|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-450 |
3.59e-135 |
|
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: 401.18 E-value: 3.59e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 29 KTNLLIIHTDEHNFRTLGCYRelmpDDQafvwgegvkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATG 108
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAG----DDP---------VKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 109 SPVNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGDAKPGF-------EPARKFGFSDNRYMMNRG-HWKGLSNINGKP 180
Cdd:cd16034 68 VFGNDVPLPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGraddytpPPERRHGFDYWKGYECNHdHNNPHYYDDDGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 181 AViglipekesakfnvsgsNPENFTTDFLTTRSLEILER--DKGKPFCLMLSIPDPHGPN-SVRPPYDTMFKNFHFENPr 257
Cdd:cd16034 148 RI-----------------YIKGYSPDAETDLAIEYLENqaDKDKPFALVLSWNPPHDPYtTAPEEYLDMYDPKKLLLR- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 258 tMDVPVESMPiwaqggkelvSELNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKGS 337
Cdd:cd16034 210 -PNVPEDKKE----------EAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 338 PFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPgIPGS-QGLNDAKAFTSPAKKVEDGRVTYITA---- 412
Cdd:cd16034 279 PYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLP-IPDTvEGRDLSPLLLGGKDDEPDSVLLQCFVpfgg 357
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1395161701 413 ----SASGWVAAVNNRCKLVISESDIPWLFDLKKDPDELINF 450
Cdd:cd16034 358 gsarDGGEWRGVRTDRYTYVRDKNGPWLLFDNEKDPYQLNNL 399
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-477 |
3.85e-103 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 318.36 E-value: 3.85e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 1 MNRRNFSMLAsatgitAMAGNALAGKSKKTNLLIIHTDEHNFRTLGCYrelmpddqafvwGEGvKVDTPHIDSIAHDGAI 80
Cdd:COG3119 1 MKRLLLLLLA------LLAAAAAAAAAKRPNILFILADDLGYGDLGCY------------GNP-LIKTPNIDRLAAEGVR 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 81 CTSYYASSPVCTPSRASFVTGLYPIATG----SPVNNMPMHDGLATFASVLKDQGYATSYVGKWHLdgdakpgfeparkf 156
Cdd:COG3119 62 FTNAYVTSPVCSPSRASLLTGRYPHRTGvtdnGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 157 gfsdnrymmnrghwkglsningkpaviglipekesakfnvsgsnpenFTTDFLTTRSLEILER--DKGKPFCLMLSIPDP 234
Cdd:COG3119 128 -----------------------------------------------YLTDLLTDKAIDFLERqaDKDKPFFLYLAFNAP 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 235 HGPNSVRPPYDTMFKnfhfenPRTMDVPVESMPiwaqggKELVSELNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADN 314
Cdd:COG3119 161 HAPYQAPEEYLDKYD------GKDIPLPPNLAP------RDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADN 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 315 TIVVFTSDHGDLMGEHK-KHNKGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQGLNDAK 393
Cdd:COG3119 229 TIVVFTSDNGPSLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 394 AFTSPAKKVEDgRVTYITASASGWVAAVNNRCKLVISESDIPW--LFDLKKDPDELINfyLNPEYAQIGKTMMDELVRQM 471
Cdd:COG3119 309 LLTGEKAEWRD-YLYWEYPRGGGNRAIRTGRWKLIRYYDDDGPweLYDLKNDPGETNN--LAADYPEVVAELRALLEAWL 385
|
....*.
gi 1395161701 472 KAYNEP 477
Cdd:COG3119 386 KELGDP 391
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
28-467 |
2.49e-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: 270.94 E-value: 2.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 28 KKTNLLIIHTDEHNFRTLGCYrelmpddqafvwGEGVkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIAT 107
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCY------------GNPI-VKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 108 GSPVNNMPMHDGLA-TFASVLKDQGYATSYVGKWHL---DGDAKPGFEparkfgfsdnrymmnrgHWKGLsNINGKPAVI 183
Cdd:cd16031 68 GVTDNNGPLFDASQpTYPKLLRKAGYQTAFIGKWHLgsgGDLPPPGFD-----------------YWVSF-PGQGSYYDP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 184 GLIPEKESAKfnvsgsnPENFTTDFLTTRSLEIL-ERDKGKPFCLMLSIPDPHGPNSVRPPYDTMFKNFHFENPRTMDV- 261
Cdd:cd16031 130 EFIENGKRVG-------QKGYVTDIITDKALDFLkERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDDd 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 262 PVESMPIWAQ----------GGKELVSELNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHK 331
Cdd:cd16031 203 DYAGRPEWAReqrnrirgvlDGRFDTPEKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 332 KHNKGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPgIPGS-QGLNDAKAFTSPAKKV-------- 402
Cdd:cd16031 283 LFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVP-IPEDmQGRSLLPLLEGEKPVDwrkefyye 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161701 403 --EDGRVTYITAsasgWVAAVNNRCKLV--ISESDIPWLFDLKKDPDELINFYLNPEYAQIGKTMMDEL 467
Cdd:cd16031 362 yyEEPNFHNVPT----HEGVRTERYKYIyyYGVWDEEELYDLKKDPLELNNLANDPEYAEVLKELRKRL 426
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-475 |
6.22e-77 |
|
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: 250.99 E-value: 6.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelmpddqafvwGEGVkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSp 110
Cdd:cd16033 2 NILFIMTDQQRYDTLGCY------------GNPI-VKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGV- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 111 VNNM----PMHDGLA----TFASVLKDQGYATSYVGKWHLDGDAKPGFeparkFGFSDNrymmnrghwkglsningkpav 182
Cdd:cd16033 68 LNNVenagAYSRGLPpgveTFSEDLREAGYRNGYVGKWHVGPEETPLD-----YGFDEY--------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 183 iglipekesakfnvsgsNPENFTTD-FLTTRSLEILER--DKGKPFCLMLSIPDPHGPNSVRPPYDTMFKNFHFENPRTM 259
Cdd:cd16033 122 -----------------LPVETTIEyFLADRAIEMLEElaADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESF 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 260 DVPVESMP-IWAQ-----GGKELVSELNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKH 333
Cdd:cd16033 185 ADDFEDKPyIYRRerkrwGVDTEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLW 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 334 NKGSP-FETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQGLNDAKAFTSpaKKVEDGRVTYITA 412
Cdd:cd16033 265 DKGPFmYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRG--EQPEDWRDEVVTE 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161701 413 SASGWV-----AAVNNRCKLVISESDIPWLFDLKKDPDELINFYLNPEYAQIGKTMMDELVRQMKAYN 475
Cdd:cd16033 343 YNGHEFylpqrMVRTDRYKYVFNGFDIDELYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETG 410
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
31-471 |
6.42e-73 |
|
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: 241.90 E-value: 6.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelmpddqafvwgEGVKVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSP 110
Cdd:cd16156 2 QFIFIMTDTQRWDMVGCY-------------GNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 111 VNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGD-------AKPGFEPARkfgFSDNRYMMN------RGHWKGLSNIn 177
Cdd:cd16156 69 TNCMALGDNVKTIGQRLSDNGIHTAYIGKWHLDGGdyfgngiCPQGWDPDY---WYDMRNYLDelteeeRRKSRRGLTS- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 178 gkpavigliPEKESAkfnvsgsnPENFTTDF-LTTRSLEILERDKGKPFCLMLSIPDPHGPNSVRPPYDTMFKNFHFENP 256
Cdd:cd16156 145 ---------LEAEGI--------KEEFTYGHrCTNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 257 RTMDVPVESMP----IWAQGGKELVSELNQKQMQIYFGMVKCIDDNVGRLLEwlEANGLADNTIVVFTSDHGDLMGEHKK 332
Cdd:cd16156 208 ENAYDDLENKPlhqrLWAGAKPHEDGDKGTIKHPLYFGCNSFVDYEIGRVLD--AADEIAEDAWVIYTSDHGDMLGAHKL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 333 HNKG-SPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPG---IPGSQGLNDAKAFTSPAKK---VEDG 405
Cdd:cd16156 286 WAKGpAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQpkvLEGESILATIEDPEIPENRgvfVEFG 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161701 406 RVTYITASASGWV---AAVNNRCKLVISESDIPWLFDLKKDPDELINFYLNPEYAQIGKTMMDELVRQM 471
Cdd:cd16156 366 RYEVDHDGFGGFQpvrCVVDGRYKLVINLLSTDELYDLEKDPYEMHNLIDDPDYADVRDQLHDELLDYM 434
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
31-390 |
2.28e-71 |
|
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: 230.02 E-value: 2.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelmpddqafvwGEGVkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSp 110
Cdd:cd16022 2 NILLIMTDDLGYDDLGCY------------GNPD-IKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGV- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 111 VNNMPMHDGLA----TFASVLKDQGYATSYVGKWHldgdakpgfeparkfgfsdnrymmnrghwkglsningkpavigli 186
Cdd:cd16022 68 RGNVGNGGGLPpdepTLAELLKEAGYRTALIGKWH--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 187 peKESAKFnvsgsnpenfttdflttrsleILERDKGKPFCLMLSIPDPHgpnsvrPPYdtmfknfhfenprtmdvpvesm 266
Cdd:cd16022 103 --DEAIDF---------------------IERRDKDKPFFLYVSFNAPH------PPF---------------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 267 piwaqggkelvselnqkqmqIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHK-KHNKGSPFETSAKI 345
Cdd:cd16022 132 --------------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGlRGKKGSLYEGGIRV 191
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1395161701 346 PFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQGLN 390
Cdd:cd16022 192 PFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
31-472 |
1.13e-67 |
|
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: 225.08 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelmpddqafvwGEGVKvdTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSP 110
Cdd:cd16027 2 NILWIIADDLSPDLGGYG------------GNVVK--TPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 111 VN---NMPMHDGLATFASVLKDQGYATSYVGKWHLDGDAKPGFEPARKFGFSDNRYMmnrghWKGLSNIngkpaviglip 187
Cdd:cd16027 68 GLrsrGFPLPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNA-----WDYASNA----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 188 ekesakfnvsgsnpenftTDFLTtrsleilERDKGKPFCLMLSIPDPHgpnsvRPPYDTMFKNFHFeNPRTMDVPvesmP 267
Cdd:cd16027 132 ------------------ADFLN-------RAKKGQPFFLWFGFHDPH-----RPYPPGDGEEPGY-DPEKVKVP----P 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 268 IWAQggkelvSELNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMgehkKHNKGSPFETSAKIPF 347
Cdd:cd16027 177 YLPD------TPEVREDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPF----PRAKGTLYDSGLRVPL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 348 LIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQGLNDAKAFTSPAKKVEDgrvtYITASASGWV-------AA 420
Cdd:cd16027 247 IVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGRD----YVFAERDRHDetydpirSV 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1395161701 421 VNNRCKLVISESdiPW-LFDLKKDPDELINFYLNPEYAQIGKTMMDELVRQMK 472
Cdd:cd16027 323 RTGRYKYIRNYM--PEeLYDLKNDPDELNNLADDPEYAEVLEELRAALDAWMK 373
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
52-449 |
5.33e-64 |
|
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: 216.65 E-value: 5.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 52 MPDDQAfvWGEGV-----KVDTPHIDSIAHDGAICTSYYASsPVCTPSRASFVTGLYPIATG----SPVNNMpMHDGLAT 122
Cdd:cd16146 7 LTDDQG--YGDLGfhgnpILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGvwhtILGRER-MRLDETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 123 FASVLKDQGYATSYVGKWHLdGDAKP------GFEPARKF---GFSDNRYMMNRGHWKGLSNINGKPAviglipekesaK 193
Cdd:cd16146 83 LAEVFKDAGYRTGIFGKWHL-GDNYPyrpqdrGFDEVLGHgggGIGQYPDYWGNDYFDDTYYHNGKFV-----------K 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 194 FnvsgsnpENFTTDFLTTRSLEILERDKGKPFCLMLSIPDPHGPNSVRPPYDTMFKNfhfenprtmdvpvesmpiwaqgg 273
Cdd:cd16146 151 T-------EGYCTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYLDPYKD----------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 274 kelvSELNQKQMQIYfGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHN------KGSPFETSAKIPF 347
Cdd:cd16146 201 ----MGLDDKLAAFY-GMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFNagmrgkKGSVYEGGHRVPF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 348 LIRYPEKIAPGKMIHTAYTTVD-FPqTILGIMGAPgIPGSQGLnDAKAF----TSPAKKVED-------GRVTYITASAS 415
Cdd:cd16146 276 FIRWPGKILAGKDVDTLTAHIDlLP-TLLDLCGVK-LPEGIKL-DGRSLlpllKGESDPWPErtlfthsGRWPPPPKKKR 352
|
410 420 430
....*....|....*....|....*....|....
gi 1395161701 416 GWvAAVNNRCKLVISESDIPWLFDLKKDPDELIN 449
Cdd:cd16146 353 NA-AVRTGRWRLVSPKGFQPELYDIENDPGEEND 385
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-469 |
1.69e-62 |
|
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: 212.79 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelMPDDqafvwgegvkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATG-- 108
Cdd:cd16144 2 NIVLILVDDLGWADLGCY---GSKF----------YETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGit 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 109 ----------------SPVNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGDAKPGFEparKFGFSDNRYMMNRGHwkg 172
Cdd:cd16144 69 dvipgrrgppdntkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPE---DQGFDVNIGGTGNGG--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 173 lsningkpavigliPEKESAKFNVSGSNPEN-----FTTDFLTTRSLEILERDKGKPFCLMLSIPDPHGPNSVRPpyDTM 247
Cdd:cd16144 143 --------------PPSYYFPPGKPNPDLEDgpegeYLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARP--ELI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 248 FKnfhFEnprtmdvpvesmpiwaqggKELVSELNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLM 327
Cdd:cd16144 207 EK---YE-------------------KKKKGLRKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 328 GEHKKHN--------KGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQ--GLNDAKAFTS 397
Cdd:cd16144 265 TRGGPPTsnaplrggKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHldGVSLVPLLKG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 398 PAKKVEDG---------RVTYITASAS----GWvaavnnrcKLVIS-ESDIPWLFDLKKDPDELINfyLNPEYAQIGKTM 463
Cdd:cd16144 345 GEADLPRRalfwhfphyHGQGGRPASAirkgDW--------KLIEFyEDGRVELYNLKNDIGETNN--LAAEMPEKAAEL 414
|
....*.
gi 1395161701 464 MDELVR 469
Cdd:cd16144 415 KKKLDA 420
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-445 |
2.71e-59 |
|
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: 201.23 E-value: 2.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 30 TNLLIIHTDEHNFRTLGCYRELMpddqafvwgegvkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGS 109
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPV-------------VRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 110 PVNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGDAKPGfeparkfGFSDNRYMMNRghwkglsningkpAViglipek 189
Cdd:cd16037 68 WDNADPYDGDVPSWGHALRAAGYETVLIGKLHFRGEDQRH-------GFRYDRDVTEA-------------AV------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 190 esakfnvsgsnpenfttDFLTTRSLeilerdKGKPFCLMLSIPDPHGPNSVRPpydtmfknfhfenprtmdvpvesmpiw 269
Cdd:cd16037 121 -----------------DWLREEAA------DDKPWFLFVGFVAPHFPLIAPQ--------------------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 270 aqggkELVSELNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKGSPFETSAKIPFLI 349
Cdd:cd16037 151 -----EFYDLYVRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVRVPMII 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 350 RYPeKIAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQGlndaKAFTSPAKKVED-GRVTYI----TASASGWVAAVNNR 424
Cdd:cd16037 226 SGP-GIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDG----RSLLPLAEGPDDpDRVVFSeyhaHGSPSGAFMLRKGR 300
|
410 420
....*....|....*....|.
gi 1395161701 425 CKLVISESDIPWLFDLKKDPD 445
Cdd:cd16037 301 WKYIYYVGYPPQLFDLENDPE 321
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-473 |
3.32e-57 |
|
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: 197.45 E-value: 3.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 29 KTNLLIIHTDEHNFRTLGCYrelmpddqafvwgeGVKVD-TPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIAT 107
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCY--------------GQPLDlTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTET 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 108 GSPVNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGdakpgfeparkfgfsdnrymmnrghwkglsningkpaviglip 187
Cdd:cd16152 67 GCFRNGIPLPADEKTLAHYFRDAGYETGYVGKWHLAG------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 188 ekesakfnvsgsnpenFTTDFLTTRSLEIL-ERDKGKPFCLMLSIPDPHGPNSVR---PP--YDTMFKNFhfenprtmDV 261
Cdd:cd16152 104 ----------------YRVDALTDFAIDYLdNRQKDKPFFLFLSYLEPHHQNDRDryvAPegSAERFANF--------WV 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 262 PVEsmpIWAQGGKElvselnQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDlmgeH-KKHN---KGS 337
Cdd:cd16152 160 PPD---LAALPGDW------AEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGC----HfRTRNaeyKRS 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 338 PFETSAKIPFLIRYPeKIAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQG--LNDAKAFTSPAKKVEdgrvTYITASAS 415
Cdd:cd16152 227 CHESSIRVPLVIYGP-GFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGrsLLPLVDGKVEDWRNE----VFIQISES 301
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395161701 416 gWVAavnnRC------KLVISESDIPW-------------LFDLKKDPDELINFYLNPEYAQIGKTMMDELVRQMKA 473
Cdd:cd16152 302 -QVG----RAirtdrwKYSVAAPDKDGwkdsgsdvyvedyLYDLEADPYELVNLIGRPEYREVAAELRERLLARMAE 373
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-446 |
6.51e-56 |
|
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: 194.70 E-value: 6.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 29 KTNLLIIHTDEHNFRTLGCYrelmpddqafvWGEGVKvdTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATG 108
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCY-----------GSPLIK--TPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 109 SPVNNMP--MHDGLA----TFASVLKDQGYATSYVGKWHLdGDAkPGFEPARkFGFsdNRY-------MMNRGHWKGlSN 175
Cdd:cd16026 68 LPGVVGPpgSKGGLPpdeiTIAEVLKKAGYRTALVGKWHL-GHQ-PEFLPTR-HGF--DEYfgipysnDMWPFPLYR-ND 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 176 INGKPAVIGLIPEKESAKfnvsgSNPENFTTDFlTTRSLEILERDKGKPFCLMLSIPDPHGPNSVRPPydtmFKnfhfen 255
Cdd:cd16026 142 PPGPLPPLMENEEVIEQP-----ADQSSLTQRY-TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEK----FK------ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 256 prtmdvpvesmpiwaqggkelvselNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHG--DLMGEHKKH 333
Cdd:cd16026 206 -------------------------GRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGGS 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 334 N------KGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPgIPGSQ---GLNDAKAFTSPAKKVED 404
Cdd:cd16026 261 AgplrggKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAP-LPEDRvidGKDISPLLLGGSKSPPH 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1395161701 405 -----GRVTYITASASG--------WVAAVNNRCKLVISESDIPWLFDLKKDPDE 446
Cdd:cd16026 340 pffyyYDGGDLQAVRSGrwklhlptTYRTGTDPGGLDPTKLEPPLLYDLEEDPGE 394
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-449 |
6.36e-52 |
|
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: 184.34 E-value: 6.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelmpddqafvwgeGVKV-DTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYP----- 104
Cdd:cd16145 2 NIIFILADDLGYGDLGCY--------------GQKKiKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTghtrv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 105 IATGSPVNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGDAKPGfEPARK-----FGFSDNRymmnRGH-------WKg 172
Cdd:cd16145 68 RGNSEPGGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPG-HPTKQgfdyfYGYLDQV----HAHnyypeylWR- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 173 lsniNGKPAVIGLIPEKESAKFNVSGSNPENFTTDFLTTRSLEILERDKGKPFCLMLSIPDPHGPNSVrpPYDTMFKNFH 252
Cdd:cd16145 142 ----NGEKVPLPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQV--PDDGPYKYKP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 253 FENPRTMDVPvesmpiWAQGGKElvselnqkqmqiYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLM--GEH 330
Cdd:cd16145 216 KDPGIYAYLP------WPQPEKA------------YAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSegGSE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 331 KKHN-----------KGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQGLNDAKAFTSPA 399
Cdd:cd16145 278 HDPDffdsngplrgyKRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGKP 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1395161701 400 KKVEDgRVTYITA-SASGWVAAVNNRCKLVIS-ESDIPW-LFDLKKDPDELIN 449
Cdd:cd16145 358 QQQQH-DYLYWEFyEGGGAQAVRMGGWKAVRHgKKDGPFeLYDLSTDPGETNN 409
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
31-477 |
1.52e-49 |
|
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: 178.61 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelmpddqafvwGEGVkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSP 110
Cdd:cd16028 2 NVLFITADQWRADCLSCL------------GHPL-VKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 111 VNNMPMHDGLATFASVLKDQGYATSYVGKwhldGDAKPGFEPARKFGFSDNRYMMNRGHWKGLSNINGKPAviglipeke 190
Cdd:cd16028 69 WNGTPLDARHLTLALELRKAGYDPALFGY----TDTSPDPRGLAPLDPRLLSYELAMPGFDPVDRLDEYPA--------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 191 sakfnvsgsnpENFTTDFLTTRSLEILERDKGKPFCLMLSIPDPHGPNSVRPPYDTMFKNFHFENP-RTMDVPVESM--P 267
Cdd:cd16028 136 -----------EDSDTAFLTDRAIEYLDERQDEPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPPiRAESLAAEAAqhP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 268 IWAQ-----------GGKELVSELNQ---KQMQ-IYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKK 332
Cdd:cd16028 205 LLAAflerieslsfsPGAANAADLDDeevAQMRaTYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 333 HNKGSPFETSAKIPFLIRYPEKIA---PGKMIHTAYTTVDFPQTILGIMGAPGIPGSQG------LNDAKAfTSPAKKV- 402
Cdd:cd16028 285 WGKDGFFDQAYRVPLIVRDPRREAdatRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGrsllplLAGAQP-SDWRDAVh 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 403 --EDGRVTY---------ITASASGWVAAVNNRCKLVISESDIPWLFDLKKDPDELINFYLNPEYAQIGKTMMDELVRQM 471
Cdd:cd16028 364 yeYDFRDVStrrpqealgLSPDECSLAVIRDERWKYVHFAALPPLLFDLKNDPGELRDLAADPAYAAVVLRYAQKLLSWR 443
|
....*.
gi 1395161701 472 KAYNEP 477
Cdd:cd16028 444 MRHADR 449
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
31-445 |
2.36e-49 |
|
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: 174.69 E-value: 2.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelmpddqafvwGEGVkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSP 110
Cdd:cd16032 2 NILLIMADQLTAAALPAY------------GNTV-VKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 111 VNNMPMHDGLATFASVLKDQGYATSYVGKWHLDG-DAKPGFEparkfgFSDNrymmnrghwkglsningkpaviglipek 189
Cdd:cd16032 69 DNAAEFPADIPTFAHYLRAAGYRTALSGKMHFVGpDQLHGFD------YDEE---------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 190 esakfnvsgsnpenftTDFLTTRSLEILER-DKGKPFCLMLSIPDPHGPNSVRPPYDTMfknfHFENPRtmdvpvesmpi 268
Cdd:cd16032 115 ----------------VAFKAVQKLYDLARgEDGRPFFLTVSFTHPHDPYVIPQEYWDL----YVRRAR----------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 269 waqggkelvselnqkqmQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKGSPFETSAKIPFL 348
Cdd:cd16032 164 -----------------RAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSARVPLI 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 349 IRYPEKIAPGKmIHTAYTTVDFPQTILGIMGAPGIPGSQGLnDAKAFTSPAKKVEDG--RVTYITASASGWVAAV----N 422
Cdd:cd16032 227 ISAPGRFAPRR-VAEPVSLVDLLPTLVDLAGGGTAPHVPPL-DGRSLLPLLEGGDSGgeDEVISEYLAEGAVAPCvmirR 304
|
410 420
....*....|....*....|...
gi 1395161701 423 NRCKLVISESDIPWLFDLKKDPD 445
Cdd:cd16032 305 GRWKFIYCPGDPDQLFDLEADPL 327
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
68-380 |
1.48e-48 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 171.84 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 68 TPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSPVNNM-PMHDGLATFASVLKDQGYATSYVGKWHLDGDA 146
Cdd:pfam00884 26 TPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPvGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 147 KPGFepaRKFGFSdnrYMMnrGHWKGLSNINGKPAVIGLIPEKEsakfnVSgsnpenftTDFLTTRSLEILERDkGKPFC 226
Cdd:pfam00884 106 NQSP---CNLGFD---KFF--GRNTGSDLYADPPDVPYNCSGGG-----VS--------DEALLDEALEFLDNN-DKPFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 227 LMLSIPDPHGPNSVRPPYDTMFKNFhfenprtmdvpvesmpiwaqggkELVSELNQKQMQIYFGMVKCIDDNVGRLLEWL 306
Cdd:pfam00884 164 LVLHTLGSHGPPYYPDRYPEKYATF-----------------------KPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKL 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161701 307 EANGLADNTIVVFTSDHGDLMGEHKKHNKGSPFETSAK----IPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGA 380
Cdd:pfam00884 221 EENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNAPEggyrVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
54-454 |
3.70e-48 |
|
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: 173.51 E-value: 3.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 54 DDQAFVWGeGVKVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSPVNNMP----------MHDGlATF 123
Cdd:cd16147 10 DDQDVELG-SMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPgggypkfwqnGLER-STL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 124 ASVLKDQGYATSYVGK----WHLDGDAK---PGFEpaRKFGFSDNRYMMNrghWKGLSNINGKPAVIGlipekesakfnv 196
Cdd:cd16147 88 PVWLQEAGYRTAYAGKylngYGVPGGVSyvpPGWD--EWDGLVGNSTYYN---YTLSNGGNGKHGVSY------------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 197 sgsnPENFTTDFLTTRSLEILER--DKGKPFCLMLSIPDPHGPNSVRPPYDTMFKNFHFENPRTM-DVPVESMPIW---- 269
Cdd:cd16147 151 ----PGDYLTDVIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPPPnNPDVSDKPHWlrrl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 270 ---AQGGKELVSELNQKQMQiyfgMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHK-KHNKGSPFETSAKI 345
Cdd:cd16147 227 pplNPTQIAYIDELYRKRLR----TLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRlPPGKRTPYEEDIRV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 346 PFLIRYPeKIAPGKMIHTAYTTVDFPQTILGIMGApgipgsqglndakaftsPAKKVEDGRVtyitasasgWVAAVNN-- 423
Cdd:cd16147 303 PLLVRGP-GIPAGVTVDQLVSNIDLAPTILDLAGA-----------------PPPSDMDGRS---------CGDSNNNty 355
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1395161701 424 RCKLVISESDIPW----------LFDLKKDPDELINFYLNP 454
Cdd:cd16147 356 KCVRTVDDTYNLLyfewctgfreLYDLTTDPYQLTNLAGDL 396
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
26-484 |
1.46e-46 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 171.39 E-value: 1.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 26 KSKKTNLLIIHTDEHNFRTLGCyrelMPDDQafvwgegvkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPI 105
Cdd:PRK13759 3 QTKKPNIILIMVDQMRGDCLGC----NGNKA---------VETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 106 ATGS-PVNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGD-AKPGFE----------PARKFG------FSDNRYMMnR 167
Cdd:PRK13759 70 HHGRvGYGDVVPWNYKNTLPQEFRDAGYYTQCIGKMHVFPQrNLLGFHnvllhdgylhSGRNEDksqfdfVSDYLAWL-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 168 GHWKGLS--------NINGKPAVIGLIPEKEsakfnvsgsNPENFTTdfltTRSLEILER-DKGKPFCLMLSIPDPHGPn 238
Cdd:PRK13759 149 EKAPGKDpdltdigwDCNSWVARPWDLEERL---------HPTNWVG----SESIEFLRRrDPTKPFFLKMSFARPHSP- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 239 sVRPP--YDTMFKNFHFENPRTMDVPVESMPIWAQGGKE-----LVSELNQKQMQIYFGMVKCIDDNVGRLLEWLEANGL 311
Cdd:PRK13759 215 -YDPPkrYFDMYKDADIPDPHIGDWEYAEDQDPEGGSIDalrgnLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 312 ADNTIVVFTSDHGDLMGEHKKHNKGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTV---DFPQTILGIMGAPgIP---- 384
Cdd:PRK13759 294 LDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNRGTVIDQVVelrDIMPTLLDLAGGT-IPddvd 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 385 GSQGLNDAKAFTSPAKKVEDGRVTYiTASASGWVaaVNNRCKLVisesdipW--------LFDLKKDPDELINFYLNPEY 456
Cdd:PRK13759 373 GRSLKNLIFGQYEGWRPYLHGEHAL-GYSSDNYL--TDGKWKYI-------WfsqtgeeqLFDLKKDPHELHNLSPSEKY 442
|
490 500
....*....|....*....|....*...
gi 1395161701 457 AQIGKTMMDELVRQMKaYNEPGLAKGKN 484
Cdd:PRK13759 443 QPRLREMRKKLVDHLR-GREEGFVKDGK 469
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-385 |
2.88e-44 |
|
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: 158.56 E-value: 2.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 30 TNLLIIHTDEHNFRTLGCYrelMPDDqafvwgegvkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATG- 108
Cdd:cd16149 1 PNILFILTDDQGPWALGCY---GNSE----------AVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGi 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 109 -----SPVNNMPMH-----DGLATFASVLKDQGYATSYVGKWHLDGDAkpgfeparkfgfsdnrymmnrghwkglsning 178
Cdd:cd16149 68 hdwivEGSHGKTKKpegylEGQTTLPEVLQDAGYRCGLSGKWHLGDDA-------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 179 kpaviglipekesakfnvsgsnpenftTDFLTTRsleileRDKGKPFCLMLSIPDPHGPnsvrppydtmfknfhfenprt 258
Cdd:cd16149 116 ---------------------------ADFLRRR------AEAEKPFFLSVNYTAPHSP--------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 259 mdvpvesmpiWAqggkelvselnqkqmqiYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEH---KKHNK 335
Cdd:cd16149 142 ----------WG-----------------YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHgiwGKGNG 194
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161701 336 GSP---FETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGA-----PGIPG 385
Cdd:cd16149 195 TFPlnmYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVdppadPRLPG 252
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
65-451 |
4.36e-44 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 162.37 E-value: 4.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 65 KVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSPVNNMPM------HDGLATFASVLKDQGYATSYVG 138
Cdd:cd16143 24 KIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGfsppliEPDRVTLAKMLKQAGYRTAMVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 139 KWHLdgdakpGFEPARKFGFSDNRYMMNRGHWkgLSNINGKPAVIGLipekeSAKFNVSGSNpenfTTDFLTTRSLEILE 218
Cdd:cd16143 104 KWHL------GLDWKKKDGKKAATGTGKDVDY--SKPIKGGPLDHGF-----DYYFGIPASE----VLPTLTDKAVEFID 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 219 --RDKGKPFCLMLSIPDPHGPNSVRPPYDtmfknfhfenprtmdvpvesmpiwaqgGKelvSELNQkqmqiYFGMVKCID 296
Cdd:cd16143 167 qhAKKDKPFFLYFALPAPHTPIVPSPEFQ---------------------------GK---SGAGP-----YGDFVYELD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 297 DNVGRLLEWLEANGLADNTIVVFTSDHG------DLMGEHKKHN--------KGSPFETSAKIPFLIRYPEKIAPGKMIH 362
Cdd:cd16143 212 WVVGRILDALKELGLAENTLVIFTSDNGpspyadYKELEKFGHDpsgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 363 TAYTTVDFPQTILGIMGAPgIPGSQGL---NDAKAFTSPAKKveDGRVTYITASASGWVA--------------AVNNRC 425
Cdd:cd16143 292 QLVSLTDLFATLAAIVGQK-LPDNAAEdsfSFLPALLGPKKQ--EVRESLVHHSGNGSFAirkgdwklidgtgsGGFSYP 368
|
410 420
....*....|....*....|....*..
gi 1395161701 426 KLVISESDIPW-LFDLKKDPDELINFY 451
Cdd:cd16143 369 RGKEKLGLPPGqLYNLSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-467 |
1.24e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 160.42 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 28 KKTNLLIIHTDEHNFRTLGCYrelmpddqafvwgeGVK-VDTPHIDSIAHDGAICTSYYA----SSPVCTPSRASFVTGL 102
Cdd:cd16155 1 KKPNILFILADDQRADTIGAL--------------GNPeIQTPNLDRLARRGTSFTNAYNmggwSGAVCVPSRAMLMTGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 103 YpiATGSPVNNMPMHD-GLATFASVLKDQGYATSYVGKWHLDgdakpgfeparkfgFSDnrymmnrghwkglsningkpA 181
Cdd:cd16155 67 T--LFHAPEGGKAAIPsDDKTWPETFKKAGYRTFATGKWHNG--------------FAD--------------------A 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 182 VIglipekesakfnvsgsnpenfttDFLTTRSleilerDKGKPFCLMLSIPDPHGPNSVRPPYDTMF--------KNF-- 251
Cdd:cd16155 111 AI-----------------------EFLEEYK------DGDKPFFMYVAFTAPHDPRQAPPEYLDMYppetiplpENFlp 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 252 -HFENPRTMDVPVEsMPIWAQGGKELVselnQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEH 330
Cdd:cd16155 162 qHPFDNGEGTVRDE-QLAPFPRTPEAV----RQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSH 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 331 KKHNKGSPFETSAKIPFLIRYPeKIAPGKMI-HTAYTTVDFPqTILGIMGAPGIPGSQGLNDAKAFTSPAKKVEDgrvTY 409
Cdd:cd16155 237 GLMGKQNLYEHSMRVPLIISGP-GIPKGKRRdALVYLQDVFP-TLCELAGIEIPESVEGKSLLPVIRGEKKAVRD---TL 311
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 410 ITASASGWVAAVNNRCKLVI--SESDIPWLFDLKKDPDELINFYLNPEYAQIGKTMMDEL 467
Cdd:cd16155 312 YGAYRDGQRAIRDDRWKLIIyvPGVKRTQLFDLKKDPDELNNLADEPEYQERLKKLLAEL 371
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-388 |
1.50e-42 |
|
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: 154.24 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYRelmpddqafvwgeGVKVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGsp 110
Cdd:cd16148 2 NVILIVIDSLRADHLGCYG-------------YDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 111 VNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGDAkPGFEparkFGFsdNRYMMNRGHwkglsningkpaviglipeke 190
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAVSSNPHLFGG-PGFD----RGF--DTFEDFRGQ--------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 191 sakfNVSGSNPENFTTDFLTTRSLEILER-DKGKPFCLMLSIPDPHGPnsvrppYDtmfknfhfenprtmdvpvesmpiw 269
Cdd:cd16148 119 ----EGDPGEEGDERAERVTDRALEWLDRnADDDPFFLFLHYFDPHEP------YL------------------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 270 aqggkelvselnqkqmqiYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHK---KHNkGSPFETSAKIP 346
Cdd:cd16148 165 ------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGlywGHG-SNLYDEQLHVP 225
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1395161701 347 FLIRYPEKiAPGKMIHTAYTTVDFPQTILGIMGAPGIPGSQG 388
Cdd:cd16148 226 LIIRWPGK-EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDG 266
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-382 |
6.92e-42 |
|
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: 153.90 E-value: 6.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEhnfrtlgcyrelmpdDQAFVWGEGVKVDT--PHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATG 108
Cdd:cd16035 2 NILLILTDQ---------------ERYPPPWPAGWAALnlPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 109 SPVN-NMPMHDGLA----TFASVLKDQGYATSYVGKWHLDGDAKPGFEparkfgfSDNRYmmnrghwkglsningkpavi 183
Cdd:cd16035 67 VTDTlGSPMQPLLSpdvpTLGHMLRAAGYYTAYKGKWHLSGAAGGGYK-------RDPGI-------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 184 glipeKESAKfnvsgsnpenfttDFLTTRsleILERDKGKPFCLMLSIPDPHgpnsvrppyDTMFknfhfenPRTMDvpv 263
Cdd:cd16035 120 -----AAQAV-------------EWLRER---GAKNADGKPWFLVVSLVNPH---------DIMF-------PPDDE--- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 264 esmpiwaqggKELVSELNqkqmqIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKG-SPFETS 342
Cdd:cd16035 160 ----------ERWRRFRN-----FYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGfNAYEEA 224
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1395161701 343 AKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPG 382
Cdd:cd16035 225 LHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDA 264
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
68-456 |
8.17e-42 |
|
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: 156.96 E-value: 8.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 68 TPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSPVNNMPM---HDGLATFASVLKDQGYATSYVGK-WHld 143
Cdd:cd16030 27 TPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFrkvAPDAVTLPQYFKENGYTTAGVGKiFH-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 144 gdakPGFEPARKFGFSDNRYMMNRGHWKglsNINGKPAVIGLIPEKESAKFNVSGSN-PENFTTDFLTTR-SLEILER-- 219
Cdd:cd16030 105 ----PGIPDGDDDPASWDEPPNPPGPEK---YPPGKLCPGKKGGKGGGGGPAWEAADvPDEAYPDGKVADeAIEQLRKlk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 220 DKGKPFCLMLSIPDPHGP-------------NSVRPPYDTMFKN--FHFENPRTMDVPVESMPIWAQGGKELVSELNQKQ 284
Cdd:cd16030 178 DSDKPFFLAVGFYKPHLPfvapkkyfdlyplESIPLPNPFDPIDlpEVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQAR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 285 --MQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHK---KHnkgSPFETSAKIPFLIRYPEKIAPGK 359
Cdd:cd16030 258 elRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGhwgKH---TLFEEATRVPLIIRAPGVTKPGK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 360 MIHTAYTTVD-FPqTILGIMGAPGIPGSQGLNDAKAFTSPAKKVEDGRVTYITASASGWVAAVNNR--------CKLVIS 430
Cdd:cd16030 335 VTDALVELVDiYP-TLAELAGLPAPPCLEGKSLVPLLKNPSAKWKDAAFSQYPRPSIMGYSIRTERyrytewvdFDKVGA 413
|
410 420
....*....|....*....|....*.
gi 1395161701 431 ESdipwLFDLKKDPDELINFYLNPEY 456
Cdd:cd16030 414 EE----LYDHKNDPNEWKNLANDPEY 435
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
68-449 |
1.12e-40 |
|
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: 152.70 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 68 TPHIDSIAHDGAICTSYYaSSPVCTPSRASFVTGLYPIATGspVNNMPMHDG--------LATFASVLKDQGYATSYVGK 139
Cdd:cd16029 26 TPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTG--MQHGVILAGepyglplnETLLPQYLKELGYATHLVGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 140 WHLdGDAKPGFEPARK-----FGF-------SDNRYMMNRGHWKGLSNINGKPAViglipekesakfnvsgSNPENFTTD 207
Cdd:cd16029 103 WHL-GFYTWEYTPTNRgfdsfYGYyggaedyYTHTSGGANDYGNDDLRDNEEPAW----------------DYNGTYSTD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 208 FLTTRSLEILER-DKGKPFCLMLSIPDPHGPNSV----RPPYDTMFKNFHFENPRTmdvpvesmpiwaqggkelvselnq 282
Cdd:cd16029 166 LFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVppeyADPYEDKFAHIKDEDRRT------------------------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 283 kqmqiYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHN-------KGSPFE----TSAKI--PFLI 349
Cdd:cd16029 222 -----YAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGGSnyplrggKNTLWEggvrVPAFVwsPLLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 350 RYPEKIAPGkMIHtaytTVD-FPqTILGIMG--APGIPGSQGLNDAKAFTSPAKKVED------GRVTYITASAsgwvAA 420
Cdd:cd16029 297 PKRGTVSDG-LMH----VTDwLP-TLLSLAGgdPDDLPPLDGVDQWDALSGGAPSPRTeillniDDITRTTGGA----AI 366
|
410 420
....*....|....*....|....*....
gi 1395161701 421 VNNRCKLVISesdiPWLFDLKKDPDELIN 449
Cdd:cd16029 367 RVGDWKLIVG----KPLFNIENDPCERND 391
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
67-381 |
2.67e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 151.21 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 67 DTPHIDSIAHDGAICTSYYASsPVCTPSRASFVTGLYPIATGspVNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGDA 146
Cdd:cd16151 25 KTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNY--VVFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 147 KPGFEPaRKFGFsDNRYMMnrgHWKGLSNINGKPA-VIGLIPEKESAKFNVSGSNPENFTtDFLttrsLEILERDKGKPF 225
Cdd:cd16151 102 GDGDYP-HEFGF-DEYCLW---QLTETGEKYSRPAtPTFNIRNGKLLETTEGDYGPDLFA-DFL----IDFIERNKDQPF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 226 CLMLSIPDPHGPNsvrppydtmfknfhfenprtmdVPVESMPIWAQGGKELvselnqKQMQIYFG-MVKCIDDNVGRLLE 304
Cdd:cd16151 172 FAYYPMVLVHDPF----------------------VPTPDSPDWDPDDKRK------KDDPEYFPdMVAYMDKLVGKLVD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 305 WLEANGLADNTIVVFTSDHGDLMGEHKKHN-------KGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGI 377
Cdd:cd16151 224 KLEELGLRENTIIIFTGDNGTHRPITSRTNgrevrggKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAEL 303
|
....
gi 1395161701 378 MGAP 381
Cdd:cd16151 304 AGAP 307
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-471 |
4.25e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 151.62 E-value: 4.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYrelmpddqafvwGEGVKVdTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSP 110
Cdd:cd16150 2 NIVIFVADQLRADSLGHL------------GNPAAV-TPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 111 VNNMPMHDGLATFASVLKDQGYATSYVGKWH-LDGDAKPGfeparkfGFSDNRYMMNRGhwkglsningkpAViglipek 189
Cdd:cd16150 69 TLHHLLRPDEPNLLKTLKDAGYHVAWAGKNDdLPGEFAAE-------AYCDSDEACVRT------------AI------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 190 esakfnvsgsnpenfttDFLTTRSLEilerdkgKPFCLMLSIPDPHGPNSVRPPYDTMFKNFH----FENPRTMDVPVES 265
Cdd:cd16150 123 -----------------DWLRNRRPD-------KPFCLYLPLIFPHPPYGVEEPWFSMIDREKlpprRPPGLRAKGKPSM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 266 MPIWAQGGKELVSELNQKQMQ-IYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKG-SPFETS- 342
Cdd:cd16150 179 LEGIEKQGLDRWSEERWRELRaTYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWpNTFEDCl 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 343 AKIPFLIRyPEKIAPGKMIHTAYTTVDFPQTILGIMG------------APGIPGSQGLNDAKAFTspakkvEDGRVTYI 410
Cdd:cd16150 259 TRVPLIIK-PPGGPAGGVSDALVELVDIPPTLLDLAGiplshthfgrslLPVLAGETEEHRDAVFS------EGGRLHGE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 411 TASASG--------W---------------VAAVNNRCKLVISESDIPWLFDLKKDPDELINFYLNPEYAQIGKTMMDEL 467
Cdd:cd16150 332 EQAMEGghgpydlkWprllqqeeppehtkaVMIRTRRYKYVYRLYEPDELYDLEADPLELHNLIGDPAYAEIIAEMKQRL 411
|
....
gi 1395161701 468 VRQM 471
Cdd:cd16150 412 LRWM 415
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-446 |
5.67e-39 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 147.29 E-value: 5.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 31 NLLIIHTDEHNFRTLGCYRElmpddqafvwGEGVKVDTPHIDSIAHDGAICTSYYASsPVCTPSRASFVTGLYPIATG-- 108
Cdd:cd16142 2 NILVILGDDIGWGDLGCYGG----------GIGRGAPTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTGlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 109 SPVnnMP-----MHDGLATFASVLKDQGYATSYVGKWHLdGDaKPGFEPARKfGFSDnrymmnrghWKGlsningkpavi 183
Cdd:cd16142 71 TVG--LPgspggLPPWEPTLAELLKDAGYATAQFGKWHL-GD-EDGRLPTDH-GFDE---------FYG----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 184 glipekesakfnvsgsNPENFTTDFLTTRSLEILER--DKGKPFCLMLSIPDPHGPNSVRPPYDTMfknfhfenprtmdv 261
Cdd:cd16142 126 ----------------NLYHTIDEEIVDKAIDFIKRnaKADKPFFLYVNFTKMHFPTLPSPEFEGK-------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 262 pVESMPIWAQGGKELvselnqkqmqiyfgmvkciDDNVGRLLEWLEANGLADNTIVVFTSDHGDLM------------GE 329
Cdd:cd16142 176 -SSGKGKYADSMVEL-------------------DDHVGQILDALDELGIADNTIVIFTTDNGPEQdvwpdggytpfrGE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 330 hkkhnKGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAP-GIPGSQGLN------DAKAFTSpaKKV 402
Cdd:cd16142 236 -----KGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPdPKDKLLGKDrhidgvDQSPFLL--GKS 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161701 403 EDGRVTYITASASGWVAAVN-NRCKLVISESD--------------IPWLFDLKKDPDE 446
Cdd:cd16142 309 EKSRRSEFFYFGEGELGAVRwKNWKVHFKAQEdtggptgepfyvltFPLIFNLRRDPKE 367
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
28-449 |
9.56e-39 |
|
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: 147.59 E-value: 9.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 28 KKTNLLIIHTDEHNFRTLGCYrelmpddqafvwgeGVKVDTPHIDSIAHDGAICTSYYASsPVCTPSRASFVTGLYP--- 104
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCF--------------GGEIPTPNLDALAAEGLRFTNFHTT-ALCSPTRAALLTGRNHhqv 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 105 -------IATGSPVNNMPMHDGLATFASVLKDQGYATSYVGKWHLDGDakpGFeparkfgfsdnrymmnrghwkglsnin 177
Cdd:cd16025 66 gmgtmaeLATGKPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD---DY--------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 178 gkpaviglipekesakfnvsgsnpenFTTDFLTTRSLEILE--RDKGKPFCLMLSIPDPHGPNSVRPPYDTMFKNFH--- 252
Cdd:cd16025 116 --------------------------YSTDDLTDKAIEYIDeqKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKYdag 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 253 --------FENPRTM-----DVPV----ESMPIWaqggKELVSE---LNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLA 312
Cdd:cd16025 170 wdalreerLERQKELglipaDTKLtprpPGVPAW----DSLSPEekkLEARRMEVYAAMVEHMDQQIGRLIDYLKELGEL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 313 DNTIVVFTSDHGdlmGEHK-----------KHNKGSPFETSAKIPFLIRYPEKIAPGKMIHTAYTTV-DFPQTILGIMGA 380
Cdd:cd16025 246 DNTLIIFLSDNG---ASAEpgwanasntpfRLYKQASHEGGIRTPLIVSWPKGIKAKGGIRHQFAHViDIAPTILELAGV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 381 PgIPGS---------QGLNDAKAFTSPAKKVEDgRVTY--ITASAS----GWVAAVNNRCKlviSESDIPWLFDLKKDPD 445
Cdd:cd16025 323 E-YPKTvngvpqlplDGVSLLPTLDGAAAPSRR-RTQYfeLFGNRAirkgGWKAVALHPPP---GWGDQWELYDLAKDPS 397
|
....
gi 1395161701 446 ELIN 449
Cdd:cd16025 398 ETHD 401
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-381 |
1.28e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 135.58 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 29 KTNLLIIHTDEHNFRTLGCYRELMPDDQAFVWGEgvkVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATG 108
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNAHTGKSESRLGY---VESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 109 SPVNNMPM---HDGLATFASVLKDQGYATSYVGKWHLDgdakpgfEPARKfgfsdnrymmnrghwkgLSNINgkpavigl 185
Cdd:cd16153 78 VYGFEAAHpalDHGLPTFPEVLKKAGYQTASFGKSHLE-------AFQRY-----------------LKNAN-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 186 ipekesakfnvsgsnpenftTDFLTTRSLEILERDKGKPFCLMLSIPDPHGPnsVRPPydtmfknfhfenprtmdvpves 265
Cdd:cd16153 126 --------------------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTP--VLPP---------------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 266 mpiwaqggKELVSELNqkqmqiYFGMVKCIDDNVGRLLEWLEANGLA---DNTIVVFTSDHGDLMGEHKKHNKGSPFETS 342
Cdd:cd16153 162 --------KEFRDRFD------YYAFCAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGILAKFTFWPQS 227
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1395161701 343 AKIPFLIRYPEKIA--PGKMIHTAYTTVDFPQTILGIMGAP 381
Cdd:cd16153 228 HRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTLLAAAGVD 268
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
68-381 |
5.03e-30 |
|
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: 124.32 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 68 TPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATG-SPVNNMPM------HDGL----ATFASVLKDQGYATSY 136
Cdd:cd16159 27 TPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGmASSHGMRVilftasSGGLppneTTFAEVLKQQGYSTAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 137 VGKWHL--------DGDAKP---GFE-----PA---RKFGFSDNRYMMnrghwkgLSNINGKPAVIGLIP---------- 187
Cdd:cd16159 107 IGKWHLglhcesrnDFCHHPlnhGFDyfyglPLtnlKDCGDGSNGEYD-------LSFDPLFPLLTAFVLitaltiflll 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 188 --EKESAKFNVS----------------GSNP-------ENF-----------TTDFLTTRSLEILERDKGKPFCLMLSI 231
Cdd:cd16159 180 ylGAVSKRFFVFllilsllfislfflllITNRyfncilmRNHevveqpmslenLTQRLTKEAISFLERNKERPFLLVMSF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 232 PDPHGPnsvrppydtMFKNFHFEnprtmdvpvesmpiwaqgGKElvselnqkQMQIYFGMVKCIDDNVGRLLEWLEANGL 311
Cdd:cd16159 260 LHVHTA---------LFTSKKFK------------------GRS--------KHGRYGDNVEEMDWSVGQILDALDELGL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 312 ADNTIVVFTSDHG------DLMGEHKKHNKG-------SPFETSAKIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIM 378
Cdd:cd16159 305 KDNTFVYFTSDNGghleeiSVGGEYGGGNGGiyggkkmGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALA 384
|
...
gi 1395161701 379 GAP 381
Cdd:cd16159 385 GAP 387
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
29-484 |
1.85e-29 |
|
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: 122.17 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 29 KTNLLIIHTDEHNFRTLGCYRElmPDDQafvwgegvkvdTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATG 108
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGH--PSSS-----------TPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 109 --------SPVNNMPMHDglATFASVLKDQGYATSYVGKWHLDGDAKPGFEPARkFGFsDNRYMMNRGHWKGL------- 173
Cdd:cd16158 68 vypgvfypGSRGGLPLNE--TTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTH-QGF-DHYLGIPYSHDQGPcqnltcf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 174 -----------SNINGKPAVIGLIPEKESAKFNVSGSNPENFTTDFLTTRSLEilerdkGKPFCLMLSIPDPHGPNsvrp 242
Cdd:cd16158 144 ppnipcfggcdQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKE------GKPFFLYYASHHTHYPQ---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 243 pydtmFKNFHFENpRTMDVPVesmpiwaqgGKELVSelnqkqmqiyfgmvkcIDDNVGRLLEWLEANGLADNTIVVFTSD 322
Cdd:cd16158 214 -----FAGQKFAG-RSSRGPF---------GDALAE----------------LDGSVGELLQTLKENGIDNNTLVFFTSD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 323 HG-DLMGEHK-------KHNKGSPFETSAKIPFLIRYPEKIAPGKMIHTAyTTVDFPQTILGIMGAPgIP---------- 384
Cdd:cd16158 263 NGpSTMRKSRggnagllKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELA-STLDILPTIAKLAGAP-LPnvtldgvdms 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 385 -----GSQGLNDAKAFTSPAKKVEDG---------RVTYITASASGWVAAVNNRCKLV--ISESDIPWLFDLKKDPDELI 448
Cdd:cd16158 341 pilfeQGKSPRQTFFYYPTSPDPDKGvfavrwgkyKAHFYTQGAAHSGTTPDKDCHPSaeLTSHDPPLLFDLSQDPSENY 420
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1395161701 449 NFYLNPEYAQIGKTMmdELVRQ-----MKaYNEPGLAKGKN 484
Cdd:cd16158 421 NLLGLPEYNQVLKQI--QQVKErfeasMK-FGESEINKGED 458
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
59-385 |
9.58e-27 |
|
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: 113.72 E-value: 9.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 59 VWGEGVKvDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSPVNNMPMH-------------DGLATFAS 125
Cdd:cd16157 19 VFGEPSR-ETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARnaytpqnivggipDSEILLPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 126 VLKDQGYATSYVGKWHLdgDAKPGFEPArKFGFSDnrymmnrghWKGLSNINGKP---AVIGLIPEKESAK--------F 194
Cdd:cd16157 98 LLKKAGYRNKIVGKWHL--GHRPQYHPL-KHGFDE---------WFGAPNCHFGPydnKAYPNIPVYRDWEmigryyeeF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 195 NVSGSNPENFTTDFLTTRSLEILER--DKGKPFCLMLSIPDPHGPNSVRPPYdtmfknfhfenprtmdvpvesmpiwaqg 272
Cdd:cd16157 166 KIDKKTGESNLTQIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPF---------------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 273 gkelvseLNQKQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKH---------NKGSPFETSA 343
Cdd:cd16157 218 -------LGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEQggsngpflcGKQTTFEGGM 290
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1395161701 344 KIPFLIRYPEKIAPGKMIHTAYTTVDFPQTILGIMGAPgIPG 385
Cdd:cd16157 291 REPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLP-IPS 331
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
66-445 |
6.20e-26 |
|
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: 109.94 E-value: 6.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 66 VDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSPVNNMPMHDGLATFASVLKDQGYATSYVGKwhLDGD 145
Cdd:cd16171 24 VDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYPTWMDRLEKHGYHTQKYGK--LDYT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 146 AKPGFEPARKFGFSDNRYMMNRGHWKGLSNINGkpaviglipekESAKFNVSGSNPENftTDfLTTRSLEILERDKGKPF 225
Cdd:cd16171 102 SGHHSVSNRVEAWTRDVPFLLRQEGRPTVNLVG-----------DRSTVRVMLKDWQN--TD-KAVHWIRKEAPNLTQPF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 226 CLMLSIPDPHgpnsvrpPY--DTMFKNFhfenprtmdvpvesmpiwaqGGKELVSELnqkqmqiYFGMVKCIDDNVGRLL 303
Cdd:cd16171 168 ALYLGLNLPH-------PYpsPSMGENF--------------------GSIRNIRAF-------YYAMCAETDAMLGEII 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 304 EWLEANGLADNTIVVFTSDHGDLMGEHKKHNKGSPFETSAKIPFLIRYPEkIAPGKMIHTAYTTVDFPQTILGIMGAPGI 383
Cdd:cd16171 214 SALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQP 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395161701 384 PGSQGLNDAKAFTSPAKKVEDGRVTY----------ITASASGWVAAVNNRCKLVISESD--IPWLFDLKKDPD 445
Cdd:cd16171 293 QNLSGYSLLPLLSESSIKESPSRVPHpdwvlsefhgCNVNASTYMLRTNSWKYIAYADGNsvPPQLFDLSKDPD 366
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
71-380 |
2.62e-24 |
|
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: 106.36 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 71 IDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSPVNNMPMHD----GL----ATFASVLKDQGYATSYVGKWHL 142
Cdd:cd16160 30 IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPwdigGLpkteVTMAEALKEAGYTTGMVGKWHL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 143 dgdakpGFEPARKfgfSDNRYM-MNRG------------HWkgLSNINGKPaviglIPEKESAK---FNVSGSNPENFTT 206
Cdd:cd16160 110 ------GINENNH---SDGAHLpSHHGfdfvgtnlpftnSW--ACDDTGRH-----VDFPDRSAcflYYNDTIVEQPIQH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 207 DFLTTRSLE----ILERDKGKPFCLMLSIPDPHGPnsvrppydtMFKNFHFEnprtmdvpvesmpiwaqggkelvselNQ 282
Cdd:cd16160 174 EHLTETLVGdaksFIEDNQENPFFLYFSFPQTHTP---------LFASKRFK--------------------------GK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 283 KQMQIYFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHG---DLMGEHK-----KHNKGSPFETSAKIPFLIRYPEK 354
Cdd:cd16160 219 SKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGphvEYCLEGGstgglKGGKGNSWEGGIRVPFIAYWPGT 298
|
330 340
....*....|....*....|....*.
gi 1395161701 355 IAPGKMiHTAYTTVDFPQTILGIMGA 380
Cdd:cd16160 299 IKPRVS-HEVVSTMDIFPTFVDLAGG 323
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
68-379 |
3.06e-24 |
|
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: 103.15 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 68 TPHIDSIAHDGAICTSYYASSPVCTPSRA--SFVTGLYPIATGSPVNNMPMHDGLATFASVLKDQGYATSYVgkwHldgd 145
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNPLPSLPSILKEQGYETIFI---H---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 146 akpgfePARKFGFSDNRYMMNRG--HWKGLSNINGkpavigliPEKESAKFNVSgsnpenftTDFLTTRSLEILERDKGK 223
Cdd:cd16015 99 ------GGDASFYNRDSVYPNLGfdEFYDLEDFPD--------DEKETNGWGVS--------DESLFDQALEELEELKKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 224 PFCL-MLSIpDPHGPNSVrPPYDTmfknfhfenprtmdvpvesmpiwaqgGKELVSELNQKQMQIYFGMVKCIDDNVGRL 302
Cdd:cd16015 157 PFFIfLVTM-SNHGPYDL-PEEKK--------------------------DEPLKVEEDKTELENYLNAIHYTDKALGEF 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395161701 303 LEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKGSPFEtSAKIPFLIRYPEKIAPGKmIHTAYTTVDFPQTILGIMG 379
Cdd:cd16015 209 IEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLD-LYRTPLLIYSPGLKKPKK-IDRVGSQIDIAPTLLDLLG 283
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
61-446 |
4.14e-24 |
|
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: 104.86 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 61 GEGVKVDTPHIDSIAHDGAICTSYYASSPVCTPSRASFVTGLYPIATGSPVNNMPMH-DGL----ATFASVLKDQGYATS 135
Cdd:cd16161 21 WAPNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSvGGLplneTTLAEVLRQAGYATG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 136 YVGKWHLdgdakpgfeparkfGFSDNRYMMNRG--HWKGlsningkpaviglIPEKESAKFnvsGSNPENFTTDFLTTRS 213
Cdd:cd16161 101 MIGKWHL--------------GQREAYLPNSRGfdYYFG-------------IPFSHDSSL---ADRYAQFATDFIQRAS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 214 leilerDKGKPFCLMLSIPDPHGPNSVRPPydtmfknfhFENPRTMDVPVesmpiwaqggKELVSELnqkqmqiyfgmvk 293
Cdd:cd16161 151 ------AKDRPFFLYAALAHVHVPLANLPR---------FQSPTSGRGPY----------GDALQEM------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 294 ciDDNVGRLLEWLEANGLADNTIVVFTSDHGDLM-----GEHKKHN-----------KGSPFETSAKIPFLIRYPEKIAP 357
Cdd:cd16161 193 --DDLVGQIMDAVKHAGLKDNTLTWFTSDNGPWEvkcelAVGPGTGdwqgnlggsvaKASTWEGGHREPAIVYWPGRIPA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 358 GKMIHTAYTTVDFPQTILGIMGAPGIPGSQ--GLNDAKAFTSPAKkvEDGRVTYITASAS---GWVAAVnnRC---KLVI 429
Cdd:cd16161 271 NSTSAALVSTLDIFPTVVALAGASLPPGRIydGKDLSPVLFGGSK--TGHRCLFHPNSGAagaGALSAV--RCgdyKAHY 346
|
410 420 430
....*....|....*....|....*....|..
gi 1395161701 430 SES---------------DIPWLFDLKKDPDE 446
Cdd:cd16161 347 ATGgalaccgstgpklyhDPPLLFDLEVDPAE 378
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
68-446 |
7.73e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 97.81 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 68 TPHIDSIAHDGAICTSYYASsPVCTPSRASFVTGLYPIATG--SPVNNMPM--HDGLATFASVLKDQGYATSYVGKWHLD 143
Cdd:cd16154 28 TPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGvlAVPDELLLseETLLQLLIKDATTAGYSSAVIGKWHLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 144 GDAkpgfeparkfgfSDNRYMMNRGHWKGLsningkpaVIGLIPEKESAKFNVSGSNPE--NFTTDFLTTRSLEILErDK 221
Cdd:cd16154 107 GND------------NSPNNPGGIPYYAGI--------LGGGVQDYYNWNLTNNGQTTNstEYATTKLTNLAIDWID-QQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 222 GKPFCLMLSIPDPHGPNSVrPPYDTMFKNfhfENPRTMDVPVESMPiwaqggkelvselnqkqmqIYFGMVKCIDDNVGR 301
Cdd:cd16154 166 TKPWFLWLAYNAPHTPFHL-PPAELHSRS---LLGDSADIEANPRP-------------------YYLAAIEAMDTEIGR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 302 LLEWLEANGLaDNTIVVFTSDHG------DLMGEhKKHNKGSPFETSAKIPFlirypekIAPGKMIHTAYT-------TV 368
Cdd:cd16154 223 LLASIDEEER-ENTIIIFIGDNGtpgqvvDLPYT-RNHAKGSLYEGGINVPL-------IVSGAGVERANEresalvnAT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 369 DFPQTILGIMG--APGIpgsqglNDAKAFTSPAKKVEDGRVTYITAS----ASGWVAAVNNRCKLVISESDIPWLFDLKK 442
Cdd:cd16154 294 DLYATIAELAGvdAAEI------HDSVSFKPLLSDVNASTRQYNYTEyespTTTGWATRNQYYKLIESENGQEELYDLIN 367
|
....
gi 1395161701 443 DPDE 446
Cdd:cd16154 368 DPSE 371
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
57-381 |
6.93e-20 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 93.56 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 57 AFVWGEGVkvdTPHIDSIAHDGAICTSYYAssPVCTPSRA--SFVTGLYPIATGSPVNNMPMHDgLATFASVLKDQGYAT 134
Cdd:COG1368 252 ALGNGKDV---TPFLDSLAKESLYFGNFYS--QGGRTSRGefAVLTGLPPLPGGSPYKRPGQNN-FPSLPSILKKQGYET 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 135 SYvgkWHldgdakpGFEPArkfgfSDNR--YMMNRG--HWKGLSNINGKPAVIGLIPEKEsakfnvsgsnpenfttdfLT 210
Cdd:COG1368 326 SF---FH-------GGDGS-----FWNRdsFYKNLGfdEFYDREDFDDPFDGGWGVSDED------------------LF 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 211 TRSLEILErDKGKPF-CLMLSIpDPHGPnsvrppydtmfknfhFENPRtmdvpvesmpiwaqgGKELVSELNQKQMQIYF 289
Cdd:COG1368 373 DKALEELE-KLKKPFfAFLITL-SNHGP---------------YTLPE---------------EDKKIPDYGKTTLNNYL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 290 GMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDH-GDLMGEHKKHNKGSPFetsaKIPFLIRYPeKIAPGKMIHTAYTTV 368
Cdd:COG1368 421 NAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHgPRSPGKTDYENPLERY----RVPLLIYSP-GLKKPKVIDTVGSQI 495
|
330
....*....|...
gi 1395161701 369 DFPQTILGIMGAP 381
Cdd:COG1368 496 DIAPTLLDLLGID 508
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
159-378 |
8.88e-15 |
|
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: 74.38 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 159 SDNRYMMNRGHWKGLSNINGKPAVIGLIPEKESAKFNVSGSNPENFTTDFLTTRSLEIL----ERDKGKPFCLMLSIPDP 234
Cdd:cd00016 51 APNHAALLTGAYPTLHGYTGNGSADPELPSRAAGKDEDGPTIPELLKQAGYRTGVIGLLkaidETSKEKPFVLFLHFDGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 235 HGPnsvrppydtmfknFHFENPrtmdvpvesmpiwaqggkelvselnqkQMQIYFGMVKCIDDNVGRLLEWLEANGLADN 314
Cdd:cd00016 131 DGP-------------GHAYGP---------------------------NTPEYYDAVEEIDERIGKVLDALKKAGDADD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161701 315 TIVVFTSDHGDLMGEH----KKHNKGSPFETSAKIPFLIRYPEKIAPGKmIHTAYTTVDFPQTILGIM 378
Cdd:cd00016 171 TVIIVTADHGGIDKGHggdpKADGKADKSHTGMRVPFIAYGPGVKKGGV-KHELISQYDIAPTLADLL 237
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
216-382 |
3.91e-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: 62.62 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 216 ILERDKGKPFCLMLSIPDPHGpNSVRPPYDTMFKNFHFENPRTMDVPVESMPIwaqggkelvseLNQKQMQIYFgmvkcI 295
Cdd:COG3083 374 LDQRDSDRPWFSYLFLDAPHA-YSFPADYPKPFQPSEDCNYLALDNESDPTPF-----------KNRYRNAVHY-----V 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 296 DDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKG-----SPFETSakIPFLIRYPEKiAPGKmIHTAYTTVDF 370
Cdd:COG3083 437 DSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQNYWGhnsnfSRYQLQ--VPLVIHWPGT-PPQV-ISKLTSHLDI 512
|
170
....*....|....*.
gi 1395161701 371 P----QTILGIMGAPG 382
Cdd:COG3083 513 VptlmQRLLGVQNPAS 528
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
299-379 |
1.04e-08 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 56.86 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 299 VGRLLEWLEANGlaDNTIVVFTSDHGDLMGEHKK--HNKGSPFETSAKIPFLI--------RYPEKIApGKMIHTAYTTV 368
Cdd:cd16017 199 LSQIIERLKKKD--KDAALIYFSDHGESLGENGLylHGAPYAPKEQYHVPFIIwssdsykqRYPVERL-RANKDRPFSHD 275
|
90
....*....|.
gi 1395161701 369 DFPQTILGIMG 379
Cdd:cd16017 276 NLFHTLLGLLG 286
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-324 |
3.97e-08 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 55.91 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 1 MNRRNFSMLASAtgitAMAGNALAGKSKKTNLLIIhtDehnfrtlGcyreLMPDDQAfvwgegvKVDTPHIDSIAHDGAI 80
Cdd:COG1524 1 MKRGLSLLLASL----LAAAAAAAPPAKKVVLILV--D-------G----LRADLLE-------RAHAPNLAALAARGVY 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 81 CTSYYASSPVCT-PSRASFVTGLYPIATG------------SPVNNMPMHDGLA---------TFASVLKDQGYATSYVG 138
Cdd:COG1524 57 ARPLTSVFPSTTaPAHTTLLTGLYPGEHGivgngwydpelgRVVNSLSWVEDGFgsnsllpvpTIFERARAAGLTTAAVF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 139 KWHLDGDakpgfeparkfGFSDnrymMNRGHWkglsnINGKPAVIGlipekesakfnvsgsnpeNFTTDFLTTRSLEILE 218
Cdd:COG1524 137 WPSFEGS-----------GLID----AARPYP-----YDGRKPLLG------------------NPAADRWIAAAALELL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 219 RDKgKPFCLMLSIPDP------HGPNSvrppydtmfknfhfenprtmdvpvesmpiwaqggKELVSELNQkqmqiyfgmv 292
Cdd:COG1524 179 REG-RPDLLLVYLPDLdyaghrYGPDS----------------------------------PEYRAALRE---------- 213
|
330 340 350
....*....|....*....|....*....|..
gi 1395161701 293 kcIDDNVGRLLEWLEANGLADNTIVVFTSDHG 324
Cdd:COG1524 214 --VDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
67-324 |
1.53e-07 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 53.58 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 67 DTPHIDSIAHDGAICTSYYASSPVCT-PSRASFVTGLYPIATGSPVNNMpmhdglatFASVLKDqgyatsyVGKWHLDGD 145
Cdd:pfam01663 19 LTPNLAALAKEGVSAPNLTPVFPTLTfPNHYTLVTGLYPGSHGIVGNTF--------YDPKTGE-------YLVFVISDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 146 AKPGF---EP----ARKFGFSDNRYMmnrghWKGlSNINgKPAVIGLIPEKESAKFNVSGSNPENFTTDFLTTR-SLEIL 217
Cdd:pfam01663 84 EDPRWwqgEPiwdtAAKAGVRAAALF-----WPG-SEVD-YSTYYGTPPRYLKDDYNNSVPFEDRVDTAVLQTWlDLPFA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 218 ERDKGKPFCLMLSIPDPhgpnsvrppyDTMFKNFHFENPRtmdvpvesmpiwaqggkelvselnqkqmqiYFGMVKCIDD 297
Cdd:pfam01663 157 DVAAERPDLLLVYLEEP----------DYAGHRYGPDSPE------------------------------VEDALRRVDR 196
|
250 260
....*....|....*....|....*..
gi 1395161701 298 NVGRLLEWLEANGLADNTIVVFTSDHG 324
Cdd:pfam01663 197 AIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
288-355 |
2.16e-07 |
|
uncharacterized Alkaline phosphatase subfamily; 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.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 52.91 E-value: 2.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161701 288 YFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKGSpFETSAkiPFL-IRYPEKI 355
Cdd:cd16021 178 YLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIRETLQGK-LEERL--PFLsISLPKWF 243
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
436-476 |
3.93e-07 |
|
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: 48.78 E-value: 3.93e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1395161701 436 W-LFDLKKDPDELINFYLNPEYAQIGKTMMDELVRQMKAYNE 476
Cdd:pfam16347 62 WeLYDLQKDPKEMNNVYGDPEYAEVQAELKEELEELRKQYKD 103
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
67-324 |
2.03e-06 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 49.51 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 67 DTPHIDSIAHDGAICTSYYASSPVCT-PSRASFVTGLYPIATGSpVNNMpMHDglatfaSVLKDQGYATSYVGKWHLDGd 145
Cdd:cd16018 21 LTPNLKRLAEEGVRAKYVKPVFPTLTfPNHYSIVTGLYPESHGI-VGNY-FYD------PKTNEEFSDSDWVWDPWWIG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 146 AKPGFEPARKFGFSDNRYMmnrghWKGlsningkpavigliPEKESAKFNVSGSNPENFTTDFLTTRSLE------ILER 219
Cdd:cd16018 92 GEPIWVTAEKAGLKTASYF-----WPG--------------SEVAIIGYNPTPIPLGGYWQPYNDSFPFEervdtiLEWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 220 DKGKPFCLMLSIPDP------HGPNSvrppydtmfknfhfenprtmdvpvesmpiwaqggkelvSELNQkqmqiyfgMVK 293
Cdd:cd16018 153 DLERPDLILLYFEEPdsaghkYGPDS--------------------------------------PEVNE--------ALK 186
|
250 260 270
....*....|....*....|....*....|.
gi 1395161701 294 CIDDNVGRLLEWLEANGLADNTIVVFTSDHG 324
Cdd:cd16018 187 RVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
288-353 |
2.99e-04 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 43.87 E-value: 2.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395161701 288 YFGMVKCIDDNVGRLLEWLEANGLADNTIVVFTSDHGDLMGEHKKHNKGSPFEtsaKIPFL-IRYPE 353
Cdd:pfam02995 306 DFNYASALDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLRRTSQGMLEE---RLPLMsIRYPP 369
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
292-379 |
2.40e-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: 40.86 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161701 292 VKCIDDNVGRLLEWLEANGladnTIVVFTSDHG--DLM------GEHKKHnkgspfeTSAKIPFLIRYPEK--------- 354
Cdd:cd16010 409 VEAVDECLGRIVEAVLENG----GTLLITADHGnaEEMidpetgGPHTAH-------TTNPVPFIIVDPGLkrkllkdgg 477
|
90 100
....*....|....*....|....*...
gi 1395161701 355 ---IAPgkmihtayttvdfpqTILGIMG 379
Cdd:cd16010 478 ladVAP---------------TILDLLG 490
|
|
| |
