|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
42-384 |
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: 544.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 196 TNESINYFKMSKRMypHRPIMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 275 TNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEPGSI 354
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 1907068827 355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
42-414 |
8.17e-87 |
|
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: 287.50 E-value: 8.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQ--DVeLGSLQ-VMNKT---RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcSSP 115
Cdd:cd16031 2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 116 SWQamhepRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHgfdyaKDYFTDLI 195
Cdd:cd16031 79 ASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTDII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 196 TNESINYFKmsKRMyPHRPIMMVISHAAPHGPEDSAPQFSKLYPNAsqHITPSYNYAPN-------------MDKHWIMQ 262
Cdd:cd16031 149 TDKALDFLK--ERD-KDKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEPETFDDDdyagrpewareqrNRIRGVLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 263 YtgpmlPIHMEFTnvLQR--KR-LQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIR 339
Cdd:cd16031 224 G-----RFDTPEK--YQRymKDyLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIR 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068827 340 VPFFIRGP-SIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDlekpgnrfrtNKKAKIWRDTFLVE 414
Cdd:cd16031 296 VPLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
42-414 |
3.73e-74 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 251.34 E-value: 3.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQDVelGSLQVMNKTR-------KIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsS 114
Cdd:COG3119 23 RPNILFILADDLGY--GDLGCYGNPLiktpnidRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--Y 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 115 PSWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDL 194
Cdd:COG3119 98 NGGLPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 195 ITNESINYfkMSKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmef 274
Cdd:COG3119 133 LTDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR----------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 275 tnvLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SIEPGS 353
Cdd:COG3119 198 ---ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGS 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068827 354 IVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLdlekpgnrfrTNKKAKiWRDTFLVE 414
Cdd:COG3119 275 VSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE-WRDYLYWE 324
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
534-678 |
6.65e-68 |
|
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: 224.15 E-value: 6.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEeLQVLPPRSIAKRH--DEGHQGFIGHQAAAGDirneMLADSNNAVGLPATV 611
Cdd:pfam12548 1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEE-YQPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPASV 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068827 612 RVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEVLQDKIKNLREVRGHLKKRKPEECGCGD 678
Cdd:pfam12548 76 KVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
43-384 |
3.33e-53 |
|
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: 186.10 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQ---DVE-LGSLQVmnKT---RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcssp 115
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 116 SWQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHgfdyakdyftdli 195
Cdd:cd16022 74 GGGLPPDEPTLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 196 tNESINYFKmskRMYPHRPIMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDkhwimqytgpmlpihmeft 275
Cdd:cd16022 103 -DEAIDFIE---RRDKDKPFFLYVSFNAPHPP---------------------FAYYAMVS------------------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 276 nvlqrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SIEPGSI 354
Cdd:cd16022 139 ------------AIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIPAGQV 206
|
330 340 350
....*....|....*....|....*....|
gi 1907068827 355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-389 |
1.28e-52 |
|
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: 190.09 E-value: 1.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDD---QDveLGSLQVMN-KTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTnneNCSSP 115
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG---NDVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 116 SwqamHEPRTFAVYLNNTGYRTAFFGKY-LNE-------YNGSYIPP----GWREWLGLIKNSRFYNYTVCRNGIKEKHG 183
Cdd:cd16034 76 P----PDAPTIADVLKDAGYRTGYIGKWhLDGperndgrADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 184 FDYAKDYFTDLItnesINYfkMSKRMYPHRPIMMVISHAAPHGPEDSAPQ-FSKLYPNASQHITPsyNYAPNMD-----K 257
Cdd:cd16034 152 KGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLLRP--NVPEDKKeeaglR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 258 HWIMQYtgpmlpihmeFTNVLqrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFD 337
Cdd:cd16034 224 EDLRGY----------YAMIT---------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPYEES 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907068827 338 IRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16034 284 IRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLL 336
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
43-397 |
1.91e-49 |
|
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: 180.01 E-value: 1.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDVELGSlqVMN---KTRKIME--QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTN-NENCSSPS 116
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 117 WQamhepRTFAVYLNNTGYRTAFFGKYlnEYNGSYIPPGWrewlgliknsrFYNYTVCRNGIKEKHGFDYAKDYFTDLIT 196
Cdd:cd16027 79 GV-----KTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 197 NE----SINYFkmskrmYPHRPIMMVISHAAPHGPEDsapqfsklypnasqhITPSYNYA--PNMDKHWIMQYTgpmlpi 270
Cdd:cd16027 141 GQpfflWFGFH------DPHRPYPPGDGEEPGYDPEK---------------VKVPPYLPdtPEVREDLADYYD------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 271 hmeftnvlqrkrlqTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYhigqfGLVKGKSMPYDFDIRVPFFIRGPS-I 349
Cdd:cd16027 194 --------------EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkI 254
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907068827 350 EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16027 255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
43-374 |
1.74e-48 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 174.92 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQ-DVELGSLQ-VMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQ 118
Cdd:pfam00884 1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 119 AMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLIT 196
Cdd:pfam00884 75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 197 NESINYfkmskRMYPHRPIMMVISHAAPHGPedsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:pfam00884 149 DEALEF-----LDNNDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL-------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 277 vlqRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGP-SIEPG 352
Cdd:pfam00884 200 ---NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPgGKAKG 276
|
330 340
....*....|....*....|..
gi 1907068827 353 SIVPQIVLNIDLAPTILDIAGL 374
Cdd:pfam00884 277 QKSEALVSHVDLFPTILDLAGI 298
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-389 |
6.23e-47 |
|
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: 174.27 E-value: 6.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDD---QDVelgSLQvMNKtrkIME--------QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYT---- 107
Cdd:cd16144 1 PNIVLILVDDlgwADL---GCY-GSK---FYEtpnidrlaKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 108 ------NNENCSSPSWQAM-HEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYipP---GWREWLGLIKNSRFYNYTVCRN 176
Cdd:cd16144 74 rrgppdNTKLIPPPSTTRLpLEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 177 GIKEKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDSAPQFSKLYpnasqhitpsYNYAPNMD 256
Cdd:cd16144 152 KPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKY----------EKKKKGLR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 257 KHWIMQYTGPMLpihmeftnvlqrkrlqtlMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV-------KG 329
Cdd:cd16144 218 KGQKNPVYAAMI------------------ESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGG 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907068827 330 KSMPYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLD--SPSDVDGKSVLKLL 389
Cdd:cd16144 280 KGSLYEGGIRVPLIVRWPGvIKPGSVSDVPVIGTDLYPTFLELAGGPlpPPQHLDGVSLVPLL 342
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-414 |
1.90e-46 |
|
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: 172.41 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDV----ELGSLQVmnKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16033 1 PNILFIMTDQQRYdtlgCYGNPIV--KTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 117 WQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgWRewlgliknsrfynytVCRNGIKEKHGFDY------AKDY 190
Cdd:cd16033 79 RGLPPGVETFSEDLREAGYRNGYVGK-------------WH---------------VGPEETPLDYGFDEylpvetTIEY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 191 FTDLITNESINYFKMSKRmyphrPIMMVISHAAPHGPEDSAPQFSKLYPNASqhITPSYNYAPNM-DKHWImQYTGPMLP 269
Cdd:cd16033 131 FLADRAIEMLEELAADDK-----PFFLRVNFWGPHDPYIPPEPYLDMYDPED--IPLPESFADDFeDKPYI-YRRERKRW 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 270 IHMEFTNVLQRKRLQ------TLMsvDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV-KGKSMpYDFDIRVPF 342
Cdd:cd16033 203 GVDTEDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPL 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907068827 343 FIRGP-SIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNrfrtnkkakiWRDTFLVE 414
Cdd:cd16033 280 IIKWPgVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
43-400 |
1.22e-40 |
|
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: 155.40 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDVelGSLQVMN----KT---RKIMEQGgATFTNaFVTTPMCCPSRSSMLTGKYVHNHNVYTnnencSSP 115
Cdd:cd16146 1 PNVILILTDDQGY--GDLGFHGnpilKTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWH-----TIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 116 SWQAMH-EPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL-----------IKNSRFYNyTVCRNGIKEK 181
Cdd:cd16146 72 GRERMRlDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdyWGNDYFDD-TYYHNGKFVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 182 HgfdyaKDYFTDLITNESINYFKMSKrmypHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYApnmdkhwim 261
Cdd:cd16146 151 T-----EGYCTDVFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG--------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 262 qytgpMLpihmefTNvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHGYHIG-----QFGLVKGKSMPYDF 336
Cdd:cd16146 213 -----MI------EN------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEG 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068827 337 DIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV--DGKSVLKLLDLEKPGNRFRT 400
Cdd:cd16146 270 GHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIklDGRSLLPLLKGESDPWPERT 336
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-398 |
3.40e-40 |
|
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: 151.54 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 74 GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpswqamhEPRTFAVYLNNTGYRTAFFGK--YLNEyngsy 151
Cdd:cd16037 36 GTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRGE----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 152 ippgwrewlgliknsrfynytvcrngiKEKHGFDYakdyfTDLITNESINYFKmsKRMYPHRPIMMVISHAAPHGPEDSA 231
Cdd:cd16037 104 ---------------------------DQRHGFRY-----DRDVTEAAVDWLR--EEAADDKPWFLFVGFVAPHFPLIAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 232 PQFSKLYpnasqhitpsynyapnmdkhwimqytgpmlpihmeftnvlqRKRLQT----LMS-VDDSVERLYNMLVESGEL 306
Cdd:cd16037 150 QEFYDLY-----------------------------------------VRRARAayygLVEfLDENIGRVLDALEELGLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 307 DNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVL 386
Cdd:cd16037 189 DNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLL 267
|
330
....*....|..
gi 1907068827 387 KLLDLEKPGNRF 398
Cdd:cd16037 268 PLAEGPDDPDRV 279
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-389 |
6.09e-39 |
|
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: 150.44 E-value: 6.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDV-ELGSL-QVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQ 118
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 119 AmhEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPP--GWREWLG--------------LIKNSR--FYNYTVCRNGIK 179
Cdd:cd16145 81 P--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGyldqvhahnyypeyLWRNGEkvPLPNNVIPPLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 180 EKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDsAPQFSklyPNASQHITPSYNYAPNMDKhw 259
Cdd:cd16145 159 GNNAGGGGGTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAPLQ-VPDDG---PYKYKPKDPGIYAYLPWPQ-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 260 imqytgpmlpihmeftnvlQRKRLQTLMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHI-------GQF-----GL 326
Cdd:cd16145 229 -------------------PEKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngPL 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907068827 327 VKGK-SMpYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16145 290 RGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-397 |
8.05e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 148.87 E-value: 8.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQDVE----LGSLQVmnKTRKI--MEQGGATFTNAFVTTPM----CCPSRSSMLTGKYVHNhnvYTNNEN 111
Cdd:cd16155 2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 112 CSSPSwqamhEPRTFAVYLNNTGYRTAFFGKYLNEYngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdyf 191
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 192 tdliTNESINYFKmsKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPnaSQHITPSYNYAPnmdKHwimQYTGPMLPIH 271
Cdd:cd16155 108 ----ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLP---QH---PFDNGEGTVR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 272 MEFT--------NVlqRKRLQ----TLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIR 339
Cdd:cd16155 174 DEQLapfprtpeAV--RQHLAeyyaMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-GKQNLYEHSMR 250
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907068827 340 VPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16155 251 VPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVR 308
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-397 |
8.48e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 146.22 E-value: 8.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQ--DVeLGSL-QVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPS 116
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 117 wqamhEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHGFDYAKDYFTDLit 196
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 197 neSINYfkMSKRMyPHRPIMMVISHAAPH---------GPEDSAPQFSKLYP---------NASQHItPSYnyapnmdkh 258
Cdd:cd16152 113 --AIDY--LDNRQ-KDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWVppdlaalpgDWAEEL-PDY--------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 259 wimqytgpmlpihmeftnvlqrkrLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHigqFGLVKG--KSMPYDF 336
Cdd:cd16152 178 ------------------------LGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068827 337 DIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWR 291
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
42-390 |
6.65e-35 |
|
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: 139.24 E-value: 6.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQDVELGSLQvmnktRKIME--------QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNencs 113
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYG-----GHPAKtpnidrlaARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 114 SPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYI--PPGWREWLGLIKNSRFYNYTVCRNGIKEKHG-------- 183
Cdd:cd16030 73 SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDddPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpawea 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 184 FDYAKDYFTD-LITNESINYFKMSKRMypHRPIMMVISHAAPHGPEdSAPQ-FSKLYPNASQHITPSYN------YAPNm 255
Cdd:cd16030 153 ADVPDEAYPDgKVADEAIEQLRKLKDS--DKPFFLAVGFYKPHLPF-VAPKkYFDLYPLESIPLPNPFDpidlpeVAWN- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 256 DKHWIMQYTGPMLPIHMEFTNVL----QRKRLQT-LMSV---DDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV 327
Cdd:cd16030 229 DLDDLPKYGDIPALNPGDPKGPLpdeqARELRQAyYASVsyvDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHW 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907068827 328 kGKSMPYDFDIRVPFFIRGPSI-EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLD 390
Cdd:cd16030 309 -GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLK 371
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
42-389 |
6.34e-34 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 135.38 E-value: 6.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQ---DVE-LGSlqVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKY-----VHNHNVYTNNE 110
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGS--PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 111 NCSSPSwqamhEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL----------IKNSRFYNYTVCRNGI 178
Cdd:cd16026 79 GGLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIpysndmwpfpLYRNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 179 KEKHGFDYAKDYFTDLITNESINYFKMSKrmypHRPIMMVISHAAPHGPEDSAPQFSklypNASQHitpsynyapnmdkh 258
Cdd:cd16026 153 EEVIEQPADQSSLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVPLFASEKFK----GRSGA-------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 259 wimqytGPmlpihmeFTNVLQrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHG--YHIGQFG-----LVKGKS 331
Cdd:cd16026 211 ------GL-------YGDVVE--------ELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGGKG 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068827 332 MPYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV--DGKSVLKLL 389
Cdd:cd16026 270 TTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDRviDGKDISPLL 330
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
72-390 |
7.93e-34 |
|
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: 133.09 E-value: 7.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 72 QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPSWQamhePrTFAVYLNNTGYRTAFFGKYlneyngsy 151
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPADI----P-TFAHYLRAAGYRTALSGKM-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 152 ippgwrewlgliknsRFYnytvcrnGIKEKHGFDY-------AKDYFTDLitnesinyfkmsKRMYPHRPIMMVISHAAP 224
Cdd:cd16032 99 ---------------HFV-------GPDQLHGFDYdeevafkAVQKLYDL------------ARGEDGRPFFLTVSFTHP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 225 HGPEDSAPQFSKLYPNASQHitpSYnYApnmdkhwIMQYtgpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESG 304
Cdd:cd16032 145 HDPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 305 ELDNTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV---D 381
Cdd:cd16032 189 LADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVpplD 267
|
....*....
gi 1907068827 382 GKSVLKLLD 390
Cdd:cd16032 268 GRSLLPLLE 276
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-387 |
8.18e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 131.52 E-value: 8.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTD----DQdvelgsLQVMNKTRKIM------EQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVytnnenc 112
Cdd:cd16148 1 MNVILIVIDslraDH------LGCYGYDRVTTpnldrlAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 113 sspsWQAMHEPR--TFAVYLNNTGYRTAFFGkylneyNGSYIPPGWREWLGliknsrfYNYTVCRNGIKEKHGFDyaKDY 190
Cdd:cd16148 68 ----WGGPLEPDdpTLAEILRKAGYYTAAVS------SNPHLFGGPGFDRG-------FDTFEDFRGQEGDPGEE--GDE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 191 FTDLITNESINYFKmskRMYPHRPIMMVISHAAPHGPEdsapqfskLYPNAsqhitpsynyapnmdkhwimqytgpmlpI 270
Cdd:cd16148 129 RAERVTDRALEWLD---RNADDDPFFLFLHYFDPHEPY--------LYDAE----------------------------V 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 271 HMeftnvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMP-YDFDIRVPFFIRGPSI 349
Cdd:cd16148 170 RY----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGK 233
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907068827 350 EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLK 387
Cdd:cd16148 234 EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
74-411 |
1.06e-33 |
|
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: 135.85 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 74 GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNnencSSPswQAMHEPrTFAVYLNNTGYRTAFFGK----------- 142
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARHL-TLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 143 YLNEYNGSY--IPPGWREwlgliknsrfynytVCR-NGIKEKHGfDYAkdYFTDlitnESINYFkmskRMYPHRPIMMVI 219
Cdd:cd16028 109 PLDPRLLSYelAMPGFDP--------------VDRlDEYPAEDS-DTA--FLTD----RAIEYL----DERQDEPWFLHL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 220 SHAAPHGP-EDSAPqFSKLYPNASqhiTPSYNYAPNMD---------KHWIMQYtgPMLPIHMEFTNV-----LQRKRLQ 284
Cdd:cd16028 164 SYIRPHPPfVAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 285 T----LMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSIE----PGSIV 355
Cdd:cd16028 238 AtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREadatRGQVV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068827 356 PQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNrfrtNKKAKIWRDTF 411
Cdd:cd16028 317 DAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSD----WRDAVHYEYDF 368
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-423 |
1.33e-33 |
|
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: 134.25 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDqdVELGSLQVMNKTRKI-------MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 116 SWqaMHEPR-TFAVYLNNTGYRTAFFGKY---LNEY--NGSYIPPGWRE---WLGLIKNSRFYnytvcrngikekHGFDY 186
Cdd:cd16143 79 PL--IEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKdvdYSKPIKGGPLD------------HGFDY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 187 akdYFT-------DLITNESINYFKMSKRmyPHRPIMMVISHAAPHGPedsapqfsklypnasqhITPS--YNYAPNMDK 257
Cdd:cd16143 145 ---YFGipasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 258 H--WIMQytgpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFGLVKGKSM 332
Cdd:cd16143 203 YgdFVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGHDP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 333 PYDF-----DI-----RVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLLdlekpgnrfr 399
Cdd:cd16143 257 SGPLrgmkaDIyegghRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL---------- 326
|
410 420
....*....|....*....|....*..
gi 1907068827 400 TNKKAKIWRDTFLVE--RGKF-LRKKE 423
Cdd:cd16143 327 LGPKKQEVRESLVHHsgNGSFaIRKGD 353
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-386 |
6.02e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 122.73 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDV----ELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNV-----YTNNENCS 113
Cdd:cd16149 1 PNILFILTDDQGPwalgCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 114 SP-SWQAMHEprTFAVYLNNTGYRTAFFGKylneyngsyippgwreW-LGliknsrfynytvcrngikekhgfDYAKDYF 191
Cdd:cd16149 81 KPeGYLEGQT--TLPEVLQDAGYRCGLSGK----------------WhLG-----------------------DDAADFL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 192 TDLITNEsinyfkmskrmyphRPIMMVISHAAPHGPedsapqfsklypnasqhitpsynyapnmdkhWimQYtgpmlpih 271
Cdd:cd16149 120 RRRAEAE--------------KPFFLSVNYTAPHSP-------------------------------W--GY-------- 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 272 meftnvlqrkrLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGlVKGK-------SMpYDFDIRVPFFI 344
Cdd:cd16149 145 -----------FAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVPFII 211
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907068827 345 RGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVD--GKSVL 386
Cdd:cd16149 212 RWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-378 |
1.04e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 123.47 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQ----DVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtnnENCSSPS-W 117
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 118 QAMHEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYippgwrewlgliknsrfynytvcrngikekhgfdYAKDyftDLIT 196
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 197 NESINY-FKMSKRMYPHRPIMMVISHAAPHgpeDsapqfsklypnasqhItpsyNYAPNMDKHWImqytgpmlpihmeft 275
Cdd:cd16035 121 AQAVEWlRERGAKNADGKPWFLVVSLVNPH---D---------------I----MFPPDDEERWR--------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 276 nVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEP-GSI 354
Cdd:cd16035 164 -RFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGtGQT 242
|
330 340
....*....|....*....|....
gi 1907068827 355 VPQIVLNIDLAPTILDIAGLDSPS 378
Cdd:cd16035 243 TDALTSHIDLLPTLLGLAGVDAEA 266
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
42-388 |
1.29e-30 |
|
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: 125.63 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDqdveLG-----------------SLQvmnktrkimeQGGATFTNaFVTTPMCCPSRSSMLTGKYVHNHN 104
Cdd:cd16025 2 RPNILLILADD----LGfsdlgcfggeiptpnldALA----------AEGLRFTN-FHTTALCSPTRAALLTGRNHHQVG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 105 VYTNNENCSS-PSWQAMHEPR--TFAVYLNNTGYRTAFFGKYlneYNGsyiPPGWrewlgliknsrfynytvcrngikek 181
Cdd:cd16025 67 MGTMAELATGkPGYEGYLPDSaaTIAEVLKDAGYHTYMSGKW---HLG---PDDY------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 182 hgfdyakdYFTDLITNESINYFKMSKRmyPHRPIMMVISHAAPHGPedsapqfsklypnasQHitpsynyAPnmdKHWIM 261
Cdd:cd16025 116 --------YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP---------------LQ-------AP---KEWID 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 262 QYTG---------------------------PMLPIHMEFT--NVL---QRKRLQTLMSV--------DDSVERLYNMLV 301
Cdd:cd16025 161 KYKGkydagwdalreerlerqkelglipadtKLTPRPPGVPawDSLspeEKKLEARRMEVyaamvehmDQQIGRLIDYLK 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 302 ESGELDNTYIIYTADHG--YHIG--QFG---LVKGKSMPYDFDIRVPFFIRGPS--IEPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd16025 241 ELGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKgiKAKGGIRHQFAHVIDIAPTILELA 320
|
410
....*....|....*.
gi 1907068827 373 GLDSPSDVDGKSVLKL 388
Cdd:cd16025 321 GVEYPKTVNGVPQLPL 336
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
43-418 |
6.41e-30 |
|
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: 124.80 E-value: 6.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQD---VELGSLQVMnKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSw 117
Cdd:cd16156 1 KQFIFIMTDTQRwdmVGCYGNKAM-KTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 118 qamhepRTFAVYLNNTGYRTAFFGKY-LN--EYNGSYI-PPGWRE--WLGL-----------IKNSRFYNYTVCRNGIKE 180
Cdd:cd16156 79 ------KTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMrnyldelteeeRRKSRRGLTSLEAEGIKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 181 KhgFDYAKDyftdlITNESINYFkmskRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYN----YAPNMD 256
Cdd:cd16156 153 E--FTYGHR-----CTNRALDFI----EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAYddleNKPLHQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 257 KHWIMQYTGP----MLPIHMEFtnvlqrkrLQTLMSVDDSVERLYNMLVEsgELDNTYIIYTADHGYHIGQFGL-VKGKS 331
Cdd:cd16156 222 RLWAGAKPHEdgdkGTIKHPLY--------FGCNSFVDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLwAKGPA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 332 MpYDFDIRVPFFIRGPSIEPGSIVPQI-VLNIDLAPTILDIAGLDSPSDVDGKSVLKLLdlekpgnrfrTNKKAKIwRDT 410
Cdd:cd16156 292 V-YDEITNIPLIIRGKGGEKAGTVTDTpVSHIDLAPTILDYAGIPQPKVLEGESILATI----------EDPEIPE-NRG 359
|
....*...
gi 1907068827 411 FLVERGKF 418
Cdd:cd16156 360 VFVEFGRY 367
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-389 |
1.85e-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: 118.86 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDVE-LGSL-QVMNKTRKI--MEQGGATFTNAFvTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPswq 118
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 119 amheprTFAVYLNNTGYRTAFFGK---YLNEYNGSYIPP-GWREWL-------GLIKNSRFYNYTVCRNGIKEKhgfDYA 187
Cdd:cd16151 77 ------TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 188 KDYFTDLITNESINYFKMSKR-----MYPhrpimMVIshaaPHGPEDSAPQFSKLYPnasqhitPSYNYAPNMDKHWIM- 261
Cdd:cd16151 148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDPFVPTPDSPDWDP-------DDKRKKDDPEYFPDMv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 262 QYTgpmlpihmeftnvlqrkrlqtlmsvDDSVERLYNMLVESGELDNTYIIYTADHGYHIG-----QFGLVKG-KSMPYD 335
Cdd:cd16151 212 AYM-------------------------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068827 336 FDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16151 267 AGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL 323
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
42-397 |
2.95e-28 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 120.16 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQDVE-LGSL---QVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsW 117
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 118 QAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY------ 190
Cdd:PRK13759 83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 191 --------FTDL-----------------------ITNESINYFKmskRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYP 239
Cdd:PRK13759 150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 240 NASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEftnVLQRKRLQTLMS---VDDSVERLYNMLVESGELDNTYIIYTA 315
Cdd:PRK13759 227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEE---YARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 316 DHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDL 391
Cdd:PRK13759 304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382
|
....*.
gi 1907068827 392 EKPGNR 397
Cdd:PRK13759 383 QYEGWR 388
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
43-385 |
1.91e-27 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 116.11 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQ---DVEL-GSLQVmnKTRKIME--QGGATFTNAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 117 WQAMHEPrTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPPGwR-------EWLGLI-----KNSRFYNYTVCRNGIKEKHG 183
Cdd:cd16029 78 GLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTN-RgfdsfygYYGGAEdyythTSGGANDYGNDDLRDNEEPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 184 FDYAKDYFTDLITNESINYFKMSKrmyPHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPsynyapnmdkhwimqy 263
Cdd:cd16029 156 WDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD---------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 264 tgpmlpihmeftnvLQRKRLQTLMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFG------LVKGKSMPYDF 336
Cdd:cd16029 217 --------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNTLWEG 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907068827 337 DIRVPFFIRGPSIEP--GSIVPQIVLNIDLAPTILDIAGLDSPS--DVDGKSV 385
Cdd:cd16029 283 GVRVPAFVWSPLLPPkrGTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQ 335
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-387 |
3.29e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 100.91 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQDVElgSLQVMNKTRKIMEQG----------------GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNV 105
Cdd:cd16153 1 KPNILWIITDDQRVD--SLSCYNNAHTGKSESrlgyvespnidalaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 106 YtNNENcsspSWQAMHE-PRTFAVYLNNTGYRTAFFGKylneyngsyipPGWREWLGLIKNSrfyNYTVCRNGIKEKHGF 184
Cdd:cd16153 79 Y-GFEA----AHPALDHgLPTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 185 DYAKdyftdlitnesinyfkmskrmyphrPIMMVISHAAPHGPedsapqfsklypnasqhITPSYNYAPNMDKHWIMQYt 264
Cdd:cd16153 140 DSDK-------------------------PFFVRLSFLQPHTP-----------------VLPPKEFRDRFDYYAFCAY- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 265 gpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESGEL---DNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVP 341
Cdd:cd16153 177 ------------------------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVP 231
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907068827 342 FFIRGPSIEP---GSIVPQIVLNIDLAPTILDIAGLD--SPSDVDGKSVLK 387
Cdd:cd16153 232 LIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRDLFE 282
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-390 |
7.08e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 102.70 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 74 GATFTNAFVTTPMCCPSRSSMLTGKY--VHNHNVYTNnencsspsWQAMHEPrTFAVYLNNTGYRTAFFGKylneyNGSY 151
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHH--------LLRPDEP-NLLKTLKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 152 IPPGWREwlgliknsrfyNYTVCrngikekhgfDYAkdyftdlITNESINYFKmskRMYPHRPIMMVISHAAPHGP-EDS 230
Cdd:cd16150 102 PGEFAAE-----------AYCDS----------DEA-------CVRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 231 APQFSKLYPNASQHITPSynyapnmdKHWIMQYtgPMLPIHMEFTNvLQR---KRLQTL--------MSVDDSVERLYNM 299
Cdd:cd16150 151 EPWFSMIDREKLPPRRPP--------GLRAKGK--PSMLEGIEKQG-LDRwseERWRELratylgmvSRLDHQFGRLLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 300 LVESGELDNTYIIYTADHGYHIGQFGLV-KGKSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPS 378
Cdd:cd16150 220 LKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSH 299
|
330
....*....|..
gi 1907068827 379 DVDGKSVLKLLD 390
Cdd:cd16150 300 THFGRSLLPVLA 311
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-389 |
2.58e-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: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDVE------LGSLQVMNKTRKIMEQGGATFTNAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 117 wqamHE-PRTFAVYLNNTGYRTAFFGKYL--NEYNGSYIPPGWREWLGLIKN--SRFYNYTVCRNGIKEKHGfDYAKDYF 191
Cdd:cd16154 80 ----ETlLQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST-EYATTKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 192 TDL----ITNEsinyfkmskrmypHRPIMMVISHAAPHGPedsapqFsklypnasqHITPSYNYAPNMdkhwimqyTGPM 267
Cdd:cd16154 155 TNLaidwIDQQ-------------TKPWFLWLAYNAPHTP------F---------HLPPAELHSRSL--------LGDS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 268 LPIHMEftnvlqrKR---LQTLMSVDDSVERLYNMLVESgELDNTYIIYTADHGYHiGQ-----FGLVKGKSMPYDFDIR 339
Cdd:cd16154 199 ADIEAN-------PRpyyLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGIN 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907068827 340 VPFFIRGPSIEPGSIVPQIVLNI-DLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16154 270 VPLIVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLL 320
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
42-389 |
1.69e-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: 99.04 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDqdVELGSLQVM-NKTRKI-----MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtnNENCSSP 115
Cdd:cd16160 1 KPNIVLFFADD--MGYGDLASYgHPTQERgpiddMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 116 SWQAMHEPR---TFAVYLNNTGYRTAFFGKY---LNEYN---GSYIPpgwrewlgliknsrfynytvcrngikEKHGFDY 186
Cdd:cd16160 77 PWDIGGLPKtevTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLP--------------------------SHHGFDF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 187 A---------------------KD------YFTDLITNESINYFKMSKRMYP----------HRPIMMVISHAAPHGPED 229
Cdd:cd16160 131 VgtnlpftnswacddtgrhvdfPDrsacflYYNDTIVEQPIQHEHLTETLVGdaksfiednqENPFFLYFSFPQTHTPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 230 SAPQFSklypNASQHitpsYNYAPNMDKhwimqytgpmlpihmeftnvlqrkrlqtlMSVddSVERLYNMLVESGELDNT 309
Cdd:cd16160 211 ASKRFK----GKSKR----GRYGDNINE-----------------------------MSW--AVGEVLDTLVDTGLDQNT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 310 YIIYTADHGYHI------GQFGLVKG-KSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--V 380
Cdd:cd16160 252 LVFFLSDHGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriY 331
|
....*....
gi 1907068827 381 DGKSVLKLL 389
Cdd:cd16160 332 DGLSITDLL 340
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
42-422 |
2.99e-19 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 93.18 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLtddqdVElgSLQ--VMNKT----------RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKY-VHNHNVYTN 108
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 109 NencsspswqAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--Y 186
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 187 AKDYFTDLITN-----------ESINYFKMSKRmyphrPIMMVISHAAPHGPedsapqfsklypnasqhitpsynYAPNM 255
Cdd:COG1368 352 DREDFDDPFDGgwgvsdedlfdKALEELEKLKK-----PFFAFLITLSNHGP-----------------------YTLPE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 256 DKHWIMQYTGPMLpihmeftnvlqRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGyhigqfGLVKGKSmPYD 335
Cdd:COG1368 404 EDKKIPDYGKTTL-----------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 336 FDI---RVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVD-GKSvlkLLDLEKPGNRFR-----TNKKAKI 406
Cdd:COG1368 466 NPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRD---LLSPDTDPFAFRnggfiTDDYVYV 542
|
410
....*....|....*.
gi 1907068827 407 WRDTFLVERGKFLRKK 422
Cdd:COG1368 543 LKTGELTEEDKELEEE 558
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
43-373 |
7.12e-19 |
|
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: 88.12 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVL-----TDDQDVELGSLQVMNKTRKIMEQGgATFTNAFVTTPMCCPSRS--SMLTGkyvhnhnVYTNNENCSSP 115
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 116 SWQAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--YAKDYFTD 193
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 194 LITNESINY------FKMSKRMY---PHRPIMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDKhwimqyt 264
Cdd:cd16015 128 DEKETNGWGvsdeslFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 265 gpmLPIHMEFTNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFdiRVPFFI 344
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 1907068827 345 RGPSIEPGSIVPQIVLNIDLAPTILDIAG 373
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
767-816 |
1.40e-18 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 89.53 E-value: 1.40e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907068827 767 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 816
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
43-389 |
1.49e-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: 88.75 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDVELgSLQVMNKTRKI-----MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtNNENCSSPSW 117
Cdd:cd16171 1 PNVVMVMSDSFDGRL-TFRPGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 118 QamheprTFAVYLNNTGYRTAFFGKyLNEYNGSYIPPGWRE-WlgliknSRFYNYTVCRNGIKEkhgfdyakdyfTDLIT 196
Cdd:cd16171 79 P------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRPT-----------VNLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 197 NESinyfkmskrmypHRPIMMvishaaphgpedsapqfsKLYPNASQHITPSYNYAPNMDKHWIMqYTGPMLPiHMEFTN 276
Cdd:cd16171 135 DRS------------TVRVML------------------KDWQNTDKAVHWIRKEAPNLTQPFAL-YLGLNLP-HPYPSP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 277 VLQrkrlQTLMSVDDSVERLYNMLVE--------------SGELDNTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPF 342
Cdd:cd16171 183 SMG----ENFGSIRNIRAFYYAMCAEtdamlgeiisalkdTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPL 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907068827 343 FIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16171 258 LIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
42-389 |
9.85e-18 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 87.52 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQDV-ELGSLQVMNK-TRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNN---ENCSS 114
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNahaRNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 115 PSWQAMHEPRT---FAVYLNNTGYRTAFFGKYLNEYNGSYIP--PGWREWLG-------LIKNSRFYNYTVCRNgikEKH 182
Cdd:cd16157 81 PQNIVGGIPDSeilLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWFGapnchfgPYDNKAYPNIPVYRD---WEM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 183 GFDYAKDYFTDLITNESiNYfkmsKRMYPHRPIMMVISHAAPHgpedsAPQFSKLYPNASQhiTPSYNYAPnmdkhwimq 262
Cdd:cd16157 158 IGRYYEEFKIDKKTGES-NL----TQIYLQEALEFIEKQHDAQ-----KPFFLYWAPDATH--APVYASKP--------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 263 ytgpmlpihmeFTNVLQRKRL-QTLMSVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFG-----LVKGKSMP 333
Cdd:cd16157 217 -----------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngpFLCGKQTT 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068827 334 YDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16157 286 FEGGMREPAIAWWPGhIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVL 344
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
43-397 |
3.13e-17 |
|
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: 85.96 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDV-ELG-----SLQVMNKTRkiMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpS 116
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 117 WQAMHEPRTFAVYLNNTGYRTAFFGKY---LNEyNGSYIPP--GWREWLGL---------IKNSRFYNYTVCRNGIKEkh 182
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPThqGFDHYLGIpyshdqgpcQNLTCFPPNIPCFGGCDQ-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 183 GFDYAKDYFTDLITNESINYFKMSKRM--YPHRpimmVISHAAphgpEDSAPQFskLYpNASQHItpsynYAPnmdkhwi 260
Cdd:cd16158 156 GEVPCPLFYNESIVQQPVDLLTLEERYakFAKD----FIADNA----KEGKPFF--LY-YASHHT-----HYP------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 261 mQYTGpmlpihMEFTNVLQRKRL-QTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHI------GQFGLVK-GKSM 332
Cdd:cd16158 213 -QFAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGT 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068827 333 PYDFDIRVPFFIRGPS-IEPGsIVPQIVLNIDLAPTILDIAGLDSPS-DVDGKSVLKLLDLEKPGNR 397
Cdd:cd16158 286 TYEGGVREPAIAYWPGrIKPG-VTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPR 351
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-379 |
4.20e-17 |
|
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: 84.51 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDV-ELGS----LQVMNKTRKI--MEQGGATFTNAFVTtPMCCPSRSSMLTGKYVhnhnvytNNENCSSP 115
Cdd:cd16142 1 PNILVILGDDIGWgDLGCygggIGRGAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTGLTTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 116 SWQ-AMH----EPRTFAVYLNNTGYRTAFFGK-YLNEYNGSYipP---GWREWLGliknsrFYNYTVcrngikEKHGFDY 186
Cdd:cd16142 73 GLPgSPGglppWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEEIVDK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 187 AKDYFTDLITNE-----SINYFKMSKRMYPHrpimmvishaaphgpEDSAPQFSKLYPNASqhitpsynyapnmdkhwim 261
Cdd:cd16142 139 AIDFIKRNAKADkpfflYVNFTKMHFPTLPS---------------PEFEGKSSGKGKYAD------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 262 qytgpmlpihmeftnvlqrkrlqTLMSVDDSVERLYNMLVESGELDNTYIIYTADHG-----YHIGQFGLVKG-KSMPYD 335
Cdd:cd16142 185 -----------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWE 241
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907068827 336 FDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD 379
Cdd:cd16142 242 GGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
42-389 |
1.00e-16 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 84.65 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDDQDV-ELGSLQvmNKTRK-----IMEQGGATFTNAFVTTPMCCPSRSSMLTGKY------VHNHNVYTNN 109
Cdd:cd16159 1 KPNIVLFMADDLGIgDVGCFG--NDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHGMRVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 110 ENCSS---PSWQAmheprTFAVYLNNTGYRTAFFGKY----------------LN-----------------------EY 147
Cdd:cd16159 79 FTASSgglPPNET-----TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 148 NGSYIPP------------------------GWRE--------------WLGLIKNSRFYNYTVCRNG-IKEKhgfDYAK 188
Cdd:cd16159 154 DLSFDPLfplltafvlitaltiflllylgavSKRFfvfllilsllfislFFLLLITNRYFNCILMRNHeVVEQ---PMSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 189 DYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDSAPQFSklypNASQHitpsYNYAPNmdkhwimqytgpml 268
Cdd:cd16159 231 ENLTQRLTKEAISFLERNKE----RPFLLVMSFLHVHTALFTSKKFK----GRSKH----GRYGDN-------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 269 pihmeftnvlqrkrlqtLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHI-----------GQFGLVKGKSMP-YDF 336
Cdd:cd16159 285 -----------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEG 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068827 337 DIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16159 348 GIRVPTIVRWPGvIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLL 403
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
43-372 |
2.88e-14 |
|
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: 73.61 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 43 PNIILVLTDDQDVELGSLQVMNKTR----KIMEQGGATFtNAFVTTPMC--CPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTtpnlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 117 WQAMHEP---RTFAVYLNNTGYRTAFFG--KYLNEyngsyippgwrewlgliknsrfynytvcrnGIKEKHGFDYakdyf 191
Cdd:cd00016 80 SRAAGKDedgPTIPELLKQAGYRTGVIGllKAIDE------------------------------TSKEKPFVLF----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 192 tdlitnesINYfkmskrmyphrpimmvishAAPHGPedsapqfsklypnasqhitpSYNYAPNMDkhwimqytgpmlpih 271
Cdd:cd00016 125 --------LHF-------------------DGPDGP--------------------GHAYGPNTP--------------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 272 mEFTNVLQRkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFGLVKGKSMPYDFDIRVPFFIRGPS 348
Cdd:cd00016 143 -EYYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPG 213
|
330 340
....*....|....*....|....
gi 1907068827 349 IEPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd00016 214 VKKGGVKHELISQYDIAPTLADLL 237
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
42-389 |
2.26e-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: 73.27 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 42 RPNIILVLTDD---QDVELGSLQVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVyTNNENCSSPS 116
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 117 WQAMHEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPpgwrewlglikNSRFYNYTVcrnGIKEKHGFDYAKDYF---TD 193
Cdd:cd16161 80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaTD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 194 LITNESINyfkmskrmypHRPIMMVISHAAPHGPEDSAPQFsklyPNASQHITPsynyapnmdkhwimqyTGpmlpihme 273
Cdd:cd16161 145 FIQRASAK----------DRPFFLYAALAHVHVPLANLPRF----QSPTSGRGP----------------YG-------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 274 ftnvlqrkrlQTLMSVDDSVERLYNMLVESGELDNTYIIYTAD---------------HGYHIGQFGLVKGKSMPYDFDI 338
Cdd:cd16161 187 ----------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGH 256
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1907068827 339 RVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16161 257 REPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
67-373 |
2.76e-08 |
|
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: 56.44 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 67 RKIMEQGGATF--TNAFVT-TpmcCPSRSSMLTGKYVHNHNVYTN-------NENCSSPSWqaMHEPR-----TFAVYLN 131
Cdd:cd16018 26 KRLAEEGVRAKyvKPVFPTlT---FPNHYSIVTGLYPESHGIVGNyfydpktNEEFSDSDW--VWDPWwiggePIWVTAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 132 NTGYRTA-FFGKY-LNEYNGSYIPPGWREWLGLIKNSRFynytvcrngikekhGFDYAKDYFtdlitnesINYFKMSkrm 209
Cdd:cd16018 101 KAGLKTAsYFWPGsEVAIIGYNPTPIPLGGYWQPYNDSF--------------PFEERVDTI--------LEWLDLE--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 210 yphRPIMMVISHAAPhgpeDSApqfsklypnasQHitpsyNYAPNmdkhwimqytgpmlpiHMEFTNVLQRkrlqtlmsV 289
Cdd:cd16018 156 ---RPDLILLYFEEP----DSA-----------GH-----KYGPD----------------SPEVNEALKR--------V 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 290 DDSVERLYNMLVESGELDNTYIIYTADHGY-----HiGQFglvkgksmPYDFDIRVPFFIRGPSIEPGSIVPQIvLNIDL 364
Cdd:cd16018 189 DRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF-RNVDI 258
|
....*....
gi 1907068827 365 APTILDIAG 373
Cdd:cd16018 259 YPLMCNLLG 267
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
342-390 |
2.24e-06 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 51.44 E-value: 2.24e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1907068827 342 FFIRGPSIEPGSIVPQIVLnIDLAPTILDIAGLDSPSDVDGKSVLKLLD 390
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
229-369 |
1.58e-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: 49.13 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 229 DSAPQFSKLYPNASQhitPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNVLQRKRLQTLMSVDDSVERLYNMLVESGELDN 308
Cdd:COG3083 379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068827 309 TYIIYTADHGYhigQFGLVKGKSMPY-----DFDIRVPFFIRGPSIEPGSIvPQIVLNIDLAPTIL 369
Cdd:COG3083 456 TIVIITADHGE---EFNENGQNYWGHnsnfsRYQLQVPLVIHWPGTPPQVI-SKLTSHLDIVPTLM 517
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
272-383 |
1.09e-03 |
|
SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 42.90 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 272 MEFTNVLQ---RKRLQTLMSVDDSVERLYNMLV--ESGEL---------DNTYIIYTADHGyhigqfglvkgksMPYDFD 337
Cdd:cd16016 342 LQMPGVAAaytADELLAGPEPTGIRERLRNGYNpkRSGDLivvlkpgwiEGDGSGKGTTHG-------------SPYDYD 408
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907068827 338 IRVPFFIRGPSIEPGSIV--PQIVlniDLAPTILDIAGLDSPSDVDGK 383
Cdd:cd16016 409 THVPLLFYGWGIKPGEIPrpVEIT---DIAPTLAALLGIQPPNGCIGK 453
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
290-375 |
6.44e-03 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 39.91 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 290 DDSVERLYNMLVESGEldNTYIIYTADHGYHIGQFGlVKGKSMPYDFD--IRVPFFI--------RGPSIEPGSIVPQIV 359
Cdd:cd16017 196 DYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRANKDRPF 272
|
90
....*....|....*.
gi 1907068827 360 LNIDLAPTILDIAGLD 375
Cdd:cd16017 273 SHDNLFHTLLGLLGIK 288
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
283-368 |
7.23e-03 |
|
GPI ethanolamine phosphate transferase 1; PIG-N; 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: 293744 Cd Length: 294 Bit Score: 39.88 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068827 283 LQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGyhIGQFGLVKGKSmpyDFDIRVPFF-----IRGPSIEPGSI--- 354
Cdd:cd16020 182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHG--MTDWGSHGDGS---PDETETPFIawgagIKHPTPGRGPSfsa 256
|
90 100
....*....|....*....|.
gi 1907068827 355 ------VPQIVLN-IDLAPTI 368
Cdd:cd16020 257 nwgglrLPRHDLDqADLAPLM 277
|
|
| |
