|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-478 |
0e+00 |
|
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: 557.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPEWNIAYSTAI 96
Cdd:cd16033 2 NILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PETDWTYTQALRDAGYNVGMVGKYHCGT-NLPDKFGCDDdtfwgaenpvaneeyvaWLkendlppvkahdiwrgklpgnr 175
Cdd:cd16033 82 PPGVETFSEDLREAGYRNGYVGKWHVGPeETPLDYGFDE-----------------YL---------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 176 dghiiaarleqPEEATFERFIADRSIARLRqyakEYKETGKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDVMLPKSFGDT 255
Cdd:cd16033 123 -----------PVETTIEYFLADRAIEMLE----ELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADD 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 256 LVGKPPVQQNYATYWSTSSFDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLNDKG 335
Cdd:cd16033 188 FEDKPYIYRRERKRWGVDTEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 336 PAMYDDIYRIPFIARIPGLTH-GTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEVPDWRRNIVCEFHGLH 414
Cdd:cd16033 268 PFMYEETYRIPLIIKWPGVIAaGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPEDWRDEVVTEYNGHE 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136219 415 FPIQQRMLRTDDYKLVINHESLDELYDLRQDPSEINNVYAAPAYDKVRREMAAELYRQLVERGD 478
Cdd:cd16033 348 FYLPQRMVRTDRYKYVFNGFDIDELYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETGD 411
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
17-478 |
4.09e-106 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 322.21 E-value: 4.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPEwniAYSTAI 96
Cdd:COG3119 25 NILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE---GYNGGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PETDWTYTQALRDAGYNVGMVGKYHcgtnlpdkFGCDDDtfwgaenpvaneeyvawlkendlppvkahdiwrgklpgnrd 176
Cdd:COG3119 102 PPDEPTLAELLKEAGYRTALFGKWH--------LYLTDL----------------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 177 ghiiaarleqpeeatferfIADRSIARLRQYAKEyketGKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDVMLPKSFGDTl 256
Cdd:COG3119 133 -------------------LTDKAIDFLERQADK----DKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPNLAPR- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 257 vgkppvqqnyatywstsSFDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLN-DKG 335
Cdd:COG3119 189 -----------------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRgGKG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 336 pAMYDDIYRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGvEVPDWRRNIVCEFHGlh 414
Cdd:COG3119 252 -TLYEGGIRVPLIVRWPGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTG-EKAEWRDYLYWEYPR-- 327
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585136219 415 fPIQQRMLRTDDYKLVINHESLD--ELYDLRQDPSEINNVYAapAYDKVRREMAAELYRQLVERGD 478
Cdd:COG3119 328 -GGGNRAIRTGRWKLIRYYDDDGpwELYDLKNDPGETNNLAA--DYPEVVAELRALLEAWLKELGD 390
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
16-471 |
7.10e-94 |
|
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: 291.74 E-value: 7.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 16 RNIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANpewniaYSTA 95
Cdd:cd16031 3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDN------NGPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 IPETDWTYTQALRDAGYNVGMVGKYHcgtnlpdkfgcdddtfwgaenpvaneeyvawLKENDLPPVKAHDIWRGkLPGNR 175
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGKWH-------------------------------LGSGGDLPPPGFDYWVS-FPGQG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 176 -----DGHIIAARLEQPEEATfeRFIADRSIARLRQYAKEyketgKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDVMLPK 250
Cdd:cd16031 125 syydpEFIENGKRVGQKGYVT--DIITDKALDFLKERDKD-----KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 251 SFG-DTLVGKPPVQQNYATYW---STSSFDNDQ-WRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEF 325
Cdd:cd16031 198 TFDdDDYAGRPEWAREQRNRIrgvLDGRFDTPEkYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 326 TGSHRLNDKGpAMYDDIYRIPFIARIPGLT-HGTKCNDYVQLIDMTATFMEIAGLD-PAQVeDGRSVVDLARGVEVPDWR 403
Cdd:cd16031 278 LGEHGLFDKR-LMYEESIRVPLIIRDPRLIkAGTVVDALVLNIDFAPTILDLAGVPiPEDM-QGRSLLPLLEGEKPVDWR 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136219 404 RNIVCEFHGL---HFPIQQRMLRTDDYKLV--INHESLDELYDLRQDPSEINNVYAAPAYDKVRREMAAELYR 471
Cdd:cd16031 356 KEFYYEYYEEpnfHNVPTHEGVRTERYKYIyyYGVWDEEELYDLKKDPLELNNLANDPEYAEVLKELRKRLEE 428
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-478 |
3.24e-85 |
|
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: 269.10 E-value: 3.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 16 RNIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPF--KHQTLanpewniayS 93
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHvnGHRTL---------H 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 94 TAIPETDWTYTQALRDAGYNVGMVGKYHCgtnLPDKFgcdddtfwgaenpvANEEYVAWlkendlppvkahdiwrgklpg 173
Cdd:cd16150 72 HLLRPDEPNLLKTLKDAGYHVAWAGKNDD---LPGEF--------------AAEAYCDS--------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 174 nrdghiiaarleqpEEATferfiADRSIARLRQYakeykETGKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDVMLPKSFG 253
Cdd:cd16150 114 --------------DEAC-----VRTAIDWLRNR-----RPDKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPPRRPPG 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 254 DTLVGKPPVQQNYATYwSTSSFDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLND 333
Cdd:cd16150 170 LRAKGKPSMLEGIEKQ-GLDRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 334 KGP-AMYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGvEVPDWRRNIVCE--- 409
Cdd:cd16150 249 KWPnTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAG-ETEEHRDAVFSEggr 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 410 -------FHGLHFP--------IQQR---------MLRTDDYKLVINHESLDELYDLRQDPSEINNVYAAPAYDKVRREM 465
Cdd:cd16150 328 lhgeeqaMEGGHGPydlkwprlLQQEeppehtkavMIRTRRYKYVYRLYEPDELYDLEADPLELHNLIGDPAYAEIIAEM 407
|
490
....*....|...
gi 585136219 466 AAELYRQLVERGD 478
Cdd:cd16150 408 KQRLLRWMVETSD 420
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
16-469 |
7.08e-79 |
|
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: 254.23 E-value: 7.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 16 RNIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANpewniaySTA 95
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN-------CMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 IPETDWTYTQALRDAGYNVGMVGKYHC-GTnlpDKFG---C----DDDTFWGAENpvaneeYVAWLKENDLppvkahDIW 167
Cdd:cd16156 74 LGDNVKTIGQRLSDNGIHTAYIGKWHLdGG---DYFGngiCpqgwDPDYWYDMRN------YLDELTEEER------RKS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 168 RgKLPGNRDGHIIaarleqPEEATFERFIADRSIARLRQYAKEyketgkPFSLDVHFFGPHLPYFLPDEWFDLMdpKDVM 247
Cdd:cd16156 139 R-RGLTSLEAEGI------KEEFTYGHRCTNRALDFIEKHKDE------DFFLVVSYDEPHHPFLCPKPYASMY--KDFE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 248 LPK--SFGDTLVGKPPVQQNYATywSTSSFDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGlmDDTAMFFCADHGEF 325
Cdd:cd16156 204 FPKgeNAYDDLENKPLHQRLWAG--AKPHEDGDKGTIKHPLYFGCNSFVDYEIGRVLDAADEIA--EDAWVIYTSDHGDM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 326 TGSHRLNDKGPAMYDDIYRIPFIARIPGLTHGTKCNDY-VQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEVPDwRR 404
Cdd:cd16156 280 LGAHKLWAKGPAVYDEITNIPLIIRGKGGEKAGTVTDTpVSHIDLAPTILDYAGIPQPKVLEGESILATIEDPEIPE-NR 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585136219 405 NIVCEFH----------GLHFpiqQRMLRTDDYKLVINHESLDELYDLRQDPSEINNVYAAPAYDKVRREMAAEL 469
Cdd:cd16156 359 GVFVEFGryevdhdgfgGFQP---VRCVVDGRYKLVINLLSTDELYDLEKDPYEMHNLIDDPDYADVRDQLHDEL 430
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
17-473 |
1.19e-76 |
|
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: 245.50 E-value: 1.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDqhriDT---LGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPfkHQTlaNPEWNIAYS 93
Cdd:cd16027 2 NILWIIAD----DLspdLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYP--HQN--GAHGLRSRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 94 TAIPETDWTYTQALRDAGYNVGMVGKYHcgtnlpdkfgcdddtfwgaENPVANEeyvAWLKENDLPPVKAHDIWRGKlpg 173
Cdd:cd16027 74 FPLPDGVKTLPELLREAGYYTGLIGKTH-------------------YNPDAVF---PFDDEMRGPDDGGRNAWDYA--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 174 nrdghiiaarleqpeeATFERFIADRsiarlrqyakeykETGKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDVMLPKSFG 253
Cdd:cd16027 129 ----------------SNAADFLNRA-------------KKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYLP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 254 DTlvgkPPVQQNYATYWSTssfdndqwrkliavywgyVAMIDFEIGRILDVARELGLMDDTAMFFCADHGE-FTGShrln 332
Cdd:cd16027 180 DT----PEVREDLADYYDE------------------IERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMpFPRA---- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 333 dKGpAMYDDIYRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEVPDWRRNI-VCEF 410
Cdd:cd16027 234 -KG-TLYDSGLRVPLIVRWPGkIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGRDYVFaERDR 311
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136219 411 HG-LHFPIqqRMLRTDDYKLVINHESlDELYDLRQDPSEINNVYAAPAYDKVRREMAAELYRQL 473
Cdd:cd16027 312 HDeTYDPI--RSVRTGRYKYIRNYMP-EELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWM 372
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-446 |
2.04e-76 |
|
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: 243.22 E-value: 2.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 16 RNIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANpewNIAYSTA 95
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDN---ADPYDGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 IPetdwTYTQALRDAGYNVGMVGKYHcgtnlpdkF-GCDDDTFWgaenpvaneeyvawlkendlppvkahdiwrgklpgn 174
Cdd:cd16037 78 VP----SWGHALRAAGYETVLIGKLH--------FrGEDQRHGF------------------------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 175 rdghiiaarleqpeeaTFERFIADRSIArlrqYAKEYKETGKPFSLDVHFFGPHLPYFLPDEWFDLmdpkdvmlpksfgd 254
Cdd:cd16037 110 ----------------RYDRDVTEAAVD----WLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDL-------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 255 tlvgkppvqqnYAtywstssfdndqwRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLNDK 334
Cdd:cd16037 156 -----------YV-------------RRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGK 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 335 GpAMYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEvpDWRRNIVCEFHGLH 414
Cdd:cd16037 212 S-TMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPD--DPDRVVFSEYHAHG 288
|
410 420 430
....*....|....*....|....*....|..
gi 585136219 415 FPIQQRMLRTDDYKLVINHESLDELYDLRQDP 446
Cdd:cd16037 289 SPSGAFMLRKGRWKYIYYVGYPPQLFDLENDP 320
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
16-469 |
3.46e-74 |
|
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: 241.39 E-value: 3.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 16 RNIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPewniaysTA 95
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNG-------TP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 IPETDWTYTQALRDAGYNVGMVGKYHCGTNlPDKFGCDDDTFWGAenpvaneeyvaWLKENDLPPVKAHDiwrgklpgnr 175
Cdd:cd16028 74 LDARHLTLALELRKAGYDPALFGYTDTSPD-PRGLAPLDPRLLSY-----------ELAMPGFDPVDRLD---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 176 dghiiaarlEQPEEATFERFIADRSIARLRQYAkeyketGKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDVMLPKSFGD- 254
Cdd:cd16028 132 ---------EYPAEDSDTAFLTDRAIEYLDERQ------DEPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPPIRAESl 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 255 -----------TLVGKPPVQQNYATYWSTSSFDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHG 323
Cdd:cd16028 197 aaeaaqhpllaAFLERIESLSFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 324 EFTGSHRLNDKGpAMYDDIYRIPFIARIPG----LTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEV 399
Cdd:cd16028 277 EQLGDHWLWGKD-GFFDQAYRVPLIVRDPRreadATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 400 PDWRRNIVCEF---HGLHFPIQQR-----------MLRTDDYKLViNHESLDE-LYDLRQDPSEINNVYAAPAYDKVRRE 464
Cdd:cd16028 356 SDWRDAVHYEYdfrDVSTRRPQEAlglspdecslaVIRDERWKYV-HFAALPPlLFDLKNDPGELRDLAADPAYAAVVLR 434
|
....*
gi 585136219 465 MAAEL 469
Cdd:cd16028 435 YAQKL 439
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
17-479 |
7.81e-71 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 233.79 E-value: 7.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLAnpewniaYSTAI 96
Cdd:PRK13759 8 NIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG-------YGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PetdWTYT----QALRDAGYNVGMVGKYH-------CGTN--LPDKFGCDDDTFWGAENPVANEEYVAWLKENDL-PPVK 162
Cdd:PRK13759 81 P---WNYKntlpQEFRDAGYYTQCIGKMHvfpqrnlLGFHnvLLHDGYLHSGRNEDKSQFDFVSDYLAWLREKAPgKDPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 163 AHDIwrgklpGNRDGHIIAARLEQPEEATFERFIADRSIARLRQYakeykETGKPFSLDVHFFGPHLPYFLPDEWFDLMd 242
Cdd:PRK13759 158 LTDI------GWDCNSWVARPWDLEERLHPTNWVGSESIEFLRRR-----DPTKPFFLKMSFARPHSPYDPPKRYFDMY- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 243 pKDVMLPKSF-GDTLVGKPPVQQNYATYWSTSSFDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCAD 321
Cdd:PRK13759 226 -KDADIPDPHiGDWEYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 322 HGEFTGSHRLNDKGPAmYDDIYRIPFIARIPG----LTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGV 397
Cdd:PRK13759 305 HGDMLGDHYLFRKGYP-YEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFGQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 398 EvPDWRRnivcEFHGLHFPIQQ--RMLRTDDYKLVIN-HESLDELYDLRQDPSEINNVYAAPAYDKVRREMAAELYRQLV 474
Cdd:PRK13759 384 Y-EGWRP----YLHGEHALGYSsdNYLTDGKWKYIWFsQTGEEQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVDHLR 458
|
....*
gi 585136219 475 ERGDS 479
Cdd:PRK13759 459 GREEG 463
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
17-389 |
3.48e-66 |
|
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: 213.45 E-value: 3.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPEWNiaysTAI 96
Cdd:cd16022 2 NILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNG----GGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PETDWTYTQALRDAGYNVGMVGKYHcgtnlpdkfgcdddtfwgaenpvaneeyvawlkendlppvkahdiwrgklpgnrd 176
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 177 ghiiaarleqpeeatferfiaDRSIARLRQYAKEyketgKPFSLDVHFFGPHLPYflpdewfdlmdpkdvmlpksfgdtl 256
Cdd:cd16022 103 ---------------------DEAIDFIERRDKD-----KPFFLYVSFNAPHPPF------------------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 257 vgkppvqqnyatywstssfdndqwrkliaVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLNDKGP 336
Cdd:cd16022 132 -----------------------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKG 182
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 585136219 337 AMYDDIYRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRS 389
Cdd:cd16022 183 SLYEGGIRVPFIVRWPGkIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-451 |
4.85e-65 |
|
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: 215.90 E-value: 4.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANpewniaySTAI 96
Cdd:cd16034 3 NILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN-------DVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PETDWTYTQALRDAGYNVGMVGKYHCGTNlPDKFGCDDDTFWgaenpvaneeyvawlkendlPPVKAH--DIWRGKlpGN 174
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLDGP-ERNDGRADDYTP--------------------PPERRHgfDYWKGY--EC 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 175 RDGHIIAAR-LEQPEEATFERFIADRSIARLRQYAKEYKETGKPFSLDVHFFGPHLPYFL-PDEWFDLMDPKDVMLPKsf 252
Cdd:cd16034 133 NHDHNNPHYyDDDGKRIYIKGYSPDAETDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRP-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 253 gdtlvgKPPVQQNYAtywstssfdnDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLN 332
Cdd:cd16034 211 ------NVPEDKKEE----------AGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 333 DKG-PamYDDIYRIPFIARIPGLTH-GTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEvPDWRRN--IVC 408
Cdd:cd16034 275 NKQvP--YEESIRVPFIIRYPGKIKaGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGK-DDEPDSvlLQC 351
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 585136219 409 EFHGLHFPIQQ----RMLRTDDYKLVI--NHESLdeLYDLRQDPSEINN 451
Cdd:cd16034 352 FVPFGGGSARDggewRGVRTDRYTYVRdkNGPWL--LFDNEKDPYQLNN 398
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
29-458 |
1.04e-62 |
|
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: 210.89 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 29 DTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPEWniaYSTAIPetDWTyT--QA 106
Cdd:cd16030 15 PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY---FRKVAP--DAV-TlpQY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 107 LRDAGYNVGMVGK-YHcgtnlPDKFGCDDDTF-WGAE-NPVANEEYvawlkendlPPVKAHDIWRGKLPGNRdgHIIAAR 183
Cdd:cd16030 89 FKENGYTTAGVGKiFH-----PGIPDGDDDPAsWDEPpNPPGPEKY---------PPGKLCPGKKGGKGGGG--GPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 184 LEQPEEATFERFIADRSIARLRQYakeyKETGKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDVMLPKSFGDtlVGKPPV- 262
Cdd:cd16030 153 ADVPDEAYPDGKVADEAIEQLRKL----KDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPLPNPFDP--IDLPEVa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 263 ------------QQNYATYWSTSSFDNDQWRKLIavyWGY---VAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTG 327
Cdd:cd16030 227 wndlddlpkygdIPALNPGDPKGPLPDEQARELR---QAYyasVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 328 SHRLNDKGpAMYDDIYRIPFIARIPGLT-HGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEVPdWRRNI 406
Cdd:cd16030 304 EHGHWGKH-TLFEEATRVPLIIRAPGVTkPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLKNPSAK-WKDAA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 585136219 407 VCEFHglHFPIQQRMLRTDDYKLVI----NHESLDELYDLRQDPSEINNVYAAPAY 458
Cdd:cd16030 382 FSQYP--RPSIMGYSIRTERYRYTEwvdfDKVGAEELYDHKNDPNEWKNLANDPEY 435
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-470 |
6.76e-60 |
|
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: 201.64 E-value: 6.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTP----SAICTPARSSMLTGQlpfkhqTLanpeWNI-- 90
Cdd:cd16155 4 NILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR------TL----FHApe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 91 AYSTAIPETDWTYTQALRDAGYNVGMVGKYHcgtnlpdkfgcdddtfwgaeNPVANeeyvawlkendlppvkahdiwrgk 170
Cdd:cd16155 74 GGKAAIPSDDKTWPETFKKAGYRTFATGKWH--------------------NGFAD------------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 171 lpgnrdghiiAArleqpeeatfERFIadrsiarlrqyaKEYKETGKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDVMLPK 250
Cdd:cd16155 110 ----------AA----------IEFL------------EEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPE 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 251 SFGDtlvgKPPVQQN--------YATYWSTSsfdnDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADH 322
Cdd:cd16155 158 NFLP----QHPFDNGegtvrdeqLAPFPRTP----EAVRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDH 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 323 GEFTGSHRLNDKgPAMYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGvEVPDW 402
Cdd:cd16155 230 GLAVGSHGLMGK-QNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRG-EKKAV 307
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 403 RRNIVCEFHGLhfpiqQRMLRTDDYKLVINHESLD--ELYDLRQDPSEINNVYAAPAYDKVRREMAAELY 470
Cdd:cd16155 308 RDTLYGAYRDG-----QRAIRDDRWKLIIYVPGVKrtQLFDLKKDPDELNNLADEPEYQERLKKLLAELK 372
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-469 |
2.47e-59 |
|
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: 201.62 E-value: 2.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQT-------------- 82
Cdd:cd16144 2 NIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdvipgrrgppdnt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 83 -LANPEWNiaysTAIPETDWTYTQALRDAGYNVGMVGKYHCG---TNLPDKFGCdDDTFWGAENPVANEEYVAWLKENDL 158
Cdd:cd16144 82 kLIPPPST----TRLPLEEVTIAEALKDAGYATAHFGKWHLGgegGYGPEDQGF-DVNIGGTGNGGPPSYYFPPGKPNPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 159 PPvkahdiwrgklPGNRDGHIIaarleqpeeatfERfIADRSIARLRQYAKeyketgKPFSLDVHFFGPHLPYFLPDEWF 238
Cdd:cd16144 157 LE-----------DGPEGEYLT------------DR-LTDEAIDFIEQNKD------KPFFLYLSHYAVHTPIQARPELI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 239 DLMDPKDvmlpksfgdtlvGKPPVQQNYATywstssfdndqwrkliavywgYVAMI---DFEIGRILDVARELGLMDDTA 315
Cdd:cd16144 207 EKYEKKK------------KGLRKGQKNPV---------------------YAAMIeslDESVGRILDALEELGLADNTL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 316 MFFCADHG-EFTGSHRLNDKGP--AMYDDIY----RIPFIARIPGLTH-GTKCNDYVQLIDMTATFMEIAGLDPAQVE-- 385
Cdd:cd16144 254 VIFTSDNGgLSTRGGPPTSNAPlrGGKGSLYeggiRVPLIVRWPGVIKpGSVSDVPVIGTDLYPTFLELAGGPLPPPQhl 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 386 DGRSVVDLARGVEVPDWRRNIVceFhglHFPIQQRM-------LRTDDYKLVINHES-LDELYDLRQDPSEINNVyaAPA 457
Cdd:cd16144 334 DGVSLVPLLKGGEADLPRRALF--W---HFPHYHGQggrpasaIRKGDWKLIEFYEDgRVELYNLKNDIGETNNL--AAE 406
|
490
....*....|..
gi 585136219 458 YDKVRREMAAEL 469
Cdd:cd16144 407 MPEKAAELKKKL 418
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
17-446 |
8.63e-56 |
|
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: 189.33 E-value: 8.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPewnIAYSTAI 96
Cdd:cd16032 2 NILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA---AEFPADI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PetdwTYTQALRDAGYNVGMVGKYH-CGtnlPDKF-GCDDDtfwgaenpvaneeyvawlkendlppvkahdiwrgklpgn 174
Cdd:cd16032 79 P----TFAHYLRAAGYRTALSGKMHfVG---PDQLhGFDYD--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 175 rdghiiaarleqpEEATFerfiadRSIARLRQYAKEykETGKPFSLDVHFFGPHLPYFLPDEWFDLmdpkdvmlpksfgd 254
Cdd:cd16032 113 -------------EEVAF------KAVQKLYDLARG--EDGRPFFLTVSFTHPHDPYVIPQEYWDL-------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 255 tlvgkppvqqnYAtywstssfdndqwRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLNDK 334
Cdd:cd16032 158 -----------YV-------------RRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYK 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 335 gPAMYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLDPAQVE---DGRSVVDLARGVEvPDWRRNIVCEFH 411
Cdd:cd16032 214 -MSFFEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVpplDGRSLLPLLEGGD-SGGEDEVISEYL 291
|
410 420 430
....*....|....*....|....*....|....*..
gi 585136219 412 --GLHFPIqqRMLRTDDYKLVINHESLDELYDLRQDP 446
Cdd:cd16032 292 aeGAVAPC--VMIRRGRWKFIYCPGDPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-475 |
8.87e-55 |
|
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: 188.21 E-value: 8.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANpewniaySTAI 96
Cdd:cd16152 3 NVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-------GIPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PETDWTYTQALRDAGYNVGMVGKYHcgtnlpdkfgcdddtfwgaenpvaneeyvawlkendlppvkahdiwrgkLPGNR- 175
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWH-------------------------------------------------LAGYRv 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 176 DghiiaarleqpeeatferFIADRSIARLRQYAKEyketgKPFSLDVHFFGPHlpyflpdewfDLMDPKDVMLPKSFgdt 255
Cdd:cd16152 107 D------------------ALTDFAIDYLDNRQKD-----KPFFLFLSYLEPH----------HQNDRDRYVAPEGS--- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 256 lvgkppvQQNYATYW---STSSFDNDqWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHgeftGSH--- 329
Cdd:cd16152 151 -------AERFANFWvppDLAALPGD-WAEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrt 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 330 RLNDKGPAMYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGvEVPDWRRNI--- 406
Cdd:cd16152 219 RNAEYKRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDG-KVEDWRNEVfiq 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 407 VCEFH-GlhfpiqqRMLRTDDYKLVINHESLD-------------ELYDLRQDPSEINNVYAAPAYDKVRREMAAELYRQ 472
Cdd:cd16152 298 ISESQvG-------RAIRTDRWKYSVAAPDKDgwkdsgsdvyvedYLYDLEADPYELVNLIGRPEYREVAAELRERLLAR 370
|
...
gi 585136219 473 LVE 475
Cdd:cd16152 371 MAE 373
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-452 |
6.34e-54 |
|
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: 187.03 E-value: 6.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPEwnIAYSTAI 96
Cdd:cd16145 2 NIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSE--PGGQDPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PETDWTYTQALRDAGYNVGMVGKYHCG----TNLPDKFGCddDTFWGAENPV-ANEEYVAWLKENDLppvkahdiwRGKL 171
Cdd:cd16145 80 PPDDVTLAEVLKKAGYATAAFGKWGLGgpgtPGHPTKQGF--DYFYGYLDQVhAHNYYPEYLWRNGE---------KVPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 172 PGNRDGHIIAARLEQPEEATF-ERFIADRSIarlrQYAKEYKEtgKPFSLDVHFFGPHLPYFLPDEWFDLMDPKDvmlpk 250
Cdd:cd16145 149 PNNVIPPLDEGNNAGGGGGTYsHDLFTDEAL----DFIRENKD--KPFFLYLAYTLPHAPLQVPDDGPYKYKPKD----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 251 sfgdtlvgkppvqqnyatywsTSSFDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHG---EFTG 327
Cdd:cd16145 218 ---------------------PGIYAYLPWPQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGphsEGGS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 328 SHR---LNDKGP------AMYDDIYRIPFIARIPGLTH-GTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGV 397
Cdd:cd16145 277 EHDpdfFDSNGPlrgykrSLYEGGIRVPFIARWPGKIPaGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGK 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 585136219 398 EVPDWRRNIVCEFhglHFPIQQRMLRTDDYKLVINHESLD--ELYDLRQDPSEINNV 452
Cdd:cd16145 357 PQQQQHDYLYWEF---YEGGGAQAVRMGGWKAVRHGKKDGpfELYDLSTDPGETNNL 410
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-453 |
1.53e-48 |
|
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: 172.00 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHA-QTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQtLANPEWNIAYSTA 95
Cdd:cd16143 2 NIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSR-LKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 IPETDWTYTQALRDAGYNVGMVGKYHcgtnlpdkFGCDDDTFWGAENPVANEEYVAWLKendlpPVKahdiwrgklpgnr 175
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKWH--------LGLDWKKKDGKKAATGTGKDVDYSK-----PIK------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 176 DGhiiaarleqPEEATFERF-----------IADRSIARLRQYAKEyketGKPFSLDVHFFGPHLPYFLPDEWfdlmdpk 244
Cdd:cd16143 135 GG---------PLDHGFDYYfgipasevlptLTDKAVEFIDQHAKK----DKPFFLYFALPAPHTPIVPSPEF------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 245 dvmlpksfgdtlVGKppvqqnyatywSTSSfdndqwrkliaVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGe 324
Cdd:cd16143 195 ------------QGK-----------SGAG-----------PYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNG- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 325 ftGSHRLNDKGPAMYD------------DIY----RIPFIARIPGLT-HGTKCNDYVQLIDMTATFMEIAG--LDPAQVE 385
Cdd:cd16143 240 --PSPYADYKELEKFGhdpsgplrgmkaDIYegghRVPFIVRWPGKIpAGSVSDQLVSLTDLFATLAAIVGqkLPDNAAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 386 DGRSVVDLARGVEVPDWRRNIVCefhglHFPIQQRMLRTDDYKLVINHESLD---------------ELYDLRQDPSEIN 450
Cdd:cd16143 318 DSFSFLPALLGPKKQEVRESLVH-----HSGNGSFAIRKGDWKLIDGTGSGGfsyprgkeklglppgQLYNLSTDPGESN 392
|
...
gi 585136219 451 NVY 453
Cdd:cd16143 393 NLY 395
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-392 |
2.07e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 157.32 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQtlanpewniAYSTAI 96
Cdd:cd16148 2 NVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG---------VWGGPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PETDWTYTQALRDAGYNVGMVgkyHCGTNLPDKFGCDDDTFwgaenpvaneeyvawlkendlppvkaHDIWRGKLPGNRD 176
Cdd:cd16148 73 EPDDPTLAEILRKAGYYTAAV---SSNPHLFGGPGFDRGFD--------------------------TFEDFRGQEGDPG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 177 GhiiaarleqpEEATFERFIADRSIARLRQYAKEyketgKPFSLDVHFFGPHLPYflpdewfdlmdpkdvmlpksfgdtl 256
Cdd:cd16148 124 E----------EGDERAERVTDRALEWLDRNADD-----DPFFLFLHYFDPHEPY------------------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 257 vgkppvqqNYAtywstssfdndqwrkliavywGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLNDK-G 335
Cdd:cd16148 164 --------LYD---------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhG 214
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 585136219 336 PAMYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVD 392
Cdd:cd16148 215 SNLYDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-392 |
3.60e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 156.24 E-value: 3.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLA-NPEWNIAYstA 95
Cdd:cd16149 2 NILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDwIVEGSHGK--T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 IPETDW-----TYTQALRDAGYNVGMVGKYHCGTNLPDKFgcdddtfwgaenpvaneeyvawlkendlppvkahdiwrgk 170
Cdd:cd16149 80 KKPEGYlegqtTLPEVLQDAGYRCGLSGKWHLGDDAADFL---------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 171 lpgnrdghiiaarleqpeeatferfiadrsiarLRQYAKEyketgKPFSLDVHFFGPHLPyflpdewfdlmdpkdvmlpk 250
Cdd:cd16149 120 ---------------------------------RRRAEAE-----KPFFLSVNYTAPHSP-------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 251 sfgdtlvgkppvqqnyatywstssfdndqwrkliavyWGYVAM---IDFEIGRILDVARELGLMDDTAMFFCADHGEFTG 327
Cdd:cd16149 142 -------------------------------------WGYFAAvtgVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMG 184
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136219 328 SHRLNDKG-----PAMYDDIYRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGLDPAQVED--GRSVVD 392
Cdd:cd16149 185 HHGIWGKGngtfpLNMYDNSVKVPFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFAD 257
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
17-469 |
7.59e-43 |
|
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: 156.94 E-value: 7.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKaFTPSAICTPARSSMLTGQLPFK---HQTlaNPEWNIAYS 93
Cdd:cd16146 2 NVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHT--ILGRERMRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 94 TaipETdwTYTQALRDAGYNVGMVGKYHCGTNLP--------DKF-----GCDDDTFwgaeNPVANEEYVAWLKENDlPP 160
Cdd:cd16146 79 D---ET--TLAEVFKDAGYRTGIFGKWHLGDNYPyrpqdrgfDEVlghggGGIGQYP----DYWGNDYFDDTYYHNG-KF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 161 VKAH----DIWrgklpgnrdghiiaarleqpeeatFERFIadrsiarlrQYAKEYKEtgKPFSLDVHFFGPHLPYFLPDE 236
Cdd:cd16146 149 VKTEgyctDVF------------------------FDEAI---------DFIEENKD--KPFFAYLATNAPHGPLQVPDK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 237 WFDLmdpkdvmlpksfgdtlvgkppvqqnyatywstssFDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAM 316
Cdd:cd16146 194 YLDP----------------------------------YKDMGLDDKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 317 FFCADHGEFTGSHRLNDKGpaM-------YDDIYRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGLD-PAQVE-D 386
Cdd:cd16146 240 IFMSDNGPAGGVPKRFNAG--MrgkkgsvYEGGHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKlPEGIKlD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 387 GRSVVDLARGVEVPDWRRNIVCEFHGLHFPIQQRM---LRTDDYKLVINHESLDELYDLRQDPSEINNVYAapAYDKVRR 463
Cdd:cd16146 318 GRSLLPLLKGESDPWPERTLFTHSGRWPPPPKKKRnaaVRTGRWRLVSPKGFQPELYDIENDPGEENDVAD--EHPEVVK 395
|
....*.
gi 585136219 464 EMAAEL 469
Cdd:cd16146 396 RLKAAY 401
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
17-452 |
4.75e-41 |
|
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: 151.95 E-value: 4.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFK---HQTLANPEWNiays 93
Cdd:cd16026 3 NIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRvglPGVVGPPGSK---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 94 TAIPETDWTYTQALRDAGYNVGMVGKYHCGTN---LPDKFGCddDTFWGAenPVANEEYVAWLKENDLPPVKAhdiwrgk 170
Cdd:cd16026 79 GGLPPDEITIAEVLKKAGYRTALVGKWHLGHQpefLPTRHGF--DEYFGI--PYSNDMWPFPLYRNDPPGPLP------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 171 lPGNRDGHIIAARLEQP-------EEATfeRFIadrsiarlrqyakeYKETGKPFSLDVHFFGPHLPYFLPDEWFDlmdp 243
Cdd:cd16026 148 -PLMENEEVIEQPADQSsltqrytDEAV--DFI--------------ERNKDQPFFLYLAHTMPHVPLFASEKFKG---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 244 kdvmlpKS----FGDTlvgkppvqqnyatywstssfdndqwrkliavywgyVAMIDFEIGRILDVARELGLMDDTAMFFC 319
Cdd:cd16026 207 ------RSgaglYGDV-----------------------------------VEELDWSVGRILDALKELGLEENTLVIFT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 320 ADHG---EFTGSHR----LNDKGPAMYDDIYRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGLD-PAQVE-DGRS 389
Cdd:cd16026 246 SDNGpwlEYGGHGGsagpLRGGKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPlPEDRViDGKD 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585136219 390 VVDLARGVEVPDwRRNIVCEFHG------------LHFPIQQRMLrTDDYKLVINHESLDELYDLRQDPSEINNV 452
Cdd:cd16026 326 ISPLLLGGSKSP-PHPFFYYYDGgdlqavrsgrwkLHLPTTYRTG-TDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
17-454 |
4.93e-40 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 149.24 E-value: 4.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDtlgcMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLAN-PEWNiAYSTA 95
Cdd:cd16147 3 NIVLILTDDQDVE----LGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNsPPGG-GYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 I---PETDW--TYtqaLRDAGYNVGMVGKYhcgtnLpdkfgcdddtfwgaenpvaNEeyvaWLKENDLPPVKAH-DIWRG 169
Cdd:cd16147 78 WqngLERSTlpVW---LQEAGYRTAYAGKY-----L-------------------NG----YGVPGGVSYVPPGwDEWDG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 170 KLPGNRDG------HIIAARLEQPEEATFERFIADRSIARLRQYAKEyketGKPFSLDVHFFGPHLPYFLPDEWFDLMDP 243
Cdd:cd16147 127 LVGNSTYYnytlsnGGNGKHGVSYPGDYLTDVIANKALDFLRRAAAD----DKPFFLVVAPPAPHGPFTPAPRYANLFPN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 244 KDVMLPKSFGDT--------LVGKPPVQQNYATYWstssfDN---DQWRKLIAVywgyvamiDFEIGRILDVARELGLMD 312
Cdd:cd16147 203 VTAPPRPPPNNPdvsdkphwLRRLPPLNPTQIAYI-----DElyrKRLRTLQSV--------DDLVERLVNTLEATGQLD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 313 DTAMFFCADHGEFTGSHRLN-DKGPAmYD-DIyRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSV 390
Cdd:cd16147 270 NTYIIYTSDNGYHLGQHRLPpGKRTP-YEeDI-RVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRSC 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585136219 391 VDLA----RGVEVPDWRRNIVCEFHGLHFpiqqrmlrtddyklvinheslDELYDLRQDPSEINNVYA 454
Cdd:cd16147 348 GDSNnntyKCVRTVDDTYNLLYFEWCTGF---------------------RELYDLTTDPYQLTNLAG 394
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
17-452 |
1.61e-39 |
|
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: 147.59 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDqhriDT----LGCMGNtHAQTPNIDSLAADGCLFTkAFTPSAICTPARSSMLTGQLPfkHQT-LANPEWNIA 91
Cdd:cd16025 4 NILLILAD----DLgfsdLGCFGG-EIPTPNLDALAAEGLRFT-NFHTTALCSPTRAALLTGRNH--HQVgMGTMAELAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 92 ----YSTAIPETDWTYTQALRDAGYNVGMVGKYHCGtnlPDKFGCDDDtfwgaenpvaneeyvawlkendlppvkahdiw 167
Cdd:cd16025 76 gkpgYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG---PDDYYSTDD-------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 168 rgklpgnrdghiiaarleqpeeatferfIADRSIarlrQYAKEYKETGKPFSLDVHFFGPHLPYFLPDEWFDLMDPK--- 244
Cdd:cd16025 121 ----------------------------LTDKAI----EYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKyda 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 245 --DVM-------------LPKsfgDTlvgKPPVQQNYATYWSTSSFDN-DQWRKLIAVYWGYVAMIDFEIGRILDVAREL 308
Cdd:cd16025 169 gwDALreerlerqkelglIPA---DT---KLTPRPPGVPAWDSLSPEEkKLEARRMEVYAAMVEHMDQQIGRLIDYLKEL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 309 GLMDDTAMFFCADHG---E------FTGSHRLNdKGPAMYDDIyRIPFIARIPG--LTHGTKCNDYVQLIDMTATFMEIA 377
Cdd:cd16025 243 GELDNTLIIFLSDNGasaEpgwanaSNTPFRLY-KQASHEGGI-RTPLIVSWPKgiKAKGGIRHQFAHVIDIAPTILELA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 378 GLD-PAQVE-------DGRSVVDLARGVEVPDWRRNIVCEFHGlhfpiqQRMLRTDDYKLVINHESLD-----ELYDLRQ 444
Cdd:cd16025 321 GVEyPKTVNgvpqlplDGVSLLPTLDGAAAPSRRRTQYFELFG------NRAIRKGGWKAVALHPPPGwgdqwELYDLAK 394
|
....*...
gi 585136219 445 DPSEINNV 452
Cdd:cd16025 395 DPSETHDL 402
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-451 |
2.18e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 144.28 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTpSAICTPARSSMLTGQLPFKHQTLANPEWNiaystai 96
Cdd:cd16151 2 NIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRNYVVFGYLDP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 peTDWTYTQALRDAGYNVGMVGKYHCGT-----NLPDKFGCDddtfwgaenpvaneEYVAW---LKENDLPPvkahdiWR 168
Cdd:cd16151 74 --KQKTFGHLLKDAGYATAIAGKWQLGGgrgdgDYPHEFGFD--------------EYCLWqltETGEKYSR------PA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 169 GKLPGNRDGHIIAARLEQPEEATFERFIADrsiarlrqYAKEYKEtgKPFSLD-----VHffGPHLPyfLPDEwfdlmDP 243
Cdd:cd16151 132 TPTFNIRNGKLLETTEGDYGPDLFADFLID--------FIERNKD--QPFFAYypmvlVH--DPFVP--TPDS-----PD 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 244 KDVMLPKSFGDtlvgkppvQQNYAtywstssfdndqwrkliavywGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHG 323
Cdd:cd16151 193 WDPDDKRKKDD--------PEYFP---------------------DMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 324 EFTGSHRLNDKGPA------MYDDIYRIPFIARIPGLT-HGTKCNDYVQLIDMTATFMEIAGLD-PAQVE-DGRSVVDLA 394
Cdd:cd16151 244 THRPITSRTNGREVrggkgkTTDAGTHVPLIVNWPGLIpAGGVSDDLVDFSDFLPTLAELAGAPlPEDYPlDGRSFAPQL 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 585136219 395 RGVEVPDWRRNIVCEFHGLHFPIQQRMLRTDDYKLvinhESLDELYDLRQDPSEINN 451
Cdd:cd16151 324 LGKTGSPRREWIYWYYRNPHKKFGSRFVRTKRYKL----YADGRFFDLREDPLEKNP 376
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-392 |
7.83e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 140.20 E-value: 7.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHA----------QTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANp 86
Cdd:cd16153 3 NILWIITDDQRVDSLSCYNNAHTgksesrlgyvESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 87 EWniaystAIPETDW---TYTQALRDAGYNVGMVGKYHCgtnlpdkfgcdddtfwgaenpvanEEYVAWLKeNDLPPVKA 163
Cdd:cd16153 82 EA------AHPALDHglpTFPEVLKKAGYQTASFGKSHL------------------------EAFQRYLK-NANQSYKS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 164 hdIWRGKLPGnrdghiiaarleqpeeatferfiADRSiarlrqyakeyketgKPFSLDVHFFGPHLPyflpdewfdlmdp 243
Cdd:cd16153 131 --FWGKIAKG-----------------------ADSD---------------KPFFVRLSFLQPHTP------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 244 kdVMLPKSFGDtlvgkppvqqnyatywstsSFDndqwrkliavYWGYVAMIDFEIGRILDVARELGL---MDDTAMFFCA 320
Cdd:cd16153 158 --VLPPKEFRD-------------------RFD----------YYAFCAYGDAQVGRAVEAFKAYSLkqdRDYTIVYVTG 206
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585136219 321 DHGEFTGSHRLNDK-GPAMYDdiYRIPFIARIPGLT---HGTKCNDYVQLIDMTATFMEIAGLDPAQVE--DGRSVVD 392
Cdd:cd16153 207 DHGWHLGEQGILAKfTFWPQS--HRVPLIVVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDylDGRDLFE 282
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
16-379 |
4.38e-35 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 132.93 E-value: 4.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 16 RNIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPEWNIAYSTA 95
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 -IPEtdwtytqALRDAGYNVGMVGKYHcgtnlpdkfgcdddTFWGAENPVANEEYVAWLkendlppvkAHDIWRGKLPGN 174
Cdd:pfam00884 81 sLPD-------LLKRAGYNTGAIGKWH--------------LGWYNNQSPCNLGFDKFF---------GRNTGSDLYADP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 175 RDGHIIAARLEQPEEATFERFIadrsiarlrqyaKEYKETGKPFSLDVHFFGPHLPYFLPDEWfdlmdpkdvmlPKSFGD 254
Cdd:pfam00884 131 PDVPYNCSGGGVSDEALLDEAL------------EFLDNNDKPFFLVLHTLGSHGPPYYPDRY-----------PEKYAT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 255 TLVGKPPVQQNYATYWSTssfdndqwrkliavywgyVAMIDFEIGRILDVARELGLMDDTAMFFCADHGE--FTGSHRLN 332
Cdd:pfam00884 188 FKPSSCSEEQLLNSYDNT------------------LLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGEslGEGGGYLH 249
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 585136219 333 D-KGPAMYDDIYRIPFIARIPGLTHGTKCND-YVQLIDMTATFMEIAGL 379
Cdd:pfam00884 250 GgKYDNAPEGGYRVPLLIWSPGGKAKGQKSEaLVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-407 |
5.72e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 127.71 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKH---QTLANPeWNIAYS 93
Cdd:cd16035 2 NILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTgvtDTLGSP-MQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 94 TAIPetdwTYTQALRDAGYNVGMVGKYHCGtnlpdkfgcddDTFWGAENpvaneeyvawlkendlppvkahdiwrgklpg 173
Cdd:cd16035 81 PDVP----TLGHMLRAAGYYTAYKGKWHLS-----------GAAGGGYK------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 174 nRDGhiiaarleqpeeatferFIADRSIARLRQYAKEyKETGKPFSLDVHFFGPHlpyflpdewfdlmdpkDVMLPksfg 253
Cdd:cd16035 115 -RDP-----------------GIAAQAVEWLRERGAK-NADGKPWFLVVSLVNPH----------------DIMFP---- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 254 dtlvgkPPvqqnyatywstssfDNDQWRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHRLND 333
Cdd:cd16035 156 ------PD--------------DEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRG 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 334 KGPAMYDDIYRIPFIARIPGL-THGTKCNDYVQLIDMTATFMEIAGLDPAQVED------GRSVVDLARGVEVPDWRRNI 406
Cdd:cd16035 216 KGFNAYEEALHVPLIISHPDLfGTGQTTDALTSHIDLLPTLLGLAGVDAEARATeapplpGRDLSPLLTDADADAVRDGI 295
|
.
gi 585136219 407 V 407
Cdd:cd16035 296 L 296
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-452 |
4.95e-29 |
|
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: 118.02 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDqhriDT----LGCMG---NTHAQTPNIDSLAADGCLFTKAFT-PSaiCTPARSSMLTGQLPFKHQTLANPew 88
Cdd:cd16142 2 NILVILGD----DIgwgdLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVePS--CTPGRAAFITGRHPIRTGLTTVG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 89 nIAYSTA-IPETDWTYTQALRDAGYNVGMVGKYHCGtnlpdkfgcdddtfwgaENPVAneeyvawlkendLPPVKAHDIW 167
Cdd:cd16142 74 -LPGSPGgLPPWEPTLAELLKDAGYATAQFGKWHLG-----------------DEDGR------------LPTDHGFDEF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 168 RGKLPgnrdghiiaarleqpeeATFERFIADRSIARLRQYAKeykeTGKPFSLDVHFFGPHLPYFLPDEWfdlmdpkdvm 247
Cdd:cd16142 124 YGNLY-----------------HTIDEEIVDKAIDFIKRNAK----ADKPFFLYVNFTKMHFPTLPSPEF---------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 248 lpksfgdtlVGKPPVQQNYAtywstssfDNdqwrkliavywgyVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTG 327
Cdd:cd16142 173 ---------EGKSSGKGKYA--------DS-------------MVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQD 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 328 SHRLNDKGP--AMYDDIY----RIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGL-DPAQVEDGRSV----VD--- 392
Cdd:cd16142 223 VWPDGGYTPfrGEKGTTWeggvRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGApDPKDKLLGKDRhidgVDqsp 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585136219 393 --LARGVEVPdwRRNIVceFHGLhfpIQQRMLRTDDYKLVINHESLDE--------------LYDLRQDPSEINNV 452
Cdd:cd16142 303 flLGKSEKSR--RSEFF--YFGE---GELGAVRWKNWKVHFKAQEDTGgptgepfyvltfplIFNLRRDPKERYDV 371
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
17-453 |
2.60e-28 |
|
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: 116.11 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTpSAICTPARSSMLTGQLPFK----HQTLANPEwniay 92
Cdd:cd16029 2 HIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHtgmqHGVILAGE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 93 STAIPETDWTYTQALRDAGYNVGMVGKYHCG----TNLP-----DKF-GcdddtFWGAEnpvanEEYVawlkendlppvk 162
Cdd:cd16029 76 PYGLPLNETLLPQYLKELGYATHLVGKWHLGfytwEYTPtnrgfDSFyG-----YYGGA-----EDYY------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 163 AHDIWRGKLPGNRDGHiiaaRLEQPEEATFERF----IADRSIARLRQYAKEyketgKPFSLDVHFFGPHLPYFLPDEWF 238
Cdd:cd16029 134 THTSGGANDYGNDDLR----DNEEPAWDYNGTYstdlFTDRAVDIIENHDPS-----KPLFLYLAFQAVHAPLQVPPEYA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 239 DLmdpkdvmlpksfgdtlvgkppvqqnyatYWSTSSFDNDQWRKliaVYWGYVAMIDFEIGRILDVARELGLMDDTAMFF 318
Cdd:cd16029 205 DP----------------------------YEDKFAHIKDEDRR---TYAAMVSALDESVGNVVDALKAKGMLDNTLIVF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 319 CADHGeftgshrlndkGPAMYDDI-----YR----------IpfiaRIPGLTH--------GTKCNDYVQLIDMTATFME 375
Cdd:cd16029 254 TSDNG-----------GPTGGGDGgsnypLRggkntlweggV----RVPAFVWspllppkrGTVSDGLMHVTDWLPTLLS 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 376 IAGLDPAQVE--DGRSVVD-LARGVEVPdwRRNIVcefHGLHFPIQQRM---LRTDDYKLVINheslDELYDLRQDPSEI 449
Cdd:cd16029 319 LAGGDPDDLPplDGVDQWDaLSGGAPSP--RTEIL---LNIDDITRTTGgaaIRVGDWKLIVG----KPLFNIENDPCER 389
|
....
gi 585136219 450 NNVY 453
Cdd:cd16029 390 NDLA 393
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
17-448 |
9.80e-28 |
|
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: 115.60 E-value: 9.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGN-THAQTPnIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPEWNIAYSTA 95
Cdd:cd16160 3 NIVLFFADDMGYGDLASYGHpTQERGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 -IPETDWTYTQALRDAGYNVGMVGKYHCGTN---------LPDKFGCDddtFWGAENPVANeeyvAWlkendlppvkAHD 165
Cdd:cd16160 82 gLPKTEVTMAEALKEAGYTTGMVGKWHLGINennhsdgahLPSHHGFD---FVGTNLPFTN----SW----------ACD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 166 IWRGKLPgnrDGHIIAARLEQPEEATFERFIADRSIARLRQYAKEYKETG--KPFSLDVHFFGPHLPYFLPDEwfdlmdp 243
Cdd:cd16160 145 DTGRHVD---FPDRSACFLYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNqeNPFFLYFSFPQTHTPLFASKR------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 244 kdvmlpksfgdtlvgkppvqqnyatywstssFDNDQWRkliAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHG 323
Cdd:cd16160 215 -------------------------------FKGKSKR---GRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 324 ---EFT---GSHRLNDKGPA-MYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAG--LDPAQVEDGRSVVDLA 394
Cdd:cd16160 261 phvEYClegGSTGGLKGGKGnSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGgtLPTDRIYDGLSITDLL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 395 RGvEVPDWRRNIV--CE--------------FHGLHFPIQ--------------QRMLRTDDYKLVINHESLDELYDLRQ 444
Cdd:cd16160 341 LG-EADSPHDDILyyCCsrlmavrygsykihFKTQPLPSQesldpncdgggplsDYIVCYDCEDECVTKHNPPLIFDVEK 419
|
....
gi 585136219 445 DPSE 448
Cdd:cd16160 420 DPGE 423
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
17-483 |
3.75e-24 |
|
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: 105.45 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFK------HQTLANPewNI 90
Cdd:cd16159 3 NIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRsgmassHGMRVIL--FT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 91 AYSTAIPETDWTYTQALRDAGYNVGMVGKYHCG--------------------------TNLPDkfgCDDDT---FWGAe 141
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGlhcesrndfchhplnhgfdyfyglplTNLKD---CGDGSngeYDLS- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 142 NPVANEEYVAWL-----------KENDLP----------PVKAHDIWRGKLPGNRDGHIIAAR----LEQPeeATFERFi 196
Cdd:cd16159 157 FDPLFPLLTAFVlitaltiflllYLGAVSkrffvfllilSLLFISLFFLLLITNRYFNCILMRnhevVEQP--MSLENL- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 197 adrsIARLRQYAKEYKETGK--PFSLDVHFFGPHLPYFLPDEWFDlmdpkdvmlpksfgdtlvgkppvqqnyatywstss 274
Cdd:cd16159 234 ----TQRLTKEAISFLERNKerPFLLVMSFLHVHTALFTSKKFKG----------------------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 275 fdndqwRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHG---EFTGSHRLND-------KGPAM--YDDI 342
Cdd:cd16159 275 ------RSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGghlEEISVGGEYGggnggiyGGKKMggWEGG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 343 YRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGLD-PA-QVEDGRSVVDLARG-VEVPD----------------W 402
Cdd:cd16159 349 IRVPTIVRWPGvIPPGSVIDEPTSLMDIFPTVAALAGAPlPSdRIIDGRDLMPLLTGqEKRSPheflfhycgaelhavrY 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 403 RRNIVCEFHGLHFPIQQRMLRTD----------DYKLVINHESlDELYDLRQDPSEINNVYAA-PAYDKVRREM--AAEL 469
Cdd:cd16159 429 RPRDGGAVWKAHYFTPNFYPGTEgccgtllcrcFGDSVTHHDP-PLLFDLSADPSESNPLDPTdEPYQEIIKKIleAVAE 507
|
570
....*....|....
gi 585136219 470 YRQLVERGDSSFAK 483
Cdd:cd16159 508 HQSSIEPVESQLSF 521
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
17-381 |
1.76e-23 |
|
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: 102.93 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLA-NPEWNIAYS-- 93
Cdd:cd16157 3 NIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTtNAHARNAYTpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 94 ---TAIPETDWTYTQALRDAGYNVGMVGKYHCGTN---LPDKFGCDddtFW-GAENPvaneeYVAWLKENDLPpvkahdi 166
Cdd:cd16157 83 nivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRpqyHPLKHGFD---EWfGAPNC-----HFGPYDNKAYP------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 167 wrgKLPGNRDGHIIAarleqpeeATFERFIADRSIAR------LRQYAKEYKE----TGKPFSLdvhffgphlpYFLPDe 236
Cdd:cd16157 148 ---NIPVYRDWEMIG--------RYYEEFKIDKKTGEsnltqiYLQEALEFIEkqhdAQKPFFL----------YWAPD- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 237 wfdlmdpkdvmlpksfgdtlvgkppvqQNYATYWSTSSFDNDQWRKLiavYWGYVAMIDFEIGRILDVARELGLMDDTAM 316
Cdd:cd16157 206 ---------------------------ATHAPVYASKPFLGTSQRGL---YGDAVMELDSSVGKILESLKSLGIENNTFV 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585136219 317 FFCADHG-------EFTGSHrlndkGPAM------YDDIYRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAGLDP 381
Cdd:cd16157 256 FFSSDNGaalisapEQGGSN-----GPFLcgkqttFEGGMREPAIAWWPGhIKPGQVSHQLGSLMDLFTTSLALAGLPI 329
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
17-447 |
1.91e-23 |
|
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: 101.85 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQlpFKHQTlanPEWNiaYSTAI 96
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGL--FTHLT---ESWN--NYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 97 PETDWTYTQALRDAGYNVGMVGK--YHCGTNlpdkfgcdddtfwGAENPVAneeyvAWLKenDLPPVKAHDiwrGK---- 170
Cdd:cd16171 75 DPNYPTWMDRLEKHGYHTQKYGKldYTSGHH-------------SVSNRVE-----AWTR--DVPFLLRQE---GRptvn 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 171 LPGNRDGHIIAARLEQpeeatferfIADRSIARLRQYAKEYKetgKPFSLdvhFFGPHLPYFLPDEWfdlmdpkdvmLPK 250
Cdd:cd16171 132 LVGDRSTVRVMLKDWQ---------NTDKAVHWIRKEAPNLT---QPFAL---YLGLNLPHPYPSPS----------MGE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 251 SFGDTlvgkppvqqnyatywstssfdndqwRKLIAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHR 330
Cdd:cd16171 187 NFGSI-------------------------RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHR 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 331 LNDKgPAMYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEV---------PD 401
Cdd:cd16171 242 QFYK-MSMYEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSESSIkespsrvphPD 320
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 585136219 402 WrrnIVCEFHGLHFPIQQRMLRTDDYKLVINHESLD---ELYDLRQDPS 447
Cdd:cd16171 321 W---VLSEFHGCNVNASTYMLRTNSWKYIAYADGNSvppQLFDLSKDPD 366
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-448 |
3.90e-23 |
|
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: 100.89 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLG--CMGNTHAQTPNIDSLAADGCLFTKAF-TPSaiCTPARSSMLTGQLPFKHQTLANPEWNIAYS 93
Cdd:cd16154 2 NILLIIADDQGLDSSAqySLSSDLPVTPTLDSLANSGIVFDNLWaTPA--CSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 94 TAIPETdwtYTQALRDAGYNVGMVGKYHCGTNL--PDKFGCDDDtFWGAeNPVANEEYVAWLKENDlppvkahdiwrgkl 171
Cdd:cd16154 80 ETLLQL---LIKDATTAGYSSAVIGKWHLGGNDnsPNNPGGIPY-YAGI-LGGGVQDYYNWNLTNN-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 172 pgnrdghiiAARLEQPEEATFErfIADRSIARLRQYAKeyketgkPFSLDVHFFGPHLPYFLPDEwfDLMDPkdvmlpks 251
Cdd:cd16154 141 ---------GQTTNSTEYATTK--LTNLAIDWIDQQTK-------PWFLWLAYNAPHTPFHLPPA--ELHSR-------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 252 fgDTLVGKPPVQQNYATYwstssfdndqwrkliavywgYVAMI---DFEIGRILDVARElGLMDDTAMFFCADHG----- 323
Cdd:cd16154 193 --SLLGDSADIEANPRPY--------------------YLAAIeamDTEIGRLLASIDE-EERENTIIIFIGDNGtpgqv 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 324 ---EFTGSHRlndKGpAMYDDIYRIPFIARIPGLTH-GTKCNDYVQLIDMTATFMEIAGLDPAQVEDGRSVVDLARGVEV 399
Cdd:cd16154 250 vdlPYTRNHA---KG-SLYEGGINVPLIVSGAGVERaNERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNA 325
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 585136219 400 PDWRRNIVCEFHGlhfPIQQRMLRTDDYKLVINHESLDELYDLRQDPSE 448
Cdd:cd16154 326 STRQYNYTEYESP---TTTGWATRNQYYKLIESENGQEELYDLINDPSE 371
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
17-483 |
3.02e-18 |
|
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: 87.12 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFK---HQTLANPewniAYS 93
Cdd:cd16158 3 NIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRsgvYPGVFYP----GSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 94 TAIPETDWTYTQALRDAGYNVGMVGKYHCGTNLPDKFgcdddtfwgaenpvaneeyvawlkendLPPvkahdiwrgklpg 173
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTY---------------------------LPT------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 174 nRDGhiiaarleqpeeatFERFIadrsiarlrqyakeyketGKPFSldvHFFGP--HLPYFLPD-EWFDLMDPKDVMLPK 250
Cdd:cd16158 119 -HQG--------------FDHYL------------------GIPYS---HDQGPcqNLTCFPPNiPCFGGCDQGEVPCPL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 251 SFGDTLVGKPP----VQQNYATYWSTSSFDNDQWRKLIAVYWGY-------------------------VAMIDFEIGRI 301
Cdd:cd16158 163 FYNESIVQQPVdlltLEERYAKFAKDFIADNAKEGKPFFLYYAShhthypqfagqkfagrssrgpfgdaLAELDGSVGEL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 302 LDVARELGLMDDTAMFFCADHGEFT------GSHRLNDKGPA-MYDDIYRIPFIARIPGLTHGTKCNDYVQLIDMTATFM 374
Cdd:cd16158 243 LQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKCGKGtTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPTIA 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 375 EIAG------------LDPAQVEDGRSV----------VDLARGVEVPDWRRnivcefHGLHFPIQQRMLR--TDD---- 426
Cdd:cd16158 323 KLAGaplpnvtldgvdMSPILFEQGKSPrqtffyyptsPDPDKGVFAVRWGK------YKAHFYTQGAAHSgtTPDkdch 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 427 -YKLVINHESlDELYDLRQDPSEINNVYAAPAYDKVRREMAA--ELYRQLVERGDSSFAK 483
Cdd:cd16158 397 pSAELTSHDP-PLLFDLSQDPSENYNLLGLPEYNQVLKQIQQvkERFEASMKFGESEINK 455
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
387-478 |
2.18e-15 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 71.90 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 387 GRSVVDLARGVEVPDWRRNIVCEFH---GLHFPIQQRMLRTDDYKLVINHESLD--ELYDLRQDPSEINNVYAAPAYDKV 461
Cdd:pfam16347 7 GKSFLPLLKGKKPKNWRDALYYHYYeypAEHAVKRHYGVRTERYKLIHFYNDIDewELYDLQKDPKEMNNVYGDPEYAEV 86
|
90
....*....|....*..
gi 585136219 462 RREMAAELYRQLVERGD 478
Cdd:pfam16347 87 QAELKEELEELRKQYKD 103
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
17-390 |
1.56e-14 |
|
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: 75.20 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 17 NIITFMTDQHRIDTLGCMGN-THAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPewNIAYSTA 95
Cdd:cd16161 3 NFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNF--LPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 96 IPETDWTYTQALRDAGYNVGMVGKYHCGTnlpdkfgcdddtfwgaenpvaNEEYvawlkendLPPVKAHDIWRGkLPGNR 175
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQ---------------------REAY--------LPNSRGFDYYFG-IPFSH 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 176 DGHiiaarleqpeeatferfIADRSIARLRQYAKEYKETGKPFSLDVHFFGPHLPyflpdewfdlmdpkdvmlpksfgdt 255
Cdd:cd16161 131 DSS-----------------LADRYAQFATDFIQRASAKDRPFFLYAALAHVHVP------------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 256 lvgkppvQQNYATYWSTSSFDndqwrkliAVYWGYVAMIDFEIGRILDVARELGLMDDTAMFFCADHG-----------E 324
Cdd:cd16161 169 -------LANLPRFQSPTSGR--------GPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelavgP 233
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136219 325 FTGSHR----LNDKGPAMYDDIYRIPFIARIPG-LTHGTKCNDYVQLIDMTATFMEIAG--LDPAQVEDGRSV 390
Cdd:cd16161 234 GTGDWQgnlgGSVAKASTWEGGHREPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGasLPPGRIYDGKDL 306
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
29-441 |
4.36e-09 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 58.90 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 29 DTLGCMGNTHAQTPNIDSLAADGCLFTKAFTPSAICTPARSSMLTGQLPFKHQTLANPEWNIAYSTaIPEtdwtytqALR 108
Cdd:COG1368 248 FFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGSPYKRPGQNNFPS-LPS-------ILK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 109 DAGYNVGMvgkYHCGTNlpdkfgcdddTFWGAENPVANEEYVAWLKENDLPPVKAHdIWrgklpgnrdghiiaarleqpe 188
Cdd:COG1368 320 KQGYETSF---FHGGDG----------SFWNRDSFYKNLGFDEFYDREDFDDPFDG-GW--------------------- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 189 eatferFIADRSIarLRQYAKEYKETGKPFsldVHFF---GPHLPYFLPDEwfdlmdpkdvmlPKSFGDTlvGKPPVQQN 265
Cdd:COG1368 365 ------GVSDEDL--FDKALEELEKLKKPF---FAFLitlSNHGPYTLPEE------------DKKIPDY--GKTTLNNY 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 266 YATYWstssfdndqwrkliavywgYVamiDFEIGRILDVARELGLMDDTAMFFCADHGeftgsHRLNDKGPA-MYDDIYR 344
Cdd:COG1368 420 LNAVR-------------------YA---DQALGEFIEKLKKSGWYDNTIFVIYGDHG-----PRSPGKTDYeNPLERYR 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 345 IPFIARIPGLTHGTKCNDYVQLIDMTATFMEIAGLD-PAQVEDGRSVVDLARGvevpdwrrnivcefhglHFPIQQRMLR 423
Cdd:COG1368 473 VPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDyPSYYAFGRDLLSPDTD-----------------PFAFRNGGFI 535
|
410
....*....|....*...
gi 585136219 424 TDDYKLVINHESLDELYD 441
Cdd:COG1368 536 TDDYVYVLKTGELTEEDK 553
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
41-378 |
4.66e-09 |
|
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: 57.31 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 41 TPNIDSLAADGCLFTKAFTPSAICTPARS--SMLTGQLPfkhqtlaNPEWNIAYSTAIPETDWTYTQALRDAGYNVGMvg 118
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPP-------LPLGSGSYTLYKLNPLPSLPSILKEQGYETIF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 119 kYHCGtnlpdkfgcdDDTFWGaenpvaneeyvawlkendlppvkahdiWRGKLPGNRDGHIIAAR-LEQPEEATFERFIA 197
Cdd:cd16015 97 -IHGG----------DASFYN---------------------------RDSVYPNLGFDEFYDLEdFPDDEKETNGWGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 198 DRSIarLRQYAKEYKET-GKPFSLdvHFF--GPHLPYFLPDEWFDLMDPKDvmlpksfgdtlvGKPPVQQNYATYwstss 274
Cdd:cd16015 139 DESL--FDQALEELEELkKKPFFI--FLVtmSNHGPYDLPEEKKDEPLKVE------------EDKTELENYLNA----- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 275 fdndqwrkliavywgyVAMIDFEIGRILDVARELGLMDDTAMFFCADHGEFTGSHrlNDKGPAMYDDIYRIPFIARIPGL 354
Cdd:cd16015 198 ----------------IHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD--YDETDEDPLDLYRTPLLIYSPGL 259
|
330 340
....*....|....*....|....
gi 585136219 355 THGTKCNDYVQLIDMTATFMEIAG 378
Cdd:cd16015 260 KKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
291-372 |
5.93e-08 |
|
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: 53.58 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 291 VAMIDFEIGRILDVARELGLMDDTAMFFCADHGeftgsHRLNDKGPAMYDDIY--------RIPFIARIPGLTHGTKCND 362
Cdd:cd00016 148 VEEIDERIGKVLDALKKAGDADDTVIIVTADHG-----GIDKGHGGDPKADGKadkshtgmRVPFIAYGPGVKKGGVKHE 222
|
90
....*....|
gi 585136219 363 YVQLIDMTAT 372
Cdd:cd00016 223 LISQYDIAPT 232
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
37-323 |
1.46e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 43.97 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 37 THAQTPNIDSLAADGCLFTK------AFTPSAIctparSSMLTGQLPFKHQtlanpewNIAYSTAIPETDwtytqalrda 110
Cdd:COG1524 40 ERAHAPNLAALAARGVYARPltsvfpSTTAPAH-----TTLLTGLYPGEHG-------IVGNGWYDPELG---------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 111 gynvgmvGKYHCGTNLPDKFGCDDD----TFW----GAENPVANeeyVAWLKENDLPPVKAHdiwrgkLPGNRDGHIIaa 182
Cdd:COG1524 98 -------RVVNSLSWVEDGFGSNSLlpvpTIFerarAAGLTTAA---VFWPSFEGSGLIDAA------RPYPYDGRKP-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 183 RLEQPEEatfERFIADRSIARLRQYakeyketgKP-FSLdVHFfgPHLpyflpdewfdlmdpkdvmlpksfgDTlvgkpp 261
Cdd:COG1524 160 LLGNPAA---DRWIAAAALELLREG--------RPdLLL-VYL--PDL------------------------DY------ 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585136219 262 VQQNYATywstssfDNDQWRKLIAvywgyvaMIDFEIGRILDVARELGLMDDTAMFFCADHG 323
Cdd:COG1524 196 AGHRYGP-------DSPEYRAALR-------EVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
291-378 |
1.33e-03 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 40.65 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 291 VAMIDFEIGRILDVARELGLMDDTAMFFCADHGeFT--GSHrlndkGpamYD---DIYRIPFIARIPGLTHGTKCnDYVQ 365
Cdd:cd16018 185 LKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG-MTdvGTH-----G---YDnelPDMRAIFIARGPAFKKGKKL-GPFR 254
|
90
....*....|...
gi 585136219 366 LIDMTATFMEIAG 378
Cdd:cd16018 255 NVDIYPLMCNLLG 267
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
222-348 |
5.05e-03 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 38.76 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136219 222 VHFFGPHLPYF--LPDEWFDLMDPKDVMLPKSFGDTLVgkppvqqnyATYwstssfDNdqwrkliAVYwgYVamiDFEIG 299
Cdd:cd16017 148 LHLMGSHGPYYdrYPEEFAKFTPDCDNELQSCSKEELI---------NAY------DN-------SIL--YT---DYVLS 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 585136219 300 RILDVARELGlmDDTAMFFCADHGEFTGSHRLNDKG-PAMYDDIYRIPFI 348
Cdd:cd16017 201 QIIERLKKKD--KDAALIYFSDHGESLGENGLYLHGaPYAPKEQYHVPFI 248
|
|
| |
