|
Name |
Accession |
Description |
Interval |
E-value |
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
58-527 |
2.00e-98 |
|
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: 304.47 E-value: 2.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLPFdkgsfdpktMENREVvdtykigidkaieaaqkSTPTLLSLMDEGVRFTNGYVAhGVSGPSRA 137
Cdd:cd16146 1 PNVILILTDDQGYGDLGF---------HGNPIL-----------------KTPNLDRLAAESVRFTNFHVS-PVCAPTRA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSNTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSkisnvpvpedkqtrdyhDNFttfsaeEWQP 217
Cdd:cd16146 54 ALLTGRYPFRTGVWHTILGRERMRLDETTLAEVFKDAGYRTGIFGKWHLG-----------------DNY------PYRP 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 218 QNRGFDYFMGFHAAGTAY--------YNSPSLFKNRERVPAKGYISDQLTDEAIGVVDRAKtlDQPFMLYLAYNAPHLPN 289
Cdd:cd16146 111 QDRGFDEVLGHGGGGIGQypdywgndYFDDTYYHNGKFVKTEGYCTDVFFDEAIDFIEENK--DKPFFAYLATNAPHGPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 290 DnpAPEQYQKQFNTGSQTAD--NYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPLPLNGAQKGYKSQT 367
Cdd:cd16146 189 Q--VPDKYLDPYKDMGLDDKlaAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFNAGMRGKKGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 368 YPGGTHTPMFMWWKGKLQPGN-YDKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKKQGEPHKNLtwitsYSHW 446
Cdd:cd16146 267 YEGGHRVPFFIRWPGKILAGKdVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL-----FTHS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 447 FDEENIPFWdnYHKFVrhqsddyphnpntedlsqfsytVRNNDYSLVyTVENNQLGLYKL-TDLQQKDNLAAANPQVVKE 525
Cdd:cd16146 342 GRWPPPPKK--KRNAA----------------------VRTGRWRLV-SPKGFQPELYDIeNDPGEENDVADEHPEVVKR 396
|
..
gi 1134749623 526 MQ 527
Cdd:cd16146 397 LK 398
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
36-540 |
1.41e-97 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 301.80 E-value: 1.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 36 KATKTNVAFSDFTPTEYSTKGKPNIIVLTMDDLGYGQLpfdkGSFDPKTMEnrevvdtykigidkaieaaqksTPTLLSL 115
Cdd:COG3119 2 KRLLLLLLALLAAAAAAAAAKRPNILFILADDLGYGDL----GCYGNPLIK----------------------TPNIDRL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 116 MDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNT-DAQDGIPLTETFLPELFQNHGYYTAAVGKWHLskisnvpv 194
Cdd:COG3119 56 AAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGeGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 195 pedkqtrdyhdnfttfsaeewqpqnrgfdyfmgfhaagtayynspslfknrervpakgYISDQLTDEAIGVVDRAKTLDQ 274
Cdd:COG3119 128 ----------------------------------------------------------YLTDLLTDKAIDFLERQADKDK 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 275 PFMLYLAYNAPHLPNDnpAPEQYQKQF------------------NTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYD 336
Cdd:COG3119 150 PFFLYLAFNAPHAPYQ--APEEYLDKYdgkdiplppnlaprdlteEELRRARAAYAAMIEEVDDQVGRLLDALEELGLAD 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 337 NTIILFTSDNGAVIDgplplNGAQKGYKSQTYPGGTHTPMFMWWKGKLQPG-NYDKLISAMDFYPTALDAADISIPKDlk 415
Cdd:COG3119 228 NTIVVFTSDNGPSLG-----EHGLRGGKGTLYEGGIRVPLIVRWPGKIKAGsVSDALVSLIDLLPTLLDLAGVPIPED-- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 416 LDGVSLLPWLQDKKQGEPHknltwiTSYSHWFDEENipfwdnyhkfvrhqsddyphnpntedlsqfSYTVRNNDYSLVYT 495
Cdd:COG3119 301 LDGRSLLPLLTGEKAEWRD------YLYWEYPRGGG------------------------------NRAIRTGRWKLIRY 344
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1134749623 496 VENNQLG-LYKL-TDLQQKDNLAAANPQVVKEMQGVVREFIDSSQPP 540
Cdd:COG3119 345 YDDDGPWeLYDLkNDPGETNNLAADYPEVVAELRALLEAWLKELGDP 391
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
58-527 |
3.21e-94 |
|
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: 294.07 E-value: 3.21e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLpfdkGSFDPKTMEnrevvdtykigidkaieaaqksTPTLLSLMDEGVRFTNGYVAHGVSGPSRA 137
Cdd:cd16144 1 PNIVLILVDDLGWADL----GCYGSKFYE----------------------TPNIDRLAKEGMRFTQAYAAAPVCSPSRA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSNTDAQ---------------DGIPLTETFLPELFQNHGYYTAAVGKWHLSKISNVpvpedkqtrd 202
Cdd:cd16144 55 SILTGQYPARLGITDVIPGRrgppdntklipppstTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGY---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 203 yhdnfttfsaeewQPQNRGFDY-FMGFHAAGTAYYNSPSLFKNR--ERVPAKGYISDQLTDEAIGVVDRAKtlDQPFMLY 279
Cdd:cd16144 125 -------------GPEDQGFDVnIGGTGNGGPPSYYFPPGKPNPdlEDGPEGEYLTDRLTDEAIDFIEQNK--DKPFFLY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 280 LAYNAPHLPNDNPA--PEQYQKQFNTGSQTADN-YYAS-VYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVI--DGP 353
Cdd:cd16144 190 LSHYAVHTPIQARPelIEKYEKKKKGLRKGQKNpVYAAmIESLDESVGRILDALEELGLADNTLVIFTSDNGGLStrGGP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 354 LPLNGAQKGYKSQTYPGGTHTPMFMWWKGKLQPGNY-DKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKKQGE 432
Cdd:cd16144 270 PTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVsDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 433 PHKNLtwitsyshwfdeenipFWdnyhkfvrHqsddYPHNPNteDLSQFSYTVRNNDYSLVYTVENNQLGLYKL-TDLQQ 511
Cdd:cd16144 350 PRRAL----------------FW--------H----FPHYHG--QGGRPASAIRKGDWKLIEFYEDGRVELYNLkNDIGE 399
|
490
....*....|....*.
gi 1134749623 512 KDNLAAANPQVVKEMQ 527
Cdd:cd16144 400 TNNLAAEMPEKAAELK 415
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
57-435 |
1.61e-84 |
|
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: 268.28 E-value: 1.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLGYGqlpfDKGSFDPKTMEnrevvdtykigidkaieaaqksTPTLLSLMDEGVRFTNGYVAHGVSGPSR 136
Cdd:cd16026 1 KPNIVVILADDLGYG----DLGCYGSPLIK----------------------TPNIDRLAAEGVRFTDFYAAAPVCSPSR 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 137 AAIMTGRAPARFGVYSN---TDAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSkisnvpvpedkqtrdyhdnfttfSAE 213
Cdd:cd16026 55 AALLTGRYPVRVGLPGVvgpPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-----------------------HQP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 214 EWQPQNRGFDYF--------MGFHAAGTAYYNSP--SLFKNRERVPAK---GYISDQLTDEAIGVVDRAKtlDQPFMLYL 280
Cdd:cd16026 112 EFLPTRHGFDEYfgipysndMWPFPLYRNDPPGPlpPLMENEEVIEQPadqSSLTQRYTDEAVDFIERNK--DQPFFLYL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 281 AYNAPHLPndNPAPEQYQkqfntGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPLPL--NG 358
Cdd:cd16026 190 AHTMPHVP--LFASEKFK-----GRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGgsAG 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749623 359 AQKGYKSQTYPGGTHTPMFMWWKGKLQPGN-YDKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKKQGEPHK 435
Cdd:cd16026 263 PLRGGKGTTWEGGVRVPFIAWWPGVIPAGTvSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHP 340
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
58-520 |
1.83e-83 |
|
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: 266.00 E-value: 1.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLpfdkGSFDPKtmenrevvdtyKIgidkaieaaqkSTPTLLSLMDEGVRFTNGYVAHGVSGPSRA 137
Cdd:cd16145 1 PNIIFILADDLGYGDL----GCYGQK-----------KI-----------KTPNLDRLAAEGMRFTQHYAGAPVCAPSRA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSNTDAQDGIPLTE--TFLPELFQNHGYYTAAVGKWHLskisnvpvpedkqtrdyhDNFTTFSaeew 215
Cdd:cd16145 55 SLLTGLHTGHTRVRGNSEPGGQDPLPPddVTLAEVLKKAGYATAAFGKWGL------------------GGPGTPG---- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 216 QPQNRGFDYFMGF--HAAGTAYYnsPS-LFKNRERVPAKG------------------YISDQLTDEAIGVVDRAKtlDQ 274
Cdd:cd16145 113 HPTKQGFDYFYGYldQVHAHNYY--PEyLWRNGEKVPLPNnvippldegnnagggggtYSHDLFTDEALDFIRENK--DK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 275 PFMLYLAYNAPHLPNDNPAPEQYQKQFNTGSQTAD--------NYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDN 346
Cdd:cd16145 189 PFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGIYAYlpwpqpekAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDN 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 347 GAVIDGPLPL-------NGAQKGYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAM-DFYPTALDAADISIPKDlkLDG 418
Cdd:cd16145 269 GPHSEGGSEHdpdffdsNGPLRGYKRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFwDFMPTLADLAGAEPPED--IDG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 419 VSLLPWLQDKKQGEPHKNLTWitsyshwfdeenipfwdNYHKFVRHQSddyphnpntedlsqfsytVRNNDYSLV-YTVE 497
Cdd:cd16145 347 ISLLPTLLGKPQQQQHDYLYW-----------------EFYEGGGAQA------------------VRMGGWKAVrHGKK 391
|
490 500
....*....|....*....|....
gi 1134749623 498 NNQLGLYKL-TDLQQKDNLAAANP 520
Cdd:cd16145 392 DGPFELYDLsTDPGETNNLAAQHP 415
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
58-420 |
2.60e-76 |
|
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: 241.19 E-value: 2.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLPFdkgsfdpktmENREVVDTykigidkaieaaqkstPTLLSLMDEGVRFTNGYVAHGVSGPSRA 137
Cdd:cd16022 1 PNILLIMTDDLGYDDLGC----------YGNPDIKT----------------PNLDRLAAEGVRFTNAYVASPVCSPSRA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSNTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHlskisnvpvpedkqtrdyhdnfttfsaeewqp 217
Cdd:cd16022 55 SLLTGRYPHRHGVRGNVGNGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 218 qnrgfdyfmgfhaagtayynspslfknrervpakgyisdqltDEAIGVVDRAKTlDQPFMLYLAYNAPHLPNdnpapeqy 297
Cdd:cd16022 103 ------------------------------------------DEAIDFIERRDK-DKPFFLYVSFNAPHPPF-------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 298 qkqfntgsqtadNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGavidGPLPLNGAqKGYKSQTYPGGTHTPMF 377
Cdd:cd16022 132 ------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHG----DMLGDHGL-RGKKGSLYEGGIRVPFI 194
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1134749623 378 MWWKGKLQPG-NYDKLISAMDFYPTALDAADISIPKdlKLDGVS 420
Cdd:cd16022 195 VRWPGKIPAGqVSDALVSLLDLLPTLLDLAGIEPPE--GLDGRS 236
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
58-437 |
1.26e-75 |
|
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: 245.19 E-value: 1.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGqlpfDKGSFDPKTmenrevvdtyKIgidkaieaaqkSTPTLLSLMDEGVRFTNGYVAHGVSGPSRA 137
Cdd:cd16143 1 PNIVIILADDLGYG----DISCYNPDS----------KI-----------PTPNIDRLAAEGMRFTDAHSPSSVCTPSRY 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARF---GVYSNTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHL-----SKISNVPVPEDKQTRDYHDNFTT 209
Cdd:cd16143 56 GLLTGRYPWRSrlkGGVLGGFSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLgldwkKKDGKKAATGTGKDVDYSKPIKG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 210 fsaeewQPQNRGFDYFMGFHAagtayynspslfknrervpakGYISDQLTDEAIGVVDRAKTLDQPFMLYLAYNAPHLPN 289
Cdd:cd16143 136 ------GPLDHGFDYYFGIPA---------------------SEVLPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 290 dNPAPEqyqkqFNtGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPLPL--------NGAQK 361
Cdd:cd16143 189 -VPSPE-----FQ-GKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYADYKElekfghdpSGPLR 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749623 362 GYKSQTYPGGTHTPMFMWWKGKLQPG-NYDKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKKQGEPHKNL 437
Cdd:cd16143 262 GMKADIYEGGHRVPFIVRWPGKIPAGsVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESL 338
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
58-408 |
3.64e-69 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 224.99 E-value: 3.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLpfdkgsfdpktmenrevvdtykigidKAIEAAQKSTPTLLSLMDEGVRFTNGYVAHGVSGPSRA 137
Cdd:pfam00884 1 PNVVLVLGESLRAPDL--------------------------GLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRF 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSNTdaQDGIPLTETFLPELFQNHGYYTAAVGKWHLSKISNVpvpedkqtrdyhdnfttfsaeewQP 217
Cdd:pfam00884 55 ALLTGLPPHNFGSYVST--PVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ-----------------------SP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 218 QNRGFDYFMGFHAAGTAYYNSPslfKNRERVPAKGYISDQLTDEAIGVVDRAktlDQPFMLYLAYNAPHLPNdnPAPEQY 297
Cdd:pfam00884 110 CNLGFDKFFGRNTGSDLYADPP---DVPYNCSGGGVSDEALLDEALEFLDNN---DKPFFLVLHTLGSHGPP--YYPDRY 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 298 QKQFNT-------GSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPlplNGAQKGYKS-QTYP 369
Cdd:pfam00884 182 PEKYATfkpsscsEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEG---GGYLHGGKYdNAPE 258
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1134749623 370 GGTHTPMFMWWKGKLQPGNYDK-LISAMDFYPTALDAADI 408
Cdd:pfam00884 259 GGYRVPLLIWSPGGKAKGQKSEaLVSHVDLFPTILDLAGI 298
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
58-421 |
7.88e-68 |
|
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: 224.35 E-value: 7.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLPFdKGSfdpktmenrevvdtykigidkaieaAQKSTPTLLSLMDEGVRFTNGYVAHgVSGPSRA 137
Cdd:cd16029 1 PHIVFILADDLGWNDVGF-HGS-------------------------DQIKTPNLDALAADGVILNNYYVQP-ICTPSRA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYS---NTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSkisnvpvpedkqtrdyhdnfttFSAEE 214
Cdd:cd16029 54 ALMTGRYPIHTGMQHgviLAGEPYGLPLNETLLPQYLKELGYATHLVGKWHLG----------------------FYTWE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 215 WQPQNRGFDYFMGFHAAGTAYYN--------SPSLFKNRERVPAKG----YISDQLTDEAIGVVDRAKTlDQPFMLYLAY 282
Cdd:cd16029 112 YTPTNRGFDSFYGYYGGAEDYYThtsggandYGNDDLRDNEEPAWDyngtYSTDLFTDRAVDIIENHDP-SKPLFLYLAF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 283 NAPHLPndNPAPEQYQKQFNTGSQTADN-----YYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPL--- 354
Cdd:cd16029 191 QAVHAP--LQVPPEYADPYEDKFAHIKDedrrtYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggs 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749623 355 --PLngaqKGYKSQTYPGGTHTPMFMWWKG--KLQPGNYDKLISAMDFYPTALDAADISIPKDLKLDGVSL 421
Cdd:cd16029 269 nyPL----RGGKNTLWEGGVRVPAFVWSPLlpPKRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQ 335
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
56-526 |
1.94e-63 |
|
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: 213.93 E-value: 1.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 56 GKPNIIVLTMDDLGYGQLPFdkgsfdpktMENREVVdtykigidkaieaaqksTPTLLSLMDEGVRFTNGYVAHGVSGPS 135
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGC---------YGNPIVK-----------------TPNIDRLAKEGVRFDNAFVTTSICAPS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 136 RAAIMTGRAPARFGVYSNTDaqDGIPLTETFLPELFQNHGYYTAAVGKWHLskisnvpvpedkqtrdyhdnfttfsAEEW 215
Cdd:cd16031 55 RASILTGQYSHRHGVTDNNG--PLFDASQPTYPKLLRKAGYQTAFIGKWHL-------------------------GSGG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 216 QPQNRGFDYFMGFHAAGTaYYNsPSLFKNRERVPAKGYISDQLTDEAIGVVDRAKTlDQPFMLYLAYNAPHLPnDNPAPe 295
Cdd:cd16031 108 DLPPPGFDYWVSFPGQGS-YYD-PEFIENGKRVGQKGYVTDIITDKALDFLKERDK-DKPFCLSLSFKAPHRP-FTPAP- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 296 QYQKQFNTGS----QTAD-------------------------------------NYYASVYSVDQGVKRILEQLKKNGQ 334
Cdd:cd16031 183 RHRGLYEDVTipepETFDdddyagrpewareqrnrirgvldgrfdtpekyqrymkDYLRTVTGVDDNVGRILDYLEEQGL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 335 YDNTIILFTSDNGAvidgplpLNGAQkGY--KSQTYPGGTHTPMFMWWKGKLQPGN-YDKLISAMDFYPTALDAADISIP 411
Cdd:cd16031 263 ADNTIIIYTSDNGF-------FLGEH-GLfdKRLMYEESIRVPLIIRDPRLIKAGTvVDALVLNIDFAPTILDLAGVPIP 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 412 KDlkLDGVSLLPWLQDKKQgEPHKNLTWitsYSHWFDeenipfwdnyhkfvrhqsDDYPHNPNtedlsqfSYTVRNNDYS 491
Cdd:cd16031 335 ED--MQGRSLLPLLEGEKP-VDWRKEFY---YEYYEE------------------PNFHNVPT-------HEGVRTERYK 383
|
490 500 510
....*....|....*....|....*....|....*....
gi 1134749623 492 LVYTVENNQLG-LYKL-TDLQQKDNLA--AANPQVVKEM 526
Cdd:cd16031 384 YIYYYGVWDEEeLYDLkKDPLELNNLAndPEYAEVLKEL 422
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
57-431 |
3.70e-62 |
|
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: 209.25 E-value: 3.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLGYGQLPFDKgsfdpktmenrevvdtykigidkaiEAAQKSTPTLLSLMDEGVRFTNGYVAHGVSGPSR 136
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANW-------------------------APNAILTPNLDKLAAEGTRFVDWYSAASVCSPSR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 137 AAIMTGRAPARFGVYSN--TDAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSkisnvpvpedkQTRDYHdnfttfsaee 214
Cdd:cd16161 56 ASLMTGRLGLRNGVGHNflPTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLG-----------QREAYL---------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 215 wqPQNRGFDYFMGFhaagtAYYNSPSLfknrervpakgyiSDQLTDEAIGVVDRAKTLDQPFMLYLAYNAPHLPNDNPAP 294
Cdd:cd16161 115 --PNSRGFDYYFGI-----PFSHDSSL-------------ADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 295 EQYQKQFNTGsqtadnYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNG--------AVIDGPLPLNGAQ--KGYK 364
Cdd:cd16161 175 FQSPTSGRGP------YGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelAVGPGTGDWQGNLggSVAK 248
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749623 365 SQTYPGGTHTPMFMWWKGKLQPGNYDK-LISAMDFYPTALDAADISIPKDLKLDGVSLLP-WLQDKKQG 431
Cdd:cd16161 249 ASTWEGGHREPAIVYWPGRIPANSTSAaLVSTLDIFPTVVALAGASLPPGRIYDGKDLSPvLFGGSKTG 317
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
56-439 |
1.71e-61 |
|
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: 208.07 E-value: 1.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 56 GKPNIIVLTMDDLGYGQL-PFdkGSfdpktmenrEVvdtykigidkaieaaqkSTPTLLSLMDEGVRFTNGYVAhGVSGP 134
Cdd:cd16025 1 GRPNILLILADDLGFSDLgCF--GG---------EI-----------------PTPNLDALAAEGLRFTNFHTT-ALCSP 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 135 SRAAIMTGRAPARFGVYSNTDAQDGIPLTETFLP-------ELFQNHGYYTAAVGKWHLskisnvpVPEDkqtrdyhdnf 207
Cdd:cd16025 52 TRAALLTGRNHHQVGMGTMAELATGKPGYEGYLPdsaatiaEVLKDAGYHTYMSGKWHL-------GPDD---------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 208 ttfsaeewqpqnrgfdyfmgFHAagtayynspslfknrervpakgyiSDQLTDEAIGVVDRAKTLDQPFMLYLAYNAPHL 287
Cdd:cd16025 115 --------------------YYS------------------------TDDLTDKAIEYIDEQKAPDKPFFLYLAFGAPHA 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 288 PNDNPAP--EQYQKQFNTG------------------------SQTADN-------------YYA---SVY-----SVDQ 320
Cdd:cd16025 151 PLQAPKEwiDKYKGKYDAGwdalreerlerqkelglipadtklTPRPPGvpawdslspeekkLEArrmEVYaamveHMDQ 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 321 GVKRILEQLKKNGQYDNTIILFTSDNGA--------VIDGPLplngaqKGYKSQTYPGGTHTPMFMWW-KGKLQPG-NYD 390
Cdd:cd16025 231 QIGRLIDYLKELGELDNTLIIFLSDNGAsaepgwanASNTPF------RLYKQASHEGGIRTPLIVSWpKGIKAKGgIRH 304
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1134749623 391 KLISAMDFYPTALDAADISIPKDLK------LDGVSLLPWLQDKKQGEPHKNLTW 439
Cdd:cd16025 305 QFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQYF 359
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
58-534 |
2.03e-61 |
|
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: 206.98 E-value: 2.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGygqlPFDKGSFDPktmenreVVdtykigidkaieaaqkSTPTLLSLMDEGVRFTNGYVAHGVSGPSRA 137
Cdd:cd16027 1 PNILWIIADDLS----PDLGGYGGN-------VV----------------KTPNLDRLAAEGVRFTNAFTTAPVCSPSRS 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSNtdAQDGIPLTETF--LPELFQNHGYYTAAVGKWHLSkisnvpvpedkqtrdyhdnfttfsaeew 215
Cdd:cd16027 54 ALLTGLYPHQNGAHGL--RSRGFPLPDGVktLPELLREAGYYTGLIGKTHYN---------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 216 QPQNRGFDYFMGFHaagtayynspslfknrervPAKGYISDQLTDEAIGVVDRAKTlDQPFMLYLAYNAPHLPNdnPAPE 295
Cdd:cd16027 104 PDAVFPFDDEMRGP-------------------DDGGRNAWDYASNAADFLNRAKK-GQPFFLWFGFHDPHRPY--PPGD 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 296 QYQKQFN---------------TGSQTADnYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGavidGPLPlngaq 360
Cdd:cd16027 162 GEEPGYDpekvkvppylpdtpeVREDLAD-YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG----MPFP----- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 361 kGYKSQTYPGGTHTPMFMWWKGKLQPGN-YDKLISAMDFYPTALDAADISIPKDlkLDGVSLLPWLQDKKQgePHKNltW 439
Cdd:cd16027 232 -RAKGTLYDSGLRVPLIVRWPGKIKPGSvSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKD--PGRD--Y 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 440 ITSYSHWFDEEnipfwdnyhkfvrhqsdDYPhnpntedlsqfSYTVRNNDYSLV---YTVEnnqlgLYKL-TDLQQKDNL 515
Cdd:cd16027 305 VFAERDRHDET-----------------YDP-----------IRSVRTGRYKYIrnyMPEE-----LYDLkNDPDELNNL 351
|
490 500
....*....|....*....|..
gi 1134749623 516 aAANP---QVVKEMQGVVREFI 534
Cdd:cd16027 352 -ADDPeyaEVLEELRAALDAWM 372
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
108-447 |
8.80e-60 |
|
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: 203.57 E-value: 8.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 108 STPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNtdaqdGIPL--TETFLPELFQNHGYYTAAVGKWH 185
Cdd:cd16034 26 KTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN-----DVPLppDAPTIADVLKDAGYRTGYIGKWH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 186 LskisNVPVPEDKQTRDYHdnfttfsaeeWQPQNR-GFDYFMGFHAagTAYYNSPSLFKNR-ERVPAKGYISDQLTDEAI 263
Cdd:cd16034 101 L----DGPERNDGRADDYT----------PPPERRhGFDYWKGYEC--NHDHNNPHYYDDDgKRIYIKGYSPDAETDLAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 264 GVVDRAKTLDQPFMLYLAYNAPHLPNDNpAPEQYQKQFNTGSQT------------------ADNYYASVYSVDQGVKRI 325
Cdd:cd16034 165 EYLENQADKDKPFALVLSWNPPHDPYTT-APEEYLDMYDPKKLLlrpnvpedkkeeaglredLRGYYAMITALDDNIGRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 326 LEQLKKNGQYDNTIILFTSDNGaviDgplpLNGAQkG--YKSQTYPGGTHTPMFMWWKGKLQPG-NYDKLISAMDFYPTA 402
Cdd:cd16034 244 LDALKELGLLENTIVVFTSDHG---D----MLGSH-GlmNKQVPYEESIRVPFIIRYPGKIKAGrVVDLLINTVDIMPTL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1134749623 403 LDAADISIPKDlkLDGVSLLPWLQDKKQGEPHKN-LTWITSYSHWF 447
Cdd:cd16034 316 LGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVlLQCFVPFGGGS 359
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
57-434 |
7.97e-58 |
|
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: 199.58 E-value: 7.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLGYGqlpfDKGSFDPKTMEnREVVDtykigidkaieaaqkstptllSLMDEGVRFTNGYVAHGVSGPSR 136
Cdd:cd16160 1 KPNIVLFFADDMGYG----DLASYGHPTQE-RGPID---------------------DMAAEGIRFTQAYSADSVCTPSR 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 137 AAIMTGRAPARFGVYSNT-----DAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSkisnvpVPEDKQTRDYHdnfttfs 211
Cdd:cd16160 55 AALLTGRLPIRSGMYGGTrvflpWDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLG------INENNHSDGAH------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 212 aeewQPQNRGFDYF-----MGFHAAGTA---YYNSPS-----LFKNRERVpAKGYISDQLTDEaigVVDRAKT-----LD 273
Cdd:cd16160 122 ----LPSHHGFDFVgtnlpFTNSWACDDtgrHVDFPDrsacfLYYNDTIV-EQPIQHEHLTET---LVGDAKSfiednQE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 274 QPFMLYLAYNAPHLPndnpapeQYQKQFNTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDgp 353
Cdd:cd16160 194 NPFFLYFSFPQTHTP-------LFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVE-- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 354 LPLNGAQ----KGYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKK 429
Cdd:cd16160 265 YCLEGGStgglKGGKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEA 344
|
....*
gi 1134749623 430 QGEPH 434
Cdd:cd16160 345 DSPHD 349
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
58-448 |
5.24e-57 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 195.51 E-value: 5.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYgqlpfdkgsfdpktmenrEVVDTYkiGidkaieAAQKSTPTLLSLMDEGVRFTNGYvAHGVSGPSRA 137
Cdd:cd16151 1 PNIILIMADDLGY------------------ECIGCY--G------GESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRV 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSNTDAQDGIplteTFlPELFQNHGYYTAAVGKWHLSKISNVPvpedkqtrDYhdnfttfsaeewqP 217
Cdd:cd16151 54 QLMTGKYNFRNYVVFGYLDPKQK----TF-GHLLKDAGYATAIAGKWQLGGGRGDG--------DY-------------P 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 218 QNRGFD-YFMGFHAAGTAYYNSPSLFKNRER---VPAKG---YISDQLTDEAIGVVDRAKtlDQPFMLYLAYNAPHLPND 290
Cdd:cd16151 108 HEFGFDeYCLWQLTETGEKYSRPATPTFNIRngkLLETTegdYGPDLFADFLIDFIERNK--DQPFFAYYPMVLVHDPFV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 291 N-PAPEQYQKQFNTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPLPLNGAQ-KGYKSQTY 368
Cdd:cd16151 186 PtPDSPDWDPDDKRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTNGREvRGGKGKTT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 369 PGGTHTPMFMWWKGKLQPGN-YDKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKKQGEPHKNLTWITSYSHWF 447
Cdd:cd16151 266 DAGTHVPLIVNWPGLIPAGGvSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKK 345
|
.
gi 1134749623 448 D 448
Cdd:cd16151 346 F 346
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
58-476 |
1.72e-53 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 185.81 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLPFdkgsfdpktmenrevvdtYKIGIDKAIEaaqksTPTLLSLMDEGVRFTNGYVAHGVSgPSRA 137
Cdd:cd16142 1 PNILVILGDDIGWGDLGC------------------YGGGIGRGAP-----TPNIDRLAKEGLRFTSFYVEPSCT-PGRA 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYS--NTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSkisnvpvpedkqtrdyhdnfttfSAEEW 215
Cdd:cd16142 57 AFITGRHPIRTGLTTvgLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG-----------------------DEDGR 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 216 QPQNRGFDYFMGFhaagtAYYnspslfknrervpakgYISDQLTDEAIGVVDRAKTLDQPFMLYLAYNAPHLPNdNPAPE 295
Cdd:cd16142 114 LPTDHGFDEFYGN-----LYH----------------TIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPT-LPSPE 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 296 qYQkqfntGSQTADNYYA-SVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPlPLNGAQ--KGYKSQTYPGGT 372
Cdd:cd16142 172 -FE-----GKSSGKGKYAdSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVW-PDGGYTpfRGEKGTTWEGGV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 373 HTPMFMWWKGKLQPGN-YDKLISAMDFYPTALDAADISIPKDLK------LDGVSLLPWLQDKkqgEPHKNLTWItsysh 445
Cdd:cd16142 245 RVPAIVRWPGKIKPGRvSNEIVSHLDWFPTLAALAGAPDPKDKLlgkdrhIDGVDQSPFLLGK---SEKSRRSEF----- 316
|
410 420 430
....*....|....*....|....*....|....
gi 1134749623 446 WFDEENIPF---WDNYhKFVRHQSDDYPHNPNTE 476
Cdd:cd16142 317 FYFGEGELGavrWKNW-KVHFKAQEDTGGPTGEP 349
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
57-429 |
9.96e-53 |
|
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: 186.52 E-value: 9.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLGYGQLpfdkGSF-DPktmeNREvvdtykigidkaieaaqksTPTLLSLMDEGVRFTNGYVAHGVSGPS 135
Cdd:cd16157 1 KPNIILMLMDDMGWGDL----GVFgEP----SRE-------------------TPNLDRMAAEGMLFTDFYSANPLCSPS 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 136 RAAIMTGRAPARFGVYSNTD-------AQD---GIPLTETFLPELFQNHGYYTAAVGKWHLSKisnvpvpedkqtrdyhd 205
Cdd:cd16157 54 RAALLTGRLPIRNGFYTTNAharnaytPQNivgGIPDSEILLPELLKKAGYRNKIVGKWHLGH----------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 206 nfttfsAEEWQPQNRGFDYFMGF---HAA---GTAYYNSPsLFKNRE------------RVPAKGYISDQLTDEAIGVVD 267
Cdd:cd16157 117 ------RPQYHPLKHGFDEWFGApncHFGpydNKAYPNIP-VYRDWEmigryyeefkidKKTGESNLTQIYLQEALEFIE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 268 RAKTLDQPFMLYLAYNAPHlpndnpAPEQYQKQFNTGSQTAdNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNG 347
Cdd:cd16157 190 KQHDAQKPFFLYWAPDATH------APVYASKPFLGTSQRG-LYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 348 AVIDGPlPLNGAQKG----YKSQTYPGGTHTPMFMWWKGKLQPGNYDK-LISAMDFYPTALDAADISIPKDLKLDGVSLL 422
Cdd:cd16157 263 AALISA-PEQGGSNGpflcGKQTTFEGGMREPAIAWWPGHIKPGQVSHqLGSLMDLFTTSLALAGLPIPSDRAIDGIDLL 341
|
....*..
gi 1134749623 423 PWLQDKK 429
Cdd:cd16157 342 PVLLNGK 348
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
57-430 |
1.07e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 165.05 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLGYGQLpfdkgsfdpKTMENREVvdtykigidkaieaaqkSTPTLLSLMDEGVRFTNGYVAHGVSG--- 133
Cdd:cd16155 2 KPNILFILADDQRADTI---------GALGNPEI-----------------QTPNLDRLARRGTSFTNAYNMGGWSGavc 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 134 -PSRAAIMTGRaparfGVYSNTD-AQDGIPLTETFLPELFQNHGYYTAAVGKWHLSkisnvpvpedkqtrdyhdnfttfs 211
Cdd:cd16155 56 vPSRAMLMTGR-----TLFHAPEgGKAAIPSDDKTWPETFKKAGYRTFATGKWHNG------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 212 aeewqpqnrgfdyfmgfhaagtayynspslfknrervpakgyisdqLTDEAIGVVDRAKTLDQPFMLYLAYNAPHLP--- 288
Cdd:cd16155 107 ----------------------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPrqa 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 289 ----------NDNPAPEQYQKQ--FNTGSQ------------TAD-------NYYASVYSVDQGVKRILEQLKKNGQYDN 337
Cdd:cd16155 141 ppeyldmyppETIPLPENFLPQhpFDNGEGtvrdeqlapfprTPEavrqhlaEYYAMITHLDAQIGRILDALEASGELDN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 338 TIILFTSDNG-AVidGPLPLNGaqkgyKSQTYPGGTHTPMFMwwKGKLQPGN--YDKLISAMDFYPTALDAADISIPKdl 414
Cdd:cd16155 221 TIIVFTSDHGlAV--GSHGLMG-----KQNLYEHSMRVPLII--SGPGIPKGkrRDALVYLQDVFPTLCELAGIEIPE-- 289
|
410
....*....|....*.
gi 1134749623 415 KLDGVSLLPWLQDKKQ 430
Cdd:cd16155 290 SVEGKSLLPVIRGEKK 305
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
109-425 |
3.41e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 164.70 E-value: 3.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 109 TPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTD----AQDGIPLTETFLPELFQNHGYYTAAVGKW 184
Cdd:cd16033 26 TPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVEnagaYSRGLPPGVETFSEDLREAGYRNGYVGKW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 185 HLSKISNvpvpedkqtrdyhdnfttfsaeewqPQNRGFDYFMGFHAAGTAYynspslfknrervpakgyisdqLTDEAIG 264
Cdd:cd16033 106 HVGPEET-------------------------PLDYGFDEYLPVETTIEYF----------------------LADRAIE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 265 VVDRAKTLDQPFMLYLAYNAPHLP-------------NDNPAPEQ-----------YQKQFNTGSQTADN---------- 310
Cdd:cd16033 139 MLEELAADDKPFFLRVNFWGPHDPyippepyldmydpEDIPLPESfaddfedkpyiYRRERKRWGVDTEDeedwkeiiah 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 311 YYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIdgplplnGAQ----KGYKS--QTYpggtHTPMFMWWKGKL 384
Cdd:cd16033 219 YWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDAL-------GAHrlwdKGPFMyeETY----RIPLIIKWPGVI 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1134749623 385 QPGN-YDKLISAMDFYPTALDAADISIPKdlKLDGVSLLPWL 425
Cdd:cd16033 288 AAGQvVDEFVSLLDLAPTILDLAGVDVPP--KVDGRSLLPLL 327
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
57-546 |
1.06e-44 |
|
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: 164.93 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLGYGQLpfdkGSFDPKTmenrevvdtykigidkaieaaqKSTPTLLSLMDEGVRFTNGYVAHGVSGPSR 136
Cdd:cd16158 1 PPNIVLLFADDLGYGDL----GCYGHPS----------------------SSTPNLDRLAANGLRFTDFYSSSPVCSPSR 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 137 AAIMTGRAPARFGVYSNT---DAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSkisnvpVPEDKQtrdyhdnfttfsae 213
Cdd:cd16158 55 AALLTGRYQVRSGVYPGVfypGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLG------VGLNGT-------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 214 eWQPQNRGFDYFMGF---HAAG-----TAYYNSPS-------------LFKNRERVP---------------AKGYISDQ 257
Cdd:cd16158 115 -YLPTHQGFDHYLGIpysHDQGpcqnlTCFPPNIPcfggcdqgevpcpLFYNESIVQqpvdlltleeryakfAKDFIADN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 258 LTDeaigvvdraktlDQPFMLYLAYNAPHLPndnpapeQYQKQFNTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDN 337
Cdd:cd16158 194 AKE------------GKPFFLYYASHHTHYP-------QFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 338 TIILFTSDNGAVI-----DGplpLNGAQKGYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPk 412
Cdd:cd16158 255 TLVFFTSDNGPSTmrksrGG---NAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLP- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 413 DLKLDGVSLLPWLQDKKQGePHKNLTWITSYShwfDEENIPFWDNYHKFVRH-QSDDYPHNPNTEDLS-QFSYTVRNNDY 490
Cdd:cd16158 331 NVTLDGVDMSPILFEQGKS-PRQTFFYYPTSP---DPDKGVFAVRWGKYKAHfYTQGAAHSGTTPDKDcHPSAELTSHDP 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749623 491 SLVYTVENNQLGLYkltDLQQKDNLAaanpQVVKEMQGVVREFIDSSQPPLSEVNQ 546
Cdd:cd16158 407 PLLFDLSQDPSENY---NLLGLPEYN----QVLKQIQQVKERFEASMKFGESEINK 455
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
57-437 |
3.88e-44 |
|
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: 164.00 E-value: 3.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLGYGqlpfDKGSFDPKTMenrevvdtykigidkaieaaqkSTPTLLSLMDEGVRFTNGYVAHGVSGPSR 136
Cdd:cd16159 1 KPNIVLFMADDLGIG----DVGCFGNDTI----------------------RTPNIDRLAKEGVKLTHHLAAAPLCTPSR 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 137 AAIMTGRAPARFG--------VYSNTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSKISnvpvpEDKQTRDYHdnft 208
Cdd:cd16159 55 AAFLTGRYPIRSGmasshgmrVILFTASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHC-----ESRNDFCHH---- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 209 tfsaeewqPQNRGFDYFMGF---------HAAGTAYYNSP------------------SLFKNRERVPAKGYIS------ 255
Cdd:cd16159 126 --------PLNHGFDYFYGLpltnlkdcgDGSNGEYDLSFdplfplltafvlitaltiFLLLYLGAVSKRFFVFllilsl 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 256 -------------------------------------DQLTDEAIGVVDRAKtlDQPFMLYLAYNAPHLPNDNpapeqyQ 298
Cdd:cd16159 198 lfislfflllitnryfncilmrnhevveqpmslenltQRLTKEAISFLERNK--ERPFLLVMSFLHVHTALFT------S 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 299 KQFnTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGA---VIDGPLPLNGAQKGY----KSQTYPGG 371
Cdd:cd16159 270 KKF-KGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGhleEISVGGEYGGGNGGIyggkKMGGWEGG 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749623 372 THTPMFMWWKGKLQPGN-YDKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKKQGEPHKNL 437
Cdd:cd16159 349 IRVPTIVRWPGVIPPGSvIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFL 415
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
58-423 |
1.28e-43 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 156.17 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLgygqlpfdkgsfdpktmeNREVVDTYkiGIDKAIeaaqksTPTLLSLMDEGVRFTNGYVAHGVSGPSRA 137
Cdd:cd16148 1 MNVILIVIDSL------------------RADHLGCY--GYDRVT------TPNLDRLAAEGVVFDNHYSGSNPTLPSRF 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSNTDAQDgipltETFLPELFQNHGYYTAAVgkwhlskisnvpvpedkqtrdyHDNFTTFSAEEWqp 217
Cdd:cd16148 55 SLFTGLYPFYHGVWGGPLEPD-----DPTLAEILRKAGYYTAAV----------------------SSNPHLFGGPGF-- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 218 qNRGFDYFMgfhaagtayynsPSLFKNRERVPAKGYISDQLTDEAIGVVDRAKTlDQPFMLYLAYNAPHLPndnpapeqY 297
Cdd:cd16148 106 -DRGFDTFE------------DFRGQEGDPGEEGDERAERVTDRALEWLDRNAD-DDPFFLFLHYFDPHEP--------Y 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 298 QkqfntgsqtadnYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGavidgpLPLN--GAQKGYKSQTYPGGTHTP 375
Cdd:cd16148 164 L------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG------EEFGehGLYWGHGSNLYDEQLHVP 225
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1134749623 376 MFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKDlkLDGVSLLP 423
Cdd:cd16148 226 LIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
58-423 |
2.39e-41 |
|
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: 149.70 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLPfdkgsfdpkTMENREVVdtykigidkaieaaqksTPTLLSLMDEGVRFTNGYVAHGVSGPSRA 137
Cdd:cd16149 1 PNILFILTDDQGPWALG---------CYGNSEAV-----------------TPNLDRLAAEGVRFENFFCTSPVCSPARA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVY------SNTDAQDGIPLTE--TFLPELFQNHGYYTAAVGKWHLSkisnvpvpedkqtrdyhdnftt 209
Cdd:cd16149 55 SLLTGRMPSQHGIHdwivegSHGKTKKPEGYLEgqTTLPEVLQDAGYRCGLSGKWHLG---------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 210 fsaeewqpqnrgfdyfmgfhaagtayynspslfknrervpakgyisdqltDEAIGVVDRAKTLDQPFMLYLAYNAPHlpn 289
Cdd:cd16149 113 --------------------------------------------------DDAADFLRRRAEAEKPFFLSVNYTAPH--- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 290 dnpAPEQYqkqfntgsqtadnyYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGavidgplpLNGAQKGYKSQtyp 369
Cdd:cd16149 140 ---SPWGY--------------FAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNG--------FNMGHHGIWGK--- 191
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749623 370 GGTHTPMFMW-----------WKGKLQPGNY-DKLISAMDFYPTALDAADISIPKDLKLDGVSLLP 423
Cdd:cd16149 192 GNGTFPLNMYdnsvkvpfiirWPGVVPAGRVvDSLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
56-431 |
1.25e-40 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 153.67 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 56 GKPNIIVLTMDdlgygQLPFDKgsfdpktmenrevvdtykIGI--DKAIEaaqksTPTLLSLMDEGVRFTNGYVAHGVSG 133
Cdd:PRK13759 5 KKPNIILIMVD-----QMRGDC------------------LGCngNKAVE-----TPNLDMLASEGYNFENAYSAVPSCT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 134 PSRAAIMTGRAPARFGV--YsntdaQDGIPLT-ETFLPELFQNHGYYTAAVGKWHLSkisnvpvPEdKQTRDYH----DN 206
Cdd:PRK13759 57 PARAALLTGLSQWHHGRvgY-----GDVVPWNyKNTLPQEFRDAGYYTQCIGKMHVF-------PQ-RNLLGFHnvllHD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 207 FTTFSAEEWQPQNRGF--DYFMGFHAAGTAYynSPSLFK---NRERVPAKGYISDQ-------LTDEAIGVVDRaKTLDQ 274
Cdd:PRK13759 124 GYLHSGRNEDKSQFDFvsDYLAWLREKAPGK--DPDLTDigwDCNSWVARPWDLEErlhptnwVGSESIEFLRR-RDPTK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 275 PFMLYLAYNAPHLPNDNPA--------------------------PEQYQKQF---NTGSQTADN----YYASVYSVDQG 321
Cdd:PRK13759 201 PFFLKMSFARPHSPYDPPKryfdmykdadipdphigdweyaedqdPEGGSIDAlrgNLGEEYARRaraaYYGLITHIDHQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 322 VKRILEQLKKNGQYDNTIILFTSDNGAVI-DGPLplngAQKGYksqTYPGGTHTPMFMWWKGKLQPGN----YDKLISAM 396
Cdd:PRK13759 281 IGRFLQALKEFGLLDNTIILFVSDHGDMLgDHYL----FRKGY---PYEGSAHIPFIIYDPGGLLAGNrgtvIDQVVELR 353
|
410 420 430
....*....|....*....|....*....|....*
gi 1134749623 397 DFYPTALDAADISIPKDlkLDGVSLLPWLQDKKQG 431
Cdd:PRK13759 354 DIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEG 386
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
57-517 |
1.37e-40 |
|
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: 152.34 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLgygqlpfdkgsfdpktmenREVVDTYkiGIDKAIeaaqksTPTLLSLMDEGVRFTNGYVAHGVSGPSR 136
Cdd:cd16030 2 KPNVLFIAVDDL-------------------RPWLGCY--GGHPAK------TPNIDRLAARGVLFTNAYCQQPVCGPSR 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 137 AAIMTGRAPARFGVYSN-TDAQDGIPLTETfLPELFQNHGYYTAAVGK-WHlskisnvpvPEDKQTRDYHDNFTTFSaee 214
Cdd:cd16030 55 ASLLTGRRPDTTGVYDNnSYFRKVAPDAVT-LPQYFKENGYTTAGVGKiFH---------PGIPDGDDDPASWDEPP--- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 215 WQPQNRGFDYFMGFHAAGTAYYNSPSLFKNRERVPAKGYISDQLTDEAIGVVDRAKTLDQPFMLYLAYNAPHLPNDnpAP 294
Cdd:cd16030 122 NPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFV--AP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 295 EQYQKQFNTGSQTADN-----------------------------------------------YYASVYSVDQGVKRILE 327
Cdd:cd16030 200 KKYFDLYPLESIPLPNpfdpidlpevawndlddlpkygdipalnpgdpkgplpdeqarelrqaYYASVSYVDAQVGRVLD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 328 QLKKNGQYDNTIILFTSDNgavidgplplngaqkGY---------KSQTYPGGTHTPMfMWW--KGKLQPGNYDKLISAM 396
Cdd:cd16030 280 ALEELGLADNTIVVLWSDH---------------GWhlgehghwgKHTLFEEATRVPL-IIRapGVTKPGKVTDALVELV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 397 DFYPTALDAADISIPKDlkLDGVSLLPWLQDKKQGEPHKNLTWitsyshwfdeenipfwdnyhkfvrhqsddYPHNPNTe 476
Cdd:cd16030 344 DIYPTLAELAGLPAPPC--LEGKSLVPLLKNPSAKWKDAAFSQ-----------------------------YPRPSIM- 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1134749623 477 dlsqfSYTVRNNDYSLVYTVENNQLG---LYKL-TDLQQKDNLAA 517
Cdd:cd16030 392 -----GYSIRTERYRYTEWVDFDKVGaeeLYDHkNDPNEWKNLAN 431
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
58-427 |
3.35e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 149.81 E-value: 3.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLPfdkgsfdpktmenrevvdTYKIGIDKAieaaqkSTPTLLSLMDEGVRFTNGYVAHGVSgPSRA 137
Cdd:cd16154 1 PNILLIIADDQGLDSSA------------------QYSLSSDLP------VTPTLDSLANSGIVFDNLWATPACS-PTRA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 138 AIMTGRAPARFGVYSntdAQDGIPLTETFLPELF----QNHGYYTAAVGKWHLSKISNVPvpedkqtrdYHDNfttfsae 213
Cdd:cd16154 56 TILTGKYGFRTGVLA---VPDELLLSEETLLQLLikdaTTAGYSSAVIGKWHLGGNDNSP---------NNPG------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 214 ewqpqnrGFDYFMG-FHAAGTAYYNSPsLFKNRERVPAKGYISDQLTDEAIGVVDRAktlDQPFMLYLAYNAPHLPNDNP 292
Cdd:cd16154 117 -------GIPYYAGiLGGGVQDYYNWN-LTNNGQTTNSTEYATTKLTNLAIDWIDQQ---TKPWFLWLAYNAPHTPFHLP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 293 aPEQYQKQFNTGSQTADN-----YY-ASVYSVDQGVKRILEQLKKNgQYDNTIILFTSDNG---AVIDGPLPLNGAqkgy 363
Cdd:cd16154 186 -PAELHSRSLLGDSADIEanprpYYlAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGtpgQVVDLPYTRNHA---- 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749623 364 KSQTYPGGTHTPMFMWWKGKLQPG-NYDKLISAMDFYPTALDAADISIPKdlKLDGVSLLPWLQD 427
Cdd:cd16154 260 KGSLYEGGINVPLIVSGAGVERANeRESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSD 322
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
109-471 |
4.00e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 148.07 E-value: 4.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 109 TPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTDAQDGIPLTetfLPELFQNHGYYTAAVGKWHlsk 188
Cdd:cd16037 26 TPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS---WGHALRAAGYETVLIGKLH--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 189 isnvpvpedkqtrdyhdnfttFSAEEwqpQNRGFDYfmgfhaagtayynspslfknrervpakgyiSDQLTDEAIGVVDR 268
Cdd:cd16037 100 ---------------------FRGED---QRHGFRY------------------------------DRDVTEAAVDWLRE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 269 AKTLDQPFMLYLAYNAPHLPNDNPaPEQYQKqFNTGSQTAdnYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGA 348
Cdd:cd16037 126 EAADDKPWFLFVGFVAPHFPLIAP-QEFYDL-YVRRARAA--YYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 349 vidgplpLNGAQKGY-KSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKDlkLDGVSLLPWLQD 427
Cdd:cd16037 202 -------MLGERGLWgKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPD--LDGRSLLPLAEG 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1134749623 428 kkqGEPHKNLtwITSYSHWFDEENIPF---WDNYhKFVRHqsDDYPH 471
Cdd:cd16037 273 ---PDDPDRV--VFSEYHAHGSPSGAFmlrKGRW-KYIYY--VGYPP 311
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
109-433 |
5.17e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 146.60 E-value: 5.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 109 TPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNtdaqdGIPL--TETFLPELFQNHGYYTAAVGKWHL 186
Cdd:cd16152 27 TPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPLpaDEKTLAHYFRDAGYETGYVGKWHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 187 SkisnvpvpedkqtrdyhdnfttfsaeewqpqnrgfdyfmgfhaagtayynspslfknrervpakGYISDQLTDEAIGVV 266
Cdd:cd16152 102 A----------------------------------------------------------------GYRVDALTDFAIDYL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 267 DRaKTLDQPFMLYLAYNAPHLPNDN---PAPEQYQKQF--------------NTGSQTADnYYASVYSVDQGVKRILEQL 329
Cdd:cd16152 118 DN-RQKDKPFFLFLSYLEPHHQNDRdryVAPEGSAERFanfwvppdlaalpgDWAEELPD-YLGCCERLDENVGRIRDAL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 330 KKNGQYDNTIILFTSDNGAVIdgpLPLNGAqkgYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADIS 409
Cdd:cd16152 196 KELGLYDNTIIVFTSDHGCHF---RTRNAE---YKRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGID 269
|
330 340
....*....|....*....|....
gi 1134749623 410 IPKDlkLDGVSLLPWLQDKKQGEP 433
Cdd:cd16152 270 VPEE--MQGRSLLPLVDGKVEDWR 291
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
57-420 |
2.74e-37 |
|
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: 142.30 E-value: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 57 KPNIIVLTMDDLgygqlpfDKGSFDPKTMenrevvdtykigidkaieaaqkstPTLLSLM-DEGVRFTNGYVAHGVSGPS 135
Cdd:cd16147 1 RPNIVLILTDDQ-------DVELGSMDPM------------------------PKTKKLLaDQGTTFTNAFVTTPLCCPS 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 136 RAAIMTGRAPARFGVYSNTDAQDGIP------LTETFLPELFQNHGYYTAAVGKW---HLSKISNVPVPedkqtrdyhdn 206
Cdd:cd16147 50 RASILTGQYAHNHGVTNNSPPGGGYPkfwqngLERSTLPVWLQEAGYRTAYAGKYlngYGVPGGVSYVP----------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 207 fttfsaeewqpqnRGFDYFMGFHAAGTAYYNSPSLFKNRERV--PAKGYISDQLTDEAIGVVDRAKTLDQPFMLYLAYNA 284
Cdd:cd16147 119 -------------PGWDEWDGLVGNSTYYNYTLSNGGNGKHGvsYPGDYLTDVIANKALDFLRRAAADDKPFFLVVAPPA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 285 PHLPNDnPAPeQYQKQF-------NTGS-----------------------QTADNYYA----SVYSVDQGVKRILEQLK 330
Cdd:cd16147 186 PHGPFT-PAP-RYANLFpnvtappRPPPnnpdvsdkphwlrrlpplnptqiAYIDELYRkrlrTLQSVDDLVERLVNTLE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 331 KNGQYDNTIILFTSDNGAVIdgplplnGA---QKGyKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAAD 407
Cdd:cd16147 264 ATGQLDNTYIIYTSDNGYHL-------GQhrlPPG-KRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAG 335
|
410
....*....|...
gi 1134749623 408 ISIPKDlkLDGVS 420
Cdd:cd16147 336 APPPSD--MDGRS 346
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
108-421 |
7.35e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 115.94 E-value: 7.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 108 STPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHls 187
Cdd:cd16153 36 ESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFEAAHPALDHGLPTFPEVLKKAGYQTASFGKSH-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 188 kisnvpvpedkqtrdyHDNFTTFSAEEWQPqnrgfdyfmgfhaagtayynspslFKNRERVPAKGyisdqltdeaigvVD 267
Cdd:cd16153 114 ----------------LEAFQRYLKNANQS------------------------YKSFWGKIAKG-------------AD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 268 RaktlDQPFMLYLAYNAPHLPNdnPAPEQYQKQFNtgsqtadnYYASVYSVDQGVKRILEQLK---KNGQYDNTIILFTS 344
Cdd:cd16153 141 S----DKPFFVRLSFLQPHTPV--LPPKEFRDRFD--------YYAFCAYGDAQVGRAVEAFKaysLKQDRDYTIVYVTG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 345 DNGAvidgPLPLNGAQKgyKSQTYPGGTHTPMFMWWKGKLQPGN---YDKLISAMDFYPTALDAADISIPKDLKLDGVSL 421
Cdd:cd16153 207 DHGW----HLGEQGILA--KFTFWPQSHRVPLIVVSSDKLKAPAgkvRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
109-407 |
9.71e-28 |
|
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: 112.78 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 109 TPTLLSLMDEGVRFTNGYVAHGVSGPSRA--AIMTGRAPARFGVYSNTDAQDGIPLTetfLPELFQNHGYYTAAVgkwHL 186
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNPLPS---LPSILKEQGYETIFI---HG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 187 SKISNvpvpedkqtrdyhDNFTTFSaeewqpQNRGFDYFMGFHAagtayynspslFKNRERVPAKGYISDQ-LTDEAIGV 265
Cdd:cd16015 100 GDASF-------------YNRDSVY------PNLGFDEFYDLED-----------FPDDEKETNGWGVSDEsLFDQALEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 266 VDRAKtlDQPFMLYLAYNAPHLPNDNPAPEQYQKQFNTGSQT-ADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTS 344
Cdd:cd16015 150 LEELK--KKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTeLENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYG 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749623 345 DNgavidgpLPLNGAQKGYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAAD 407
Cdd:cd16015 228 DH-------LPSLGSDYDETDEDPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
31-441 |
2.63e-27 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 115.91 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 31 DDVKLKATKTNVAFSDFTPTEYSTKGKPNIIVLTMDDLGygqlpfdkgsfdpktmenREVVDTYKIGIDkaieaaqkSTP 110
Cdd:COG1368 208 SEEEALEIKKYLKSNRPTPNPFGPAKKPNVVVILLESFS------------------DFFIGALGNGKD--------VTP 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 111 TLLSLMDEGVRFTNGYVAHGVSgpSRA--AIMTGRAPARFGVYSNTDAQDGIPltetFLPELFQNHGYYTAAvgkwhlsk 188
Cdd:COG1368 262 FLDSLAKESLYFGNFYSQGGRT--SRGefAVLTGLPPLPGGSPYKRPGQNNFP----SLPSILKKQGYETSF-------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 189 isnvpvpedkqtrdYHDNFTTFsaeeWqpqNR-------GFDYFMGfhaagTAYYNSPslFKNrervpakGY-ISDQ-LT 259
Cdd:COG1368 328 --------------FHGGDGSF----W---NRdsfyknlGFDEFYD-----REDFDDP--FDG-------GWgVSDEdLF 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 260 DEAIgvvDRAKTLDQPFMLYLAYNAPHLPNDnpAPEQYQKQFNTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTI 339
Cdd:COG1368 373 DKAL---EELEKLKKPFFAFLITLSNHGPYT--LPEEDKKIPDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 340 ILFTSDNGAVIDGPLPLNGAQKGYksqtypggtHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKDLKLdGV 419
Cdd:COG1368 448 FVIYGDHGPRSPGKTDYENPLERY---------RVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GR 517
|
410 420
....*....|....*....|..
gi 1134749623 420 SLlpwLQDKKQGEPHKNLTWIT 441
Cdd:COG1368 518 DL---LSPDTDPFAFRNGGFIT 536
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
108-428 |
2.04e-26 |
|
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: 112.48 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 108 STPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTdaqdgIPLTETF--LPELFQNHGYYTAAVGKWH 185
Cdd:cd16156 25 KTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNC-----MALGDNVktIGQRLSDNGIHTAYIGKWH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 186 LskisnvpvpedkqtrDYHDNF-TTFSAEEWQPqNRGFD---YFMGFHAAGTAYYNSPSLFKNRERVPAKGYISDQLTDE 261
Cdd:cd16156 100 L---------------DGGDYFgNGICPQGWDP-DYWYDmrnYLDELTEEERRKSRRGLTSLEAEGIKEEFTYGHRCTNR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 262 AIGVVDRAKtlDQPFMLYLAYNAPHLPNDNPAP--EQY--------QKQFNT---------------GSQTADN------ 310
Cdd:cd16156 164 ALDFIEKHK--DEDFFLVVSYDEPHHPFLCPKPyaSMYkdfefpkgENAYDDlenkplhqrlwagakPHEDGDKgtikhp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 311 -YYASVYSVDQGVKRILEQLKKNgqYDNTIILFTSDNGavidgplPLNGAQK--GYKSQTYPGGTHTPMFMWWKGKLQPG 387
Cdd:cd16156 242 lYFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHG-------DMLGAHKlwAKGPAVYDEITNIPLIIRGKGGEKAG 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1134749623 388 NY-DKLISAMDFYPTALDAADISIPKdlKLDGVSLLPWLQDK 428
Cdd:cd16156 313 TVtDTPVSHIDLAPTILDYAGIPQPK--VLEGESILATIEDP 352
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
109-431 |
2.51e-26 |
|
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: 109.59 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 109 TPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSN-TDAQDGIPlteTFlPELFQNHGYYTAAVGKWHLs 187
Cdd:cd16032 26 TPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNaAEFPADIP---TF-AHYLRAAGYRTALSGKMHF- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 188 kisnvpV-PEDKQTRDYhDNFTTFSAEEWqpqnrgfdyfmgfhaagtayynspsLFknrervpakgyisdqltdeaigvv 266
Cdd:cd16032 101 ------VgPDQLHGFDY-DEEVAFKAVQK-------------------------LY------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 267 DRAKTLD-QPFMLYLAYNAPHLPNDnpAPEQYQKQFNTGSQTAdnYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSD 345
Cdd:cd16032 125 DLARGEDgRPFFLTVSFTHPHDPYV--IPQEYWDLYVRRARRA--YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 346 NGAVIdgplplngAQKG--YKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKD-LKLDGVSLL 422
Cdd:cd16032 201 HGDML--------GERGlwYKMSFFEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHvPPLDGRSLL 272
|
....*....
gi 1134749623 423 PWLQDKKQG 431
Cdd:cd16032 273 PLLEGGDSG 281
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
109-439 |
7.04e-26 |
|
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: 110.43 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 109 TPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNtdaqdGIPLT--ETFLPELFQNHGYYTAAVGKWHL 186
Cdd:cd16028 26 TPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN-----GTPLDarHLTLALELRKAGYDPALFGYTDT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 187 SKisnvpvpeDKQTRDYHDNfTTFSAEEWQPqnrGFDY--FMGFHAAGtayyNSPSLFknrervpakgyisdqLTDEAIG 264
Cdd:cd16028 101 SP--------DPRGLAPLDP-RLLSYELAMP---GFDPvdRLDEYPAE----DSDTAF---------------LTDRAIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 265 VVDRAKtlDQPFMLYLAYNAPHLPNDNPAP-------------------EQYQKQ---------------FNTGSQTADN 310
Cdd:cd16028 150 YLDERQ--DEPWFLHLSYIRPHPPFVAPAPyhalydpadvpppiraeslAAEAAQhpllaaflerieslsFSPGAANAAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 311 ------------YYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIdGPLPLNGaqkgyKSQTYPGGTHTPMFM 378
Cdd:cd16028 228 lddeevaqmratYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQL-GDHWLWG-----KDGFFDQAYRVPLIV 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 379 WWkgklqPGNY---------DKLISAMDFYPTALDAADISIPKDlkLDGVSLLPWLQDKKQGEPHKNLTW 439
Cdd:cd16028 302 RD-----PRREadatrgqvvDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGAQPSDWRDAVHY 364
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
104-427 |
2.71e-25 |
|
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: 106.52 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 104 AAQKSTPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTDaQDGIPLTETFLPEL---FQNHGYYTAA 180
Cdd:cd16035 21 WAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLG-SPMQPLLSPDVPTLghmLRAAGYYTAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 181 VGKWHLSkisnvpvpedkqtrdyhdnfttfsaeewqpqnrgfdyfmgfhAAGTAYYNSPSLFKNRervpAKGYISDQltd 260
Cdd:cd16035 100 KGKWHLS------------------------------------------GAAGGGYKRDPGIAAQ----AVEWLRER--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 261 eaigvvDRAKTLDQPFMLYLAYNAPH----LPNDnpaPEQYQKQFNTgsqtadnYYASVYSVDQGVKRILEQLKKNGQYD 336
Cdd:cd16035 131 ------GAKNADGKPWFLVVSLVNPHdimfPPDD---EERWRRFRNF-------YYNLIRDVDRQIGRVLDALDASGLAD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 337 NTIILFTSDNGAvidgplpLNGA----QKGYKSqtYPGGTHTPMFMWWKG-KLQPGNYDKLISAMDFYPTALDAADISIP 411
Cdd:cd16035 195 NTIVVFTSDHGE-------MGGAhglrGKGFNA--YEEALHVPLIISHPDlFGTGQTTDALTSHIDLLPTLLGLAGVDAE 265
|
330 340
....*....|....*....|
gi 1134749623 412 KDLK----LDGVSLLPWLQD 427
Cdd:cd16035 266 ARATeappLPGRDLSPLLTD 285
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
119-479 |
7.58e-22 |
|
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: 97.23 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 119 GVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTDaqdGIPLTETFLPELFQNHGYYTAAVGKW-----HLSKISNVp 193
Cdd:cd16171 36 GSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYK---GLDPNYPTWMDRLEKHGYHTQKYGKLdytsgHHSVSNRV- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 194 vpeDKQTRDYhdNFTTfsAEEWQPqnrgfdyfmgfhaagtayynSPSLFKNR--ERVPAKGYisdQLTDEAIG-VVDRAK 270
Cdd:cd16171 112 ---EAWTRDV--PFLL--RQEGRP--------------------TVNLVGDRstVRVMLKDW---QNTDKAVHwIRKEAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 271 TLDQPFMLYLAYNAPHlpndnPAPEQYQ-KQFNTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAv 349
Cdd:cd16171 162 NLTQPFALYLGLNLPH-----PYPSPSMgENFGSIRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGE- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 350 idgpLPLNGAQKgYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKDlkLDGVSLLPWLQDKK 429
Cdd:cd16171 236 ----LAMEHRQF-YKMSMYEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESS 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749623 430 QGE-----PHKNltWITSYSHWFDEENIPF--WDNYHKFVRHqSDDYPHNPNTEDLS 479
Cdd:cd16171 309 IKEspsrvPHPD--WVLSEFHGCNVNASTYmlRTNSWKYIAY-ADGNSVPPQLFDLS 362
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
58-406 |
1.48e-19 |
|
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: 87.86 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 58 PNIIVLTMDDLGYGQLPfdkgsfdpktmENREVVDTykigidkaieaaqksTPTLLSLMDEGVRF-TNGYVAHGVSGPSR 136
Cdd:cd00016 1 KHVVLIVLDGLGADDLG-----------KAGNPAPT---------------TPNLKRLASEGATFnFRSVSPPTSSAPNH 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 137 AAIMTGRAPARFGVYSNTDAQDGIP-------LTETFLPELFQNHGYYTAAVGkwhlskisnvpvpedkqTRDYHDNFTt 209
Cdd:cd00016 55 AALLTGAYPTLHGYTGNGSADPELPsraagkdEDGPTIPELLKQAGYRTGVIG-----------------LLKAIDETS- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 210 fsaeewqpqnrgfdyfmgfhaagtayynspslfknrervpakgyisdqltdeaigvvdraktLDQPFMLYLAYNAPHLPN 289
Cdd:cd00016 117 --------------------------------------------------------------KEKPFVLFLHFDGPDGPG 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 290 DNPAPEQYqkqfntgsqtadNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAvIDGPLPlNGAQKGYKSQTYP 369
Cdd:cd00016 135 HAYGPNTP------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG-IDKGHG-GDPKADGKADKSH 200
|
330 340 350
....*....|....*....|....*....|....*..
gi 1134749623 370 GGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAA 406
Cdd:cd00016 201 TGMRVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
223-425 |
4.57e-19 |
|
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: 90.73 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 223 DYFMGFHAAGTayYNSP----SLFKN----RERVPAKGYISD-QLTDEAIGVVDRaKTLDQPFMLYLAYNAPH---LPND 290
Cdd:COG3083 324 GYQFGLFSSAG--FNSPlfrqTIFSDvslpRLHTPGGPAQRDrQITAQWLQWLDQ-RDSDRPWFSYLFLDAPHaysFPAD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 291 NPAPEQYQKQFNTGSQTAD--------NYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGavidgpLPLNGAQK- 361
Cdd:COG3083 401 YPKPFQPSEDCNYLALDNEsdptpfknRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHG------EEFNENGQn 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749623 362 --GYKSQTYPGGTHTPMFMWWKGKlQPGNYDKLISAMDFYPTAL--------DAADISIPKDLkLDGVSLLPWL 425
Cdd:COG3083 475 ywGHNSNFSRYQLQVPLVIHWPGT-PPQVISKLTSHLDIVPTLMqrllgvqnPASDYSQGEDL-FDPQRRRDWV 546
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
109-533 |
1.63e-15 |
|
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: 78.82 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 109 TPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTDAQDgiPLTETFLPELfQNHGYYTAAVGKWHLSK 188
Cdd:cd16150 26 TPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLR--PDEPNLLKTL-KDAGYHVAWAGKNDDLP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 189 isnvpvpedkqtrdyhDNFTTFSAEEWqpqnrgfdyfmgfhaagtayynspslfknrervpakgyisdqltDEAigVVDR 268
Cdd:cd16150 103 ----------------GEFAAEAYCDS--------------------------------------------DEA--CVRT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 269 A------KTLDQPFMLYLAYNAPHLPNDNPAP---------------------------EQYQKQfNTGSQTAD------ 309
Cdd:cd16150 121 AidwlrnRRPDKPFCLYLPLIFPHPPYGVEEPwfsmidreklpprrppglrakgkpsmlEGIEKQ-GLDRWSEErwrelr 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 310 -NYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGaviD--GPLPLngAQKgyksqtYPGG-----THTPMFMWWK 381
Cdd:cd16150 200 aTYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHG---DytGDYGL--VEK------WPNTfedclTRVPLIIKPP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 382 GKLQPGNYDKLISAMDFYPTALDAADisIPKDLKLDGVSLLPWLQDkkQGEPHKNltwiTSYSH-WFDEENIPFWDNYHk 460
Cdd:cd16150 269 GGPAGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAG--ETEEHRD----AVFSEgGRLHGEEQAMEGGH- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 461 fvrhqsddYPHNPNTEDLSQFSYT--------VRNNDYSLVY-TVENNQlgLYKL-TDLQQKDNLAAAnpqvvKEMQGVV 530
Cdd:cd16150 340 --------GPYDLKWPRLLQQEEPpehtkavmIRTRRYKYVYrLYEPDE--LYDLeADPLELHNLIGD-----PAYAEII 404
|
...
gi 1134749623 531 REF 533
Cdd:cd16150 405 AEM 407
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
96-357 |
2.31e-10 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 62.46 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 96 IGID----KAIEAAQksTPTLLSLMDEGVRFTNGY-VAHGVSGPSRAAIMTGRAPARFGVYSNTdaqdgiplteTFLPEL 170
Cdd:COG1524 29 ILVDglraDLLERAH--APNLAALAARGVYARPLTsVFPSTTAPAHTTLLTGLYPGEHGIVGNG----------WYDPEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 171 FQNHGYYTAAVGKWHLSkiSNVPVPedkqtrdyhdnfTTFsaEEWQPQNRGFDYFMGFHAAGTAYYNSPSLFKNRERVPA 250
Cdd:COG1524 97 GRVVNSLSWVEDGFGSN--SLLPVP------------TIF--ERARAAGLTTAAVFWPSFEGSGLIDAARPYPYDGRKPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 251 KGYISdqlTDEAIgvVDRAKTL---DQPFMLYLaynapHLPNdnpaPEQYQKQFNTGSqtaDNYYASVYSVDQGVKRILE 327
Cdd:COG1524 161 LGNPA---ADRWI--AAAALELlreGRPDLLLV-----YLPD----LDYAGHRYGPDS---PEYRAALREVDAALGRLLD 223
|
250 260 270
....*....|....*....|....*....|.
gi 1134749623 328 QLKKNGQYDNTIILFTSDNGAV-IDGPLPLN 357
Cdd:COG1524 224 ALKARGLYEGTLVIVTADHGMVdVPPDIDLN 254
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
107-349 |
9.17e-07 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 51.27 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 107 KSTPTLLSLMDEGVRFTN---GYVAhgVSGPSRAAIMTGRAPARFGVYSNTDaqdgipltetFLPELFQNHGYYTAAVGK 183
Cdd:pfam01663 18 ELTPNLAALAKEGVSAPNltpVFPT--LTFPNHYTLVTGLYPGSHGIVGNTF----------YDPKTGEYLVFVISDPED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 184 WHLskISNVPVPEDKQtrdyHDNFTTFSAeewqpqnrgfdYFMGFHAAGTAYYNSPSLFKNRERVPAKGY---ISDQLTD 260
Cdd:pfam01663 86 PRW--WQGEPIWDTAA----KAGVRAAAL-----------FWPGSEVDYSTYYGTPPRYLKDDYNNSVPFedrVDTAVLQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 261 EAIGVVDRAKTLDQPFMLYLAYnaphlpndnPAPEQYQKQFNTGSQTADNYYAsvySVDQGVKRILEQLKKNGQYDNTII 340
Cdd:pfam01663 149 TWLDLPFADVAAERPDLLLVYL---------EEPDYAGHRYGPDSPEVEDALR---RVDRAIGDLLEALDERGLFEDTNV 216
|
....*....
gi 1134749623 341 LFTSDNGAV 349
Cdd:pfam01663 217 IVVSDHGMT 225
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
303-409 |
3.76e-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: 45.69 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 303 TGSQTADNYYASVYSVDQGVKRILEQLKKNGQydNTIILFTSDNG-AVIDGPLPLNGAQKGYKSQtypggTHTPMFMW-- 379
Cdd:cd16017 180 SKEELINAYDNSILYTDYVLSQIIERLKKKDK--DAALIYFSDHGeSLGENGLYLHGAPYAPKEQ-----YHVPFIIWss 252
|
90 100 110
....*....|....*....|....*....|....*.
gi 1134749623 380 ------WKGKLQPGNYDKLISAMDFYPTALDAADIS 409
Cdd:cd16017 253 dsykqrYPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
107-347 |
3.54e-04 |
|
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: 42.57 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 107 KSTPTLLSLMDEGVRF---TNGYVAhgVSGPSRAAIMTGRAPARFGVYSNT--DAQDGIPLT-------------ETFLp 168
Cdd:cd16018 20 GLTPNLKRLAEEGVRAkyvKPVFPT--LTFPNHYSIVTGLYPESHGIVGNYfyDPKTNEEFSdsdwvwdpwwiggEPIW- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 169 ELFQNHGYYTAAVGkWhlskisnvPVPEdkqtRDYHDNFTTFSAEEWQPQNrgfdyfmgfhaagtayynspslfknrerv 248
Cdd:cd16018 97 VTAEKAGLKTASYF-W--------PGSE----VAIIGYNPTPIPLGGYWQP----------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749623 249 pakgYISDQLTDEAIGVVDRAKTLDQPFMLYLaynapHLPNdnpaPEQYQKQFNTGSQTADnyyASVYSVDQGVKRILEQ 328
Cdd:cd16018 135 ----YNDSFPFEERVDTILEWLDLERPDLILL-----YFEE----PDSAGHKYGPDSPEVN---EALKRVDRRLGYLIEA 198
|
250
....*....|....*....
gi 1134749623 329 LKKNGQYDNTIILFTSDNG 347
Cdd:cd16018 199 LKERGLLDDTNIIVVSDHG 217
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
115-153 |
4.16e-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: 39.82 E-value: 4.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1134749623 115 LMDEGVRFTNGYVAHG--VSGPSRAAIMTGRAPARFGVYSN 153
Cdd:cd16016 33 LLNEGFVFENAHYNYAptDTAPGHATIYTGTTPAIHGIIGN 73
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