|
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: 542.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNE--NCSSPSWQA 120
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 121 QHEGRTFAVYLNSTGYRTAFFGKYLNEY----NGSYVPPGWKEWVGLLKNSRFYNYTLCrNGVKEKHGFDYSKDYLTDLV 196
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 197 TNDSVNFFRTSKKMypHRPVLMVISHAAPHGPEDSAPQYSHLFPNAS-QHITPSYNYAPNPDKHWIMRYTGPMkPIHMEF 275
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLN-PTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 276 TNMLQRKRLQTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGSL 355
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 1387538414 356 NPHIVLNIDLAPTILDIAGLDIPSDMDGKS 385
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
43-415 |
3.48e-90 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 291.74 E-value: 3.48e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQ--DVeLGSMQ-VMNKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcSSP 116
Cdd:cd16031 2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 117 SWQaqhegRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGvkekhGFDYSKDYLTDLV 196
Cdd:cd16031 79 ASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENG-----KRVGQKGYVTDII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 197 TNDSVNFFRTSKKmypHRPVLMVISHAAPHGPEDSAPQYSHLFPNAsqHITP-----SYNYAPNPD--KHWIMRYTGPMK 269
Cdd:cd16031 149 TDKALDFLKERDK---DKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEpetfdDDDYAGRPEwaREQRNRIRGVLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 270 -PIHMEFT---NMlqRKRLQTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYV 345
Cdd:cd16031 224 gRFDTPEKyqrYM--KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLII 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387538414 346 RGP-NVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERPVnrfhlkkkmrVWRDSFLVE 415
Cdd:cd16031 301 RDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKPV----------DWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
43-428 |
5.33e-69 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 233.62 E-value: 5.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQDV-ELGSM-QVMNKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPs 117
Cdd:COG3119 23 RPNILFILADDLGYgDLGCYgNPLIKTpniDRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 wqAQHEGRTFAVYLNSTGYRTAFFGKYLNeyngsyvppgwkewvgllknsrfynytlcrngvkekhgfdyskdYLTDLVT 197
Cdd:COG3119 101 --LPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLLT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 198 NDSVNFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSHLFPNasQHITPSYNYAPNPDKHWIMRYtgpmkpihmeftn 277
Cdd:COG3119 135 DKAIDFLERQAD--KDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 278 mLQRKRLQTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPN-VEAGSLN 356
Cdd:COG3119 198 -ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVS 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387538414 357 PHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERPVNR------FHLKKKMRVWRDsflvERGKLLHKRDSDKV 428
Cdd:COG3119 277 DALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKAEWRdylyweYPRGGGNRAIRT----GRWKLIRYYDDDGP 350
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
530-663 |
9.56e-61 |
|
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: 202.19 E-value: 9.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 530 YARNRSIRSVAIEMNGETHHVGLDDAPQ---LRNLTKQRwpgAPEDQDDKDGG-DFSGTGGLPD----YSAPNPIKVTHR 601
Cdd:pfam12548 4 FVRTRQKRSLSVEFEGEVYDIDLEEEYQplePRNLLKRH---ARDDGEEGEEGeESSGTGSKRDssnsVGPPASVKVTHR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387538414 602 CYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHK 663
Cdd:pfam12548 81 CYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-395 |
1.47e-47 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 174.29 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDD---QDveLGSMQVMN-KT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencss 115
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTpnlDRLAKEG-VVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 116 pSWQAQHEGRTFAVYLNSTGYRTAFFGK--------YLNEYNGSYVPP----GWKEWVGLLKNSRFYNYTLCRNGVKEKH 183
Cdd:cd16034 72 -DVPLPPDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 184 GFDYSKDYLTDLVtndsVNFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQ-YSHLFPNASQHitpsynYAPNPDKhwim 262
Cdd:cd16034 151 IKGYSPDAETDLA----IEYLENQAD--KDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLL------LRPNVPE---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 263 rytgpmkpihmeftNMLQRKRLQTLM--------SVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVkGKSMP 334
Cdd:cd16034 215 --------------DKKEEAGLREDLrgyyamitALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVP 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387538414 335 YEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERP 395
Cdd:cd16034 280 YEESIRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKD 341
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
44-385 |
1.90e-46 |
|
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: 166.07 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQ---DVE-LGSMQVmnKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcssP 116
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 117 SWQAQHEgRTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHgfdyskdyltdlv 196
Cdd:cd16022 75 GGLPPDE-PTLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 197 tNDSVNFFRTSKKmypHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpsYNYApnpdkhwimrytgpmkpiHMeft 276
Cdd:cd16022 103 -DEAIDFIERRDK---DKPFFLYVSFNAPHPP---------------------FAYY------------------AM--- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 277 nmlqrkrlqtLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNV-EAGSL 355
Cdd:cd16022 137 ----------VSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKiPAGQV 206
|
330 340 350
....*....|....*....|....*....|
gi 1387538414 356 NPHIVLNIDLAPTILDIAGLDIPSDMDGKS 385
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
44-398 |
1.89e-45 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 167.69 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQDVELGSmqVMN---KTRRIME--QGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTN-NENCSSPS 117
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 WQaqhegRTFAVYLNSTGYRTAFFGKYlnEYNGSYVPPGWKEWVGLLKNSRFYNytlcrngvkekHGFDYSKDYLTDLVT 197
Cdd:cd16027 79 GV-----KTLPELLREAGYYTGLIGKT--HYNPDAVFPFDDEMRGPDDGGRNAW-----------DYASNAADFLNRAKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 198 ND----SVNFFrtskkmYPHRPVLMVISHAAPHGPEDsapqyshlfpnasqhITPSYNYAPNPdkhwIMRYtgpmkpihm 273
Cdd:cd16027 141 GQpfflWFGFH------DPHRPYPPGDGEEPGYDPEK---------------VKVPPYLPDTP----EVRE--------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 274 EFTNMLQrkrlqTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYhigqfGLVKGKSMPYEFDIRVPFYVRGPN-VEA 352
Cdd:cd16027 187 DLADYYD-----EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKP 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1387538414 353 GSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERPVNR 398
Cdd:cd16027 257 GSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-390 |
3.50e-44 |
|
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: 165.41 E-value: 3.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDqdveLGSMQV---MNK---TRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKY--------VHNHNTY 107
Cdd:cd16144 1 PNIVLILVDD----LGWADLgcyGSKfyeTPNIdrLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 108 TNNENCSSPSWQAQH---EGRTFAVYLNSTGYRTAFFGKY-LNEYNGSYvpP---GWKEWVGLLKNSRFYNYTLCRNGVK 180
Cdd:cd16144 77 PPDNTKLIPPPSTTRlplEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 181 EKHGFDYSKDYLTDLVTNDSVNFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSHLFPNAsqhitpsynYAPNPDKHW 260
Cdd:cd16144 155 PDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKYEKK---------KKGLRKGQK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 261 IMRYTGpmkpihmeftnMLQrkrlqtlmSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLV-------KGKSM 333
Cdd:cd16144 222 NPVYAA-----------MIE--------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGGKGS 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 334 PYEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPS--DMDGKSILKLL 390
Cdd:cd16144 283 LYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLL 342
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-390 |
4.58e-40 |
|
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: 153.13 E-value: 4.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQDV-ELGSM-QVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKyvHNHNTY--TNNENCSSPS 117
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTGHTRvrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 WQAqhEGRTFAVYLNSTGYRTAFFGKY-LNEYNGSYVPP--GWKEWVGLLKNSR---FYNYTLCRNGVKE---------- 181
Cdd:cd16145 79 LPP--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGYLDQVHahnYYPEYLWRNGEKVplpnnvippl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 182 -------KHGFDYSkdylTDLVTNDSVNFFRTSKKmyphRPVLMVISHAAPHGPedsapqyshlfpnasqHITPSYNYAP 254
Cdd:cd16145 157 degnnagGGGGTYS----HDLFTDEALDFIRENKD----KPFFLYLAYTLPHAP----------------LQVPDDGPYK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 255 NPDKHWIMRYTGPMKPIHMEFTNMLQRkrlqtlmsVDDSMETLYNMLVETGELDNTYLVYTADHGYHI-------GQF-- 325
Cdd:cd16145 213 YKPKDPGIYAYLPWPQPEKAYAAMVTR--------LDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfd 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 326 ---GLVKGK-SMpYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLL 390
Cdd:cd16145 285 sngPLRGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
44-375 |
2.35e-39 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 147.95 E-value: 2.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQ---DVELGSMqVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcssPSW 118
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLYGY-PRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV---GLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 119 QAQHegrTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGLLKNSRFYNYTlcrngvKEKHGFDYSKDYLTDLV 196
Cdd:pfam00884 77 RTEP---SLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADP------PDVPYNCSGGGVSDEAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 197 TNDSVNFFRTskkmyPHRPVLMVISHAAPHGPEDSAPQYshlfPNASQHITPSYNYAPNPDkhwimrytgpmkpihmeft 276
Cdd:pfam00884 148 LDEALEFLDN-----NDKPFFLVLHTLGSHGPPYYPDRY----PEKYATFKPSSCSEEQLL------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 277 nmlqRKRLQTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFG--LVKGKSM-PYEFDIRVPFYVRGPNVEA- 352
Cdd:pfam00884 200 ----NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAk 275
|
330 340
....*....|....*....|...
gi 1387538414 353 GSLNPHIVLNIDLAPTILDIAGL 375
Cdd:pfam00884 276 GQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-395 |
2.33e-37 |
|
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: 144.29 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQ--DVeLGSM-QVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNenCSSPS 117
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 wqaqhEGRTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHGFDYSKDYLTDLVt 197
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDFA- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 198 ndsVNFFRTSKKmypHRPVLMVISHAAPH---------GPEDSAPQYSHLFP---------NASQHItpsynyapnPDkh 259
Cdd:cd16152 114 ---IDYLDNRQK---DKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWVppdlaalpgDWAEEL---------PD-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 260 wimrYTGpmkpihmeftnMLQRkrlqtlmsVDDSMETLYNMLVETGELDNTYLVYTADHGYHigqFGLVKG--KSMPYEF 337
Cdd:cd16152 177 ----YLG-----------CCER--------LDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387538414 338 DIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERP 395
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVE 288
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-415 |
2.56e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 141.97 E-value: 2.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQ--DVELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQ 119
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 120 AQHEGRTFAVYLNSTGYRTAFFGKY--LNEYN-GSYvppGWKEWVGllknsrfynytlcrngvKEKHgFDYskdYLTDLV 196
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWhvGPEETpLDY---GFDEYLP-----------------VETT-IEY---FLADRA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 197 tndsVNFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSHLFPNASQHITPSYN--YAPNPDKHWIMRytgpMKPIHME 274
Cdd:cd16033 137 ----IEMLEELAA--DDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFAddFEDKPYIYRRER----KRWGVDT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 275 FTNMLQRKRLQ------TLMsvDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLV-KGKSMpYEFDIRVPFYVRG 347
Cdd:cd16033 207 EDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKW 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387538414 348 PNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERPVNrfhlkkkmrvWRDSFLVE 415
Cdd:cd16033 284 PGViAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
44-390 |
2.63e-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: 141.92 E-value: 2.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQ---DVELGSMQVMnKT---RRIMEQGgAHFINaFVTTPMCCPSRSSILTGKYVHN---HNTYTNNENCS 114
Cdd:cd16146 1 PNVILILTDDQgygDLGFHGNPIL-KTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHTILGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 115 SpswqaqhEGRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGL----------LKNSRFYNYTLCRNGVKEK 182
Cdd:cd16146 78 L-------DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdYWGNDYFDDTYYHNGKFVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 183 HgfdysKDYLTDLVTNDSVNFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSHLFPNASQHITPSYNYApnpdkhwim 262
Cdd:cd16146 151 T-----EGYCTDVFFDEAIDFIEENKD----KPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG--------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 263 rytgpmkpihmeftnMLQRkrlqtlmsVDDSMETLYNMLVETGELDNTYLVYTADHGYHIG-----QFGLVKGKSMPYEF 337
Cdd:cd16146 213 ---------------MIEN--------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEG 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387538414 338 DIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPS--DMDGKSILKLL 390
Cdd:cd16146 270 GHRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPEgiKLDGRSLLPLL 325
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-420 |
1.61e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 138.85 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQDVE----LGSMQVmnKTRRI--MEQGGAHFINAFVTTPM----CCPSRSSILTGKYVHNhntYTNNEN 112
Cdd:cd16155 2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 113 CSSPSwqaqhEGRTFAVYLNSTGYRTAFFGKYLNEYngsyvppgwkewvgllknsrfynytlcrngvkekhgfdyskdyl 192
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 193 tdlvTNDSVNFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSHLFPnaSQHITPSYNYAP-NPdkhwimrytgpmkpi 271
Cdd:cd16155 108 ----ADAAIEFLEEYKD--GDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLPqHP--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 272 hmeFTNMLQRKRLQTL-------------------MS--VDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVkG 330
Cdd:cd16155 165 ---FDNGEGTVRDEQLapfprtpeavrqhlaeyyaMIthLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-G 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 331 KSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERPVNRFHLKKKMRVWRD 410
Cdd:cd16155 241 KQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDTLYGAYRDGQR 320
|
410
....*....|
gi 1387538414 411 SFLVERGKLL 420
Cdd:cd16155 321 AIRDDRWKLI 330
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
69-399 |
8.22e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 126.50 E-value: 8.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 69 RIMEQGGAhFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpswqaqhEGRTFAVYLNSTGYRTAFFGK--YLN 146
Cdd:cd16037 31 RLAARGTR-FENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 147 EyngsyvppgwkewvgllknsrfynytlcrngvKEKHGFDYSKDyltdlVTNDSVNFFRTSKkmyPH-RPVLMVISHAAP 225
Cdd:cd16037 103 E--------------------------------DQRHGFRYDRD-----VTEAAVDWLREEA---ADdKPWFLFVGFVAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 226 HgpedsapqyshlFPnasqhitpsynyapnpdkhwimrYTGPMkpihmEFTNMLQRKRLQT---LMS-VDDSMETLYNML 301
Cdd:cd16037 143 H------------FP-----------------------LIAPQ-----EFYDLYVRRARAAyygLVEfLDENIGRVLDAL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 302 VETGELDNTYLVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDM 381
Cdd:cd16037 183 EELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL 261
|
330
....*....|....*...
gi 1387538414 382 DGKSILKLLDTERPVNRF 399
Cdd:cd16037 262 DGRSLLPLAEGPDDPDRV 279
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-390 |
9.68e-31 |
|
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: 125.37 E-value: 9.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQ---DVE-LGSMQVmnKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTNNE 111
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGSPLI--KTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 112 NCSSPSwqaqhEgRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGLL------------KNSRFYNYTLCRN 177
Cdd:cd16026 79 GGLPPD-----E-ITIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIPysndmwpfplyrNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 178 GVKEKHGFDYSkdYLTDLVTNDSVNFFRTSKKmyphRPVLMVISHAAPHGPedsapqyshLFPNasqhitpsynyapnpd 257
Cdd:cd16026 153 EEVIEQPADQS--SLTQRYTDEAVDFIERNKD----QPFFLYLAHTMPHVP---------LFAS---------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 258 khwimrytgpmkpihMEFTNMLQRKRL-QTLMSVDDSMETLYNMLVETGELDNTYLVYTADHG--YHIGQFG-----LVK 329
Cdd:cd16026 202 ---------------EKFKGRSGAGLYgDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRG 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387538414 330 GKSMPYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLL 390
Cdd:cd16026 267 GKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLL 330
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-390 |
1.64e-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: 124.62 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDqdVELGSMQVMNKTRRI-------MEQGGAHFINAFVTTPMCCPSRSSILTGKYvhNHNTYTNNENCSSP 116
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY--PWRSRLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 117 SWQAQHEGR-TFAVYLNSTGYRTAFFGKY---LNEY--NGSYVPPGWKEWVGLLKNsrfynytlCRNGVKEkHGFDYSkd 190
Cdd:cd16143 77 SPPLIEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKDVDYSKP--------IKGGPLD-HGFDYY-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 191 YLT------DLVTNDSVNFFRTSKKmyPHRPVLMVISHAAPHGPedsapqyshlfpnasqhITPSYNYAPNPDkhwimry 264
Cdd:cd16143 146 FGIpasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSPEFQGKSG------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 265 TGPmkpiHMEFTnmlqrkrlqtlMSVDDSMETLYNMLVETGELDNTYLVYTADHG---YHIGQFGLVKG----------K 331
Cdd:cd16143 200 AGP----YGDFV-----------YELDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgplrgmK 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387538414 332 SMPYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLL 390
Cdd:cd16143 265 ADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL 326
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
75-395 |
2.99e-29 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 121.98 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 75 GAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencSSPswQAQHEgRTFAVYLNSTGYRTAFFGK----------- 143
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARH-LTLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 144 YLNEYNGSY--VPPGWkEWVGLLknsrfynytlcrNGVKEKHGfdySKDYLTDLVtndsVNFFRTskkmYPHRPVLMVIS 221
Cdd:cd16028 109 PLDPRLLSYelAMPGF-DPVDRL------------DEYPAEDS---DTAFLTDRA----IEYLDE----RQDEPWFLHLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 222 HAAPHGPEdSAPQYSHLFPNASQhiTPSYNYAPNPD---------KHWIMRYtgPMKPIHMEFTNM-----LQRKRLQT- 286
Cdd:cd16028 165 YIRPHPPF-VAPAPYHALYDPAD--VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMRAt 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 287 ---LMS-VDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNVEA----GSLNPH 358
Cdd:cd16028 240 ylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREAdatrGQVVDA 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1387538414 359 IVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERP 395
Cdd:cd16028 319 FTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQP 355
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
44-398 |
1.83e-28 |
|
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: 119.79 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQDVELGS------MQVMNKTRriMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnenCSSPS 117
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcygnkaMKTPNLDR--LAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN---CMALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 WQAQHEGRtfavYLNSTGYRTAFFGKY-LN--EYNGSYV-PPGWKE--WVGLlKN------------SRFYNYTLCRNGV 179
Cdd:cd16156 76 DNVKTIGQ----RLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDM-RNyldelteeerrkSRRGLTSLEAEGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 180 KEKHGFDYSkdyltdlVTNDSVNFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSHLFPNASQHITPSY--NYAPNPD 257
Cdd:cd16156 151 KEEFTYGHR-------CTNRALDFIEKHKD----EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 258 KH--WIMRYTGP----MKPIHMEFtnmlqrkrLQTLMSVDDSMETLYNMLVETGEldNTYLVYTADHGYHIGQFGL-VKG 330
Cdd:cd16156 220 HQrlWAGAKPHEdgdkGTIKHPLY--------FGCNSFVDYEIGRVLDAADEIAE--DAWVIYTSDHGDMLGAHKLwAKG 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 331 KSMpYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLL-DTERPVNR 398
Cdd:cd16156 290 PAV-YDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIeDPEIPENR 358
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-379 |
3.95e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 115.77 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQ----DVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnENCSSPS-W 118
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 119 QAQHEGRTFAVYLNSTGYRTAFFGKY-LNEYNGSYvppgwkewvgllknsrfynytlcrngvkekhgfdYSKDyltDLVT 197
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 198 NDSVNFFRTSKKMYPHR-PVLMVISHAAPHgpeDsapqySHLFPNASQHITPSYNYapnpdkhwimrytgpmkpihmeFT 276
Cdd:cd16035 121 AQAVEWLRERGAKNADGkPWFLVVSLVNPH---D-----IMFPPDDEERWRRFRNF----------------------YY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 277 NMLQRkrlqtlmsVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAG--- 353
Cdd:cd16035 171 NLIRD--------VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGTgqt 242
|
330 340
....*....|....*....|....*...
gi 1387538414 354 --SLNPHivlnIDLAPTILDIAGLDIPS 379
Cdd:cd16035 243 tdALTSH----IDLLPTLLGLAGVDAEA 266
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-390 |
4.36e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 116.93 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQDVE-LGSM-QVMNKTRRI--MEQGGAHFINAFvTTPMCCPSRSSILTGKYvhNHNTYTNNencsSPSWQ 119
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKY--NFRNYVVF----GYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 120 AQHegrTFAVYLNSTGYRTAFFGK---YLNEYNGSYVPP-GWKEWV-------GLLKNSRFYNYTLCRNGVKEKhgfDYS 188
Cdd:cd16151 74 KQK---TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 189 KDYLTDLVTNDSVNFFRTSKK-----MYPhrpvlMVIshaaPHGPedsapqyshlfpnasqhitpsynYAPNPD-KHWiM 262
Cdd:cd16151 148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDP-----------------------FVPTPDsPDW-D 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 263 RYTGPMKPIHMEFTNMLQrkrlqtlmSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIG-----QFGLVKG-KSMPYE 336
Cdd:cd16151 195 PDDKRKKDDPEYFPDMVA--------YMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387538414 337 FDIRVPFYVRGP-NVEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLL 390
Cdd:cd16151 267 AGTHVPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL 323
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
73-395 |
7.99e-27 |
|
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: 112.29 E-value: 7.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 73 QGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNenCSSPSwqaqhEGRTFAVYLNSTGYRTAFFGKYlneyngSY 152
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPA-----DIPTFAHYLRAAGYRTALSGKM------HF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 153 VPPgwkewvgllknsrfynytlcrngvKEKHGFDYSkdyltDLVTndsvnfFRTSKKMYPH------RPVLMVISHAAPH 226
Cdd:cd16032 101 VGP------------------------DQLHGFDYD-----EEVA------FKAVQKLYDLargedgRPFFLTVSFTHPH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 227 GPEDSAPQYSHLFPNASQHitpSYnYApnpdkhwIMRYtgpmkpihmeftnmlqrkrlqtlmsVDDSMETLYNMLVETGE 306
Cdd:cd16032 146 DPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTGL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 307 LDNTYLVYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAG---LDIPSDMDG 383
Cdd:cd16032 190 ADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGggtAPHVPPLDG 268
|
330
....*....|..
gi 1387538414 384 KSILKLLDTERP 395
Cdd:cd16032 269 RSLLPLLEGGDS 280
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
43-412 |
3.87e-26 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 113.23 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQDVE-LGSM---QVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSspsW 118
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 119 QAQHegrTFAVYLNSTGYRTAFFGKYlneyngsYVPPGwkewvgllKNSRFYNYTLCRNG------VKEKHGFDYSKDYL 192
Cdd:PRK13759 83 NYKN---TLPQEFRDAGYYTQCIGKM-------HVFPQ--------RNLLGFHNVLLHDGylhsgrNEDKSQFDFVSDYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 193 -------------------------------------TDLVTNDSVNFFRTSKkmyPHRPVLMVISHAAPHGPEDSAPQY 235
Cdd:PRK13759 145 awlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLRRRD---PTKPFFLKMSFARPHSPYDPPKRY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 236 SHLFPNASQHITPSYNYA----PNPDKHWIMRYTGPMKPihmeftNMLQRKRLQTLMS---VDDSMETLYNMLVETGELD 308
Cdd:PRK13759 222 FDMYKDADIPDPHIGDWEyaedQDPEGGSIDALRGNLGE------EYARRARAAYYGLithIDHQIGRFLQALKEFGLLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 309 NTYLVYTADHGYHIGQFGLVKgKSMPYEFDIRVPFYVRGP----NVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGK 384
Cdd:PRK13759 296 NTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGR 374
|
410 420
....*....|....*....|....*...
gi 1387538414 385 SILKLLDTERPVNRFHLKKKMRVWRDSF 412
Cdd:PRK13759 375 SLKNLIFGQYEGWRPYLHGEHALGYSSD 402
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
43-391 |
1.10e-25 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 111.13 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQDVELGSMqvmnktrrimeqgGAHFI----------------NAFVTTPMCCPSRSSILTGKYVHNHNT 106
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCY-------------GGHPAktpnidrlaargvlftNAYCQQPVCGPSRASLLTGRRPDTTGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 107 YTNNencsSPSWQAQHEGRTFAVYLNSTGYRTAFFGKYL--NEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHG 184
Cdd:cd16030 69 YDNN----SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFhpGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 185 F---------------------DYSKDYLTDLVTND-----SVNFFRtskkmyPHRP-----------VLMVISHAAPHG 227
Cdd:cd16030 145 GggpaweaadvpdeaypdgkvaDEAIEQLRKLKDSDkpfflAVGFYK------PHLPfvapkkyfdlyPLESIPLPNPFD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 228 PEDSAPQYSHlfpnasqhitpSYNYAPNPDKHWIMRYTGPMKPIHMEFtnmlQRKRLQT-LMSV---DDSMETLYNMLVE 303
Cdd:cd16030 219 PIDLPEVAWN-----------DLDDLPKYGDIPALNPGDPKGPLPDEQ----ARELRQAyYASVsyvDAQVGRVLDALEE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 304 TGELDNTYLVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPSDMD 382
Cdd:cd16030 284 LGLADNTIVVLWSDHGWHLGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLE 362
|
....*....
gi 1387538414 383 GKSILKLLD 391
Cdd:cd16030 363 GKSLVPLLK 371
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-388 |
1.38e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 107.25 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTD----DQdvelgsMQVMNKTRRIM------EQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnenc 113
Cdd:cd16148 1 MNVILIVIDslraDH------LGCYGYDRVTTpnldrlAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 114 sspSWQAQHEGRTFAVYLNSTGYRTAFFGkylneyNGSYVPPGWkewvGLlkNSRFYNYTLCRNGVKEKHGFDYSKDylt 193
Cdd:cd16148 69 ---GGPLEPDDPTLAEILRKAGYYTAAVS------SNPHLFGGP----GF--DRGFDTFEDFRGQEGDPGEEGDERA--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 194 DLVTNDSVNFFRTSKKmypHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpsYNYApnpdkhwimryTGpmkpIHM 273
Cdd:cd16148 131 ERVTDRALEWLDRNAD---DDPFFLFLHYFDPHEP---------------------YLYD-----------AE----VRY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 274 eftnmlqrkrlqtlmsVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVKGKSMP-YEFDIRVPFYVRGPNVEA 352
Cdd:cd16148 172 ----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEP 235
|
330 340 350
....*....|....*....|....*....|....*.
gi 1387538414 353 GSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILK 388
Cdd:cd16148 236 GKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
43-391 |
2.16e-24 |
|
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: 106.37 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDqdveLG-----------SMQVMNKtrriMEQGGAHFiNAFVTTPMCCPSRSSILTGkyVHNHNTYTNNE 111
Cdd:cd16025 2 RPNILLILADD----LGfsdlgcfggeiPTPNLDA----LAAEGLRF-TNFHTTALCSPTRAALLTG--RNHHQVGMGTM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 112 NCSSPSWQAqHEGR------TFAVYLNSTGYRTAFFGKYLNeyngsyVPPGWkewvgllknsrfynytlcrngvkekhgf 185
Cdd:cd16025 71 AELATGKPG-YEGYlpdsaaTIAEVLKDAGYHTYMSGKWHL------GPDDY---------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 186 dyskdYLTDLVTNDSVNFFRTSKKmyPHRPVLMVISHAAPHGPedsapqysHlfpnasqHitpsynyAPnpdKHWIMRYT 265
Cdd:cd16025 116 -----YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP--------L-------Q-------AP---KEWIDKYK 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 266 GP---------------MK-----PIHMEFTNML------------QRKRLQTLMSV--------DDSMETLYNMLVETG 305
Cdd:cd16025 164 GKydagwdalreerlerQKelgliPADTKLTPRPpgvpawdslspeEKKLEARRMEVyaamvehmDQQIGRLIDYLKELG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 306 ELDNTYLVYTADHG--YHIG--QFG---LVKGKSMPYEFDIRVPFYVRGPNV--EAGSLNPHIVLNIDLAPTILDIAGLD 376
Cdd:cd16025 244 ELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELAGVE 323
|
410 420
....*....|....*....|...
gi 1387538414 377 IPSD--------MDGKSILKLLD 391
Cdd:cd16025 324 YPKTvngvpqlpLDGVSLLPTLD 346
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
44-401 |
2.69e-24 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 106.10 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQ---DVEL-GSMQVmnKTRRIME--QGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 WQAQHEgRTFAVYLNSTGYRTAFFGKY-LNEYNGSYVPPG----------------WKEWVGLLKNsrFYNYTLCRNgvk 180
Cdd:cd16029 78 GLPLNE-TLLPQYLKELGYATHLVGKWhLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSGGAND--YGNDDLRDN--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 181 EKHGFDYSKDYLTDLVTNDSVNFFRTSKkmyPHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpsyNYAPnpdKHW 260
Cdd:cd16029 152 EEPAWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAP----------------------LQVP---PEY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 261 IMRYTGPMKPIHMEftnmlQRKRLQTLMS-VDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFG------LVKGKSM 333
Cdd:cd16029 204 ADPYEDKFAHIKDE-----DRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNT 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387538414 334 PYEFDIRVPFYVRGP--NVEAGSLNPHIVLNIDLAPTILDIAGLDIPS--DMDGKSILKLLDTERPVNRFHL 401
Cdd:cd16029 279 LWEGGVRVPAFVWSPllPPKRGTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQWDALSGGAPSPRTEI 350
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-387 |
9.40e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 101.55 E-value: 9.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQ---------DVELgSMQVMNKtrriMEQGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTN 109
Cdd:cd16149 1 PNILFILTDDQgpwalgcygNSEA-VTPNLDR----LAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgIHDWIVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 110 NENCSSP-SWQAQHEgrTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHGFDYS 188
Cdd:cd16149 76 HGKTKKPeGYLEGQT--TLPEVLQDAGYRCGLSGK----------------W----------------------HLGDDA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 189 KDYLTDLVTNDsvnffrtskkmyphRPVLMVISHAAPHGPEdsapQYshlfpnasqhitpsynYApnpdkhwimrytgpm 268
Cdd:cd16149 116 ADFLRRRAEAE--------------KPFFLSVNYTAPHSPW----GY----------------FA--------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 269 kpihmeftnmlqrkrlqTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGlVKGK-------SMpYEFDIRV 341
Cdd:cd16149 147 -----------------AVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKV 207
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1387538414 342 PFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMD--GKSIL 387
Cdd:cd16149 208 PFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-400 |
1.98e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 100.12 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQDVE------LGSMQVMNKTRRIMEQGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 WQAQhegRTFAVYLNSTGYRTAFFGKYL--NEYNGSYVPPGWKEWVGLLKN--SRFYNYTLCRNGVKEKHgfdysKDYLT 193
Cdd:cd16154 80 ETLL---QLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-----TEYAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 194 DLVTNDSVNFFRTSkkmypHRPVLMVISHAAPHGPedsapqySHLFPNA--SQHITPSYnyapnPDkhwimrytgpmkpI 271
Cdd:cd16154 152 TKLTNLAIDWIDQQ-----TKPWFLWLAYNAPHTP-------FHLPPAElhSRSLLGDS-----AD-------------I 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 272 HMEftnmlqrkRLQTLMSVDDSMETLYNMLVET---GELDNTYLVYTADHGYHiGQ-----FGLVKGKSMPYEFDIRVPF 343
Cdd:cd16154 202 EAN--------PRPYYLAAIEAMDTEIGRLLASideEERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVPL 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387538414 344 YVRGPNVEAGSLNPHIVLNI-DLAPTILDIAGLDIPSDMDGKSILKLLDTERPVNRFH 400
Cdd:cd16154 273 IVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQY 330
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-388 |
2.32e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 97.83 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQDV------------ELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYt 108
Cdd:cd16153 1 KPNILWIITDDQRVdslscynnahtgKSESRLGYVESPNIdaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 109 NNENcsspSWQAQHEGR-TFAVYLNSTGYRTAFFGKylneyngsyvpPGWKEWVGLLKNSrfyNYTLCRNGVKEKHGFDY 187
Cdd:cd16153 80 GFEA----AHPALDHGLpTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGADS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 188 SKdyltdlvtndsvnffrtskkmyphrPVLMVISHAAPHgpedsapqyshlfpnasqhiTPSYnyapnPDKHWIMRYTgp 267
Cdd:cd16153 142 DK-------------------------PFFVRLSFLQPH--------------------TPVL-----PPKEFRDRFD-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 268 mkpiHMEFTNMLQRKrlqtlmsVDDSMETLYNmLVETGELDNTYLVYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRG 347
Cdd:cd16153 170 ----YYAFCAYGDAQ-------VGRAVEAFKA-YSLKQDRDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVPLIVVS 236
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1387538414 348 PNVE---AGSLNPHIVLNIDLAPTILDIAGLDI--PSDMDGKSILK 388
Cdd:cd16153 237 SDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDLFE 282
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
43-390 |
2.57e-21 |
|
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: 97.89 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQDV-----------ELGSM-QVMNKtrrimeqgGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnN 110
Cdd:cd16160 1 KPNIVLFFADDMGYgdlasyghptqERGPIdDMAAE--------GIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 111 ENCSSPSWQA---QHEGRTFAVYLNSTGYRTAFFGKY---LNEYN---GSYVPP--GWkEWVGllKNSRFYNYTLCR--- 176
Cdd:cd16160 71 GTRVFLPWDIgglPKTEVTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLPShhGF-DFVG--TNLPFTNSWACDdtg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 177 ---NGVKEKHGFDYSKD----------YLTDLVTNDSVNFFRTSKkmypHRPVLMVISHAAPHGPedsapqyshLFPNAs 243
Cdd:cd16160 148 rhvDFPDRSACFLYYNDtiveqpiqheHLTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTHTP---------LFASK- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 244 qhitpsynyapnpdkhwimrytgpmkpihmEFTNMLQRKRL-QTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHI 322
Cdd:cd16160 214 ------------------------------RFKGKSKRGRYgDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHV 263
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387538414 323 ------GQFGLVKG-KSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLL 390
Cdd:cd16160 264 eyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDLL 340
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
44-390 |
1.71e-18 |
|
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: 88.37 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQDVEL----GSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtNNENCSSPSWQ 119
Cdd:cd16171 1 PNVVMVMSDSFDGRLtfrpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 120 aqhegrTFAVYLNSTGYRTAFFGKyLNEYNGSYVPPGWKE-WvgllknSRFYNYTLCRNGVKekhgfdyskdyLTDLVTN 198
Cdd:cd16171 80 ------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRP-----------TVNLVGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 199 DSVNffRTSKKMYPhrpvlmvISHAAPHGPEDSAPQYSHLF--------PnasqHITPSYNYAPNpdkhwimryTGPMKP 270
Cdd:cd16171 136 RSTV--RVMLKDWQ-------NTDKAVHWIRKEAPNLTQPFalylglnlP----HPYPSPSMGEN---------FGSIRN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 271 IHMEFTNMLQRkrlqtlmsVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPNV 350
Cdd:cd16171 194 IRAFYYAMCAE--------TDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGPGI 264
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1387538414 351 EAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLL 390
Cdd:cd16171 265 KAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
75-394 |
1.06e-17 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 86.52 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 75 GAHFINAFVTTPMCCPSRSSILTGKY--VHNHNTYTNNENCSSPSwqaqhegrtFAVYLNSTGYRTAFFGKylneyNGSY 152
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHHLLRPDEPN---------LLKTLKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 153 VPPGWKEwvgllknsrfyNYTLCrngvkekhgfdyskDYLtdlVTNDSVNFFRTSKkmyPHRPVLMVISHAAPHGP-EDS 231
Cdd:cd16150 102 PGEFAAE-----------AYCDS--------------DEA---CVRTAIDWLRNRR---PDKPFCLYLPLIFPHPPyGVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 232 APQYShlfpnasqhitpSYNYAPNPDkhwimryTGPMKPIHMEFTNMLQRKRLQTLMSVDDSM-----ETLYNM------ 300
Cdd:cd16150 151 EPWFS------------MIDREKLPP-------RRPPGLRAKGKPSMLEGIEKQGLDRWSEERwrelrATYLGMvsrldh 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 301 --------LVETGELDNTYLVYTADHGYHIGQFGLV-KGKSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILD 371
Cdd:cd16150 212 qfgrlleaLKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLD 291
|
330 340
....*....|....*....|...
gi 1387538414 372 IAGLDIPSDMDGKSILKLLDTER 394
Cdd:cd16150 292 LAGIPLSHTHFGRSLLPVLAGET 314
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
728-777 |
2.61e-17 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 84.91 E-value: 2.61e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1387538414 728 CTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNAVNTL 777
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-380 |
8.25e-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: 80.27 E-value: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDqdveLGSMQV--------M-NKTRRI--MEQGGAHFINAFVTtPMCCPSRSSILTGKYVhnhntytNNEN 112
Cdd:cd16142 1 PNILVILGDD----IGWGDLgcygggigRgAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 113 CSSPSWQAQHEG-----RTFAVYLNSTGYRTAFFGK-YLNEYNGSYvpP---GWKEWVGllknsrFYNYTLcrngvkEKH 183
Cdd:cd16142 69 LTTVGLPGSPGGlppwePTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 184 GFDYSKDYLTDLVTND-----SVNFFRTSKKMYPHrpvlmvishaaphgpedsaPQYSHLFPNASQhitpsynYApnpdk 258
Cdd:cd16142 135 IVDKAIDFIKRNAKADkpfflYVNFTKMHFPTLPS-------------------PEFEGKSSGKGK-------YA----- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 259 hwimrytgpmkpihmeftnmlqrkrlQTLMSVDDSMETLYNMLVETGELDNTYLVYTADHG-----YHIGQFGLVKG-KS 332
Cdd:cd16142 184 --------------------------DSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKG 237
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1387538414 333 MPYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSD 380
Cdd:cd16142 238 TTWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-400 |
1.93e-15 |
|
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: 79.82 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDQDV-ELGSMQVMNK-TRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpSW 118
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARN-AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 119 QAQH-------EGRTFAVYLNSTGYRTAFFGKYLNEYNGSYVP--PGWKEW-------VGLLKNSRFYNYTLCRNgvkEK 182
Cdd:cd16157 80 TPQNivggipdSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWfgapnchFGPYDNKAYPNIPVYRD---WE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 183 HGFDYSKDYLTDLVTNDSvNFfrtsKKMYPHRPVLMVISHAAPHgpedsAPQYSHLFPNASQhiTPSYNYAPnpdkhwim 262
Cdd:cd16157 157 MIGRYYEEFKIDKKTGES-NL----TQIYLQEALEFIEKQHDAQ-----KPFFLYWAPDATH--APVYASKP-------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 263 rytgpmkpihmeFTNMLQRKRL-QTLMSVDDSMETLYNMLVETGELDNTYLVYTADHG---YHIGQFG-----LVKGKSM 333
Cdd:cd16157 217 ------------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngpFLCGKQT 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387538414 334 PYEFDIRVPFYVRGP-NVEAGSLNpHIVLNI-DLAPTILDIAGLDIPSD--MDGKSILKLLDTERPVNRFH 400
Cdd:cd16157 285 TFEGGMREPAIAWWPgHIKPGQVS-HQLGSLmDLFTTSLALAGLPIPSDraIDGIDLLPVLLNGKEKDRPI 354
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
43-401 |
1.07e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 77.77 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLtddqdVElgSMQ--VMNKT----------RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKY-VHNHNTYTN 109
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 110 NencsspswqAQHEGRTFAVYLNSTGYRTAFFgkylneYNGsyvppgwkewvgllkNSRFYNytlcRNGVKEKHGFD--Y 187
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 188 SKDYLTDLVTN-----DSVnFFRTSKKMYPhrpvlmvishaaphgpEDSAPQYSHLFpNASQHiTPsYNYaPNPDKHWIm 262
Cdd:COG1368 352 DREDFDDPFDGgwgvsDED-LFDKALEELE----------------KLKKPFFAFLI-TLSNH-GP-YTL-PEEDKKIP- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 263 rytgpmkpihmEFTNMLQRKRLQTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGyhigqfGLVKGKSmPYEFDI--- 339
Cdd:COG1368 410 -----------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLery 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387538414 340 RVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSD-MDGKSILKLLDTERPVNRFHL 401
Cdd:COG1368 472 RVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDLLSPDTDPFAFRNGGF 534
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
43-399 |
2.42e-14 |
|
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: 76.56 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDDqdveLGSMQVM---NKTRR-----IMEQGGAHFINAFVTTPMCCPSRSSILTGKY------VHNHNtYT 108
Cdd:cd16159 1 KPNIVLFMADD----LGIGDVGcfgNDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHG-MR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 109 NNENCSSPSWQAQHEgRTFAVYLNSTGYRTAFFGKY----------------LN-----------------------EYN 149
Cdd:cd16159 76 VILFTASSGGLPPNE-TTFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 150 GSYVPPGWKE--------------------------------------WVGLLKNSRFYNYTLCRNG-VKEKhgfDYSKD 190
Cdd:cd16159 155 LSFDPLFPLLtafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHeVVEQ---PMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 191 YLTDLVTNDSVNFFRTSKkmypHRPVLMVISHAAPHGPEDSAPqyshLFPNASQHitpsYNYAPNpdkhwimrytgpmkp 270
Cdd:cd16159 232 NLTQRLTKEAISFLERNK----ERPFLLVMSFLHVHTALFTSK----KFKGRSKH----GRYGDN--------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 271 ihmeftnmlqrkrlqtLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHI-----------GQFGLVKGKSMP-YEFD 338
Cdd:cd16159 285 ----------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEGG 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387538414 339 IRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLLD--TERPVNRF 399
Cdd:cd16159 349 IRVPTIVRWPGViPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTgqEKRSPHEF 414
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
44-398 |
7.26e-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: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDDQDV-ELG-----SMQVMNKTRriMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpS 117
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 WQAQHEGRTFAVYLNSTGYRTAFFGKY---LNEyNGSYVPPgwkewvgllknsrfynytlcRNGVKEKHGFDYSKDY--- 191
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT--------------------HQGFDHYLGIPYSHDQgpc 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 192 --LTDLVTNDSVnfFRTSKKMYPHRPVLM--VISHAAPHGPeDSAPQY----SHLFPNASQHITPSYNYAPNPDKHWiMR 263
Cdd:cd16158 138 qnLTCFPPNIPC--FGGCDQGEVPCPLFYneSIVQQPVDLL-TLEERYakfaKDFIADNAKEGKPFFLYYASHHTHY-PQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 264 YTGpmkpihMEFTNMLQRKRL-QTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHI------GQFGLVK-GKSMPY 335
Cdd:cd16158 214 FAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTY 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387538414 336 EFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPS-DMDGKSILKLLDTERPVNR 398
Cdd:cd16158 288 EGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPR 351
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
43-390 |
2.04e-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: 72.89 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 43 RPNIILVLTDD---QDVELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYvHNHNTYTNNENCSSPS 117
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRL-GLRNGVGHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 WQAQHEgRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPpgwkewvgllkNSRFYNYTLcrngvkekhGFDYSKD-YLTDLV 196
Cdd:cd16161 80 GLPLNE-TTLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---------GIPFSHDsSLADRY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 197 TNDSVNFF-RTSKKmypHRPVLMVISHAAPHGPEDSAPqyshLFPNASQHITPsynyapnpdkhwimryTGpmkpihmef 275
Cdd:cd16161 139 AQFATDFIqRASAK---DRPFFLYAALAHVHVPLANLP----RFQSPTSGRGP----------------YG--------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 276 tnmlqrkrlQTLMSVDDSMETLYNMLVETGELDNTYLVYTAD---------------HGYHIGQFGLVKGKSMPYEFDIR 340
Cdd:cd16161 187 ---------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHR 257
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1387538414 341 VPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPSD--MDGKSILKLL 390
Cdd:cd16161 258 EPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
44-374 |
4.55e-13 |
|
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: 70.40 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVL-----TDDQDVELGSMQVMNKTRRIMEQGgAHFINAFVTTPMCCPSRS--SILTGkyvhnhnTYTNNENCSSP 116
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 117 SWQAQHEGRTFAVYLNSTGYRTAFFgkylneYNGsyvppgwkewvgllkNSRFYNytlcRNGVKEKHGFD--YSKDYLTD 194
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 195 LVTNDSVN------FFRTSKKMY---PHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpsYNYAPNPDKhwimryt 265
Cdd:cd16015 128 DEKETNGWgvsdesLFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 266 gpmKPIHMEFTNMLQRKRLQTLMSVDDSMETLYNMLVETGELDNTYLVYTADHGYHIGQFGLVKGKSMPYEFdiRVPFYV 345
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 1387538414 346 RGPNVEAGSLNPHIVLNIDLAPTILDIAG 374
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
44-373 |
6.73e-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: 68.99 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 44 PNIILVLTDD---QDVELGSMQVMNKTR-RIMEQGGAHFiNAFVTTPMC--CPSRSSILTGKYVHNHNTYTNNENCSSPS 117
Cdd:cd00016 1 KHVVLIVLDGlgaDDLGKAGNPAPTTPNlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 118 WQAQHE---GRTFAVYLNSTGYRTAffgkylneyngsyvppgwkeWVGLLknsrfynytlcrngvkekhgfdyskDYLtd 194
Cdd:cd00016 80 SRAAGKdedGPTIPELLKQAGYRTG--------------------VIGLL-------------------------KAI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 195 lvtndsvnffrtsKKMYPHRPVLMVISHAAPHGPedsapqyshlfpnasqhitpSYNYAPNPDkhwimrytgpmkpihmE 274
Cdd:cd00016 113 -------------DETSKEKPFVLFLHFDGPDGP--------------------GHAYGPNTP----------------E 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 275 FTNMLQRkrlqtlmsVDDSMETLYNMLVETGELDNTYLVYTADHG---YHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVE 351
Cdd:cd00016 144 YYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVK 215
|
330 340
....*....|....*....|..
gi 1387538414 352 AGSLNPHIVLNIDLAPTILDIA 373
Cdd:cd00016 216 KGGVKHELISQYDIAPTLADLL 237
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
341-387 |
1.93e-06 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 51.26 E-value: 1.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1387538414 341 VPFYVRGPNV-----EAGSLnphivlnIDLAPTILDIAGLDIPSDMDGKSIL 387
Cdd:cd16010 459 VPFIIVDPGLkrkllKDGGL-------ADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
68-374 |
3.09e-06 |
|
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: 49.51 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 68 RRIMEQGgAHF---INAFVT-TpmcCPSRSSILTGKYVHNH----NTY---TNNENCSSPSWQAQH---EGRTFAVYLNS 133
Cdd:cd16018 26 KRLAEEG-VRAkyvKPVFPTlT---FPNHYSIVTGLYPESHgivgNYFydpKTNEEFSDSDWVWDPwwiGGEPIWVTAEK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 134 TGYRTA-FFgkylneyngsyvppgwkeWVGLLKNSRFYNYTLCRNgvkekhgFDYSKDYLTDLVTNDSVNFFRTSKKMYp 212
Cdd:cd16018 102 AGLKTAsYF------------------WPGSEVAIIGYNPTPIPL-------GGYWQPYNDSFPFEERVDTILEWLDLE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 213 hRPVLMVISHAAPhgpeDSApqyshlfpnasQHitpsyNYAPNpdkhwimrytgpmkpiHMEFTNMLQRkrlqtlmsVDD 292
Cdd:cd16018 156 -RPDLILLYFEEP----DSA-----------GH-----KYGPD----------------SPEVNEALKR--------VDR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 293 SMETLYNMLVETGELDNTYLVYTADHGY-----HiGQFglvkgksmPYEFDIRVPFYVRGP----NVEAGSLNphivlNI 363
Cdd:cd16018 191 RLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPafkkGKKLGPFR-----NV 256
|
330
....*....|.
gi 1387538414 364 DLAPTILDIAG 374
Cdd:cd16018 257 DIYPLMCNLLG 267
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
341-388 |
4.87e-06 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 50.10 E-value: 4.87e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1387538414 341 VPF-YVRGPNV--EAGSLNphivlniDLAPTILDIAGLDIPSDMDGKSILK 388
Cdd:PRK05434 464 VPFiLVGGKALrlEGGKLA-------DIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
343-392 |
8.56e-06 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 49.13 E-value: 8.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1387538414 343 FYVRGPNVEAGSLNPHIVLnIDLAPTILDIAGLDIPSDMDGKSILKLLDT 392
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFAR 470
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
341-388 |
8.70e-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: 8.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1387538414 341 VPFYVRGPNvEAGSLNPHIVLnIDLAPTILDIAGLDIPSDMDGKSILK 388
Cdd:COG0696 465 VPFILVGGD-KGVKLREDGRL-ADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
230-370 |
4.88e-05 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 46.82 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 230 DSAPQYSHLFPNASQhitPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETLYNMLVETGELDN 309
Cdd:COG3083 379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387538414 310 TYLVYTADHGY-----------HIGQFGlvkgksmPYEfdIRVPFYVRGPNVEAGSLNpHIVLNIDLAPTIL 370
Cdd:COG3083 456 TIVIITADHGEefnengqnywgHNSNFS-------RYQ--LQVPLVIHWPGTPPQVIS-KLTSHLDIVPTLM 517
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
291-386 |
4.86e-03 |
|
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: 39.86 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538414 291 DDSMETLYNMLVETGELDNTYLVYTADHGY-----HigqfglvkGKSMPYEfdIRVPFYVRGPNVEAGSLNPH------- 358
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHGMtdagnH--------GGSSPGE--TSVPLLFISPKFSSKPSNADgelsyye 246
|
90 100
....*....|....*....|....*...
gi 1387538414 359 IVLNIDLAPTILDIAGLDIPSDMDGKSI 386
Cdd:cd16024 247 TVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| |
