|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
43-385 |
0e+00 |
|
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: 545.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNE--NCSSPSWQA 120
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 121 QHESRTFAVYLNSTGYRTAFFGKYLNEY----NGSYVPPGWKEWVGLLKNSRFYNYTLCrNGVKEKHGSDYSKDYLTDLI 196
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 197 TNDSVSFFRTSKKMypHRPVLMVISHAAPHGPEDSAPQYSRLFPNAS-QHITPSYNYAPNPDKHWIMRYTGPMkPIHMEF 275
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLN-PTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 276 TNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGCL 355
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 29789100 356 NPHIVLNIDLAPTILDIAGLDIPADMDGKS 385
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
43-415 |
3.72e-89 |
|
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: 289.43 E-value: 3.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQ--DVeLGSMQ-VMNKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcSSP 116
Cdd:cd16031 2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 117 SWQaqhesRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGvkekhGSDYSKDYLTDLI 196
Cdd:cd16031 79 ASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENG-----KRVGQKGYVTDII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 197 TNDSVSFFRTSKKmypHRPVLMVISHAAPHGPEDSAPQYSRLFPNAsqHITP-----SYNYAPNPD--KHWIMRYTGPMK 269
Cdd:cd16031 149 TDKALDFLKERDK---DKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEpetfdDDDYAGRPEwaREQRNRIRGVLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 270 -PIHMEFT---NMlqRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYV 345
Cdd:cd16031 224 gRFDTPEKyqrYM--KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLII 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789100 346 RGP-NVEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVnrfhlkkkmrVWRDSFLVE 415
Cdd:cd16031 301 RDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKPV----------DWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
43-428 |
1.24e-69 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 235.93 E-value: 1.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQDV-ELGSM-QVMNKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPs 117
Cdd:COG3119 23 RPNILFILADDLGYgDLGCYgNPLIKTpniDRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 wqAQHESRTFAVYLNSTGYRTAFFGKYLNeyngsyvppgwkewvgllknsrfynytlcrngvkekhgsdyskdYLTDLIT 197
Cdd:COG3119 101 --LPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLLT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 198 NDSVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPNasQHITPSYNYAPNPDKHWIMRYtgpmkpihmeftn 277
Cdd:COG3119 135 DKAIDFLERQAD--KDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 278 mLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPN-VEAGCLN 356
Cdd:COG3119 198 -ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVS 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789100 357 PHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNR------FHLKKKMRVWRDsflvERGKLLHKRDNDKV 428
Cdd:COG3119 277 DALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKAEWRdylyweYPRGGGNRAIRT----GRWKLIRYYDDDGP 350
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
529-664 |
1.74e-63 |
|
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.
Pssm-ID: 463628 Cd Length: 142 Bit Score: 209.89 E-value: 1.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 529 ASYVRSRSIRSVAIEVDGRVYHVGLGDAAQP---RNLTKRHwpgAPEDQDDKDGG-DFSGTGGLPD----YSAANPIKVT 600
Cdd:pfam12548 2 PRFVRTRQKRSLSVEFEGEVYDIDLEEEYQPlepRNLLKRH---ARDDGEEGEEGeESSGTGSKRDssnsVGPPASVKVT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789100 601 HRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHK 664
Cdd:pfam12548 79 HRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-395 |
7.00e-50 |
|
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: 181.23 E-value: 7.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDD---QDveLGSMQVMN-KT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencss 115
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTpnlDRLAKEG-VVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 116 pSWQAQHESRTFAVYLNSTGYRTAFFGK--------YLNEYNGSYVPP----GWKEWVGLLKNSRFYNYTLCRNGVKEKH 183
Cdd:cd16034 72 -DVPLPPDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 184 GSDYSKDYLTDLItndsVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQ-YSRLFPNASQHitpsynYAPNPDKhwim 262
Cdd:cd16034 151 IKGYSPDAETDLA----IEYLENQAD--KDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLL------LRPNVPE---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 263 rytgpmkpihmeftNMLQRKRLQTLM--------SVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVkGKSMP 334
Cdd:cd16034 215 --------------DKKEEAGLREDLrgyyamitALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVP 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789100 335 YEFDIRVPFYVRGPNV-EAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERP 395
Cdd:cd16034 280 YEESIRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKD 341
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
44-385 |
8.50e-47 |
|
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: 167.23 E-value: 8.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQ---DVE-LGSMQVmnKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcssP 116
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 117 SWQAQHEsRTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHgsdyskdyltdli 196
Cdd:cd16022 75 GGLPPDE-PTLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 197 tNDSVSFFRTSKKmypHRPVLMVISHAAPHGPedsapqysrlfpnasqhitpsYNYApnpdkhwimrytgpmkpiHMeft 276
Cdd:cd16022 103 -DEAIDFIERRDK---DKPFFLYVSFNAPHPP---------------------FAYY------------------AM--- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 277 nmlqrkrlqtLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNV-EAGCL 355
Cdd:cd16022 137 ----------VSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKiPAGQV 206
|
330 340 350
....*....|....*....|....*....|
gi 29789100 356 NPHIVLNIDLAPTILDIAGLDIPADMDGKS 385
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-390 |
1.49e-45 |
|
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: 169.26 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDqdveLGSMQV---MNK---TRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKY--------VHNHNTY 107
Cdd:cd16144 1 PNIVLILVDD----LGWADLgcyGSKfyeTPNIdrLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 108 TNNENCSSPSWQAQH---ESRTFAVYLNSTGYRTAFFGKY-LNEYNGSYvpP---GWKEWVGLLKNSRFYNYTLCRNGVK 180
Cdd:cd16144 77 PPDNTKLIPPPSTTRlplEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 181 EKHGSDYSKDYLTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSRLFPNAsqhitpsynYAPNPDKHW 260
Cdd:cd16144 155 PDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKYEKK---------KKGLRKGQK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 261 IMRYTGpmkpihmeftnMLQrkrlqtlmSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLV-------KGKSM 333
Cdd:cd16144 222 NPVYAA-----------MIE--------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGGKGS 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 334 PYEFDIRVPFYVRGPNV-EAGCLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLL 390
Cdd:cd16144 283 LYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLL 342
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
44-398 |
4.44e-45 |
|
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: 166.53 E-value: 4.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQDVELGSmqVMN---KTRRIME--QGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencSSPSW 118
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGL----RSRGF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 119 QAQHESRTFAVYLNSTGYRTAFFGKYlnEYNGSYVPPGWKEWVGllknsrfynytlcrngvkEKHGSDYSKDYLtdlitn 198
Cdd:cd16027 75 PLPDGVKTLPELLREAGYYTGLIGKT--HYNPDAVFPFDDEMRG------------------PDDGGRNAWDYA------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 199 DSVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASqhITPSYNYAPNPdkhwIMRYtgpmkpihmEFTNM 278
Cdd:cd16027 129 SNAADFLNRAK--KGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEK--VKVPPYLPDTP----EVRE---------DLADY 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 279 LQrkrlqTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYhigqfGLVKGKSMPYEFDIRVPFYVRGPN-VEAGCLNP 357
Cdd:cd16027 192 YD-----EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKPGSVSD 261
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 29789100 358 HIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNR 398
Cdd:cd16027 262 ALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-390 |
6.82e-42 |
|
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: 158.53 E-value: 6.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQDV-ELGSM-QVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKyvHNHNTY--TNNENCSSPS 117
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTGHTRvrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 WQAqhESRTFAVYLNSTGYRTAFFGKY-LNEYNGSYVPP--GWKEWVGLLKNSR---FYNYTLCRNGVKEK--------- 182
Cdd:cd16145 79 LPP--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGYLDQVHahnYYPEYLWRNGEKVPlpnnvippl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 183 ----HGSDYSKDYLTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPedsapqysrlfpnasqHITPSYNYAPNPDK 258
Cdd:cd16145 157 degnNAGGGGGTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAP----------------LQVPDDGPYKYKPK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 259 HWIMRYTGPMKPIHMEFTNMLQRkrlqtlmsVDDSMETIYNMLVETGELDNTYIVYTADHGYHI-------GQF-----G 326
Cdd:cd16145 217 DPGIYAYLPWPQPEKAYAAMVTR--------LDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngP 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789100 327 LVKGK-SMpYEFDIRVPFYVRGPN-VEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLL 390
Cdd:cd16145 289 LRGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-395 |
2.48e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 150.07 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQ--DVeLGSM-QVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNenCSSPS 117
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 wqaqhESRTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHGSDYSKDYLTDLit 197
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 198 ndSVSFFRTSKKmypHRPVLMVISHAAPH---------GPEDSAPQYS--------RLFP-NASQHItpsynyapnPDkh 259
Cdd:cd16152 113 --AIDYLDNRQK---DKPFFLFLSYLEPHhqndrdryvAPEGSAERFAnfwvppdlAALPgDWAEEL---------PD-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 260 wimrYTGpmkpihmeftnMLQRkrlqtlmsVDDSMETIYNMLVETGELDNTYIVYTADHGYHigqFGLVKG--KSMPYEF 337
Cdd:cd16152 177 ----YLG-----------CCER--------LDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789100 338 DIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERP 395
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVE 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
44-375 |
4.65e-39 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 4.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQ---DVELGSMqVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNEncsspsW 118
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLYGY-PRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 119 QAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGLLKNSRFYNYTlCRNGVKEKHGSDYSKDYLTDLI 196
Cdd:pfam00884 74 GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADP-PDVPYNCSGGGVSDEALLDEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 197 TNDSVsffrtskkmyPHRPVLMVISHAAPHGPedsaPQYSRLFPNASQHITPSYNYAPNPDkhwimrytgpmkpihmeft 276
Cdd:pfam00884 153 EFLDN----------NDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 277 nmlqRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFG--LVKGKSM-PYEFDIRVPFYVRGPNVEA- 352
Cdd:pfam00884 200 ----NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAk 275
|
330 340
....*....|....*....|...
gi 29789100 353 GCLNPHIVLNIDLAPTILDIAGL 375
Cdd:pfam00884 276 GQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-420 |
1.96e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 141.55 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQDVE----LGSMQVmnKTRRI--MEQGGAHFINAFVTTPM----CCPSRSSILTGKYVHNhntYTNNEN 112
Cdd:cd16155 2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 113 CSSPSwqaqhESRTFAVYLNSTGYRTAFFGKYLNEYngsyvppgwkewvgllknsrfynytlcrngvkekhgsdyskdyl 192
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 193 tdliTNDSVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPnaSQHITPSYNYAP-NPdkhwimrytgpmkpi 271
Cdd:cd16155 108 ----ADAAIEFLEEYKD--GDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLPqHP--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 272 hmeFTNMLQRKRLQTL-------------------MS--VDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVkG 330
Cdd:cd16155 165 ---FDNGEGTVRDEQLapfprtpeavrqhlaeyyaMIthLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-G 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 331 KSMPYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNRFHLKKKMRVWRD 410
Cdd:cd16155 241 KQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDTLYGAYRDGQR 320
|
410
....*....|
gi 29789100 411 SFLVERGKLL 420
Cdd:cd16155 321 AIRDDRWKLI 330
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-415 |
5.04e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 141.20 E-value: 5.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQ--DVELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQ 119
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 120 AQHESRTFAVYLNSTGYRTAFFGKY--LNEYN-GSYvppGWKEWVGllknsrfynytlcrngvKEKHGsDYskdYLTDLi 196
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWhvGPEETpLDY---GFDEYLP-----------------VETTI-EY---FLADR- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 197 tndSVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYN--YAPNPDKHWIMRytgpMKPIHME 274
Cdd:cd16033 136 ---AIEMLEELAA--DDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFAddFEDKPYIYRRER----KRWGVDT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 275 FTNMLQRKRLQ------TLMsvDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLV-KGKSMpYEFDIRVPFYVRG 347
Cdd:cd16033 207 EDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKW 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789100 348 PNV-EAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNrfhlkkkmrvWRDSFLVE 415
Cdd:cd16033 284 PGViAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
44-390 |
4.36e-35 |
|
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: 138.45 E-value: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQ---DVELGSMQVMnKT---RRIMEQGgAHFINaFVTTPMCCPSRSSILTGKYVHN---HNTYTNNENCS 114
Cdd:cd16146 1 PNVILILTDDQgygDLGFHGNPIL-KTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHTILGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 115 SpswqaqhESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGL----------LKNSRFYNYTLCRNGVKEK 182
Cdd:cd16146 78 L-------DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdYWGNDYFDDTYYHNGKFVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 183 HgsdysKDYLTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYApnpdkhwim 262
Cdd:cd16146 151 T-----EGYCTDVFFDEAIDFIEENKD----KPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG--------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 263 rytgpmkpihmeftnMLQRkrlqtlmsVDDSMETIYNMLVETGELDNTYIVYTADHGYHIG-----QFGLVKGKSMPYEF 337
Cdd:cd16146 213 ---------------MIEN--------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEG 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 29789100 338 DIRVPFYVRGPNV-EAGCLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLL 390
Cdd:cd16146 270 GHRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPEgiKLDGRSLLPLL 325
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-390 |
9.08e-33 |
|
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: 131.53 E-value: 9.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQ---DVE-LGSMQVmnKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTNNE 111
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGSPLI--KTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 112 NCSSPSwqaqheSRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGLL------------KNSRFYNYTLCRN 177
Cdd:cd16026 79 GGLPPD------EITIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIPysndmwpfplyrNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 178 GVKEKHGSDYSkdYLTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPedsapqysrLFPNasqhitpsynyapnpd 257
Cdd:cd16026 153 EEVIEQPADQS--SLTQRYTDEAVDFIERNKD----QPFFLYLAHTMPHVP---------LFAS---------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 258 khwimrytgpmkpihMEFTNMLQRKRL-QTLMSVDDSMETIYNMLVETGELDNTYIVYTADHG--YHIGQFG-----LVK 329
Cdd:cd16026 202 ---------------EKFKGRSGAGLYgDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRG 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789100 330 GKSMPYEFDIRVPFYVRGPN-VEAGCLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 390
Cdd:cd16026 267 GKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLL 330
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
69-399 |
3.34e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 121.88 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 69 RIMEQGGAhFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpswqaqhESRTFAVYLNSTGYRTAFFGK--YLN 146
Cdd:cd16037 31 RLAARGTR-FENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 147 EyngsyvppgwkewvgllknsrfynytlcrngvKEKHGSDYSKDyltdlITNDSVSFFRTSKkmyPH-RPVLMVISHAAP 225
Cdd:cd16037 103 E--------------------------------DQRHGFRYDRD-----VTEAAVDWLREEA---ADdKPWFLFVGFVAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 226 HgpedsapqysrlFPnasqhitpsynyapnpdkhwimrYTGPMkpihmEFTNMLQRKRLQT---LMS-VDDSMETIYNML 301
Cdd:cd16037 143 H------------FP-----------------------LIAPQ-----EFYDLYVRRARAAyygLVEfLDENIGRVLDAL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 302 VETGELDNTYIVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPADM 381
Cdd:cd16037 183 EELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL 261
|
330
....*....|....*...
gi 29789100 382 DGKSILKLLDTERPVNRF 399
Cdd:cd16037 262 DGRSLLPLAEGPDDPDRV 279
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-379 |
1.47e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 120.00 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQ----DVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnENCSSPS-W 118
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 119 QAQHESRTFAVYLNSTGYRTAFFGKY-LNEYNGSYvppgwkewvgllknsrfynytlcrngvkekhgsdYSKDyltDLIT 197
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 198 NDSVSFFRTSKKMYPHR-PVLMVISHAAPH----GPEDsAPQYsRLFPNAsqhitpsynYApnpdkhwimrytgpmkpih 272
Cdd:cd16035 121 AQAVEWLRERGAKNADGkPWFLVVSLVNPHdimfPPDD-EERW-RRFRNF---------YY------------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 273 meftNMLQRkrlqtlmsVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEA 352
Cdd:cd16035 171 ----NLIRD--------VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFG 238
|
330 340 350
....*....|....*....|....*....|..
gi 29789100 353 G-----CLNPHivlnIDLAPTILDIAGLDIPA 379
Cdd:cd16035 239 TgqttdALTSH----IDLLPTLLGLAGVDAEA 266
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
75-395 |
2.40e-29 |
|
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: 122.37 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 75 GAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencSSPswQAQHEsRTFAVYLNSTGYRTAFFGK----------- 143
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARH-LTLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 144 YLNEYNGSY--VPPGWkEWVGLLknsrfynytlcrNGVKEKHgSDYSkdYLTDlitnDSVSFFRTskkmYPHRPVLMVIS 221
Cdd:cd16028 109 PLDPRLLSYelAMPGF-DPVDRL------------DEYPAED-SDTA--FLTD----RAIEYLDE----RQDEPWFLHLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 222 HAAPHGP-EDSAPqYSRLFPNASqhiTPSYNYAPNPD---------KHWIMRYtgPMKPIHMEFTNM-----LQRKRLQT 286
Cdd:cd16028 165 YIRPHPPfVAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 287 ----LMS-VDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNVEA----GCLNP 357
Cdd:cd16028 239 tylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREAdatrGQVVD 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 29789100 358 HIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERP 395
Cdd:cd16028 318 AFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQP 355
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-390 |
1.53e-28 |
|
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: 118.84 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDqdVELGSMQVMNKTRRI-------MEQGGAHFINAFVTTPMCCPSRSSILTGKYvhNHNTYTNNENCSSP 116
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY--PWRSRLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 117 SWQAQHESR-TFAVYLNSTGYRTAFFGKY---LNEY--NGSYVPPGWKEWVGLLKNsrfynytlCRNGVKEkHGSDYSkd 190
Cdd:cd16143 77 SPPLIEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKDVDYSKP--------IKGGPLD-HGFDYY-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 191 YLT------DLITNDSVSFFRTSKKmyPHRPVLMVISHAAPHGPedsapqysrlfpnasqhITPSYNYAPNPDkhwimry 264
Cdd:cd16143 146 FGIpasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSPEFQGKSG------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 265 TGPmkpiHMEFTnmlqrkrlqtlMSVDDSMETIYNMLVETGELDNTYIVYTADHG---YHIGQFGLVKG----------K 331
Cdd:cd16143 200 AGP----YGDFV-----------YELDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgplrgmK 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789100 332 SMPYEFDIRVPFYVRGPN-VEAGCLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 390
Cdd:cd16143 265 ADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL 326
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-390 |
5.88e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 116.54 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQDVE-LGSM-QVMNKTRRI--MEQGGAHFINAFvTTPMCCPSRSSILTGKYvhNHNTYTNNencsSPSWQ 119
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKY--NFRNYVVF----GYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 120 AQHesrTFAVYLNSTGYRTAFFGK---YLNEYNGSYVPP-GWKE---WVGLLKNSRFYNYTLCRNGVKEKHGSDYSK-DY 191
Cdd:cd16151 74 KQK---TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEyclWQLTETGEKYSRPATPTFNIRNGKLLETTEgDY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 192 LTDLITNDSVSFFRTSKK-----MYPhrpvlMVIshaaPHGPedsapqysrlfpnasqhitpsynYAPNPD-KHWiMRYT 265
Cdd:cd16151 151 GPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDP-----------------------FVPTPDsPDW-DPDD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 266 GPMKPIHMEFTNMLQrkrlqtlmSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIG-----QFGLVKG-KSMPYEFDI 339
Cdd:cd16151 198 KRKKDDPEYFPDMVA--------YMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTDAGT 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 29789100 340 RVPFYVRGP-NVEAGCLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 390
Cdd:cd16151 270 HVPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL 323
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
44-398 |
3.80e-27 |
|
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: 115.94 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQDVELGS------MQVMNKTRriMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSps 117
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcygnkaMKTPNLDR--LAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 wqaqhESRTFAVYLNSTGYRTAFFGKY-LN--EYNGSYV-PPGWKEwvgllknSRFY---NY---------TLCRNGVKE 181
Cdd:cd16156 77 -----NVKTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDP-------DYWYdmrNYldelteeerRKSRRGLTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 182 KHGSDYSKDY-LTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSY--NYAPNPDK 258
Cdd:cd16156 145 LEAEGIKEEFtYGHRCTNRALDFIEKHKD----EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPLH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 259 H--WIMRYTGP----MKPIHMEFtnmlqrkrLQTLMSVDDSMETIYNMLVETGEldNTYIVYTADHGYHIGQFGL-VKGK 331
Cdd:cd16156 221 QrlWAGAKPHEdgdkGTIKHPLY--------FGCNSFVDYEIGRVLDAADEIAE--DAWVIYTSDHGDMLGAHKLwAKGP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789100 332 SMpYEFDIRVPFYVRGPN-VEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLL-DTERPVNR 398
Cdd:cd16156 291 AV-YDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIeDPEIPENR 358
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
43-412 |
2.89e-26 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 113.61 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQDVE-LGSM---QVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSspsW 118
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 119 QAQHesrTFAVYLNSTGYRTAFFGKYlneyngsYVPPGwkewvgllKNSRFYNYTLCRNG------VKEKHGSDYSKDYL 192
Cdd:PRK13759 83 NYKN---TLPQEFRDAGYYTQCIGKM-------HVFPQ--------RNLLGFHNVLLHDGylhsgrNEDKSQFDFVSDYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 193 -------------------------------------TDLITNDSVSFFRTSKkmyPHRPVLMVISHAAPHGPEDSaPQY 235
Cdd:PRK13759 145 awlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLRRRD---PTKPFFLKMSFARPHSPYDP-PKR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 236 ------SRLFPNAsqhITPSYNYAPNPDKHWIMRYTGpmkpiHMEFTNMLQRKRLQT---LMS-VDDSMETIYNMLVETG 305
Cdd:PRK13759 221 yfdmykDADIPDP---HIGDWEYAEDQDPEGGSIDAL-----RGNLGEEYARRARAAyygLIThIDHQIGRFLQALKEFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 306 ELDNTYIVYTADHGYHIGQFGLVKgKSMPYEFDIRVPFYVRGP----NVEAGCLNPHIVLNIDLAPTILDIAGLDIPADM 381
Cdd:PRK13759 293 LLDNTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDV 371
|
410 420 430
....*....|....*....|....*....|.
gi 29789100 382 DGKSILKLLDTERPVNRFHLKKKMRVWRDSF 412
Cdd:PRK13759 372 DGRSLKNLIFGQYEGWRPYLHGEHALGYSSD 402
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
43-391 |
5.36e-26 |
|
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: 111.38 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDqdveLG-----------SMQVMNKtrriMEQGGAHFiNAFVTTPMCCPSRSSILTGKYVH-NHNTYTNN 110
Cdd:cd16025 2 RPNILLILADD----LGfsdlgcfggeiPTPNLDA----LAAEGLRF-TNFHTTALCSPTRAALLTGRNHHqVGMGTMAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 111 ENCSSPSWQAQ--HESRTFAVYLNSTGYRTAFFGKYLNeyngsyVPPGWkewvgllknsrfynytlcrngvkekhgsdys 188
Cdd:cd16025 73 LATGKPGYEGYlpDSAATIAEVLKDAGYHTYMSGKWHL------GPDDY------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 189 kdYLTDLITNDSVSFFRTSKKmyPHRPVLMVISHAAPHGPedsapqysrlfpnasQHitpsynyAPnpdKHWIMRYTGP- 267
Cdd:cd16025 116 --YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP---------------LQ-------AP---KEWIDKYKGKy 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 268 --------------MK-----PIHMEFTNML------------QRKRLQTLMSV--------DDSMETIYNMLVETGELD 308
Cdd:cd16025 167 dagwdalreerlerQKelgliPADTKLTPRPpgvpawdslspeEKKLEARRMEVyaamvehmDQQIGRLIDYLKELGELD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 309 NTYIVYTADHG--YHIG--QFG---LVKGKSMPYEFDIRVPFYVRGPNV--EAGCLNPHIVLNIDLAPTILDIAGLDIPA 379
Cdd:cd16025 247 NTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELAGVEYPK 326
|
410 420
....*....|....*....|
gi 29789100 380 D--------MDGKSILKLLD 391
Cdd:cd16025 327 TvngvpqlpLDGVSLLPTLD 346
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-388 |
1.41e-25 |
|
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: 107.25 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTD----DQdvelgsMQVMNKTRRIM------EQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnenc 113
Cdd:cd16148 1 MNVILIVIDslraDH------LGCYGYDRVTTpnldrlAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 114 sspSWQAQHESRTFAVYLNSTGYRTAFFGkylneyNGSYVPPGWkewvGLlkNSRFYNYTLCRNGVKEKHGSDYSKDylt 193
Cdd:cd16148 69 ---GGPLEPDDPTLAEILRKAGYYTAAVS------SNPHLFGGP----GF--DRGFDTFEDFRGQEGDPGEEGDERA--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 194 DLITNDSVSFFRTSKKmypHRPVLMVISHAAPHGPedsapqysrlfpnasqhitpsYNYApnpdkhwimryTGpmkpIHM 273
Cdd:cd16148 131 ERVTDRALEWLDRNAD---DDPFFLFLHYFDPHEP---------------------YLYD-----------AE----VRY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 274 eftnmlqrkrlqtlmsVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMP-YEFDIRVPFYVRGPNVEA 352
Cdd:cd16148 172 ----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEP 235
|
330 340 350
....*....|....*....|....*....|....*.
gi 29789100 353 GCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILK 388
Cdd:cd16148 236 GKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
43-391 |
5.02e-25 |
|
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: 109.20 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQDVELGSMqvmnktrrimeqgGAHFI----------------NAFVTTPMCCPSRSSILTGKYVHNHNT 106
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCY-------------GGHPAktpnidrlaargvlftNAYCQQPVCGPSRASLLTGRRPDTTGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 107 YTNNencsSPSWQAQHESRTFAVYLNSTGYRTAFFGKYL--NEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHG 184
Cdd:cd16030 69 YDNN----SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFhpGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 185 --------SDYSKDYLTD-LITNDSVSFFRTSKKMypHRPVLMVISHAAPHGPEdSAPQ-YSRLFPNASQHITPSYNYAP 254
Cdd:cd16030 145 gggpaweaADVPDEAYPDgKVADEAIEQLRKLKDS--DKPFFLAVGFYKPHLPF-VAPKkYFDLYPLESIPLPNPFDPID 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 255 NP-----DKHWIMRYTGPMKPIHMEFTNML----QRKRLQT-LMSV---DDSMETIYNMLVETGELDNTYIVYTADHGYH 321
Cdd:cd16030 222 LPevawnDLDDLPKYGDIPALNPGDPKGPLpdeqARELRQAyYASVsyvDAQVGRVLDALEELGLADNTIVVLWSDHGWH 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789100 322 IGQFGLVkGKSMPYEFDIRVPFYVRGPNV-EAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLD 391
Cdd:cd16030 302 LGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLK 371
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
73-395 |
7.01e-25 |
|
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: 106.51 E-value: 7.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 73 QGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNenCSSPSwqaqhESRTFAVYLNSTGYRTAFFGKYlneyngSY 152
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPA-----DIPTFAHYLRAAGYRTALSGKM------HF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 153 VPPgwkewvgllknsrfynytlcrngvKEKHGSDYskdyltdlitNDSVSFfRTSKKMYPH------RPVLMVISHAAPH 226
Cdd:cd16032 101 VGP------------------------DQLHGFDY----------DEEVAF-KAVQKLYDLargedgRPFFLTVSFTHPH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 227 GPEDSAPQYSRLFPNASQHitpSYnYApnpdkhwIMRYtgpmkpihmeftnmlqrkrlqtlmsVDDSMETIYNMLVETGE 306
Cdd:cd16032 146 DPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTGL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 307 LDNTYIVYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAG---LDIPADMDG 383
Cdd:cd16032 190 ADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGggtAPHVPPLDG 268
|
330
....*....|..
gi 29789100 384 KSILKLLDTERP 395
Cdd:cd16032 269 RSLLPLLEGGDS 280
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-387 |
2.63e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 103.09 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQ---------DVELgSMQVMNKtrriMEQGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTN 109
Cdd:cd16149 1 PNILFILTDDQgpwalgcygNSEA-VTPNLDR----LAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgIHDWIVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 110 NENCSSPSWQAQHESrTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHGSDYSK 189
Cdd:cd16149 76 HGKTKKPEGYLEGQT-TLPEVLQDAGYRCGLSGK----------------W----------------------HLGDDAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 190 DYLTDLITNDsvsffrtskkmyphRPVLMVISHAAPHGPEdsapQYsrlfpnasqhitpsynYApnpdkhwimrytgpmk 269
Cdd:cd16149 117 DFLRRRAEAE--------------KPFFLSVNYTAPHSPW----GY----------------FA---------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 270 pihmeftnmlqrkrlqTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGlVKGK-------SMpYEFDIRVP 342
Cdd:cd16149 147 ----------------AVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 29789100 343 FYVRGPN-VEAGCLNPHIVLNIDLAPTILDIAGLDIPADMD--GKSIL 387
Cdd:cd16149 209 FIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
44-401 |
2.81e-24 |
|
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: 106.10 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQ---DVEL-GSMQVmnKTRRIME--QGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 WQAQHEsRTFAVYLNSTGYRTAFFGKY-LNEYNGSYVPPG----------------WKEWVGLLKNsrFYNYTLCRNgvk 180
Cdd:cd16029 78 GLPLNE-TLLPQYLKELGYATHLVGKWhLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSGGAND--YGNDDLRDN--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 181 EKHGSDYSKDYLTDLITNDSVSFFRTSKkmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPsynyapnpdkhw 260
Cdd:cd16029 152 EEPAWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 261 imrytgpmkpihmeftnmLQRKRLQTLMS-VDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFG------LVKGKSM 333
Cdd:cd16029 217 ------------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNT 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789100 334 PYEFDIRVPFYVRGP--NVEAGCLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLLDTERPVNRFHL 401
Cdd:cd16029 279 LWEGGVRVPAFVWSPllPPKRGTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQWDALSGGAPSPRTEI 350
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
43-440 |
4.31e-23 |
|
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: 103.28 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQDV-----------ELGSM-QVMNKtrrimeqgGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnN 110
Cdd:cd16160 1 KPNIVLFFADDMGYgdlasyghptqERGPIdDMAAE--------GIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 111 ENCSSPSWQA---QHESRTFAVYLNSTGYRTAFFGKY---LNEYN---GSYVPP--GWkEWVGllKNSRFYNYTLCRNGV 179
Cdd:cd16160 71 GTRVFLPWDIgglPKTEVTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLPShhGF-DFVG--TNLPFTNSWACDDTG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 180 KEKHGSDYSK----------------DYLTDLITNDSVSFFRTSKkmypHRPVLMVISHAAPHGPedsapqysrLFPNAs 243
Cdd:cd16160 148 RHVDFPDRSAcflyyndtiveqpiqhEHLTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTHTP---------LFASK- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 244 qhitpsynyapnpdkhwimrytgpmkpihmEFTNMLQRKRL-QTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHI 322
Cdd:cd16160 214 ------------------------------RFKGKSKRGRYgDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 323 ------GQFGLVKG-KSMPYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL--- 390
Cdd:cd16160 264 eyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDLLlge 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 29789100 391 -DTERPVNRFHLKKK-MRVWRDSFLVERgKLLHKRDNDKVDAQEENFLPKYQ 440
Cdd:cd16160 344 aDSPHDDILYYCCSRlMAVRYGSYKIHF-KTQPLPSQESLDPNCDGGGPLSD 394
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-400 |
8.67e-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: 101.27 E-value: 8.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQDVE------LGSMQVMNKTRRIMEQGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 wqaqHES-RTFAVYLNSTGYRTAFFGKYL--NEYNGSYVPPGWKEWVGLLKN--SRFYNYTLCRNGVKEKHgsdysKDYL 192
Cdd:cd16154 80 ----ETLlQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-----TEYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 193 TDLITNDSVSFFRTSkkmypHRPVLMVISHAAPHGPedsapqysrlFpnasqHITPSYNYAPNPdkhwimryTGPMKPIH 272
Cdd:cd16154 151 TTKLTNLAIDWIDQQ-----TKPWFLWLAYNAPHTP----------F-----HLPPAELHSRSL--------LGDSADIE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 273 MEftnmlqrkRLQTLMSVDDSMETIYNMLVET---GELDNTYIVYTADHGYHiGQ-----FGLVKGKSMPYEFDIRVPFY 344
Cdd:cd16154 203 AN--------PRPYYLAAIEAMDTEIGRLLASideEERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVPLI 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 29789100 345 VRGPNVE-AGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNRFH 400
Cdd:cd16154 274 VSGAGVErANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQY 330
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-388 |
1.12e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 98.99 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQDV------------ELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYt 108
Cdd:cd16153 1 KPNILWIITDDQRVdslscynnahtgKSESRLGYVESPNIdaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 109 NNENcsspSWQAQHESR-TFAVYLNSTGYRTAFFGKylneyngsyvpPGWKEWVGLLKNSrfyNYTLCRNGVKEKHGSDY 187
Cdd:cd16153 80 GFEA----AHPALDHGLpTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGADS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 188 SKDYLTdlitndSVSFfrtskkMYPHRPVLmvishaaphgpedsapqysrlfpnasqhitpsynyapnPDKHWIMRYTgp 267
Cdd:cd16153 142 DKPFFV------RLSF------LQPHTPVL--------------------------------------PPKEFRDRFD-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 268 mkpiHMEFTNMLQRKRLQTLMSVDDsmetiynmLVETGELDNTYIVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRG 347
Cdd:cd16153 170 ----YYAFCAYGDAQVGRAVEAFKA--------YSLKQDRDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVPLIVVS 236
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 29789100 348 PNVE---AGCLNPHIVLNIDLAPTILDIAGLDI--PADMDGKSILK 388
Cdd:cd16153 237 SDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDLFE 282
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
44-390 |
2.87e-19 |
|
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: 90.68 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQDVEL----GSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtNNENCSSPSWQ 119
Cdd:cd16171 1 PNVVMVMSDSFDGRLtfrpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 120 aqhesrTFAVYLNSTGYRTAFFGKyLNEYNGSYVPPGWKE-WvgllknSRFYNYTLCRNGVKekhgsdyskdyLTDLITN 198
Cdd:cd16171 80 ------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRP-----------TVNLVGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 199 DSVSffRTSKKMYPhrpvlmvISHAAPHGPEDSAPQYSRLF--------PnasqHITPSYNYAPNpdkhwimryTGPMKP 270
Cdd:cd16171 136 RSTV--RVMLKDWQ-------NTDKAVHWIRKEAPNLTQPFalylglnlP----HPYPSPSMGEN---------FGSIRN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 271 IHMEFTNMLQRkrlqtlmsVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPNV 350
Cdd:cd16171 194 IRAFYYAMCAE--------TDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGPGI 264
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 29789100 351 EAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLL 390
Cdd:cd16171 265 KAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
75-394 |
7.32e-18 |
|
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: 86.90 E-value: 7.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 75 GAHFINAFVTTPMCCPSRSSILTGKY--VHNHNTYTNNENCSSPSwqaqhesrtFAVYLNSTGYRTAFFGKylneyNGSY 152
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHHLLRPDEPN---------LLKTLKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 153 VPPGWKEwvgllknsrfyNYTLCrngvkekhgsdyskDYLTdliTNDSVSFFRTSKkmyPHRPVLMVISHAAPHGP-EDS 231
Cdd:cd16150 102 PGEFAAE-----------AYCDS--------------DEAC---VRTAIDWLRNRR---PDKPFCLYLPLIFPHPPyGVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 232 APQYSRLFPNAS-QHITPSYNYAPNPDKHWIMRYTGpMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNT 310
Cdd:cd16150 151 EPWFSMIDREKLpPRRPPGLRAKGKPSMLEGIEKQG-LDRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 311 YIVYTADHGYHIGQFGLV-KGKSMPYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKL 389
Cdd:cd16150 230 AVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPV 309
|
....*
gi 29789100 390 LDTER 394
Cdd:cd16150 310 LAGET 314
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
749-798 |
2.16e-17 |
|
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: 85.29 E-value: 2.16e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 29789100 749 CTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNAVNTL 798
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
43-399 |
5.09e-16 |
|
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: 81.95 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDqdveLGSMQVM---NKTRR-----IMEQGGAHFINAFVTTPMCCPSRSSILTGKY------VHNHNtYT 108
Cdd:cd16159 1 KPNIVLFMADD----LGIGDVGcfgNDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHG-MR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 109 NNENCSSPSWQAQHESrTFAVYLNSTGYRTAFFGKY----------------LN-----------------------EYN 149
Cdd:cd16159 76 VILFTASSGGLPPNET-TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 150 GSYVPPGWKE--------------------------------------WVGLLKNSRFYNYTLCRNG-VKEKhgsDYSKD 190
Cdd:cd16159 155 LSFDPLFPLLtafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHeVVEQ---PMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 191 YLTDLITNDSVSFFRTSKkmypHRPVLMVISHAAPHGPEDSAPqysrLFPNASQHitpsYNYAPNpdkhwimrytgpmkp 270
Cdd:cd16159 232 NLTQRLTKEAISFLERNK----ERPFLLVMSFLHVHTALFTSK----KFKGRSKH----GRYGDN--------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 271 ihmeftnmlqrkrlqtLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHI-----------GQFGLVKGKSMP-YEFD 338
Cdd:cd16159 285 ----------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEGG 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 339 IRVPFYVRGPNVeagcLNPHIVL-----NIDLAPTILDIAGLDIPAD--MDGKSILKLLD--TERPVNRF 399
Cdd:cd16159 349 IRVPTIVRWPGV----IPPGSVIdeptsLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTgqEKRSPHEF 414
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-400 |
5.51e-16 |
|
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: 81.74 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDDQDV-ELGSMQVMNK-TRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpSW 118
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARN-AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 119 QAQH-------ESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVP--PGWKEW-------VGLLKNSRFYNYTLCRNgvkEK 182
Cdd:cd16157 80 TPQNivggipdSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWfgapnchFGPYDNKAYPNIPVYRD---WE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 183 HGSDYSKDY----------LTDLITNDSVSFFrtSKKMYPHRPVLMVISHAAPHgpedsAPQYsrlfpnASQHitpsyny 252
Cdd:cd16157 157 MIGRYYEEFkidkktgesnLTQIYLQEALEFI--EKQHDAQKPFFLYWAPDATH-----APVY------ASKP------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 253 apnpdkhwimrytgpmkpihmeFTNMLQRKRL-QTLMSVDDSMETIYNMLVETGELDNTYIVYTADHG---YHIGQFG-- 326
Cdd:cd16157 217 ----------------------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgs 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 327 ---LVKGKSMPYEFDIRVPFYVRGP-NVEAGCLNpHIVLNI-DLAPTILDIAGLDIPAD--MDGKSILKLLDTERPVNRF 399
Cdd:cd16157 275 ngpFLCGKQTTFEGGMREPAIAWWPgHIKPGQVS-HQLGSLmDLFTTSLALAGLPIPSDraIDGIDLLPVLLNGKEKDRP 353
|
.
gi 29789100 400 H 400
Cdd:cd16157 354 I 354
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-380 |
1.01e-15 |
|
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: 79.88 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDqdveLGSMQV--------M-NKTRRI--MEQGGAHFINAFVTtPMCCPSRSSILTGKYVhnhntytNNEN 112
Cdd:cd16142 1 PNILVILGDD----IGWGDLgcygggigRgAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 113 CSSPSWQAQ-----HESRTFAVYLNSTGYRTAFFGK-YLNEYNGSYvpP---GWKEWVGllknsrFYNYTLcrngvkEKH 183
Cdd:cd16142 69 LTTVGLPGSpgglpPWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 184 GSDYSKDYLTDLITNDSvSFFrtskkMYpHRPVLMvishaapHgpedsapqysrlFPNasqhitpsynyapNPDKHWIMR 263
Cdd:cd16142 135 IVDKAIDFIKRNAKADK-PFF-----LY-VNFTKM-------H------------FPT-------------LPSPEFEGK 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 264 YTGpmkpihmeftnmlQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHG-----YHIGQFGLVKG-KSMPYEF 337
Cdd:cd16142 176 SSG-------------KGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWEG 242
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 29789100 338 DIRVPFYVRGPN-VEAGCLNPHIVLNIDLAPTILDIAGLDIPAD 380
Cdd:cd16142 243 GVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
44-398 |
5.49e-14 |
|
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: 75.56 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDDQDV-ELG-----SMQVMNKTRriMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpS 117
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 WQAQHESRTFAVYLNSTGYRTAFFGKY---LNEyNGSYVPPgwkewvgllknsrfynytlcRNGVKEKHGSDYSKDY--- 191
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT--------------------HQGFDHYLGIPYSHDQgpc 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 192 --LTDLITNDSVsfFRTSKKMYPHRPVLM--VISHAAPHGPeDSAPQY----SRLFPNASQHITPSYNYAPNPDKHWiMR 263
Cdd:cd16158 138 qnLTCFPPNIPC--FGGCDQGEVPCPLFYneSIVQQPVDLL-TLEERYakfaKDFIADNAKEGKPFFLYYASHHTHY-PQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 264 YTGpmkpihMEFTNMLQRKRL-QTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHI------GQFGLVK-GKSMPY 335
Cdd:cd16158 214 FAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTY 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789100 336 EFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIP-ADMDGKSILKLLDTERPVNR 398
Cdd:cd16158 288 EGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPnVTLDGVDMSPILFEQGKSPR 351
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
44-373 |
4.71e-13 |
|
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: 69.76 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVLTDD---QDVELGSMQVMNKTR-RIMEQGGAHFiNAFVTTPMC--CPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd00016 1 KHVVLIVLDGlgaDDLGKAGNPAPTTPNlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 WQAQHES---RTFAVYLNSTGYRTAffgkylneyngsyvppgwkeWVGLLknsrfynytlcrngvkekhgsdyskDYLtd 194
Cdd:cd00016 80 SRAAGKDedgPTIPELLKQAGYRTG--------------------VIGLL-------------------------KAI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 195 litndsvsffrtsKKMYPHRPVLMVISHAAPHGPedsapqysrlfpnasqhitpSYNYAPNPDkhwimrytgpmkpihmE 274
Cdd:cd00016 113 -------------DETSKEKPFVLFLHFDGPDGP--------------------GHAYGPNTP----------------E 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 275 FTNMLQRkrlqtlmsVDDSMETIYNMLVETGELDNTYIVYTADHG---YHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVE 351
Cdd:cd00016 144 YYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVK 215
|
330 340
....*....|....*....|..
gi 29789100 352 AGCLNPHIVLNIDLAPTILDIA 373
Cdd:cd00016 216 KGGVKHELISQYDIAPTLADLL 237
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
43-390 |
6.19e-13 |
|
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: 71.35 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLTDD---QDVELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYvHNHNTYTNNENCSSPS 117
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRL-GLRNGVGHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 118 WQAQHESrTFAVYLNSTGYRTAFFGKYLNEYNGSYVPpgwkewvgllkNSRFYNYTLcrnGVKEKHGSDYSKDYL---TD 194
Cdd:cd16161 80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaTD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 195 LITNDSVSffrtskkmypHRPVLMVISHAAPHGPEDSAPqysrLFPNASQHITPsynyapnpdkhwimryTGpmkpihme 274
Cdd:cd16161 145 FIQRASAK----------DRPFFLYAALAHVHVPLANLP----RFQSPTSGRGP----------------YG-------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 275 ftnmlqrkrlQTLMSVDDSMETIYNMLVETGELDNTYIVYTAD---------------HGYHIGQFGLVKGKSMPYEFDI 339
Cdd:cd16161 187 ----------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGH 256
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 29789100 340 RVPFYVRGPN-VEAGCLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 390
Cdd:cd16161 257 REPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
44-374 |
1.61e-11 |
|
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: 65.78 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 44 PNIILVL-----TDDQDVELGSMQVMNKTRRIMEQGgAHFINAFVTTPMCCPSRS--SILTGkyvhnhnTYTNNENCSSP 116
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 117 SWQAQHESRTFAVYLNSTGYRTAFFgkylneYNGsyvppgwkewvgllkNSRFYNytlcRNGVKEKHGSD--YSKDYLTD 194
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 195 LITNDSV------SFFRTSKKMY---PHRPVLMVISHAAPHGPedsapqysrlfpnasqhitpsYNYAPNPDKhwimryt 265
Cdd:cd16015 128 DEKETNGwgvsdeSLFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 266 gpmKPIHMEFTNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFdiRVPFYV 345
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 29789100 346 RGPNVEAGCLNPHIVLNIDLAPTILDIAG 374
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
43-401 |
4.40e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 66.60 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 43 RPNIILVLtddqdVElgSMQ--VMNKT----------RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKY-VHNHNTYTN 109
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 110 NencsspswqAQHESRTFAVYLNSTGYRTAFFgkylneYNGsyvppgwkewvgllkNSRFYNytlcRNGVKEKHGSD--Y 187
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 188 SKDYLTDLITN-----DSvSFFRTSKKMYPhrpvlmvishaaphgpEDSAPQYSRLFpNASQHiTPsYNYaPNPDKHWIm 262
Cdd:COG1368 352 DREDFDDPFDGgwgvsDE-DLFDKALEELE----------------KLKKPFFAFLI-TLSNH-GP-YTL-PEEDKKIP- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 263 rytgpmkpihmEFTNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGyhigqfGLVKGKSmPYEFDI--- 339
Cdd:COG1368 410 -----------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLery 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789100 340 RVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPAD-MDGKSILKLLDTERPVNRFHL 401
Cdd:COG1368 472 RVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDLLSPDTDPFAFRNGGF 534
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
341-388 |
1.54e-06 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 51.64 E-value: 1.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 29789100 341 VPF-YVRGPNV--EAGCLNphivlniDLAPTILDIAGLDIPADMDGKSILK 388
Cdd:PRK05434 464 VPFiLVGGKALrlEGGKLA-------DIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
341-388 |
4.10e-06 |
|
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440460 Cd Length: 511 Bit Score: 50.44 E-value: 4.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 29789100 341 VPFYVRGPNVEA-----GCLnphivlnIDLAPTILDIAGLDIPADMDGKSILK 388
Cdd:COG0696 465 VPFILVGGDKGVklredGRL-------ADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
341-387 |
5.96e-06 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 49.72 E-value: 5.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 29789100 341 VPFYVRGPNV-----EAGCLnphivlnIDLAPTILDIAGLDIPADMDGKSIL 387
Cdd:cd16010 459 VPFIIVDPGLkrkllKDGGL-------ADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
343-392 |
2.64e-05 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 47.59 E-value: 2.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 29789100 343 FYVRGPNVEAGCLNPHIVLnIDLAPTILDIAGLDIPADMDGKSILKLLDT 392
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFAR 470
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
68-374 |
4.16e-05 |
|
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: 46.04 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 68 RRIMEQGgAHF---INAFVT-TpmcCPSRSSILTGKYVHNH----NTY---TNNENCSSPSWQAQH---ESRTFAVYLNS 133
Cdd:cd16018 26 KRLAEEG-VRAkyvKPVFPTlT---FPNHYSIVTGLYPESHgivgNYFydpKTNEEFSDSDWVWDPwwiGGEPIWVTAEK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 134 TGYRTA-FFgkylneyngsyvppgwkeWVGLLKNSRFYNYTLCRNGvkekhgsDYSKDYLTDLITNDSVSFFRTSKKMYp 212
Cdd:cd16018 102 AGLKTAsYF------------------WPGSEVAIIGYNPTPIPLG-------GYWQPYNDSFPFEERVDTILEWLDLE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 213 hRPVLMVISHAAPhgpeDSApqysrlfpnasQHitpsyNYAPNpdkhwimrytgpmkpiHMEFTNMLQRkrlqtlmsVDD 292
Cdd:cd16018 156 -RPDLILLYFEEP----DSA-----------GH-----KYGPD----------------SPEVNEALKR--------VDR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 293 SMETIYNMLVETGELDNTYIVYTADHGY-----HiGQFglvkgksmPYEFDIRVPFYVRGPNVEAGCLNPHIvLNIDLAP 367
Cdd:cd16018 191 RLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF-RNVDIYP 260
|
....*..
gi 29789100 368 TILDIAG 374
Cdd:cd16018 261 LMCNLLG 267
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
284-370 |
9.32e-05 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 46.05 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789100 284 LQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGY-----------HIGQFGlvkgksmPYEfdIRVPFYVRGPNVEA 352
Cdd:COG3083 430 RNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS-------RYQ--LQVPLVIHWPGTPP 500
|
90
....*....|....*...
gi 29789100 353 GCLNpHIVLNIDLAPTIL 370
Cdd:COG3083 501 QVIS-KLTSHLDIVPTLM 517
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
291-386 |
1.50e-03 |
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GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 41.40 E-value: 1.50e-03
10 20 30 40 50 60 70 80
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gi 29789100 291 DDSMETIYNMLVETGELDNTYIVYTADHGY-----HigqfglvkGKSMPYEfdIRVPFYVRGPNVEAGCLNPH------- 358
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHGMtdagnH--------GGSSPGE--TSVPLLFISPKFSSKPSNADgelsyye 246
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90 100
....*....|....*....|....*...
gi 29789100 359 IVLNIDLAPTILDIAGLDIPADMDGKSI 386
Cdd:cd16024 247 TVQQVDLAPTLALLLGLPIPKNSVGVLI 274
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