|
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: 542.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 196 TNESINYFKMSKRMypHRPVMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 275 TNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSI 354
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 189571638 355 VPQIVLNIDLAPTILDIAGLDTPPDVDGKS 384
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
42-414 |
1.05e-85 |
|
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: 280.18 E-value: 1.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQ--DVeLGSLQ-VMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcSSPS 116
Cdd:cd16031 2 RPNIIFILTDDHryDA-LGCYGnPIVKTPNIdrLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQamhepRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHgfdyaKDYFTDLIT 196
Cdd:cd16031 80 SQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTDIIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESINYFKmsKRMyPHRPVMMVISHAAPHGPEDSAPQFSKLYPNAsqHITPSYNYAPN-------------MDKHWIMQY 263
Cdd:cd16031 150 DKALDFLK--ERD-KDKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEPETFDDDdyagrpewareqrNRIRGVLDG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 264 tgpmlPIHMEFTniLQR--KR-LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRV 340
Cdd:cd16031 225 -----RFDTPEK--YQRymKDyLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRV 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189571638 341 PFFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDpekpgnrfrtNKKAKIWRDTFLVE 414
Cdd:cd16031 297 PLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
42-414 |
9.64e-73 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 244.02 E-value: 9.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQDVelGSLQVMNKTRKIMEH------GGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsSP 115
Cdd:COG3119 23 RPNILFILADDLGY--GDLGCYGNPLIKTPNidrlaaEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--YN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDLI 195
Cdd:COG3119 99 GGLPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 196 TNESINYfkMSKRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmeft 275
Cdd:COG3119 134 TDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR------------ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 276 niLQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SVEPGSI 354
Cdd:COG3119 198 --ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGSV 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 355 VPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLdpekpgnrfrTNKKAKiWRDTFLVE 414
Cdd:COG3119 276 SDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE-WRDYLYWE 324
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
534-679 |
1.93e-69 |
|
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: 226.07 E-value: 1.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEEelQVLQPRNIAKRH--DEGHKGPRDLQASSGGnrgrMLADSSNAVGPPTT 611
Cdd:pfam12548 1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEEY--QPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPAS 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189571638 612 VRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSK 679
Cdd:pfam12548 75 VKVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
43-384 |
1.88e-51 |
|
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: 180.33 E-value: 1.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQ---DVE-LGSLQVmnKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsspS 116
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN----G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHgfdyakdyftdlit 196
Cdd:cd16022 75 GGLPPDEPTLAELLKEAGYRTALIGK----------------W----------------------H-------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESINYFKmskRMYPHRPVMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:cd16022 103 DEAIDFIE---RRDKDKPFFLYVSFNAPHPP---------------------FAYYAMVS-------------------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 277 ilqrkrlqtlmSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SVEPGSIV 355
Cdd:cd16022 139 -----------AIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIPAGQVS 207
|
330 340
....*....|....*....|....*....
gi 189571638 356 PQIVLNIDLAPTILDIAGLDTPPDVDGKS 384
Cdd:cd16022 208 DALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-400 |
2.83e-51 |
|
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: 185.08 E-value: 2.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDD---QDveLGSLQVMN-KTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTnneNCSSP 115
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG---NDVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SwqamHEPRTFAVYLNNTGYRTAFFGKY-LNE-------YNGSYIPP----GWREWLGLIKNSRFYNYTVCRNGIKEKHG 183
Cdd:cd16034 76 P----PDAPTIADVLKDAGYRTGYIGKWhLDGperndgrADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 184 FDYAKDYFTDLItnesINYfkMSKRMYPHRPVMMVISHAAPHGPEDSAPQ-FSKLYPNASQHITPsyNYAPNMD-----K 257
Cdd:cd16034 152 KGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLLRP--NVPEDKKeeaglR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 258 HWIMQYtgpmlpihmeFTNILqrkrlqtlmSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFD 337
Cdd:cd16034 224 EDLRGY----------YAMIT---------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPYEES 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189571638 338 IRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNRFRT 400
Cdd:cd16034 284 IRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSV 347
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
43-397 |
1.10e-47 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 174.23 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDVELGSlqVMN---KTRKIME--HGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTN-NENCSSPS 116
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQamhepRTFAVYLNNTGYRTAFFGKYlnEYNGSYIPPGWrewlgliknsrFYNYTVCRNGIKEKHGFDYAKDYFTDLIT 196
Cdd:cd16027 79 GV-----KTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NE----SINYFkmskrmYPHRPVMMVISHAAPHGPEDsapqfsklypnasqhITPSYNYA--PNMDKHWIMQYTgpmlpi 270
Cdd:cd16027 141 GQpfflWFGFH------DPHRPYPPGDGEEPGYDPEK---------------VKVPPYLPdtPEVREDLADYYD------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 271 hmeftnilqrkrlqTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYhigqfGLVKGKSMPYDFDIRVPFFIRGPS-V 349
Cdd:cd16027 194 --------------EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkI 254
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 189571638 350 EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 397
Cdd:cd16027 255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
43-374 |
1.93e-46 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 168.37 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQ-DVELGSLQ-VMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQ 118
Cdd:pfam00884 1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 119 AMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLIT 196
Cdd:pfam00884 75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESINYfkmskRMYPHRPVMMVISHAAPHGPedsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:pfam00884 149 DEALEF-----LDNNDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL-------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 277 ilqRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGPSVEP-G 352
Cdd:pfam00884 200 ---NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAkG 276
|
330 340
....*....|....*....|..
gi 189571638 353 SIVPQIVLNIDLAPTILDIAGL 374
Cdd:pfam00884 277 QKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-414 |
6.84e-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: 170.09 E-value: 6.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDV----ELGSLQVmnKT---RKIMEHGgATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16033 1 PNILFIMTDQQRYdtlgCYGNPIV--KTpniDRLAAEG-VRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgWRewlgliknsrfynytVCRNGIKEKHGFDY------AKD 189
Cdd:cd16033 78 SRGLPPGVETFSEDLREAGYRNGYVGK-------------WH---------------VGPEETPLDYGFDEylpvetTIE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 190 YFTDLITNESINYFKMSKRmyphrPVMMVISHAAPHGPEDSAPQFSKLYPNASqhITPSYNYAPNM-DKHWImQYTGPML 268
Cdd:cd16033 130 YFLADRAIEMLEELAADDK-----PFFLRVNFWGPHDPYIPPEPYLDMYDPED--IPLPESFADDFeDKPYI-YRRERKR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 269 PIHMEFTNILQRKRLQ------TLMsvDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV-KGKSMpYDFDIRVP 341
Cdd:cd16033 202 WGVDTEDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIP 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189571638 342 FFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNrfrtnkkakiWRDTFLVE 414
Cdd:cd16033 279 LIIKWPgVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-397 |
7.26e-46 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 170.42 E-value: 7.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDD---QDVelgSLQvMNKtrkIME--------HGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYT---- 107
Cdd:cd16144 1 PNIVLILVDDlgwADL---GCY-GSK---FYEtpnidrlaKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 108 ------NNENCSSPSWQAM-HEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYipP---GWREWLGLIKNSRFYNYTVCRN 176
Cdd:cd16144 74 rrgppdNTKLIPPPSTTRLpLEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 177 GIKEKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPVMMVISHAAPHGPEDSAPQFSKLYpnasqhitpsYNYAPNMD 256
Cdd:cd16144 152 KPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKY----------EKKKKGLR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 257 KHWIMQYTGPMLpihmeftnilqrkrlqtlMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV-------KG 329
Cdd:cd16144 218 KGQKNPVYAAMI------------------ESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGG 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189571638 330 KSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPP--DVDGKSVLKLL-DPEKPGNR 397
Cdd:cd16144 280 KGSLYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLLkGGEADLPR 351
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
43-413 |
8.23e-39 |
|
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: 149.62 E-value: 8.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDVelGSLQVMN----KTRKI--MEHGGATFINaFVTTPMCCPSRSSMLTGKYVHNHNVYTnnencSSPS 116
Cdd:cd16146 1 PNVILILTDDQGY--GDLGFHGnpilKTPNLdrLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWH-----TILG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMH-EPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL-----------IKNSRFYNyTVCRNGIKEKH 182
Cdd:cd16146 73 RERMRlDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdyWGNDYFDD-TYYHNGKFVKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 183 gfdyaKDYFTDLITNESINYFKMSKrmypHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYApnmdkhwimq 262
Cdd:cd16146 152 -----EGYCTDVFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG---------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 263 ytgpMLpihmefTNIlqrkrlqtlmsvDDSVERLYNMLVETGELENTYIIYTADHGYHIG-----QFGLVKGKSMPYDFD 337
Cdd:cd16146 213 ----MI------ENI------------DDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEGG 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189571638 338 IRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPDV--DGKSVLKLLdpekpgnrfrTNKKAKiWRDTFLV 413
Cdd:cd16146 271 HRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIklDGRSLLPLL----------KGESDP-WPERTLF 338
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-398 |
9.47e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 146.92 E-value: 9.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 74 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpswqamhEPRTFAVYLNNTGYRTAFFGK--YLNEyngsy 151
Cdd:cd16037 36 GTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRGE----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 152 ippgwrewlgliknsrfynytvcrngiKEKHGFDYakdyfTDLITNESINYFKmsKRMYPHRPVMMVISHAAPHGPEDSA 231
Cdd:cd16037 104 ---------------------------DQRHGFRY-----DRDVTEAAVDWLR--EEAADDKPWFLFVGFVAPHFPLIAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 232 PQFSKLYpnasqhitpsynyapnmdkhwimqytgpmlpihmeftnilqRKRLQT----LMS-VDDSVERLYNMLVETGEL 306
Cdd:cd16037 150 QEFYDLY-----------------------------------------VRRARAayygLVEfLDENIGRVLDALEELGLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 307 ENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVL 386
Cdd:cd16037 189 DNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLL 267
|
330
....*....|..
gi 189571638 387 KLLDPEKPGNRF 398
Cdd:cd16037 268 PLAEGPDDPDRV 279
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-397 |
1.35e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 145.06 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQ--DVeLGSL-QVMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPS 116
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 wqamhEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHGFDYAKDYFTDLit 196
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 neSINYfkMSKRMyPHRPVMMVISHAAPH---------GPEDSAPQFSKLYP---------NASQHItPSYnyapnmdkh 258
Cdd:cd16152 113 --AIDY--LDNRQ-KDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWVppdlaalpgDWAEEL-PDY--------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 259 wimqytgpmlpihmeftnilqrkrLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHigqFGLVKG--KSMPYDF 336
Cdd:cd16152 178 ------------------------LGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189571638 337 DIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 397
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWR 291
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-397 |
1.61e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 144.63 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQDVE----LGSLQVmnKTRKI--MEHGGATFINAFVTTPM----CCPSRSSMLTGKYVHNhnvYTNNEN 111
Cdd:cd16155 2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 112 CSSPSwqamhEPRTFAVYLNNTGYRTAFFGKYLNEYngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdyf 191
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 192 tdliTNESINYFKmsKRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPnaSQHITPSYNYAPnmdKHwimQYTGPMLPIH 271
Cdd:cd16155 108 ----ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLP---QH---PFDNGEGTVR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 272 MEFT--------NIlqRKRLQ----TLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIR 339
Cdd:cd16155 174 DEQLapfprtpeAV--RQHLAeyyaMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-GKQNLYEHSMR 250
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 189571638 340 VPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 397
Cdd:cd16155 251 VPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVR 308
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-389 |
2.06e-36 |
|
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: 142.73 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDV-ELGSL-QVMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQ 118
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 119 AmhEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPP--GWREWLG--------------LIKNSR--FYNYTVCRNGIK 179
Cdd:cd16145 81 P--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGyldqvhahnyypeyLWRNGEkvPLPNNVIPPLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 180 EKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPVMMVISHAAPHGPEDsAPQFSklyPNASQHITPSYNYAPNMDKhw 259
Cdd:cd16145 159 GNNAGGGGGTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAPLQ-VPDDG---PYKYKPKDPGIYAYLPWPQ-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 260 imqytgpmlpihmeftnilQRKRLQTLMS-VDDSVERLYNMLVETGELENTYIIYTADHGYHI-------GQF-----GL 326
Cdd:cd16145 229 -------------------PEKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngPL 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189571638 327 VKGK-SMpYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLL 389
Cdd:cd16145 290 RGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-387 |
6.05e-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: 6.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTD----DQdvelgsLQVMNKTRKIMEH------GGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVytnnenc 112
Cdd:cd16148 1 MNVILIVIDslraDH------LGCYGYDRVTTPNldrlaaEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 113 sspsWQAMHEPR--TFAVYLNNTGYRTAFFGkylneyNGSYIPPGWREWLGliknsrfYNYTVCRNGIKEKHGFDyaKDY 190
Cdd:cd16148 68 ----WGGPLEPDdpTLAEILRKAGYYTAAVS------SNPHLFGGPGFDRG-------FDTFEDFRGQEGDPGEE--GDE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 191 FTDLITNESINYFKmskRMYPHRPVMMVISHAAPHGPEdsapqfskLYPNAsqhitpsynyapnmdkhwimqytgpmlpI 270
Cdd:cd16148 129 RAERVTDRALEWLD---RNADDDPFFLFLHYFDPHEPY--------LYDAE----------------------------V 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 271 HMeftnilqrkrlqtlmsVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMP-YDFDIRVPFFIRGPSV 349
Cdd:cd16148 170 RY----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGK 233
|
330 340 350
....*....|....*....|....*....|....*...
gi 189571638 350 EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLK 387
Cdd:cd16148 234 EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
42-397 |
6.05e-34 |
|
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: 135.78 E-value: 6.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQDVELGSL--QVMnKT-------RKimehgGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenc 112
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYggHPA-KTpnidrlaAR-----GVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 113 sSPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYI--PPGWREWLGLIKNSRFYNYTVCRNGIKEKHG------- 183
Cdd:cd16030 73 -SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDddPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpawe 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 184 -FDYAKDYFTD-LITNESINYFKMSKRMypHRPVMMVISHAAPHGPEdSAPQ-FSKLYPNASQHITPSYN------YAPN 254
Cdd:cd16030 152 aADVPDEAYPDgKVADEAIEQLRKLKDS--DKPFFLAVGFYKPHLPF-VAPKkYFDLYPLESIPLPNPFDpidlpeVAWN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 255 mDKHWIMQYTGPMLPIHMEFTNIL----QRKRLQT-LMSV---DDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGL 326
Cdd:cd16030 229 -DLDDLPKYGDIPALNPGDPKGPLpdeqARELRQAyYASVsyvDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGH 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189571638 327 VkGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLL-DPEKPGNR 397
Cdd:cd16030 308 W-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLkNPSAKWKD 379
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
72-390 |
9.39e-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: 132.70 E-value: 9.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 72 HGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPSWQamhePrTFAVYLNNTGYRTAFFGKYlneyngsy 151
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPADI----P-TFAHYLRAAGYRTALSGKM-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 152 ippgwrewlgliknsRFYnytvcrnGIKEKHGFDY-------AKDYFTDLitnesinyfkmsKRMYPHRPVMMVISHAAP 224
Cdd:cd16032 99 ---------------HFV-------GPDQLHGFDYdeevafkAVQKLYDL------------ARGEDGRPFFLTVSFTHP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 225 HGPEDSAPQFSKLYPNASQHitpSYnYApnmdkhwIMQYtgpmlpihmeftnilqrkrlqtlmsVDDSVERLYNMLVETG 304
Cdd:cd16032 145 HDPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 305 ELENTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDV---D 381
Cdd:cd16032 189 LADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVpplD 267
|
....*....
gi 189571638 382 GKSVLKLLD 390
Cdd:cd16032 268 GRSLLPLLE 276
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
74-411 |
1.08e-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: 135.46 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 74 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNnencSSPswQAMHEPrTFAVYLNNTGYRTAFFGK----------- 142
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARHL-TLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 143 YLNEYNGSY--IPPGWREwlgliknsrfynytVCR-NGIKEKHGfDYAkdYFTDlitnESINYFkmskRMYPHRPVMMVI 219
Cdd:cd16028 109 PLDPRLLSYelAMPGFDP--------------VDRlDEYPAEDS-DTA--FLTD----RAIEYL----DERQDEPWFLHL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 220 SHAAPHGP-EDSAPqFSKLYPNASqhiTPSYNYAPNMD---------KHWIMQYtgPMLPIHMEFTNI-----LQRKRLQ 284
Cdd:cd16028 164 SYIRPHPPfVAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 285 T----LMS-VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVE----PGSIV 355
Cdd:cd16028 238 AtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREadatRGQVV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 189571638 356 PQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNrfrtNKKAKIWRDTF 411
Cdd:cd16028 317 DAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSD----WRDAVHYEYDF 368
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-397 |
2.62e-32 |
|
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: 130.01 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDqdVELGSLQVMNKTRKI-------MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWqaMHEPR-TFAVYLNNTGYRTAFFGKY---LNEY--NGSYIPPGWRE---WLGLIKNSRFYnytvcrngikekHGFDY 186
Cdd:cd16143 79 PL--IEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKdvdYSKPIKGGPLD------------HGFDY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 187 akdYFT-------DLITNESINYFKMSKRmyPHRPVMMVISHAAPHGPedsapqfsklypnasqhITPS--YNYAPNMDK 257
Cdd:cd16143 145 ---YFGipasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 258 H--WIMQytgpmlpihmeftnilqrkrlqtlmsVDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFGLVKGKSM 332
Cdd:cd16143 203 YgdFVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGHDP 256
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189571638 333 PYDF-----DI-----RVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLK-LLDPEKPGNR 397
Cdd:cd16143 257 SGPLrgmkaDIyegghRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPaLLGPKKQEVR 335
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
42-398 |
1.77e-31 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 127.68 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQ---DVE-LGSlqVMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKY-----VHNHNVYTNNE 110
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGS--PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 111 NCSSPSwqamhEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL----------IKNSRFYNYTVCRNGI 178
Cdd:cd16026 79 GGLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIpysndmwpfpLYRNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 179 KEKHGFDYAKDYFTDLITNESINYFKMSKrmypHRPVMMVISHAAPHGPedsapqfskLYPNasqhitpsynyapnmdkh 258
Cdd:cd16026 153 EEVIEQPADQSSLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVP---------LFAS------------------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 259 wimqytgpmlpihMEFTNILQRKRL-QTLMSVDDSVERLYNMLVETGELENTYIIYTADHG--YHIGQFG-----LVKGK 330
Cdd:cd16026 202 -------------EKFKGRSGAGLYgDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGGK 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189571638 331 SMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDV--DGKSVLKLL--DPEKPGNRF 398
Cdd:cd16026 269 GTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDRviDGKDISPLLlgGSKSPPHPF 341
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
43-397 |
1.45e-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: 126.34 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQD---VELGSLQVMnKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSw 117
Cdd:cd16156 1 KQFIFIMTDTQRwdmVGCYGNKAM-KTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 qamhepRTFAVYLNNTGYRTAFFGKY-LN--EYNGSYI-PPGWRE--WLGL-----------IKNSRFYNYTVCRNGIKE 180
Cdd:cd16156 79 ------KTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMrnyldelteeeRRKSRRGLTSLEAEGIKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 181 KhgFDYAKDyftdlITNESINYFkmskRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNyaPNMDKHWI 260
Cdd:cd16156 153 E--FTYGHR-----CTNRALDFI----EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAY--DDLENKPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 261 MQ--YTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETgeLENTYIIYTADHGYHIGQFGL-VKGKSMpYDFD 337
Cdd:cd16156 220 HQrlWAGAKPHEDGDKGTIKHPLYFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHKLwAKGPAV-YDEI 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189571638 338 IRVPFFIRGPSVEPGSIVPQI-VLNIDLAPTILDIAGLDTPPDVDGKSVLKLL-DPEKPGNR 397
Cdd:cd16156 297 TNIPLIIRGKGGEKAGTVTDTpVSHIDLAPTILDYAGIPQPKVLEGESILATIeDPEIPENR 358
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-375 |
1.59e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 119.62 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQ----DVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtnnENCSSPS-W 117
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 QAMHEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYippgwrewlgliknsrfynytvcrngikekhgfdYAKDyftDLIT 196
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESINY-FKMSKRMYPHRPVMMVISHAAPH----GPEDSapqfsklypnasqhitPSYNYAPNMdkhwimqYtgpmlpih 271
Cdd:cd16035 121 AQAVEWlRERGAKNADGKPWFLVVSLVNPHdimfPPDDE----------------ERWRRFRNF-------Y-------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 272 meftnilqrkrLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEP 351
Cdd:cd16035 170 -----------YNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFG 238
|
330 340
....*....|....*....|....*
gi 189571638 352 -GSIVPQIVLNIDLAPTILDIAGLD 375
Cdd:cd16035 239 tGQTTDALTSHIDLLPTLLGLAGVD 263
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-386 |
9.25e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 116.18 E-value: 9.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQ-----------DVELGSLQVMNKTrkimehgGATFINAFVTTPMCCPSRSSMLTGKYVHNHNV-----Y 106
Cdd:cd16149 1 PNILFILTDDQgpwalgcygnsEAVTPNLDRLAAE-------GVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 107 TNNENCSSP-SWQAMHEprTFAVYLNNTGYRTAFFGKylneyngsyippgwreW-LGliknsrfynytvcrngikekhgf 184
Cdd:cd16149 74 GSHGKTKKPeGYLEGQT--TLPEVLQDAGYRCGLSGK----------------WhLG----------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 185 DYAKDYFTDLITNEsinyfkmskrmyphRPVMMVISHAAPHGPedsapqfsklypnasqhitpsynyapnmdkhWimQYt 264
Cdd:cd16149 113 DDAADFLRRRAEAE--------------KPFFLSVNYTAPHSP-------------------------------W--GY- 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 265 gpmlpihmeftnilqrkrLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGlVKGK-------SMpYDFD 337
Cdd:cd16149 145 ------------------FAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNS 204
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 189571638 338 IRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVD--GKSVL 386
Cdd:cd16149 205 VKVPFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
42-388 |
5.30e-28 |
|
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: 117.54 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDqdveLG-----------------SLQvmnktrkimeHGGATFiNAFVTTPMCCPSRSSMLTGKYVHNHN 104
Cdd:cd16025 2 RPNILLILADD----LGfsdlgcfggeiptpnldALA----------AEGLRF-TNFHTTALCSPTRAALLTGRNHHQVG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 105 VYTNNENCSS-PSWQAMHEPR--TFAVYLNNTGYRTAFFGKYlneYNGsyiPPGWrewlgliknsrfynytvcrngikek 181
Cdd:cd16025 67 MGTMAELATGkPGYEGYLPDSaaTIAEVLKDAGYHTYMSGKW---HLG---PDDY------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 182 hgfdyakdYFTDLITNESINYFKMSKRmyPHRPVMMVISHAAPHGPedsapqfsklypnasQHitpsynyAPnmdKHWIM 261
Cdd:cd16025 116 --------YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP---------------LQ-------AP---KEWID 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 262 QYTG---------------------------PMLPIHMEFT--NIL---QRKRLQTLMSV--------DDSVERLYNMLV 301
Cdd:cd16025 161 KYKGkydagwdalreerlerqkelglipadtKLTPRPPGVPawDSLspeEKKLEARRMEVyaamvehmDQQIGRLIDYLK 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 302 ETGELENTYIIYTADHG--YHIG--QFG---LVKGKSMPYDFDIRVPFFIRGPSV--EPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd16025 241 ELGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELA 320
|
410
....*....|....*.
gi 189571638 373 GLDTPPDVDGKSVLKL 388
Cdd:cd16025 321 GVEYPKTVNGVPQLPL 336
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
42-397 |
5.47e-28 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 118.62 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQDVE-LGSL---QVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsW 117
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 QAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY------ 190
Cdd:PRK13759 83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 191 --------FTDL-----------------------ITNESINYFKmskRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYP 239
Cdd:PRK13759 150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 240 NASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEFtniLQRKRLQTLMS---VDDSVERLYNMLVETGELENTYIIYTA 315
Cdd:PRK13759 227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEEY---ARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 316 DHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDP 391
Cdd:PRK13759 304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382
|
....*.
gi 189571638 392 EKPGNR 397
Cdd:PRK13759 383 QYEGWR 388
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
43-385 |
1.55e-26 |
|
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: 112.64 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQ---DVEL-GSLQVmnKT---RKIMEHGgaTFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTpnlDALAADG--VILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPrTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPPGwR-------EWLGLI-----KNSRFYNYTVCRNGIKEKH 182
Cdd:cd16029 77 YGLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTN-RgfdsfygYYGGAEdyythTSGGANDYGNDDLRDNEEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 183 GFDYAKDYFTDLITNESINYFKMSKrmyPHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPsynyapnmdkhwimq 262
Cdd:cd16029 155 AWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD--------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 263 ytgpmlpihmeftniLQRKRLQTLMS-VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG------LVKGKSMPYD 335
Cdd:cd16029 217 ---------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNTLWE 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 189571638 336 FDIRVPFFIRGPSVEP--GSIVPQIVLNIDLAPTILDIAGLDTP--PDVDGKSV 385
Cdd:cd16029 282 GGVRVPAFVWSPLLPPkrGTVSDGLMHVTDWLPTLLSLAGGDPDdlPPLDGVDQ 335
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-389 |
2.60e-26 |
|
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: 111.92 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDVE-LGSL-QVMNKTRKI--MEHGGATFINAFvTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPswq 118
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 119 amheprTFAVYLNNTGYRTAFFGK---YLNEYNGSYIPP-GWREWL-------GLIKNSRFYNYTVCRNGIKEKhgfDYA 187
Cdd:cd16151 77 ------TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 188 KDYFTDLITNESINYFKMSKR-----MYPhrpvmMVIshaaPHGPEDSAPQFSKLYPnasqhitPSYNYAPNMDKHWIM- 261
Cdd:cd16151 148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDPFVPTPDSPDWDP-------DDKRKKDDPEYFPDMv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 262 QYTgpmlpihmeftnilqrkrlqtlmsvDDSVERLYNMLVETGELENTYIIYTADHGYHIG-----QFGLVKG-KSMPYD 335
Cdd:cd16151 212 AYM-------------------------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 189571638 336 FDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 389
Cdd:cd16151 267 AGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL 323
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-397 |
7.86e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 105.39 E-value: 7.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 74 GATFINAFVTTPMCCPSRSSMLTGKY--VHNHNVYTNnencsspsWQAMHEPrTFAVYLNNTGYRTAFFGKylneyNGSY 151
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHH--------LLRPDEP-NLLKTLKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 152 IPPGWREwlgliknsrfyNYTVCrngikekhgfDYAkdyftdlITNESINYFKmskRMYPHRPVMMVISHAAPHGP-EDS 230
Cdd:cd16150 102 PGEFAAE-----------AYCDS----------DEA-------CVRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 231 APQFSKLYPNASQHITPSynyapnmdKHWIMQYtgPMLPIHMEFTNiLQR---KRLQTL--------MSVDDSVERLYNM 299
Cdd:cd16150 151 EPWFSMIDREKLPPRRPP--------GLRAKGK--PSMLEGIEKQG-LDRwseERWRELratylgmvSRLDHQFGRLLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 300 LVETGELENTYIIYTADHGYHIGQFGLV-KGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPP 378
Cdd:cd16150 220 LKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSH 299
|
330 340
....*....|....*....|
gi 189571638 379 DVDGKSVLKLL-DPEKPGNR 397
Cdd:cd16150 300 THFGRSLLPVLaGETEEHRD 319
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-387 |
1.16e-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: 101.68 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQDVElgSLQVMNKTR---KIMEHG-------------GATFINAFVTTPMCCPSRSSMLTGKYVHNHNV 105
Cdd:cd16153 1 KPNILWIITDDQRVD--SLSCYNNAHtgkSESRLGyvespnidalaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 106 YtNNENcsspSWQAMHE-PRTFAVYLNNTGYRTAFFGKylneyngsyipPGWREWLGLIKNSrfyNYTVCRNGIKEKHGF 184
Cdd:cd16153 79 Y-GFEA----AHPALDHgLPTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 185 DYAKdyftdlitnesinyfkmskrmyphrPVMMVISHAAPHGPedsapqfsklypnasqhITPSYNYAPNMDKHWIMQYt 264
Cdd:cd16153 140 DSDK-------------------------PFFVRLSFLQPHTP-----------------VLPPKEFRDRFDYYAFCAY- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 265 gpmlpihmeftnilqrkrlqtlmsVDDSVERLYNMLVETGEL---ENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVP 341
Cdd:cd16153 177 ------------------------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVP 231
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 189571638 342 FFIRGPSVEP---GSIVPQIVLNIDLAPTILDIAGLD--TPPDVDGKSVLK 387
Cdd:cd16153 232 LIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRDLFE 282
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-400 |
5.47e-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: 98.96 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDVE------LGSLQVMNKTRKIMEHGGATFINAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 wqamHE-PRTFAVYLNNTGYRTAFFGKYL--NEYNGSYIPPGWREWLGLIKN--SRFYNYTVCRNGIKEKHGfDYAKDYF 191
Cdd:cd16154 80 ----ETlLQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST-EYATTKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 192 TDL----ITNESINYFkmskrmyphrpvmMVISHAAPHGPedsapqFsKLYPNA--SQHITPSYnyapnmdkhwimqytg 265
Cdd:cd16154 155 TNLaidwIDQQTKPWF-------------LWLAYNAPHTP------F-HLPPAElhSRSLLGDS---------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 266 pmlpihmefTNILQRKR---LQTLMSVDDSVERLYNMLVETgELENTYIIYTADHGYHiGQ-----FGLVKGKSMPYDFD 337
Cdd:cd16154 199 ---------ADIEANPRpyyLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGG 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189571638 338 IRVPFFIRGPSVEPGSIVPQIVLNI-DLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNRFRT 400
Cdd:cd16154 268 INVPLIVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQYN 331
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
42-394 |
1.18e-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: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDqdVELGSLQVMNKTRKimEHG--------GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtnNENCS 113
Cdd:cd16160 1 KPNIVLFFADD--MGYGDLASYGHPTQ--ERGpiddmaaeGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 114 SPSWQAMHEPR---TFAVYLNNTGYRTAFFGKY---LNEYN---GSYIPpgwrewlgliknsrfynytvcrngikEKHGF 184
Cdd:cd16160 75 FLPWDIGGLPKtevTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLP--------------------------SHHGF 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 185 DYA---------------------KD------YFTDLITNESINYFKMSKRMYP----------HRPVMMVISHAAPHGP 227
Cdd:cd16160 129 DFVgtnlpftnswacddtgrhvdfPDrsacflYYNDTIVEQPIQHEHLTETLVGdaksfiednqENPFFLYFSFPQTHTP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 228 EDSAPQFSklypNASQHitpsYNYAPNMDKhwimqytgpmlpihmeftnilqrkrlqtlMSVddSVERLYNMLVETGELE 307
Cdd:cd16160 209 LFASKRFK----GKSKR----GRYGDNINE-----------------------------MSW--AVGEVLDTLVDTGLDQ 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 308 NTYIIYTADHGYHI------GQFGLVKG-KSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPD- 379
Cdd:cd16160 250 NTLVFFLSDHGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDr 329
|
410
....*....|....*.
gi 189571638 380 -VDGKSVLKLLDPEKP 394
Cdd:cd16160 330 iYDGLSITDLLLGEAD 345
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
43-389 |
1.87e-19 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 91.06 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDVELgSLQVMNKTRKI-----MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtNNENCSSPSW 117
Cdd:cd16171 1 PNVVMVMSDSFDGRL-TFRPGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 QamheprTFAVYLNNTGYRTAFFGKyLNEYNGSYIPPGWRE-WlgliknSRFYNYTVCRNGIKEkhgfdyakdyfTDLIT 196
Cdd:cd16171 79 P------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRPT-----------VNLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESinyfkmskrmypHRPVMMvishaaphgpedsapqfsKLYPNASQHITPSYNYAPNMDKHWIMqYTGPMLP------- 269
Cdd:cd16171 135 DRS------------TVRVML------------------KDWQNTDKAVHWIRKEAPNLTQPFAL-YLGLNLPhpypsps 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 270 IHMEFTNILQRKRLQTLM--SVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGP 347
Cdd:cd16171 184 MGENFGSIRNIRAFYYAMcaETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGP 262
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 189571638 348 SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLL 389
Cdd:cd16171 263 GIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
768-817 |
1.01e-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: 89.15 E-value: 1.01e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189571638 768 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 817
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
42-422 |
8.84e-18 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 87.79 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLtddqdVElgSLQ--VMNKT----------RKIMEHGgATFINAFVTTPMCCPSRSSMLTGKY-VHNHNVYTN 108
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 109 NencsspswqAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--Y 186
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 187 AKDYFTDLITN-----------ESINYFKMSKRmyphrPVMMVISHAAPHGPedsapqfsklypnasqhitpsynYAPNM 255
Cdd:COG1368 352 DREDFDDPFDGgwgvsdedlfdKALEELEKLKK-----PFFAFLITLSNHGP-----------------------YTLPE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 256 DKHWIMQYTGPMLpihmeftnilqRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGyhigqfGLVKGKSmPYD 335
Cdd:COG1368 404 EDKKIPDYGKTTL-----------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 336 FDI---RVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVD-GKSvlkLLDPEKPGNRFR-----TNKKAKI 406
Cdd:COG1368 466 NPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRD---LLSPDTDPFAFRnggfiTDDYVYV 542
|
410
....*....|....*.
gi 189571638 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 |
2.87e-17 |
|
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: 83.12 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVL-----TDDQDVELGSLQVMNKTRKIMEHGgATFINAFVTTPMCCPSRS--SMLTGkyvhnhnVYTNNENCSSP 115
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--YAKDYFTD 193
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 194 LITNESINY------FKMSKRMY---PHRPVMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDKhwimqyt 264
Cdd:cd16015 128 DEKETNGWGvsdeslFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 265 gpmLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFdiRVPFFI 344
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 189571638 345 RGPSVEPGSIVPQIVLNIDLAPTILDIAG 373
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
42-389 |
8.00e-17 |
|
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: 84.06 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDQDV-ELGSLQVMNK-TRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE---NCSS 114
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 115 PSWQAMHEPRT---FAVYLNNTGYRTAFFGKYLNEYNGSYIP--PGWREWLG-------LIKNSRFYNYTVCRNgikEKH 182
Cdd:cd16157 81 PQNIVGGIPDSeilLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWFGapnchfgPYDNKAYPNIPVYRD---WEM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 183 GFDYAKDYFTDLITNESiNYfkmsKRMYPHRPVMMVISHAAPHgpedsAPQFSKLYPNASQhiTPSYNYAPnmdkhwimq 262
Cdd:cd16157 158 IGRYYEEFKIDKKTGES-NL----TQIYLQEALEFIEKQHDAQ-----KPFFLYWAPDATH--APVYASKP--------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 263 ytgpmlpihmeFTNILQRKRL-QTLMSVDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFG-----LVKGKSMP 333
Cdd:cd16157 217 -----------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngpFLCGKQTT 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 189571638 334 YDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 389
Cdd:cd16157 286 FEGGMREPAIAWWPGhIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVL 344
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
43-397 |
6.88e-16 |
|
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: 81.34 E-value: 6.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDV-ELG-----SLQVMNKTRkiMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpS 116
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMHEPRTFAVYLNNTGYRTAFFGKY---LNEyNGSYIPP--GWREWLGL---------IKNSRFYNYTVCRNGIKEkh 182
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPThqGFDHYLGIpyshdqgpcQNLTCFPPNIPCFGGCDQ-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 183 GFDYAKDYFTDLITNESINYFKMSKRM--YPHRpvmmVISHAAphgpEDSAPQFskLYpNASQHItpsynYAPnmdkhwi 260
Cdd:cd16158 156 GEVPCPLFYNESIVQQPVDLLTLEERYakFAKD----FIADNA----KEGKPFF--LY-YASHHT-----HYP------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 261 mQYTGpmlpihMEFTNILQRKRL-QTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHI------GQFGLVK-GKSM 332
Cdd:cd16158 213 -QFAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGT 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189571638 333 PYDFDIRVPFFIRGPS-VEPGsIVPQIVLNIDLAPTILDIAGLDTPP-DVDGKSVLKLLDPEKPGNR 397
Cdd:cd16158 286 TYEGGVREPAIAYWPGrIKPG-VTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPR 351
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-379 |
1.42e-15 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 79.50 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDV-ELGS----LQVMNKTRKI--MEHGGATFINAFVTtPMCCPSRSSMLTGKYVhnhnvytNNENCSSP 115
Cdd:cd16142 1 PNILVILGDDIGWgDLGCygggIGRGAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTGLTTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQ-AMH----EPRTFAVYLNNTGYRTAFFGK-YLNEYNGSYipP---GWREWLGliknsrFYNYTVcrngikEKHGFDY 186
Cdd:cd16142 73 GLPgSPGglppWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEEIVDK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 187 AKDYFTDLITNE-----SINYFKMSKRMYPHrpvmmvishaaphgpEDSAPQFSKLYPNASqhitpsynyapnmdkhwim 261
Cdd:cd16142 139 AIDFIKRNAKADkpfflYVNFTKMHFPTLPS---------------PEFEGKSSGKGKYAD------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 262 qytgpmlpihmeftnilqrkrlqTLMSVDDSVERLYNMLVETGELENTYIIYTADHG-----YHIGQFGLVKG-KSMPYD 335
Cdd:cd16142 185 -----------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWE 241
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 189571638 336 FDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD 379
Cdd:cd16142 242 GGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
42-389 |
2.11e-14 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 76.94 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDDqdveLG----------SLQVMNKTR------KIMEHGGATfinafvttPMCCPSRSSMLTGKY------ 99
Cdd:cd16159 1 KPNIVLFMADD----LGigdvgcfgndTIRTPNIDRlakegvKLTHHLAAA--------PLCTPSRAAFLTGRYpirsgm 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 100 VHNHNVYTNNENCSS---PSWQAmheprTFAVYLNNTGYRTAFFGKY----------------LN--------------- 145
Cdd:cd16159 69 ASSHGMRVILFTASSgglPPNET-----TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlk 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 146 --------EYNGSYIPP------------------------GWRE--------------WLGLIKNSRFYNYTVCRNG-I 178
Cdd:cd16159 144 dcgdgsngEYDLSFDPLfplltafvlitaltiflllylgavSKRFfvfllilsllfislFFLLLITNRYFNCILMRNHeV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 179 KEKhgfDYAKDYFTDLITNESINYFKMSKRmyphRPVMMVISHAAPHGPEDSAPQFSklypNASQHitpsYNYAPNmdkh 258
Cdd:cd16159 224 VEQ---PMSLENLTQRLTKEAISFLERNKE----RPFLLVMSFLHVHTALFTSKKFK----GRSKH----GRYGDN---- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 259 wimqytgpmlpihmeftnilqrkrlqtLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHI-----------GQFGLV 327
Cdd:cd16159 285 ---------------------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIY 337
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189571638 328 KGKSMP-YDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 389
Cdd:cd16159 338 GGKKMGgWEGGIRVPTIVRWPGViPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLL 403
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
42-389 |
1.19e-13 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 73.66 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 42 RPNIILVLTDD---QDVELGSLQVMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVyTNNENCSSPS 116
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMHEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPpgwrewlglikNSRFYNYTVcrnGIKEKHGFDYAKDYF---TD 193
Cdd:cd16161 80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaTD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 194 LITNESINyfkmskrmypHRPVMMVISHAAPHGPEDSAPQFsklyPNASQHITPsynyapnmdkhwimqyTGpmlpihme 273
Cdd:cd16161 145 FIQRASAK----------DRPFFLYAALAHVHVPLANLPRF----QSPTSGRGP----------------YG-------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 274 ftnilqrkrlQTLMSVDDSVERLYNMLVETGELENTYIIYTAD---------------HGYHIGQFGLVKGKSMPYDFDI 338
Cdd:cd16161 187 ----------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGH 256
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 189571638 339 RVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 389
Cdd:cd16161 257 REPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
43-372 |
2.63e-13 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 70.53 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 43 PNIILVLTDDQDVELGSLQVMNKTR----KIMEHGGATFiNAFVTTPMC--CPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTtpnlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMHEP---RTFAVYLNNTGYRTAFFG--KYLNEyngsyippgwrewlgliknsrfynytvcrnGIKEKHGFDYakdyf 191
Cdd:cd00016 80 SRAAGKDedgPTIPELLKQAGYRTGVIGllKAIDE------------------------------TSKEKPFVLF----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 192 tdlitnesINYfkmskrmyphrpvmmvishAAPHGPEDSAPQFSKLYPNASQHItpsynyapnmdkhwimqytgpmlpih 271
Cdd:cd00016 125 --------LHF-------------------DGPDGPGHAYGPNTPEYYDAVEEI-------------------------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 272 meftnilqrkrlqtlmsvDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFGLVKGKSMPYDFDIRVPFFIRGPS 348
Cdd:cd00016 152 ------------------DERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPG 213
|
330 340
....*....|....*....|....
gi 189571638 349 VEPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd00016 214 VKKGGVKHELISQYDIAPTLADLL 237
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
284-373 |
1.35e-07 |
|
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: 53.74 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 284 QTLMSVDDSVERLYNMLVETGELENTYIIYTADHGY-----HiGQFglvkgksmPYDFDIRVPFFIRGPSVEPGSIVPQI 358
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF 253
|
90
....*....|....*
gi 189571638 359 vLNIDLAPTILDIAG 373
Cdd:cd16018 254 -RNVDIYPLMCNLLG 267
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
342-390 |
2.90e-06 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 50.67 E-value: 2.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 189571638 342 FFIRGPSVEPGSIVPQIVLnIDLAPTILDIAGLDTPPDVDGKSVLKLLD 390
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
229-378 |
7.78e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 49.52 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 229 DSAPQFSKLYPNASQhitPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELEN 308
Cdd:COG3083 379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 309 TYIIYTADHGY-----------HIGQFGlvkgksmpyDFDIRVPFFIRGPSVEPGSIvPQIVLNIDLAPTIL-DIAGLDT 376
Cdd:COG3083 456 TIVIITADHGEefnengqnywgHNSNFS---------RYQLQVPLVIHWPGTPPQVI-SKLTSHLDIVPTLMqRLLGVQN 525
|
..
gi 189571638 377 PP 378
Cdd:COG3083 526 PA 527
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
289-387 |
2.20e-03 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 41.63 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 289 VDDSVERLYNMLVETGeleNTYIIyTADHG-------YHIGQfglvkgksmPY------DfdirVPFFIRGPSV---EPG 352
Cdd:PRK05434 417 VDECLGRVVDAVLKVG---GTLLI-TADHGnaeqmidPETGQ---------PHtahttnP----VPFILVGGKAlrlEGG 479
|
90 100 110
....*....|....*....|....*....|....*
gi 189571638 353 SIvpqivlnIDLAPTILDIAGLDTPPDVDGKSVLK 387
Cdd:PRK05434 480 KL-------ADIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
290-375 |
4.07e-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: 40.30 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 290 DDSVERLYNMLVETGEleNTYIIYTADHGYHIGQFGlVKGKSMPYDFD--IRVPFFI--------RGPSVEPGSIVPQIV 359
Cdd:cd16017 196 DYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRANKDRPF 272
|
90
....*....|....*.
gi 189571638 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 |
5.31e-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: 5.31e-03
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gi 189571638 283 LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGyhIGQFGLVKGKSmpyDFDIRVPFF-----IRGPSVEPGSI--- 354
Cdd:cd16020 182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHG--MTDWGSHGDGS---PDETETPFIawgagIKHPTPGRGPSfsa 256
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gi 189571638 355 ------VPQIVLN-IDLAPTI 368
Cdd:cd16020 257 nwgglrLPRHDLDqADLAPLM 277
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