|
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: 543.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQDVELGSMQVMNKTRRIMEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNE--NCSSPSWQA 120
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 121 QHEIRTFAVYLNNTGYRTAFFGKYLNEY----NGSYVPPGWKEWVGLLKNSRFYNYTLCrNGVKEKHGYDYSRDYLTDLI 196
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 197 TNDSITFFRISKKMypHRPVLMVISHAAPHGPEDSAPQYSHLFPNAS-QHITPSYNYAPNPDKHWIMRYTGPMkPIHMEF 275
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLN-PTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 276 TNMLQRKRLQTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGSL 355
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 697472297 356 NPHIVLNIDLAPTILDIAGLDIPSDMDGKS 385
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
43-415 |
6.28e-91 |
|
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: 294.44 E-value: 6.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQ--DVeLGSMQ-VMNKT---RRIMEhGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcSSP 116
Cdd:cd16031 2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAK-EGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 117 SWQaqheiRTFAVYLNNTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGvkekhGYDYSRDYLTDLI 196
Cdd:cd16031 79 ASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENG-----KRVGQKGYVTDII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 197 TNDSITFFRISKKmypHRPVLMVISHAAPHGPEDSAPQYSHLFPNAsqHITP-----SYNYAPNPD--KHWIMRYTGPMK 269
Cdd:cd16031 149 TDKALDFLKERDK---DKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEpetfdDDDYAGRPEwaREQRNRIRGVLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 270 -PIHMEFT---NMlqRKRLQTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYV 345
Cdd:cd16031 224 gRFDTPEKyqrYM--KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLII 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697472297 346 RGP-NVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDSERPvnrfhlkkkmKVWRDSFLVE 415
Cdd:cd16031 301 RDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKP----------VDWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
43-423 |
1.52e-71 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 240.94 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQDV-ELGSM-QVMNKTRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPsw 118
Cdd:COG3119 23 RPNILFILADDLGYgDLGCYgNPLIKTPNIdrLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 119 qAQHEIRTFAVYLNNTGYRTAFFGKYLNeyngsyvppgwkewvgllknsrfynytlcrngvkekhgydysrdYLTDLITN 198
Cdd:COG3119 101 -LPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLLTD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 199 DSITFfrISKKMYPHRPVLMVISHAAPHGPEDSAPQYSHLFPNasQHITPSYNYAPNPDKHWIMRYtgpmkpihmeftnm 278
Cdd:COG3119 136 KAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR-------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 279 LQRKRLQTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPN-VEAGSLNP 357
Cdd:COG3119 198 ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVSD 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697472297 358 HIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDSERPvnrfhlkkkmkVWRDSFLVERGKLLHKR 423
Cdd:COG3119 278 ALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKA-----------EWRDYLYWEYPRGGGNR 332
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
533-673 |
6.57e-70 |
|
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: 227.23 E-value: 6.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 533 PNYVRNRSIRSVSVELDGEVYNFGLEDGYQPVLPRNITKRHKmQRDIAREEEDRdtgEYSGTGGIAE----YTAPNLIKV 608
Cdd:pfam12548 2 PRFVRTRQKRSLSVEFEGEVYDIDLEEEYQPLEPRNLLKRHA-RDDGEEGEEGE---ESSGTGSKRDssnsVGPPASVKV 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697472297 609 THRCYILENDTVQCDTDLYRSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCNK 673
Cdd:pfam12548 78 THRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
44-385 |
1.41e-49 |
|
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: 174.93 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQ---DVE-LGSMQVmnKTRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcsspS 117
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN----G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 WQAQHEIRTFAVYLNNTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHgyDYSRDYLtdlit 197
Cdd:cd16022 75 GGLPPDEPTLAELLKEAGYRTALIGK----------------W----------------------H--DEAIDFI----- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 198 ndsitffrisKKMYPHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpsYNYApnpdkhwimrytgpmkpiHMeftn 277
Cdd:cd16022 110 ----------ERRDKDKPFFLYVSFNAPHPP---------------------FAYY------------------AM---- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 278 mlqrkrlqtLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNV-EAGSLN 356
Cdd:cd16022 137 ---------VSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKiPAGQVS 207
|
330 340
....*....|....*....|....*....
gi 697472297 357 PHIVLNIDLAPTILDIAGLDIPSDMDGKS 385
Cdd:cd16022 208 DALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-395 |
2.64e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 179.69 E-value: 2.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDD---QDveLGSMQVMN-KT---RRIMEHGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencss 115
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTpnlDRLAKEG-VVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 116 pSWQAQHEIRTFAVYLNNTGYRTAFFGK--------YLNEYNGSYVPP----GWKEWVGLLKNSRFYNYTLCRNGVKEKH 183
Cdd:cd16034 72 -DVPLPPDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 184 GYDYSRDYLTDLItndsITFfrISKKMYPHRPVLMVISHAAPHGPEDSAPQ-YSHLFPNASQHitpsynYAPNPDKhwim 262
Cdd:cd16034 151 IKGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLL------LRPNVPE---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 263 rytgpmkpihmeftNMLQRKRLQTLM--------SVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVkGKSMP 334
Cdd:cd16034 215 --------------DKKEEAGLREDLrgyyamitALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVP 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697472297 335 YEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDSERP 395
Cdd:cd16034 280 YEESIRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKD 341
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
44-398 |
2.06e-47 |
|
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: 173.46 E-value: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQDVELGSmqVMN---KTRRIME--HGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencSSPSW 118
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGL----RSRGF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 119 QAQHEIRTFAVYLNNTGYRTAFFGKYlnEYNGSYVPPGWKEWVGLLKNSRFYNytlcrngvkekHGYDYSRDYLTDLITN 198
Cdd:cd16027 75 PLPDGVKTLPELLREAGYYTGLIGKT--HYNPDAVFPFDDEMRGPDDGGRNAW-----------DYASNAADFLNRAKKG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 199 D----SITFFriskkmYPHRPVLMVISHAAPHGPEDsapqyshlfpnasqhITPSYNYAPNPdkhwIMRYtgpmkpihmE 274
Cdd:cd16027 142 QpfflWFGFH------DPHRPYPPGDGEEPGYDPEK---------------VKVPPYLPDTP----EVRE---------D 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 275 FTNMLQrkrlqTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYhigqfGLVKGKSMPYEFDIRVPFYVRGPN-VEAG 353
Cdd:cd16027 188 LADYYD-----EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKPG 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 697472297 354 SLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDSERPVNR 398
Cdd:cd16027 258 SVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-390 |
1.54e-46 |
|
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: 172.34 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDqdveLGSMQV---MNK---TRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKY--------VHNHNTY 107
Cdd:cd16144 1 PNIVLILVDD----LGWADLgcyGSKfyeTPNIdrLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 108 TNNENCSSPSWQAQH---EIRTFAVYLNNTGYRTAFFGKY-LNEYNGSYvpP---GWKEWVGLLKNSRFYNYTLCRNGVK 180
Cdd:cd16144 77 PPDNTKLIPPPSTTRlplEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 181 EKHGYDYSRDYLTDLITNDSITFFRISKKmyphRPVLMVISHAAPHGPEDSAPQYSHLFPNAsqhitpsynYAPNPDKHW 260
Cdd:cd16144 155 PDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKYEKK---------KKGLRKGQK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 261 IMRYTGpmkpihmeftnMLQrkrlqtlmSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLV-------KGKSM 333
Cdd:cd16144 222 NPVYAA-----------MIE--------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGGKGS 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 334 PYEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPS--DMDGKSILKLL 390
Cdd:cd16144 283 LYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLL 342
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-394 |
8.09e-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: 8.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQDV-ELGSM-QVMNKTRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKyvHNHNTY--TNNENCSSPS 117
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTGHTRvrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 WQAqhEIRTFAVYLNNTGYRTAFFGKY-LNEYNGSYVPP--GWKEWVGLLKNSR---FYNYTLCRNGVKEKH-------- 183
Cdd:cd16145 79 LPP--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGYLDQVHahnYYPEYLWRNGEKVPLpnnvippl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 184 ----GYDYSR-DYLTDLITNDSITFFRISKKmyphRPVLMVISHAAPHGPedsapqyshlfpnasqHITPSYNYAPNPDK 258
Cdd:cd16145 157 degnNAGGGGgTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAP----------------LQVPDDGPYKYKPK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 259 HWIMRYTGPMKPIHMEFTNMLQRkrlqtlmsVDDSMEMIYNTLVETGELDNTYIIYTADHGYHI-------GQF-----G 326
Cdd:cd16145 217 DPGIYAYLPWPQPEKAYAAMVTR--------LDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngP 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 327 LVKGK-SMpYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDSER 394
Cdd:cd16145 289 LRGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGKP 357
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
44-375 |
2.40e-39 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 147.95 E-value: 2.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQ---DVELGSMqVMNKTRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNEncsspsW 118
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLYGY-PRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 119 QAQHEIRTFAVYLNNTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGLLKNSRFYNYTlcrngvKEKHGYDYSRDYLTDLI 196
Cdd:pfam00884 74 GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADP------PDVPYNCSGGGVSDEAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 197 TNDSITFfriskKMYPHRPVLMVISHAAPHGPEDSAPQYshlfPNASQHITPSYNYAPNPDkhwimrytgpmkpihmeft 276
Cdd:pfam00884 148 LDEALEF-----LDNNDKPFFLVLHTLGSHGPPYYPDRY----PEKYATFKPSSCSEEQLL------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 277 nmlqRKRLQTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFG--LVKGKSM-PYEFDIRVPFYVRGPNVEA- 352
Cdd:pfam00884 200 ----NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAk 275
|
330 340
....*....|....*....|...
gi 697472297 353 GSLNPHIVLNIDLAPTILDIAGL 375
Cdd:pfam00884 276 GQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-395 |
1.27e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 148.15 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQ--DVeLGSM-QVMNKTRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNenCSSPS 117
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 wqaqhEIRTFAVYLNNTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHGYDYSRDYLTDLit 197
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 198 ndSITFFRiskKMYPHRPVLMVISHAAPH---------GPEDSAPQYSHLFP---------NASQHItpsynyapnPDkh 259
Cdd:cd16152 113 --AIDYLD---NRQKDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWVppdlaalpgDWAEEL---------PD-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 260 wimrYTGpmkpihmeftnMLQRkrlqtlmsVDDSMEMIYNTLVETGELDNTYIIYTADHGYHigqFGLVKG--KSMPYEF 337
Cdd:cd16152 177 ----YLG-----------CCER--------LDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 697472297 338 DIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDSERP 395
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVE 288
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-415 |
2.08e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 148.52 E-value: 2.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQ--DVELGSMQVMNKT---RRIMEHGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSW 118
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTpniDRLAAEG-VRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 119 QAQHEIRTFAVYLNNTGYRTAFFGKylneyngsyvppgwkeW-VGLLKNSRFYnytlcrnGVKEKHGYDYSRDYLtdlIT 197
Cdd:cd16033 80 GLPPGVETFSEDLREAGYRNGYVGK----------------WhVGPEETPLDY-------GFDEYLPVETTIEYF---LA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 198 NDSITFFRISKKmyPHRPVLMVISHAAPHGPEDSAPQYSHLFPNASQHITPSYN--YAPNPDKHWIMRytgpMKPIHMEF 275
Cdd:cd16033 134 DRAIEMLEELAA--DDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFAddFEDKPYIYRRER----KRWGVDTE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 276 TNMLQRKRLQ------TLMsvDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLV-KGKSMpYEFDIRVPFYVRGP 348
Cdd:cd16033 208 DEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKWP 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697472297 349 NV-EAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDSERPVNrfhlkkkmkvWRDSFLVE 415
Cdd:cd16033 285 GViAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-420 |
6.89e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 145.79 E-value: 6.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQDVE----LGSMQVmnKTRRI--MEHGGAHFINAFVTTPM----CCPSRSSILTGKYVHNhntYTNNEN 112
Cdd:cd16155 2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 113 CSSPSwqaqhEIRTFAVYLNNTGYRTAFFGKYLNEYngsyvppgwkewvgllknsrfynytlcrngvkekhgydysrdyl 192
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 193 tdliTNDSITFFRisKKMYPHRPVLMVISHAAPHGPEDSAPQYSHLFPnaSQHITPSYNYAP-NPdkhwimrytgpmkpi 271
Cdd:cd16155 108 ----ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLPqHP--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 272 hmeFTNMLQRKRLQTL-------------------MS--VDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVkG 330
Cdd:cd16155 165 ---FDNGEGTVRDEQLapfprtpeavrqhlaeyyaMIthLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-G 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 331 KSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDSERPVNRFHLKKKMKVWRD 410
Cdd:cd16155 241 KQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDTLYGAYRDGQR 320
|
410
....*....|
gi 697472297 411 SFLVERGKLL 420
Cdd:cd16155 321 AIRDDRWKLI 330
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
44-393 |
8.32e-36 |
|
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: 140.76 E-value: 8.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQ---DVELGSMQVMnKTRRI--MEHGGAHFINaFVTTPMCCPSRSSILTGKYVHN---HNTYTNNENCSS 115
Cdd:cd16146 1 PNVILILTDDQgygDLGFHGNPIL-KTPNLdrLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHTILGRERMRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 116 pswqaqhEIRTFAVYLNNTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGL----------LKNSRFYNYTLCRNGVKEKH 183
Cdd:cd16146 79 -------DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdYWGNDYFDDTYYHNGKFVKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 184 gydysRDYLTDLITNDSITFFRISKKmyphRPVLMVISHAAPHGPEDSAPQYSHLFPNASQHITPSYNYApnpdkhwimr 263
Cdd:cd16146 152 -----EGYCTDVFFDEAIDFIEENKD----KPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG---------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 264 ytgpmkpihmeftnMLQRkrlqtlmsVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIG-----QFGLVKGKSMPYEFD 338
Cdd:cd16146 213 --------------MIEN--------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEGG 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 697472297 339 IRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPS--DMDGKSILKLLDSE 393
Cdd:cd16146 271 HRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPEgiKLDGRSLLPLLKGE 328
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
69-399 |
3.11e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 136.52 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 69 RIMEHGGAhFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpswqaqhEIRTFAVYLNNTGYRTAFFGK--YLN 146
Cdd:cd16037 31 RLAARGTR-FENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 147 EyngsyvppgwkewvgllknsrfynytlcrngvKEKHGYDYSRDyltdlITNDSITFFRisKKMYPHRPVLMVISHAAPH 226
Cdd:cd16037 103 E--------------------------------DQRHGFRYDRD-----VTEAAVDWLR--EEAADDKPWFLFVGFVAPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 227 gpedsapqyshlFPnasqhitpsynyapnpdkhwimrYTGPMkpihmEFTNMLQRKRLQT---LMS-VDDSMEMIYNTLV 302
Cdd:cd16037 144 ------------FP-----------------------LIAPQ-----EFYDLYVRRARAAyygLVEfLDENIGRVLDALE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 303 ETGELDNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMD 382
Cdd:cd16037 184 ELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLD 262
|
330
....*....|....*..
gi 697472297 383 GKSILKLLDSERPVNRF 399
Cdd:cd16037 263 GRSLLPLAEGPDDPDRV 279
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-398 |
9.63e-34 |
|
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: 134.23 E-value: 9.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQ---DVE-LGSMQVmnKTRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTNNE 111
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGSPLI--KTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 112 NCSSPSwqaqhEIrTFAVYLNNTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGLL------------KNSRFYNYTLCRN 177
Cdd:cd16026 79 GGLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIPysndmwpfplyrNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 178 GVKEKHGYDYSRdyLTDLITNDSITFFRISKKmyphRPVLMVISHAAPHGPedsapqyshLFPNasqhitpsynyapnpd 257
Cdd:cd16026 153 EEVIEQPADQSS--LTQRYTDEAVDFIERNKD----QPFFLYLAHTMPHVP---------LFAS---------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 258 khwimrytgpmkpihMEFTNMLQRKRL-QTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHG--YHIGQFG-----LVK 329
Cdd:cd16026 202 ---------------EKFKGRSGAGLYgDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRG 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697472297 330 GKSMPYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLLDSERPVNR 398
Cdd:cd16026 267 GKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLLLGGSKSPP 338
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
75-395 |
1.87e-31 |
|
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: 128.53 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 75 GAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencSSPswQAQHEiRTFAVYLNNTGYRTAFFGKylneynGSYVP 154
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARH-LTLALELRKAGYDPALFGY------TDTSP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 155 PGwkewVGLLKN---SRFYNYTLCrngvkekhGYDYsRDYLTDLITNDSITFFRISKKM-----YPHRPVLMVISHAAPH 226
Cdd:cd16028 103 DP----RGLAPLdprLLSYELAMP--------GFDP-VDRLDEYPAEDSDTAFLTDRAIeyldeRQDEPWFLHLSYIRPH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 227 GPEdSAPQYSHLFPNASQhiTPSYNYAPNPD---------KHWIMRYtgPMKPIHMEFTNM-----LQRKRLQT----LM 288
Cdd:cd16028 170 PPF-VAPAPYHALYDPAD--VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMRAtylgLI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 289 S-VDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNVEA----GSLNPHIVLNI 363
Cdd:cd16028 245 AeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREAdatrGQVVDAFTESV 323
|
330 340 350
....*....|....*....|....*....|..
gi 697472297 364 DLAPTILDIAGLDIPSDMDGKSILKLLDSERP 395
Cdd:cd16028 324 DVMPTILDWLGGEIPHQCDGRSLLPLLAGAQP 355
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-379 |
4.45e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 124.24 E-value: 4.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQ----DVELGSMQVMNKTR-RIMEHGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnENCSSPS- 117
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPAReRLAANG-LSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 WQAQHEIRTFAVYLNNTGYRTAFFGKY-LNEYNGSyvppgwkewvgllknsrfynytlcrngvkekhGYDYsrdylTDLI 196
Cdd:cd16035 77 PLLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGG--------------------------------GYKR-----DPGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 197 TNDSITFFR-ISKKMYPHRPVLMVISHAAPHgpeDsapqySHLFPNASQHITPSYNYapnpdkhwimrytgpmkpihmeF 275
Cdd:cd16035 120 AAQAVEWLReRGAKNADGKPWFLVVSLVNPH---D-----IMFPPDDEERWRRFRNF----------------------Y 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 276 TNMLQRkrlqtlmsVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAG-- 353
Cdd:cd16035 170 YNLIRD--------VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGTgq 241
|
330 340
....*....|....*....|....*....
gi 697472297 354 ---SLNPHivlnIDLAPTILDIAGLDIPS 379
Cdd:cd16035 242 ttdALTSH----IDLLPTLLGLAGVDAEA 266
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
73-395 |
6.24e-30 |
|
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: 121.53 E-value: 6.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 73 HGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNenCSSPSwqaqhEIRTFAVYLNNTGYRTAFFGKYlneyngSY 152
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPA-----DIPTFAHYLRAAGYRTALSGKM------HF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 153 VPPgwkewvgllknsrfynytlcrngvKEKHGYDYsrdyltdlitnDSITFFRISKKMYPH------RPVLMVISHAAPH 226
Cdd:cd16032 101 VGP------------------------DQLHGFDY-----------DEEVAFKAVQKLYDLargedgRPFFLTVSFTHPH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 227 GPEDSAPQYSHLFPNASQHitpSYnYApnpdkhwIMRYtgpmkpihmeftnmlqrkrlqtlmsVDDSMEMIYNTLVETGE 306
Cdd:cd16032 146 DPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTGL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 307 LDNTYIIYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAG---LDIPSDMDG 383
Cdd:cd16032 190 ADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGggtAPHVPPLDG 268
|
330
....*....|..
gi 697472297 384 KSILKLLDSERP 395
Cdd:cd16032 269 RSLLPLLEGGDS 280
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-390 |
7.70e-30 |
|
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: 122.69 E-value: 7.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDqdVELGSMQVMNKTRRI-------MEHGGAHFINAFVTTPMCCPSRSSILTGKYvhNHNTYTNNENCSSP 116
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY--PWRSRLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 117 SWQAQHEIR-TFAVYLNNTGYRTAFFGKY---LNEY--NGSYVPPGWKEWVGLLKNsrfynytlCRNGVKEkHGYDYS-- 188
Cdd:cd16143 77 SPPLIEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKDVDYSKP--------IKGGPLD-HGFDYYfg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 189 --RDYLTDLITNDSITFfrISKKMYPHRPVLMVISHAAPHGPedsapqyshlfpnasqhITPSYNYAPNPDkhwimryTG 266
Cdd:cd16143 148 ipASEVLPTLTDKAVEF--IDQHAKKDKPFFLYFALPAPHTP-----------------IVPSPEFQGKSG-------AG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 267 PmkpiHMEFTnmlqrkrlqtlMSVDDSMEMIYNTLVETGELDNTYIIYTADHG---YHIGQFGLVKG----------KSM 333
Cdd:cd16143 202 P----YGDFV-----------YELDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgplrgmKAD 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 334 PYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLL 390
Cdd:cd16143 267 IYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL 326
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-434 |
2.14e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 121.17 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQDVE-LGSM-QVMNKTRRI--MEHGGAHFINAFvTTPMCCPSRSSILTGKYvhNHNTYTNNencsSPSWQ 119
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKY--NFRNYVVF----GYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 120 AQHeirTFAVYLNNTGYRTAFFGK---YLNEYNGSYVPP-GWKEWV-------GLLKNSRFYNYTLCRNGVKEKhgyDYS 188
Cdd:cd16151 74 KQK---TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 189 RDYLTDLITNDSITFFRISKK-----MYPhrpvlMVIshaaPHGPedsapqyshlfpnasqhitpsynYAPNPD-KHWiM 262
Cdd:cd16151 148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDP-----------------------FVPTPDsPDW-D 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 263 RYTGPMKPIHMEFTNMLQrkrlqtlmSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIG-----QFGLVKG-KSMPYE 336
Cdd:cd16151 195 PDDKRKKDDPEYFPDMVA--------YMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 337 FDIRVPFYVRGP-NVEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLL-----DSERPVNRFHLKKKMKVW 408
Cdd:cd16151 267 AGTHVPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQLlgktgSPRREWIYWYYRNPHKKF 346
|
410 420 430
....*....|....*....|....*....|...
gi 697472297 409 RDSFLVER-------GKLLHKREnekvDAQEEN 434
Cdd:cd16151 347 GSRFVRTKryklyadGRFFDLRE----DPLEKN 375
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
44-398 |
9.48e-29 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 120.95 E-value: 9.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQDVELGS------MQVMNKTRriMEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSps 117
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcygnkaMKTPNLDR--LAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 wqaqhEIRTFAVYLNNTGYRTAFFGKY-LN--EYNGSYV-PPGWKE--WVGLlKN------------SRFYNYTLCRNGV 179
Cdd:cd16156 77 -----NVKTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDM-RNyldelteeerrkSRRGLTSLEAEGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 180 KEKHGYDYSrdyltdlITNDSITFFRiskkMYPHRPVLMVISHAAPHGPEDSAPQYSHLFPNASQHITPSY--NYAPNPD 257
Cdd:cd16156 151 KEEFTYGHR-------CTNRALDFIE----KHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 258 KH--WIMRYTGP----MKPIHMEFtnmlqrkrLQTLMSVDDSMEMIYNTLVETGEldNTYIIYTADHGYHIGQFGL-VKG 330
Cdd:cd16156 220 HQrlWAGAKPHEdgdkGTIKHPLY--------FGCNSFVDYEIGRVLDAADEIAE--DAWVIYTSDHGDMLGAHKLwAKG 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 331 KSMpYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLL-DSERPVNR 398
Cdd:cd16156 290 PAV-YDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIeDPEIPENR 358
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
43-412 |
1.38e-27 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 117.46 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQDVE-LGSM---QVMNKTRRIMEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSspsW 118
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 119 QAQHEI-RTFAvylnNTGYRTAFFGKYlneyngsYVPPGwkewvgllKNSRFYNYTLCRNG------VKEKHGYDYSRDY 191
Cdd:PRK13759 83 NYKNTLpQEFR----DAGYYTQCIGKM-------HVFPQ--------RNLLGFHNVLLHDGylhsgrNEDKSQFDFVSDY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 192 L-------------------------------------TDLITNDSITFFRiskKMYPHRPVLMVISHAAPHGPEDSAPQ 234
Cdd:PRK13759 144 LawlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 235 YSHLFPNASQHITPSYNYA----PNPDKHWIMRYTGPMKPihmeftNMLQRKRLQTLMS---VDDSMEMIYNTLVETGEL 307
Cdd:PRK13759 221 YFDMYKDADIPDPHIGDWEyaedQDPEGGSIDALRGNLGE------EYARRARAAYYGLithIDHQIGRFLQALKEFGLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 308 DNTYIIYTADHGYHIGQFGLVKgKSMPYEFDIRVPFYVRGP----NVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDG 383
Cdd:PRK13759 295 DNTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDG 373
|
410 420
....*....|....*....|....*....
gi 697472297 384 KSILKLLDSERPVNRFHLKKKMKVWRDSF 412
Cdd:PRK13759 374 RSLKNLIFGQYEGWRPYLHGEHALGYSSD 402
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
43-391 |
1.73e-27 |
|
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: 116.52 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQDVELGSMqvmnktrrimehgGAHFI----------------NAFVTTPMCCPSRSSILTGKYVHNHNT 106
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCY-------------GGHPAktpnidrlaargvlftNAYCQQPVCGPSRASLLTGRRPDTTGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 107 YTNNencsSPSWQAQHEIRTFAVYLNNTGYRTAFFGKYL--NEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHG 184
Cdd:cd16030 69 YDNN----SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFhpGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 185 YDYSR---------DYLTDLITNDSITF-----------------------FRISKK---MYPHRPVLMVISHAAPHGPE 229
Cdd:cd16030 145 GGGPAweaadvpdeAYPDGKVADEAIEQlrklkdsdkpfflavgfykphlpFVAPKKyfdLYPLESIPLPNPFDPIDLPE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 230 DSAPQYSHLfpnasqhitpsynyaPNPDKHWIMRYTGPMKPIHMEFtnmlQRKRLQT-LMSV---DDSMEMIYNTLVETG 305
Cdd:cd16030 225 VAWNDLDDL---------------PKYGDIPALNPGDPKGPLPDEQ----ARELRQAyYASVsyvDAQVGRVLDALEELG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 306 ELDNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGK 384
Cdd:cd16030 286 LADNTIVVLWSDHGWHLGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGK 364
|
....*..
gi 697472297 385 SILKLLD 391
Cdd:cd16030 365 SLVPLLK 371
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-388 |
3.03e-27 |
|
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: 111.87 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTD----DQdvelgsMQVMNKTRRIMEH------GGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnenc 113
Cdd:cd16148 1 MNVILIVIDslraDH------LGCYGYDRVTTPNldrlaaEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 114 sspSWQAQHEIRTFAVYLNNTGYRTAFFGkylneyNGSYVPPGWkewvGLlkNSRFYNYTLCRNGVKEKHGYDYSRDylt 193
Cdd:cd16148 69 ---GGPLEPDDPTLAEILRKAGYYTAAVS------SNPHLFGGP----GF--DRGFDTFEDFRGQEGDPGEEGDERA--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 194 DLITNDSITFFrisKKMYPHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpsYNYApnpdkhwimryTGpmkpIHM 273
Cdd:cd16148 131 ERVTDRALEWL---DRNADDDPFFLFLHYFDPHEP---------------------YLYD-----------AE----VRY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 274 eftnmlqrkrlqtlmsVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVKGKSMP-YEFDIRVPFYVRGPNVEA 352
Cdd:cd16148 172 ----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEP 235
|
330 340 350
....*....|....*....|....*....|....*.
gi 697472297 353 GSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILK 388
Cdd:cd16148 236 GKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
43-393 |
1.18e-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: 113.31 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDqdveLG-----------SMQVMNKtrriMEHGGAHFiNAFVTTPMCCPSRSSILTGKYVH-NHNTYTNN 110
Cdd:cd16025 2 RPNILLILADD----LGfsdlgcfggeiPTPNLDA----LAAEGLRF-TNFHTTALCSPTRAALLTGRNHHqVGMGTMAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 111 ENCSSPSWQAQ--HEIRTFAVYLNNTGYRTAFFGKYLNeyngsyVPPGWkewvgllknsrfynytlcrngvkekhgydys 188
Cdd:cd16025 73 LATGKPGYEGYlpDSAATIAEVLKDAGYHTYMSGKWHL------GPDDY------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 189 rdYLTDLITNDSITFFRISKKmyPHRPVLMVISHAAPHGPedsapqysHlfpnasqHitpsynyAPnpdKHWIMRYTGP- 267
Cdd:cd16025 116 --YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP--------L-------Q-------AP---KEWIDKYKGKy 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 268 --------------MK-----PIHMEFTNML-----------QRKRLQTLMsvddsME----MIYNT----------LVE 303
Cdd:cd16025 167 dagwdalreerlerQKelgliPADTKLTPRPpgvpawdslspEEKKLEARR-----MEvyaaMVEHMdqqigrlidyLKE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 304 TGELDNTYIIYTADHG--YHIG--QFG---LVKGKSMPYEFDIRVPFYVRGPNV--EAGSLNPHIVLNIDLAPTILDIAG 374
Cdd:cd16025 242 LGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELAG 321
|
410 420
....*....|....*....|....*..
gi 697472297 375 LDIPSD--------MDGKSILKLLDSE 393
Cdd:cd16025 322 VEYPKTvngvpqlpLDGVSLLPTLDGA 348
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
44-401 |
1.30e-25 |
|
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: 109.95 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQ---DVEL-GSMQVmnKTRRIME--HGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 WQAQHEiRTFAVYLNNTGYRTAFFGKY-LNEYNGSYVPPG----------------WKEWVGLLKNsrFYNYTLCRNgvk 180
Cdd:cd16029 78 GLPLNE-TLLPQYLKELGYATHLVGKWhLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSGGAND--YGNDDLRDN--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 181 EKHGYDYSRDYLTDLITNDSItffRISKKMYPHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpsyNYAPnpdKHW 260
Cdd:cd16029 152 EEPAWDYNGTYSTDLFTDRAV---DIIENHDPSKPLFLYLAFQAVHAP----------------------LQVP---PEY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 261 IMRYTGPMKPIHMEftnmlQRKRLQTLMS-VDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFG------LVKGKSM 333
Cdd:cd16029 204 ADPYEDKFAHIKDE-----DRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNT 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697472297 334 PYEFDIRVPFYVRGP--NVEAGSLNPHIVLNIDLAPTILDIAGLDIPS--DMDGKSILKLLDSERPVNRFHL 401
Cdd:cd16029 279 LWEGGVRVPAFVWSPllPPKRGTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQWDALSGGAPSPRTEI 350
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-387 |
1.71e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 106.55 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQ---------DVELgSMQVMNKtrriMEHGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTN 109
Cdd:cd16149 1 PNILFILTDDQgpwalgcygNSEA-VTPNLDR----LAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgIHDWIVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 110 NENCSSPSWQAQHEIrTFAVYLNNTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHGYDYSR 189
Cdd:cd16149 76 HGKTKKPEGYLEGQT-TLPEVLQDAGYRCGLSGK----------------W----------------------HLGDDAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 190 DYLTDLITNDsitffriskkmyphRPVLMVISHAAPHGPEdsapQYshlfpnasqhitpsynYApnpdkhwimrytgpmk 269
Cdd:cd16149 117 DFLRRRAEAE--------------KPFFLSVNYTAPHSPW----GY----------------FA---------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 270 pihmeftnmlqrkrlqTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGlVKGK-------SMpYEFDIRVP 342
Cdd:cd16149 147 ----------------AVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 697472297 343 FYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMD--GKSIL 387
Cdd:cd16149 209 FIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-400 |
7.27e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 107.44 E-value: 7.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQDVE------LGSMQVMNKTRRIMEHGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 wqaqHEI-RTFAVYLNNTGYRTAFFGKYL--NEYNGSYVPPGWKEWVGLLKN--SRFYNYTLCRNGVKEKHgydysRDYL 192
Cdd:cd16154 80 ----ETLlQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-----TEYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 193 TDLITNDSITFfrISKKmypHRPVLMVISHAAPHGPedsapqySHLFPNA--SQHITPSYnyapnPDkhwimrytgpmkp 270
Cdd:cd16154 151 TTKLTNLAIDW--IDQQ---TKPWFLWLAYNAPHTP-------FHLPPAElhSRSLLGDS-----AD------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 271 IHMEftnmlqrkRLQTLMSVDDSMEMIYNTLVET---GELDNTYIIYTADHGYHiGQ-----FGLVKGKSMPYEFDIRVP 342
Cdd:cd16154 201 IEAN--------PRPYYLAAIEAMDTEIGRLLASideEERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVP 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 697472297 343 FYVRGPNVEAGSLNPHIVLNI-DLAPTILDIAGLDIPSDMDGKSILKLLDSERPVNRFH 400
Cdd:cd16154 272 LIVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQY 330
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
43-440 |
1.08e-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: 105.20 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQDV-----------ELGSM-QVMNKtrrimehgGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnN 110
Cdd:cd16160 1 KPNIVLFFADDMGYgdlasyghptqERGPIdDMAAE--------GIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 111 ENCSSPSWQA---QHEIRTFAVYLNNTGYRTAFFGKY---LNEYN---GSYVPP--GWkEWVGllKNSRFYNYTLCR--- 176
Cdd:cd16160 71 GTRVFLPWDIgglPKTEVTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLPShhGF-DFVG--TNLPFTNSWACDdtg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 177 ---NGVKEKHGYDYSRD----------YLTDLITNDSITFFRISKkmypHRPVLMVISHAAPHGPedsapqyshLFPNAs 243
Cdd:cd16160 148 rhvDFPDRSACFLYYNDtiveqpiqheHLTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTHTP---------LFASK- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 244 qhitpsynyapnpdkhwimrytgpmkpihmEFTNMLQRKRLQtlmsvDDSMEM------IYNTLVETGELDNTYIIYTAD 317
Cdd:cd16160 214 ------------------------------RFKGKSKRGRYG-----DNINEMswavgeVLDTLVDTGLDQNTLVFFLSD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 318 HGYHI------GQFGLVKG-KSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILK 388
Cdd:cd16160 259 HGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITD 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 697472297 389 LL----DSERPVNRFHLKKK-MKVWRDSFLVERgKLLHKRENEKVDAQEENFLPKYQ 440
Cdd:cd16160 339 LLlgeaDSPHDDILYYCCSRlMAVRYGSYKIHF-KTQPLPSQESLDPNCDGGGPLSD 394
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-388 |
3.90e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 94.36 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQDV------------ELGSMQVMNKTRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYt 108
Cdd:cd16153 1 KPNILWIITDDQRVdslscynnahtgKSESRLGYVESPNIdaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 109 NNENcsspSWQAQHEIR-TFAVYLNNTGYRTAFFGKylneyngsyvpPGWKEWVGLLKNSrfyNYTLCRNGVKEKHGYDy 187
Cdd:cd16153 80 GFEA----AHPALDHGLpTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGAD- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 188 srdyltdlitndsitffriskkmyPHRPVLMVISHAAPHgpedsapqyshlfpnasqhiTPSYnyapnPDKHWIMRYTgp 267
Cdd:cd16153 141 ------------------------SDKPFFVRLSFLQPH--------------------TPVL-----PPKEFRDRFD-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 268 mkpiHMEFTNMlqrkrlqtlmsVDDSMEMIYNTLVETGEL---DNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFY 344
Cdd:cd16153 170 ----YYAFCAY-----------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVPLI 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 697472297 345 VRGPNVE---AGSLNPHIVLNIDLAPTILDIAGLDI--PSDMDGKSILK 388
Cdd:cd16153 234 VVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDLFE 282
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
44-390 |
6.17e-20 |
|
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: 92.60 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQDVEL----GSMQVMNKTRRIMEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtNNENCSSPSWQ 119
Cdd:cd16171 1 PNVVMVMSDSFDGRLtfrpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 120 aqheirTFAVYLNNTGYRTAFFGKyLNEYNGSYVPPGWKE-WvgllknSRFYNYTLCRNGVKekhgydysrdyLTDLITN 198
Cdd:cd16171 80 ------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRP-----------TVNLVGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 199 DSITffRISKKMYPhrpvlmvISHAAPHGPEDSAPQYSHLF--------PnasqHITPSYNYAPNpdkhwimryTGPMKP 270
Cdd:cd16171 136 RSTV--RVMLKDWQ-------NTDKAVHWIRKEAPNLTQPFalylglnlP----HPYPSPSMGEN---------FGSIRN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 271 IHMEFTNMLQRkrlqtlmsVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPNV 350
Cdd:cd16171 194 IRAFYYAMCAE--------TDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGPGI 264
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 697472297 351 EAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLL 390
Cdd:cd16171 265 KAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
75-394 |
1.27e-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: 89.22 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 75 GAHFINAFVTTPMCCPSRSSILTGKY--VHNHNTYTNNENCSSPSwqaqheirtFAVYLNNTGYRTAFFGKylneyNGSY 152
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHHLLRPDEPN---------LLKTLKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 153 VPPGWKEwvgllknsrfyNYTLCrngvkekhgydysrDYLTdliTNDSITFFRiskKMYPHRPVLMVISHAAPHGP-EDS 231
Cdd:cd16150 102 PGEFAAE-----------AYCDS--------------DEAC---VRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 232 APQYSHLFPNAS-QHITPSYNYAPNPDKHWIMRYTGpMKPIHMEFTNMLQRKRLQTLMSVDDSMEMIYNTLVETGELDNT 310
Cdd:cd16150 151 EPWFSMIDREKLpPRRPPGLRAKGKPSMLEGIEKQG-LDRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 311 YIIYTADHGYHIGQFGLV-KGKSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKL 389
Cdd:cd16150 230 AVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPV 309
|
....*
gi 697472297 390 LDSER 394
Cdd:cd16150 310 LAGET 314
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
758-807 |
3.63e-18 |
|
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: 87.61 E-value: 3.63e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 697472297 758 CTSANNNTYWCLRTINETHNFLFCEFATGFLEYFDLNTDPYQLINAVNTL 807
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-400 |
9.36e-18 |
|
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: 87.14 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDQDV-ELGSMQVMNK-TRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNE---NCSS 115
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 116 P----SWQAQHEIrTFAVYLNNTGYRTAFFGKYLNEYNGSYVP--PGWKEW-------VGLLKNSRFYNYTLCRNGVKEK 182
Cdd:cd16157 81 PqnivGGIPDSEI-LLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWfgapnchFGPYDNKAYPNIPVYRDWEMIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 183 HGYDY-------SRDYLTDLITNDSITFfrISKKMYPHRPVLMVISHAAPHgpedsAPQYshlfpnASQHitpsynyapn 255
Cdd:cd16157 160 RYYEEfkidkktGESNLTQIYLQEALEF--IEKQHDAQKPFFLYWAPDATH-----APVY------ASKP---------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 256 pdkhwimrytgpmkpihmeFTNMLQRKRL-QTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHG---YHIGQFG----- 326
Cdd:cd16157 217 -------------------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngp 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697472297 327 LVKGKSMPYEFDIRVPFYVRGP-NVEAGSLNpHIVLNI-DLAPTILDIAGLDIPSD--MDGKSILKLLDSERPVNRFH 400
Cdd:cd16157 278 FLCGKQTTFEGGMREPAIAWWPgHIKPGQVS-HQLGSLmDLFTTSLALAGLPIPSDraIDGIDLLPVLLNGKEKDRPI 354
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
43-399 |
6.19e-17 |
|
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: 85.03 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDDqdveLGSMQVM---NKTRR-----IMEHGGAHFINAFVTTPMCCPSRSSILTGKY------VHNHNtYT 108
Cdd:cd16159 1 KPNIVLFMADD----LGIGDVGcfgNDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHG-MR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 109 NNENCSSPSWQAQHEIrTFAVYLNNTGYRTAFFGKY----------------LN-----------------------EYN 149
Cdd:cd16159 76 VILFTASSGGLPPNET-TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 150 GSYVPPGWKE--------------------------------------WVGLLKNSRFYNYTLCRNGVKEKHGYDYSRdy 191
Cdd:cd16159 155 LSFDPLFPLLtafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHEVVEQPMSLEN-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 192 LTDLITNDSITFFRISKkmypHRPVLMVISHAAPHGPEDSAPqyshLFPNASQHitpsYNYAPNpdkhwimrytgpmkpi 271
Cdd:cd16159 233 LTQRLTKEAISFLERNK----ERPFLLVMSFLHVHTALFTSK----KFKGRSKH----GRYGDN---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 272 hmeftnmlqrkrlqtLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHI-----------GQFGLVKGKSMP-YEFDI 339
Cdd:cd16159 285 ---------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEGGI 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697472297 340 RVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLLD--SERPVNRF 399
Cdd:cd16159 350 RVPTIVRWPGViPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTgqEKRSPHEF 414
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-380 |
9.40e-16 |
|
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: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDqdveLGSMQV--------M-NKTRRI--MEHGGAHFINAFVTtPMCCPSRSSILTGKYVhnhntytNNEN 112
Cdd:cd16142 1 PNILVILGDD----IGWGDLgcygggigRgAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 113 CSSPSWQAQ-----HEIRTFAVYLNNTGYRTAFFGK-YLNEYNGSYvpP---GWKEWVGllknsrFYNYTLcrngvkEKH 183
Cdd:cd16142 69 LTTVGLPGSpgglpPWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 184 GYDYSRDYLTDLITNDSiTFFriskkMYpHRPVLMvishaapHGPEDSAPQYSHLFPNASQhitpsynYApnpdkhwimr 263
Cdd:cd16142 135 IVDKAIDFIKRNAKADK-PFF-----LY-VNFTKM-------HFPTLPSPEFEGKSSGKGK-------YA---------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 264 ytgpmkpihmeftnmlqrkrlQTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHG-----YHIGQFGLVKG-KSMPYEF 337
Cdd:cd16142 184 ---------------------DSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWEG 242
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 697472297 338 DIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSD 380
Cdd:cd16142 243 GVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
43-401 |
8.82e-15 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 78.16 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLtddqdVElgSMQ--VMNKT----------RRIMEHGgAHFINAFVTTPMCCPSRSSILTGKY-VHNHNTYTN 109
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 110 NencsspswqAQHEIRTFAVYLNNTGYRTAFFgkylneYNGsyvppgwkewvgllkNSRFYNytlcRNGVKEKHGYD--Y 187
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 188 SRDYLTDLITN-----DSITFFRISKKMyphrpvlmvishaaphgPEDSAPQYSHLFpNASQHiTPsYNYaPNPDKHWIm 262
Cdd:COG1368 352 DREDFDDPFDGgwgvsDEDLFDKALEEL-----------------EKLKKPFFAFLI-TLSNH-GP-YTL-PEEDKKIP- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 263 rytgpmkpihmEFTNMLQRKRLQTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGyhigqfGLVKGKSmPYEFDI--- 339
Cdd:COG1368 410 -----------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLery 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697472297 340 RVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSD-MDGKSILKLLDSERPVNRFHL 401
Cdd:COG1368 472 RVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDLLSPDTDPFAFRNGGF 534
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
44-390 |
7.45e-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: 74.79 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDDQDV-ELG-----SMQVMNKTRriMEHGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 WQAQHEIrTFAVYLNNTGYRTAFFGKY---LNEyNGSYVPPgwkewvgllknsrfynytlcRNGVKEKHGYDYSRDY--- 191
Cdd:cd16158 80 GLPLNET-TIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT--------------------HQGFDHYLGIPYSHDQgpc 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 192 --LTDLITNDSItfFRISKKMYPHRPVLM--VISHAAPHGPeDSAPQY----SHLFPNASQHITPSYNYAPNPDKHWiMR 263
Cdd:cd16158 138 qnLTCFPPNIPC--FGGCDQGEVPCPLFYneSIVQQPVDLL-TLEERYakfaKDFIADNAKEGKPFFLYYASHHTHY-PQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 264 YTGpmkpihMEFTNMLQRKRL-QTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHI------GQFGLVK-GKSMPY 335
Cdd:cd16158 214 FAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTY 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 697472297 336 EFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPS-DMDGKSILKLL 390
Cdd:cd16158 288 EGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPIL 343
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
43-390 |
3.41e-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: 72.12 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 43 RPNIILVLTDD---QDVELGSMQVMNKTRRI--MEHGGAHFINAFVTTPMCCPSRSSILTGKYvHNHNTYTNNENCSSPS 117
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRL-GLRNGVGHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 WQAQHEIrTFAVYLNNTGYRTAFFGKYLNEYNGSYVPpgwkewvgllkNSRFYNYTLcrngvkekhGYDYSRD-YLTDLI 196
Cdd:cd16161 80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---------GIPFSHDsSLADRY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 197 TNDSITFfrISKKMYPHRPVLMVISHAAPHGPEDSAPqyshLFPNASQHITPsynyapnpdkhwimryTGpmkpihmeft 276
Cdd:cd16161 139 AQFATDF--IQRASAKDRPFFLYAALAHVHVPLANLP----RFQSPTSGRGP----------------YG---------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 277 nmlqrkrlQTLMSVDDSMEMIYNTLVETGELDNTYIIYTAD---------------HGYHIGQFGLVKGKSMPYEFDIRV 341
Cdd:cd16161 187 --------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHRE 258
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 697472297 342 PFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLL 390
Cdd:cd16161 259 PAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
44-373 |
4.91e-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: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVLTDD---QDVELGSMQVMNKTR-RIMEHGGAHFiNAFVTTPMC--CPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd00016 1 KHVVLIVLDGlgaDDLGKAGNPAPTTPNlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 118 WQAQHEI---RTFAVYLNNTGYRTAffgkylneyngsyvppgwkeWVGLLknsrfynytlcrngvkekhgydysrDYLtd 194
Cdd:cd00016 80 SRAAGKDedgPTIPELLKQAGYRTG--------------------VIGLL-------------------------KAI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 195 litndsitffrisKKMYPHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpSYNYAPNPDkhwimrytgpmkpihmE 274
Cdd:cd00016 113 -------------DETSKEKPFVLFLHFDGPDGP--------------------GHAYGPNTP----------------E 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 275 FTNMLQRkrlqtlmsVDDSMEMIYNTLVETGELDNTYIIYTADHG---YHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVE 351
Cdd:cd00016 144 YYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVK 215
|
330 340
....*....|....*....|..
gi 697472297 352 AGSLNPHIVLNIDLAPTILDIA 373
Cdd:cd00016 216 KGGVKHELISQYDIAPTLADLL 237
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
44-374 |
1.07e-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: 66.55 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 44 PNIILVL-----TDDQDVELGSMQVMNKTRRIMEHGgAHFINAFVTTPMCCPSRS--SILTGkyvhnhnTYTNNENCSSP 116
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 117 SWQAQHEIRTFAVYLNNTGYRTAFFgkylneYNGsyvppgwkewvgllkNSRFYNytlcRNGVKEKHGYD--YSRDYLTD 194
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 195 LITNDSI------TFFRISKKMY---PHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpsYNYAPNPDKhwimryt 265
Cdd:cd16015 128 DEKETNGwgvsdeSLFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 266 gpmKPIHMEFTNMLQRKRLQTLMSVDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFdiRVPFYV 345
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 697472297 346 RGPNVEAGSLNPHIVLNIDLAPTILDIAG 374
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
290-387 |
3.99e-07 |
|
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: 53.57 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 290 VDDSMEMIYNTLVETGeldNTYIIyTADHG-----YHIGQFGLVKGKSMPyefdiRVPFYVRGPNV-----EAGSLnphi 359
Cdd:cd16010 412 VDECLGRIVEAVLENG---GTLLI-TADHGnaeemIDPETGGPHTAHTTN-----PVPFIIVDPGLkrkllKDGGL---- 478
|
90 100
....*....|....*....|....*...
gi 697472297 360 vlnIDLAPTILDIAGLDIPSDMDGKSIL 387
Cdd:cd16010 479 ---ADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
230-370 |
3.46e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 50.67 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 230 DSAPQYSHLFPNASQhitPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMEMIYNTLVETGELDN 309
Cdd:COG3083 379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697472297 310 TYIIYTADHGY-----------HIGQFGlvkgksmPYEfdIRVPFYVRGPNVEAGSLNpHIVLNIDLAPTIL 370
Cdd:COG3083 456 TIVIITADHGEefnengqnywgHNSNFS-------RYQ--LQVPLVIHWPGTPPQVIS-KLTSHLDIVPTLM 517
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
341-388 |
5.09e-06 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 50.10 E-value: 5.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 697472297 341 VPF-YVRGPNV--EAGSLNphivlniDLAPTILDIAGLDIPSDMDGKSILK 388
Cdd:PRK05434 464 VPFiLVGGKALrlEGGKLA-------DIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
341-388 |
9.09e-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: 49.28 E-value: 9.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 697472297 341 VPFYVRGPNvEAGSLNPHIVLnIDLAPTILDIAGLDIPSDMDGKSILK 388
Cdd:COG0696 465 VPFILVGGD-KGVKLREDGRL-ADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
343-391 |
1.04e-05 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 49.13 E-value: 1.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 697472297 343 FYVRGPNVEAGSLNPHIVLnIDLAPTILDIAGLDIPSDMDGKSILKLLD 391
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
68-374 |
2.83e-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: 46.81 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 68 RRIMEhGGAHF---INAFVT-TpmcCPSRSSILTGKYVHNH----NTY---TNNENCSSPSWQAQH---EIRTFAVYLNN 133
Cdd:cd16018 26 KRLAE-EGVRAkyvKPVFPTlT---FPNHYSIVTGLYPESHgivgNYFydpKTNEEFSDSDWVWDPwwiGGEPIWVTAEK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 134 TGYRTA-FFgkylneyngsyvppgwkeWVGLLKNSRFYNYTLCRNGvkekhgyDYSRDYltdlitNDSITFFRIS----K 208
Cdd:cd16018 102 AGLKTAsYF------------------WPGSEVAIIGYNPTPIPLG-------GYWQPY------NDSFPFEERVdtilE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 209 KMYPHRPVLMVISHAAPhgpeDSApqyshlfpnasQHitpsyNYAPNpdkhwimrytgpmkpiHMEFTNMLQRkrlqtlm 288
Cdd:cd16018 151 WLDLERPDLILLYFEEP----DSA-----------GH-----KYGPD----------------SPEVNEALKR------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 289 sVDDSMEMIYNTLVETGELDNTYIIYTADHGY-----HiGQFglvkgksmPYEFDIRVPFYVRGP----NVEAGSLNphi 359
Cdd:cd16018 188 -VDRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPafkkGKKLGPFR--- 254
|
330
....*....|....*
gi 697472297 360 vlNIDLAPTILDIAG 374
Cdd:cd16018 255 --NVDIYPLMCNLLG 267
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
290-394 |
4.13e-04 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 43.87 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 290 VDDSMEMIYNTLVETGELDNTYIIYTADHGYHIGQF-GLVKGK---SMPYEFdIRVP--FYVRGPN-VEAGSLNPH-IVL 361
Cdd:pfam02995 313 LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLrRTSQGMleeRLPLMS-IRYPpwFRETYPQaVENLELNANrLTT 391
|
90 100 110
....*....|....*....|....*....|...
gi 697472297 362 NIDLAPTILDIAGLDIPSDMDGKSILKLLDSER 394
Cdd:pfam02995 392 PFDLHATLKDILHLGELSDKELQDRMKALDCPR 424
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
291-386 |
6.98e-04 |
|
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: 42.55 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697472297 291 DDSMEMIYNTLVETGELDNTYIIYTADHGY-----HigqfglvkGKSMPYEfdIRVPFYVRGPNVEAGSLNPH------- 358
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHGMtdagnH--------GGSSPGE--TSVPLLFISPKFSSKPSNADgelsyye 246
|
90 100
....*....|....*....|....*...
gi 697472297 359 IVLNIDLAPTILDIAGLDIPSDMDGKSI 386
Cdd:cd16024 247 TVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| |
