|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
45-387 |
0e+00 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 531.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDIELGSMQAMNKTKRIMMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNE--NCSSPSWQA 122
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 123 HHEPHTFAVHLNNSGYRTAFFGKYLNEY----NGSYVPPGWREWVALVKNSRFYNYTLCrNGIREKHGTQYPKDYLTDVI 198
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 199 TNDSINYFRMSKRMypHRPVMMVLSHAAPHGPEDAAPQYSSAFPNAS-QHITPSYNHAPNPDKHWILRYTGPMkPVHMQF 277
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLN-PTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 278 TNMLQRRRLQTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVKGKSMPYEFDIRIPFYVRGPNVEAGAI 357
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 528494291 358 NPHIVLNTDLAPTLLDMAGIDIPQDMDGKS 387
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
45-420 |
1.30e-85 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 280.18 E-value: 1.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDIE-LGSMQA-MNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENcSSPSW 120
Cdd:cd16031 2 RPNIIFILTDDHRYDaLGCYGNpIVKTPNIdrLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 121 QahhepHTFAVHLNNSGYRTAFFGKYLNEYNGSYVPPGWREWVALVKNSRFYNYTlcrNGIREKHGTQYPkdYLTDVITN 200
Cdd:cd16031 81 Q-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPE---FIENGKRVGQKG--YVTDIITD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 201 DSINYFRmsKRMyPHRPVMMVLSHAAPHGPEDAAPQYSSAFPNAsqHITP-------SYNHAPNPDK------HWIL--R 265
Cdd:cd16031 151 KALDFLK--ERD-KDKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEpetfdddDYAGRPEWAReqrnriRGVLdgR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 266 YTGPMKpvhmqFTNMLqRRRLQTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVkGKSMPYEFDIRIPF 345
Cdd:cd16031 226 FDTPEK-----YQRYM-KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPL 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528494291 346 YVRGP-NVEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETERPVNsftrfhsykkaklWRDSFLVE 420
Cdd:cd16031 299 IIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKPVD-------------WRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
45-429 |
3.53e-71 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 240.17 E-value: 3.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDI-ELGSM-QAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENcsSPSW 120
Cdd:COG3119 23 RPNILFILADDLGYgDLGCYgNPLIKTPNIdrLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--YNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 121 QAHHEPhTFAVHLNNSGYRTAFFGKYLNeyngsyvppgwrewvalvknsrfynytlcrngirekhgtqypkdYLTDVITN 200
Cdd:COG3119 101 LPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLLTD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 201 DSINYfrMSKRMYPHRPVMMVLSHAAPHGPEDAAPQYSSAFPNasQHITPSYNHAPNPDKHWILRYtgpmkpvhmqftnm 280
Cdd:COG3119 136 KAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR-------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 281 LQRRRLQTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVKGKSMPYEFDIRIPFYVRGPN-VEAGAINP 359
Cdd:COG3119 198 ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVSD 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 360 HIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLEterpvnsftrfhsyKKAKLWRDSFLVERGKPLHKLA 429
Cdd:COG3119 278 ALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLT--------------GEKAEWRDYLYWEYPRGGGNRA 333
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
536-673 |
6.08e-65 |
|
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.
Pssm-ID: 463628 Cd Length: 142 Bit Score: 213.75 E-value: 6.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 536 SVPRNRWARSVPYHLDSNVYTLDLEKGYRPLNL-NTSLMLGRKQAV-YGQNEEYSGMGPTEDNFNSLTPPAALKVTYRCS 613
Cdd:pfam12548 3 RFVRTRQKRSLSVEFEGEVYDIDLEEEYQPLEPrNLLKRHARDDGEeGEEGEESSGTGSKRDSSNSVGPPASVKVTHRCY 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 614 ILMNDTVKCDGGLYKSLQAWKDHKLHIEHEIETLQTKIKNLREVKGHLKEVRPKECECNK 673
Cdd:pfam12548 83 ILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-397 |
5.83e-52 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 187.01 E-value: 5.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDD---QDieLGSMQAMN-KTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNnencssp 118
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 119 SWQAHHEPHTFAVHLNNSGYRTAFFGK--------YLNEYNGSYVPP----GWREWVALVKNSRFYNYTLCRNGIREKHG 186
Cdd:cd16034 72 DVPLPPDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 187 TQYPKDYLTDVItndsINYfrMSKRMYPHRPVMMVLSHAAPHGPEDAAPQ-YSSAFPNASQHItpsynhAPNPDKhwilr 265
Cdd:cd16034 152 KGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLL------RPNVPE----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 266 ytgpmkpvhmqftNMLQRRRLQTLL--------SVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVkGKSMPY 337
Cdd:cd16034 215 -------------DKKEEAGLREDLrgyyamitALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPY 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528494291 338 EFDIRIPFYVRGPNV-EAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETERP 397
Cdd:cd16034 281 EESIRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKD 341
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
46-387 |
1.55e-49 |
|
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: 174.93 E-value: 1.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQ---DIE-LGSMQAmnKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENcssPS 119
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---GG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 120 WQAHHEPhTFAVHLNNSGYRTAFFGKylneyngsyvppgwreWvalvknsrfynytlcrngirekHgtqypkdyltdvit 199
Cdd:cd16022 76 GLPPDEP-TLAELLKEAGYRTALIGK----------------W----------------------H-------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 200 NDSINYFRmskRMYPHRPVMMVLSHAAPHGPedaapqyssafpnasqhitpsynhapnpdkhwiLRYTGpmkpvhmqftn 279
Cdd:cd16022 103 DEAIDFIE---RRDKDKPFFLYVSFNAPHPP---------------------------------FAYYA----------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 280 MLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVKGKSMPYEFDIRIPFYVRGPNV-EAGAIN 358
Cdd:cd16022 136 MVSA--------IDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKiPAGQVS 207
|
330 340
....*....|....*....|....*....
gi 528494291 359 PHIVLNTDLAPTLLDMAGIDIPQDMDGKS 387
Cdd:cd16022 208 DALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-393 |
2.31e-49 |
|
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: 180.43 E-value: 2.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDD---QDieLGSMqaMNK---TKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKY--------VHNHHTY 109
Cdd:cd16144 1 PNIVLILVDDlgwAD--LGCY--GSKfyeTPNIdrLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 110 TNNENCSSPSWQAHHEPH---TFAVHLNNSGYRTAFFGKY-LNEYNGSYvpP---GWREWVALVKNSRFYNYTLCRNGIR 182
Cdd:cd16144 77 PPDNTKLIPPPSTTRLPLeevTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 183 EKHGTQYPKDYLTDVITNDSINYFRMSKRmyphRPVMMVLSHAAPHGPEDAapqyssafpnasqhitpsynhapnpDKHW 262
Cdd:cd16144 155 PDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQA-------------------------RPEL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 263 ILRYTGPMKPVHMQFTN-----MLQrrrlqtllSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLV------- 330
Cdd:cd16144 206 IEKYEKKKKGLRKGQKNpvyaaMIE--------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplr 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528494291 331 KGKSMPYEFDIRIPFYVRGPNV-EAGAINPHIVLNTDLAPTLLDMAGIDIP--QDMDGKSILKLLE 393
Cdd:cd16144 278 GGKGSLYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPppQHLDGVSLVPLLK 343
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
46-397 |
1.88e-44 |
|
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: 164.99 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQDIELGS-MQAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNnencSSPSWQA 122
Cdd:cd16027 1 PNILWIIADDLSPDLGGyGGNVVKTPNLdrLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGL----RSRGFPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 123 HHEPHTFAVHLNNSGYRTAFFGKYlnEYNGSYVPPGWrewvalvknsrFYNYTLCRNGIREKHGTQYPKDYLTDVITND- 201
Cdd:cd16027 77 PDGVKTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKKGQp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 202 ---SINYFrmskrmYPHRPVMMVLSHAAPHGPEDAAPqyssafpnasqhitPSYnHAPNPD-KHWILRYTgpmkpvhmqf 277
Cdd:cd16027 144 fflWFGFH------DPHRPYPPGDGEEPGYDPEKVKV--------------PPY-LPDTPEvREDLADYY---------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 278 tNMLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHGYhigqfGLVKGKSMPYEFDIRIPFYVRGPN-VEAGA 356
Cdd:cd16027 193 -DEIER--------LDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKPGS 258
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 528494291 357 INPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETERP 397
Cdd:cd16027 259 VSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKD 299
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-392 |
1.54e-41 |
|
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: 157.76 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQDI-ELGSM-QAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKyvHNHHTY--TNNENCSSPS 119
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTGHTRvrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 120 WQAhhEPHTFAVHLNNSGYRTAFFGK----------------------YLNEYNG-SYVPP-GWR--EWVALVKNSRFYN 173
Cdd:cd16145 79 LPP--DDVTLAEVLKKAGYATAAFGKwglggpgtpghptkqgfdyfygYLDQVHAhNYYPEyLWRngEKVPLPNNVIPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 174 YTLCRNGIREKhgtqypkDYLTDVITNDSINYFRMSKRmyphRPVMMVLSHAAPHGPedaapqyssafpnasqHITPSYN 253
Cdd:cd16145 157 DEGNNAGGGGG-------TYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAP----------------LQVPDDG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 254 HAPNPDKHWILRYTGPMKPVHMQFTNMLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHI-------GQ 326
Cdd:cd16145 210 PYKYKPKDPGIYAYLPWPQPEKAYAAMVTR--------LDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPD 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494291 327 F-----GLVKGK-SMpYEFDIRIPFYVRGPN-VEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLL 392
Cdd:cd16145 282 FfdsngPLRGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
46-377 |
1.49e-40 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 151.42 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQ---DIEL--GSMQAMNKTKRiMMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNEncsspsW 120
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLygYPRPTTPFLDR-LAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 121 QAHHEPHTFAVHLNNSGYRTAFFGKYLNEYNGSYVPPGWrewvalvKNSRFYNYTLCRNGI--REKHGTQYP-KDYLTDV 197
Cdd:pfam00884 74 GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNL-------GFDKFFGRNTGSDLYadPPDVPYNCSgGGVSDEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 198 ITNDSINYfrmskRMYPHRPVMMVLSHAAPHGPEDAAPQYSSAFPnASQHITPSYNHAPNpdkhwilrytgpmkpvhmqf 277
Cdd:pfam00884 147 LLDEALEF-----LDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYA-TFKPSSCSEEQLLN-------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 278 tnmlqrRRLQTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFG--LVKGKSM-PYEFDIRIPFYVRGPNVEA 354
Cdd:pfam00884 201 ------SYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKA 274
|
330 340
....*....|....*....|....
gi 528494291 355 -GAINPHIVLNTDLAPTLLDMAGI 377
Cdd:pfam00884 275 kGQKSEALVSHVDLFPTILDLAGI 298
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
46-395 |
6.13e-39 |
|
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 150.01 E-value: 6.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQDIelGSMQAMN----KT---KRIMMQGgTHFSNaFATTPMCCPSRSTILTGKYVHN---HHTYTNNENc 115
Cdd:cd16146 1 PNVILILTDDQGY--GDLGFHGnpilKTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHTILGRER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 116 sspswqAHHEPHTFAVHLNNSGYRTAFFGKYLNEYNGSYVPP--GWREWVAL----------VKNSRFYNYTLCRNGIRE 183
Cdd:cd16146 76 ------MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdYWGNDYFDDTYYHNGKFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 184 KHgtqypKDYLTDVITNDSINYFRMSKrmypHRPVMMVLSHAAPHGPEDAAPQYSsafpnasqhitpsynhAPNPDKHWi 263
Cdd:cd16146 150 KT-----EGYCTDVFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYL----------------DPYKDMGL- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 264 lrytgpmKPVHMQFTNMLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIG-----QFGLVKGKSMPYE 338
Cdd:cd16146 204 -------DDKLAAFYGMIEN--------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYE 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 339 FDIRIPFYVRGPNV-EAGAINPHIVLNTDLAPTLLDMAGIDIP--QDMDGKSILKLLETE 395
Cdd:cd16146 269 GGHRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPegIKLDGRSLLPLLKGE 328
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-397 |
3.93e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 143.52 E-value: 3.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQ--DIeLGSM-QAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNenCSSPS 119
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 120 wqahhEPHTFAVHLNNSGYRTAFFGKylneyngsyvppgwreWvalvknsrfynytlcrngirekHGTQYPKDYLTDVit 199
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 200 ndSINYFR-MSKRmyphRPVMMVLSHAAPH---------GPEDAAPQYSS--------AFP-NASQHItpsynhapnPDk 260
Cdd:cd16152 113 --AIDYLDnRQKD----KPFFLFLSYLEPHhqndrdryvAPEGSAERFANfwvppdlaALPgDWAEEL---------PD- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 261 hwilrYTGpmkpvhmqftnMLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHigqFGLVKG--KSMPYE 338
Cdd:cd16152 177 -----YLG-----------CCER--------LDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHE 229
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494291 339 FDIRIPFYVRGPNVEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETERP 397
Cdd:cd16152 230 SSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVE 288
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-408 |
1.01e-36 |
|
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: 142.32 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDIElgSMQAMN----KTKRI--MMQGGTHFSNAF---ATTP-MCCPSRSTILTGKYVHNhhtYTNNEN 114
Cdd:cd16155 2 KPNILFILADDQRAD--TIGALGnpeiQTPNLdrLARRGTSFTNAYnmgGWSGaVCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 115 CSSPSwqahhEPHTFAVHLNNSGYRTAFFGKYLNEYngsyvppgwrewvalvknsrfynytlcrngirekhgtqypkdyl 194
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 195 tdviTNDSINYFRmsKRMYPHRPVMMVLSHAAPHGPEDAapqyssafpnasqhiTPSYNHAPNPDKHwilrytgPMKPVH 274
Cdd:cd16155 108 ----ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQA---------------PPEYLDMYPPETI-------PLPENF 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 275 M---QFTNMLQRRRLQTLLS---------------------VDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLV 330
Cdd:cd16155 160 LpqhPFDNGEGTVRDEQLAPfprtpeavrqhlaeyyamithLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM 239
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494291 331 kGKSMPYEFDIRIPFYVRGPNVEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETERPVNSFTRFHSYK 408
Cdd:cd16155 240 -GKQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDTLYGAYR 316
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-420 |
7.07e-36 |
|
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: 140.82 E-value: 7.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQ--DIELGSMQAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENCSSPSWQ 121
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 122 AHHEPHTFAVHLNNSGYRTAFFGKY--LNEYN-GSYvppGWREWVALvknsrfynytlcrngirEKHGTQYpkdyltdvI 198
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWhvGPEETpLDY---GFDEYLPV-----------------ETTIEYF--------L 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 199 TNDSINYfrMSKRMYPHRPVMMVLSHAAPHGPEDAAPQYSSAFPNASQHITPSYNHAPNpDKHWILRYTgpMKPVHM-QF 277
Cdd:cd16033 133 ADRAIEM--LEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFE-DKPYIYRRE--RKRWGVdTE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 278 TNMLQRRRLQ------TLLsvDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLV-KGKSMpYEFDIRIPFYVRGP 350
Cdd:cd16033 208 DEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKWP 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528494291 351 NV-EAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETERPVNsftrfhsykkaklWRDSFLVE 420
Cdd:cd16033 285 GViAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED-------------WRDEVVTE 342
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-406 |
6.42e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 135.75 E-value: 6.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTD--DQDIeLGSM-QAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENCSS--P 118
Cdd:cd16037 1 PNILIIMSDehNPDA-MGCYgHPVVRTPNLdrLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGdvP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 119 SWqAHHephtfavhLNNSGYRTAFFGKylneyngsyvppgwrewvalvknsrfynytLCRNGIREKHGTQYpkdylTDVI 198
Cdd:cd16037 80 SW-GHA--------LRAAGYETVLIGK------------------------------LHFRGEDQRHGFRY-----DRDV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 199 TNDSINYFRmsKRMYPHRPVMMVLSHAAPHgpedaapqyssaFPnasqHITPsynhapnpdKHWILRYtgpmkpvhmqft 278
Cdd:cd16037 116 TEAAVDWLR--EEAADDKPWFLFVGFVAPH------------FP----LIAP---------QEFYDLY------------ 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 279 nmlqRRRLQT----LLS-VDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVkGKSMPYEFDIRIPFYVRGPNVE 353
Cdd:cd16037 157 ----VRRARAayygLVEfLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIP 231
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494291 354 AGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLE----TERPVnsFTRFHS 406
Cdd:cd16037 232 AGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEgpddPDRVV--FSEYHA 286
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
77-397 |
3.04e-33 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 133.92 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 77 GTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNnencSSPsWQAHHEphTFAVHLNNSGYRTAFFGK----------- 145
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP-LDARHL--TLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 146 YLNEYNGSY--VPPGWREWVALvknsrfynytlcrNGIREKHGtqyPKDYLTDvitnDSINYFRMskrmYPHRPVMMVLS 223
Cdd:cd16028 109 PLDPRLLSYelAMPGFDPVDRL-------------DEYPAEDS---DTAFLTD----RAIEYLDE----RQDEPWFLHLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 224 HAAPHGPEDAAPQYSSAFPNASqhiTPSYNHAPNPD---------KHWILRYtgPMKPVHMQFTNM-----LQRRRLQT- 288
Cdd:cd16028 165 YIRPHPPFVAPAPYHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMRAt 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 289 ---LLS-VDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVkGKSMPYEFDIRIPFYVRGPNVEAGA----INPH 360
Cdd:cd16028 240 ylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREADAtrgqVVDA 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 528494291 361 IVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETERP 397
Cdd:cd16028 319 FTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQP 355
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
45-433 |
7.37e-33 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 133.64 E-value: 7.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDIE-LGSMQamNKTKR-----IMMQGGTHFSNAFATTPMCCPSRSTILTGKyVHNHHTYTNNENCSSp 118
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNG--NKAVEtpnldMLASEGYNFENAYSAVPSCTPARAALLTGL-SQWHHGRVGYGDVVP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 119 sWqahHEPHTFAVHLNNSGYRTAFFGKYlneyngsYVPPGwrewvalvKNSRFYNYTLCRNGI----REKHGTQYP--KD 192
Cdd:PRK13759 82 -W---NYKNTLPQEFRDAGYYTQCIGKM-------HVFPQ--------RNLLGFHNVLLHDGYlhsgRNEDKSQFDfvSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 193 YL-------------------------------------TDVITNDSINYFRmskRMYPHRPVMMVLSHAAPHGPEDAaP 235
Cdd:PRK13759 143 YLawlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDP-P 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 236 QYssAFPnasqhitpSYNHAPNPDKH---WilRYTGPMKP-------VHMQFTNMLQRRRLQTLLS----VDDSVEKVYN 301
Cdd:PRK13759 219 KR--YFD--------MYKDADIPDPHigdW--EYAEDQDPeggsidaLRGNLGEEYARRARAAYYGlithIDHQIGRFLQ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 302 MLVETGELDNTYIIYMSDHGYHIGQFGLVKgKSMPYEFDIRIPFYVRGP----NVEAGAINPHIVLNTDLAPTLLDMAGI 377
Cdd:PRK13759 287 ALKEFGLLDNTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGG 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494291 378 DIPQDMDGKSILKLLETERPVnsftrfhsykkaklWRDSFLVER---GKPLHKLADGKE 433
Cdd:PRK13759 366 TIPDDVDGRSLKNLIFGQYEG--------------WRPYLHGEHalgYSSDNYLTDGKW 410
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-418 |
1.00e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 127.72 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQDIE-LGSM-QAMNKTKRI--MMQGGTHFSNAFATtPMCCPSRSTILTGKYvhNHHTYTNNencsspsWQ 121
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAYAQ-PLCTPSRVQLMTGKY--NFRNYVVF-------GY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 122 AHHEPHTFAVHLNNSGYRTAFFGK---YLNEYNGSYVPP-GWRE---WVALVKNSRFYNYTLCRNGIREKHGTQY-PKDY 193
Cdd:cd16151 71 LDPKQKTFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEyclWQLTETGEKYSRPATPTFNIRNGKLLETtEGDY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 194 LTDVITNDSINYFRMSKR-----MYPhrpvmMVLshaaPHGPedaapqyssafpnasqhitpsynHAPNPD-KHWiLRYT 267
Cdd:cd16151 151 GPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDP-----------------------FVPTPDsPDW-DPDD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 268 GPMKPVHMQFTNMLQrrrlqtllSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIG-----QFGLVKG-KSMPYEFDI 341
Cdd:cd16151 198 KRKKDDPEYFPDMVA--------YMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTDAGT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 342 RIPFYVRGPnveaGAINPHIVLN-----TDLAPTLLDMAGIDIPQD--MDGKSILKLL--ETERPVNSFTRFHSYKKAKL 412
Cdd:cd16151 270 HVPLIVNWP----GLIPAGGVSDdlvdfSDFLPTLAELAGAPLPEDypLDGRSFAPQLlgKTGSPRREWIYWYYRNPHKK 345
|
....*.
gi 528494291 413 WRDSFL 418
Cdd:cd16151 346 FGSRFV 351
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
45-393 |
2.79e-30 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 124.09 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDD---QDIE-LGS---MQAMNKtkriMMQGGTHFSNaFATTPMCCPSRSTILTGkyvHNHH-----TYTNN 112
Cdd:cd16025 2 RPNILLILADDlgfSDLGcFGGeipTPNLDA----LAAEGLRFTN-FHTTALCSPTRAALLTG---RNHHqvgmgTMAEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 113 ENcSSPSWQAHHEPH--TFAVHLNNSGYRTAFFGKylneyngsyvppgwreWvalvknsrfynytlcrngirekHGTqyP 190
Cdd:cd16025 74 AT-GKPGYEGYLPDSaaTIAEVLKDAGYHTYMSGK----------------W----------------------HLG--P 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 191 KD-YLTDVITNDSINYFRMSKRmyPHRPVMMVLSHAAPHGPedaapqyssafpnasqHitpsynHAPnpdKHWILRYTGP 269
Cdd:cd16025 113 DDyYSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP----------------L------QAP---KEWIDKYKGK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 270 ---------------MK-----PVHMQFTNML-----------QRRRLQTLL---------SVDDSVEKVYNMLVETGEL 309
Cdd:cd16025 166 ydagwdalreerlerQKelgliPADTKLTPRPpgvpawdslspEEKKLEARRmevyaamveHMDQQIGRLIDYLKELGEL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 310 DNTYIIYMSDHG--YHIG--QFG---LVKGKSMPYEFDIRIPFYVRGPNV--EAGAINPHIVLNTDLAPTLLDMAGIDIP 380
Cdd:cd16025 246 DNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELAGVEYP 325
|
410 420
....*....|....*....|.
gi 528494291 381 --------QDMDGKSILKLLE 393
Cdd:cd16025 326 ktvngvpqLPLDGVSLLPTLD 346
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
45-412 |
5.10e-30 |
|
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: 123.44 E-value: 5.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQ---DIE-LGSmqAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKY-----VHNHHTYTNNE 113
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGS--PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 114 NCSSPSwqahhEPhTFAVHLNNSGYRTAFFGK--------YL------NEY------NGSYVPPGWREWVALVKNSRFYN 173
Cdd:cd16026 79 GGLPPD-----EI-TIAEVLKKAGYRTALVGKwhlghqpeFLptrhgfDEYfgipysNDMWPFPLYRNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 174 YTLcrngirekhgTQYPKDY--LTDVITNDSINYFRMSKrmypHRPVMMVLSHAAPHGPEDAapqySSAFPNASQHitps 251
Cdd:cd16026 153 EEV----------IEQPADQssLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVPLFA----SEKFKGRSGA---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 252 ynhapnpdkhwilrytGPMKPVhMQftnmlqrrrlqtllSVDDSVEKVYNMLVETGELDNTYIIYMSDHG--YHIGQFG- 328
Cdd:cd16026 211 ----------------GLYGDV-VE--------------ELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGg 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 329 ----LVKGKSMPYEFDIRIPFYVRGPN-VEAGAINPHIVLNTDLAPTLLDMAGIDIPQD--MDGKSILKLLETERPVNSF 401
Cdd:cd16026 260 sagpLRGGKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLLLGGSKSPPH 339
|
410
....*....|.
gi 528494291 402 TRFHSYKKAKL 412
Cdd:cd16026 340 PFFYYYDGGDL 350
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
45-405 |
1.94e-29 |
|
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: 122.30 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDIELGSMQAMN-KTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENcsspsWQ 121
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYGGHPaKTPNIdrLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY-----FR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 122 AHHEPH-TFAVHLNNSGYRTAFFGKYL--NEYNGSYVPPGWREWVALVKNSRFYNYTLCRNGIREKHGTQYP-------- 190
Cdd:cd16030 77 KVAPDAvTLPQYFKENGYTTAGVGKIFhpGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPaweaadvp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 191 -KDYLTDVITNDSINY-----------------------FRMSKR---MYPHRPVMMVLSHAAPHGPEDAAPQYSSAfpn 243
Cdd:cd16030 157 dEAYPDGKVADEAIEQlrklkdsdkpfflavgfykphlpFVAPKKyfdLYPLESIPLPNPFDPIDLPEVAWNDLDDL--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 244 asqhitPSYNHAPNPDKHWilrYTGPMKPVhmqftnmLQRRRLQTLLS----VDDSVEKVYNMLVETGELDNTYIIYMSD 319
Cdd:cd16030 234 ------PKYGDIPALNPGD---PKGPLPDE-------QARELRQAYYAsvsyVDAQVGRVLDALEELGLADNTIVVLWSD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 320 HGYHIGQFGLVkGKSMPYEFDIRIPFYVRGPNV-EAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLL---ETE 395
Cdd:cd16030 298 HGWHLGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLknpSAK 376
|
410
....*....|
gi 528494291 396 RPVNSFTRFH 405
Cdd:cd16030 377 WKDAAFSQYP 386
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
75-390 |
1.62e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 112.64 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 75 QGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHtytnnencsspSWQAHHEPH--TFAVHLNNSGYRTAFFGkylneyNG 152
Cdd:cd16148 34 AEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG-----------VWGGPLEPDdpTLAEILRKAGYYTAAVS------SN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 153 SYVPPGWREWvalvknsRFYNYTLCRNGIREKHGTqyPKDYLTDVITNDSINYFrmsKRMYPHRPVMMVLSHAAPHGPEd 232
Cdd:cd16148 97 PHLFGGPGFD-------RGFDTFEDFRGQEGDPGE--EGDERAERVTDRALEWL---DRNADDDPFFLFLHYFDPHEPY- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 233 aapQYSSAfpnasqhitpsynhapnpdkhwiLRYtgpmkpvhmqftnmlqrrrlqtllsVDDSVEKVYNMLVETGELDNT 312
Cdd:cd16148 164 ---LYDAE-----------------------VRY-------------------------VDEQIGRLLDKLKELGLLEDT 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494291 313 YIIYMSDHGYHIGQFGLVKGKSMP-YEFDIRIPFYVRGPNVEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILK 390
Cdd:cd16148 193 LVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-393 |
3.17e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 113.07 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQ----DIELGSMQAMNKTKRIMMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYtnnENCSSPS-W 120
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 121 QAHHEPHTFAVHLNNSGYRTAFFGKY-LNEYNGSYvppgwrewvalvknsrfynytlcrngirekhgtqYPKDyltDVIT 199
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 200 NDSINYFR-MSKRMYPHRPVMMVLSHAAPH---GPEDAAPQYssafpnasqhitpsynhapnpdkHWILRYTGpmkpvhm 275
Cdd:cd16035 121 AQAVEWLReRGAKNADGKPWFLVVSLVNPHdimFPPDDEERW-----------------------RRFRNFYY------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 276 qftNMLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVKGKSMPYEFDIRIPFYVRGPNVEAG 355
Cdd:cd16035 171 ---NLIRD--------VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGT 239
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 528494291 356 -----AINPHIvlntDLAPTLLDMAGIDIPQ------DMDGKSILKLLE 393
Cdd:cd16035 240 gqttdALTSHI----DLLPTLLGLAGVDAEArateapPLPGRDLSPLLT 284
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-407 |
5.12e-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: 113.98 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQDIE------LGSMQAMNKTKRIMMQGGTHFSNAFATtPMCCPSRSTILTGKY-VHNHHTYTNNENCSSP 118
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYgFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 119 swqaHHEPHTFAVHLNNSGYRTAFFGKYL--NEYNGSYVPPGWREWVALVKN--SRFYNYTLCRNGIREKHgtqypKDYL 194
Cdd:cd16154 80 ----ETLLQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-----TEYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 195 TDVITNDSINYFRMSkrmypHRPVMMVLSHAAPHGPedaapqyssaFpnasqHITPSYNHAPNPdkhwilryTGpmkpvh 274
Cdd:cd16154 151 TTKLTNLAIDWIDQQ-----TKPWFLWLAYNAPHTP----------F-----HLPPAELHSRSL--------LG------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 275 mQFTNMLQRRR---LQTLLSVDDSVEKVYNMLVETgELDNTYIIYMSDHGYHiGQ-----FGLVKGKSMPYEFDIRIPFY 346
Cdd:cd16154 197 -DSADIEANPRpyyLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVPLI 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494291 347 VRGPNVE-AGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETerpVNSFTRFHSY 407
Cdd:cd16154 274 VSGAGVErANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSD---VNASTRQYNY 332
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
46-407 |
8.32e-27 |
|
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: 114.79 E-value: 8.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQD---IELGSMQAMnKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENCSSPSw 120
Cdd:cd16156 1 KQFIFIMTDTQRwdmVGCYGNKAM-KTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 121 qahhepHTFAVHLNNSGYRTAFFGKY-LN--EYNGSYV-PPGWRE--WVALV-----------KNSRFYNYTLCRNGIRE 183
Cdd:cd16156 79 ------KTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMRnyldelteeerRKSRRGLTSLEAEGIKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 184 KHGTQYPkdyltdvITNDSINYFRMskrmYPHRPVMMVLSHAAPHGPEDAAPQYSSAFPNASQHITPSY--NHAPNPDKH 261
Cdd:cd16156 153 EFTYGHR-------CTNRALDFIEK----HKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPLHQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 262 WIlrYTGPMK-PVHMQFTnmlqrRRLQTLLS----VDDSVEKVYNMLVETGEldNTYIIYMSDHGYHIGQFGL-VKGKSM 335
Cdd:cd16156 222 RL--WAGAKPhEDGDKGT-----IKHPLYFGcnsfVDYEIGRVLDAADEIAE--DAWVIYTSDHGDMLGAHKLwAKGPAV 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494291 336 pYEFDIRIPFYVRGPN-VEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETE-----RPVnsFTRFHSY 407
Cdd:cd16156 293 -YDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDPeipenRGV--FVEFGRY 367
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-392 |
2.37e-26 |
|
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: 112.29 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDqdIELGSMQAMNKTKRI-------MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENCSSP 118
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 119 SWQAHHEPhTFAVHLNNSGYRTAFFGKY---LNEY--NGSYVPPGWREWVALVK------NSR-F-YNYTLCRNgirekh 185
Cdd:cd16143 79 PLIEPDRV-TLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKDVDYSKpikggpLDHgFdYYFGIPAS------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 186 gtqypkdYLTDVITNDSINYFRMSKRmyPHRPVMMVLSHAAPHGPedaapqyssafpnasqhITPS--YNHAPNPDKHwi 263
Cdd:cd16143 152 -------EVLPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGPY-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 264 lrytGPMkpVHMqftnmlqrrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHG---YHIGQFGLVKG-------- 332
Cdd:cd16143 204 ----GDF--VYE----------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgplr 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528494291 333 --KSMPYEFDIRIPFYVRGPN-VEAGAINPHIVLNTDLAPTLLDMAGIDIPQD--MDGKSILKLL 392
Cdd:cd16143 262 gmKADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL 326
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-389 |
3.53e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 108.48 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQ---------DIELgSMQAMNKtkriMMQGGTHFSNAFATTPMCCPSRSTILTGKY-----VHNHHTYTN 111
Cdd:cd16149 1 PNILFILTDDQgpwalgcygNSEA-VTPNLDR----LAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgIHDWIVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 112 NENCSSP-SWQAHHEphTFAVHLNNSGYRTAFFGKylneyngsyvppgwreWVALVKNSRFynytlcrngIREKHGTQYP 190
Cdd:cd16149 76 HGKTKKPeGYLEGQT--TLPEVLQDAGYRCGLSGK----------------WHLGDDAADF---------LRRRAEAEKP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 191 KdYLtdvitndSINYFrmskrmyphrpvmmvlshaAPHGPEdaapQYSSAfpnasqhitpsynhapnpdkhwilrytgpm 270
Cdd:cd16149 129 F-FL-------SVNYT-------------------APHSPW----GYFAA------------------------------ 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 271 kpvhmqftnmlqrrrlqtLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGlVKGK-------SMpYEFDIRI 343
Cdd:cd16149 148 ------------------VTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKV 207
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 528494291 344 PFYVRGPN-VEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMD--GKSIL 389
Cdd:cd16149 208 PFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
45-430 |
1.60e-24 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 107.52 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDqdIELGSMQAM-NKTKRI-----MMQGGTHFSNAFATTPMCCPSRSTILTGKYvhNHHTYTNNENCSSP 118
Cdd:cd16160 1 KPNIVLFFADD--MGYGDLASYgHPTQERgpiddMAAEGIRFTQAYSADSVCTPSRAALLTGRL--PIRSGMYGGTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 119 SWQAHHEPH---TFAVHLNNSGYRTAFFGKY---LNEYN---GSYVPP--GWrEWVAlvKNSRFYNYTLCRN-GIREKHG 186
Cdd:cd16160 77 PWDIGGLPKtevTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLPShhGF-DFVG--TNLPFTNSWACDDtGRHVDFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 187 -------------TQYP--KDYLTDVITNDSINYFRMSKrmypHRPVMMVLSHAAPHgpedaAPQYSSA-FPNASQHitP 250
Cdd:cd16160 154 drsacflyyndtiVEQPiqHEHLTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTH-----TPLFASKrFKGKSKR--G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 251 SYNHAPNpDKHWilrytgpmkpvhmqftnmlqrrrlqtllsvddSVEKVYNMLVETGELDNTYIIYMSDHGYHI------ 324
Cdd:cd16160 223 RYGDNIN-EMSW--------------------------------AVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeycleg 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 325 GQFGLVKG-KSMPYEFDIRIPFYVRGPNVEAGAINPHIVLNTDLAPTLLDMAGIDIPQD--MDGKSILKLL--ETERPVN 399
Cdd:cd16160 270 GSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDLLlgEADSPHD 349
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 528494291 400 SFTRFHS--------------YKKAKLWRDSFLVERGKPLHKLAD 430
Cdd:cd16160 350 DILYYCCsrlmavrygsykihFKTQPLPSQESLDPNCDGGGPLSD 394
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
46-397 |
2.21e-24 |
|
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: 106.48 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQ---DIEL-GSMQAmnKTKRI--MMQGGTHFSNAFaTTPMCCPSRSTILTGKYVHNHHTYTNNENCSSPS 119
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLdaLAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 120 WQAHHEPhTFAVHLNNSGYRTAFFGKY-LNEYNGSYVPPG----------------WREWVALVKNsrFYNYTLCRNgir 182
Cdd:cd16029 78 GLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSGGAND--YGNDDLRDN--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 183 EKHGTQYPKDYLTDVITNDSINYFRMSKrmyPHRPVMMVLSHAAPHGPEDAAPQYSSAFPNASQHITPsynhapnpdkhw 262
Cdd:cd16029 152 EEPAWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 263 ilrytgpmkpvhmqftnmLQRRRLQTLLS-VDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFG------LVKGKSM 335
Cdd:cd16029 217 ------------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNT 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528494291 336 PYEFDIRIPFYVRGP--NVEAGAINPHIVLNTDLAPTLLDMAGIDIP--QDMDGKSILKLLETERP 397
Cdd:cd16029 279 LWEGGVRVPAFVWSPllPPKRGTVSDGLMHVTDWLPTLLSLAGGDPDdlPPLDGVDQWDALSGGAP 344
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
75-397 |
7.25e-23 |
|
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: 100.73 E-value: 7.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 75 QGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNenCSSPSWQahhePhTFAVHLNNSGYRTAFFGKYlneyngSY 154
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPADI----P-TFAHYLRAAGYRTALSGKM------HF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 155 VPPgwrewvalvknsrfynytlcrngiREKHGTQYpkDyltDVITNDSINYFRMSKRMYPHRPVMMVLSHAAPHGPedaa 234
Cdd:cd16032 101 VGP------------------------DQLHGFDY--D---EEVAFKAVQKLYDLARGEDGRPFFLTVSFTHPHDP---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 235 pqYssafpnasqHITPSYnhapnpdkhW---ILRytgpmkpvhmqftnmlQRRRLQTLLS-VDDSVEKVYNMLVETGELD 310
Cdd:cd16032 148 --Y---------VIPQEY---------WdlyVRR----------------ARRAYYGMVSyVDDKVGQLLDTLERTGLAD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 311 NTYIIYMSDHGYHIGQFGLVKGKSMpYEFDIRIPFYVRGPNVEAGAINPHIVLNTDLAPTLLDMAGIDIPQD---MDGKS 387
Cdd:cd16032 192 DTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHvppLDGRS 270
|
330
....*....|
gi 528494291 388 ILKLLETERP 397
Cdd:cd16032 271 LLPLLEGGDS 280
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-396 |
3.01e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 100.39 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 77 GTHFSNAFATTPMCCPSRSTILTGKY--VHNHHTYTNnencsspsWQAHHEPHTFAVhLNNSGYRTAFFGKylneyNGSY 154
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHH--------LLRPDEPNLLKT-LKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 155 VPPGWREWVALVknsrfynytlcrngirekhgtqypkDYLTdviTNDSINYFRmskRMYPHRPVMMVLSHAAPHGP-EDA 233
Cdd:cd16150 102 PGEFAAEAYCDS-------------------------DEAC---VRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 234 APQYSSafpnasqhitpsYNHAPNPDkhwilryTGPMKPVHMQFTNMLQRRRLQTLLSVDDS----VEKVY-NM------ 302
Cdd:cd16150 151 EPWFSM------------IDREKLPP-------RRPPGLRAKGKPSMLEGIEKQGLDRWSEErwreLRATYlGMvsrldh 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 303 --------LVETGELDNTYIIYMSDHGYHIGQFGLV-KGKSMPYEFDIRIPFYVRGPNVEAGAINPHIVLNTDLAPTLLD 373
Cdd:cd16150 212 qfgrlleaLKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLD 291
|
330 340
....*....|....*....|...
gi 528494291 374 MAGIDIPQDMDGKSILKLLETER 396
Cdd:cd16150 292 LAGIPLSHTHFGRSLLPVLAGET 314
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-390 |
2.92e-21 |
|
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: 94.75 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDIElgSMQAMNK--------------TKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHT 108
Cdd:cd16153 1 KPNILWIITDDQRVD--SLSCYNNahtgksesrlgyveSPNIdaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 109 YtNNENcsspSWQA-HHEPHTFAVHLNNSGYRTAFFGKylneyngsyvppgwrewvalvknSRFYNYTlcrngirekhgt 187
Cdd:cd16153 79 Y-GFEA----AHPAlDHGLPTFPEVLKKAGYQTASFGK-----------------------SHLEAFQ------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 188 qypkDYLTDVITNDSINYFRMSKRMYPHRPVMMVLSHAAPHgpedaapqyssafpnasqhiTPSYnhapnPDKHWILRYT 267
Cdd:cd16153 119 ----RYLKNANQSYKSFWGKIAKGADSDKPFFVRLSFLQPH--------------------TPVL-----PPKEFRDRFD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 268 gpmkpvHMQFTNMlqrrrlqtllsVDDSVEKVYNMLVETGEL---DNTYIIYMSDHGYHIGQFGLVkGKSMPYEFDIRIP 344
Cdd:cd16153 170 ------YYAFCAY-----------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVP 231
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 528494291 345 FYVRGPNVE---AGAINPHIVLNTDLAPTLLDMAGIDI--PQDMDGKSILK 390
Cdd:cd16153 232 LIVVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDLFE 282
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
46-392 |
1.46e-17 |
|
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: 85.29 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQDIELgSMQAMNKTKRI-----MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYtNNENCSSPSW 120
Cdd:cd16171 1 PNVVMVMSDSFDGRL-TFRPGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 121 QahhephTFAVHLNNSGYRTAFFGKyLNEYNGSYVPPGWRE-WvalvknSRFYNYTLCRNGirekhgtqYPKDYLTDVIT 199
Cdd:cd16171 79 P------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEG--------RPTVNLVGDRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 200 NDsinyfRMSKRMYPhrpvmmvLSHAAPHGPEDAAPQYSSAF--------PnasqHITPSYNHAPNpdkhwilryTGPMK 271
Cdd:cd16171 138 TV-----RVMLKDWQ-------NTDKAVHWIRKEAPNLTQPFalylglnlP----HPYPSPSMGEN---------FGSIR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 272 PVHMQFTNMLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVKGKSMpYEFDIRIPFYVRGPN 351
Cdd:cd16171 193 NIRAFYYAMCAE--------TDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGPG 263
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 528494291 352 VEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLL 392
Cdd:cd16171 264 IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
758-807 |
2.24e-16 |
|
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: 82.21 E-value: 2.24e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 528494291 758 CTSANNNTYWCLRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNGVSTL 807
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
46-375 |
1.01e-15 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 77.46 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDD---QDIELGSMQAMNKT-KRIMMQGGTHFsNAFATTPMC--CPSRSTILTGKYVHNHHTYTNNENCSS-P 118
Cdd:cd00016 1 KHVVLIVLDGlgaDDLGKAGNPAPTTPnLKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPElP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 119 SWQAHHEPH--TFAVHLNNSGYRTAFFGKYlneyngsyvppgwrewvalvknsrfynytlcrngirekhgtqypkdyltd 196
Cdd:cd00016 80 SRAAGKDEDgpTIPELLKQAGYRTGVIGLL-------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 197 vitnDSINYFRMSKrmyphrPVMMVLSHAAPHGPEdaapqyssafpNASQHITPSYnhapnpdkhwilrytgpmkpvhmq 276
Cdd:cd00016 110 ----KAIDETSKEK------PFVLFLHFDGPDGPG-----------HAYGPNTPEY------------------------ 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 277 fTNMLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHG---YHIGQFGLVKGKSMPYEFDIRIPFYVRGPNVE 353
Cdd:cd00016 145 -YDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVK 215
|
330 340
....*....|....*....|..
gi 528494291 354 AGAINPHIVLNTDLAPTLLDMA 375
Cdd:cd00016 216 KGGVKHELISQYDIAPTLADLL 237
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
45-392 |
1.99e-14 |
|
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: 75.97 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDD---QDIELGSMQAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKY-VHNhhTYTNNENCSSP 118
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLgLRN--GVGHNFLPTSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 119 SWQAHHEPhTFAVHLNNSGYRTAFFGKYLNEYNGSYVPpgwrewvalvkNSRFYNYTLcrnGIREKHGTQYPKDYL---T 195
Cdd:cd16161 79 GGLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 196 DVITNDSINyfrmskrmypHRPVMMVLSHAAPHGPEdaapQYSSAFPNASQHITPsynhapnpdkhwilryTGpmkpvhm 275
Cdd:cd16161 144 DFIQRASAK----------DRPFFLYAALAHVHVPL----ANLPRFQSPTSGRGP----------------YG------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 276 qftnmlqrrrlQTLLSVDDSVEKVYNMLVETGELDNTYIIYMSD---------------HGYHIGQFGLVKGKSMPYEFD 340
Cdd:cd16161 187 -----------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGG 255
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 528494291 341 IRIPFYVRGPN-VEAGAINPHIVLNTDLAPTLLDMAGIDIPQD--MDGKSILKLL 392
Cdd:cd16161 256 HREPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
45-398 |
2.47e-13 |
|
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: 73.27 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDI-ELGSMQAMNK-TKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNE---NCSS 117
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 118 PSWQAHHEPHT---FAVHLNNSGYRTAFFGKYLNEYNGSYVP--PGWREW-------VALVKNSRFYNYTLCRNgirEKH 185
Cdd:cd16157 81 PQNIVGGIPDSeilLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWfgapnchFGPYDNKAYPNIPVYRD---WEM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 186 GTQYPKDY----------LTDVITNDSINYfrMSKRMYPHRPVMMVLSHAAPHgpedaAPQYSS-AFPNASQHitPSYNH 254
Cdd:cd16157 158 IGRYYEEFkidkktgesnLTQIYLQEALEF--IEKQHDAQKPFFLYWAPDATH-----APVYASkPFLGTSQR--GLYGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 255 ApnpdkhwilrytgpmkpvhmqftnmlqrrrlqtLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHG---YHIGQFG--- 328
Cdd:cd16157 229 A---------------------------------VMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsn 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494291 329 --LVKGKSMPYEFDIRIPFYVRGP-NVEAGAINPHIVLNTDLAPTLLDMAGIDIPQD--MDGKSILKLL----ETERPV 398
Cdd:cd16157 276 gpFLCGKQTTFEGGMREPAIAWWPgHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVLlngkEKDRPI 354
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
45-415 |
9.56e-13 |
|
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: 71.55 E-value: 9.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILTDDQDI-ELGSMQamNKTKR-----IMMQGGTHFSNAFATTPMCCPSRSTILTGKY------VHNHHTYTNN 112
Cdd:cd16159 1 KPNIVLFMADDLGIgDVGCFG--NDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHGMRVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 113 ENCSS---PSWQAhhephTFAVHLNNSGYRTAFFGKY----------------LN-----------------------EY 150
Cdd:cd16159 79 FTASSgglPPNET-----TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 151 NGSYVPPGW--REWVALV------------------------------------KNSRFYNYTLCRNG-IREKhgtqyPK 191
Cdd:cd16159 154 DLSFDPLFPllTAFVLITaltiflllylgavskrffvfllilsllfislfflllITNRYFNCILMRNHeVVEQ-----PM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 192 DY--LTDVITNDSINYFRMSKRmyphRPVMMVLSHAAPHGPEDAAPQyssaFPNASQHitPSYNHApnpdkhwilrytgp 269
Cdd:cd16159 229 SLenLTQRLTKEAISFLERNKE----RPFLLVMSFLHVHTALFTSKK----FKGRSKH--GRYGDN-------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 270 mkpvhmqftnmlqrrrlqtLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHI-----------GQFGLVKGKSMP-Y 337
Cdd:cd16159 285 -------------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgW 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 338 EFDIRIPFYVRGPnveaGAINPHIVL-----NTDLAPTLLDMAGIDIPQD--MDGKSILKLL--ETERPVNSFTrFHsYK 408
Cdd:cd16159 346 EGGIRVPTIVRWP----GVIPPGSVIdeptsLMDIFPTVAALAGAPLPSDriIDGRDLMPLLtgQEKRSPHEFL-FH-YC 419
|
490
....*....|.
gi 528494291 409 KAKL----WRD 415
Cdd:cd16159 420 GAELhavrYRP 430
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
46-423 |
2.43e-12 |
|
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: 70.17 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDQDI-ELGSM-QAMNKTKRI--MMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENCSSPSWQ 121
Cdd:cd16158 2 PNIVLLFADDLGYgDLGCYgHPSSSTPNLdrLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 122 AHHEPhTFAVHLNNSGYRTAFFGKY---LNEyNGSYVPPgwrewvalvkNSRFYNYTlcrnGIREKHgTQYPKDYLTDVI 198
Cdd:cd16158 82 PLNET-TIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT----------HQGFDHYL----GIPYSH-DQGPCQNLTCFP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 199 TNDSInyFRMSKRMYPHRPVMMVLS-HAAPHGPEDAAPQYSSAfpnASQHITpsynHAPNPDKHWILRYtgPMKPVH--- 274
Cdd:cd16158 145 PNIPC--FGGCDQGEVPCPLFYNESiVQQPVDLLTLEERYAKF---AKDFIA----DNAKEGKPFFLYY--ASHHTHypq 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 275 ---MQFTNMLQRRRL-QTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHI------GQFGLVK-GKSMPYEFDIRI 343
Cdd:cd16158 214 fagQKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTYEGGVRE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 344 PFYVRGPNVEAGAINPHIVLNTDLAPTLLDMAGIDIPQ-DMDGKSILKLLETERPVNSFTRFHSYKKAKLWRDSFLVERG 422
Cdd:cd16158 294 PAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVFAVRWG 373
|
.
gi 528494291 423 K 423
Cdd:cd16158 374 K 374
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-382 |
6.08e-12 |
|
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: 68.33 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 46 PNMILILTDDqdieLGSMQ--------AM-NKTKRI--MMQGGTHFSNAFATtPMCCPSRSTILTGKYVhnhhtytNNEN 114
Cdd:cd16142 1 PNILVILGDD----IGWGDlgcygggiGRgAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 115 CSSPSWQA-----HHEPHTFAVHLNNSGYRTAFFGK-YLNEYNGSYvpP---GWREWVAlvknsrFYNYTLcrngirEKH 185
Cdd:cd16142 69 LTTVGLPGspgglPPWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 186 GTQYPKDYLTDVITND-----SINYFRMSKRMYPHrpvmmvlshaaphgpedaaPQYssafpnasQHITPSYNhaPNPDk 260
Cdd:cd16142 135 IVDKAIDFIKRNAKADkpfflYVNFTKMHFPTLPS-------------------PEF--------EGKSSGKG--KYAD- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 261 hwilrytgpmkpvhmqftnmlqrrrlqTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHG-----YHIGQFGLVKG-KS 334
Cdd:cd16142 185 ---------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKG 237
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 528494291 335 MPYEFDIRIPFYVRGPN-VEAGAINPHIVLNTDLAPTLLDMAGIDIPQD 382
Cdd:cd16142 238 TTWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
45-401 |
9.79e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 65.44 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 45 RPNMILILtddqdIElgSMQA-----MNKTKRIM------MQGGTHFSNAFATTPMCCPSRSTILTGKY-VHNHHTYTNN 112
Cdd:COG1368 234 KPNVVVIL-----LE--SFSDffigaLGNGKDVTpfldslAKESLYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKRP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 113 encsspswqAHHEPHTFAVHLNNSGYRTAFFgkylneYNGsyvppgwrewvalvkNSRFYNytlcRNGIREKHG--TQYP 190
Cdd:COG1368 307 ---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGfdEFYD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 191 KDYltdvITNDSINYFRMS-KRMYphRPVMMVLShaaphgpEDAAPQYSSAFpnasqhiTPSyNHAPnpdkhwilrYTGP 269
Cdd:COG1368 353 RED----FDDPFDGGWGVSdEDLF--DKALEELE-------KLKKPFFAFLI-------TLS-NHGP---------YTLP 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 270 MKPVHM-QFTNMLQRRRLQTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGyhigqfGLVKGKSmPYEFDI---RIPF 345
Cdd:COG1368 403 EEDKKIpDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLeryRVPL 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494291 346 YVRGPNVEAGAINPHIVLNTDLAPTLLDMAGIDIPQD-MDGKSILKLLETERPVNSF 401
Cdd:COG1368 476 LIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDLLSPDTDPFAFRNG 532
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
73-376 |
5.38e-09 |
|
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: 58.46 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 73 MMQGGTHFSNAFATTPMCCPSRS--TILTGkyvhnhhTYTNNENCSSPSWQAHHEPHTFAVHLNNSGYRTAFFgkylneY 150
Cdd:cd16015 32 LAKEGLYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSYTLYKLNPLPSLPSILKEQGYETIFI------H 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 151 NGsyvppgwrewvalvkNSRFYNytlcRNGIREKHG--TQYPKDYLTDVITNDSINY------FRMSKRMYPHRpvmmvl 222
Cdd:cd16015 99 GG---------------DASFYN----RDSVYPNLGfdEFYDLEDFPDDEKETNGWGvsdeslFDQALEELEEL------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 223 shaaphgpeDAAPQYSSAfpnasqhITPSyNHAPnpdkhWILRYTGPMKPVHMQFTNMLQRRRLQTLLSVDDSVEKVYNM 302
Cdd:cd16015 154 ---------KKKPFFIFL-------VTMS-NHGP-----YDLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEK 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528494291 303 LVETGELDNTYIIYMSDHGYHIGQFGLVKGKSMPYEFdiRIPFYVRGPNVEAGAINPHIVLNTDLAPTLLDMAG 376
Cdd:cd16015 212 LKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
345-394 |
6.13e-06 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 49.52 E-value: 6.13e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 528494291 345 FYVRGPNVEAGAINPHIVLnTDLAPTLLDMAGIDIPQDMDGKSILKLLET 394
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFAR 470
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
214-372 |
7.88e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 49.52 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 214 PHRPVMMVLSHAAPHGPEDAAPQYSSAFP-NASQHITPSYNHAPNPDKHwilRYtgpmkpvhmqftnmlqrrrLQTLLSV 292
Cdd:COG3083 379 SDRPWFSYLFLDAPHAYSFPADYPKPFQPsEDCNYLALDNESDPTPFKN---RY-------------------RNAVHYV 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 293 DDSVEKVYNMLVETGELDNTYIIYMSDHGY-----------HIGQFGlvkgksmPYEfdIRIPFYVRGPNVEAGAINpHI 361
Cdd:COG3083 437 DSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS-------RYQ--LQVPLVIHWPGTPPQVIS-KL 506
|
170
....*....|.
gi 528494291 362 VLNTDLAPTLL 372
Cdd:COG3083 507 TSHLDIVPTLM 517
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
288-378 |
1.95e-05 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 47.23 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 288 TLLSVDDSVEKVYNMLVETGEldNTYIIYMSDHGYHIGQFGlVKGKSMPYEFD--IRIPFYV--------RGPNVEAGAI 357
Cdd:cd16017 191 SILYTDYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRAN 267
|
90 100
....*....|....*....|.
gi 528494291 358 NPHIVLNTDLAPTLLDMAGID 378
Cdd:cd16017 268 KDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
366-390 |
1.06e-04 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 45.86 E-value: 1.06e-04
10 20
....*....|....*....|....*
gi 528494291 366 DLAPTLLDMAGIDIPQDMDGKSILK 390
Cdd:PRK05434 483 DIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
366-390 |
1.09e-04 |
|
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440460 Cd Length: 511 Bit Score: 45.81 E-value: 1.09e-04
10 20
....*....|....*....|....*
gi 528494291 366 DLAPTLLDMAGIDIPQDMDGKSILK 390
Cdd:COG0696 486 DIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
344-389 |
2.04e-04 |
|
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: 44.71 E-value: 2.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 528494291 344 PFYVRGPNV-----EAGAInphivlnTDLAPTLLDMAGIDIPQDMDGKSIL 389
Cdd:cd16010 460 PFIIVDPGLkrkllKDGGL-------ADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
254-376 |
1.57e-03 |
|
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: 41.42 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 254 HAPNPD--KHwilRYtGPMKPvhmQFTNMLQRrrlqtllsVDDSVEKVYNMLVETGELDNTYIIYMSDHGY-----HiGQ 326
Cdd:cd16018 163 YFEEPDsaGH---KY-GPDSP---EVNEALKR--------VDRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GY 226
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 528494291 327 FglvkgksmPYEFDIRIPFYVRGPNVEAGAINPHIvLNTDLAPTLLDMAG 376
Cdd:cd16018 227 D--------NELPDMRAIFIARGPAFKKGKKLGPF-RNVDIYPLMCNLLG 267
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| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
283-389 |
4.41e-03 |
|
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 40.59 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 283 RRRLQTLLSVDDSVEKVYNML-VETGElDNTYIIYMSDHGYHIGQFGLV---------------KGKS--MPYEFDIRIP 344
Cdd:cd16016 334 QAAAAEFLLQMPGVAAAYTADeLLAGP-EPTGIRERLRNGYNPKRSGDLivvlkpgwiegdgsgKGTThgSPYDYDTHVP 412
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90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 528494291 345 FYVRGPNVEAGAIN--PHIvlnTDLAPTLLDMAGIDIPQDMDGKSIL 389
Cdd:cd16016 413 LLFYGWGIKPGEIPrpVEI---TDIAPTLAALLGIQPPNGCIGKPLL 456
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| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
277-396 |
4.43e-03 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 40.41 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 277 FTNMLQRRRLQTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQF-GLVKGK---SMPYEFdIRIP--FYVRGP 350
Cdd:pfam02995 298 WSNSLSHDDFNYASALDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLrRTSQGMleeRLPLMS-IRYPpwFRETYP 376
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 528494291 351 N-VEAGAINPH-IVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETER 396
Cdd:pfam02995 377 QaVENLELNANrLTTPFDLHATLKDILHLGELSDKELQDRMKALDCPR 424
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|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
293-388 |
8.12e-03 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 39.09 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494291 293 DDSVEKVYNMLVETGELDNTYIIYMSDHGY-----HigqfglvkGKSMPYEfdIRIPFYVRGPNVEAGAINPH------- 360
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHGMtdagnH--------GGSSPGE--TSVPLLFISPKFSSKPSNADgelsyye 246
|
90 100
....*....|....*....|....*...
gi 528494291 361 IVLNTDLAPTLLDMAGIDIPQDMDGKSI 388
Cdd:cd16024 247 TVQQVDLAPTLALLLGLPIPKNSVGVLI 274
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