|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
29-468 |
0e+00 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 689.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 29 EKPNVLFIAVDDLRPELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTVP 108
Cdd:cd16030 1 KKPNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 109 DVVTLTQQFMKHGYHSVGMGKIYHGSL---NDDP-SWDRYLKVKAKGYQLPETQAAIRAKTKGLNlkkmsrkkrsrltRG 184
Cdd:cd16030 81 DAVTLPQYFKENGYTTAGVGKIFHPGIpdgDDDPaSWDEPPNPPGPEKYPPGKLCPGKKGGKGGG-------------GG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 185 PATEMADVPDHLYRDGAIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLaENPFLPKDAPQWA 264
Cdd:cd16030 148 PAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 265 STNWGELRNYSDIPR------KGDLTEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHA 338
Cdd:cd16030 227 WNDLDDLPKYGDIPAlnpgdpKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 339 GWCKHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENPNRPWKPAAFSQYP 418
Cdd:cd16030 307 HWGKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLKNPSAKWKDAAFSQYP 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1718789962 419 RGSMMGYSMKTDRYRYTEWRERKsgKIVGRELYDHQHDSAENKNIANQPD 468
Cdd:cd16030 387 RPSIMGYSIRTERYRYTEWVDFD--KVGAEELYDHKNDPNEWKNLANDPE 434
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
11-490 |
2.18e-136 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 398.87 E-value: 2.18e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 11 FCLVIFSGCLASSNSVASEKPNVLFIAVDDLRP-ELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGL 89
Cdd:COG3119 4 LLLLLLALLAAAAAAAAAKRPNILFILADDLGYgDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 90 RPDSTKVYDLETHFRKTVP-DVVTLTQQFMKHGYHSVGMGKiyhgslnddpsWdrylkvkakgyqlpetqaairaktkgl 168
Cdd:COG3119 84 YPHRTGVTDNGEGYNGGLPpDEPTLAELLKEAGYRTALFGK-----------W--------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 169 nlkkmsrkkrsrltrgpatemadvpdHLYRDGAIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEI 248
Cdd:COG3119 126 --------------------------HLYLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 249 KLAENpFLPKDapqwastnwgelrnysdiprkgdLTEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWG 328
Cdd:COG3119 180 PLPPN-LAPRD-----------------------LTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTS 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 329 DHGWKLGEHA-GWCKHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENPNR 407
Cdd:COG3119 236 DNGPSLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 408 PWKPAAFSQYPRGsMMGYSMKTDRYRYTEWRERKSgkivGRELYDHQHDSAENKNIANqpDQKTVVGQLSRQLKKNWKGA 487
Cdd:COG3119 316 EWRDYLYWEYPRG-GGNRAIRTGRWKLIRYYDDDG----PWELYDLKNDPGETNNLAA--DYPEVVAELRALLEAWLKEL 388
|
...
gi 1718789962 488 VVP 490
Cdd:COG3119 389 GDP 391
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
31-485 |
2.70e-96 |
|
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: 295.57 E-value: 2.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTVPDV 110
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 111 VTLTQQFMKHGYHSVGMGKIYHGSLNDDPSWDrylkvkakgyqlpetqaairaktkglnlkkmsrkkrsrltrgpatEMA 190
Cdd:cd16027 81 KTLPELLREAGYYTGLIGKTHYNPDAVFPFDD---------------------------------------------EMR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 191 DVPDHLYRDGAIAEQALKTLQRQKQhQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLAenPFLPkDAPqwastnwgE 270
Cdd:cd16027 116 GPDDGGRNAWDYASNAADFLNRAKK-GQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVP--PYLP-DTP--------E 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 271 LRNysdiprkgDLTeeqalklrhGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGehagWCKHTNFELDT 350
Cdd:cd16027 184 VRE--------DLA---------DYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 351 RVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENPNRPWKPAAFSQYPRGSMMGY---SM 427
Cdd:cd16027 243 RVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGRDYVFAERDRHDETYDpirSV 322
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 428 KTDRYRYTE--WRErksgkivgrELYDHQHDSAENKNIANQPDQKTVVGQLSRQLKKNWK 485
Cdd:cd16027 323 RTGRYKYIRnyMPE---------ELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWMK 373
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
29-481 |
6.49e-89 |
|
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: 278.64 E-value: 6.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 29 EKPNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKtv 107
Cdd:cd16031 1 KRPNIIFILTDDHRYDaLGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 PDVVTLTQQFMKHGYHsVGM-GK--IYHGSLNDDPSWDRYLKVKAKGYQLPET--QAAIRAKTKGlnlkkmsrkkrsrlt 182
Cdd:cd16031 79 ASQPTYPKLLRKAGYQ-TAFiGKwhLGSGGDLPPPGFDYWVSFPGQGSYYDPEfiENGKRVGQKG--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 183 rgpatemadvpdhlYRDGAIAEQALKTLQRQKQhQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLAENPFLP--KDA 260
Cdd:cd16031 143 --------------YVTDIITDKALDFLKERDK-DKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDDDdyAGR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 261 PQWASTNWGELRNYSDIPrkgDLTEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHaGW 340
Cdd:cd16031 208 PEWAREQRNRIRGVLDGR---FDTPEKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEH-GL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 341 C-KHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENPN-RPWKPAAFSQY- 417
Cdd:cd16031 284 FdKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKpVDWRKEFYYEYy 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718789962 418 --------PRgsMMGysMKTDRYRYTEWrerkSGKIVGRELYDHQHDSAENKNIANQPDQKTVVGQLSRQLK 481
Cdd:cd16031 364 eepnfhnvPT--HEG--VRTERYKYIYY----YGVWDEEELYDLKKDPLELNNLANDPEYAEVLKELRKRLE 427
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-481 |
1.12e-88 |
|
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: 275.98 E-value: 1.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 29 EKPNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQ----QAVCSPSRTSLMTGlrpdsTKVYDLE-TH 102
Cdd:cd16155 1 KKPNILFILADDQRADtIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTG-----RTLFHAPeGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 103 FRKTVPDVVTLTQQFMKHGYHSVGMGKiYHgslNDdpswdrylkvkakgyqlpetqaairaktkglnlkkmsrkkrsrlt 182
Cdd:cd16155 76 KAAIPSDDKTWPETFKKAGYRTFATGK-WH---NG--------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 183 rgpatemadvpdhlyrdgaIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLAEN--PFLPKDA 260
Cdd:cd16155 107 -------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENflPQHPFDN 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 261 pqwastNWGELR--NYSDIPRkgdlTEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHA 338
Cdd:cd16155 168 ------GEGTVRdeQLAPFPR----TPEAVRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 339 GWCKHTNFELDTRVPLIIRAPQIQAsGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENPNRPWKPAAFsqyp 418
Cdd:cd16155 238 LMGKQNLYEHSMRVPLIISGPGIPK-GKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDTLY---- 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718789962 419 rGSMMGY--SMKTDRYRYTewreRKSGKIVGRELYDHQHDSAENKNIANQPDQKTVVGQLSRQLK 481
Cdd:cd16155 313 -GAYRDGqrAIRDDRWKLI----IYVPGVKRTQLFDLKKDPDELNNLADEPEYQERLKKLLAELK 372
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-480 |
3.95e-81 |
|
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: 257.92 E-value: 3.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVY----DLETHFRK 105
Cdd:cd16033 1 PNILFIMTDQQRYDtLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 106 TVPDVVTLTQQFMKHGYHSVGMGKiYHGSLNDDPSwDRylkvkakGYQlpetqaairaktkglnlkkmsrkkrsrltrgp 185
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGK-WHVGPEETPL-DY-------GFD-------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 186 atemADVPDHLYRDGAIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLAEN---PFLPKDAPQ 262
Cdd:cd16033 120 ----EYLPVETTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESfadDFEDKPYIY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 263 wastnwgelRNYSDIPRKGDLTEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAGWCK 342
Cdd:cd16033 196 ---------RRERKRWGVDTEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 343 HTN-FELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENPNRP-WKPAAFSQYPRG 420
Cdd:cd16033 267 GPFmYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPEdWRDEVVTEYNGH 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718789962 421 SMMGYSM--KTDRYRYTEwrerkSGKIVGrELYDHQHDSAENKNIANQPDQKTVVGQLSRQL 480
Cdd:cd16033 347 EFYLPQRmvRTDRYKYVF-----NGFDID-ELYDLESDPYELNNLIDDPEYEEILREMRTRL 402
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-434 |
2.28e-79 |
|
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: 250.15 E-value: 2.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTVPd 109
Cdd:cd16037 1 PNILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 110 vvTLTQQFMKHGYHSVGMGKI-YHGslNDDPSWDRYlkvkakgyqlpetqaairaktkglnlkkmsrkkrsrltrgpate 188
Cdd:cd16037 80 --SWGHALRAAGYETVLIGKLhFRG--EDQRHGFRY-------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 189 madvpdhlyrDGAIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRseiklaenpflpkdapqwastnw 268
Cdd:cd16037 112 ----------DRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLYVR----------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 269 gelrnysdiprkgdlteeqalKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAGWCKHTNFEL 348
Cdd:cd16037 159 ---------------------RARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 349 DTRVPLIIRAPQIqASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENPNrPWKPAAFSQYP-RGSMMGYSM 427
Cdd:cd16037 218 SVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPD-DPDRVVFSEYHaHGSPSGAFM 295
|
....*...
gi 1718789962 428 -KTDRYRY 434
Cdd:cd16037 296 lRKGRWKY 303
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-463 |
3.33e-75 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 242.09 E-value: 3.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYdleTHFRKTVP 108
Cdd:cd16034 1 KPNILFIFADQHRAQaLGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF---GNDVPLPP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 109 DVVTLTQQFMKHGY--------HSVGMGKIYHGSLNDDPS---------------WDRYLKvkaKGYQLPETqaairakt 165
Cdd:cd16034 78 DAPTIADVLKDAGYrtgyigkwHLDGPERNDGRADDYTPPperrhgfdywkgyecNHDHNN---PHYYDDDG-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 166 kglnlKKMSRKKRSrltrgpatemadvPDHLyrdgaiAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFV-APQKYWDLYD 244
Cdd:cd16034 147 -----KRIYIKGYS-------------PDAE------TDLAIEYLENQADKDKPFALVLSWNPPHDPYTtAPEEYLDMYD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 245 RSEIKLAENpfLPKDAPQwastnwgelrnysdiprkgdltEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIV 324
Cdd:cd16034 203 PKKLLLRPN--VPEDKKE----------------------EAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 325 ILWGDHGWKLGEHAGWCKHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLEN 404
Cdd:cd16034 259 VFTSDHGDMLGSHGLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLG 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718789962 405 PNRPWKPAA-------FSQYPRGSMMGYS-MKTDRYRYTEWRERKsgkivgRELYDHQHDSAENKNI 463
Cdd:cd16034 339 GKDDEPDSVllqcfvpFGGGSARDGGEWRgVRTDRYTYVRDKNGP------WLLFDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
31-397 |
3.88e-75 |
|
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: 236.18 E-value: 3.88e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTVPD 109
Cdd:cd16022 1 PNILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 110 VVTLTQQFMKHGYHSVGMGKiyhgslnddpsWdrylkvkakgyqlpetqaairaktkglnlkkmsrkkrsrltrgpatem 189
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGK-----------W------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 190 advpdHlyrdgaiaEQALKTLQRQKQhQKPFFLAVGFLKPHLPFVapqkywdlydrseiklaenpflpkdapqwastnwg 269
Cdd:cd16022 102 -----H--------DEAIDFIERRDK-DKPFFLYVSFNAPHPPFA----------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 270 elrnysdiprkgdlteeqalklrhgYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAG-WCKHTNFEL 348
Cdd:cd16022 133 -------------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEG 187
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1718789962 349 DTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTS 397
Cdd:cd16022 188 GIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
31-417 |
6.67e-72 |
|
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: 230.93 E-value: 6.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTVPd 109
Cdd:cd16032 1 PNILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 110 vvTLTQQFMKHGYHSVGMGKI-------YHGSLNDDpswdrylkvkakgyqlpETQAAIRAKtkglnLKKMSRKKRSRlt 182
Cdd:cd16032 80 --TFAHYLRAAGYRTALSGKMhfvgpdqLHGFDYDE-----------------EVAFKAVQK-----LYDLARGEDGR-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 183 rgpatemadvpdhlyrdgaiaeqalktlqrqkqhqkPFFLAVGFLKPHLPFVAPQKYWDLYDRseiklaenpflpkdapq 262
Cdd:cd16032 134 ------------------------------------PFFLTVSFTHPHDPYVIPQEYWDLYVR----------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 263 wastnwgelrnysdiprkgdlteeqalKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAGWCK 342
Cdd:cd16032 161 ---------------------------RARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYK 213
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718789962 343 HTNFELDTRVPLIIRAPQIQASGKTTrALVEFVDIYPTLCELARIPLPDH---LEGTSFKPLLENPNRPWKPAAFSQY 417
Cdd:cd16032 214 MSFFEGSARVPLIISAPGRFAPRRVA-EPVSLVDLLPTLVDLAGGGTAPHvppLDGRSLLPLLEGGDSGGEDEVISEY 290
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
26-486 |
8.65e-71 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 233.02 E-value: 8.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 26 VASEKPNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDstkvydleTHFR 104
Cdd:PRK13759 2 VQTKKPNIILIMVDQMRGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQW--------HHGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 105 KTVPDVV------TLTQQFMKHGYHSVGMGKI----------YHGSL----------NDDPSW----DRY---LKVKAKG 151
Cdd:PRK13759 74 VGYGDVVpwnyknTLPQEFRDAGYYTQCIGKMhvfpqrnllgFHNVLlhdgylhsgrNEDKSQfdfvSDYlawLREKAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 152 YQLPETqaairaktkGLNLKKMSRKKRSrltrgpatemADVPDHLYRDGAIAEQALKTLQRqKQHQKPFFLAVGFLKPHL 231
Cdd:PRK13759 154 KDPDLT---------DIGWDCNSWVARP----------WDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 232 PFVAPQKYWDLYDRSEIklaENPFLPkdapQWASTNWGELRNYSDIPRKGDLTEEQALKLRHGYYASVSFTDANIGKILD 311
Cdd:PRK13759 214 PYDPPKRYFDMYKDADI---PDPHIG----DWEYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 312 ELKRLELDDNTIVILWGDHGWKLGEHAGWCKHTNFELDTRVPLIIRAP---QIQASGKTTRALVEFVDIYPTLCELARIP 388
Cdd:PRK13759 287 ALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 389 LPDHLEGTSFKPLLENPNRPWKPaafsqYPRGS-MMGYS----MKTDRYRYTeWRERKsgkivGRE-LYDHQHDSAENKN 462
Cdd:PRK13759 367 IPDDVDGRSLKNLIFGQYEGWRP-----YLHGEhALGYSsdnyLTDGKWKYI-WFSQT-----GEEqLFDLKKDPHELHN 435
|
490 500
....*....|....*....|....
gi 1718789962 463 IANQPDQKTVVGQLSRQLKKNWKG 486
Cdd:PRK13759 436 LSPSEKYQPRLREMRKKLVDHLRG 459
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-480 |
4.23e-66 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 219.03 E-value: 4.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPdSTKVYDLETHFRKtvPD 109
Cdd:cd16150 1 PNIVIFVADQLRADsLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYP-HVNGHRTLHHLLR--PD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 110 VVTLTQQFMKHGYHSVGMGKiyhgslNDDPSWDrylkvKAKG-YQLPETqAAIRAktkglnlkkmsrkkrsrltrgpate 188
Cdd:cd16150 78 EPNLLKTLKDAGYHVAWAGK------NDDLPGE-----FAAEaYCDSDE-ACVRT------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 189 madvpdhlyrdgaiAEQALktlqRQKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEiklaenpfLPKDAPqwASTNW 268
Cdd:cd16150 121 --------------AIDWL----RNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDREK--------LPPRRP--PGLRA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 269 GELRNYSDIPRKGDL---TEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAGWCKHTN 345
Cdd:cd16150 173 KGKPSMLEGIEKQGLdrwSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 346 -FELD-TRVPLIIRAPQiQASGKTTRALVEFVDIYPTLCELARIPlPDHLE-GTSFKPLLENPNRPWKPAAFS------- 415
Cdd:cd16150 253 tFEDClTRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAGIP-LSHTHfGRSLLPVLAGETEEHRDAVFSeggrlhg 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 416 ------------QYPRGSMM----------GYSMKTDRYRYTeWRERKSGkivgrELYDHQHDSAENKNIANQPDQKTVV 473
Cdd:cd16150 331 eeqamegghgpyDLKWPRLLqqeeppehtkAVMIRTRRYKYV-YRLYEPD-----ELYDLEADPLELHNLIGDPAYAEII 404
|
....*..
gi 1718789962 474 GQLSRQL 480
Cdd:cd16150 405 AEMKQRL 411
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
31-480 |
1.53e-63 |
|
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: 212.89 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVydlethFRKTVP- 108
Cdd:cd16028 1 RNVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRS------VWNGTPl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 109 DV--VTLTQQFMKHGYHSVGMGKIyHGSLND------DPSWDRYLKVkAKGYQlpetqaairaktkglnlkkmsrkkrsr 180
Cdd:cd16028 75 DArhLTLALELRKAGYDPALFGYT-DTSPDPrglaplDPRLLSYELA-MPGFD--------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 181 ltrgPATEMADVPDHLYRDGAIAEQALKTLQRQKQhqKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLAE-NPFLPKD 259
Cdd:cd16028 126 ----PVDRLDEYPAEDSDTAFLTDRAIEYLDERQD--EPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPPIrAESLAAE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 260 APQ--WASTnWGELR----NYSDIPRKGDLTEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWK 333
Cdd:cd16028 200 AAQhpLLAA-FLERIeslsFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 334 LGEHAGWCKHTNFELDTRVPLIIRAPQIQA---SGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLEN-PNRPW 409
Cdd:cd16028 279 LGDHWLWGKDGFFDQAYRVPLIVRDPRREAdatRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGaQPSDW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 410 KPAAFSQY------PRGSMMGYSMKTDRYRYTEWRERKSgKIVGRE-----LYDHQHDSAENKNIANQPDQKTVVGQLSR 478
Cdd:cd16028 359 RDAVHYEYdfrdvsTRRPQEALGLSPDECSLAVIRDERW-KYVHFAalpplLFDLKNDPGELRDLAADPAYAAVVLRYAQ 437
|
..
gi 1718789962 479 QL 480
Cdd:cd16028 438 KL 439
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-482 |
3.72e-63 |
|
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: 211.25 E-value: 3.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDL-RPELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTV-- 107
Cdd:cd16144 1 PNIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 -------------PDVVTLTQQFMKHGYHSVGMGKiYHGSLNDDPSwdrylkVKAKGYqlpETQAAIRAKTKGLNLKKMS 174
Cdd:cd16144 81 tklipppsttrlpLEEVTIAEALKDAGYATAHFGK-WHLGGEGGYG------PEDQGF---DVNIGGTGNGGPPSYYFPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 175 RKKRSRLTRGPATEmadvpdhlYRDGAIAEQALKTLQRQKQhqKPFFLAVGFLKPHLPFVAPQKYWDLYDRseiklaenp 254
Cdd:cd16144 151 GKPNPDLEDGPEGE--------YLTDRLTDEAIDFIEQNKD--KPFFLYLSHYAVHTPIQARPELIEKYEK--------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 255 flpKDAPQWAstnwgelrnysdiprkgdlteeqalKLRHGYYAS-VSFTDANIGKILDELKRLELDDNTIVILWGDHG-- 331
Cdd:cd16144 212 ---KKKGLRK-------------------------GQKNPVYAAmIESLDESVGRILDALEELGLADNTLVIFTSDNGgl 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 332 WKLGEHA-------GWcKHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPD--HLEGTSFKPLL 402
Cdd:cd16144 264 STRGGPPtsnaplrGG-KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 403 ENPNRPWKPAAF-----SQYPRGSMMGYSMKTDRYRYTEWRERKSgkivgRELYDHQHDSAENKNIANQPDQKtvVGQLS 477
Cdd:cd16144 343 KGGEADLPRRALfwhfpHYHGQGGRPASAIRKGDWKLIEFYEDGR-----VELYNLKNDIGETNNLAAEMPEK--AAELK 415
|
....*
gi 1718789962 478 RQLKK 482
Cdd:cd16144 416 KKLDA 420
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
31-485 |
8.46e-62 |
|
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: 207.40 E-value: 8.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDL-RPELGCYGATHIKSPNIDRLAASGLLFERAYcQQAVCSPSRTSLMTGLRPDSTKVYDleTHFRKTV-- 107
Cdd:cd16146 1 PNVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWH--TILGRERmr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 PDVVTLTQQFMKHGYHSvGM-GK-------------------IYHGS---------LNDDPSWDRYL----KVKAKGYql 154
Cdd:cd16146 78 LDETTLAEVFKDAGYRT-GIfGKwhlgdnypyrpqdrgfdevLGHGGggigqypdyWGNDYFDDTYYhngkFVKTEGY-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 155 petqaairaktkglnlkkmsrkkrsrltrgpateMADVpdhlyrdgaIAEQALKTLQRQKQhqKPFFLAVGFLKPHLPFV 234
Cdd:cd16146 155 ----------------------------------CTDV---------FFDEAIDFIEENKD--KPFFAYLATNAPHGPLQ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 235 APQKYWDLYdrseiklaenpflpkdapqwastnwgelrnysdipRKGDLTEEQAlklrhGYYASVSFTDANIGKILDELK 314
Cdd:cd16146 190 VPDKYLDPY-----------------------------------KDMGLDDKLA-----AFYGMIENIDDNVGRLLAKLK 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 315 RLELDDNTIVILWGDHGWKLGEHAGW------CKHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIP 388
Cdd:cd16146 230 ELGLEENTIVIFMSDNGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVK 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 389 LPDH--LEGTSFKPLLENPNRPWKPAA-FSQYPRG-----SMMGYSMKTDRYRYTewrerkSGKIVGRELYDHQHDSAEN 460
Cdd:cd16146 310 LPEGikLDGRSLLPLLKGESDPWPERTlFTHSGRWppppkKKRNAAVRTGRWRLV------SPKGFQPELYDIENDPGEE 383
|
490 500
....*....|....*....|....*.
gi 1718789962 461 KNIANQ-PDqktVVGQLSRQLKKNWK 485
Cdd:cd16146 384 NDVADEhPE---VVKRLKAAYEAWWD 406
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-397 |
4.47e-61 |
|
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: 201.45 E-value: 4.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDLRPE-LGCYG----------ATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYD 98
Cdd:cd16153 1 KPNILWIITDDQRVDsLSCYNnahtgksesrLGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 99 LETHFRKTVPDVVTLTQQFMKHGYHSVGMGKIYHGSLNddpswdRYLKVKAKGYQLPETQAAIRAKTKglnlkkmsrkkr 178
Cdd:cd16153 81 FEAAHPALDHGLPTFPEVLKKAGYQTASFGKSHLEAFQ------RYLKNANQSYKSFWGKIAKGADSD------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 179 srltrgpatemadvpdhlyrdgaiaeqalktlqrqkqhqKPFFLAVGFLKPHLPFVAPQKYWDLYDrseiklaenpflpk 258
Cdd:cd16153 143 ---------------------------------------KPFFVRLSFLQPHTPVLPPKEFRDRFD-------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 259 dapqwastnwgelrnysdiprkgdlteeqalklrhgYYASVSFTDANIGKILDELKRLELD---DNTIVILWGDHGWKLG 335
Cdd:cd16153 170 ------------------------------------YYAFCAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLG 213
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718789962 336 EHAGWCKHTNFELDTRVPLIIRAPQIQASGKTTRA--LVEFVDIYPTLCELARIPL--PDHLEGTS 397
Cdd:cd16153 214 EQGILAKFTFWPQSHRVPLIVVSSDKLKAPAGKVRhdFVEFVDLAPTLLAAAGVDVdaPDYLDGRD 279
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-466 |
7.60e-60 |
|
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: 202.44 E-value: 7.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRP-ELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTV-- 107
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 PDVVTLTQQFMKHGYHSVGMGKIYHGSLNDDPS-----WDR---YLK-VKAKGYqLPETQaaIRaktkglNLKKMSRKKR 178
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHptkqgFDYfygYLDqVHAHNY-YPEYL--WR------NGEKVPLPNN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 179 SRLTRGPAtEMADVPDHLYRDGAIAEQALKTLQRQKQhqKPFFLAVGFLKPHLPFVAPqkywdlydrseiKLAENPFLPK 258
Cdd:cd16145 152 VIPPLDEG-NNAGGGGGTYSHDLFTDEALDFIRENKD--KPFFLYLAYTLPHAPLQVP------------DDGPYKYKPK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 259 DAPQWASTNWGElrnysdiPRKGdlteeqalklrhgYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGwklGEHA 338
Cdd:cd16145 217 DPGIYAYLPWPQ-------PEKA-------------YAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG---PHSE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 339 GWCKHTNFELDT----------------RVPLIIRAP-QIQAsGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPL 401
Cdd:cd16145 274 GGSEHDPDFFDSngplrgykrslyeggiRVPFIARWPgKIPA-GSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPT 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718789962 402 L--ENPNRPWKPAAFSQYPRGSMMGYSMKtdryrytEWRERKSGKIVGR-ELYDHQHDSAENKNIANQ 466
Cdd:cd16145 353 LlgKPQQQQHDYLYWEFYEGGGAQAVRMG-------GWKAVRHGKKDGPfELYDLSTDPGETNNLAAQ 413
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-482 |
1.24e-58 |
|
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: 197.84 E-value: 1.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVydlethFRKTVP 108
Cdd:cd16152 1 KPNVIVFFTDQQRWDtLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC------FRNGIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 109 ---DVVTLTQQFMKHGYHSVGMGKiyhgslnddpsWdrylkvkakgyqlpetqaairaktkglnlkkmsrkkrsrltrgp 185
Cdd:cd16152 75 lpaDEKTLAHYFRDAGYETGYVGK-----------W-------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 186 atemadvpdHL--YRDGAIAEQALKTLqRQKQHQKPFFLAVGFLKPHLP-----FVAPQKYWDLYdrseiklaENPFLPK 258
Cdd:cd16152 100 ---------HLagYRVDALTDFAIDYL-DNRQKDKPFFLFLSYLEPHHQndrdrYVAPEGSAERF--------ANFWVPP 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 259 DapqwastnwgeLRnysdiPRKGDLTEEQAlklrhGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGwklgeha 338
Cdd:cd16152 162 D-----------LA-----ALPGDWAEELP-----DYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHG------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 339 gwC---------KHTNFELDTRVPLIIRAPQIQAsGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENPNRPW 409
Cdd:cd16152 214 --ChfrtrnaeyKRSCHESSIRVPLVIYGPGFNG-GGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDW 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 410 KPAAFSQYpRGSMMGYSMKTDRYRY-------TEWRERKSGKIVGRELYDHQHDSAENKNIANQPDQKTVVGQLSRQLKK 482
Cdd:cd16152 291 RNEVFIQI-SESQVGRAIRTDRWKYsvaapdkDGWKDSGSDVYVEDYLYDLEADPYELVNLIGRPEYREVAAELRERLLA 369
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-400 |
4.85e-55 |
|
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: 185.06 E-value: 4.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPdstkvYDLETHFRKTVPD 109
Cdd:cd16148 1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-----FYHGVWGGPLEPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 110 VVTLTQQFMKHGYHSVGMGKIYHgsLNDDPSWDRylkvkakGYQLPEtqaairaktkglnlkkmsrkkrsrltRGPATEM 189
Cdd:cd16148 76 DPTLAEILRKAGYYTAAVSSNPH--LFGGPGFDR-------GFDTFE--------------------------DFRGQEG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 190 ADVPDHLYRDGAIAEQALKTLQRQKQHqKPFFLAVGFLKPHLPFvapqkywdLYDrseiklaenpflpkdapqwastnwg 269
Cdd:cd16148 121 DPGEEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPY--------LYD------------------------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 270 elrnysdiprkgdlteeqalklrhgyyASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAGWCKHtNFELD 349
Cdd:cd16148 167 ---------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGH-GSNLY 218
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1718789962 350 ---TRVPLIIRAPQiQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKP 400
Cdd:cd16148 219 deqLHVPLIIRWPG-KEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
31-480 |
1.30e-54 |
|
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: 189.90 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDlethfrKTVP- 108
Cdd:cd16156 1 KQFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWT------NCMAl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 109 --DVVTLTQQFMKHGYHSVGMGKI------YHGSLNDDPSWD--------RYLKvkakgyQLPEtqaairaktkglnlkK 172
Cdd:cd16156 75 gdNVKTIGQRLSDNGIHTAYIGKWhldggdYFGNGICPQGWDpdywydmrNYLD------ELTE---------------E 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 173 MSRKKRSRLTRGPATEMADVPDHLYRdgaIAEQALKTLQRQKQhqKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLAE 252
Cdd:cd16156 134 ERRKSRRGLTSLEAEGIKEEFTYGHR---CTNRALDFIEKHKD--EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 253 NPF-----LPKDAPQWASTNWGELRNysdiprkgdlteeqALKLRH-GYYASVSFTDANIGKILDELKrlELDDNTIVIL 326
Cdd:cd16156 209 NAYddlenKPLHQRLWAGAKPHEDGD--------------KGTIKHpLYFGCNSFVDYEIGRVLDAAD--EIAEDAWVIY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 327 WGDHGWKLGEHAGWCKHTN-FELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLLENP 405
Cdd:cd16156 273 TSDHGDMLGAHKLWAKGPAvYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 406 NRPWKPAAFSQYPR---------GSMMGYSMKTDRYrytewrerksgKIV-----GRELYDHQHDSAENKNIANQPDQKT 471
Cdd:cd16156 353 EIPENRGVFVEFGRyevdhdgfgGFQPVRCVVDGRY-----------KLVinllsTDELYDLEKDPYEMHNLIDDPDYAD 421
|
....*....
gi 1718789962 472 VVGQLSRQL 480
Cdd:cd16156 422 VRDQLHDEL 430
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-463 |
2.12e-50 |
|
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: 176.25 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPE-LGCYGATHIKSPNIDRLAASGLLFERAYcQQAVCSPSRTSLMTGLRPDSTKVydletHFRKTVPD 109
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYGGESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYV-----VFGYLDPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 110 VVTLTQQFMKHGYHSVGMGKIYHGSLNDDPS------WDRYLKvkakgYQLPETqaaIRAKTKGLNLKKMSRKKRSRLTR 183
Cdd:cd16151 75 QKTFGHLLKDAGYATAIAGKWQLGGGRGDGDyphefgFDEYCL-----WQLTET---GEKYSRPATPTFNIRNGKLLETT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 184 ----GPatemaDVpdhlyrdgaIAEQALKTLQRQKQhqKPFFLavgflkphlpfvapqkYWdlydrSEIkLAENPFLP-K 258
Cdd:cd16151 147 egdyGP-----DL---------FADFLIDFIERNKD--QPFFA----------------YY-----PMV-LVHDPFVPtP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 259 DAPQWastnwgelrNYSDIPRKGDLteeqalklrhGYY-ASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEH 337
Cdd:cd16151 189 DSPDW---------DPDDKRKKDDP----------EYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPIT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 338 AGWC-------KHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPD--HLEGTSFKPLLE-NPNR 407
Cdd:cd16151 250 SRTNgrevrggKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEdyPLDGRSFAPQLLgKTGS 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1718789962 408 PWKPAAFSQYPRGSMMGYSmktDRYRYTEWRERKSGKivgreLYDHQHDSAENKNI 463
Cdd:cd16151 330 PRREWIYWYYRNPHKKFGS---RFVRTKRYKLYADGR-----FFDLREDPLEKNPL 377
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
29-463 |
2.72e-50 |
|
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: 176.48 E-value: 2.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 29 EKPNVLFIAVDDLRP-ELGCYGAtHIKSPNIDRLAASGLLFERAYcQQAVCSPSRTSLMTGLRPdstkvydlethfrktv 107
Cdd:cd16025 1 GRPNILLILADDLGFsDLGCFGG-EIPTPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNH---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 pdvvtltqqfmkhgyHSVGMGKIYhgslNDDPSWDRYlkvkaKGYqLPETQAAIrAKTkglnLKKmsrkkrsrltRGPAT 187
Cdd:cd16025 63 ---------------HQVGMGTMA----ELATGKPGY-----EGY-LPDSAATI-AEV----LKD----------AGYHT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 188 EMA----DVPDHLYRDGAIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYD----------RSE-----I 248
Cdd:cd16025 103 YMSgkwhLGPDDYYSTDDLTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKgkydagwdalREErlerqK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 249 KL------AENPFLPKDAPQWASTNwgelrnysdiprkgdlTEEQALKLRHG--YYASVSFTDANIGKILDELKRLELDD 320
Cdd:cd16025 183 ELglipadTKLTPRPPGVPAWDSLS----------------PEEKKLEARRMevYAAMVEHMDQQIGRLIDYLKELGELD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 321 NTIVILWGD------HGWKlgeHAG-----WCKHTNFELDTRVPLIIRAP-QIQASGKTTRALVEFVDIYPTLCELARIP 388
Cdd:cd16025 247 NTLIIFLSDngasaePGWA---NASntpfrLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 389 LPDH--------LEGTSFKPLLENPNRPwkpaafsqyPRGSMMGYSMKTDRYRYTE-----WRERKSGKIVGRELYDHQH 455
Cdd:cd16025 324 YPKTvngvpqlpLDGVSLLPTLDGAAAP---------SRRRTQYFELFGNRAIRKGgwkavALHPPPGWGDQWELYDLAK 394
|
....*...
gi 1718789962 456 DSAENKNI 463
Cdd:cd16025 395 DPSETHDL 402
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-400 |
2.35e-49 |
|
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: 169.73 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRP-ELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTG-----------LRPDSTKVYD 98
Cdd:cd16149 1 PNILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGrmpsqhgihdwIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 99 LETHFrktVPDVVTLTQQFMKHGYHSvGM-GKiyhgslnddpsWdrylkvkakgyqlpetqaairaktkglnlkkmsrkk 177
Cdd:cd16149 81 KPEGY---LEGQTTLPEVLQDAGYRC-GLsGK-----------W------------------------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 178 rsrltrgpatemadvpdHLyrdgaiAEQALKTLQRQKQHQKPFFLAVGFLKPHLPfvapqkywdlydrseiklaenpflp 257
Cdd:cd16149 110 -----------------HL------GDDAADFLRRRAEAEKPFFLSVNYTAPHSP------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 258 kdapqwastnwgelrnysdiprkgdlteeqalklrHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEH 337
Cdd:cd16149 142 -----------------------------------WGYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHH 186
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718789962 338 AGWCKHT-----NFeLDT--RVPLIIRAP-QIQASGKTTrALVEFVDIYPTLCELARIPLPDH--LEGTSFKP 400
Cdd:cd16149 187 GIWGKGNgtfplNM-YDNsvKVPFIIRWPgVVPAGRVVD-SLVSAYDFFPTLLELAGVDPPADprLPGRSFAD 257
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
30-464 |
1.09e-47 |
|
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: 169.67 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDL-RPELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTV- 107
Cdd:cd16026 1 KPNIVVILADDLgYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 --PDVVTLTQQFMKHGYHSVGMGKiYHgsLNDDPSW-------DRYLKVKA----KGYQLPETQAAIRAKTKGLNLKKMS 174
Cdd:cd16026 81 lpPDEITIAEVLKKAGYRTALVGK-WH--LGHQPEFlptrhgfDEYFGIPYsndmWPFPLYRNDPPGPLPPLMENEEVIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 175 RKK-RSRLTRgpatemadvpdhLYrdgaiAEQALKTLQRQKQhqKPFFLAVGFLKPHLPFVAPQKYwdlYDRSEiklaen 253
Cdd:cd16026 158 QPAdQSSLTQ------------RY-----TDEAVDFIERNKD--QPFFLYLAHTMPHVPLFASEKF---KGRSG------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 254 pflpkdapqwastnWGElrnYsdiprkGDLTEEqalklrhgyyasvsfTDANIGKILDELKRLELDDNTIVILWGDHG-W 332
Cdd:cd16026 210 --------------AGL---Y------GDVVEE---------------LDWSVGRILDALKELGLEENTLVIFTSDNGpW 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 333 KLGEHAGWC-------KHTNFELDTRVPLIIRAP-QIQAsGKTTRALVEFVDIYPTLCELARIPLPDH--LEGTSFKPLL 402
Cdd:cd16026 252 LEYGGHGGSagplrggKGTTWEGGVRVPFIAWWPgVIPA-GTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLL 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718789962 403 EN-PNRPWKPAAFsqYPRGSM-----MG---YSMKTDRYRYTEWRERKSGKIVGRELYDHQHDSAENKNIA 464
Cdd:cd16026 331 LGgSKSPPHPFFY--YYDGGDlqavrSGrwkLHLPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-464 |
1.32e-45 |
|
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: 163.91 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRP-ELGCYGATH-IKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGlRpdstkvYDLETHFRKTV- 107
Cdd:cd16143 1 PNIVIILADDLGYgDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTG-R------YPWRSRLKGGVl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 ---------PDVVTLTQQFMKHGYHSVGMGKiYHGSLNDdpswdrylkvKAKGYQLPETQAAIRAK-TKGLnlkkmsrkK 177
Cdd:cd16143 74 ggfsppliePDRVTLAKMLKQAGYRTAMVGK-WHLGLDW----------KKKDGKKAATGTGKDVDySKPI--------K 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 178 RSRLTRG-------PATEMADVpdhlyrdgaIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFVAPqkywdlydrseikl 250
Cdd:cd16143 135 GGPLDHGfdyyfgiPASEVLPT---------LTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPS-------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 251 aenpflpkdaPQWA-STNWGelrnysdiPRkGDLTEEqalklrhgyyasvsfTDANIGKILDELKRLELDDNTIVI---- 325
Cdd:cd16143 192 ----------PEFQgKSGAG--------PY-GDFVYE---------------LDWVVGRILDALKELGLAENTLVIftsd 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 326 ---LWGDHGWKLGEHAGWC-------KHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDH--L 393
Cdd:cd16143 238 ngpSPYADYKELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaE 317
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718789962 394 EGTSFKPLLENPNRPW-KPAAFSQYPRGSMM---G---YSMKTDRYRYTEWRERKSGKIVGRELYDHQHDSAENKNIA 464
Cdd:cd16143 318 DSFSFLPALLGPKKQEvRESLVHHSGNGSFAirkGdwkLIDGTGSGGFSYPRGKEKLGLPPGQLYNLSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-435 |
1.53e-45 |
|
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: 161.22 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLR-PELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYD-LETHFRKTV- 107
Cdd:cd16035 1 PNILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLLs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 PDVVTLTQQFMKHGYHSVGMGKiyhgslnddpsWdrYLkvkakgyqlpetqaairaktkglnlkkmsrkkrSRLTRGPAT 187
Cdd:cd16035 81 PDVPTLGHMLRAAGYYTAYKGK-----------W--HL---------------------------------SGAAGGGYK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 188 emadvpdhlyRDGAIAEQA---LKTLQRQKQHQKPFFLAVGFLKPHlpfvapqkywDLYdrseiklaenpFLPKDAPQWA 264
Cdd:cd16035 115 ----------RDPGIAAQAvewLRERGAKNADGKPWFLVVSLVNPH----------DIM-----------FPPDDEERWR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 265 stnwgELRNYsdiprkgdlteeqalklrhgYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAGWCKHT 344
Cdd:cd16035 164 -----RFRNF--------------------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGF 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 345 N-FELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDH------LEGTSFKPLLEN-PNRPWKPAAFSQ 416
Cdd:cd16035 219 NaYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARateappLPGRDLSPLLTDaDADAVRDGILFT 298
|
410
....*....|....*....
gi 1718789962 417 YprgsmmgysmktDRYRYT 435
Cdd:cd16035 299 Y------------DRYKFA 305
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
31-385 |
1.01e-42 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 153.35 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLR-PELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTVPD 109
Cdd:pfam00884 1 PNVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 110 vvTLTQQFMKHGYHSVGMGKiYHGslnddpSWDRYLKVKAKGYQlpetqaaiRAKTKGLNLKKMSRKKRSRLTRgpatem 189
Cdd:pfam00884 81 --SLPDLLKRAGYNTGAIGK-WHL------GWYNNQSPCNLGFD--------KFFGRNTGSDLYADPPDVPYNC------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 190 advPDHLYRDGAIAEQALKTLQrqkQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRseiklaenpFLPKDAPQWASTNwg 269
Cdd:pfam00884 138 ---SGGGVSDEALLDEALEFLD---NNDKPFFLVLHTLGSHGPPYYPDRYPEKYAT---------FKPSSCSEEQLLN-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 270 elrnysdiprkgdlteeqalklrhGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAGWCKHTNFEL- 348
Cdd:pfam00884 201 ------------------------SYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNa 256
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1718789962 349 ---DTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELA 385
Cdd:pfam00884 257 pegGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLA 296
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
30-467 |
1.83e-42 |
|
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: 155.40 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDLRPELGcyGATHIKsPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDL------ETHF 103
Cdd:cd16147 1 RPNIVLILTDDQDVELG--SMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNsppgggYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 104 RKTVPDVVTLTQQFMKHGYHSVGMGKiY---HGSLNDD----PSWDRYlkvkakgyqlpetQAAIRAKTKGLNLKKMSRK 176
Cdd:cd16147 78 WQNGLERSTLPVWLQEAGYRTAYAGK-YlngYGVPGGVsyvpPGWDEW-------------DGLVGNSTYYNYTLSNGGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 177 KRSrltrgpatemADVPDHLYRDGAIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLAENPFL 256
Cdd:cd16147 144 GKH----------GVSYPGDYLTDVIANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPPPNN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 257 PK--DAPQWastnwgeLRnysdipRKGDLTEEQALKLRHGYYA------SVsftDANIGKILDELKRLELDDNTIVILWG 328
Cdd:cd16147 214 PDvsDKPHW-------LR------RLPPLNPTQIAYIDELYRKrlrtlqSV---DDLVERLVNTLEATGQLDNTYIIYTS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 329 DHGWKLGEHA-GWCKHTNFELDTRVPLIIRAPQIQAsGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSfkPLLENPNR 407
Cdd:cd16147 278 DNGYHLGQHRlPPGKRTPYEEDIRVPLLVRGPGIPA-GVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRS--CGDSNNNT 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718789962 408 pWKpaafsqyprgsmmgySMKTDRYR----YTEWRERKsgkivgRELYDHQHDSAENKNIANQP 467
Cdd:cd16147 355 -YK---------------CVRTVDDTynllYFEWCTGF------RELYDLTTDPYQLTNLAGDL 396
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
31-456 |
3.62e-37 |
|
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: 140.37 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRPELGCYGATH-IKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDletHFRKTVPD 109
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQvVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWN---NYKGLDPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 110 VVTLTQQFMKHGYHSVGMGKI-----YHGSLNDDPSWDRYLKVKAKGYQLPETqaairaktkglNLKKMSRKKRSRLtrg 184
Cdd:cd16171 78 YPTWMDRLEKHGYHTQKYGKLdytsgHHSVSNRVEAWTRDVPFLLRQEGRPTV-----------NLVGDRSTVRVML--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 185 patemadvpdhlyRDGAIAEQALKTLQRQKQ-HQKPFFLAVGFLKPHlPFVAPQkywdlydrseiklaenpflpkdapqw 263
Cdd:cd16171 144 -------------KDWQNTDKAVHWIRKEAPnLTQPFALYLGLNLPH-PYPSPS-------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 264 ASTNWGELRNysdiprkgdlteeqalkLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAGWCKH 343
Cdd:cd16171 184 MGENFGSIRN-----------------IRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKM 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 344 TNFELDTRVPLIIRAPQIQAsGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPLL------ENPNRPWKPA-AFSQ 416
Cdd:cd16171 247 SMYEGSSHVPLLIMGPGIKA-GQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLsessikESPSRVPHPDwVLSE 325
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1718789962 417 YpRGS---MMGYSMKTDRYRYTEWRErksGKIVGRELYDHQHD 456
Cdd:cd16171 326 F-HGCnvnASTYMLRTNSWKYIAYAD---GNSVPPQLFDLSKD 364
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-392 |
1.44e-30 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 121.87 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDL-RPELGCYG---ATHIKSPNIDRLAASGLLFERAYCQQAvCSPSRTSLMTGLRPdstkvydlethFRkt 106
Cdd:cd16142 1 PNILVILGDDIgWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP-----------IR-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 107 vpdvvtltqqfmkHGYHSVGMGKIYHGSLNDDPSWDRYLKvkAKGYQ---------------LPETQaairaktkGLNlk 171
Cdd:cd16142 67 -------------TGLTTVGLPGSPGGLPPWEPTLAELLK--DAGYAtaqfgkwhlgdedgrLPTDH--------GFD-- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 172 kmsrkkrsrltrgpatEMADVPDHLYrDGAIAEQALKTLQRQKQHQKPFFLAVGFLKPHLP-FVAPQkywdlydrseikl 250
Cdd:cd16142 122 ----------------EFYGNLYHTI-DEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPtLPSPE------------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 251 aenpFLPKdapqwaSTNWGElrnYSDiprkgdlteeqalklrhgyyaSVSFTDANIGKILDELKRLELDDNTIVIL---- 326
Cdd:cd16142 172 ----FEGK------SSGKGK---YAD---------------------SMVELDDHVGQILDALDELGIADNTIVIFttdn 217
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718789962 327 ------WGDHG---WKlGEhagwcKHTNFELDTRVPLIIRAP-QIQAsGKTTRALVEFVDIYPTLCELARIPLPDH 392
Cdd:cd16142 218 gpeqdvWPDGGytpFR-GE-----KGTTWEGGVRVPAIVRWPgKIKP-GRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-460 |
2.78e-27 |
|
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: 112.83 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDL----RPELGcYGATHIKSPNIDRLAASGLLFERAYCQqAVCSPSRTSLMTGLRPDSTKVydlethfrKT 106
Cdd:cd16154 1 PNILLIIADDQgldsSAQYS-LSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGV--------LA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 107 VPDVV----TLTQQFMK-----HGYHSVGMGKIYHG----SLNDDPSWDRYlkvkakgyqlpetqaairaktKGLNLKKM 173
Cdd:cd16154 71 VPDELllseETLLQLLIkdattAGYSSAVIGKWHLGgndnSPNNPGGIPYY---------------------AGILGGGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 174 SRKKRSRLTRGPATEmadvPDHLYRDGAIAEQALKTLQRQkqhQKPFFLAVGFLKPHLPFVAPQKywDLYDRseiklaen 253
Cdd:cd16154 130 QDYYNWNLTNNGQTT----NSTEYATTKLTNLAIDWIDQQ---TKPWFLWLAYNAPHTPFHLPPA--ELHSR-------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 254 pflpkdapqwastnwGELRNYSDI---PRKgdlteeqalklrhgYY-ASVSFTDANIGKILDELKRLELDdNTIVILWGD 329
Cdd:cd16154 193 ---------------SLLGDSADIeanPRP--------------YYlAAIEAMDTEIGRLLASIDEEERE-NTIIIFIGD 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 330 HG--------WKLGEHAgwcKHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPDHLEGTSFKPL 401
Cdd:cd16154 243 NGtpgqvvdlPYTRNHA---KGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPL 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1718789962 402 LENPNRPWKPAAFSQYPRGSMMGYSMKTDRYRYTEWRERKsgkivgRELYDHQHDSAEN 460
Cdd:cd16154 320 LSDVNASTRQYNYTEYESPTTTGWATRNQYYKLIESENGQ------EELYDLINDPSEQ 372
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
31-394 |
5.43e-27 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 112.26 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDL-RPELGCYGATHIKSPNIDRLAASGLLFERAYCQQaVCSPSRTSLMTGLrpdstkvYDLETHFRKTV-- 107
Cdd:cd16029 1 PHIVFILADDLgWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGR-------YPIHTGMQHGVil 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 --------PDVVTLTQQFMKHGYHSVGMGKIYHGSLNDD--PSW---DRYLkvkakGYQLPE----TQAAIRAKTKGLNl 170
Cdd:cd16029 73 agepyglpLNETLLPQYLKELGYATHLVGKWHLGFYTWEytPTNrgfDSFY-----GYYGGAedyyTHTSGGANDYGND- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 171 kkmsrkkRSRLTRGPATEMADVpdhlYRDGAIAEQALKTLQRQKQhQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEikl 250
Cdd:cd16029 147 -------DLRDNEEPAWDYNGT----YSTDLFTDRAVDIIENHDP-SKPLFLYLAFQAVHAPLQVPPEYADPYEDKF--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 251 aenpflpkdapqwastnwgelrnySDIPRKGdlteeqalklRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDH 330
Cdd:cd16029 212 ------------------------AHIKDED----------RRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDN 257
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718789962 331 G-WKLGEHAGW------CKHTNFELDTRVPLIIRAPQIQA-SGKTTRALVEFVDIYPTLCELARIPLPDHLE 394
Cdd:cd16029 258 GgPTGGGDGGSnyplrgGKNTLWEGGVRVPAFVWSPLLPPkRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPP 329
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
30-479 |
1.04e-25 |
|
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: 109.84 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDL-RPELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYD--LETHFRKT 106
Cdd:cd16158 1 PPNIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPgvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 107 VP-DVVTLTQQFMKHGYHSVGMGKiyhgslnddpsWdrYLKVKAKGYQLPETQAAIR------AKTKGLNLKKMSRKKRS 179
Cdd:cd16158 81 LPlNETTIAEVLKTVGYQTAMVGK-----------W--HLGVGLNGTYLPTHQGFDHylgipySHDQGPCQNLTCFPPNI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 180 RLTRGPATEMADVPdhLYRDGAIAEQALKTLQRQKQHQ--------------KPFFLAVGFLKPHLPFVAPQKYwdlydr 245
Cdd:cd16158 148 PCFGGCDQGEVPCP--LFYNESIVQQPVDLLTLEERYAkfakdfiadnakegKPFFLYYASHHTHYPQFAGQKF------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 246 seiklaenpflpkdapqwastnwgelRNYSDIPRKGDlteeqalklrhgyyaSVSFTDANIGKILDELKRLELDDNTIVI 325
Cdd:cd16158 220 --------------------------AGRSSRGPFGD---------------ALAELDGSVGELLQTLKENGIDNNTLVF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 326 LWGDHG----WKL-GEHAGW--C-KHTNFELDTRVPLIIRAPQIQASGKtTRALVEFVDIYPTLCELARIPLPD-HLEGT 396
Cdd:cd16158 259 FTSDNGpstmRKSrGGNAGLlkCgKGTTYEGGVREPAIAYWPGRIKPGV-THELASTLDILPTIAKLAGAPLPNvTLDGV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 397 SFKPLLENPNRPWKPAAFSQYPRGSMMG--YSMKTDRYR---YTEWRE----------RKSGKIVGRE---LYDHQHDSA 458
Cdd:cd16158 338 DMSPILFEQGKSPRQTFFYYPTSPDPDKgvFAVRWGKYKahfYTQGAAhsgttpdkdcHPSAELTSHDpplLFDLSQDPS 417
|
490 500
....*....|....*....|.
gi 1718789962 459 ENKNIANQPDQKTVVGQLSRQ 479
Cdd:cd16158 418 ENYNLLGLPEYNQVLKQIQQV 438
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
30-406 |
3.02e-25 |
|
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: 108.53 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDLR-PELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTkvyDLETHFRKTV- 107
Cdd:cd16159 1 KPNIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRS---GMASSHGMRVi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 108 ----------PDVVTLTQQFMKHGYHSVGMGKiYHGSLNDDPSWDRYLKVKAKG----YQLPETqaairaktkglNLKKM 173
Cdd:cd16159 78 lftassgglpPNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDFCHHPLNHGfdyfYGLPLT-----------NLKDC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 174 SRKKRSRLTRGPatemaDVPDHLYRDG-AIAEQALKTLQ-RQKQHQKPFF--LAVGFLKPHLPFVAPQ--KYWD--LYDR 245
Cdd:cd16159 146 GDGSNGEYDLSF-----DPLFPLLTAFvLITALTIFLLLyLGAVSKRFFVflLILSLLFISLFFLLLItnRYFNciLMRN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 246 SEIklAENP--------FLPKDAPQWASTNWGE----LRNYSDIPRKGDLTEEQALKLRHGYY-ASVSFTDANIGKILDE 312
Cdd:cd16159 221 HEV--VEQPmslenltqRLTKEAISFLERNKERpfllVMSFLHVHTALFTSKKFKGRSKHGRYgDNVEEMDWSVGQILDA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 313 LKRLELDDNTIVILWGDHGWKL------GEHAGWC-------KHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYP 379
Cdd:cd16159 299 LDELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGNggiyggkKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFP 378
|
410 420
....*....|....*....|....*....
gi 1718789962 380 TLCELARIPLPD--HLEGTSFKPLLENPN 406
Cdd:cd16159 379 TVAALAGAPLPSdrIIDGRDLMPLLTGQE 407
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
30-404 |
3.78e-25 |
|
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: 107.94 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDLR-PELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLETHFRKT-- 106
Cdd:cd16157 1 KPNIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 107 -------VPDV-VTLTQQFMKHGYHSVGMGKiYHgsLNDDPSwdrYLKVKakgYQLPETQAAIRAKTKGLNLKKMSRKkr 178
Cdd:cd16157 81 pqnivggIPDSeILLPELLKKAGYRNKIVGK-WH--LGHRPQ---YHPLK---HGFDEWFGAPNCHFGPYDNKAYPNI-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 179 srltrgPATEMADVPDHLYRDGAI-------------AEQALKTLQRQKQHQKPFFLavgflkphlpfvapqkYWDLYDR 245
Cdd:cd16157 150 ------PVYRDWEMIGRYYEEFKIdkktgesnltqiyLQEALEFIEKQHDAQKPFFL----------------YWAPDAT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 246 SEIKLAENPFLPKdapqwastnwgelrnySDIPRKGDLTEEqalklrhgyyasvsfTDANIGKILDELKRLELDDNTIVI 325
Cdd:cd16157 208 HAPVYASKPFLGT----------------SQRGLYGDAVME---------------LDSSVGKILESLKSLGIENNTFVF 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 326 LWGDHGWKL---GEHAG------WCKHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLPD--HLE 394
Cdd:cd16157 257 FSSDNGAALisaPEQGGsngpflCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSdrAID 336
|
410
....*....|
gi 1718789962 395 GTSFKPLLEN 404
Cdd:cd16157 337 GIDLLPVLLN 346
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
30-390 |
1.55e-23 |
|
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: 102.16 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDLR-PELGCYGA-THIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTG---LR--------PDSTKV 96
Cdd:cd16161 1 KPNFLLLFADDLGwGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGrlgLRngvghnflPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 97 YDL-EThfrktvpdvvTLTQQFMKHGYHSVGMGKIYHGSLnddpswDRYLKvKAKG----YQLPETQaairaktkglnlk 171
Cdd:cd16161 81 LPLnET----------TLAEVLRQAGYATGMIGKWHLGQR------EAYLP-NSRGfdyyFGIPFSH------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 172 kmsrkkrsrltrgpATEMADvpdhlyrdgAIAEQALKTLQRQKQHQKPFFLAVGFLKPHLPfvapqkywdlydrseikla 251
Cdd:cd16161 131 --------------DSSLAD---------RYAQFATDFIQRASAKDRPFFLYAALAHVHVP------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 252 eNPFLPKDAPqwastnwgelrnysdiprkgdlteeqALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHG 331
Cdd:cd16161 169 -LANLPRFQS--------------------------PTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNG 221
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718789962 332 --------------WKLGEHAGW--CKHTNFELDTRVPLIIRAPQIQASGKTTRALVEFVDIYPTLCELARIPLP 390
Cdd:cd16161 222 pwevkcelavgpgtGDWQGNLGGsvAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLP 296
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
21-435 |
1.48e-20 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 94.72 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 21 ASSNSVASEKPNVLFIAVDDL-RPELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLrPDSTKVYDL 99
Cdd:COG1368 225 TPNPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGL-PPLPGGSPY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 100 ETHFRKTVPdvvTLTQQFMKHGYHSVgmgkIYHGslnDDPSWDRYLKV-KAKGYQLPETQAAIRAKTKGlnlkkmsrkkr 178
Cdd:COG1368 304 KRPGQNNFP---SLPSILKKQGYETS----FFHG---GDGSFWNRDSFyKNLGFDEFYDREDFDDPFDG----------- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 179 srlTRGpatemadvpdhlYRDGAIAEQALKTLqrqKQHQKPFFLAVGFLKPHLPFVAPQKYWDLYDRSEIKLAEnpflpk 258
Cdd:COG1368 363 ---GWG------------VSDEDLFDKALEEL---EKLKKPFFAFLITLSNHGPYTLPEEDKKIPDYGKTTLNN------ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 259 dapqwastnwgelrnysdiprkgdlteeqalklrhgYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGwklGEHA 338
Cdd:COG1368 419 ------------------------------------YLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG---PRSP 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 339 GWCKHTNFELDTRVPLIIRAPQIQAsGKTTRALVEFVDIYPTLCELARIPLPdhlEGTSF-KPLLENPNRPWkpaafsqy 417
Cdd:COG1368 460 GKTDYENPLERYRVPLLIYSPGLKK-PKVIDTVGSQIDIAPTLLDLLGIDYP---SYYAFgRDLLSPDTDPF-------- 527
|
410
....*....|....*...
gi 1718789962 418 prgSMMGYSMKTDRYRYT 435
Cdd:COG1368 528 ---AFRNGGFITDDYVYV 542
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
30-402 |
1.05e-19 |
|
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: 91.34 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 30 KPNVLFIAVDDL-RPELGCYGATHIKSPNIDRLAASGLLFERAYCQQAVCSPSRTSLMTGLRPDSTKVYDLEthfRKTVP 108
Cdd:cd16160 1 KPNIVLFFADDMgYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGT---RVFLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 109 --------DVVTLTQQFMKHGYhSVGM-GKiYHGSLNDDPSWDRYLKVKAKGYQ-----LPETQaAIRAKTKGLNLKKMS 174
Cdd:cd16160 78 wdigglpkTEVTMAEALKEAGY-TTGMvGK-WHLGINENNHSDGAHLPSHHGFDfvgtnLPFTN-SWACDDTGRHVDFPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 175 RKKRSRLTRGPATEMADVPDHL---YRDGAiaeqalKTLQRQKQHqKPFFLAVGFLKPHlpfvapqkywdlydrseikla 251
Cdd:cd16160 155 RSACFLYYNDTIVEQPIQHEHLtetLVGDA------KSFIEDNQE-NPFFLYFSFPQTH--------------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 252 enpflpkdAPQWASTnwgELRNYSDIPRKGDlteeqalklrhgyyaSVSFTDANIGKILDELKRLELDDNTIVILWGDHg 331
Cdd:cd16160 207 --------TPLFASK---RFKGKSKRGRYGD---------------NINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDH- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 332 wklGEHAGWC------------KHTNFELDTRVPLIIRAPQIQASGKTTrALVEFVDIYPTLCELARIPLPD--HLEGTS 397
Cdd:cd16160 260 ---GPHVEYCleggstgglkggKGNSWEGGIRVPFIAYWPGTIKPRVSH-EVVSTMDIFPTFVDLAGGTLPTdrIYDGLS 335
|
....*
gi 1718789962 398 FKPLL 402
Cdd:cd16160 336 ITDLL 340
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
31-385 |
4.71e-19 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 87.35 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFI---AVDDLR--PELGCYGAThiksPNIDRLAASGLLFERAYcqqAVCSPSRTS-----LMTGLRPDSTKVYDLE 100
Cdd:cd16015 1 PNVIVIlleSFSDPYidKDVGGEDLT----PNLNKLAKEGLYFGNFY---SPGFGGGTAngefeVLTGLPPLPLGSGSYT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 101 THFRKTVPdvvTLTQQFMKHGYHSVGMgkiyHGSLNDdpSWDRYLKVKAKGYQlpetqaairaKTKGLNLKKMSRKKRSR 180
Cdd:cd16015 74 LYKLNPLP---SLPSILKEQGYETIFI----HGGDAS--FYNRDSVYPNLGFD----------EFYDLEDFPDDEKETNG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 181 LtrgpatemadvpdhLYRDGAIAEQALKTLQrqKQHQKPFFLavgF---LKPHLPFVAPQKYwdlydrseiklaenpflp 257
Cdd:cd16015 135 W--------------GVSDESLFDQALEELE--ELKKKPFFI---FlvtMSNHGPYDLPEEK------------------ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 258 KDAPQWASTNWGELRNYsdiprkgdlteeqalklrhgyYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEH 337
Cdd:cd16015 178 KDEPLKVEEDKTELENY---------------------LNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1718789962 338 AGWCKHTNFELDtRVPLIIRAPQIQASGKTTRaLVEFVDIYPTLCELA 385
Cdd:cd16015 237 YDETDEDPLDLY-RTPLLIYSPGLKKPKKIDR-VGSQIDIAPTLLDLL 282
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
31-385 |
4.67e-17 |
|
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: 80.54 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 31 PNVLFIAVDDLRP-ELGCYGATHIKSPNIDRLAASGLLFErAYCQQAVCS--PSRTSLMTGLRPDSTKVY-------DLE 100
Cdd:cd00016 1 KHVVLIVLDGLGAdDLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTSsaPNHAALLTGAYPTLHGYTgngsadpELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 101 THFRKTVPDVVTLTQQFMKHGYHSVGMGkiyhgslnddpswdrylkvkakgyqlpetqaairaktkglnlkkmsrkkrsr 180
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 181 ltrgpatemadvpdhlyrdgaiaeqALKTLQRQKQHqKPFFLAVGFLKPHLPFVAPqkywdlydrseiklaeNPFLPkda 260
Cdd:cd00016 108 -------------------------LLKAIDETSKE-KPFVLFLHFDGPDGPGHAY----------------GPNTP--- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 261 pqwastnwgelrnysdiprkgdlteeqalklrhGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAG- 339
Cdd:cd00016 143 ---------------------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGd 189
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1718789962 340 ---WCKHTNFELDTRVPLIIRAPQIQAsGKTTRALVEFVDIYPTLCELA 385
Cdd:cd00016 190 pkaDGKADKSHTGMRVPFIAYGPGVKK-GGVKHELISQYDIAPTLADLL 237
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
198-381 |
1.03e-12 |
|
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: 70.32 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 198 RDGAIAEQALKTLQRQKqHQKPFFLAVGFLKPHlPFVAPQKYwdlydrseiklaENPFLPkdapqwastnwgelrnYSDI 277
Cdd:COG3083 362 RDRQITAQWLQWLDQRD-SDRPWFSYLFLDAPH-AYSFPADY------------PKPFQP----------------SEDC 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 278 PRKGDLTEEQALKLRHGYYASVSFTDANIGKILDELKRLELDDNTIVILWGDHGWKLGEHAG--WCKHTNF-ELDTRVPL 354
Cdd:COG3083 412 NYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFsRYQLQVPL 491
|
170 180
....*....|....*....|....*....
gi 1718789962 355 IIRAPQIQAS--GKTTRALvefvDIYPTL 381
Cdd:COG3083 492 VIHWPGTPPQviSKLTSHL----DIVPTL 516
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
10-388 |
1.75e-11 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 65.54 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 10 IFCLVIFSGCLASSNSVASEKPNVLFIAVDDLRPELgcygATHIKSPNIDRLAASGLLFERAYCQQ-AVCSPSRTSLMTG 88
Cdd:COG1524 3 RGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADL----LERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 89 LRPDSTKVYDLETHFRKTVpdvvtltqqfmkhgyhsvgmGKIYHGSLNDDPSWDRYLkvkakgyqLPETQAAIRAKTKGL 168
Cdd:COG1524 79 LYPGEHGIVGNGWYDPELG--------------------RVVNSLSWVEDGFGSNSL--------LPVPTIFERARAAGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 169 NLKKMS--RKKRSRLTRGPATEMADVPDHLY----RDGAIAEQALKTLQRqkqhQKPFFLAVgflkpHLPFV--APQKY- 239
Cdd:COG1524 131 TTAAVFwpSFEGSGLIDAARPYPYDGRKPLLgnpaADRWIAAAALELLRE----GRPDLLLV-----YLPDLdyAGHRYg 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 240 --WDLYdRSEIKLAEN---PFLP--KDAPQWASTNW------GElrnySDIPRK---GDLTEEQALKLRHGYYASVSFTD 303
Cdd:COG1524 202 pdSPEY-RAALREVDAalgRLLDalKARGLYEGTLVivtadhGM----VDVPPDidlNRLRLAGLLAVRAGESAHLYLKD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 304 ANIGKIL------------DELKRLELDDNTI--VILWGDHGW-----KLGEHAGWckhtnFELDTRVPLIIRAPQIqas 364
Cdd:COG1524 277 GADAEVRallglparvltrEELAAGHFGPHRIgdLVLVAKPGWaldapLKGSHGGL-----PDEEMRVPLLASGPGF--- 348
|
410 420
....*....|....*....|....
gi 1718789962 365 gkttRALVEFVDIYPTLCELARIP 388
Cdd:COG1524 349 ----RPGVRNVDVAPTIARLLGLP 368
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
292-384 |
6.15e-08 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 53.74 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 292 RHGY-------YASVSFTDANIGKILDELKRLELDDNTIVILWGDHGW-KLGEHaGWckhTNFELDTRVPLIIRAPQIqa 363
Cdd:cd16018 171 GHKYgpdspevNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMtDVGTH-GY---DNELPDMRAIFIARGPAF-- 244
|
90 100
....*....|....*....|...
gi 1718789962 364 sgKTTRALVEF--VDIYPTLCEL 384
Cdd:cd16018 245 --KKGKKLGPFrnVDIYPLMCNL 265
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
390-482 |
7.57e-06 |
|
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: 44.55 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 390 PDHLEGTSFKPLLENPNRPWKPAA----FSQYPRGSMMG--YSMKTDRY-------RYTEWrerksgkivgrELYDHQHD 456
Cdd:pfam16347 2 PADMQGKSFLPLLKGKKPKNWRDAlyyhYYEYPAEHAVKrhYGVRTERYklihfynDIDEW-----------ELYDLQKD 70
|
90 100
....*....|....*....|....*.
gi 1718789962 457 SAENKNIANQPDQKTVVGQLSRQLKK 482
Cdd:pfam16347 71 PKEMNNVYGDPEYAEVQAELKEELEE 96
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
306-390 |
2.24e-05 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 46.02 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 306 IGKILDELKRLELDDNTIVILWGDHGWK-LGEHAGwckhtNFELDTRVPLII------RAPQIQASGKTTRALVEFVDIY 378
Cdd:cd16024 180 IKRIYESLEEQSSNNPTLLVVCGDHGMTdAGNHGG-----SSPGETSVPLLFispkfsSKPSNADGELSYYETVQQVDLA 254
|
90
....*....|..
gi 1718789962 379 PTLCELARIPLP 390
Cdd:cd16024 255 PTLALLLGLPIP 266
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
349-403 |
4.10e-05 |
|
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 45.99 E-value: 4.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1718789962 349 DTRVPLIIRAPQIQAsGKTTRAlVEFVDIYPTLCELARIPLPDhleGTSFKPLLE 403
Cdd:cd16016 408 DTHVPLLFYGWGIKP-GEIPRP-VEITDIAPTLAALLGIQPPN---GCIGKPLLE 457
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
33-331 |
1.45e-04 |
|
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: 43.95 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 33 VLFIAVDDLRPE-LGCYGAThiksPNIDRLAASGLLFERAYCQ-QAVCSPSRTSLMTGLRPDSTKVYDLETHFRKTVPDV 110
Cdd:pfam01663 1 LLVISLDGFRADyLDRFELT----PNLAALAKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 111 VTLTQQFMKHGYhsvgmgkiyhgsLNDDPSWDRYLK--VKAKGYQLPETQAAIRAKtkglnlkkmsRKKRSRLTRGPATE 188
Cdd:pfam01663 77 VFVISDPEDPRW------------WQGEPIWDTAAKagVRAAALFWPGSEVDYSTY----------YGTPPRYLKDDYNN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 189 MADVPDHLyrDGAIAEQALKTLQRQKQHQKPFFLAVgflkphlpfvapqkYWDLYDRSEIKLaenpflpkdapQWASTNW 268
Cdd:pfam01663 135 SVPFEDRV--DTAVLQTWLDLPFADVAAERPDLLLV--------------YLEEPDYAGHRY-----------GPDSPEV 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718789962 269 GElrnysdiprkgdlteeqalklrhgYYASVsftDANIGKILDELKRLELDDNTIVILWGDHG 331
Cdd:pfam01663 188 ED------------------------ALRRV---DRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
299-397 |
8.55e-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: 38.55 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718789962 299 VSFTDANIGKILDELKRLelddNTIVILWGDHG-----WKLGEHAGWCKHTNFeldtRVPLIIRAPQIQASGKTTRALVe 373
Cdd:cd16010 409 VEAVDECLGRIVEAVLEN----GGTLLITADHGnaeemIDPETGGPHTAHTTN----PVPFIIVDPGLKRKLLKDGGLA- 479
|
90 100
....*....|....*....|....
gi 1718789962 374 fvDIYPTLCELARIPLPDHLEGTS 397
Cdd:cd16010 480 --DVAPTILDLLGIEKPKEMTGKS 501
|
|
| |
