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Conserved domains on  [gi|1864524943|ref|XP_035145519|]
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arylsulfatase L isoform X4 [Callithrix jacchus]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
34-556 0e+00

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


The actual alignment was detected with superfamily member cd16159:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 521  Bit Score: 750.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 113
Cdd:cd16159     2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAHweLSEKRVDLEQKL 193
Cdd:cd16159    82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSFDP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 NFLFQVLALVTLTLAAGKFMHLISISWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTITEQPMRFQRVTPLI 271
Cdd:cd16159   160 LFPLLTAFVLITALTIFLLLYLGAVSKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEVVEQPMSLENLTQRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 272 LQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 351
Cdd:cd16159   238 TKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 352 GSLENQFANSQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGR 431
Cdd:cd16159   318 GHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGR 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 432 DLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTLWKVHFVTPVFQPEGAGaCYGRKVCPCSGEKVVHHDPPLLFD 511
Cdd:cd16159   398 DLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFD 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1864524943 512 LSRDPSEAHVLTPASEPlFYHVMERVQQAVWEHQQTLSPVALQLD 556
Cdd:cd16159   477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
34-556 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: 750.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 113
Cdd:cd16159     2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAHweLSEKRVDLEQKL 193
Cdd:cd16159    82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSFDP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 NFLFQVLALVTLTLAAGKFMHLISISWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTITEQPMRFQRVTPLI 271
Cdd:cd16159   160 LFPLLTAFVLITALTIFLLLYLGAVSKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEVVEQPMSLENLTQRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 272 LQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 351
Cdd:cd16159   238 TKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 352 GSLENQFANSQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGR 431
Cdd:cd16159   318 GHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGR 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 432 DLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTLWKVHFVTPVFQPEGAGaCYGRKVCPCSGEKVVHHDPPLLFD 511
Cdd:cd16159   398 DLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFD 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1864524943 512 LSRDPSEAHVLTPASEPlFYHVMERVQQAVWEHQQTLSPVALQLD 556
Cdd:cd16159   477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
15-520 1.29e-90

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 284.46  E-value: 1.29e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  15 LSVLLSLAPSASSDVSASWPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRY 94
Cdd:COG3119     5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  95 PVRSGMVSSVGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesagdhchhplhhgfdyfygmplsmt 174
Cdd:COG3119    85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 175 gdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrn 254
Cdd:COG3119       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 255 htiteqpmrfqrvTPLILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGK----------------------- 309
Cdd:COG3119   130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 310 SAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQ-FA---NSQY-GGwngiykggkgmggweggIR 384
Cdd:COG3119   197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHgLRggkGTLYeGG-----------------IR 259
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 385 VPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQ 464
Cdd:COG3119   260 VPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTG 337
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1864524943 465 RdrgtlWKVHFvtpvfqpegagaCYGRKvcpcsgekvvhhDPPLLFDLSRDPSEAH 520
Cdd:COG3119   338 R-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
444-578 1.28e-56

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 186.36  E-value: 1.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 444 SDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGACYGRKVCpcsgekVVHHDPPLLFDLSRDPSEAHVLT 523
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1864524943 524 PASePLFYHVMERVQQAVWEHQQTLSPVALQLDSLGNLWRPWLQPCCGPFPLCWC 578
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
PRK13759 PRK13759
arylsulfatase; Provisional
34-527 2.88e-34

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 135.95  E-value: 2.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvGYrvlqwt 112
Cdd:PRK13759    7 PNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 gASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesagdhchHP--LHHGFDYfygmplSMTGDcahWELSEKRVDLE 190
Cdd:PRK13759   77 -GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNEDK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 191 QKLNFLFQVLALVTLTlAAGKFMHLISISWMPVIWSAllavfllttsyfagalivhadcflmRNHTITEQpmrfQRVTPL 270
Cdd:PRK13759  135 SQFDFVSDYLAWLREK-APGKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPTNW 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 271 ILQEVKSFLKR-NKLGPFLLLVSFLHVHIPLITTKNFL-------------------------GKSAHGLYGD------- 317
Cdd:PRK13759  185 VGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeeyar 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 318 --------NVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL--ENQFANS-QYGGwngiykggkgmggwegGIRVP 386
Cdd:PRK13759  265 raraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLgdHYLFRKGyPYEG----------------SAHIP 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 387 GIFRWPG---VLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLG-TAQHSDHEFLMH-YCERFLHaar 461
Cdd:PRK13759  329 FIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYSSDN--- 403
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524943 462 WHQRDRgtlWKV--HFVTPVFQpegagacygrkvcpcsgekvvhhdpplLFDLSRDPSEAHVLTPASE 527
Cdd:PRK13759  404 YLTDGK---WKYiwFSQTGEEQ---------------------------LFDLKKDPHELHNLSPSEK 441
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
34-556 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: 750.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 113
Cdd:cd16159     2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAHweLSEKRVDLEQKL 193
Cdd:cd16159    82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSFDP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 NFLFQVLALVTLTLAAGKFMHLISISWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTITEQPMRFQRVTPLI 271
Cdd:cd16159   160 LFPLLTAFVLITALTIFLLLYLGAVSKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEVVEQPMSLENLTQRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 272 LQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 351
Cdd:cd16159   238 TKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 352 GSLENQFANSQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGR 431
Cdd:cd16159   318 GHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGR 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 432 DLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTLWKVHFVTPVFQPEGAGaCYGRKVCPCSGEKVVHHDPPLLFD 511
Cdd:cd16159   398 DLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFD 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1864524943 512 LSRDPSEAHVLTPASEPlFYHVMERVQQAVWEHQQTLSPVALQLD 556
Cdd:cd16159   477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
34-523 5.84e-151

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: 439.69  E-value: 5.84e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgYRVLQWTG 113
Cdd:cd16026     2 PNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagDH-CHHPLHHGFDYFYGMPLSMTGDCAHWELSEKRVDLeqk 192
Cdd:cd16026    77 SKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPL--- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 193 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadCFLMRNHTITEQPMRFQRVTPLIL 272
Cdd:cd16026   147 --------------------------------------------------------PPLMENEEVIEQPADQSSLTQRYT 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 273 QEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG 352
Cdd:cd16026   171 DEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGP 250
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 353 SLENQFAN-----------SQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGG 420
Cdd:cd16026   251 WLEYGGHGgsagplrggkgTTWeGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGA 313
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 421 EVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGacygrkvcpcsGEK 500
Cdd:cd16026   314 PLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG-----------GLD 376
                         490       500
                  ....*....|....*....|...
gi 1864524943 501 VVHHDPPLLFDLSRDPSEAHVLT 523
Cdd:cd16026   377 PTKLEPPLLYDLEEDPGETYNVA 399
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
34-541 6.05e-131

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: 390.25  E-value: 6.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsvGYRV-LQWT 112
Cdd:cd16160     2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPWD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 gaSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDyFYGMPLSMTGdcaHWELSekrvdleqk 192
Cdd:cd16160    80 --IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGTNLPFTN---SWACD--------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 193 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllTTSYFagalIVHAD---CFLMRNHTITEQPMRFQRVTP 269
Cdd:cd16160   145 ------------------------------------------DTGRH----VDFPDrsaCFLYYNDTIVEQPIQHEHLTE 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 270 LILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 349
Cdd:cd16160   179 TLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSD 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 350 HG------------GSLENQFANSQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTVVQL 417
Cdd:cd16160   259 HGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDL 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 418 AGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtlWKVHFVT---PVFQPEGAGACYGRKVC 494
Cdd:cd16160   321 AGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGGGPLS 393
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1864524943 495 P------CSGEKVVHHDPPLLFDLSRDPSEAHVLTPAsepLFYHVMERVQQAV 541
Cdd:cd16160   394 DyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPS---VYEHMLEAVEKLI 443
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
34-578 3.66e-97

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: 304.75  E-value: 3.66e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqwTG 113
Cdd:cd16158     2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAgdhcHHPLHHGFDYFYGMPLSMT-GDCAHwelsekrvdleqk 192
Cdd:cd16158    77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHDqGPCQN------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 193 lnflfqvlalvtltlaagkfmhlisiswmpviwsalLAVFLLTTSYFAGALIVHADCFLMRNHTITEQPMRFQRVTPLIL 272
Cdd:cd16158   140 ------------------------------------LTCFPPNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 273 QEVKSFL----KRNKlgPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFAS 348
Cdd:cd16158   184 KFAKDFIadnaKEGK--PFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 349 DHGGSLENQfansQYGGwNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVQLAGGEVPqDRVI 428
Cdd:cd16158   262 DNGPSTMRK----SRGG-NAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTL 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 429 DGRDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdrgtlWKVHFVT---PVFQPEGAGACYGRKvcpcsgeKV 501
Cdd:cd16158   335 DGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCHPSA-------EL 401
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 502 VHHDPPLLFDLSRDPSEAHVLTPASEplFYHVMERVQQAVWEHQQTLSPVALQLDSLGNlwrPWLQPC----CGPFPLCW 577
Cdd:cd16158   402 TSHDPPLLFDLSQDPSENYNLLGLPE--YNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPCckpgCTPKPSCC 476

                  .
gi 1864524943 578 C 578
Cdd:cd16158   477 Q 477
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
34-518 3.69e-94

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


Pssm-ID: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 292.90  E-value: 3.69e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEFGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvSSVGyrvlq 110
Cdd:cd16142     1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-TTVG----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 111 WTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncESAGdhcHHPLHHGFDYFYGMPLsmtgdcahwelsekrvdle 190
Cdd:cd16142    74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDG---RLPTDHGFDEFYGNLY------------------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 191 qklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnHTITEQpmrfqrvtpl 270
Cdd:cd16142   129 ----------------------------------------------------------------HTIDEE---------- 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 271 ILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGKS-AHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFA 347
Cdd:cd16142   135 IVDKAIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSsGKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 348 SDHGGSLeNQFANSQY------------GGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVV 415
Cdd:cd16142   215 TDNGPEQ-DVWPDGGYtpfrgekgttweGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLA 276
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 416 QLAGGEVP------QDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVtpVFQPEGAGACY 489
Cdd:cd16142   277 ALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGE 348
                         490       500
                  ....*....|....*....|....*....
gi 1864524943 490 GRKVCPCsgekvvhhdpPLLFDLSRDPSE 518
Cdd:cd16142   349 PFYVLTF----------PLIFNLRRDPKE 367
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
15-520 1.29e-90

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 284.46  E-value: 1.29e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  15 LSVLLSLAPSASSDVSASWPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRY 94
Cdd:COG3119     5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  95 PVRSGMVSSVGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesagdhchhplhhgfdyfygmplsmt 174
Cdd:COG3119    85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 175 gdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrn 254
Cdd:COG3119       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 255 htiteqpmrfqrvTPLILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGK----------------------- 309
Cdd:COG3119   130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 310 SAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQ-FA---NSQY-GGwngiykggkgmggweggIR 384
Cdd:COG3119   197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHgLRggkGTLYeGG-----------------IR 259
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 385 VPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQ 464
Cdd:COG3119   260 VPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTG 337
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1864524943 465 RdrgtlWKVHFvtpvfqpegagaCYGRKvcpcsgekvvhhDPPLLFDLSRDPSEAH 520
Cdd:COG3119   338 R-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
34-523 6.16e-90

arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.


Pssm-ID: 293780 [Multi-domain]  Cd Length: 383  Bit Score: 282.44  E-value: 6.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRvlqwt 112
Cdd:cd16161     2 PNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 gASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGdcahwELSEKRVDleqk 192
Cdd:cd16161    77 -SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFSHDS-----SLADRYAQ---- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 193 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyFAGAlivhadcFLMRNHTITEqpmrfqrvtplil 272
Cdd:cd16161   141 ----------------------------------------------FATD-------FIQRASAKDR------------- 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 273 qevksflkrnklgPFLLLVSFLHVHIPLITTKNFLGKSAH-GLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 351
Cdd:cd16161   155 -------------PFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNG 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 352 ---------GSLENQFANSQyGGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEV 422
Cdd:cd16161   222 pwevkcelaVGPGTGDWQGN-LGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASL 295
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 423 PQDRVIDGRDLLPLLLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtlWKVHFVTpvfqpEGAGACYGRKvCPcs 497
Cdd:cd16161   296 PPGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALACCGST-GP-- 360
                         490       500
                  ....*....|....*....|....*.
gi 1864524943 498 gekVVHHDPPLLFDLSRDPSEAHVLT 523
Cdd:cd16161   361 ---KLYHDPPLLFDLEVDPAESFPLT 383
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
34-520 7.31e-88

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


Pssm-ID: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 278.27  E-value: 7.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGM--VSSVGYRVLQW 111
Cdd:cd16144     1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 112 TGA-----SGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGmplsmtGDCAHwelsekr 186
Cdd:cd16144    81 TKLipppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG------GTGNG------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 187 vdleqklnflfqvlalvtltlaAGKfmhlisiswmpviwsallavfllttSYFAGALIVHADCFLmrnhtITEQPMRFQR 266
Cdd:cd16144   142 ----------------------GPP-------------------------SYYFPPGKPNPDLED-----GPEGEYLTDR 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 267 VTplilQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTK----NFLGKSAHGLYGDN-------VEEMDWMVGQILDALDT 335
Cdd:cd16144   170 LT----DEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPelieKYEKKKKGLRKGQKnpvyaamIESLDESVGRILDALEE 245
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 336 EGLTNSTLIYFASDHGG-SLENQFANSQY-----------GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGE 403
Cdd:cd16144   246 LGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRWPGVIKPGSVSDV 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 404 PTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMhycerflhaarWHQrdrgtlwkvhfvtPVFQPE 483
Cdd:cd16144   309 PVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALF-----------WHF-------------PHYHGQ 364
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1864524943 484 GAGacygrkvcPCS----GE-KVVHH---DPPLLFDLSRDPSEAH 520
Cdd:cd16144   365 GGR--------PASairkGDwKLIEFyedGRVELYNLKNDIGETN 401
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
34-520 1.12e-87

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: 277.16  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVgyrvlqWT 112
Cdd:cd16143     1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV------LG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 GASGGL-PTNETTFAKILKEKGYATGLIGKWHLGLN-CESAGDHCHH---------------PLHHGFDYFYGMPLSmtg 175
Cdd:cd16143    75 GFSPPLiEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwKKKDGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPAS--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 176 dcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnh 255
Cdd:cd16143       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 256 titeqpmrfqRVTPLILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDAL 333
Cdd:cd16143   152 ----------EVLPTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDAL 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 334 DTEGLTNSTLIYFASDHGGSLENQF---------ANSQY---------GGwngiykggkgmggweggIRVPGIFRWPGVL 395
Cdd:cd16143   222 KELGLAENTLVIFTSDNGPSPYADYkelekfghdPSGPLrgmkadiyeGG-----------------HRVPFIVRWPGKI 284
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 396 PAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTLWKVhf 475
Cdd:cd16143   285 PAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL-- 356
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1864524943 476 vtpVFQPEGAGACYGRKvcpcsgeKVVHHDPP-LLFDLSRDPSEAH 520
Cdd:cd16143   357 ---IDGTGSGGFSYPRG-------KEKLGLPPgQLYNLSTDPGESN 392
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
34-556 6.06e-84

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: 269.72  E-value: 6.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 113
Cdd:cd16157     2 PNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 AS--GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsagdhcHHPLHHGFDYFYGMPlsmtgDCaHWelseKRVDLEQ 191
Cdd:cd16157    82 QNivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NC-HF----GPYDNKA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 192 KLNflfqvLALVTLTLAAGKFMHLISIswmpviwsallavfllttsyfagalivhadcflmrNHTITEQpmrfqRVTPLI 271
Cdd:cd16157   146 YPN-----IPVYRDWEMIGRYYEEFKI-----------------------------------DKKTGES-----NLTQIY 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 272 LQEVKSFLKR--NKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 349
Cdd:cd16157   181 LQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSD 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 350 HGGSLenqFANSQYGGWNGIYKGGKGMGGWEGgIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVID 429
Cdd:cd16157   261 NGAAL---ISAPEQGGSNGPFLCGKQTTFEGG-MREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAID 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 430 GRDLLPLLLgtAQHSDHEFLMHYCERFLHAARwhqrdRGtLWKVHFVT----PVFQPEGAGACYGRKVCPCSGEKVVHH- 504
Cdd:cd16157   337 GIDLLPVLL--NGKEKDRPIFYYRGDELMAVR-----LG-QYKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQTDHt 408
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1864524943 505 DPPLLFDLSRDPSEAHVLTPASePLFYHVMERVQQAVWEHQQTLSPVALQLD 556
Cdd:cd16157   409 KLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
34-520 2.47e-75

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


Pssm-ID: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 245.58  E-value: 2.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyRVLQWTG 113
Cdd:cd16145     1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESAGdhchHPLHHGFDYFYGmplsmtgdcahwelsekrvdleqkl 193
Cdd:cd16145    75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGP-GTPG----HPTKQGFDYFYG------------------------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nFLFQVLAlvtltlaagkfmHlisiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-------EQPMRFQR 266
Cdd:cd16145   125 -YLDQVHA------------H----------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTY 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 267 VTPLILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTK---NFLGKSAHGLYGDN------------VEEMDWMVGQILD 331
Cdd:cd16145   170 SHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDdgpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILA 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 332 ALDTEGLTNSTLIYFASDHGGSLE------NQFANSQ----------Y-GGwngiykggkgmggweggIRVPGIFRWPGV 394
Cdd:cd16145   250 LLKELGIDENTLVVFTSDNGPHSEggsehdPDFFDSNgplrgykrslYeGG-----------------IRVPFIARWPGK 312
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 395 LPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdrgtl 470
Cdd:cd16145   313 IPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG------ 382
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 1864524943 471 WKVhfvtpVFQPEGAGacygrkvcpcsgekvvhhdPPLLFDLSRDPSEAH 520
Cdd:cd16145   383 WKA-----VRHGKKDG-------------------PFELYDLSTDPGETN 408
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
34-432 3.90e-71

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: 228.48  E-value: 3.90e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssvgyrVLQWTG 113
Cdd:cd16022     1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHlglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqkl 193
Cdd:cd16022    73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilQ 273
Cdd:cd16022   103 -------------------------------------------------------------------------------D 103
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 EVKSFLKRN-KLGPFLLLVSFLHVHIPLIttknflgksahglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG 352
Cdd:cd16022   104 EAIDFIERRdKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 353 SLENQfaNSQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRD 432
Cdd:cd16022   171 MLGDH--GLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-462 1.02e-66

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 221.70  E-value: 1.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqwtg 113
Cdd:cd16151     1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 aSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESAGDhchHPLHHGFDYFygmplsmtgdCAhWELSEKRVDLEQKL 193
Cdd:cd16151    68 -FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEY----------CL-WQLTETGEKYSRPA 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 NFLFQVLALVTLTLAAGKFmhlisiswMPVIWSAllavfllttsyfagalivhadcFLMRnhtiteqpmrfqrvtplilq 273
Cdd:cd16151   132 TPTFNIRNGKLLETTEGDY--------GPDLFAD----------------------FLID-------------------- 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 evksFLKRNKLGPFLLLVSFLHVHIPLITT----------KNFLGKSAHglYGDNVEEMDWMVGQILDALDTEGLTNSTL 343
Cdd:cd16151   162 ----FIERNKDQPFFAYYPMVLVHDPFVPTpdspdwdpddKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 344 IYFASDHGGSLE-NQFANSQY--GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGG 420
Cdd:cd16151   236 IIFTGDNGTHRPiTSRTNGREvrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGA 306
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1864524943 421 EVPQDRVIDGRDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 462
Cdd:cd16151   307 PLPEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
34-520 1.12e-65

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: 220.11  E-value: 1.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSVGYRVLqwt 112
Cdd:cd16146     1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEkrvdleqk 192
Cdd:cd16146    76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND-------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 193 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsYFagalivhaDCFLMRNHTI--TEQpmrFqrVTPL 270
Cdd:cd16146   137 ---------------------------------------------YF--------DDTYYHNGKFvkTEG---Y--CTDV 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 271 ILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNF--------LGKSAHGLYGdNVEEMDWMVGQILDALDTEGLTNST 342
Cdd:cd16146   159 FFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIENIDDNVGRLLAKLKELGLEENT 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 343 LIYFASDHG--GSLENQF-AN------SQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFP 412
Cdd:cd16146   238 IVIFMSDNGpaGGVPKRFnAGmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLP 300
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 413 TVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTLWKVHFVtpVFQPEgagacYgRK 492
Cdd:cd16146   301 TLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W-RL 363
                         490       500
                  ....*....|....*....|....*...
gi 1864524943 493 VCPcsgekvvHHDPPLLFDLSRDPSEAH 520
Cdd:cd16146   364 VSP-------KGFQPELYDIENDPGEEN 384
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
34-522 2.58e-61

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: 207.79  E-value: 2.58e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMVSSVGyrvlqWTG 113
Cdd:cd16029     1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGMQHGVI-----LAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdHCHH---PLHHGFDYFYGMPLSMTGdcaHWelsekrvdle 190
Cdd:cd16029    75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGYYGGAED---YY---------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 191 qklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-EQPMRFqrVTP 269
Cdd:cd16029   134 ----------------------------------------------THTSGGANDYGNDDLRDNEEPAwDYNGTY--STD 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 270 LILQEVKSFLKR-NKLGPFLLLVSFLHVHIPLITTKNFL----GKSAHGLYGD------NVEEMDWMVGQILDALDTEGL 338
Cdd:cd16029   166 LFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYAdpyeDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKGM 245
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 339 TNSTLIYFASDHGGSLENQFANSQY-----------GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIGEPT 405
Cdd:cd16029   246 LDNTLIVFTSDNGGPTGGGDGGSNYplrggkntlweGG-----------------VRVPA-FVWSPLLPpkRGTVSDGLM 307
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 406 SLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRGTLWKVHfvtpvfqpegA 485
Cdd:cd16029   308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDDITRTTGG----------A 364
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1864524943 486 GACYGRKvcpcsgeKVVHHDPplLFDLSRDPSEAHVL 522
Cdd:cd16029   365 AIRVGDW-------KLIVGKP--LFNIENDPCERNDL 392
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-520 1.34e-58

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: 200.87  E-value: 1.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqwtg 113
Cdd:cd16034     2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 asggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHH----PLHHGFDYFYGMplsmtgDCAH-------WEL 182
Cdd:cd16034    75 ----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------ECNHdhnnphyYDD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 183 SEKRVDLEQklnflfqvlalvtltlaagkfmhlisisWMPvIWSALLAVfllttSYfagalivhadcflMRNHTITEQP- 261
Cdd:cd16034   145 DGKRIYIKG----------------------------YSP-DAETDLAI-----EY-------------LENQADKDKPf 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 262 ----------MRFQRVtPlilQEVKSFLKRNKLgpflllvsFLHVHIPLIT-TKNFLGKSAHGLYGdNVEEMDWMVGQIL 330
Cdd:cd16034   178 alvlswnpphDPYTTA-P---EEYLDMYDPKKL--------LLRPNVPEDKkEEAGLREDLRGYYA-MITALDDNIGRLL 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 331 DALDTEGLTNSTLIYFASDHG---GSLENQFANSQYGGwngiykggkgmggwegGIRVPGIFRWPGVLPAGRVIGEPTSL 407
Cdd:cd16034   245 DALKELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYPGKIKAGRVVDLLINT 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 408 MDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTL----WKvhFVtpvfqpe 483
Cdd:cd16034   309 VDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtdrYT--YV------- 377
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1864524943 484 gagacygrkvcpcsgekVVHHDPPLLFDLSRDPSEAH 520
Cdd:cd16034   378 -----------------RDKNGPWLLFDNEKDPYQLN 397
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
444-578 1.28e-56

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 186.36  E-value: 1.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 444 SDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGACYGRKVCpcsgekVVHHDPPLLFDLSRDPSEAHVLT 523
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1864524943 524 PASePLFYHVMERVQQAVWEHQQTLSPVALQLDSLGNLWRPWLQPCCGPFPLCWC 578
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
34-546 5.82e-55

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


Pssm-ID: 293751 [Multi-domain]  Cd Length: 373  Bit Score: 190.41  E-value: 5.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssVGYRVLQWTg 113
Cdd:cd16027     1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 asggLPTNETTFAKILKEKGYATGLIGKWHlgLNCESAGDHCHHPLHHGFDYFYGMPlsMTGDCAHWelsEKRVDLEQkl 193
Cdd:cd16027    76 ----LPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWD--YASNAADF---LNRAKKGQ-- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nflfqvlalvtltlaagkfmhlisiswmPviwsallavFllttsyfagalivhadcFLMRNHTITEQPMRFQRVTPLI-- 271
Cdd:cd16027   143 ----------------------------P---------F-----------------FLWFGFHDPHRPYPPGDGEEPGyd 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 272 LQEVksflkrnKLGPFLllvsflhVHIPLIttknflgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 351
Cdd:cd16027   169 PEKV-------KVPPYL-------PDTPEV-------REDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 352 GslenQFANS-----QYGgwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDr 426
Cdd:cd16027   228 M----PFPRAkgtlyDSG------------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY- 284
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 427 vIDGRDLLPLLLG-TAQHSDHEFLMH-------YCERFLHAARWHqrdrgtlwkvhfvtpvfqpegagacYgrkvcpcsg 498
Cdd:cd16027   285 -LQGRSFLPLLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK-------------------------Y--------- 329
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1864524943 499 ekVVHHDPPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEHQQ 546
Cdd:cd16027   330 --IRNYMPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
Sulfatase pfam00884
Sulfatase;
34-419 2.78e-54

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 186.09  E-value: 2.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqwtg 113
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAgdhchhPLHHGFDYFYGmplsmtgdcahwelsekrvdleqkl 193
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nflfqvlalvtltlaagkfmhlisiswmpviwsallavFLLTTSYFAGALIVHADCFLMRNHTiteqpmrfQRVTPLILQ 273
Cdd:pfam00884 120 --------------------------------------RNTGSDLYADPPDVPYNCSGGGVSD--------EALLDEALE 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 evksFLKRNKlGPFLLLVSFLHVHIPLITTKNFLGKSA------------HGLYGDNVEEMDWMVGQILDALDTEGLTNS 341
Cdd:pfam00884 154 ----FLDNND-KPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524943 342 TLIYFASDHGGSLENQFANSQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 419
Cdd:pfam00884 229 TLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
34-520 1.36e-51

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: 182.73  E-value: 1.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqwTG 113
Cdd:cd16031     3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT----------DN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesaGDHCHHPlhHGFDYFYGMPlsmtgdcahwelsekrvdlEQkl 193
Cdd:cd16031    73 NGPLFDASQPTYPKLLRKAGYQTAFIGKWHLG------SGGDLPP--PGFDYWVSFP-------------------GQ-- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nflfqvlalvtltlaagkfmhlisiswmpviwsallavflltTSYFAGALIVhadcflMRNHTITEQPmrfqrVTPLILQ 273
Cdd:cd16031   124 ------------------------------------------GSYYDPEFIE------NGKRVGQKGY-----VTDIITD 150
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 EVKSFLKRNKLG-PFLLLVSFLHVH-----------------IPLITT---KNFLGKS-------------------AHG 313
Cdd:cd16031   151 KALDFLKERDKDkPFCLSLSFKAPHrpftpaprhrglyedvtIPEPETfddDDYAGRPewareqrnrirgvldgrfdTPE 230
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 314 LYGDNVE-------EMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-ENQFA-------NSqyggwngiykggkgmgg 378
Cdd:cd16031   231 KYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLgEHGLFdkrlmyeES----------------- 293
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 379 weggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHS-DHEFLMHYCE--R 455
Cdd:cd16031   294 ----IRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepN 367
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 456 FLHAARWH--QRDRgtlWK-VHFvtpvfqpegagacygrkvcpcsgekvvHHDPPL--LFDLSRDPSEAH 520
Cdd:cd16031   368 FHNVPTHEgvRTER---YKyIYY---------------------------YGVWDEeeLYDLKKDPLELN 407
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-463 2.28e-48

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: 173.56  E-value: 2.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqWTG 113
Cdd:cd16033     1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 A-SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdhcHHPLHHGFDYFygMPLSMTGDcaHWeLSEKRVDLEQK 192
Cdd:cd16033    76 AySRGLPPGVETFSEDLREAGYRNGYVGKWHVGPE--------ETPLDYGFDEY--LPVETTIE--YF-LADRAIEMLEE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 193 LnflfqvlalvtltLAAGK-FMHLISIsWMPviwsallavfllttsyfagalivHADCF-------LMRNHTItEQPMRF 264
Cdd:cd16033   143 L-------------AADDKpFFLRVNF-WGP-----------------------HDPYIppepyldMYDPEDI-PLPESF 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 265 QRvtPLILqevKSFLKRNKLGPFLLLVSFLHVHIPLIttknflgksAHglYGDNVEEMDWMVGQILDALDTEGLTNSTLI 344
Cdd:cd16033   185 AD--DFED---KPYIYRRERKRWGVDTEDEEDWKEII---------AH--YWGYITLIDDAIGRILDALEELGLADDTLV 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 345 YFASDHGGSLENQfansqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQ 424
Cdd:cd16033   249 IFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPP 316
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1864524943 425 DrvIDGRDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWH 463
Cdd:cd16033   317 K--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYK 361
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
34-520 5.85e-48

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: 172.24  E-value: 5.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEFGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSVGYRVLQWT 112
Cdd:cd16025     3 PNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGKP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLN----CESAGDH-----------------------CHHPLH----- 160
Cdd:cd16025    79 GYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPDdyysTDDLTDKaieyideqkapdkpfflylafgaPHAPLQapkew 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 161 ---------HGFDyfygmplsmtgdcahwELSEKRvdLE-QKlnflfqvlalvtltlAAGkfmhlisiswmpviwsalla 230
Cdd:cd16025   159 idkykgkydAGWD----------------ALREER--LErQK---------------ELG-------------------- 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 231 vfllttsyfagalIVHADCFLM-RNHTI-------TEQPMRFQRvtpliLQEVksflkrnklgpflllvsflhvhiplit 302
Cdd:cd16025   186 -------------LIPADTKLTpRPPGVpawdslsPEEKKLEAR-----RMEV--------------------------- 220
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 303 tknflgksahglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFAN------------SQYGGwngiy 370
Cdd:cd16025   221 ------------YAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPGWANasntpfrlykqaSHEGG----- 283
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 371 kggkgmggweggIRVPGIFRWP-GVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRV------IDGRDLLPLLLGTAQH 443
Cdd:cd16025   284 ------------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAP 351
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 444 SDHEFLmhYCERFLHAARWHQRdrgtlWKVhfvtpvfqpegagacygrkvcpcsgekVVHHDPPL------LFDLSRDPS 517
Cdd:cd16025   352 SRRRTQ--YFELFGNRAIRKGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPS 397

                  ...
gi 1864524943 518 EAH 520
Cdd:cd16025   398 ETH 400
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-516 4.94e-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: 167.33  E-value: 4.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 113
Cdd:cd16037     1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGV----------WDN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGgLPTNETTFAKILKEKGYATGLIGKWHLglncESAGDHchhplhHGFDYfygmplsmtgdcahwelsekrvDLEqkl 193
Cdd:cd16037    71 ADP-YDGDVPSWGHALRAAGYETVLIGKLHF----RGEDQR------HGFRY----------------------DRD--- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplILQ 273
Cdd:cd16037   115 -----------------------------------------------------------------------------VTE 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 EVKSFLKRNKL--GPFLLLVSFLHVHIPLITTKNFLGKSAHGL---YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFAS 348
Cdd:cd16037   118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 349 DHGgslENQFANSQYGgwngiykggkGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRvi 428
Cdd:cd16037   198 DHG---DMLGERGLWG----------KSTMYEESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-- 261
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 429 DGRDLLPLLLGTAQHSDHEFlmhyCErfLHAA---------RWHQrdrgtlWK-VHFVtpvfqpegagacygrkvcpcsg 498
Cdd:cd16037   262 DGRSLLPLAEGPDDPDRVVF----SE--YHAHgspsgafmlRKGR------WKyIYYV---------------------- 307
                         490
                  ....*....|....*...
gi 1864524943 499 ekvvhHDPPLLFDLSRDP 516
Cdd:cd16037   308 -----GYPPQLFDLENDP 320
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
34-516 5.39e-45

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: 161.98  E-value: 5.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 113
Cdd:cd16032     1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGgLPTNETTFAKILKEKGYATGLIGKWHLglncesagdhCHHPLHHGFDYfygmplsmtgdcahwelsekrvDLEqkl 193
Cdd:cd16032    71 AAE-FPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFDY----------------------DEE--- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nflfqvlalvtltlaagkfmhlisiswmpVIWSALLAVFllttsyfagalivhaDcfLMRNHTiteqpmrfqrvtplilq 273
Cdd:cd16032   115 -----------------------------VAFKAVQKLY---------------D--LARGED----------------- 131
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 evksflKRnklgPFLLLVSFLHVHIPLITTKNFLG----KSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 349
Cdd:cd16032   132 ------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 350 HGGSL--------ENQFANSqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVQLAGGE 421
Cdd:cd16032   201 HGDMLgerglwykMSFFEGS---------------------ARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGG 258
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 422 VPQDRV-IDGRDLLPLLLGTAQHSDHEFLMHYC-ERFLHAARWHQRDRgtlWKvhFVtpvfqpegagacygrkvcpcsge 499
Cdd:cd16032   259 TAPHVPpLDGRSLLPLLEGGDSGGEDEVISEYLaEGAVAPCVMIRRGR---WK--FI----------------------- 310
                         490
                  ....*....|....*..
gi 1864524943 500 kVVHHDPPLLFDLSRDP 516
Cdd:cd16032   311 -YCPGDPDQLFDLEADP 326
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-435 8.95e-41

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 148.54  E-value: 8.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 113
Cdd:cd16149     1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqkl 193
Cdd:cd16149    81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagaliVHADCFLMRNHtiteqpmrfqrvtplilq 273
Cdd:cd16149   113 ---------------------------------------------------DDAADFLRRRA------------------ 123
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 evksflKRNKlgPFLLLVSFLHVHIPlittknflgksaHGlYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGgs 353
Cdd:cd16149   124 ------EAEK--PFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNG-- 180
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 354 lenqFANSQYGGW---------NgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQ 424
Cdd:cd16149   181 ----FNMGHHGIWgkgngtfplN----------MYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPA 246
                         410
                  ....*....|.
gi 1864524943 425 DRVIDGRDLLP 435
Cdd:cd16149   247 DPRLPGRSFAD 257
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-435 2.88e-38

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 141.92  E-value: 2.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssvgyrvLQWT 112
Cdd:cd16148     1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesagDHCHHPLHHGFDyfygmplsmtgdcahwelseKRVDleqk 192
Cdd:cd16148    67 VWGGPLEPDDPTLAEILRKAGYYTAAVS------------SNPHLFGGPGFD--------------------RGFD---- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 193 lnflfqvlalvtltlaagkfmhlisiSWMPVIWsallavfllttsyfagalivhadcflMRNHTITEQPMRFQRVTplil 272
Cdd:cd16148   111 --------------------------TFEDFRG--------------------------QEGDPGEEGDERAERVT---- 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 273 QEVKSFLKRNKLG-PFlllvsFLHVHIplittknFlgkSAHGLYG-DN-VEEMDWMVGQILDALDTEGLTNSTLIYFASD 349
Cdd:cd16148   135 DRALEWLDRNADDdPF-----FLFLHY-------F---DPHEPYLyDAeVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 350 HGgslENQFANSQYGGWNgiykggkgMGGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVQLAGGEVPQDrvID 429
Cdd:cd16148   200 HG---EEFGEHGLYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SD 265

                  ....*.
gi 1864524943 430 GRDLLP 435
Cdd:cd16148   266 GRSLLP 271
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
34-544 2.92e-37

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: 143.94  E-value: 2.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqWTG 113
Cdd:cd16028     1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASggLPTNETTFAKILKEKGYATGLIGKWHLglnceSAGDHCHHPLH----------HGFDY-----FYGMPLSmtgDCA 178
Cdd:cd16028    72 TP--LDARHLTLALELRKAGYDPALFGYTDT-----SPDPRGLAPLDprllsyelamPGFDPvdrldEYPAEDS---DTA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 179 HweLSEKrvdleqklnflfqvlALVTLTLAAGK--FMHLISISWMPviwsallavfllttsyfagALIVHADCFLMRNHT 256
Cdd:cd16028   142 F--LTDR---------------AIEYLDERQDEpwFLHLSYIRPHP-------------------PFVAPAPYHALYDPA 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 257 ITEQPMRfqRVTPLILQEVKSFLKRnklgpflllvsflhvHIPLITTKNFLGKSAHGLYGDN-------------VEEMD 323
Cdd:cd16028   186 DVPPPIR--AESLAAEAAQHPLLAA---------------FLERIESLSFSPGAANAADLDDeevaqmratylglIAEVD 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 324 WMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQyGGWNGIYKggkgmggweggiRVPGIFRWPGVL---PAGRV 400
Cdd:cd16028   249 DHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGK-DGFFDQAY------------RVPLIVRDPRREadaTRGQV 315
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 401 IGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQRDRGTlwkv 473
Cdd:cd16028   316 VDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALGL---- 382
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864524943 474 hfvtpvfQPEGAGACYGRkvcpcSGE-KVVHHD--PPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEH 544
Cdd:cd16028   383 -------SPDECSLAVIR-----DERwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSW 442
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
34-446 5.58e-37

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: 142.71  E-value: 5.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqWTG 113
Cdd:cd16030     3 PNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----FRK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGglptNETTFAKILKEKGYATGLIGKWHlglncesagdhchhplHHGFDYFYGMPLSmtgdcahWELSEKRVDLEQKL 193
Cdd:cd16030    78 VAP----DAVTLPQYFKENGYTTAGVGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEKYP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 NFLFQVLALVTLTLAAGKFMHLISI--SWMPVIWSALLAVFLLTT------SYFAGA--------LIVHADCFLMRNHTI 257
Cdd:cd16030   131 PGKLCPGKKGGKGGGGGPAWEAADVpdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPLES 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 258 TEQPMRFQRV-TPLI----LQEVksflkRNKLGPFLLLVSFLHVHIPLITTKNFLgksaHGLYGdNVEEMDWMVGQILDA 332
Cdd:cd16030   211 IPLPNPFDPIdLPEVawndLDDL-----PKYGDIPALNPGDPKGPLPDEQARELR----QAYYA-SVSYVDAQVGRVLDA 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 333 LDTEGLTNSTLIYFASDHGGSL-ENQ----FANsqyggWNgiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSL 407
Cdd:cd16030   281 LEELGLADNTIVVLWSDHGWHLgEHGhwgkHTL-----FE-------------EATRVPLIIRAPGVTKPGKVTDALVEL 342
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1864524943 408 MDVFPTVVQLAGgeVPQDRVIDGRDLLPLLLGTAQHSDH 446
Cdd:cd16030   343 VDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKD 379
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-442 2.78e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 133.51  E-value: 2.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgYRvlqwtg 113
Cdd:cd16152     2 PNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR------ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesAGdhchhplhhgfdYfygmplsmtgdcahwelsekRVDleqkl 193
Cdd:cd16152    71 NGIPLPADEKTLAHYFRDAGYETGYVGKWHL------AG------------Y--------------------RVD----- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 nflfqvlalvTLTLAAGKFMHlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilq 273
Cdd:cd16152   108 ----------ALTDFAIDYLD----------------------------------------------------------- 118
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 evksflKRNKLGPFLLLVSFLHVH----------------------IP--LittKNFLGKSAHGL---YGdNVEEMDWMV 326
Cdd:cd16152   119 ------NRQKDKPFFLFLSYLEPHhqndrdryvapegsaerfanfwVPpdL---AALPGDWAEELpdyLG-CCERLDENV 188
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 327 GQILDALDTEGLTNSTLIYFASDHGgsleNQFA--NSQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEP 404
Cdd:cd16152   189 GRIRDALKELGLYDNTIIVFTSDHG----CHFRtrNAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEEL 252
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1864524943 405 TSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQ 442
Cdd:cd16152   253 VSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVE 288
PRK13759 PRK13759
arylsulfatase; Provisional
34-527 2.88e-34

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 135.95  E-value: 2.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvGYrvlqwt 112
Cdd:PRK13759    7 PNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 gASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesagdhchHP--LHHGFDYfygmplSMTGDcahWELSEKRVDLE 190
Cdd:PRK13759   77 -GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNEDK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 191 QKLNFLFQVLALVTLTlAAGKFMHLISISWMPVIWSAllavfllttsyfagalivhadcflmRNHTITEQpmrfQRVTPL 270
Cdd:PRK13759  135 SQFDFVSDYLAWLREK-APGKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPTNW 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 271 ILQEVKSFLKR-NKLGPFLLLVSFLHVHIPLITTKNFL-------------------------GKSAHGLYGD------- 317
Cdd:PRK13759  185 VGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeeyar 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 318 --------NVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL--ENQFANS-QYGGwngiykggkgmggwegGIRVP 386
Cdd:PRK13759  265 raraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLgdHYLFRKGyPYEG----------------SAHIP 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 387 GIFRWPG---VLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLG-TAQHSDHEFLMH-YCERFLHaar 461
Cdd:PRK13759  329 FIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYSSDN--- 403
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524943 462 WHQRDRgtlWKV--HFVTPVFQpegagacygrkvcpcsgekvvhhdpplLFDLSRDPSEAHVLTPASE 527
Cdd:PRK13759  404 YLTDGK---WKYiwFSQTGEEQ---------------------------LFDLKKDPHELHNLSPSEK 441
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-552 1.77e-31

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: 126.58  E-value: 1.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssvGYRVLQWT 112
Cdd:cd16150     1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHChhplhhgfdyfygmplsmTGDcahWELSEKRVD-LEQ 191
Cdd:cd16150    74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC------------------DSD---EACVRTAIDwLRN 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 192 KLN----FLFqvlalVTLTL------AAGKFMHLISISWMPVIWSAllavfLLTTSYFAGALIvhadcfLMRNHtiteqp 261
Cdd:cd16150   128 RRPdkpfCLY-----LPLIFphppygVEEPWFSMIDREKLPPRRPP-----GLRAKGKPSMLE------GIEKQ------ 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 262 mRFQRVTPLILQEVKsflkrnklgpflllvsflhvhiplittKNFLGKsahglygdnVEEMDWMVGQILDALDTEGLTNS 341
Cdd:cd16150   186 -GLDRWSEERWRELR---------------------------ATYLGM---------VSRLDHQFGRLLEALKETGLYDD 228
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 342 TLIYFASDHG------GSLE---NQFANSQyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFP 412
Cdd:cd16150   229 TAVFFFSDHGdytgdyGLVEkwpNTFEDCL--------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPP 287
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 413 TVVQLAGgeVPQDRVIDGRDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHQRDRGTlwKVHFVTPVFQPEGAGACYG 490
Cdd:cd16150   288 TLLDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQAMEGGHG--PYDLKWPRLLQQEEPPEHT 359
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864524943 491 RKVCPCSGE-KVV--HHDPPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEHQQTLSPVA 552
Cdd:cd16150   360 KAVMIRTRRyKYVyrLYEPDELYDLEADPLELHNL--IGDPAYAEIIAEMKQRLLRWMVETSDVV 422
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-528 1.89e-31

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: 125.75  E-value: 1.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssvgyrv 108
Cdd:cd16155     3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 109 lqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLnCESAGDHCHHP--------LHHGF----DyfygmPLSMTGd 176
Cdd:cd16155    74 ----GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF-ADAAIEFLEEYkdgdkpffMYVAFtaphD-----PRQAPP- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 177 cahwELSEK--RVDLEQKLNFLFQvlalvtltlaagkfmHlisiswmPviwsallavfllttsyFAGALIVHADcflmrn 254
Cdd:cd16155   143 ----EYLDMypPETIPLPENFLPQ---------------H-------P----------------FDNGEGTVRD------ 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 255 htitEQPMRFQRvTPlilQEVKSFLKRNklgpflllvsflhvhiplittknflgksahglYGdNVEEMDWMVGQILDALD 334
Cdd:cd16155   175 ----EQLAPFPR-TP---EAVRQHLAEY--------------------------------YA-MITHLDAQIGRILDALE 213
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 335 TEGLTNSTLIYFASDHGGSL--------ENQFANSqyggwngiykggkgmggweggIRVPGIFRWPGVlPAGRVIGEPTS 406
Cdd:cd16155   214 ASGELDNTIIVFTSDHGLAVgshglmgkQNLYEHS---------------------MRVPLIISGPGI-PKGKRRDALVY 271
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 407 LMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQhsdheflMHYCERFLHAARWHQRDRGTLWKVHFVTPvfqpegag 486
Cdd:cd16155   272 LQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKK-------AVRDTLYGAYRDGQRAIRDDRWKLIIYVP-------- 334
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1864524943 487 acygrkvcpcsGEKVVhhdppLLFDLSRDPSEAHVLtpASEP 528
Cdd:cd16155   335 -----------GVKRT-----QLFDLKKDPDELNNL--ADEP 358
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
34-437 1.41e-29

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


Pssm-ID: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 122.11  E-value: 1.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 113
Cdd:cd16156     1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 aSGGLPTNETTFAKILKEKGYATGLIGKWHLglnceSAGDH-----ChhPLHHGFDYFYGMplsmtgDCAHWELSEKRVd 188
Cdd:cd16156    71 -CMALGDNVKTIGQRLSDNGIHTAYIGKWHL-----DGGDYfgngiC--PQGWDPDYWYDM------RNYLDELTEEER- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 189 leqklnflfqvlalvtltlaagkfmhlisiswmpVIWSALLAVfllttsyfagalivhadcflMRNHTITEQPMRFQRVT 268
Cdd:cd16156   136 ----------------------------------RKSRRGLTS--------------------LEAEGIKEEFTYGHRCT 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 269 PLILQevksFLKRNKLGPFLLLVSFLHVHIPLITTKNF----------LGKSAHglygDNVEE----------------- 321
Cdd:cd16156   162 NRALD----FIEKHKDEDFFLVVSYDEPHHPFLCPKPYasmykdfefpKGENAY----DDLENkplhqrlwagakphedg 233
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 322 ----------------MDWMVGQILDALDtEGLTNSTLIYfASDHGgslENQFANSQYGgwngiykggKGMGGWEGGIRV 385
Cdd:cd16156   234 dkgtikhplyfgcnsfVDYEIGRVLDAAD-EIAEDAWVIY-TSDHG---DMLGAHKLWA---------KGPAVYDEITNI 299
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1864524943 386 PGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGgeVPQDRVIDGRDLLPLL 437
Cdd:cd16156   300 PLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-433 2.42e-29

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


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 117.48  E-value: 2.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSS 103
Cdd:cd16153     2 PNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 104 VGYrvlqWTGASGGLPtnetTFAKILKEKGYATGLIGKWHlglncesagdhchhplhhgfdyfygmplsmtgdcahwels 183
Cdd:cd16153    82 EAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH---------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 184 ekrvdLEQKLNFLFQvlALVTLTLAAGKfmhlisISWMPviwsallavfllttsyfagalivhadcflmrnhtiteqpmr 263
Cdd:cd16153   114 -----LEAFQRYLKN--ANQSYKSFWGK------IAKGA----------------------------------------- 139
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 264 fqrvtplilqevksflKRNKlgPFLLLVSFLHVHIPLITTKNFLGKSA-HGL--YGDNveemdwMVGQILDALDTEGLTN 340
Cdd:cd16153   140 ----------------DSDK--PFFVRLSFLQPHTPVLPPKEFRDRFDyYAFcaYGDA------QVGRAVEAFKAYSLKQ 195
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 341 ---STLIYFASDHGGSLENQFANSQYGGWNgiykggkgmggweGGIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTVV 415
Cdd:cd16153   196 drdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLL 262
                         410
                  ....*....|....*...
gi 1864524943 416 QLAGGEVPQDRVIDGRDL 433
Cdd:cd16153   263 AAAGVDVDAPDYLDGRDL 280
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
34-418 5.31e-29

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: 115.21  E-value: 5.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSvGYRVLQWT 112
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGN-GSADPELP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 113 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqk 192
Cdd:cd00016    80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 193 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplil 272
Cdd:cd00016       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 273 qeVKSFLKRNKLG-PFLLLVSFLHVHIPLittknFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 351
Cdd:cd00016   108 --LLKAIDETSKEkPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864524943 352 GSLEnqfansqygGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLA 418
Cdd:cd00016   181 GIDK---------GHGGDPKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
34-431 1.06e-26

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: 112.26  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSVGYRVL 109
Cdd:cd16147     2 PNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPKF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 110 QWTGAsgglptNETTFAKILKEKGYATGLIGKWhlgLN-CESAGDHCHHPLhhGFDYFYGMP---------LSMTGDCAH 179
Cdd:cd16147    78 WQNGL------ERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVgnstyynytLSNGGNGKH 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 180 WELSEKR--VDL--EQKLNFLfqvlalvTLTLAAGKfmhlisiswmPviwsallavFLLTTSYFAgaliVHAdcflmrNH 255
Cdd:cd16147   147 GVSYPGDylTDViaNKALDFL-------RRAAADDK----------P---------FFLVVAPPA----PHG------PF 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 256 TITEQPMR-FQRVTPL--------ILQEVKSFLKRNKlgpflllvsflhvhiplittknflgksahGLYGDNVEEMDW-- 324
Cdd:cd16147   191 TPAPRYANlFPNVTAPprpppnnpDVSDKPHWLRRLP-----------------------------PLNPTQIAYIDEly 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 325 ------------MVGQILDALDTEGLTNSTLIYFASDHG---GSLENQFANSQ-YggwngiykggkgmggwEGGIRVPGI 388
Cdd:cd16147   242 rkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHRLPPGKRTpY----------------EEDIRVPLL 305
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1864524943 389 FRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGR 431
Cdd:cd16147   306 VRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-452 7.20e-24

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: 102.29  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYR 107
Cdd:cd16035     1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 108 VlQWTgasggLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdhchhplhhgfdyfygmplSMTGDCAHwelsekrv 187
Cdd:cd16035    75 M-QPL-----LSPDVPTLGHMLRAAGYYTAYKGKWHLS--------------------------GAAGGGYK-------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 188 dleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmRNHTITEQPMRFqrv 267
Cdd:cd16035   115 -----------------------------------------------------------------RDPGIAAQAVEW--- 126
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 268 tpliLQEVKSflKRNKLGPFLLLVSFL--H-VHIPLITTKNFlgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLI 344
Cdd:cd16035   127 ----LRERGA--KNADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIV 198
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 345 YFASDHG---GS--LENQFANSqYGgwngiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 419
Cdd:cd16035   199 VFTSDHGemgGAhgLRGKGFNA-YE----------------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAG 261
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1864524943 420 GEVPQDRVID----GRDLLPLLLGTAQHSDHE-FLMHY 452
Cdd:cd16035   262 VDAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
34-444 9.84e-24

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: 103.20  E-value: 9.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEFGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSVGYRVLQw 111
Cdd:cd16154     1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 112 tgasgglpTNETTFAKILKE---KGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEKRVD 188
Cdd:cd16154    78 --------SEETLLQLLIKDattAGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQT 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 189 LEQKlnflfqvlalvtlTLAAGKFMHLiSISWM-----PviWSALLAvfllttsYFAgalivhadcflmrNHTiteqpmr 263
Cdd:cd16154   144 TNST-------------EYATTKLTNL-AIDWIdqqtkP--WFLWLA-------YNA-------------PHT------- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 264 fqrvtplilqevksflkrnklgPFLLLVSFLHvhiplitTKNFLGKSAHglYGDN--------VEEMDWMVGQILDALDT 335
Cdd:cd16154   181 ----------------------PFHLPPAELH-------SRSLLGDSAD--IEANprpyylaaIEAMDTEIGRLLASIDE 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 336 EGLTNsTLIYFASDHG--------GSLENQFANSQY-GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPTS 406
Cdd:cd16154   230 EEREN-TIIIFIGDNGtpgqvvdlPYTRNHAKGSLYeGG-----------------INVPLIVSGAGV---ERANERESA 288
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1864524943 407 LM---DVFPTVVQLAGGEVPQdrVIDGRDLLPLLLGTAQHS 444
Cdd:cd16154   289 LVnatDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNAST 327
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
34-517 3.58e-16

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: 80.28  E-value: 3.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssvgyRVLQWTG 113
Cdd:cd16171     1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESWN 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 114 ASGGLPTNETTFAKILKEKGYATGLIGKwhlglncesagdhchhplhhgFDYFYGmplsmtgdcaHWELSEKRVDLEQKL 193
Cdd:cd16171    70 NYKGLDPNYPTWMDRLEKHGYHTQKYGK---------------------LDYTSG----------HHSVSNRVEAWTRDV 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 194 NFLFQVLALVTLTLAAGKfmhlisiswmpviwsallavfllttsyfagalivHADCFLMRNHTITEQPMRFQRVTPLILQ 273
Cdd:cd16171   119 PFLLRQEGRPTVNLVGDR----------------------------------STVRVMLKDWQNTDKAVHWIRKEAPNLT 164
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 274 EvksflkrnklgPFLLlvsFLHVHIPLITTKNFLGKSAHGL------YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFA 347
Cdd:cd16171   165 Q-----------PFAL---YLGLNLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTYVFFT 230
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 348 SDHGG-SLEN-QFAN-SQYGGwngiykggkgmggwegGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQ 424
Cdd:cd16171   231 SDHGElAMEHrQFYKmSMYEG----------------SSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 425 DrvIDGRDLLPLLLGTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTLWKvhFVTpvfqpegagacYGrkv 493
Cdd:cd16171   294 N--LSGYSLLPLLSESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YA--- 349
                         490       500
                  ....*....|....*....|....
gi 1864524943 494 cpcSGEKVvhhdPPLLFDLSRDPS 517
Cdd:cd16171   350 ---DGNSV----PPQLFDLSKDPD 366
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
34-419 4.23e-10

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: 60.77  E-value: 4.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  34 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSVGYRvl 109
Cdd:cd16015     1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 110 qwtgasgglPTNETTFAKILKEKGYATGLIgkwhlglncesagdHCHHP---------LHHGFDYFYG---MPLSMTGDc 177
Cdd:cd16015    77 ---------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFYDledFPDDEKET- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 178 AHWELSEKrvdleqklnFLFQVLALVTLTLAAGKFMhlisiswmpviwsallaVFLLTTSyfagalivhadcflmrNHti 257
Cdd:cd16015   133 NGWGVSDE---------SLFDQALEELEELKKKPFF-----------------IFLVTMS----------------NH-- 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 258 teqpmrfqrvtplilqevksflkrnklGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYgdnveEMDWMVGQILDALDTEG 337
Cdd:cd16015   169 ---------------------------GPYDLPEEKKDEPLKVEEDKTELENYLNAIH-----YTDKALGEFIEKLKKSG 216
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 338 LTNSTLIYFASDHGGSLENQFANSQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTVVQL 417
Cdd:cd16015   217 LYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDL 281

                  ..
gi 1864524943 418 AG 419
Cdd:cd16015   282 LG 283
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
22-434 9.87e-08

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 55.04  E-value: 9.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  22 APSASSDVSASWPNILLLM----ADDLgigdIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVR 97
Cdd:COG1368   223 RPTPNPFGPAKKPNVVVILlesfSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLP 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  98 SG-MVSSVGYRVLQwtgasgglptnetTFAKILKEKGYATgligkwhlglncesagdHCHHP------------LHHGFD 164
Cdd:COG1368   299 GGsPYKRPGQNNFP-------------SLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFD 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 165 YFYG---MPLSMTGdcaHWELSEKrvdleqklnFLFQvLALVTLTLAAGKFMhlisiswmpviwsallaVFLLTTSyfag 241
Cdd:COG1368   349 EFYDredFDDPFDG---GWGVSDE---------DLFD-KALEELEKLKKPFF-----------------AFLITLS---- 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 242 alivhadcflmrNHTITEQPMRFQRVTPLILQEVKSFLKrnklgpflllvsflHVHiplittknflgksahglygdnveE 321
Cdd:COG1368   395 ------------NHGPYTLPEEDKKIPDYGKTTLNNYLN--------------AVR-----------------------Y 425
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 322 MDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYggwngiykggkgmggwEGGIRVPGIFRWPGvLPAGRVI 401
Cdd:COG1368   426 ADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENP----------------LERYRVPLLIYSPG-LKKPKVI 488
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1864524943 402 GEPTSLMDVFPTVVQLAGGEVPQDRVIdGRDLL 434
Cdd:COG1368   489 DTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
15-189 1.25e-06

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 50.90  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  15 LSVLLSLAPSASSDVSASWPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEFGVKLTQHISAA-SLCTPSRAAFLTGR 93
Cdd:COG1524     5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943  94 YPVRSGMVSSVGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIGKWHLGlncESAGDHCHHPLHH-G 162
Cdd:COG1524    80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdG 156
                         170       180
                  ....*....|....*....|....*....
gi 1864524943 163 FDYFYGMPLS--MTGDCAHWELSEKRVDL 189
Cdd:COG1524   157 RKPLLGNPAAdrWIAAAALELLREGRPDL 185
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
319-416 2.41e-06

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: 50.29  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524943 319 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-ENQ----FANSQYGGWNgiykggkgmggweggIRVPGIFRWPG 393
Cdd:COG3083   433 VHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnENGqnywGHNSNFSRYQ---------------LQVPLVIHWPG 497
                          90       100
                  ....*....|....*....|...
gi 1864524943 394 VLPagRVIGEPTSLMDVFPTVVQ 416
Cdd:COG3083   498 TPP--QVISKLTSHLDIVPTLMQ 518
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
317-351 6.26e-03

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


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 38.94  E-value: 6.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1864524943 317 DNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 351
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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