|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
41-495 |
0e+00 |
|
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: 687.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 41 KYNVLMIAVDDLRPEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKTLPD 120
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 121 VITLPQHFKNHGYHTQGLSKIYHGGL----DDPASWSVPHWSPSKPMYGKPETLADLDRRReemrkkagpatrvlekdpk 196
Cdd:cd16030 82 AVTLPQYFKENGYTTAGVGKIFHPGIpdgdDDPASWDEPPNPPGPEKYPPGKLCPGKKGGK------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 197 tgiplrlsapqYRVYGPAWEDPDVPDDALPDGETTNRAIELLQELKDRR--FFLAVGYLKPHLPFVAPKKYYDLYRKEDI 274
Cdd:cd16030 143 -----------GGGGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDkpFFLAVGFYKPHLPFVAPKKYFDLYPLESI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 275 PLAaNPFPPKDCPPIALTNWGELRAYQGIPAA------GPLPDSMARDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDST 348
Cdd:cd16030 212 PLP-NPFDPIDLPEVAWNDLDDLPKYGDIPALnpgdpkGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 349 IVVLWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLF 428
Cdd:cd16030 291 IVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLL 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238332949 429 ENPQRPWQKAAFSQYPRGKVMGYSMRTDRYRYTEWRPsgGGEPVAVELYDHTTDPLENVNLAGRPEY 495
Cdd:cd16030 371 KNPSAKWKDAAFSQYPRPSIMGYSIRTERYRYTEWVD--FDKVGAEELYDHKNDPNEWKNLANDPEY 435
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
30-514 |
6.38e-128 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 378.45 E-value: 6.38e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 30 FASETANKPSGKYNVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVY 108
Cdd:COG3119 12 LAAAAAAAAAKRPNILFILADDLGYGDlGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 109 DLQTHFRKTLP-DVITLPQHFKNHGYHTQglskiyhgglddpaswsvphwspskpMYGKpetladldrrreemrkkagpa 187
Cdd:COG3119 92 DNGEGYNGGLPpDEPTLAELLKEAGYRTA--------------------------LFGK--------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 188 trvlekdpktgiplrlsapqYRVYgpawedpdvpddalPDGETTNRAIELLQEL--KDRRFFLAVGYLKPHLPFVAPKKY 265
Cdd:COG3119 125 --------------------WHLY--------------LTDLLTDKAIDFLERQadKDKPFFLYLAFNAPHAPYQAPEEY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 266 YDLYRKEDIPLAANPFPPKDCPPIAltnwgelrayqgipaagplpdsmaRDLVHGYYAATSYVDAQIGRLLAEVDRLGLR 345
Cdd:COG3119 171 LDKYDGKDIPLPPNLAPRDLTEEEL------------------------RRARAAYAAMIEEVDDQVGRLLDALEELGLA 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 346 DSTIVVLWGDHGWHLGDHGL-WCKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSL 424
Cdd:COG3119 227 DNTIVVFTSDNGPSLGEHGLrGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSL 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 425 VPLFENPQRPWQKAAFSQYPRGKvMGYSMRTDRYRYTEWRPSGGGEpvavELYDHTTDPLENVNLAGrpEYKDLVAQLHQ 504
Cdd:COG3119 307 LPLLTGEKAEWRDYLYWEYPRGG-GNRAIRTGRWKLIRYYDDDGPW----ELYDLKNDPGETNNLAA--DYPEVVAELRA 379
|
490
....*....|
gi 1238332949 505 QLEAGWKAAK 514
Cdd:COG3119 380 LLEAWLKELG 389
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
43-508 |
1.90e-88 |
|
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: 276.70 E-value: 1.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKTLPDVI 122
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 123 TLPQHFKNHGYHTqGLSKIYHGGlddpaswsvphwsPSKPMYGKPETLADLDRRREeMRKKAGPATRVLEKDPKtgiplr 202
Cdd:cd16027 82 TLPELLREAGYYT-GLIGKTHYN-------------PDAVFPFDDEMRGPDDGGRN-AWDYASNAADFLNRAKK------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 203 lsapqyrvygpawedpdvpddalpdgettnraiellqelkDRRFFLAVGYLKPHLPFVAPKKYYDLYRKEDIPLaanpfp 282
Cdd:cd16027 141 ----------------------------------------GQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKV------ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 283 pkdcPPialtnwgelrayqgipaagPLPDS--MARDLVHgYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHL 360
Cdd:cd16027 175 ----PP-------------------YLPDTpeVREDLAD-YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPF 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 361 gdhgLWCKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLFENPQRPWQKAAF 440
Cdd:cd16027 231 ----PRAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGRDYVF 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238332949 441 SQYPRGKVMGY---SMRTDRYRYTeWRPSgggepvAVELYDHTTDPLENVNLAGRPEYKDLVAQLHQQLEA 508
Cdd:cd16027 307 AERDRHDETYDpirSVRTGRYKYI-RNYM------PEELYDLKNDPDELNNLADDPEYAEVLEELRAALDA 370
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
43-508 |
1.36e-84 |
|
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: 268.63 E-value: 1.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKtlPDV 121
Cdd:cd16031 4 NIIFILTDDHRYDAlGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFD--ASQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 ITLPQHFKNHGYHTQGLSK--IYHGGLDDPASWSvpHWSpSKPMYGKPETLADLDRRREemRKKAGPATRVLekdpktgi 199
Cdd:cd16031 82 PTYPKLLRKAGYQTAFIGKwhLGSGGDLPPPGFD--YWV-SFPGQGSYYDPEFIENGKR--VGQKGYVTDII-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 200 plrlsapqyrvygpawedpdvpddalpdgetTNRAIELLQEL-KDRRFFLAVGYLKPHLPFVAPKKYYDLYRKEDIPLAA 278
Cdd:cd16031 149 -------------------------------TDKALDFLKERdKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 279 N----PFPPKdcpPIALTNWgeLRAYQGIPAAGPLPDSMARDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWG 354
Cdd:cd16031 198 TfdddDYAGR---PEWAREQ--RNRIRGVLDGRFDTPEKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 355 DHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLFENPQ-R 433
Cdd:cd16031 273 DNGFFLGEHGLFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKpV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 434 PWQKAAFSQY--PRGKVMGYSM---RTDRYRYTEWRpsggGEPVAVELYDHTTDPLENVNLAGRPEYKDLVAQLHQQLEA 508
Cdd:cd16031 353 DWRKEFYYEYyeEPNFHNVPTHegvRTERYKYIYYY----GVWDEEELYDLKKDPLELNNLANDPEYAEVLKELRKRLEE 428
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-506 |
7.15e-80 |
|
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: 255.61 E-value: 7.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDT----TRVYDLQTHFRKT 117
Cdd:cd16033 2 NILFIMTDQQRYDTlGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEhgvlNNVENAGAYSRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 118 LPDVITLPQHFKNHGYHTqglskIYHGglddpaSWsvpHWSPSKpmygkpetladldrrreemrkkaGPATRvlekdpkt 197
Cdd:cd16033 82 PPGVETFSEDLREAGYRN-----GYVG------KW---HVGPEE-----------------------TPLDY-------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 198 GIplrlsapqyrvygpaweDPDVPDDALPDGETTNRAIELLQELK--DRRFFLAVGYLKPHLPFVAPKKYYDLYRKEDIP 275
Cdd:cd16033 117 GF-----------------DEYLPVETTIEYFLADRAIEMLEELAadDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 276 LAAN---PFPPKdcPPI---ALTNWGELRAYqgipaagplpDSMARDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDSTI 349
Cdd:cd16033 180 LPESfadDFEDK--PYIyrrERKRWGVDTED----------EEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 350 VVLWGDHGWHLGDHGLWCKHTN-FETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLF 428
Cdd:cd16033 248 VIFTSDHGDALGAHRLWDKGPFmYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 429 ENPQRP-WQKAAFSQYPRGKVMGYSM--RTDRYRYTeWRPSGGGepvavELYDHTTDPLENVNLAGRPEYKDLVAQLHQQ 505
Cdd:cd16033 328 RGEQPEdWRDEVVTEYNGHEFYLPQRmvRTDRYKYV-FNGFDID-----ELYDLESDPYELNNLIDDPEYEEILREMRTR 401
|
.
gi 1238332949 506 L 506
Cdd:cd16033 402 L 402
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-506 |
1.45e-78 |
|
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: 250.94 E-value: 1.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQ----QAVCSPSRTSLLLGRRpdttrVYDLQ-THFRK 116
Cdd:cd16155 4 NILFILADDQRADTiGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGRT-----LFHAPeGGKAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 117 TLPDVITLPQHFKNHGYHTQGLSKiyhgglddpasWSVPHwspskpmygkpetladldrrreemrkkagpatrvlekdpk 196
Cdd:cd16155 79 IPSDDKTWPETFKKAGYRTFATGK-----------WHNGF---------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 197 tgiplrlsapqyrvygpawedpdvpddalpdgetTNRAIELLQELKDRR--FFLAVGYLKPHLPFVAPKKYYDLYRKEDI 274
Cdd:cd16155 108 ----------------------------------ADAAIEFLEEYKDGDkpFFMYVAFTAPHDPRQAPPEYLDMYPPETI 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 275 PLAAN--PFPPKDcppialTNWGELRAYQGipAAGP-LPDSMARDLVHgYYAATSYVDAQIGRLLAEVDRLGLRDSTIVV 351
Cdd:cd16155 154 PLPENflPQHPFD------NGEGTVRDEQL--APFPrTPEAVRQHLAE-YYAMITHLDAQIGRILDALEASGELDNTIIV 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 352 LWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQPhPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLFENP 431
Cdd:cd16155 225 FTSDHGLAVGSHGLMGKQNLYEHSMRVPLIISGPGIP-KGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGE 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238332949 432 QRPWQKAAFSQYprgkvMGY--SMRTDRYRYTEWRPSGGgepvAVELYDHTTDPLENVNLAGRPEYKDLVAQLHQQL 506
Cdd:cd16155 304 KKAVRDTLYGAY-----RDGqrAIRDDRWKLIIYVPGVK----RTQLFDLKKDPDELNNLADEPEYQERLKKLLAEL 371
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-489 |
9.54e-75 |
|
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: 241.70 E-value: 9.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYdlqTHFRKTLPDV 121
Cdd:cd16034 3 NILFIFADQHRAQAlGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF---GNDVPLPPDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 ITLPQHFKNHGYHTQGLSKiYHggLDDPASWSVPHWSPSKP-----------------MYGKPetladldrrreemrkka 184
Cdd:cd16034 80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNP----------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 185 gpatRVLEKDPKTgiplrlsaPQYRVYGPAWEdpdvpddalpdgetTNRAIELLQELKDRR--FFLAVGYLKPHLPFV-A 261
Cdd:cd16034 140 ----HYYDDDGKR--------IYIKGYSPDAE--------------TDLAIEYLENQADKDkpFALVLSWNPPHDPYTtA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 262 PKKYYDLYRKEDIPLaanpfpPKDCPPIALTNWGELRAYqgipaagplpdsmardlvHGYYAATSYVDAQIGRLLAEVDR 341
Cdd:cd16034 194 PEEYLDMYDPKKLLL------RPNVPEDKKEEAGLREDL------------------RGYYAMITALDDNIGRLLDALKE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 342 LGLRDSTIVVLWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEG 421
Cdd:cd16034 250 LGLLENTIVVFTSDHGDMLGSHGLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEG 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238332949 422 TSLVPLFENPQRPWQKAA-------FSQYPRGKVMGYS-MRTDRYRYTEWRpsgGGEPVaveLYDHTTDPLENVNL 489
Cdd:cd16034 330 RDLSPLLLGGKDDEPDSVllqcfvpFGGGSARDGGEWRgVRTDRYTYVRDK---NGPWL---LFDNEKDPYQLNNL 399
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
43-506 |
3.61e-74 |
|
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: 241.78 E-value: 3.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKTLPdv 121
Cdd:cd16028 2 NVLFITADQWRADClSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDARHL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 iTLPQHFKNHGYhtqglskiyhggldDPAswsvphwspskpMYGKPETLADLDRRreemrKKAGPATRVLEkdpktgipl 201
Cdd:cd16028 80 -TLALELRKAGY--------------DPA------------LFGYTDTSPDPRGL-----APLDPRLLSYE--------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 202 rLSAPQYRVYGPaweDPDVPDDalpDGET---TNRAIELLQELKDRRFFLAVGYLKPHLPFVAPKKYYDLYRKEDIPL-- 276
Cdd:cd16028 119 -LAMPGFDPVDR---LDEYPAE---DSDTaflTDRAIEYLDERQDEPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpi 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 277 -AANPFPPKDCPPIaLTNWGELR----AYQGIPAAGPLPDSMARDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVV 351
Cdd:cd16028 192 rAESLAAEAAQHPL-LAAFLERIeslsFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 352 LWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQP---HPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLF 428
Cdd:cd16028 271 FTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRREadaTRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 429 ENPQ-RPWQKAAFSQYPRGKVMGYS----------------MRTDRYRYTEWrpsGGGEPVaveLYDHTTDPLENVNLAG 491
Cdd:cd16028 351 AGAQpSDWRDAVHYEYDFRDVSTRRpqealglspdecslavIRDERWKYVHF---AALPPL---LFDLKNDPGELRDLAA 424
|
490
....*....|....*
gi 1238332949 492 RPEYKDLVAQLHQQL 506
Cdd:cd16028 425 DPAYAAVVLRYAQKL 439
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
39-506 |
7.15e-70 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 231.87 E-value: 7.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 39 SGKYNVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKT 117
Cdd:PRK13759 4 TKKPNIILIMVDQMRGDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 118 LPDviTLPQHFKNHGYHTQGLSKIyhgglddpaswsvpHWSPSKPMYGKPETLADlDRRREEMRKKAGPA---------- 187
Cdd:PRK13759 84 YKN--TLPQEFRDAGYYTQCIGKM--------------HVFPQRNLLGFHNVLLH-DGYLHSGRNEDKSQfdfvsdylaw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 188 --TRVLEKDPK-TGIPLRLSAPQYRVYgpawedpDVPDDALPDGETTNRAIELLQElKDRR--FFLAVGYLKPHLPFVAP 262
Cdd:PRK13759 147 lrEKAPGKDPDlTDIGWDCNSWVARPW-------DLEERLHPTNWVGSESIEFLRR-RDPTkpFFLKMSFARPHSPYDPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 263 KKYYDLYRKEDIPLaanpfppkdcPPIAltNWGEL-----RAYQGIPAAGPLPDSMARDLVHGYYAATSYVDAQIGRLLA 337
Cdd:PRK13759 219 KRYFDMYKDADIPD----------PHIG--DWEYAedqdpEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 338 EVDRLGLRDSTIVVLWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPG---QPHPGAKTDALVEFVDIYPTLCELCGLP 414
Cdd:PRK13759 287 ALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 415 IPEGLEGTSLVPLFENPQRPWQKaafsqYPRGK-VMGYS----MRTDRYRYTeWRPSGGGEpvavELYDHTTDPLENVNL 489
Cdd:PRK13759 367 IPDDVDGRSLKNLIFGQYEGWRP-----YLHGEhALGYSsdnyLTDGKWKYI-WFSQTGEE----QLFDLKKDPHELHNL 436
|
490
....*....|....*..
gi 1238332949 490 AGRPEYKDLVAQLHQQL 506
Cdd:PRK13759 437 SPSEKYQPRLREMRKKL 453
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-483 |
3.43e-69 |
|
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: 224.73 E-value: 3.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKTLPdv 121
Cdd:cd16037 2 NILIIMSDEHNPDAmGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVP-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 iTLPQHFKNHGYHTQGLSKIYHGGLDDPASWsvphwspskpmygkpetlaDLDRRReemrkkagpatrvlekdpktgipl 201
Cdd:cd16037 80 -SWGHALRAAGYETVLIGKLHFRGEDQRHGF-------------------RYDRDV------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 202 rlsapqyrvygpawedpdvpddalpdgetTNRAIELLQE--LKDRRFFLAVGYLKPHLPFVAPKKYYDLYRKEdiplaan 279
Cdd:cd16037 116 -----------------------------TEAAVDWLREeaADDKPWFLFVGFVAPHFPLIAPQEFYDLYVRR------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 280 pfppkdcppialtnwgeLRAyqgipaagplpdsmardlvhGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWH 359
Cdd:cd16037 160 -----------------ARA--------------------AYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDM 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 360 LGDHGLWCKHTNFETATRSLLIFRVPGQPhPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLFENPqRPWQKAA 439
Cdd:cd16037 203 LGERGLWGKSTMYEESVRVPMIISGPGIP-AGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGP-DDPDRVV 280
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1238332949 440 FSQYPRG--KVMGYSMRTDRY---RYTEWRPsgggepvavELYDHTTDP 483
Cdd:cd16037 281 FSEYHAHgsPSGAFMLRKGRWkyiYYVGYPP---------QLFDLENDP 320
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
43-423 |
3.58e-67 |
|
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: 216.53 E-value: 3.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKTLPDV 121
Cdd:cd16022 2 NILLIMTDDLGYDDlGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 ITLPQHFKNHGYHTQglskiyhgglddpaswsvphwspskpMYGKpetladldrrreemrkkagpatrvlekdpktgipl 201
Cdd:cd16022 82 PTLAELLKEAGYRTA--------------------------LIGK----------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 202 rlsapqyrvygpaWEDpdvpddalpdgettnRAIELLQEL-KDRRFFLAVGYLKPHLPFVapkkyydlyrkediplaanp 280
Cdd:cd16022 101 -------------WHD---------------EAIDFIERRdKDKPFFLYVSFNAPHPPFA-------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 281 fppkdcppialtnwgelrayqgipaagplpdsmardlvhgYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHL 360
Cdd:cd16022 133 ----------------------------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDML 172
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238332949 361 GDHGL-WCKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTS 423
Cdd:cd16022 173 GDHGLrGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-506 |
1.05e-66 |
|
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: 221.72 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTtRVYDLQTHFRKtlPDV 121
Cdd:cd16150 2 NIVIFVADQLRADSlGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHV-NGHRTLHHLLR--PDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 ITLPQHFKNHGYHTqglskiYHGGLDDpaswsvphwspskpmygkpetlaDLDRRReemrkkagpatrvlekdpktgipl 201
Cdd:cd16150 79 PNLLKTLKDAGYHV------AWAGKND-----------------------DLPGEF------------------------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 202 rlsapqyrvygpAWEDPDVPDDAlpdgeTTNRAIELLQELK-DRRFFLAVGYLKPHLPFVAPKKYYDLYRKEDIPLAANP 280
Cdd:cd16150 106 ------------AAEAYCDSDEA-----CVRTAIDWLRNRRpDKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPPRRPP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 281 FPPKDCPPIALtnwgELRAYQGIpaaGPLPDSMARDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHL 360
Cdd:cd16150 169 GLRAKGKPSML----EGIEKQGL---DRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 361 GDHGLWCKHTN-FETA-TRSLLIFRVPGQPhPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLFENPQRPWQKA 438
Cdd:cd16150 242 GDYGLVEKWPNtFEDClTRVPLIIKPPGGP-AGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAGETEEHRDA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 439 AFS---------------------QYPR----------GKVMgySMRTDRYRYTeWRPSGGGepvavELYDHTTDPLENV 487
Cdd:cd16150 321 VFSeggrlhgeeqamegghgpydlKWPRllqqeeppehTKAV--MIRTRRYKYV-YRLYEPD-----ELYDLEADPLELH 392
|
490
....*....|....*....
gi 1238332949 488 NLAGRPEYKDLVAQLHQQL 506
Cdd:cd16150 393 NLIGDPAYAEIIAEMKQRL 411
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
43-514 |
2.77e-65 |
|
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: 217.42 E-value: 2.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDD-----LrpeaGCYGVPIIKTPHIDALASQGLLFNRAYcQQAVCSPSRTSLLLGRRPDTTRVYDlqTHFRKT 117
Cdd:cd16146 2 NVILILTDDqgygdL----GFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWH--TILGRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 118 L--PDVITLPQHFKNHGYHTqGLSKIYHGGLDDPaswsvphwspskpmygkpetladldrrreeMRkkagpatrvlekdp 195
Cdd:cd16146 75 RmrLDETTLAEVFKDAGYRT-GIFGKWHLGDNYP------------------------------YR-------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 196 ktgiplrlsaPQYR----VYG---------PAWEDPDVPDDALPDGET------------TNRAIELLQELKDRRFFLAV 250
Cdd:cd16146 110 ----------PQDRgfdeVLGhggggigqyPDYWGNDYFDDTYYHNGKfvktegyctdvfFDEAIDFIEENKDKPFFAYL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 251 GYLKPHLPFVAPKKYYDLYRKEDiplaanpfppkdcppialtnwgelrayqgipaagpLPDSMARdlvhgYYAATSYVDA 330
Cdd:cd16146 180 ATNAPHGPLQVPDKYLDPYKDMG-----------------------------------LDDKLAA-----FYGMIENIDD 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 331 QIGRLLAEVDRLGLRDSTIVVLWGDHGWHLGDHGLW------CKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIY 404
Cdd:cd16146 220 NVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLL 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 405 PTLCELCGLPIPEG--LEGTSLVPLFENPQRPW-QKAAFSQYPRGKVMGY-----SMRTDRYRYTewrpsgGGEPVAVEL 476
Cdd:cd16146 300 PTLLDLCGVKLPEGikLDGRSLLPLLKGESDPWpERTLFTHSGRWPPPPKkkrnaAVRTGRWRLV------SPKGFQPEL 373
|
490 500 510
....*....|....*....|....*....|....*...
gi 1238332949 477 YDHTTDPLENVNLAGrpEYKDLVAQLHQQLEAGWKAAK 514
Cdd:cd16146 374 YDIENDPGEENDVAD--EHPEVVKRLKAAYEAWWDDVK 409
|
|
| chol_sulfatase |
TIGR03417 |
choline-sulfatase; |
43-510 |
2.78e-61 |
|
choline-sulfatase;
Pssm-ID: 274570 [Multi-domain] Cd Length: 500 Bit Score: 209.55 E-value: 2.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYG-VPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKTLPd 120
Cdd:TIGR03417 4 NILIIMADQLNGTLlPDYGpARWLHAPNLKRLAARSVVFDNAYCASPLCAPSRASFMSGQLPSRTGAYDNAAEFASDIP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 121 viTLPQHFKNHGYHTQGLSKIYHGGLDD-------------PASWSvphWSPSkpmYGKPETLADLDRRREEMRKkAGPA 187
Cdd:TIGR03417 83 --TYAHYLRRAGYRTALSGKMHFCGPDQlhgfeerlttdiyPADFG---WTPD---WRKPGERIDWYHNMGSVTG-AGPC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 188 TRVLEKDpktgiplrlsapqyrvygpawEDPDVPDDAlpdgetTNRAIELLQELKDRRFFLAVGYLKPHLPFVAPKKYYD 267
Cdd:TIGR03417 154 ERTNQLD---------------------YDDEVAFHA------RQKLYDLARGKDDRPFCLTVSFTHPHDPYVIRRKYWD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 268 LYRKEDIPL--AANPFPPKDCPPIALTNWGELRAYqgipaagPLPDSMARDLVHGYYAATSYVDAQIGRLLAEVDRLGLR 345
Cdd:TIGR03417 207 LYEDCEILMpeVAIPYAEQDPHSQRLLDACDLRNF-------PITDEQIRRARRAYFGAISYIDDKIGELLDTLEETRQA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 346 DSTIVVLWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQPHPGaKTDALVEFVDIYPTLCELCGLPIPEG---LEGT 422
Cdd:TIGR03417 280 DDTIIVFTSDHGDMLGERGLWYKMSFFEGSARVPLMIAAPGRFAPG-RVDAPVSTLDLLPTLVDLAGGDMDEVapwTDGR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 423 SLVPLFENPQRPwqKAAFSQY----PRGKVMgySMRTDRYRY--TEWRPSgggepvavELYDHTTDPLENVNLAGRPEYK 496
Cdd:TIGR03417 359 SLVPHLQGKGGH--DEVIGEYaaegSIAPLV--MIRRGRYKFvyCEADPD--------QLYDLEADPHELTNLADDPAHA 426
|
490
....*....|....
gi 1238332949 497 DLVAQLHQQLEAGW 510
Cdd:TIGR03417 427 DTLAAFRAEAAARW 440
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-508 |
3.36e-61 |
|
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: 207.01 E-value: 3.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDL-RPEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYD------------ 109
Cdd:cd16144 2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipgrrgppdnt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 110 --LQTHFRKTLP-DVITLPQHFKNHGYHTQGLSK--IYHGGLDDPAS----WSVPHWSPSKPMYGKPEtladldrrreem 180
Cdd:cd16144 82 klIPPPSTTRLPlEEVTIAEALKDAGYATAHFGKwhLGGEGGYGPEDqgfdVNIGGTGNGGPPSYYFP------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 181 rkkagpatrvlekdpktgiplrlsapqYRVYGPAWEDPDvPDDALPDGeTTNRAIELLQELKDRRFFLAVGYLKPHLPFV 260
Cdd:cd16144 150 ---------------------------PGKPNPDLEDGP-EGEYLTDR-LTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 261 APKKYYDLYRKedipLAANPFPPKDCPpialtnwgelrayqgipaagplpdsmardlvhgYYAA-TSYVDAQIGRLLAEV 339
Cdd:cd16144 201 ARPELIEKYEK----KKKGLRKGQKNP---------------------------------VYAAmIESLDESVGRILDAL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 340 DRLGLRDSTIVVLWGDHG-WHLGDHGLWC-------KHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELC 411
Cdd:cd16144 244 EELGLADNTLVIFTSDNGgLSTRGGPPTSnaplrggKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELA 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 412 GLPIPEG--LEGTSLVPLFENPQRPWQKAAF-----SQYPRGKVMGYSMRTDRYRYTEWRpsgggEPVAVELYDHTTDPL 484
Cdd:cd16144 324 GGPLPPPqhLDGVSLVPLLKGGEADLPRRALfwhfpHYHGQGGRPASAIRKGDWKLIEFY-----EDGRVELYNLKNDIG 398
|
490 500
....*....|....*....|....
gi 1238332949 485 ENVNLAGrpEYKDLVAQLHQQLEA 508
Cdd:cd16144 399 ETNNLAA--EMPEKAAELKKKLDA 420
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
42-484 |
1.77e-58 |
|
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: 197.03 E-value: 1.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 42 YNVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKTLPd 120
Cdd:cd16032 1 PNILLIMADQLTAAAlPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 121 viTLPQHFKNHGYHTQgLSkiyhgglddpaswsvphwspskpmyGK-----PETLADLDrrreemrkkagpatrvlekdp 195
Cdd:cd16032 80 --TFAHYLRAAGYRTA-LS-------------------------GKmhfvgPDQLHGFD--------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 196 ktgiplrlsapqyrvYgpawedpdvpddalpDGETTNRAIELLQEL---KDRR-FFLAVGYLKPHLPFVAPKKYYDLYrk 271
Cdd:cd16032 111 ---------------Y---------------DEEVAFKAVQKLYDLargEDGRpFFLTVSFTHPHDPYVIPQEYWDLY-- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 272 ediplaanpfppkdcppialtnwgeLRAyqgipaagplpdsmARdlvHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVV 351
Cdd:cd16032 159 -------------------------VRR--------------AR---RAYYGMVSYVDDKVGQLLDTLERTGLADDTIVI 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 352 LWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQPHPGAKTDAlVEFVDIYPTLCELCG---LPIPEGLEGTSLVPLF 428
Cdd:cd16032 197 FTSDHGDMLGERGLWYKMSFFEGSARVPLIISAPGRFAPRRVAEP-VSLVDLLPTLVDLAGggtAPHVPPLDGRSLLPLL 275
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 429 ENPQRPWQKAAFSQYPRGKVMG--YSMRTDRYRY--TEWRPSgggepvavELYDHTTDPL 484
Cdd:cd16032 276 EGGDSGGEDEVISEYLAEGAVApcVMIRRGRWKFiyCPGDPD--------QLFDLEADPL 327
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-426 |
4.67e-56 |
|
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: 188.91 E-value: 4.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVydlqtHFRKTLPDV 121
Cdd:cd16148 2 NVILIVIDSLRADHlGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV-----WGGPLEPDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 ITLPQHFKNHGYHTQGLSkiyhgglddpaswSVPHWSPSkpmygkpetlADLDRRREEMRKKAGPatrvlekdpktgipl 201
Cdd:cd16148 77 PTLAEILRKAGYYTAAVS-------------SNPHLFGG----------PGFDRGFDTFEDFRGQ--------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 202 rlsapqyrvygpawEDPDVPDDALPDGETTNRAIELLQELK-DRRFFLAVGYLKPHLPFvapkkyydlyrkediplaanp 280
Cdd:cd16148 119 --------------EGDPGEEGDERAERVTDRALEWLDRNAdDDPFFLFLHYFDPHEPY--------------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 281 fppkdcppialtnwgelrayqgipaagplpdsmardlvhGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHL 360
Cdd:cd16148 164 ---------------------------------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEF 204
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238332949 361 GDHGLWCKH--TNFETATRSLLIFRVPGQPhPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVP 426
Cdd:cd16148 205 GEHGLYWGHgsNLYDEQLHVPLIIRWPGKE-PGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-490 |
1.17e-53 |
|
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: 186.65 E-value: 1.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRP-EAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYD--LQTHFRKTLP 119
Cdd:cd16145 2 NIIFILADDLGYgDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGnsEPGGQDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 120 DVITLPQHFKNHGYHTQGLSKIyhgGLDDPASWSVP------HWspskpmYGK----------PETLadldRRREEmrkk 183
Cdd:cd16145 82 DDVTLAEVLKKAGYATAAFGKW---GLGGPGTPGHPtkqgfdYF------YGYldqvhahnyyPEYL----WRNGE---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 184 agpatrvlekdpKTGIPlrlsapqyrvyGPAWEDPDVPDDALPDGET------TNRAIELLQELKDRRFFLAVGYLKPHL 257
Cdd:cd16145 145 ------------KVPLP-----------NNVIPPLDEGNNAGGGGGTyshdlfTDEALDFIRENKDKPFFLYLAYTLPHA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 258 PFVAPKKYYDLYRkediplaanpfpPKDCPPIALTNWGELRAyqgipaagplpdsmardlvhGYYAATSYVDAQIGRLLA 337
Cdd:cd16145 202 PLQVPDDGPYKYK------------PKDPGIYAYLPWPQPEK--------------------AYAAMVTRLDRDVGRILA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 338 EVDRLGLRDSTIVVLWGDHGWHLgDHGLWCKHTNFETA------TRSL--------LIFRVPGQPHPGAKTDALVEFVDI 403
Cdd:cd16145 250 LLKELGIDENTLVVFTSDNGPHS-EGGSEHDPDFFDSNgplrgyKRSLyeggirvpFIARWPGKIPAGSVSDHPSAFWDF 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 404 YPTLCELCGLPIPEGLEGTSLVP-LFENPQRpwQKAAFSQYPRGKVMG-YSMRTDRYRYTewRPSGGGEPvaVELYDHTT 481
Cdd:cd16145 329 MPTLADLAGAEPPEDIDGISLLPtLLGKPQQ--QQHDYLYWEFYEGGGaQAVRMGGWKAV--RHGKKDGP--FELYDLST 402
|
....*....
gi 1238332949 482 DPLENVNLA 490
Cdd:cd16145 403 DPGETNNLA 411
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-508 |
1.63e-53 |
|
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: 185.12 E-value: 1.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 41 KYNVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYdlqtHFRKTLP 119
Cdd:cd16152 1 KPNVIVFFTDQQRWDTlGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF----RNGIPLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 120 -DVITLPQHFKNHGYHTQglskiYHGglddpaSWsvpHwspskpmygkpetLAdldrrreemrkkagpatrvlekdpktg 198
Cdd:cd16152 77 aDEKTLAHYFRDAGYETG-----YVG------KW---H-------------LA--------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 199 iplrlsapQYRVygpawedpdvpdDALpdgetTNRAIELLQEL-KDRRFFLAVGYLKPHLP-----FVAPKKYYDLYrke 272
Cdd:cd16152 103 --------GYRV------------DAL-----TDFAIDYLDNRqKDKPFFLFLSYLEPHHQndrdrYVAPEGSAERF--- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 273 diplaANPFPPKDcppialtnwgeLRAYQGIPAAGpLPDsmardlvhgYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVL 352
Cdd:cd16152 155 -----ANFWVPPD-----------LAALPGDWAEE-LPD---------YLGCCERLDENVGRIRDALKELGLYDNTIIVF 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 353 WGDHGWHL----GDHglwcKHTNFETATRSLLIFRVPGQPHpGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLF 428
Cdd:cd16152 209 TSDHGCHFrtrnAEY----KRSCHESSIRVPLVIYGPGFNG-GGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 429 ENPQRPWQKAAFSQYPRGKVmGYSMRTDRYRY-------TEWRPSGGGEPVAVELYDHTTDPLENVNLAGRPEYKDLVAQ 501
Cdd:cd16152 284 DGKVEDWRNEVFIQISESQV-GRAIRTDRWKYsvaapdkDGWKDSGSDVYVEDYLYDLEADPYELVNLIGRPEYREVAAE 362
|
....*..
gi 1238332949 502 LHQQLEA 508
Cdd:cd16152 363 LRERLLA 369
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-425 |
2.25e-53 |
|
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: 182.19 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 41 KYNVLMIAVDDLRPEA-GCYGVPI----------IKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYd 109
Cdd:cd16153 1 KPNILWIITDDQRVDSlSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 110 lqtHFRKTLP----DVITLPQHFKNHGYHTQglskiyhgglddpaswsvphwspskpMYGKpetladldrrreemrKKAG 185
Cdd:cd16153 80 ---GFEAAHPaldhGLPTFPEVLKKAGYQTA--------------------------SFGK---------------SHLE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 186 PATRVLEKDPKTgiplrlsapQYRVYGPAWEDPDvpddalpdgettnraiellqelKDRRFFLAVGYLKPHLPFVAPKKY 265
Cdd:cd16153 116 AFQRYLKNANQS---------YKSFWGKIAKGAD----------------------SDKPFFVRLSFLQPHTPVLPPKEF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 266 YDLYRkediplaanpfppkdcppialtnwgelrayqgipaagplpdsmardlvhgYYAATSYVDAQIGRLLAEVDRLGL- 344
Cdd:cd16153 165 RDRFD--------------------------------------------------YYAFCAYGDAQVGRAVEAFKAYSLk 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 345 --RDSTIVVLWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQPHPGAKT--DALVEFVDIYPTLCELCGLPI--PEG 418
Cdd:cd16153 195 qdRDYTIVYVTGDHGWHLGEQGILAKFTFWPQSHRVPLIVVSSDKLKAPAGKvrHDFVEFVDLAPTLLAAAGVDVdaPDY 274
|
....*..
gi 1238332949 419 LEGTSLV 425
Cdd:cd16153 275 LDGRDLF 281
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
43-506 |
1.42e-52 |
|
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: 185.28 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPE-AGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDlqthfrKTLP-- 119
Cdd:cd16156 2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWT------NCMAlg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 120 -DVITLPQHFKNHGYHTQGLSKIYHGGLDD------PASWSVPHWspskpmYGKPETLADLDRrrEEMRKKagpaTRVLE 192
Cdd:cd16156 76 dNVKTIGQRLSDNGIHTAYIGKWHLDGGDYfgngicPQGWDPDYW------YDMRNYLDELTE--EERRKS----RRGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 193 KDPKTGIPLRLSApQYRVygpawedpdvpddalpdgetTNRAIELLQELKDRRFFLAVGYLKPHLPFVAPKKYYDLYRKE 272
Cdd:cd16156 144 SLEAEGIKEEFTY-GHRC--------------------TNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 273 DIPLAANPFPPKDCPPIALTNWGELRayqgipaagPLPDSMARDLVH-GYYAATSYVDAQIGRLLAEVDRlgLRDSTIVV 351
Cdd:cd16156 203 EFPKGENAYDDLENKPLHQRLWAGAK---------PHEDGDKGTIKHpLYFGCNSFVDYEIGRVLDAADE--IAEDAWVI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 352 LWGDHGWHLGDHGLWCKHTN-FETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLFEN 430
Cdd:cd16156 272 YTSDHGDMLGAHKLWAKGPAvYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIED 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 431 PQRPWQKAAFSQYPRgkvmgYSMRTDRYrytewrpsGGGEPV-AV---------------ELYDHTTDPLENVNLAGRPE 494
Cdd:cd16156 352 PEIPENRGVFVEFGR-----YEVDHDGF--------GGFQPVrCVvdgryklvinllstdELYDLEKDPYEMHNLIDDPD 418
|
490
....*....|..
gi 1238332949 495 YKDLVAQLHQQL 506
Cdd:cd16156 419 YADVRDQLHDEL 430
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-426 |
1.37e-43 |
|
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: 155.09 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYD--LQTHFRKT-- 117
Cdd:cd16149 2 NILFILTDDQGPWAlGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDwiVEGSHGKTkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 118 ----LPDVITLPQHFKNHGYHTqGLSKIYHGGLDdpaswsvphwspskpmygkpeTLADLDRRREemrkkagpatrvlek 193
Cdd:cd16149 82 pegyLEGQTTLPEVLQDAGYRC-GLSGKWHLGDD---------------------AADFLRRRAE--------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 194 dpktgiplrlsapqyrvygpawedpdvpddalpdgettnraiellqelKDRRFFLAVGYLKPHLPfvapkkyydlyrked 273
Cdd:cd16149 125 ------------------------------------------------AEKPFFLSVNYTAPHSP--------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 274 iplaanpfppkdcppialtnwgelrayqgipaagplpdsmardlvHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLW 353
Cdd:cd16149 142 ---------------------------------------------WGYFAAVTGVDRNVGRLLDELEELGLTENTLVIFT 176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 354 GDHGWHLGDHGLWCKHT-----NF-ETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEG--LEGTSLV 425
Cdd:cd16149 177 SDNGFNMGHHGIWGKGNgtfplNMyDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADprLPGRSFA 256
|
.
gi 1238332949 426 P 426
Cdd:cd16149 257 D 257
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-489 |
1.56e-43 |
|
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: 158.53 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEA-GCYGVPIIKTPHIDALASQGLLFNRAYcQQAVCSPSRTSLLLGRRPDTTRVydlqtHFRKTLPDV 121
Cdd:cd16151 2 NIILIMADDLGYECiGCYGGESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYV-----VFGYLDPKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 ITLPQHFKNHGYHT----------QGLSKIY--HGGLDDPASWSVPHwspskpmygkpetladldrrreEMRKKAGPATR 189
Cdd:cd16151 76 KTFGHLLKDAGYATaiagkwqlggGRGDGDYphEFGFDEYCLWQLTE----------------------TGEKYSRPATP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 190 VLE----KDPKTGiplrlsapqYRVYGPawedpDVpddalpdgeTTNRAIELLQELKDRRFFLavgylkphlpfvapkkY 265
Cdd:cd16151 134 TFNirngKLLETT---------EGDYGP-----DL---------FADFLIDFIERNKDQPFFA----------------Y 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 266 YdlyrkediplaanpfppkdcpPIALTNWgelrayqgiPAaGPLPDSMARDLVHG-------YYAA-TSYVDAQIGRLLA 337
Cdd:cd16151 175 Y---------------------PMVLVHD---------PF-VPTPDSPDWDPDDKrkkddpeYFPDmVAYMDKLVGKLVD 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 338 EVDRLGLRDSTIVVLWGDHGWHLGDHGLWC-------KHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCEL 410
Cdd:cd16151 224 KLEELGLRENTIIIFTGDNGTHRPITSRTNgrevrggKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAEL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 411 CGLPIPEG--LEGTSLVPLF----ENPQRPWqkaaFSQYPRGKvmGYSMRTDRYRYTEWRPSGGGepvavELYDHTTDPL 484
Cdd:cd16151 304 AGAPLPEDypLDGRSFAPQLlgktGSPRREW----IYWYYRNP--HKKFGSRFVRTKRYKLYADG-----RFFDLREDPL 372
|
....*
gi 1238332949 485 ENVNL 489
Cdd:cd16151 373 EKNPL 377
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-490 |
5.88e-41 |
|
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: 151.95 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDL-RPEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYD-LQTHFRKTL-- 118
Cdd:cd16026 3 NIVVILADDLgYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGvVGPPGSKGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 119 PDVITLPQHFKNHGYHTQglskiyhgglddpaswsvphwspskpMYGK------PETLadldrrreemrkkagPATRVLe 192
Cdd:cd16026 83 PDEITIAEVLKKAGYRTA--------------------------LVGKwhlghqPEFL---------------PTRHGF- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 193 kDPKTGIPLrlSAPQYRvYGPAWEDPDVPDDALPDGET---------------TNRAIELLQELKDRRFFLAVGYLKPHL 257
Cdd:cd16026 121 -DEYFGIPY--SNDMWP-FPLYRNDPPGPLPPLMENEEvieqpadqssltqryTDEAVDFIERNKDQPFFLYLAHTMPHV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 258 PFVAPKKYydlyrkediplaanpfppkdcppialtnwgelrayQGIPAAGPLPDSMArdlvhgyyaatsYVDAQIGRLLA 337
Cdd:cd16026 197 PLFASEKF-----------------------------------KGRSGAGLYGDVVE------------ELDWSVGRILD 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 338 EVDRLGLRDSTIVVL------WGDHGWHLGDHGLW--CKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCE 409
Cdd:cd16026 230 ALKELGLEENTLVIFtsdngpWLEYGGHGGSAGPLrgGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 410 LCGLPIPEG--LEGTSLVPLFENPQRPWQKAAFSQYPRGKVMGYsmRTDRYRY---------TEWRPSGGGEPVAVELYD 478
Cdd:cd16026 310 LAGAPLPEDrvIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAV--RSGRWKLhlpttyrtgTDPGGLDPTKLEPPLLYD 387
|
490
....*....|..
gi 1238332949 479 HTTDPLENVNLA 490
Cdd:cd16026 388 LEEDPGETYNVA 399
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
43-489 |
1.94e-40 |
|
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: 150.67 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRP-EAGCYGVPIiKTPHIDALASQGLLFNRAYcQQAVCSPSRTSLLLGRrpDTTRV-YDLQTHFRKTLP- 119
Cdd:cd16025 4 NILLILADDLGFsDLGCFGGEI-PTPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGR--NHHQVgMGTMAELATGKPg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 120 -------DVITLPQHFKNHGYHTQGLSKiYHGGLDDpaswsvphwspskpMYgkpetladldrrreemrkkagpATRVLe 192
Cdd:cd16025 80 yegylpdSAATIAEVLKDAGYHTYMSGK-WHLGPDD--------------YY----------------------STDDL- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 193 kdpktgiplrlsapqyrvygpawedpdvpddalpdgetTNRAIELLQELK--DRRFFLAVGYLKPHLPFVAPKKYYDLYR 270
Cdd:cd16025 122 --------------------------------------TDKAIEYIDEQKapDKPFFLYLAFGAPHAPLQAPKEWIDKYK 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 271 -KED-------------------IPLAANPFPPKDcppiALTNWGEL----RAYQGipaagplpDSMArdlVhgyYAA-T 325
Cdd:cd16025 164 gKYDagwdalreerlerqkelglIPADTKLTPRPP----GVPAWDSLspeeKKLEA--------RRME---V---YAAmV 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 326 SYVDAQIGRLLAEVDRLGLRDSTIVVLWGD------HGW-HLGDHGL-WCKHTNFETATRSLLIFRVP-GQPHPGAKTDA 396
Cdd:cd16025 226 EHMDQQIGRLIDYLKELGELDNTLIIFLSDngasaePGWaNASNTPFrLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHQ 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 397 LVEFVDIYPTLCELCGLPIPEG--------LEGTSLVPLFENPQRPwqkaafsqyPRGKVMGYSMRTDRYRYTE-----W 463
Cdd:cd16025 306 FAHVIDIAPTILELAGVEYPKTvngvpqlpLDGVSLLPTLDGAAAP---------SRRRTQYFELFGNRAIRKGgwkavA 376
|
490 500
....*....|....*....|....*.
gi 1238332949 464 RPSGGGEPVAVELYDHTTDPLENVNL 489
Cdd:cd16025 377 LHPPPGWGDQWELYDLAKDPSETHDL 402
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
43-413 |
3.04e-37 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 139.09 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLR-PEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKTLPDv 121
Cdd:pfam00884 2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRTEP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 122 iTLPQHFKNHGYHTQGLSKiyhgglddpasWSVPHWSPSKPMYGKPETLADldrrreemrkkaGPATRVLEKDPKTgipl 201
Cdd:pfam00884 81 -SLPDLLKRAGYNTGAIGK-----------WHLGWYNNQSPCNLGFDKFFG------------RNTGSDLYADPPD---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 202 rlsapqyrvYGPAWEDPDVPDDALpdgetTNRAIELLQElKDRRFFLAVGYLKPHLPFVAPKKYYDLYRKediplaanpF 281
Cdd:pfam00884 133 ---------VPYNCSGGGVSDEAL-----LDEALEFLDN-NDKPFFLVLHTLGSHGPPYYPDRYPEKYAT---------F 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 282 PPKDCPpialtnwgelrayqgipaagplpdsmARDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHLG 361
Cdd:pfam00884 189 KPSSCS--------------------------EEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLG 242
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238332949 362 DHGLWCKHTNFETATRSL----LIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGL 413
Cdd:pfam00884 243 EGGGYLHGGKYDNAPEGGyrvpLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-490 |
8.65e-37 |
|
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: 140.41 E-value: 8.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRP-EAGCYGvP--IIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRV-YDLQTHFRKTL 118
Cdd:cd16143 2 NIVIILADDLGYgDISCYN-PdsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 119 --PDVITLPQHFKNHGYHTQGLSKiYHGGLDdpaswsvphWSPSKPMYGKPETLADLDrrreemrkkagpatrvLEKDPK 196
Cdd:cd16143 81 iePDRVTLAKMLKQAGYRTAMVGK-WHLGLD---------WKKKDGKKAATGTGKDVD----------------YSKPIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 197 TGiPLRLSAPQYrvYGpawedpdvpddaLPDGE----TTNRAIELLQEL--KDRRFFLAVGYLKPHLPFVAPKKyydlyr 270
Cdd:cd16143 135 GG-PLDHGFDYY--FG------------IPASEvlptLTDKAVEFIDQHakKDKPFFLYFALPAPHTPIVPSPE------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 271 kediplaanpfppkdcppialtnwgelraYQGIPAAGPLPDSMARdlvhgyyaatsyVDAQIGRLLAEVDRLGLRDSTIV 350
Cdd:cd16143 194 -----------------------------FQGKSGAGPYGDFVYE------------LDWVVGRILDALKELGLAENTLV 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 351 V-------LWGDHGWHLGDHGLWC-------KHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIP 416
Cdd:cd16143 233 IftsdngpSPYADYKELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 417 --EGLEGTSLVPLFENPQRPWQKAAFSQypRGKVMGYSMR---------TDRYRYTEWRPSGGGEPVAVELYDHTTDPLE 485
Cdd:cd16143 313 dnAAEDSFSFLPALLGPKKQEVRESLVH--HSGNGSFAIRkgdwklidgTGSGGFSYPRGKEKLGLPPGQLYNLSTDPGE 390
|
....*
gi 1238332949 486 NVNLA 490
Cdd:cd16143 391 SNNLY 395
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
41-493 |
1.63e-34 |
|
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: 134.21 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 41 KYNVLMIAVDDLRPEAGCYGVpiiKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQ------THF 114
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDP---MPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSppgggyPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 115 RKTLPDVITLPQHFKNHGYHTQGLSKIYHG-GLDDPASWSVPHWSPSKPMYgkpetladldrrreemrkkagpatrvlek 193
Cdd:cd16147 78 WQNGLERSTLPVWLQEAGYRTAYAGKYLNGyGVPGGVSYVPPGWDEWDGLV----------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 194 DPKTGIPLRLSAPQYRVYGPAWED---PDVpddalpdgeTTNRAIELLQEL--KDRRFFLAVGYLKPHLPFVAPKKYYDL 268
Cdd:cd16147 129 GNSTYYNYTLSNGGNGKHGVSYPGdylTDV---------IANKALDFLRRAaaDDKPFFLVVAPPAPHGPFTPAPRYANL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 269 YRKEDIPLAANPFPPKDcPPIAltNWgeLRAYqgipaAGPLPDSMAR-DLVHGYYAAT--SyVDAQIGRLLAEVDRLGLR 345
Cdd:cd16147 200 FPNVTAPPRPPPNNPDV-SDKP--HW--LRRL-----PPLNPTQIAYiDELYRKRLRTlqS-VDDLVERLVNTLEATGQL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 346 DSTIVVLWGDHGWHLGDHGL-WCKHTNFETATRSLLIFRVPGQPhPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSl 424
Cdd:cd16147 269 DNTYIIYTSDNGYHLGQHRLpPGKRTPYEEDIRVPLLVRGPGIP-AGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRS- 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238332949 425 vplfenpqrpWQKAAFSQYprgkvmgYSMRTDRYR----YTEWRPsggGEpvaVELYDHTTDPLENVNLAGRP 493
Cdd:cd16147 347 ----------CGDSNNNTY-------KCVRTVDDTynllYFEWCT---GF---RELYDLTTDPYQLTNLAGDL 396
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-430 |
3.17e-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: 117.31 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 42 YNVLMIAVDDLR-PEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYD-LQTHFRKTL- 118
Cdd:cd16035 1 PNILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLLs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 119 PDVITLPQHFKNHGYHTQglskiYHGglddpaSWsvpHWSpskpmygkpetladldrrreemrkkagpatrvlekdpktg 198
Cdd:cd16035 81 PDVPTLGHMLRAAGYYTA-----YKG------KW---HLS---------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 199 iplrlsapqyrvyGPAWEDPDVpddalpDGETTNRAIELLQELKDRR-----FFLAVGYLKPHlpfvapkkyydlyrkeD 273
Cdd:cd16035 107 -------------GAAGGGYKR------DPGIAAQAVEWLRERGAKNadgkpWFLVVSLVNPH----------------D 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 274 IPlaanpFPPKDcppiaLTNWGELRAYqgipaagplpdsmardlvhgYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLW 353
Cdd:cd16035 152 IM-----FPPDD-----EERWRRFRNF--------------------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFT 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 354 GDHGWHLGDHGLWCKHTN-FETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPE------GLEGTSLVP 426
Cdd:cd16035 202 SDHGEMGGAHGLRGKGFNaYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEArateapPLPGRDLSP 281
|
....
gi 1238332949 427 LFEN 430
Cdd:cd16035 282 LLTD 285
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
43-483 |
7.60e-27 |
|
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: 111.86 E-value: 7.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDD------LRPEAGcygvpIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDlqtHFRK 116
Cdd:cd16171 2 NVVMVMSDSfdgrltFRPGNQ-----VVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWN---NYKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 117 TLPDVITLPQHFKNHGYHTQGLSKIYHGGLDDPASWSVPHWSPSKPMY----GKPETLADLDRRReemrkkagpaTRVLE 192
Cdd:cd16171 74 LDPNYPTWMDRLEKHGYHTQKYGKLDYTSGHHSVSNRVEAWTRDVPFLlrqeGRPTVNLVGDRST----------VRVML 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 193 KDpktgiplrlsapqyrvygpaWEDPDVPDDALpdgetTNRAIELLQElkdrrFFLAVGYLKPHlpfvapkkyydlyrke 272
Cdd:cd16171 144 KD--------------------WQNTDKAVHWI-----RKEAPNLTQP-----FALYLGLNLPH---------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 273 diplaanPFPPkdcpPIALTNWG---ELRAYqgipaagplpdsmardlvhgYYAATSYVDAQIGRLLAEVDRLGLRDSTI 349
Cdd:cd16171 178 -------PYPS----PSMGENFGsirNIRAF--------------------YYAMCAETDAMLGEIISALKDTGLLDKTY 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 350 VVLWGDHGWHLGDHGLWCKHTNFETATRSLLIFRVPGQPhPGAKTDALVEFVDIYPTLCELCGLPIPEGLEGTSLVPLFE 429
Cdd:cd16171 227 VFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPGIK-AGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLS 305
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238332949 430 N----------PQRPWqkaAFSQYPRGKVMG--YSMRTDRYRYTEWrpsGGGEPVAVELYDHTTDP 483
Cdd:cd16171 306 EssikespsrvPHPDW---VLSEFHGCNVNAstYMLRTNSWKYIAY---ADGNSVPPQLFDLSKDP 365
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
43-507 |
5.05e-24 |
|
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: 105.22 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDL-RPEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYD--LQTHFRKTLP 119
Cdd:cd16158 3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPgvFYPGSRGGLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 120 -DVITLPQHFKNHGYHTQGLSKiYHGGLDDPASWSVPHWSPSKpMYGKPETLADldrrreemrkkaGPATRVLEKDPKTG 198
Cdd:cd16158 83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNGTYLPTHQGFDH-YLGIPYSHDQ------------GPCQNLTCFPPNIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 199 ---------IPLRLSAPQYRVYGPAWedpdvpddaLPDGET--TNRAIELLQE--LKDRRFFLAVGYLKPHLPFVAPKKY 265
Cdd:cd16158 149 cfggcdqgeVPCPLFYNESIVQQPVD---------LLTLEEryAKFAKDFIADnaKEGKPFFLYYASHHTHYPQFAGQKF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 266 ydlyrkediplaanpfppkdcppialtnwgelrayQGIPAAGPLPDSMARdlvhgyyaatsyVDAQIGRLLAEVDRLGLR 345
Cdd:cd16158 220 -----------------------------------AGRSSRGPFGDALAE------------LDGSVGELLQTLKENGID 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 346 DSTIVVLWGDHGWHL------GDHGLW-C-KHTNFETATRSLLIFRVPGQPHPGaKTDALVEFVDIYPTLCELCGLPIPE 417
Cdd:cd16158 253 NNTLVFFTSDNGPSTmrksrgGNAGLLkCgKGTTYEGGVREPAIAYWPGRIKPG-VTHELASTLDILPTIAKLAGAPLPN 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 418 -GLEGTSLVP-LFENPQRPWQKAAF-SQYPRGKVMGYSMRTDRYR---YTEWRPSGGGEP-----VAVE--------LYD 478
Cdd:cd16158 332 vTLDGVDMSPiLFEQGKSPRQTFFYyPTSPDPDKGVFAVRWGKYKahfYTQGAAHSGTTPdkdchPSAEltshdpplLFD 411
|
490 500
....*....|....*....|....*....
gi 1238332949 479 HTTDPLENVNLAGRPEYKDLVAQLHQQLE 507
Cdd:cd16158 412 LSQDPSENYNLLGLPEYNQVLKQIQQVKE 440
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-416 |
1.20e-23 |
|
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: 102.61 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDL-RPEAGCYGVPII---KTPHIDALASQGLLFNRAYCQQAvCSPSRTSLLLGR---RPDTTRVydLQTHFR 115
Cdd:cd16142 2 NILVILGDDIgWGDLGCYGGGIGrgaPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRhpiRTGLTTV--GLPGSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 116 KTLPD-VITLPQHFKNHGYHTQglskiyhgglddpaswsvphwspskpMYGKPEtLADLDRRR------EEMRkkagpat 188
Cdd:cd16142 79 GGLPPwEPTLAELLKDAGYATA--------------------------QFGKWH-LGDEDGRLptdhgfDEFY------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 189 rvlekdpktGIPLrlsapqYRVygpawedpdvpddalpDGETTNRAIELLQELK--DRRFFLAVGYLKPHLP-FVAPKky 265
Cdd:cd16142 125 ---------GNLY------HTI----------------DEEIVDKAIDFIKRNAkaDKPFFLYVNFTKMHFPtLPSPE-- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 266 ydlyrkediplaanpfppkdcppialtnwgelraYQGI-PAAGPLPDSMARdlvhgyyaatsyVDAQIGRLLAEVDRLGL 344
Cdd:cd16142 172 ----------------------------------FEGKsSGKGKYADSMVE------------LDDHVGQILDALDELGI 205
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238332949 345 RDSTIVVLWGDHG-----WHLGDHGLW--CKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIP 416
Cdd:cd16142 206 ADNTIVIFTTDNGpeqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDP 284
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
43-490 |
3.25e-20 |
|
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: 92.61 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDL--------RPEagcygvpIIKTPHIDALASQGLLFNRAYCQQaVCSPSRTSLLLGRRPDTTRVYD---LQ 111
Cdd:cd16029 2 HIVFILADDLgwndvgfhGSD-------QIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHgviLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 112 THFRKTLPDVITLPQHFKNHGYHTQ-------GLSKI--------------YHGGLDDpaswsvpHWSpskPMYGKPETL 170
Cdd:cd16029 74 GEPYGLPLNETLLPQYLKELGYATHlvgkwhlGFYTWeytptnrgfdsfygYYGGAED-------YYT---HTSGGANDY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 171 ADLDRRREEmrkkagpatrvlekdpktgiplrlsapqyrvyGPAWEDPDVPDDALpdgeTTNRAIELLQEL-KDRRFFLA 249
Cdd:cd16029 144 GNDDLRDNE--------------------------------EPAWDYNGTYSTDL----FTDRAVDIIENHdPSKPLFLY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 250 VGYLKPHLPFVAPKKYYDLYrkediplaanpfpPKDCPPIALTNwgelRAYqgipaagplpdsmardlvhgYYAATSYVD 329
Cdd:cd16029 188 LAFQAVHAPLQVPPEYADPY-------------EDKFAHIKDED----RRT--------------------YAAMVSALD 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 330 AQIGRLLAEVDRLGLRDSTIVVLWGDHG-WHLGDHGLW------CKHTNFETATRSLLIFRVPG-QPHPGAKTDALVEFV 401
Cdd:cd16029 231 ESVGNVVDALKAKGMLDNTLIVFTSDNGgPTGGGDGGSnyplrgGKNTLWEGGVRVPAFVWSPLlPPKRGTVSDGLMHVT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 402 DIYPTLCELCGLPIP--EGLEGTSLVP-LFENPQRPWQKAAFSQYPRGKVMGYS-MRTDRYRYTEwrpsggGEPvaveLY 477
Cdd:cd16029 311 DWLPTLLSLAGGDPDdlPPLDGVDQWDaLSGGAPSPRTEILLNIDDITRTTGGAaIRVGDWKLIV------GKP----LF 380
|
490
....*....|...
gi 1238332949 478 DHTTDPLENVNLA 490
Cdd:cd16029 381 NIENDPCERNDLA 393
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-486 |
8.80e-18 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 85.09 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 43 NVLMIAVDDLRPEAGC-YGVP--IIKTPHIDALASQGLLFNRAYCQqAVCSPSRTSLLLGRRPDTTRVydlqthfrKTLP 119
Cdd:cd16154 2 NILLIIADDQGLDSSAqYSLSsdLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGV--------LAVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 120 DVITLPQHF---------KNHGYHTQGLSKiYHGGLDDPAswsvPHWSPSKPMYgkpetladldrrreemrkkAGPATRV 190
Cdd:cd16154 73 DELLLSEETllqllikdaTTAGYSSAVIGK-WHLGGNDNS----PNNPGGIPYY-------------------AGILGGG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 191 LekDPKTGIPLRLSAPQYRVYGPAWEDpdvpddalpdgeTTNRAIELLQElKDRRFFLAVGYLKPHLPFVAPkkyydlyr 270
Cdd:cd16154 129 V--QDYYNWNLTNNGQTTNSTEYATTK------------LTNLAIDWIDQ-QTKPWFLWLAYNAPHTPFHLP-------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 271 kediplaanpfppkdcpPIALTNWGELRAYQGIpAAGPLPdsmardlvhgYY-AATSYVDAQIGRLLAEVDRlGLRDSTI 349
Cdd:cd16154 186 -----------------PAELHSRSLLGDSADI-EANPRP----------YYlAAIEAMDTEIGRLLASIDE-EERENTI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 350 VVLWGDHG--------WHLGDHGlwcKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIPEGLEG 421
Cdd:cd16154 237 IIFIGDNGtpgqvvdlPYTRNHA---KGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDS 313
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238332949 422 TSLVPLFENPQRPWQKAAFSQYPRGKVMGYSMRTDRYRYTEWrpSGGGEpvavELYDHTTDPLEN 486
Cdd:cd16154 314 VSFKPLLSDVNASTRQYNYTEYESPTTTGWATRNQYYKLIES--ENGQE----ELYDLINDPSEQ 372
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
66-412 |
2.36e-16 |
|
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: 79.26 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 66 TPHIDALASQGLLFNRAYcqqAVCSPSRTS-----LLLGRRPDTTRVYDLQTHFRKTLPdviTLPQHFKNHGYHTQglsk 140
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFY---SPGFGGGTAngefeVLTGLPPLPLGSGSYTLYKLNPLP---SLPSILKEQGYETI---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 141 IYHGGldDPASWsvphwspskpmygkpetladldRRReemrkkagpatRVLekdPKTGIplrlsapqYRVYGPAWEDPDV 220
Cdd:cd16015 96 FIHGG--DASFY----------------------NRD-----------SVY---PNLGF--------DEFYDLEDFPDDE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 221 PDDA---LPDGETTNRAIELLQELKDRRFFLAVGYLKPHLPFVAPKKYYDLYRKEDIplaanpfppkdcppialtnwgel 297
Cdd:cd16015 130 KETNgwgVSDESLFDQALEELEELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEE----------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 298 rayqgipaagplpdsmARDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHLGDHglwckhtNFETATR 377
Cdd:cd16015 187 ----------------DKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD-------YDETDED 243
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1238332949 378 SLLIFRVP-----GQPHPGAKTDALVEFVDIYPTLCELCG 412
Cdd:cd16015 244 PLDLYRTPlliysPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
41-430 |
1.85e-15 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 78.66 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 41 KYNVLMIAVDDLR-PEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDLQTHFRKT-- 117
Cdd:cd16157 1 KPNIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 118 -------LPDV-ITLPQHFKNHGYHTQGLSKiyhgglddpasWSVPHWSPSKPMygkpetladldrrreemrkkagpatr 189
Cdd:cd16157 81 pqnivggIPDSeILLPELLKKAGYRNKIVGK-----------WHLGHRPQYHPL-------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 190 vlekdpKTGIPLRLSAPQYRvYGPaWEDPDVPDdaLP---DGETTNRAIELLQ-ELKDRRFFLAVGYLKPHLPFVapkky 265
Cdd:cd16157 124 ------KHGFDEWFGAPNCH-FGP-YDNKAYPN--IPvyrDWEMIGRYYEEFKiDKKTGESNLTQIYLQEALEFI----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 266 ydlYRKEDiplAANPFppkdcppiaLTNWGELRAYQGIPAAGPLPDSMARDLvhgYYAATSYVDAQIGRLLAEVDRLGLR 345
Cdd:cd16157 189 ---EKQHD---AQKPF---------FLYWAPDATHAPVYASKPFLGTSQRGL---YGDAVMELDSSVGKILESLKSLGIE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 346 DSTIVVLWGDHG-------WHLGDHG--LWCKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPIP 416
Cdd:cd16157 251 NNTFVFFSSDNGaalisapEQGGSNGpfLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIP 330
|
410
....*....|....*.
gi 1238332949 417 EG--LEGTSLVPLFEN 430
Cdd:cd16157 331 SDraIDGIDLLPVLLN 346
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
41-418 |
2.05e-15 |
|
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: 77.89 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 41 KYNVLMIAVDDLR-PEAGCYGVP-IIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYDlqtHFRKT- 117
Cdd:cd16161 1 KPNFLLLFADDLGwGDLGANWAPnAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH---NFLPTs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 118 ---LP-DVITLPQHFKNHGYHTQGLSKiyhgglddpasWSVPHwspskpmygkpetladldrrreemRKKAGPATRVLek 193
Cdd:cd16161 78 vggLPlNETTLAEVLRQAGYATGMIGK-----------WHLGQ------------------------REAYLPNSRGF-- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 194 DPKTGIPLRlsapqyrvygpawedpdvPDDALPDgETTNRAIELLQE--LKDRRFFLAVGYLKPHLPfvapkkyydlyrk 271
Cdd:cd16161 121 DYYFGIPFS------------------HDSSLAD-RYAQFATDFIQRasAKDRPFFLYAALAHVHVP------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 272 ediplaaNPFPPKDCPPIAltnwgelrayqgipAAGPlpdsmardlvhgYYAATSYVDAQIGRLLAEVDRLGLRDSTIVV 351
Cdd:cd16161 169 -------LANLPRFQSPTS--------------GRGP------------YGDALQEMDDLVGQIMDAVKHAGLKDNTLTW 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 352 LWGDHG-WHLG-------DHGLW--------CKHTNFETATRSLLIFRVPGQPHPGAKTDALVEFVDIYPTLCELCGLPI 415
Cdd:cd16161 216 FTSDNGpWEVKcelavgpGTGDWqgnlggsvAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASL 295
|
...
gi 1238332949 416 PEG 418
Cdd:cd16161 296 PPG 298
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
41-430 |
6.24e-15 |
|
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: 77.33 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 41 KYNVLMIAVDDLR-PEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRP--------DTTRVYdLQ 111
Cdd:cd16159 1 KPNIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirsgmassHGMRVI-LF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 112 THFRKTLP-DVITLPQHFKNHGYHTQGLSKiYHGGLD---------DPASWSVPHWspskpmYGKPETLadldrrreemr 181
Cdd:cd16159 80 TASSGGLPpNETTFAEVLKQQGYSTALIGK-WHLGLHcesrndfchHPLNHGFDYF------YGLPLTN----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 182 kkagpatrVLEKDPKTGIPLRLSAPQYRVYGPAWedpdvpddaLPDGETTNRAIELLQELKDRRFF--LAVGYLKPHLPF 259
Cdd:cd16159 142 --------LKDCGDGSNGEYDLSFDPLFPLLTAF---------VLITALTIFLLLYLGAVSKRFFVflLILSLLFISLFF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 260 VAPKKYYD----LYRKEDI---PLA-----------ANPF--PPKDCPPIALTNWgeLRAYQGIPAAgplPDSMARDLvH 319
Cdd:cd16159 205 LLLITNRYfnciLMRNHEVveqPMSlenltqrltkeAISFleRNKERPFLLVMSF--LHVHTALFTS---KKFKGRSK-H 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 320 GYY-AATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHL------GDHGLWC-------KHTNFETATRSLLIFRVP 385
Cdd:cd16159 279 GRYgDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGNggiyggkKMGGWEGGIRVPTIVRWP 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1238332949 386 GQPHPGAKTDALVEFVDIYPTLCELCGLPIPEG--LEGTSLVPLFEN 430
Cdd:cd16159 359 GVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTG 405
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
66-417 |
3.89e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 75.07 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 66 TPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRrPDTTRVYDLQTHFRKTLPdviTLPQHFKNHGYHTQglskIYHGG 145
Cdd:COG1368 260 TPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGL-PPLPGGSPYKRPGQNNFP---SLPSILKKQGYETS----FFHGG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 146 ldDPASWSVPHWSPS---KPMYGkpetladldrrREEMrkkagpatrvleKDPKTGiplrlsapqyrVYGpawedpdvpd 222
Cdd:COG1368 332 --DGSFWNRDSFYKNlgfDEFYD-----------REDF------------DDPFDG-----------GWG---------- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 223 daLPDGETTNRAIELLQELKDRRFFLAVGyLKPHLPFVAPKKYYDLYRKEDiplaanpfppkdcppialtnwgelrayqg 302
Cdd:COG1368 366 --VSDEDLFDKALEELEKLKKPFFAFLIT-LSNHGPYTLPEEDKKIPDYGK----------------------------- 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 303 ipaagplpdsmarDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDH-GWHLGDHGLWCKHTNFETAtrslLI 381
Cdd:COG1368 414 -------------TTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHgPRSPGKTDYENPLERYRVP----LL 476
|
330 340 350
....*....|....*....|....*....|....*.
gi 1238332949 382 FRVPGQPHPGaKTDALVEFVDIYPTLCELCGLPIPE 417
Cdd:COG1368 477 IYSPGLKKPK-VIDTVGSQIDIAPTLLDLLGIDYPS 511
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
320-410 |
2.53e-11 |
|
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: 63.59 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 320 GYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHLGDHG----LWCKHTNFETATRSLLIFRVPGQPHPGAKtD 395
Cdd:cd00016 143 EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGgdpkADGKADKSHTGMRVPFIAYGPGVKKGGVK-H 221
|
90
....*....|....*
gi 1238332949 396 ALVEFVDIYPTLCEL 410
Cdd:cd00016 222 ELISQYDIAPTLADL 236
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
203-407 |
1.19e-10 |
|
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: 63.77 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 203 LSAPQYRVYGPAWEdpdvpddalPDGETTNRAIELLQE-LKDRRFFLAVGYLKPHlPFVAPKKYYDLYrkediplaanpF 281
Cdd:COG3083 348 VSLPRLHTPGGPAQ---------RDRQITAQWLQWLDQrDSDRPWFSYLFLDAPH-AYSFPADYPKPF-----------Q 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 282 PPKDCPPIALTNwgelrayqgipaagplpDSMARDLVHGYYAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWHLG 361
Cdd:COG3083 407 PSEDCNYLALDN-----------------ESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFN 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1238332949 362 DHGL--WCKHTNFETA-TRSLLIFRVPGQPhPGaKTDALVEFVDIYPTL 407
Cdd:COG3083 470 ENGQnyWGHNSNFSRYqLQVPLVIHWPGTP-PQ-VISKLTSHLDIVPTL 516
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
41-434 |
1.40e-09 |
|
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: 60.14 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 41 KYNVLMIAVDDL-RPEAGCYGVPIIKTPHIDALASQGLLFNRAYCQQAVCSPSRTSLLLGRRPDTTRVYD----LQTHFR 115
Cdd:cd16160 1 KPNIVLFFADDMgYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGgtrvFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 116 KTLP-DVITLPQHFKNHGYHTqGLSKIYHGGLDDPASWSVPHWsPSKPMYGKPETLAdldrrreemrkkagPATRVLEKD 194
Cdd:cd16160 81 GGLPkTEVTMAEALKEAGYTT-GMVGKWHLGINENNHSDGAHL-PSHHGFDFVGTNL--------------PFTNSWACD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 195 PkTGIPLRLSAPQ--YRVYGpaweDPDVPDDALPDGET---TNRAIELLQELKDRRFFLAVGYLKPHLPfvapkkyydLY 269
Cdd:cd16160 145 D-TGRHVDFPDRSacFLYYN----DTIVEQPIQHEHLTetlVGDAKSFIEDNQENPFFLYFSFPQTHTP---------LF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 270 RKEDiplaanpfppkdcppialtnwgelraYQGIPAAGPLPDSMardlvhgyyaatSYVDAQIGRLLAEVDRLGLRDSTI 349
Cdd:cd16160 211 ASKR--------------------------FKGKSKRGRYGDNI------------NEMSWAVGEVLDTLVDTGLDQNTL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 350 VVLWGDHGWHL------GDHGLW--CKHTNFETATRSLLIFRVPGQPHPGAKtDALVEFVDIYPTLCELCG--LPIPEGL 419
Cdd:cd16160 253 VFFLSDHGPHVeyclegGSTGGLkgGKGNSWEGGIRVPFIAYWPGTIKPRVS-HEVVSTMDIFPTFVDLAGgtLPTDRIY 331
|
410
....*....|....*.
gi 1238332949 420 EGTSLVP-LFENPQRP 434
Cdd:cd16160 332 DGLSITDlLLGEADSP 347
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
415-508 |
1.59e-09 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 55.33 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 415 IPEGLEGTSLVPLFE-NPQRPWQKAA---FSQYP-RGKVMG-YSMRTDRY-------RYTEWrpsgggepvavELYDHTT 481
Cdd:pfam16347 1 IPADMQGKSFLPLLKgKKPKNWRDALyyhYYEYPaEHAVKRhYGVRTERYklihfynDIDEW-----------ELYDLQK 69
|
90 100
....*....|....*....|....*..
gi 1238332949 482 DPLENVNLAGRPEYKDLVAQLHQQLEA 508
Cdd:pfam16347 70 DPKEMNNVYGDPEYAEVQAELKEELEE 96
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
310-412 |
7.57e-09 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 56.82 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 310 PDSMArdlvHGY-------YAATSYVDAQIGRLLAEVDRLGLRDSTIVVLWGDHGWH-LGDHGlwckHTNFETATRSLLI 381
Cdd:cd16018 167 PDSAG----HKYgpdspevNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFI 238
|
90 100 110
....*....|....*....|....*....|....
gi 1238332949 382 FRvpgqpHPGAKTDALVEF---VDIYPTLCELCG 412
Cdd:cd16018 239 AR-----GPAFKKGKKLGPfrnVDIYPLMCNLLG 267
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
328-425 |
2.59e-04 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 43.55 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 328 VDAQIGRLLAEVDRLGlrdsTIVVLWGDHGwhlgdhglwckhtNFETatrslLIFRVPGQPHpGAKTDALVEFV------ 401
Cdd:PRK05434 417 VDECLGRVVDAVLKVG----GTLLITADHG-------------NAEQ-----MIDPETGQPH-TAHTTNPVPFIlvggka 473
|
90 100 110
....*....|....*....|....*....|...
gi 1238332949 402 ---------DIYPTLCELCGLPIPEGLEGTSLV 425
Cdd:PRK05434 474 lrleggklaDIAPTILDLLGLEQPAEMTGKSLI 506
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
29-357 |
8.26e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 41.66 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 29 TFASETANKPSGKYNVLMIAVDDLRPEAgcygVPIIKTPHIDALASQGLLFNRAYCQQ-AVCSPSRTSLLLGRRPDTTRV 107
Cdd:COG1524 11 SLLAAAAAAAPPAKKVVLILVDGLRADL----LERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 108 YDlqthfrktlpdvitlpqhfkNHGYHTQGLSKIYHGGLDDPASWSVPHWspskpmygKPETLADLdrrreemRKKAGPA 187
Cdd:COG1524 87 VG--------------------NGWYDPELGRVVNSLSWVEDGFGSNSLL--------PVPTIFER-------ARAAGLT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 188 TRVLekdpktGIPLRLSAPQYRVYGPAWEDPDVPDDALPDGE--TTNRAIELLQElKDRRFFLAvgYLkPHLpfvapkky 265
Cdd:COG1524 132 TAAV------FWPSFEGSGLIDAARPYPYDGRKPLLGNPAADrwIAAAALELLRE-GRPDLLLV--YL-PDL-------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 266 yDLYRKEdiplaanpfppkdcppialtnwgelrayQGipaagplPDSMArdlvhgYYAATSYVDAQIGRLLAEVDRLGLR 345
Cdd:COG1524 194 -DYAGHR----------------------------YG-------PDSPE------YRAALREVDAALGRLLDALKARGLY 231
|
330
....*....|..
gi 1238332949 346 DSTIVVLWGDHG 357
Cdd:COG1524 232 EGTLVIVTADHG 243
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
316-425 |
2.26e-03 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 40.48 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 316 DLV-H-GYYAAT----SYVDAQIGRLLAEVDRLGlrdsTIVVLWGDHG-----WHLGDHGLWCKHTNFetatrsllifRV 384
Cdd:cd16010 394 DMVgHtGNLEAAvkavEAVDECLGRIVEAVLENG----GTLLITADHGnaeemIDPETGGPHTAHTTN----------PV 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1238332949 385 P----GQPHPGAKTD--ALVefvDIYPTLCELCGLPIPEGLEGTSLV 425
Cdd:cd16010 460 PfiivDPGLKRKLLKdgGLA---DVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
314-423 |
2.36e-03 |
|
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.
Pssm-ID: 293733 Cd Length: 382 Bit Score: 40.51 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 314 ARDlVHGYYAATSYVDAQIGRLLAEvdrlgLRDSTIVVLWGDHG----WHLGDHglwckhtnfetaTR---SLLIFrvpg 386
Cdd:cd16009 288 RRD-PEGYAEALEEFDRRLPELLAK-----LKEDDLLIITADHGndptIGGTDH------------TReyvPLLVY---- 345
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1238332949 387 qpHPGAKTDALVE---FVDIYPTLCELCGLPIPEGleGTS 423
Cdd:cd16009 346 --GKGLKGVNLGTretFADIGATIADNFGVEPPEN--GTS 381
|
|
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
307-418 |
2.46e-03 |
|
GPI ethanolamine phosphate transferase 3, PIG-O; 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: 293747 Cd Length: 289 Bit Score: 39.85 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 307 GPLPDSMARDLvhgyyaatSYVDAQIGRLLAEVDrlglrDSTIVVLWGDHGWHL-GDHG----------LWCKHT--NFE 373
Cdd:cd16023 178 GPNHPEMARKL--------TQMDQFIRDIIERLD-----DDTLLLVFGDHGMTEtGDHGgdsdeevdaaLFAYSKrpFNN 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1238332949 374 TATRSLLIFRVPGQPHPgaktdaLVEFVDIYPTLCELCGLPIPEG 418
Cdd:cd16023 245 SDEPIESNGPGDPSKVR------SVPQIDLVPTLSLLLGLPIPFS 283
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
328-425 |
3.58e-03 |
|
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440460 Cd Length: 511 Bit Score: 40.04 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 328 VDAQIGRLLAEVDRLGlrdSTIVVLwgdhgwhlGDHGlwckhtNFETatrslLIFRVPGQPHPgAKTDALVEFV------ 401
Cdd:COG0696 418 VDECLGRVVDAVLAAG---GTLLIT--------ADHG------NAEQ-----MIDPDTGGPHT-AHTTNPVPFIlvggdk 474
|
90 100 110
....*....|....*....|....*....|....*
gi 1238332949 402 -----------DIYPTLCELCGLPIPEGLEGTSLV 425
Cdd:COG0696 475 gvklredgrlaDIAPTILELMGLPQPAEMTGKSLI 509
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
329-418 |
4.29e-03 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 39.09 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238332949 329 DAQIGRLLAEVDRLGLRDSTIVVLWGDHGW-HLGDHGlwcKHTNFETATRSLLIF----RVPGQPHPGAKTDALVEFVDI 403
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHGMtDAGNHG---GSSPGETSVPLLFISpkfsSKPSNADGELSYYETVQQVDL 253
|
90
....*....|....*
gi 1238332949 404 YPTLCELCGLPIPEG 418
Cdd:cd16024 254 APTLALLLGLPIPKN 268
|
|
| |
