvflkgteksi 184
Cdd:cd16026    77 SKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQ------PEFLPTRHGFDEYFGIPYSNDMWPFPLYR----------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffYNFRYLNCFLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16026   140 ------------------------------------------------NDPPGPLPPLMENEEVIEQPADQSSLTQRYTD 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 344
Cdd:cd16026   172 EAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPW 251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 345 VEEISssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRIIDGHDL 424
Cdd:cd16026   252 LEYGG-----HGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDI 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 425 MPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTPNFNPEDSngchdshvcfcYGSFITRHDPPLLFDLS 504
Cdd:cd16026   327 SPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDP-----------GGLDPTKLEPPLLYDLE 389
                         490
                  ....*....|
gi 1444497654 505 RDPEEKVPLT 514
Cdd:cd16026   390 EDPGETYNVA 399
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
25-528 2.30e-146

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: 429.93  E-value: 2.30e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaYSRVGVFLFSa 104
Cdd:cd16160     2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGM--YGGTRVFLPW- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHHPLSHGFDyFYGltmTNLRdcklgqgsvflkgteksi 184
Cdd:cd16160    79 DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVG---TNLP------------------ 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqiFGITLLSLATVHFIGFlkvPFQALgycllitaillvvllfffynfrylnCFLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16160   137 ------FTNSWACDDTGRHVDF---PDRSA-------------------------CFLYYNDTIVEQPIQHEHLTETLVG 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 344
Cdd:cd16160   183 DAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPH 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 345 VEEISssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYiDEPTSNMDIFPTVIKLAGAQLPCDRIIDGHDL 424
Cdd:cd16160   263 VEYCL-----EGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVS-HEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSI 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 425 MPLLQGKiIQSKHEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTPNFNPEDSN------GCHDSH--VC-FCYGSFITRH 495
Cdd:cd16160   337 TDLLLGE-ADSPHDDILYYCCSRLMAVRYGS------YKIHFKTQPLPSQESLdpncdgGGPLSDyiVCyDCEDECVTKH 409
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1444497654 496 DPPLLFDLSRDPEEKVPLTPET-ESRFYEVLHVI 528
Cdd:cd16160   410 NPPLIFDVEKDPGEQYPLQPSVyEHMLEAVEKLI 443
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
25-561 1.39e-108

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: 334.03  E-value: 1.39e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAysrvGVFlFSA 104
Cdd:cd16158     2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYP----GVF-YPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSndfcHHPLSHGFDYFYGltmtnlrdcklgqgsvflkgteksi 184
Cdd:cd16158    77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLG------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqifgitllslatvhfigflkVPF-QALGYCLLITAILLVVLLFFFYNFRYLNCFLMRNHQIIQQPLSYENLTQRLT 263
Cdd:cd16158   128 ------------------------IPYsHDQGPCQNLTCFPPNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 264 KEAVQFIGRNT--DAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQ 341
Cdd:cd16158   184 KFAKDFIADNAkeGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDN 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 342 GAhveeiSSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIdEPTSNMDIFPTVIKLAGAQLPcDRIIDG 421
Cdd:cd16158   264 GP-----STMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDG 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 422 HDLMPLL--QGKiiqSKHEFLFHY-----CNAYLNAVRWHPrnsesiWKVFFFT---PNFNPEDSNGCHDShvcfcygSF 491
Cdd:cd16158   337 VDMSPILfeQGK---SPRQTFFYYptspdPDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCHPS-------AE 400
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444497654 492 ITRHDPPLLFDLSRDPEEKVPL--TPEtesrFYEVLHVILRAVDNHTKSLHAVPDQLSWDNllwKPWLQPCC 561
Cdd:cd16158   401 LTSHDPPLLFDLSQDPSENYNLlgLPE----YNQVLKQIQQVKERFEASMKFGESEINKGE---DPALEPCC 465
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
25-510 3.65e-107

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: 328.35  E-value: 3.65e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFSA 104
Cdd:cd16144     1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 -------SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGltmtnlrDCKLGQGSVFl 177
Cdd:cd16144    81 tklipppSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVNIG-------GTGNGGPPSY- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 178 kgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRYLNcflmrnhqiIQQPLSYEN 257
Cdd:cd16144   147 ----------------------------------------------------YFPPGKPNPD---------LEDGPEGEY 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 258 LTQRLTKEAVQFIGRNTDAPFLLILSYLHVHTALYASKNFI-----------GKSKHGLYGDAVEEMDWSVGRILDVLEK 326
Cdd:cd16144   166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIekyekkkkglrKGQKNPVYAAMIESLDESVGRILDALEE 245
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 327 SNLNNKTLVYFTSDQGAHveeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVI 406
Cdd:cd16144   246 LGLADNTLVIFTSDNGGL-----STRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFL 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 407 KLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNavrwHPRNSESI-----WK-VFFFtpnfnpedsngcH 480
Cdd:cd16144   321 ELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWHFPHYHG----QGGRPASAirkgdWKlIEFY------------E 384
                         490       500       510
                  ....*....|....*....|....*....|
gi 1444497654 481 DSHVcfcygsfitrhdppLLFDLSRDPEEK 510
Cdd:cd16144   385 DGRV--------------ELYNLKNDIGET 400
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
25-548 7.12e-106

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293776 [Multi-domain]  Cd Length: 466  Bit Score: 326.73  E-value: 7.12e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGM---AAYSRVGvFL 101
Cdd:cd16157     2 PNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFyttNAHARNA-YT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 102 FSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCEssndfcHHPLSHGFDYFYGLTmtnlrDCKLGQgsvflkgte 181
Cdd:cd16157    81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGP--------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 182 ksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNCFLMRNHQIIQQplSYE----- 256
Cdd:cd16157   141 --------------------------------------------------YDNKAYPNIPVYRDWEMIGR--YYEefkid 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 257 ------NLTQRLTKEAVQFIGR--NTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSN 328
Cdd:cd16157   169 kktgesNLTQIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLG 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 329 LNNKTLVYFTSDQGAHVeeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKL 408
Cdd:cd16157   249 IENNTFVFFSSDNGAAL----ISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLAL 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 409 AGAQLPCDRIIDGHDLMP-LLQGKIIQSKHeflFHYCNAYLNAVRwhprnsESIWKVFFFT-PNFNPEDSNGCHdshvcF 486
Cdd:cd16157   325 AGLPIPSDRAIDGIDLLPvLLNGKEKDRPI---FYYRGDELMAVR------LGQYKAHFWTwSNSWEEFRKGIN-----F 390
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444497654 487 CYGSFI---TRH------DPPLLFDLSRDPEEKVPLTPETeSRFYEVLHVILRAVDNHTKSLHAVPDQLSW 548
Cdd:cd16157   391 CPGQNVpgvTTHnqtdhtKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLNV 460
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
1-533 3.41e-105

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 322.21  E-value: 3.41e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654   1 MRLLSFLIICqCAIKSLSSHSASNPNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAF 80
Cdd:COG3119     1 MKRLLLLLLA-LLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  81 LTGRYPIRSGMAaysrvgvFLFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLgmncessndfchhplshgfdyfygl 160
Cdd:COG3119    80 LTGRYPHRTGVT-------DNGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 161 tmtnlrdcklgqgsvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylnc 240
Cdd:COG3119       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 241 flmrnhqiiqqplsyeNLTQRLTKEAVQFIGRNT--DAPFLLILSYLHVHTALYASKNFIGK------------------ 300
Cdd:COG3119   128 ----------------YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlt 191
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 301 -----SKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVEEisssgevHGgyngiYKGGKSMNWEGGIR 375
Cdd:COG3119   192 eeelrRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGE-------HG-----LRGGKGTLYEGGIR 259
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 376 VPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLN-AVRWH 454
Cdd:COG3119   260 VPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNrAIRTG 337
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 455 PrnsesiWK-VFFFTPNfnpedsngchdshvcfcygsfitrhDPPLLFDLSRDPEEKVPL---TPETESRFYEVLHVILR 530
Cdd:COG3119   338 R------WKlIRYYDDD-------------------------GPWELYDLKNDPGETNNLaadYPEVVAELRALLEAWLK 386

                  ...
gi 1444497654 531 AVD 533
Cdd:COG3119   387 ELG 389
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
25-514 9.89e-102

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: 313.25  E-value: 9.89e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLR-TPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAaysrvGVFLfS 103
Cdd:cd16161     2 PNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVG-----HNFL-P 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 104 ASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcESsndfcHHPLSHGFDYFYGLtmtnlrdcklgqgsvflkgteks 183
Cdd:cd16161    76 TSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR-EA-----YLPNSRGFDYYFGI----------------------- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 184 ivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqPLSYE-NLTQRL 262
Cdd:cd16161   127 --------------------------------------------------------------------PFSHDsSLADRY 138
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 263 TKEAVQFIGRNTDA--PFLLILSYLHVHTAL-YASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTS 339
Cdd:cd16161   139 AQFATDFIQRASAKdrPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTS 218
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 340 DQGAHVEEISSSGEVHGGY---NGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCD 416
Cdd:cd16161   219 DNGPWEVKCELAVGPGTGDwqgNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPG 298
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 417 RIIDGHDLMPLLQGKiIQSKHEFLFHYCNAY-----LNAVRWHPrnsesiWKVFFFTPNFNPEDSNGCHDSHvcfcygsf 491
Cdd:cd16161   299 RIYDGKDLSPVLFGG-SKTGHRCLFHPNSGAagagaLSAVRCGD------YKAHYATGGALACCGSTGPKLY-------- 363
                         490       500
                  ....*....|....*....|...
gi 1444497654 492 itrHDPPLLFDLSRDPEEKVPLT 514
Cdd:cd16161   364 ---HDPPLLFDLEVDPAESFPLT 383
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
25-514 2.47e-98

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: 303.69  E-value: 2.47e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYG---NRTLRTPNIDRLAKEGVTLTQHIAaSPLCTPSRAAFLTGRYPIRSGMaaySRVGvfl 101
Cdd:cd16142     1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTGL---TTVG--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 102 FSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCEssndfcHHPLSHGFDYFYGltmtnlrdcklgqgsvflkgte 181
Cdd:cd16142    74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG------RLPTDHGFDEFYG---------------------- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 182 ksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfFFYNFrylncflmrnhqiiqqplsyenLTQR 261
Cdd:cd16142   126 -------------------------------------------------NLYHT----------------------IDEE 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 262 LTKEAVQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSK-HGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFT 338
Cdd:cd16142   135 IVDKAIDFIKRNakADKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 339 SDQGAHVEEISSSGevhggyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLP---- 414
Cdd:cd16142   215 TDNGPEQDVWPDGG------YTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkl 288
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 415 --CDRIIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTpnfnpEDSNGCHDSHVcFCYGSFi 492
Cdd:cd16142   289 lgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFKA-----QEDTGGPTGEP-FYVLTF- 355
                         490       500
                  ....*....|....*....|..
gi 1444497654 493 trhdpPLLFDLSRDPEEKVPLT 514
Cdd:cd16142   356 -----PLIFNLRRDPKERYDVT 372
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
25-510 1.00e-96

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


Pssm-ID: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 300.66  E-value: 1.00e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYG-NRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSgmaaYSRVGVFLFS 103
Cdd:cd16143     1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRS----RLKGGVLGGF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 104 ASSGgLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHH----------------PLSHGFDYFYGLTMTNLRD 167
Cdd:cd16143    77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIPASEVLP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 168 cklgqgsvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhq 247
Cdd:cd16143       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 248 iiqqplsyenltqRLTKEAVQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLE 325
Cdd:cd16143   156 -------------TLTDKAVEFIDQHakKDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 326 KSNLNNKTLVYFTSDQGAHVEEISSSGEVHGGY-NGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPT 404
Cdd:cd16143   223 ELGLAENTLVIFTSDNGPSPYADYKELEKFGHDpSGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFAT 302
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 405 VIKLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNAVRwhprnsESIWKVFFftpnfnpedsngCHDSHV 484
Cdd:cd16143   303 LAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIR------KGDWKLID------------GTGSGG 364
                         490       500
                  ....*....|....*....|....*..
gi 1444497654 485 CFCYGSFITRHDPP-LLFDLSRDPEEK 510
Cdd:cd16143   365 FSYPRGKEKLGLPPgQLYNLSTDPGES 391
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
25-510 9.69e-89

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: 280.21  E-value: 9.69e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQ-HiaASPLCTPSRAAFLTGRYPIRSGmaaysrvgvfLFS 103
Cdd:cd16146     1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTG----------VWH 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 104 ASSGG--LPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGltmtnlrdckLGQGSVflkgte 181
Cdd:cd16146    69 TILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLG----------HGGGGI------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 182 ksivtsIQIFGitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNCFLMRNHQIIQqplsYEN-LTQ 260
Cdd:cd16146   127 ------GQYPD---------------------------------------YWGNDYFDDTYYHNGKFVK----TEGyCTD 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 261 RLTKEAVQFIGRNTDAPFLLILSYLHVHTALYA----SKNFIGKSKH----GLYGdAVEEMDWSVGRILDVLEKSNLNNK 332
Cdd:cd16146   158 VFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVpdkyLDPYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEEN 236
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 333 TLVYFTSDQGahveeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQ 412
Cdd:cd16146   237 TIVIFMSDNG-------PAGGVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVK 309
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 413 LPCDRIIDGHDLMPLLQGKIIQSKHEFLF-HYCNAYLNAVRWHP---RNSEsiWKVffftpnFNPEDsngchdshvcfcy 488
Cdd:cd16146   310 LPEGIKLDGRSLLPLLKGESDPWPERTLFtHSGRWPPPPKKKRNaavRTGR--WRL------VSPKG------------- 368
                         490       500
                  ....*....|....*....|..
gi 1444497654 489 gsfitrhDPPLLFDLSRDPEEK 510
Cdd:cd16146   369 -------FQPELYDIENDPGEE 383
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
25-510 1.58e-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: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 272.16  E-value: 1.58e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLfsa 104
Cdd:cd16145     1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQD--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 ssgGLPSEEITFSKLLKQRGYSTALIGKWHLGmnCESSNDfchHPLSHGFDYFYGltmtnlrdcklgqgsvFLKgteksi 184
Cdd:cd16145    78 ---PLPPDDVTLAEVLKKAGYATAAFGKWGLG--GPGTPG---HPTKQGFDYFYG----------------YLD------ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiQIFGitllslatvHFigflkvpfqalgycllitaillvvllFFFYnfrylncFLMRNHQIIQQPLSYENL------ 258
Cdd:cd16145   128 ----QVHA---------HN--------------------------YYPE-------YLWRNGEKVPLPNNVIPPldegnn 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 259 ---------TQRLTKEAVQFIGRNTDAPFLLILSYL---------HVHTALYASKNFIGKSKHGL------YGDAVEEMD 314
Cdd:cd16145   162 agggggtysHDLFTDEALDFIRENKDKPFFLYLAYTlphaplqvpDDGPYKYKPKDPGIYAYLPWpqpekaYAAMVTRLD 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 315 WSVGRILDVLEKSNLNNKTLVYFTSDQGAHVE-EISSSGEVHGGyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYID 393
Cdd:cd16145   242 RDVGRILALLKELGIDENTLVVFTSDNGPHSEgGSEHDPDFFDS-NGPLRGYKRSLYEGGIRVPFIARWPGKIPAGSVSD 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 394 EPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLF--HYCNAYLNAVRWHPrnsesiWKVFfftpNF 471
Cdd:cd16145   321 HPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLYweFYEGGGAQAVRMGG------WKAV----RH 388
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1444497654 472 NPEDsngchdshvcfcygsfitrhDPPLLFDLSRDPEEK 510
Cdd:cd16145   389 GKKD--------------------GPFELYDLSTDPGET 407
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
25-423 2.00e-77

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: 244.65  E-value: 2.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFLFSA 104
Cdd:cd16022     1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYP--------HRHGVRGNVG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHlgmncessndfchhplshgfdyfygltmtnlrdcklgqgsvflkgteksi 184
Cdd:cd16022    73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenltqrltK 264
Cdd:cd16022   103 -------------------------------------------------------------------------------D 103
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRN-TDAPFLLILSYLHVHTALYasknfigkskhglYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGA 343
Cdd:cd16022   104 EAIDFIERRdKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 344 HVEEisssgevHGGyngiyKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHD 423
Cdd:cd16022   171 MLGD-------HGL-----RGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
25-513 2.44e-75

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: 244.77  E-value: 2.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAAsPLCTPSRAAFLTGRYPIRSGMaaYSRVgvfLFSA 104
Cdd:cd16029     1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGM--QHGV---ILAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMnceSSNDFChhPLSHGFDYFYGltmtnlrdcklgqgsvFLKGTEksi 184
Cdd:cd16029    75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLGF---YTWEYT--PTNRGFDSFYG----------------YYGGAE--- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfFFYNFR------YLNCFLMRNHQIiqqPLSYEN- 257
Cdd:cd16029   131 ----------------------------------------------DYYTHTsggandYGNDDLRDNEEP---AWDYNGt 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 258 -LTQRLTKEAVQFIGR-NTDAPFLLILSYLHVHTALYASKNFI----GKSKHGLYGD------AVEEMDWSVGRILDVLE 325
Cdd:cd16029   162 ySTDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYAdpyeDKFAHIKDEDrrtyaaMVSALDESVGNVVDALK 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 326 KSNLNNKTLVYFTSDQGAHVeeisssGEVHGGYNGIYKGGKSMNWEGGIRVPGlLLWPGVI--QAGTYIDEPTSNMDIFP 403
Cdd:cd16029   242 AKGMLDNTLIVFTSDNGGPT------GGGDGGSNYPLRGGKNTLWEGGVRVPA-FVWSPLLppKRGTVSDGLMHVTDWLP 314
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 404 TVIKLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFL----FHYCNAYLNAVRWHPrnsesiWKVFFFTPnfnpedsngc 479
Cdd:cd16029   315 TLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILlnidDITRTTGGAAIRVGD------WKLIVGKP---------- 378
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1444497654 480 hdshvcfcygsfitrhdpplLFDLSRDPEEKVPL 513
Cdd:cd16029   379 --------------------LFNIENDPCERNDL 392
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-513 4.61e-69

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: 227.87  E-value: 4.61e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTqHIAASPLCTPSRAAFLTGRYPIRSGMaaysrvgVFlfsa 104
Cdd:cd16151     1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYV-------VF---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 ssGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNdfchHPLSHGFDYFYGLTMTNLRDCKLGQGSV-FLKGTEKS 183
Cdd:cd16151    69 --GYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYCLWQLTETGEKYSRPATPtFNIRNGKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 184 IVTSIQIFGITLLSlatvhfigflkvpfqalgycllitaillvvllfffynfRYLNcflmrnhqiiqqplsyenltqrlt 263
Cdd:cd16151   143 LETTEGDYGPDLFA--------------------------------------DFLI------------------------ 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 264 keavQFIGRNTDAPFLLILSYLHVHT----------ALYASKNFIGKSKHglYGDAVEEMDWSVGRILDVLEKSNLNNKT 333
Cdd:cd16151   161 ----DFIERNKDQPFFAYYPMVLVHDpfvptpdspdWDPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENT 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 334 LVYFTSDQGAHveeisssGEVHGGYNG-IYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQ 412
Cdd:cd16151   235 IIIFTGDNGTH-------RPITSRTNGrEVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAP 307
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 413 LPCDRIIDGHDLMPLLQGKIIQSKHEFLFhycnaylnavrWHPRNSESIW-KVFFFTPNFNpedsngchdshvcfcygsf 491
Cdd:cd16151   308 LPEDYPLDGRSFAPQLLGKTGSPRREWIY-----------WYYRNPHKKFgSRFVRTKRYK------------------- 357
                         490       500
                  ....*....|....*....|..
gi 1444497654 492 itRHDPPLLFDLSRDPEEKVPL 513
Cdd:cd16151   358 --LYADGRFFDLREDPLEKNPL 377
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-513 1.81e-67

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: 224.37  E-value: 1.81e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVgvflfsa 104
Cdd:cd16034     2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 ssggLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHH----PLSHGFDYFYGltmtnlrdcklgqgsvflkgt 180
Cdd:cd16034    75 ----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKG--------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 181 eksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNfRYLNCFLMRNHQIIQQPLSYEnlTQ 260
Cdd:cd16034   130 -------------------------------------------------YECNH-DHNNPHYYDDDGKRIYIKGYS--PD 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 261 RLTKEAVQFIGR--NTDAPFLLILSYLHVHT----------ALYASKN---------------FIGKSKHGLYGdAVEEM 313
Cdd:cd16034   158 AETDLAIEYLENqaDKDKPFALVLSWNPPHDpyttapeeylDMYDPKKlllrpnvpedkkeeaGLREDLRGYYA-MITAL 236
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 314 DWSVGRILDVLEKSNLNNKTLVYFTSDqgaHveeisssGEVHGGYNGIYKGgksmNW-EGGIRVPGLLLWPGVIQAGTYI 392
Cdd:cd16034   237 DDNIGRLLDALKELGLLENTIVVFTSD---H-------GDMLGSHGLMNKQ----VPyEESIRVPFIIRYPGKIKAGRVV 302
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 393 DEPTSNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQGKIIQSKHEFLFhYCNAYLNavrWHPRNSESIWKvffftpnfn 472
Cdd:cd16034   303 DLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLL-QCFVPFG---GGSARDGGEWR--------- 367
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1444497654 473 pedsnGCHDSHVCFCygsfITRHDPPLLFDLSRDPEEKVPL 513
Cdd:cd16034   368 -----GVRTDRYTYV----RDKNGPWLLFDNEKDPYQLNNL 399
Sulfatase pfam00884
Sulfatase;
25-411 1.31e-66

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 218.83  E-value: 1.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVgvflfsa 104
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 ssgGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSndfchhPLSHGFDYFYGL--TMTNLRDCKlgqgsvflkgtek 182
Cdd:pfam00884  74 ---GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFGRntGSDLYADPP------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 183 sivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRYLNCflmrnhqiiqqplsyenLTQRL 262
Cdd:pfam00884 132 -----------------------------------------------DVPYNCSGGGV-----------------SDEAL 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 263 TKEAVQFIGRNTDaPFLLILSYLHVHTALYASKNFIGKSK------------HGLYGDAVEEMDWSVGRILDVLEKSNLN 330
Cdd:pfam00884 148 LDEALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLL 226
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 331 NKTLVYFTSDQGAHVEEisssgevhggYNGIYKGGKSMN-WEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLA 409
Cdd:pfam00884 227 DNTLVVYTSDHGESLGE----------GGGYLHGGKYDNaPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLA 296

                  ..
gi 1444497654 410 GA 411
Cdd:pfam00884 297 GI 298
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
25-511 1.07e-64

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: 217.78  E-value: 1.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaysrvgVFLFSA 104
Cdd:cd16031     3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGV-------TDNNGP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SsggLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndfcHHPLSHGFDYFYGLTmtnlrdcklGQGSvflkgteksi 184
Cdd:cd16031    76 L---FDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSFP---------GQGS---------- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrYLNCFLMRNHQIIQQplsYENLTQRLTK 264
Cdd:cd16031   126 ----------------------------------------------------YYDPEFIENGKRVGQ---KGYVTDIITD 150
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRNTDA-PFLLILSYLHVHT--------------------ALYASKNFIGKSK---------HGLYGD------ 308
Cdd:cd16031   151 KALDFLKERDKDkPFCLSLSFKAPHRpftpaprhrglyedvtipepETFDDDDYAGRPEwareqrnriRGVLDGrfdtpe 230
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 309 -----------AVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgGKSMNWEGGIRVP 377
Cdd:cd16031   231 kyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL------GE-HGLF------DKRLMYEESIRVP 297
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 378 GLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQS-KHEFLFHYcnaYLNAVRWHPR 456
Cdd:cd16031   298 LIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY---YEEPNFHNVP 372
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1444497654 457 NSESI----WKVFFFtPNFNPEDSngchdshvcfcygsfitrhdpplLFDLSRDPEEKV 511
Cdd:cd16031   373 THEGVrterYKYIYY-YGVWDEEE-----------------------LYDLKKDPLELN 407
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
25-513 1.16e-56

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: 195.03  E-value: 1.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIgDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAysrvgvflFSA 104
Cdd:cd16027     1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHG--------LRS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHlgMNCESSNDFCHHPLSHGFDYFYG-LTMTNLRDcklgqgsvFLKGTEKs 183
Cdd:cd16027    72 RGFPLPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAwDYASNAAD--------FLNRAKK- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 184 ivtsiqifgitllslatvhfigflKVPFqalgycllitaillvvllFFFYNFRYlncflmrNHQiIQQPLSYENLTQRLT 263
Cdd:cd16027   141 ------------------------GQPF------------------FLWFGFHD-------PHR-PYPPGDGEEPGYDPE 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 264 KEAVQFIGRNTDApfllilsyLHVHTALYAsknfigkskhglygDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGa 343
Cdd:cd16027   171 KVKVPPYLPDTPE--------VREDLADYY--------------DEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG- 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 344 hveeisssgevhggynGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHD 423
Cdd:cd16027   228 ----------------MPFPRAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPP--EYLQGRS 289
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 424 LMPLLQGKiIQSKHEFLFHYCNaylnavrWHPRNSE---SI----WK-VFfftpNFNPEDsngchdshvcfcygsfitrh 495
Cdd:cd16027   290 FLPLLKGE-KDPGRDYVFAERD-------RHDETYDpirSVrtgrYKyIR----NYMPEE-------------------- 337
                         490
                  ....*....|....*...
gi 1444497654 496 dpplLFDLSRDPEEKVPL 513
Cdd:cd16027   338 ----LYDLKNDPDELNNL 351
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
435-570 3.48e-52

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 174.42  E-value: 3.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 435 SKHEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTPNFNPEDSNGCHDSHVCfcygsfITRHDPPLLFDLSRDPEEKVPLT 514
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1444497654 515 PETEsRFYEVLHVILRAVDNHTKSLHAVPDQLSWDNLLWKPWLQPCCSSlFQSCYC 570
Cdd:pfam14707  69 PDSP-EYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPT-FPACTC 122
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
25-456 1.15e-51

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: 182.26  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRtLRTPNIDRLAKEGVTLTQ-HiaASPLCTPSRAAFLTGRYPIRSGMA--AYSRVGvfl 101
Cdd:cd16025     3 PNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGMGtmAELATG--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 102 FSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndfchhplshgfDYFygltmtnlrdcklgqgsvflkgte 181
Cdd:cd16025    77 KPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYY------------------------ 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 182 ksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenLTQR 261
Cdd:cd16025   117 ----------------------------------------------------------------------------STDD 120
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 262 LTKEAVQFI--GRNTDAPFLLILSYLHVHTALYASKNFIGKSKhGLYG---DA--------------------------- 309
Cdd:cd16025   121 LTDKAIEYIdeQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYK-GKYDagwDAlreerlerqkelglipadtkltprppg 199
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 310 -------------------------VEEMDWSVGRILDVLEKSN-LNNkTLVYFTSDQGAhveeissSGEVHGGY--NGI 361
Cdd:cd16025   200 vpawdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGeLDN-TLIIFLSDNGA-------SAEPGWANasNTP 271
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 362 YKGGKSMNWEGGIRVPGLLLWPGVIQA-GTYIDEPTSNMDIFPTVIKLAGAQLPcDRI-------IDGHDLMPLLQGKII 433
Cdd:cd16025   272 FRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYP-KTVngvpqlpLDGVSLLPTLDGAAA 350
                         490       500       510
                  ....*....|....*....|....*....|
gi 1444497654 434 QSKHEFLF--HYCNAYL-----NAVRWHPR 456
Cdd:cd16025   351 PSRRRTQYfeLFGNRAIrkggwKAVALHPP 380
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-426 3.05e-49

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 171.27  E-value: 3.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYP--------IRSGMAAYSR 96
Cdd:cd16149     1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPsqhgihdwIVEGSHGKTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  97 VGVflfsassgGLPSEEITFSKLLKQRGYSTALIGKWHLGmncessndfchhplshgfdyfygltmtnlrdcklgqgsvf 176
Cdd:cd16149    81 KPE--------GYLEGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 177 lkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfRYLNCFLMRNHQiiqqplsye 256
Cdd:cd16149   113 -----------------------------------------------------------DDAADFLRRRAE--------- 124
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 257 nltqrltkeavqfigrnTDAPFLLILSYLHVHtalyasknfigkSKHGlYGDAVEEMDWSVGRILDVLEKSNLNNKTLVY 336
Cdd:cd16149   125 -----------------AEKPFFLSVNYTAPH------------SPWG-YFAAVTGVDRNVGRLLDELEELGLTENTLVI 174
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 337 FTSDqgahveeisssgevHG---GYNGIY-KG-GKS-MN-WEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLA 409
Cdd:cd16149   175 FTSD--------------NGfnmGHHGIWgKGnGTFpLNmYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELA 240
                         410
                  ....*....|....*..
gi 1444497654 410 GAQLPCDRIIDGHDLMP 426
Cdd:cd16149   241 GVDPPADPRLPGRSFAD 257
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
25-508 1.70e-47

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: 168.91  E-value: 1.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFLFSA 104
Cdd:cd16032     1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLP--------SRIGAYDNAA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SsggLPSEEITFSKLLKQRGYSTALIGKWHlgmncessndFCHHPLSHGFDYfygltmtnlrDcklgqgsvflkgtEksi 184
Cdd:cd16032    73 E---FPADIPTFAHYLRAAGYRTALSGKMH----------FVGPDQLHGFDY----------D-------------E--- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqifgitllslatvhfigflKVPFQAlgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenlTQRLTK 264
Cdd:cd16032   114 -----------------------EVAFKA---------------------------------------------VQKLYD 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAvqfiGRNTDAPFLLILSYLHVHTALYASKNF----IGKSKHGLYGdAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSD 340
Cdd:cd16032   126 LA----RGEDGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 341 QGAHVeeisssGEvHGGYngiYKggksMNW-EGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQL-PCDRI 418
Cdd:cd16032   201 HGDML------GE-RGLW---YK----MSFfEGSARVPLIISAPGRFAPRR-VAEPVSLVDLLPTLVDLAGGGTaPHVPP 265
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 419 IDGHDLMPLLQGKIIQSKHEFLFHYCN----AYLNAVRwhprnsESIWKvFFFTPNfnpedsngchdshvcfcygsfitr 494
Cdd:cd16032   266 LDGRSLLPLLEGGDSGGEDEVISEYLAegavAPCVMIR------RGRWK-FIYCPG------------------------ 314
                         490
                  ....*....|....
gi 1444497654 495 hDPPLLFDLSRDPE 508
Cdd:cd16032   315 -DPDQLFDLEADPL 327
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-508 2.33e-47

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: 168.49  E-value: 2.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFlfsA 104
Cdd:cd16037     1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYV--------HETGVW---D 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmncesSNDFChhplsHGFDYfygltmtnlrdcklgqgsvflkgteksi 184
Cdd:cd16037    70 NADPYDGDVPSWGHALRAAGYETVLIGKLHFR-----GEDQR-----HGFRY---------------------------- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenlTQRLTK 264
Cdd:cd16037   112 --------------------------------------------------------------------------DRDVTE 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSKHGL---YGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTS 339
Cdd:cd16037   118 AAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 340 DQGAHVeeisssgevhgGYNGIYkgGKSMNWEGGIRVPGLLLWPGvIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRii 419
Cdd:cd16037   198 DHGDML-----------GERGLW--GKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-- 261
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 420 DGHDLMPLLQGK-----IIQSkhEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTpnfnpedsngchdshvcfcygsfitr 494
Cdd:cd16037   262 DGRSLLPLAEGPddpdrVVFS--EYHAHGSPSGAFMLRKGR------WKYIYYV-------------------------- 307
                         490
                  ....*....|....
gi 1444497654 495 HDPPLLFDLSRDPE 508
Cdd:cd16037   308 GYPPQLFDLENDPE 321
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
25-430 2.58e-43

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: 160.43  E-value: 2.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGiGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFLFSA 104
Cdd:cd16030     3 PNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRP--------DTTGVYDNNS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGK-WHlGMNCESSND------FCHHPLSHGFDYFYGLTMTNLRDCKLGQGSVFL 177
Cdd:cd16030    74 YFRKVAPDAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDpaswdePPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 178 KGTEKSIVTSIQI--FGITLLS----------LAtvhfIGFLK--VPFQA---------LGYCLLITAILLVVLLFFFYN 234
Cdd:cd16030   153 ADVPDEAYPDGKVadEAIEQLRklkdsdkpffLA----VGFYKphLPFVApkkyfdlypLESIPLPNPFDPIDLPEVAWN 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 235 fRYLNCFLMRNHQIIQQPLSYENLTQRLTKEAVQfigrntdapfllilSYlhvhtalYASknfigkskhglygdaVEEMD 314
Cdd:cd16030   229 -DLDDLPKYGDIPALNPGDPKGPLPDEQARELRQ--------------AY-------YAS---------------VSYVD 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 315 WSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgGKSMNWEGGIRVPglLLW--PGVIQAGTYI 392
Cdd:cd16030   272 AQVGRVLDALEELGLADNTIVVLWSDHGWHL------GE-HGHW------GKHTLFEEATRVP--LIIraPGVTKPGKVT 336
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1444497654 393 DEPTSNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQG 430
Cdd:cd16030   337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKN 372
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-432 7.79e-42

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


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 155.84  E-value: 7.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaYSRVGVFLfsA 104
Cdd:cd16033     1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGV--LNNVENAG--A 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmNCESSNDFC---HHPLSHGFDYFYG-LTMTNLRDCKLGQGSVFLkgt 180
Cdd:cd16033    77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVG-PEETPLDYGfdeYLPVETTIEYFLAdRAIEMLEELAADDKPFFL--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 181 eksivtsiqifgitllslaTVHFIG-----FLKVPFqalgycllitaillvvllfffynfrylncFLMRNHQIIQQPLSY 255
Cdd:cd16033   153 -------------------RVNFWGphdpyIPPEPY-----------------------------LDMYDPEDIPLPESF 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 256 ENltQRLTKEAVQfigRNTDAPFLLILSYLHVHtalyasKNFIGKskhglYGDAVEEMDWSVGRILDVLEKSNLNNKTLV 335
Cdd:cd16033   185 AD--DFEDKPYIY---RRERKRWGVDTEDEEDW------KEIIAH-----YWGYITLIDDAIGRILDALEELGLADDTLV 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 336 YFTSDQGAHVeeisssGEvHGGYNgiyKgGKSMnWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAqlPC 415
Cdd:cd16033   249 IFTSDHGDAL------GA-HRLWD---K-GPFM-YEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGV--DV 314
                         410
                  ....*....|....*..
gi 1444497654 416 DRIIDGHDLMPLLQGKI 432
Cdd:cd16033   315 PPKVDGRSLLPLLRGEQ 331
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-426 3.57e-40

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 147.31  E-value: 3.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLgIGD-LGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIrsgmaaYSRVGVFLfs 103
Cdd:cd16148     1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPF------YHGVWGGP-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 104 assggLPSEEITFSKLLKQRGYSTALIGkwhlgmncessnDFCHHPLSHGFDyfygltmtnlrdcklgQGsvflkgteks 183
Cdd:cd16148    72 -----LEPDDPTLAEILRKAGYYTAAVS------------SNPHLFGGPGFD----------------RG---------- 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 184 ivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRylncflmRNHQIIQQPLSYENlTQRLT 263
Cdd:cd16148   109 ----------------------------------------------FDTFEDF-------RGQEGDPGEEGDER-AERVT 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 264 KEAVQFIGRN-TDAPFLLILSYLHVHtALYasknfigkskhgLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQG 342
Cdd:cd16148   135 DRALEWLDRNaDDDPFFLFLHYFDPH-EPY------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 343 ahvEEIsssGEvhggyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGH 422
Cdd:cd16148   202 ---EEF---GE-----HGLYWGHGSNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPP--DYSDGR 267

                  ....
gi 1444497654 423 DLMP 426
Cdd:cd16148   268 SLLP 271
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-520 3.61e-40

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 150.02  E-value: 3.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  23 SNPNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQ-HIAAS---PLCTPSRAAFLTGRYpirsgmaaysrvg 98
Cdd:cd16155     1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMGGwsgAVCVPSRAMLMTGRT------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  99 vfLFSASSGG---LPSEEITFSKLLKQRGYSTALIGKWHlgmncessNDFCHHPLShgfdyfygltmtnlrdcklgqgsv 175
Cdd:cd16155    68 --LFHAPEGGkaaIPSDDKTWPETFKKAGYRTFATGKWH--------NGFADAAIE------------------------ 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 176 FLKGTEKSivtsiqifgitllslatvhfigflKVPFqalgycllitaillvvllfffynFRYLnCFL------------- 242
Cdd:cd16155   114 FLEEYKDG------------------------DKPF-----------------------FMYV-AFTaphdprqappeyl 145
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 243 -MRNHQIIQQPLSYENLTqrlTKEAVQFIGRntD---APFLLILSYLHVHTALYasknfigkskhglYGdAVEEMDWSVG 318
Cdd:cd16155   146 dMYPPETIPLPENFLPQH---PFDNGEGTVR--DeqlAPFPRTPEAVRQHLAEY-------------YA-MITHLDAQIG 206
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 319 RILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgGKSMNWEGGIRVPGLLLWPGvIQAGTYIDEPTSN 398
Cdd:cd16155   207 RILDALEASGELDNTIIVFTSDHGLAV------GS-HGLM------GKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYL 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 399 MDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKiIQSKHEFLFHycnAYLN---AVRwhprnsESIWKVFFFTPnfnped 475
Cdd:cd16155   273 QDVFPTLCELAGIEIPES--VEGKSLLPVIRGE-KKAVRDTLYG---AYRDgqrAIR------DDRWKLIIYVP------ 334
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1444497654 476 sngchdshvcfcyGSFITRhdpplLFDLSRDPEEKVPL--TPETESR 520
Cdd:cd16155   335 -------------GVKRTQ-----LFDLKKDPDELNNLadEPEYQER 363
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
25-513 1.94e-36

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: 141.24  E-value: 1.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGiGD-LGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAaysRVGVflfs 103
Cdd:cd16028     1 RNVLFITADQWR-ADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---WNGT---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 104 assgGLPSEEITFSKLLKQRGYSTALIGKWHL-----GMNCESSNDFCHHPLSHGFDyfYGLTMTNLRDcklgqgsvflk 178
Cdd:cd16028    73 ----PLDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFD--PVDRLDEYPA----------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 179 gtEKSIVTSIqifgitllslaTVHFIGFLKV----PFqalgyCLLITAIllvvllfffynfrylncflmRNHQIIQQPLS 254
Cdd:cd16028   136 --EDSDTAFL-----------TDRAIEYLDErqdePW-----FLHLSYI--------------------RPHPPFVAPAP 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 255 YENLTQrltKEAVQFIGRNTDA-------PFlliLSYLHVHtalYASKNFIGKSKHGLYGDA-------------VEEMD 314
Cdd:cd16028   178 YHALYD---PADVPPPIRAESLaaeaaqhPL---LAAFLER---IESLSFSPGAANAADLDDeevaqmratylglIAEVD 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 315 WSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGgyngiyKGGKSMNWEGGIRVPGLLLWPGV---IQAGTY 391
Cdd:cd16028   249 DHLGRLFDYLKETGQWDDTLIVFTSDHGEQL------GD-HW------LWGKDGFFDQAYRVPLIVRDPRReadATRGQV 315
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 392 IDEPTSNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQGKIIQSKHEFLfHYCNAYLNAVRWHPRNSESIwkvffftpnf 471
Cdd:cd16028   316 VDAFTESVDVMPTILDWLG--GEIPHQCDGRSLLPLLAGAQPSDWRDAV-HYEYDFRDVSTRRPQEALGL---------- 382
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1444497654 472 NPEDSNGC---HDSHVCFCYGSFitrhdPPLLFDLSRDPEEKVPL 513
Cdd:cd16028   383 SPDECSLAvirDERWKYVHFAAL-----PPLLFDLKNDPGELRDL 422
PRK13759 PRK13759
arylsulfatase; Provisional
25-509 1.72e-35

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 139.42  E-value: 1.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGiGD-LGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFs 103
Cdd:PRK13759    7 PNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPWNY- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 104 assgglpseEITFSKLLKQRGYSTALIGKWHLgmncessndfchHP--LSHGFDYfygltmTNLRDCKLGQGSVFLKGTE 181
Cdd:PRK13759   85 ---------KNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHDGYLHSGRNEDKSQF 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 182 KSIVTSIQIFGItllslatvhfigflkvpfQALGYCLLITAIllvvllfffynfrYLNCflmrnHQIIQQPLSY-ENL-- 258
Cdd:PRK13759  138 DFVSDYLAWLRE------------------KAPGKDPDLTDI-------------GWDC-----NSWVARPWDLeERLhp 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 259 TQRLTKEAVQFI-GRNTDAPFLLILSYLHVH------------------------------------TALYASKNFIGK- 300
Cdd:PRK13759  182 TNWVGSESIEFLrRRDPTKPFFLKMSFARPHspydppkryfdmykdadipdphigdweyaedqdpegGSIDALRGNLGEe 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 301 ----SKHGLYGDaVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDqgaHveeisssGEVHGGYngiYKGGKSMNWEGGIRV 376
Cdd:PRK13759  262 yarrARAAYYGL-ITHIDHQIGRFLQALKEFGLLDNTIILFVSD---H-------GDMLGDH---YLFRKGYPYEGSAHI 327
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 377 PGLLLWPG---VIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKiiqskheflfhycnaylnavrw 453
Cdd:PRK13759  328 PFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ---------------------- 383
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1444497654 454 hprnsESIWKVFFFTPNFNPEDSNgcH---DSHVCFCYGSFITRHDpplLFDLSRDPEE 509
Cdd:PRK13759  384 -----YEGWRPYLHGEHALGYSSD--NyltDGKWKYIWFSQTGEEQ---LFDLKKDPHE 432
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-520 8.50e-35

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


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 135.05  E-value: 8.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFlfsA 104
Cdd:cd16152     2 PNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYP--------TETGCF---R 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmncessndfchhplshgfdyfygltmtnlrdcklgqgsvflkgteksi 184
Cdd:cd16152    71 NGIPLPADEKTLAHYFRDAGYETGYVGKWHLA------------------------------------------------ 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 vtsiqifgitllslatvhfigflkvpfqalGYcllitaillvvllfffynfRylncflmrnhqiiqqplsyenlTQRLTK 264
Cdd:cd16152   103 ------------------------------GY-------------------R----------------------VDALTD 111
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFI-GRNTDAPFLLILSYLHVH----------TALYASK---NFIGKSKHGLYGDA----------VEEMDWSVGRI 320
Cdd:cd16152   112 FAIDYLdNRQKDKPFFLFLSYLEPHhqndrdryvaPEGSAERfanFWVPPDLAALPGDWaeelpdylgcCERLDENVGRI 191
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 321 LDVLEKSNLNNKTLVYFTSDQGAHVEEisssgevhggYNGIYKggKSMNwEGGIRVPGLLLWPGvIQAGTYIDEPTSNMD 400
Cdd:cd16152   192 RDALKELGLYDNTIIVFTSDHGCHFRT----------RNAEYK--RSCH-ESSIRVPLVIYGPG-FNGGGRVEELVSLID 257
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 401 IFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLFHYcnaylnavrwhprnSESI---------WKVFFFTPnf 471
Cdd:cd16152   258 LPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQI--------------SESQvgrairtdrWKYSVAAP-- 319
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1444497654 472 npeDSNGCHDShvcfcyGS--FITRHdpplLFDLSRDPEEKVPLTPETESR 520
Cdd:cd16152   320 ---DKDGWKDS------GSdvYVEDY----LYDLEADPYELVNLIGRPEYR 357
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-424 1.30e-34

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


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 132.11  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGN----------RTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSgmaay 94
Cdd:cd16153     2 PNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRT----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  95 srvGVFLFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmncessndfchhplshgfdyfygltmtnlrdcklgqgs 174
Cdd:cd16153    77 ---GVYGFEAAHPALDHGLPTFPEVLKKAGYQTASFGKSHLE-------------------------------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 175 vflkgteksivtsiqifgitllslatvhfigflkvPFQalgycllitaillvvllfffynfRYLNcflmrnhqiiQQPLS 254
Cdd:cd16153   116 -----------------------------------AFQ-----------------------RYLK----------NANQS 127
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 255 YENLTQRLTKeavqfiGRNTDAPFLLILSYLHVHTALYASKNFIGK-SKHGL--YGDAVeemdwsVGRILDVLEKSNLNN 331
Cdd:cd16153   128 YKSFWGKIAK------GADSDKPFFVRLSFLQPHTPVLPPKEFRDRfDYYAFcaYGDAQ------VGRAVEAFKAYSLKQ 195
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 332 K---TLVYFTSDQGAHVeeisssgevhgGYNGIYkgGKSMNWEGGIRVPGLLLWPGVIQ--AGTYIDEPTSNMDIFPTVI 406
Cdd:cd16153   196 DrdyTIVYVTGDHGWHL-----------GEQGIL--AKFTFWPQSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTLL 262
                         410
                  ....*....|....*...
gi 1444497654 407 KLAGAQLPCDRIIDGHDL 424
Cdd:cd16153   263 AAAGVDVDAPDYLDGRDL 280
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
25-409 3.48e-34

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: 129.85  E-value: 3.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTL-TQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFS 103
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 104 aSSGGLPSEEITFSKLLKQRGYSTALIGkwhlgmncessndfchhplshgfdyfygltmtnlrdcklgqgsvflkgteks 183
Cdd:cd00016    81 -RAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 184 ivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenltqrlt 263
Cdd:cd00016       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 264 keAVQFIGRNTDA-PFLLILSYLHVHTALYASKnfigkSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQG 342
Cdd:cd00016   108 --LLKAIDETSKEkPFVLFLHFDGPDGPGHAYG-----PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444497654 343 AHVEEisssgevHGGYNGiyKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLA 409
Cdd:cd00016   181 GIDKG-------HGGDPK--ADGKADKSHTGMRVPFIAYGPGVKKGGV-KHELISQYDIAPTLADLL 237
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
25-414 8.26e-34

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: 132.67  E-value: 8.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLgigDLGCYGNRTLRtPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFLFSA 104
Cdd:cd16147     2 PNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYA--------HNHGVTNNSP 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPS------EEITFSKLLKQRGYSTALIGKWhlgMN-CESSNDFCHHPLshGFDYFYGLTMtnlrdcklgqgsvfl 177
Cdd:cd16147    70 PGGGYPKfwqnglERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVG--------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 178 kgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffyNFRYLNCFLmRNHQIIQQPLSYEN 257
Cdd:cd16147   130 --------------------------------------------------------NSTYYNYTL-SNGGNGKHGVSYPG 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 258 --LTQRLTKEAVQFIGR--NTDAPFLLILSYL--HV-------HTALYA--------SKNFIGKS--KHGL--------- 305
Cdd:cd16147   153 dyLTDVIANKALDFLRRaaADDKPFFLVVAPPapHGpftpaprYANLFPnvtapprpPPNNPDVSdkPHWLrrlpplnpt 232
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 306 ---YGD-----------AVEEMdwsVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGgyngiYKGGKSMNWE 371
Cdd:cd16147   233 qiaYIDelyrkrlrtlqSVDDL---VERLVNTLEATGQLDNTYIIYTSDNGYHL------GQ-HR-----LPPGKRTPYE 297
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1444497654 372 GGIRVPGLLLWPGvIQAGTYIDEPTSNMDIFPTVIKLAGAQLP 414
Cdd:cd16147   298 EDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPP 339
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-430 5.47e-32

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: 127.08  E-value: 5.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTL--RTPNIDRLAKEGVTLTqHIAASPLCTPSRAAFLTGRYPIRSGMaaysrvgvfLF 102
Cdd:cd16154     1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV---------LA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 103 SASSGGLPSEEITFSKLLKQR--GYSTALIGKWHLGmNCESSNDfcHHPlshGFDYFYGLTMTNLRDcklgqgsvflkgt 180
Cdd:cd16154    71 VPDELLLSEETLLQLLIKDATtaGYSSAVIGKWHLG-GNDNSPN--NPG---GIPYYAGILGGGVQD------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 181 eksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNcflmrNHqiiQQPLSYENLTQ 260
Cdd:cd16154   132 ---------------------------------------------------YYNWNLTN-----NG---QTTNSTEYATT 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 261 RLTKEAVQFIGRNTDaPFLLILSYLHVHT-------ALYASKNF-----IGKSKHGLYGDAVEEMDWSVGRILDVLEKSN 328
Cdd:cd16154   153 KLTNLAIDWIDQQTK-PWFLWLAYNAPHTpfhlppaELHSRSLLgdsadIEANPRPYYLAAIEAMDTEIGRLLASIDEEE 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 329 LNNkTLVYFTSDQGAHVEEISSSGEVHGGYNGIYkggksmnwEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKL 408
Cdd:cd16154   232 REN-TIIIFIGDNGTPGQVVDLPYTRNHAKGSLY--------EGGINVPLIVSGAGVERANERESALVNATDLYATIAEL 302
                         410       420
                  ....*....|....*....|..
gi 1444497654 409 AGAQLPcdRIIDGHDLMPLLQG 430
Cdd:cd16154   303 AGVDAA--EIHDSVSFKPLLSD 322
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
25-440 4.31e-31

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: 126.34  E-value: 4.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAaysrvgvflfsA 104
Cdd:cd16156     1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSW-----------T 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFChhPLSHGFDYFYglTMTNLRDcKLgqgsvflkgTEKSI 184
Cdd:cd16156    70 NCMALGDNVKTIGQRLSDNGIHTAYIGKWHLDGGDYFGNGIC--PQGWDPDYWY--DMRNYLD-EL---------TEEER 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 VTSiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfRYLNCFLMRNHqiIQQPLSYenlTQRLTK 264
Cdd:cd16156   136 RKS------------------------------------------------RRGLTSLEAEG--IKEEFTY---GHRCTN 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRNTDAPFLLILSYLHVH-----TALYASK--------------NFIGKSKH------GLYGDAVEEM------ 313
Cdd:cd16156   163 RALDFIEKHKDEDFFLVVSYDEPHhpflcPKPYASMykdfefpkgenaydDLENKPLHqrlwagAKPHEDGDKGtikhpl 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 314 --------DWSVGRILDVLEKSNLNnkTLVYFTSD----QGAHveeisssgevhggynGIYKGGKSMnWEGGIRVPGLLL 381
Cdd:cd16156   243 yfgcnsfvDYEIGRVLDAADEIAED--AWVIYTSDhgdmLGAH---------------KLWAKGPAV-YDEITNIPLIIR 304
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1444497654 382 WPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHDLMPLLQGKIIQSKHEFL 440
Cdd:cd16156   305 GKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP--KVLEGESILATIEDPEIPENRGVF 361
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-430 2.56e-28

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 117.34  E-value: 2.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGmaaySRVGVFLfsa 104
Cdd:cd16150     1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG----HRTLHHL--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 105 ssggLPSEEITFSKLLKQRGYSTALIGKwhlgmncessNDFchhplshgFDYFYGLTMTNLRDcklgqgsvflkgtEKSI 184
Cdd:cd16150    74 ----LRPDEPNLLKTLKDAGYHVAWAGK----------NDD--------LPGEFAAEAYCDSD-------------EACV 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 185 VTSIQifgitllslatvhfigFLKVPFQALGYCLlitaillvvllfffynfrYLNcfLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16150   119 RTAID----------------WLRNRRPDKPFCL------------------YLP--LIFPHPPYGVEEPWFSMIDREKL 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 265 EAVQFIGRNTDAPFLLIlsylhvhtalyasknfIGKSKHGLYG--DA------------VEEMDWSVGRILDVLEKSNLN 330
Cdd:cd16150   163 PPRRPPGLRAKGKPSML----------------EGIEKQGLDRwsEErwrelratylgmVSRLDHQFGRLLEALKETGLY 226
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 331 NKTLVYFTSDqgahveeisssgevHGGYNGIYkgGKSMNWEGGI-----RVPGLLLWPGVIQAGTyIDEPTSNMDIFPTV 405
Cdd:cd16150   227 DDTAVFFFSD--------------HGDYTGDY--GLVEKWPNTFedcltRVPLIIKPPGGPAGGV-SDALVELVDIPPTL 289
                         410       420
                  ....*....|....*....|....*
gi 1444497654 406 IKLAGAQLPCDRIidGHDLMPLLQG 430
Cdd:cd16150   290 LDLAGIPLSHTHF--GRSLLPVLAG 312
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
25-443 4.53e-22

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: 96.89  E-value: 4.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADD--------LGIGDLGCygnrtlrtPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaYSR 96
Cdd:cd16035     1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGV--TDT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  97 VGvflfSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLgmncesSNdfchhplshgfdyfygltmtnlrdckLGQGsvf 176
Cdd:cd16035    71 LG----SPMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHL------SG--------------------------AAGG--- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 177 lkgteksivtsiqifgitllslatvhfigflkvpfqalGYcllitaillvvllfffynfrylncflMRNHQIIQQplsye 256
Cdd:cd16035   112 --------------------------------------GY--------------------------KRDPGIAAQ----- 122
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 257 nltqrltkeAVQFI---GRNTDA--PFLLILSYLHVHTALY---ASKNFIGKSKhgLYGDAVEEMDWSVGRILDVLEKSN 328
Cdd:cd16035   123 ---------AVEWLrerGAKNADgkPWFLVVSLVNPHDIMFppdDEERWRRFRN--FYYNLIRDVDRQIGRVLDALDASG 191
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 329 LNNKTLVYFTSD----QGAHveeisssGEVHGGYNgIYkggksmnwEGGIRVPglLLW--PGVIQAGTYIDEPTSNMDIF 402
Cdd:cd16035   192 LADNTIVVFTSDhgemGGAH-------GLRGKGFN-AY--------EEALHVP--LIIshPDLFGTGQTTDALTSHIDLL 253
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1444497654 403 PTVIKLAGAQLPCDRIID----GHDLMPLLQGKIIQS-KHEFLFHY 443
Cdd:cd16035   254 PTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAvRDGILFTY 299
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
25-508 6.92e-21

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: 94.53  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMADDLGiGDLGCY-GNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYP-IRSGMAAYSrvgvflf 102
Cdd:cd16171     1 PNVVMVMSDSFD-GRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFThLTESWNNYK------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 103 sassgGLPSEEITFSKLLKQRGYSTALIGKwhlgmncessNDFC--HHPLSHGFDYFYGLTMTNLRdcKLGQGSVFLKGT 180
Cdd:cd16171    73 -----GLDPNYPTWMDRLEKHGYHTQKYGK----------LDYTsgHHSVSNRVEAWTRDVPFLLR--QEGRPTVNLVGD 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 181 EKSivTSIQIFGITLLSLATvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenltQ 260
Cdd:cd16171   136 RST--VRVMLKDWQNTDKAV-----------------------------------------------------------H 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 261 RLTKEAVqfigrNTDAPFLLIL--SYLHVHTALYASKNFIG-KSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYF 337
Cdd:cd16171   155 WIRKEAP-----NLTQPFALYLglNLPHPYPSPSMGENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFF 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 338 TSDQGAHVEEisssgevhggYNGIYKggKSMnWEGGIRVPGLLLWPGvIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDr 417
Cdd:cd16171   230 TSDHGELAME----------HRQFYK--MSM-YEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN- 294
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 418 iIDGHDLMPLLQGKIIQSKHEFL---------FHYCNAylNAVRWHPRNSEsiWKvffftpnfnpedsngchdsHVCFCY 488
Cdd:cd16171   295 -LSGYSLLPLLSESSIKESPSRVphpdwvlseFHGCNV--NASTYMLRTNS--WK-------------------YIAYAD 350
                         490       500
                  ....*....|....*....|
gi 1444497654 489 GSFItrhdPPLLFDLSRDPE 508
Cdd:cd16171   351 GNSV----PPQLFDLSKDPD 366
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
245-407 6.05e-11

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


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 65.31  E-value: 6.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 245 NHQIIQQPLSYENLTQRLTKEAVQFIG-RNTDAPFLLILSYLHVHtALYASKNFIGKSKHGLYGD--------------- 308
Cdd:COG3083   349 SLPRLHTPGGPAQRDRQITAQWLQWLDqRDSDRPWFSYLFLDAPH-AYSFPADYPKPFQPSEDCNylaldnesdptpfkn 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 309 ----AVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGahvEEISSSGEVHGGYNGIYKggksmnwEGGIRVPGLLLWPG 384
Cdd:COG3083   428 ryrnAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHG---EEFNENGQNYWGHNSNFS-------RYQLQVPLVIHWPG 497
                         170       180
                  ....*....|....*....|...
gi 1444497654 385 vIQAGTyIDEPTSNMDIFPTVIK 407
Cdd:COG3083   498 -TPPQV-ISKLTSHLDIVPTLMQ 518
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
1-137 1.61e-08

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 56.68  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654   1 MRLLSFLIICQCAIkSLSSHSASNPNVILLMADDLGIGDLgcygnRTLRTPNIDRLAKEGVTLTQHIAASPLCT-PSRAA 79
Cdd:COG1524     1 MKRGLSLLLASLLA-AAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFPSTTaPAHTT 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444497654  80 FLTGRYPIRSGMAAYS-------RVGVFLFSASSGGLPSEEI---TFSKLLKQRGYSTALIGKWHLGM 137
Cdd:COG1524    75 LLTGLYPGEHGIVGNGwydpelgRVVNSLSWVEDGFGSNSLLpvpTIFERARAAGLTTAAVFWPSFEG 142
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
25-410 1.80e-08

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


Pssm-ID: 293739 [Multi-domain]  Cd Length: 283  Bit Score: 56.15  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  25 PNVILLMA---DDLGIGDLGCYGNRTlrtPNIDRLAKEGVTLTQHIAASPLCTPSRA--AFLTGRYPIRSGMAAYSRVGV 99
Cdd:cd16015     1 PNVIVILLesfSDPYIDKDVGGEDLT---PNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 100 FLFSassgglpseeiTFSKLLKQRGYSTALIgkwhlgmncessndfchhplsHGFD-YFYGltmtnlrdcklgQGSVFlk 178
Cdd:cd16015    78 NPLP-----------SLPSILKEQGYETIFI---------------------HGGDaSFYN------------RDSVY-- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 179 gteksivtsiqifgitllslatvhfigflkvpfQALGycllitaillvvllffFYNFRYLNCFLMRNHQIIQQPLSYENL 258
Cdd:cd16015   112 ---------------------------------PNLG----------------FDEFYDLEDFPDDEKETNGWGVSDESL 142
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 259 TQRLTKEavqfIGRNTDAPFLLIL---------SYLHVHTALYASKNFiGKSKHGLYGDAVEEMDWSVGRILDVLEKSNL 329
Cdd:cd16015   143 FDQALEE----LEELKKKPFFIFLvtmsnhgpyDLPEEKKDEPLKVEE-DKTELENYLNAIHYTDKALGEFIEKLKKSGL 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 330 NNKTLVYFTSDqgahveeisssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLA 409
Cdd:cd16015   218 YENTIIVIYGD--------------HLPSLGSDYDETDEDPLDLYRTPLLIYSPGLKKPKK-IDRVGSQIDIAPTLLDLL 282

                  .
gi 1444497654 410 G 410
Cdd:cd16015   283 G 283
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
21-425 3.82e-06

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 49.65  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  21 SASNPNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGmaaysrvgVF 100
Cdd:COG1368   231 PAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGG--------SP 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 101 LFSASSGGLPSeeitFSKLLKQRGYSTALI----GKWhlgMNCessNDFCHHplsHGFDYFYGLT-MTNLRDCKLGQ--G 173
Cdd:COG1368   303 YKRPGQNNFPS----LPSILKKQGYETSFFhggdGSF---WNR---DSFYKN---LGFDEFYDREdFDDPFDGGWGVsdE 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 174 SVFLKgteksivtSIQIFGItllslatvhfigfLKVPFqalgYCLLITaillvvllfffynfrylncflMRNHQiiqqPL 253
Cdd:COG1368   370 DLFDK--------ALEELEK-------------LKKPF----FAFLIT---------------------LSNHG----PY 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 254 SYENLTQRLTKeavqfigrntdapfllilsylhvhtalyasknfIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKT 333
Cdd:COG1368   400 TLPEEDKKIPD---------------------------------YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNT 446
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 334 LVYFTSDqgahveeisssgevHGGynGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQL 413
Cdd:COG1368   447 IFVIYGD--------------HGP--RSPGKTDYENPLERYRVPLLIYSPGLKKPKV-IDTVGSQIDIAPTLLDLLGIDY 509
                         410
                  ....*....|..
gi 1444497654 414 PcDRIIDGHDLM 425
Cdd:COG1368   510 P-SYYAFGRDLL 520
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
27-95 1.35e-04

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


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 44.33  E-value: 1.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654  27 VILLMADDLGIGDLgcygNRTLRTPNIDRLAKEGVTLTQHIAASPLCT-PSRAAFLTGRYPIRSGMAAYS 95
Cdd:pfam01663   1 LLVISLDGFRADYL----DRFELTPNLAALAKEGVSAPNLTPVFPTLTfPNHYTLVTGLYPGSHGIVGNT 66
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
27-62 3.97e-03

uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).


Pssm-ID: 293735  Cd Length: 368  Bit Score: 39.76  E-value: 3.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1444497654  27 VILLMADdlGIGDLG--CYGNRT-L---RTPNIDRLAKEGVT 62
Cdd:cd16011     3 YVLLILD--GLGDRPipELGGKTpLeaaKTPNLDRLAAEGIC 42
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
308-410 7.07e-03

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 38.72  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497654 308 DAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGahveeISSSGeVHGGYNGIykggKSMNweggirvPGLLLWPGVIQ 387
Cdd:cd16018   183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG-----MTDVG-THGYDNEL----PDMR-------AIFIARGPAFK 245
                          90       100
                  ....*....|....*....|...
gi 1444497654 388 AGTYIdEPTSNMDIFPTVIKLAG 410
Cdd:cd16018   246 KGKKL-GPFRNVDIYPLMCNLLG 267
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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