|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
87-537 |
0e+00 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 624.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDLDVSIGGMIPLVKTKKLIGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSSTAWQK 166
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 167 TQEPDSFPAFLQKHGtYQTFFAGKYLNEYGSKkaGGVEHVPPGWDHWFALERNSKYYNYTLSvNGRAQRHGQNYSEDYLT 246
Cdd:cd16147 81 GLERSTLPVWLQEAG-YRTAYAGKYLNGYGVP--GGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 247 DVLANISIDFLEN-KSNRRPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPRDPNFN--IHGKDKHWLIRQAKTPMTnsSV 323
Cdd:cd16147 157 DVIANKALDFLRRaAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPPPNnpDVSDKPHWLRRLPPLNPT--QI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 324 EFLDNAYRKRWRTLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLPMDKRQLYEFDIRVPLLVRGPDIKPN 403
Cdd:cd16147 235 AYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 404 QTSSLLVANVDLGPTILDIAGYNVNETkMDGMSflpimigkgnsstwrsdvlveyegegsnisdpacpllgpgvsecfpd 483
Cdd:cd16147 315 VTVDQLVSNIDLAPTILDLAGAPPPSD-MDGRS----------------------------------------------- 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1515217839 484 cvCEDSYNNTYACVRTVSQAANLQYCEFDDNevFVEVYNLTADPFQLSNIAKSI 537
Cdd:cd16147 347 --CGDSNNNTYKCVRTVDDTYNLLYFEWCTG--FRELYDLTTDPYQLTNLAGDL 396
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
87-552 |
3.68e-102 |
|
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: 316.01 E-value: 3.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL--DvSIGGM-IPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNtlEGNcSS 161
Cdd:cd16031 2 RPNIIFILTDDHryD-ALGCYgNPIVKTPNIdrLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDN--NGP-LF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TAWQKTqepdsFPAFLQKHGtYQTFFAGKY-LNEYGskkaggvEHVPPGWDHWFALERNSKYYNYTLSVNG-RAQRHGqn 239
Cdd:cd16031 78 DASQPT-----YPKLLRKAG-YQTAFIGKWhLGSGG-------DLPPPGFDYWVSFPGQGSYYDPEFIENGkRVGQKG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 240 ysedYLTDVLANISIDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPRDPNFNI---HGKDKhWLiRQAKt 316
Cdd:cd16031 143 ----YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDDddyAGRPE-WA-REQR- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 317 pmtNSSVEFLDNAYRKRW----------RTLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLpMDKRQLYE 386
Cdd:cd16031 216 ---NRIRGVLDGRFDTPEkyqrymkdylRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGL-FDKRLMYE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 387 FDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNVNEtKMDGMSFLPIMIGKgNSSTWRSDVLVEYEGEGsni 465
Cdd:cd16031 292 ESIRVPLIIRDPRlIKAGTVVDALVLNIDFAPTILDLAGVPIPE-DMQGRSLLPLLEGE-KPVDWRKEFYYEYYEEP--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 466 sdpacpllgpgvsecfpdcvcedSYNNTYAC--VRTvSQAANLQYCEFDDNEvfvEVYNLTADPFQLSNIAKSID-QEVL 542
Cdd:cd16031 367 -----------------------NFHNVPTHegVRT-ERYKYIYYYGVWDEE---ELYDLKKDPLELNNLANDPEyAEVL 419
|
490
....*....|
gi 1515217839 543 EKMNHRLMML 552
Cdd:cd16031 420 KELRKRLEEL 429
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
66-549 |
8.30e-93 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 290.63 E-value: 8.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 66 HFILICVTLHCNNLAEAKTNvRPNIVLILTDDL---DVSIGGMiPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASIL 140
Cdd:COG3119 3 RLLLLLLALLAAAAAAAAAK-RPNILFILADDLgygDLGCYGN-PLIKTPNIdrLAAEGVRFTNAYVTSPVCSPSRASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 141 TGKYPHNHHVVNNTLEGNCSSTAWQKTqepdsFPAFLQKHGtYQTFFAGKYlneygskkaggveHVppgwdhwfalerns 220
Cdd:COG3119 81 TGRYPHRTGVTDNGEGYNGGLPPDEPT-----LAELLKEAG-YRTALFGKW-------------HL-------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 221 kyynytlsvngraqrhgqnysedYLTDVLANISIDFLENKSNR-RPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPRDPN 299
Cdd:COG3119 128 -----------------------YLTDLLTDKAIDFLERQADKdKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 300 FNIHGKDKhwlirqaktpmtnssvEFLDNAYRKRWRTLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLPM 379
Cdd:COG3119 185 LAPRDLTE----------------EELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 380 DKRQLYEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNVNEtKMDGMSFLPIMigKGNSSTWRSDVLVEY 458
Cdd:COG3119 249 GKGTLYEGGIRVPLIVRWPGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPLL--TGEKAEWRDYLYWEY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 459 EGEGSNisdpacpllgpgvsecfpdcvcedsynntyACVRTvsqaANLQYCEFDDNEVFVEVYNLTADPFQLSNIAKSiD 538
Cdd:COG3119 326 PRGGGN------------------------------RAIRT----GRWKLIRYYDDDGPWELYDLKNDPGETNNLAAD-Y 370
|
490
....*....|.
gi 1515217839 539 QEVLEKMNHRL 549
Cdd:COG3119 371 PEVVAELRALL 381
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
88-549 |
1.21e-64 |
|
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: 216.22 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDLDVSIGG-MIPLVKTKKLigDA----GITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTlegncsST 162
Cdd:cd16027 1 PNILWIIADDLSPDLGGyGGNVVKTPNL--DRlaaeGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR------SR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 163 AWQKTQEPDSFPAFLQKHGtYQTFFAGKYlneygskkaggveHVPPGWDHWFalernskyynytlsvngRAQRHGQNYSE 242
Cdd:cd16027 73 GFPLPDGVKTLPELLREAG-YYTGLIGKT-------------HYNPDAVFPF-----------------DDEMRGPDDGG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 243 DYLTDVLANISiDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPRDPNFnihgkdkhwlirqAKTPMTNSS 322
Cdd:cd16027 122 RNAWDYASNAA-DFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYL-------------PDTPEVRED 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 323 V-EFLDNAYRkrwrtllsVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYhtgqfSLPMDKRQLYEFDIRVPLLVRGPD-I 400
Cdd:cd16027 188 LaDYYDEIER--------LDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkI 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 401 KPNQTSSLLVANVDLGPTILDIAGYNVNEtKMDGMSFLPIMigKGNSSTWRSDVLVEYEGEGsnisdpacpllgpgvsec 480
Cdd:cd16027 255 KPGSVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLL--KGEKDPGRDYVFAERDRHD------------------ 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1515217839 481 fpdcvcedsynNTYACVRTVSqaanlqycefDD------NEVFVEVYNLTADPFQLSNIAKSID-QEVLEKMNHRL 549
Cdd:cd16027 314 -----------ETYDPIRSVR----------TGrykyirNYMPEELYDLKNDPDELNNLADDPEyAEVLEELRAAL 368
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
88-456 |
8.50e-63 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 212.79 E-value: 8.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSIGGMiPLVKTKKLigDA----GITFTNTFVASPLCCPSRASILTGKYPHNHHVVN------NT 154
Cdd:cd16144 1 PNIVLILVDDLgwaDLGCYGS-KFYETPNI--DRlakeGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipgrrGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 155 LEGNCSSTAWQKTQEPDSFPAF---LQKHGtYQTFFAGKYlNEYGSKKAGGVEHvppGWDHWFALERNSKYYNYTLSVNG 231
Cdd:cd16144 78 PDNTKLIPPPSTTRLPLEEVTIaeaLKDAG-YATAHFGKW-HLGGEGGYGPEDQ---GFDVNIGGTGNGGPPSYYFPPGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 232 RAQRHGQNYSEDYLTDVLANISIDFLEnKSNRRPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPrdpnfnihGKDKHWLI 311
Cdd:cd16144 153 PNPDLEDGPEGEYLTDRLTDEAIDFIE-QNKDKPFFLYLSHYAVHTPIQARPELIEKYEKKKKG--------LRKGQKNP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 312 RQAktpmtnSSVEfldnayrkrwrtllSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLPMD-------KRQL 384
Cdd:cd16144 224 VYA------AMIE--------------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSnaplrggKGSL 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1515217839 385 YEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNVNETK-MDGMSFLPIMigKGNSSTWRSDVLV 456
Cdd:cd16144 284 YEGGIRVPLIVRWPGvIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQhLDGVSLVPLL--KGGEADLPRRALF 355
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
88-436 |
5.02e-62 |
|
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: 204.59 E-value: 5.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSIGGMiPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST 162
Cdd:cd16022 1 PNILLIMTDDLgydDLGCYGN-PDIKTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 163 awqktqEPDSFPAFLQKHGtYQTFFAGKylneygskkaggvehvppgwdhWfalernskyynytlsvngraqrHGQnyse 242
Cdd:cd16022 80 ------DEPTLAELLKEAG-YRTALIGK----------------------W----------------------HDE---- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 243 dyltdvlaniSIDFLENKSNRRPFFMMVSTPAPHSPWtaapqyessfsnvkaprdpnfnihgkdkhwlirqaktpmtnss 322
Cdd:cd16022 105 ----------AIDFIERRDKDKPFFLYVSFNAPHPPF------------------------------------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 323 vefldnAYrkrWRTLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLPMDKRQLYEFDIRVPLLVRGPD-IK 401
Cdd:cd16022 132 ------AY---YAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGkIP 202
|
330 340 350
....*....|....*....|....*....|....*
gi 1515217839 402 PNQTSSLLVANVDLGPTILDIAGYNVNETkMDGMS 436
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPPEG-LDGRS 236
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
88-425 |
7.56e-62 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 206.50 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSI-GGMIPLVKTKKLIGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLegncssta 163
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLyGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 164 WQKTQEPDSFPAFLQKHGtYQTFFAGKYLNEYGSKKAGGVEhvppGWDHWFALERNSKYYNYtlsvngRAQRHGQNYSED 243
Cdd:pfam00884 73 VGLPRTEPSLPDLLKRAG-YNTGAIGKWHLGWYNNQSPCNL----GFDKFFGRNTGSDLYAD------PPDVPYNCSGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 244 YLTDVLANISIDFLENKSnrRPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPRDpnfnihgkdkhwlirqaktpmtnssv 323
Cdd:pfam00884 142 VSDEALLDEALEFLDNND--KPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSC-------------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 324 eFLDNAYRKRWRTLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQF---SLPMDKRQLYEFDIRVPLLVRGPD- 399
Cdd:pfam00884 194 -SEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGggyLHGGKYDNAPEGGYRVPLLIWSPGg 272
|
330 340
....*....|....*....|....*.
gi 1515217839 400 IKPNQTSSLLVANVDLGPTILDIAGY 425
Cdd:pfam00884 273 KAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
87-533 |
1.28e-61 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 208.96 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL---DVSIGGMIPlVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVnntleGNCSS 161
Cdd:cd16034 1 KPNILFIFADQHraqALGCAGDDP-VKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-----GNDVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TawqKTQEPdSFPAFLQKHGtYQTFFAGKY-LNEYGSKKAGGVEHVPP-----GWDHWFALERNSKYYNYTLSVNGRAQR 235
Cdd:cd16034 75 L---PPDAP-TIADVLKDAG-YRTGYIGKWhLDGPERNDGRADDYTPPperrhGFDYWKGYECNHDHNNPHYYDDDGKRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 236 HGQNYSEDYLTDVLanisIDFLEN-KSNRRPFFMMVSTPAPHSPWTAAPQ-YESSFSNVKAPRDPNFNIHGKDKHWLIRQ 313
Cdd:cd16034 150 YIKGYSPDAETDLA----IEYLENqADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLLRPNVPEDKKEEAGLRED 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 314 AKTPMtnSSVEfldnayrkrwrtllSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLpMDKRQLYEFDIRVPL 393
Cdd:cd16034 226 LRGYY--AMIT--------------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGL-MNKQVPYEESIRVPF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 394 LVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNVNETkMDGMSFLPIMIGKGNSST-WRSDVLVEYEGEGSNISDPacp 471
Cdd:cd16034 289 IIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT-VEGRDLSPLLLGGKDDEPdSVLLQCFVPFGGGSARDGG--- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515217839 472 llgpgvsecfpdcvcedsynnTYACVRTVsqaanlQY---CEFDDNEVFvevYNLTADPFQLSNI 533
Cdd:cd16034 365 ---------------------EWRGVRTD------RYtyvRDKNGPWLL---FDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-549 |
7.45e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 196.67 E-value: 7.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTD----DLdVSIGGMiPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSS 161
Cdd:cd16033 1 PNILFIMTDqqryDT-LGCYGN-PIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TAWQKTQEpdSFPAFLQKHGtYQTFFAGKYlneygskkaggveHVPP-------GWDHWFALERNSKYYnytlsvngraq 234
Cdd:cd16033 79 RGLPPGVE--TFSEDLREAG-YRNGYVGKW-------------HVGPeetpldyGFDEYLPVETTIEYF----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 235 rhgqnysedyltdvLANISIDFLEN-KSNRRPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPRDPNFNIHGKDKHWLIRQ 313
Cdd:cd16033 132 --------------LADRAIEMLEElAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYRR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 314 AKTPMTnssvefLDNAYRKRWRTLLS--------VDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLpMDKRQ-L 384
Cdd:cd16033 198 ERKRWG------VDTEDEEDWKEIIAhywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRL-WDKGPfM 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 385 YEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNVNEtKMDGMSFLPIMIGKGNSStWRSDVLVEYEGEGS 463
Cdd:cd16033 271 YEETYRIPLIIKWPGvIAAGQVVDEFVSLLDLAPTILDLAGVDVPP-KVDGRSLLPLLRGEQPED-WRDEVVTEYNGHEF 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 464 nisdpacpllgpgvsecfpdcvcedsynntYACVRTVsqaanlqyceFDDNEVFV-------EVYNLTADPFQLSN-IAK 535
Cdd:cd16033 349 ------------------------------YLPQRMV----------RTDRYKYVfngfdidELYDLESDPYELNNlIDD 388
|
490
....*....|....
gi 1515217839 536 SIDQEVLEKMNHRL 549
Cdd:cd16033 389 PEYEEILREMRTRL 402
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
88-545 |
3.87e-52 |
|
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: 183.91 E-value: 3.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSIGGMiPLVKTKKL--IGDAGITFTNtFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNcsst 162
Cdd:cd16146 1 PNVILILTDDQgygDLGFHGN-PILKTPNLdrLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWHTILGRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 163 awqkTQEPD--SFPAFLQKHGtYQTFFAGKY--------------LNEYGSKKAGGVEHVPPGWdhwfalerNSKYYNYT 226
Cdd:cd16146 75 ----RMRLDetTLAEVFKDAG-YRTGIFGKWhlgdnypyrpqdrgFDEVLGHGGGGIGQYPDYW--------GNDYFDDT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 227 LSVNGRAQRHgqnysEDYLTDVLANISIDFLENKSNRrPFFMMVSTPAPHSPWTAAPQYESSFSNvKAPRDPNFNIHGKd 306
Cdd:cd16146 142 YYHNGKFVKT-----EGYCTDVFFDEAIDFIEENKDK-PFFAYLATNAPHGPLQVPDKYLDPYKD-MGLDDKLAAFYGM- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 307 khwlirqaktpMTNssvefldnayrkrwrtllsVDDLVEKVVKKLEVRGELSNTYIIFTSDNG---YHTGQFSLPM--DK 381
Cdd:cd16146 214 -----------IEN-------------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGpagGVPKRFNAGMrgKK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 382 RQLYEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNVNET-KMDGMSFLPIMigKGNSSTWRSDVLVEYE 459
Cdd:cd16146 264 GSVYEGGHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGiKLDGRSLLPLL--KGESDPWPERTLFTHS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 460 GEGSNisdpacpllgpgvsecfpdcvcEDSYNNTYAcVRtvsqaaNLQYCEFDDNEVFVEVYNLTADPFQLSNIAKSIdQ 539
Cdd:cd16146 342 GRWPP----------------------PPKKKRNAA-VR------TGRWRLVSPKGFQPELYDIENDPGEENDVADEH-P 391
|
....*.
gi 1515217839 540 EVLEKM 545
Cdd:cd16146 392 EVVKRL 397
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
87-535 |
1.49e-50 |
|
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: 180.46 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDLDVSIGGMI-PLVKTKKLigDA----GITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNtlegncsS 161
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYGgHPAKTPNI--DRlaarGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDN-------N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TAWQKTQePD--SFPAFLQKHGtYQTFFAGKYLNEYGSKKaggvEHVPPGWDHWFALERNSKYYNYTLSVNGRAQRHGQN 239
Cdd:cd16030 73 SYFRKVA-PDavTLPQYFKENG-YTTAGVGKIFHPGIPDG----DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 240 YS---------EDYLTDVLANISIDFLENKSNR-RPFFMMVSTPAPHSPWTaAPQ-----YESSFSNVKAPRDPNF--NI 302
Cdd:cd16030 147 GPaweaadvpdEAYPDGKVADEAIEQLRKLKDSdKPFFLAVGFYKPHLPFV-APKkyfdlYPLESIPLPNPFDPIDlpEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 303 HGKDKHWLIRQAKTPMTNSSVEF--LDNAYrkrWRTLLS--------VDDLVEKVVKKLEVRGELSNTYIIFTSDNGYH- 371
Cdd:cd16030 226 AWNDLDDLPKYGDIPALNPGDPKgpLPDEQ---ARELRQayyasvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGWHl 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 372 --TGQFSlpmdKRQLYEFDIRVPLLVRGPDI-KPNQTSSLLVANVDLGPTILDIAGYNVNEtKMDGMSFLPIMigKGNSS 448
Cdd:cd16030 303 geHGHWG----KHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPP-CLEGKSLVPLL--KNPSA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 449 TWRSDVLVEYegegsnisdPACPLLGpgvsecfpdcvcedsynntYAcVRTvsqaANLQYCEF--DDNEVFVEVYNLTAD 526
Cdd:cd16030 376 KWKDAAFSQY---------PRPSIMG-------------------YS-IRT----ERYRYTEWvdFDKVGAEELYDHKND 422
|
....*....
gi 1515217839 527 PFQLSNIAK 535
Cdd:cd16030 423 PNEWKNLAN 431
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
88-445 |
2.17e-48 |
|
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: 173.93 E-value: 2.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSIGGMiPLVKTKKLigDA----GITFTNTFVASPLCCPSRASILTGKyphnhHVVNNTLEGNcS 160
Cdd:cd16145 1 PNIIFILADDLgygDLGCYGQ-KKIKTPNL--DRlaaeGMRFTQHYAGAPVCAPSRASLLTGL-----HTGHTRVRGN-S 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 161 STAWQKTQEPDS--FPAFLQKHGtYQTFFAGKY-LNEYGSkkAGGVEhvPPGWDHWFA--------------LERNSKY- 222
Cdd:cd16145 72 EPGGQDPLPPDDvtLAEVLKKAG-YATAAFGKWgLGGPGT--PGHPT--KQGFDYFYGyldqvhahnyypeyLWRNGEKv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 223 -YNYTLSVNGRAQRHGQNYSEDYLTDVLANISIDFL-ENKSnrRPFFMMVSTPAPHSPWtAAPQyessfsnvkapRDPNF 300
Cdd:cd16145 147 pLPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIrENKD--KPFFLYLAYTLPHAPL-QVPD-----------DGPYK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 301 NihgKDKHWLIRqAKTPMTNSsvefldnayRKRWRTLLS-VDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHT-GQFSLP 378
Cdd:cd16145 213 Y---KPKDPGIY-AYLPWPQP---------EKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeGGSEHD 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515217839 379 MD-----------KRQLYEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNVnETKMDGMSFLPIMIGKG 445
Cdd:cd16145 280 PDffdsngplrgyKRSLYEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEP-PEDIDGISLLPTLLGKP 357
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-452 |
7.85e-48 |
|
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: 171.24 E-value: 7.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDLDV----SIGGMIplVKTKKL--IGDAGITFTNTFvASPLCCPSRASILTGKYPHNHHVVNNTLEGNcss 161
Cdd:cd16151 1 PNIILIMADDLGYecigCYGGES--YKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 tawQKTqepdsFPAFLQKHGtYQTFFAGKY-LNEYGSKKAGGVEHvppGWDHWFA---LERNSKYYNYTLSVNGRAQRHG 237
Cdd:cd16151 75 ---QKT-----FGHLLKDAG-YATAIAGKWqLGGGRGDGDYPHEF---GFDEYCLwqlTETGEKYSRPATPTFNIRNGKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 238 QNYSE-DYLTDVLANISIDFLENKSNrRPFFMMVSTPAPHSPWTAAPQyessfSNVKAPRDPNFNihGKDKHwlirqakt 316
Cdd:cd16151 143 LETTEgDYGPDLFADFLIDFIERNKD-QPFFAYYPMVLVHDPFVPTPD-----SPDWDPDDKRKK--DDPEY-------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 317 pmtnssveFLD-NAYrkrwrtllsVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLPMD------KRQLYEFDI 389
Cdd:cd16151 207 --------FPDmVAY---------MDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTNGrevrggKGKTTDAGT 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515217839 390 RVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNV-NETKMDGMSFLPIMIGKGNSSTWRS 452
Cdd:cd16151 270 HVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLpEDYPLDGRSFAPQLLGKTGSPRREW 334
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-464 |
1.32e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 161.17 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDLDVSIGGMI--PLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNtlegncsSTA 163
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYghPVVRTPNLdrLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDN-------ADP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 164 WQKTqePDSFPAFLQKHGtYQTFFAGKylneygskkaggvehvppgwdhwfalernskyynytLSVNGRAQRHGQNYSED 243
Cdd:cd16037 74 YDGD--VPSWGHALRAAG-YETVLIGK------------------------------------LHFRGEDQRHGFRYDRD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 244 yltdvLANISIDFL-ENKSNRRPFFMMVSTPAPHSPWTAaPQyessfsnvkaprdpnfnihgkdkhwlirqaktpmtnss 322
Cdd:cd16037 115 -----VTEAAVDWLrEEAADDKPWFLFVGFVAPHFPLIA-PQ-------------------------------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 323 vEFLDnAYRKRWRT----LLS-VDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLpMDKRQLYEFDIRVPLLVRG 397
Cdd:cd16037 151 -EFYD-LYVRRARAayygLVEfLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGL-WGKSTMYEESVRVPMIISG 227
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1515217839 398 PDIKPNQTSSLLVANVDLGPTILDIAGYNVNETkMDGMSFLPIMIGKGNsstWRSDVLVEYEGEGSN 464
Cdd:cd16037 228 PGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPD-LDGRSLLPLAEGPDD---PDRVVFSEYHAHGSP 290
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
88-448 |
2.93e-44 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 161.99 E-value: 2.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSIGGMIPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST 162
Cdd:cd16143 1 PNIVIILADDLgygDISCYNPDSKIPTPNIdrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 163 AwqktqEPD--SFPAFLQKHGtYQTFFAGKY---LNEYGSKKAGGVEHVPP---------------GWDHWFALeRNSKy 222
Cdd:cd16143 81 I-----EPDrvTLAKMLKQAG-YRTAMVGKWhlgLDWKKKDGKKAATGTGKdvdyskpikggpldhGFDYYFGI-PASE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 223 ynytlsvngraqrhgqnysedyLTDVLANISIDFL-ENKSNRRPFFMMVSTPAPHSPWTAAPQYessfsNVKAprdpNFN 301
Cdd:cd16143 153 ----------------------VLPTLTDKAVEFIdQHAKKDKPFFLYFALPAPHTPIVPSPEF-----QGKS----GAG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 302 IHGkDkhwLIRQaktpmtnssvefldnayrkrwrtllsVDDLVEKVVKKLEVRGELSNTYIIFTSDNG---YHTGQFSLP 378
Cdd:cd16143 202 PYG-D---FVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEK 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 379 MD----------KRQLYEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNV-NETKMDGMSFLPIMIGKGN 446
Cdd:cd16143 252 FGhdpsgplrgmKADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLpDNAAEDSFSFLPALLGPKK 331
|
..
gi 1515217839 447 SS 448
Cdd:cd16143 332 QE 333
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
87-460 |
1.10e-43 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 160.04 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL---DVSIGGMiPLVKTKKLigDA----GITFTNTFVA---SP-LCCPSRASILTGKYphnhhVVNNTL 155
Cdd:cd16155 2 KPNILFILADDQradTIGALGN-PEIQTPNL--DRlarrGTSFTNAYNMggwSGaVCVPSRAMLMTGRT-----LFHAPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 156 EGNCSSTAWQKTqepdsFPAFLQKHGtYQTFFAGKYLNEYgskkaggvehvppgwdhwfalernskyynytlsvngraqr 235
Cdd:cd16155 74 GGKAAIPSDDKT-----WPETFKKAG-YRTFATGKWHNGF---------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 236 hgqnysedyltdvlANISIDFLENKSNR-RPFFMMVSTPAPHSPWTAAPQYES--SFSNVKAPrdPNF-NIHGKDKHWL- 310
Cdd:cd16155 108 --------------ADAAIEFLEEYKDGdKPFFMYVAFTAPHDPRQAPPEYLDmyPPETIPLP--ENFlPQHPFDNGEGt 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 311 IRQ---AKTPMTNSSV-EFLDNAYRkrwrtLLS-VDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLpMDKRQLY 385
Cdd:cd16155 172 VRDeqlAPFPRTPEAVrQHLAEYYA-----MIThLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGL-MGKQNLY 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515217839 386 EFDIRVPLLVRGPDIKPNQTSSLLVANVDLGPTILDIAGYNVNETkMDGMSFLPIMigKGNSSTWRSDVLVEYEG 460
Cdd:cd16155 246 EHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPES-VEGKSLLPVI--RGEKKAVRDTLYGAYRD 317
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-555 |
7.36e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 150.46 E-value: 7.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDLDV-SIGGM-IPLVKTKKLigDA----GITFTNTFVASPLCCPSRASILTGKYPHnhhvVNntleGNCSS 161
Cdd:cd16150 1 PNIVIFVADQLRAdSLGHLgNPAAVTPNL--DAlaaeGVRFSNAYCQNPVCSPSRCSFLTGWYPH----VN----GHRTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TAWQKTQEPDSFPAfLQKHGtYQTFFAGKylneygskkaggvEHVPPGWDHWFALErnskyynytlsvngraqrhgqnyS 241
Cdd:cd16150 71 HHLLRPDEPNLLKT-LKDAG-YHVAWAGK-------------NDDLPGEFAAEAYC-----------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 242 EDYLTdvlANISIDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFSNVKAP-RDPNFNIHGKDKHWLIRqaktpMTN 320
Cdd:cd16150 113 SDEAC---VRTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPpRRPPGLRAKGKPSMLEG-----IEK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 321 SSVEFLDNAyrkRWRTLLSV--------DDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLpMDKRQ--LYEFDIR 390
Cdd:cd16150 185 QGLDRWSEE---RWRELRATylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGL-VEKWPntFEDCLTR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 391 VPLLVRGPDIKPNQTSSLLVANVDLGPTILDIAGYNVNETKMdGMSFLPIMigKGNSSTWRSDVLVE---YEGEGSNISD 467
Cdd:cd16150 261 VPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVL--AGETEEHRDAVFSEggrLHGEEQAMEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 468 PACP--LLGPGVSECF-PDCVCedsynntyACVRTVSQAANLQYCEFDDNevfvEVYNLTADPFQLSNIAKSID-QEVLE 543
Cdd:cd16150 338 GHGPydLKWPRLLQQEePPEHT--------KAVMIRTRRYKYVYRLYEPD----ELYDLEADPLELHNLIGDPAyAEIIA 405
|
490
....*....|....
gi 1515217839 544 KMNHRLM--MLQSC 555
Cdd:cd16150 406 EMKQRLLrwMVETS 419
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
87-448 |
2.35e-38 |
|
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: 145.78 E-value: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL---DVSIGGMiPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPH---NHHVVnntlegn 158
Cdd:cd16026 1 KPNIVVILADDLgygDLGCYGS-PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVrvgLPGVV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 159 csSTAWQKTQEPDS---FPAFLQKHGtYQTFFAGKY-LneyGSKKaggvEHVPP--GWDHWFAL--------ERNSKYYN 224
Cdd:cd16026 73 --GPPGSKGGLPPDeitIAEVLKKAG-YRTALVGKWhL---GHQP----EFLPTrhGFDEYFGIpysndmwpFPLYRNDP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 225 YTLSVNGRAQR--HGQNYSEDYLTDVLANISIDFLENKSNrRPFFMMVSTPAPHSPWTAAPQYEssfsnvkaprdpnfni 302
Cdd:cd16026 143 PGPLPPLMENEevIEQPADQSSLTQRYTDEAVDFIERNKD-QPFFLYLAHTMPHVPLFASEKFK---------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 303 hGKDKHWLIRQAktpmtnssVEfldnayrkrwrtllSVDDLVEKVVKKLEVRGELSNTYIIFTSDNG-----YHTGQFSL 377
Cdd:cd16026 206 -GRSGAGLYGDV--------VE--------------ELDWSVGRILDALKELGLEENTLVIFTSDNGpwleyGGHGGSAG 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515217839 378 PMD--KRQLYEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNV-NETKMDGMSFLPIMIGKGNSS 448
Cdd:cd16026 263 PLRggKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLpEDRVIDGKDISPLLLGGSKSP 337
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-463 |
4.70e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 141.72 E-value: 4.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDLDV------SIGGMIPLVKTKKLIGDAGITFTNtFVASPLCCPSRASILTGKYPHNHHVvnNTLEGNCSS 161
Cdd:cd16154 1 PNILLIIADDQGLdssaqySLSSDLPVTPTLDSLANSGIVFDN-LWATPACSPTRATILTGKYGFRTGV--LAVPDELLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TawqktqePDSFPAFLQKHGT---YQTFFAGKYlneygsKKAGGVEHV--PPGWDHWFALERN--SKYYNYTLSVNGraq 234
Cdd:cd16154 78 S-------EETLLQLLIKDATtagYSSAVIGKW------HLGGNDNSPnnPGGIPYYAGILGGgvQDYYNWNLTNNG--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 235 rhGQNYSEDYLTDVLANISIDFLENKSNrrPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPRDpnfnihgkdkhwlIRQA 314
Cdd:cd16154 142 --QTTNSTEYATTKLTNLAIDWIDQQTK--PWFLWLAYNAPHTPFHLPPAELHSRSLLGDSAD-------------IEAN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 315 KTPMTNSSVEFLDNAYRkrwRTLLSVDDlvekvvkklevrGELSNTYIIFTSDNGyhT-GQ-----FSLPMDKRQLYEFD 388
Cdd:cd16154 205 PRPYYLAAIEAMDTEIG---RLLASIDE------------EERENTIIIFIGDNG--TpGQvvdlpYTRNHAKGSLYEGG 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1515217839 389 IRVPLLVRGPDI-KPNQTSSLLVANVDLGPTILDIAGYNVNETKmDGMSFLPIMigKGNSSTWRSDVLVEYEGEGS 463
Cdd:cd16154 268 INVPLIVSGAGVeRANERESALVNATDLYATIAELAGVDAAEIH-DSVSFKPLL--SDVNASTRQYNYTEYESPTT 340
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
87-444 |
9.53e-36 |
|
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: 138.73 E-value: 9.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL---DVSI-GGMIPlvkTKKL--IGDAGITFTNtFVASPLCCPSRASILTGkypHNHHVVNNtleGNCS 160
Cdd:cd16025 2 RPNILLILADDLgfsDLGCfGGEIP---TPNLdaLAAEGLRFTN-FHTTALCSPTRAALLTG---RNHHQVGM---GTMA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 161 STAWQK----TQEPDSFPAF---LQKHGtYQTFFAGKYlneygskkaggveHV-PPGWdhwfalernskyynytlsvngr 232
Cdd:cd16025 72 ELATGKpgyeGYLPDSAATIaevLKDAG-YHTYMSGKW-------------HLgPDDY---------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 233 aqrhgqnysedYLTDVLANISIDFL-ENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFsnvkaprdpnfniHGK-DKHW- 309
Cdd:cd16025 116 -----------YSTDDLTDKAIEYIdEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKY-------------KGKyDAGWd 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 310 ------LIRQ-------AKTPMT--NSSV---EFLDNAYRKRWRTLLSV--------DDLVEKVVKKLEVRGELSNTYII 363
Cdd:cd16025 172 alreerLERQkelglipADTKLTprPPGVpawDSLSPEEKKLEARRMEVyaamvehmDQQIGRLIDYLKELGELDNTLII 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 364 FTSDNG--YHTG--QFS---LPMDKRQLYEFDIRVPLLVRGPD--IKPNQTSSLLVANVDLGPTILDIAG-------YNV 427
Cdd:cd16025 252 FLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKgiKAKGGIRHQFAHVIDIAPTILELAGveypktvNGV 331
|
410
....*....|....*..
gi 1515217839 428 NETKMDGMSFLPIMIGK 444
Cdd:cd16025 332 PQLPLDGVSLLPTLDGA 348
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
87-550 |
1.43e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 137.36 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTD----DldvSIGGM-IPLVKTKKLIGDA--GITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNtlegNC 159
Cdd:cd16152 1 KPNVIVFFTDqqrwD---TLGCYgQPLDLTPNLDALAeeGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN----GI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 160 SSTAWQKTqepdsFPAFLQKHGtYQTFFAGKylneygskkaggvehvppgwdhWfalernskyynytlsvngraqrHGQN 239
Cdd:cd16152 74 PLPADEKT-----LAHYFRDAG-YETGYVGK----------------------W----------------------HLAG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 240 YSEDYLTDvlanISIDFLENKSNRRPFFMMVSTPAPH----SPWTAAPQ-YESSFSNVKAPRDpnfnihgkdkhwLIRQA 314
Cdd:cd16152 104 YRVDALTD----FAIDYLDNRQKDKPFFLFLSYLEPHhqndRDRYVAPEgSAERFANFWVPPD------------LAALP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 315 KTpmtnssvefldnayrkrWRTLL--------SVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYH----TGQFslpmdKR 382
Cdd:cd16152 168 GD-----------------WAEELpdylgcceRLDENVGRIRDALKELGLYDNTIIVFTSDHGCHfrtrNAEY-----KR 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 383 QLYEFDIRVPLLVRGPDIKPNQTSSLLVANVDLGPTILDIAGYNVNETkMDGMSFLPIMIGKGNssTWRSDVLVEyegeg 462
Cdd:cd16152 226 SCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEE-MQGRSLLPLVDGKVE--DWRNEVFIQ----- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 463 snisdpacpllgpgVSECFpdcvcedsynnTYACVRT-----VSQAANLQYCEFDDNEVFVE--VYNLTADPFQLSNIAK 535
Cdd:cd16152 298 --------------ISESQ-----------VGRAIRTdrwkySVAAPDKDGWKDSGSDVYVEdyLYDLEADPYELVNLIG 352
|
490
....*....|....*.
gi 1515217839 536 SID-QEVLEKMNHRLM 550
Cdd:cd16152 353 RPEyREVAAELRERLL 368
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-439 |
1.51e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 134.60 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL--D-VSIGGMiPLVKTKKLigDA----GITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEgncs 160
Cdd:cd16148 1 MNVILIVIDSLraDhLGCYGY-DRVTTPNL--DRlaaeGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 161 stawqktQEPDSFPAFLQKHGtYQT--FFAGKYLNEYgskkaggvehvpPGWDHWFalernskyynyTLSVNGRAQRHGQ 238
Cdd:cd16148 74 -------PDDPTLAEILRKAG-YYTaaVSSNPHLFGG------------PGFDRGF-----------DTFEDFRGQEGDP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 239 NYSEDYLTDVLANISIDFLENKSNRRPFFMMVSTPAPHSPWtaapQYESSfsnvkaprdpnfnihgkdkhwlIRQaktpm 318
Cdd:cd16148 123 GEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEPY----LYDAE----------------------VRY----- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 319 tnssvefldnayrkrwrtllsVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLpMDKRQ--LYEFDIRVPLLVR 396
Cdd:cd16148 172 ---------------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGL-YWGHGsnLYDEQLHVPLIIR 229
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1515217839 397 GPDIKPNQTSSLLVANVDLGPTILDIAGYNVNETkMDGMSFLP 439
Cdd:cd16148 230 WPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDY-SDGRSLLP 271
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-439 |
6.06e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 132.36 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDLDV-SIGG-MIPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST- 162
Cdd:cd16149 1 PNILFILTDDQGPwALGCyGNSEAVTPNLdrLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 163 ---AWQKTQepDSFPAFLQKHGtYQTFFAGKylneygskkaggvehvppgwdhWfalernskyynytlsvngraqrHgqn 239
Cdd:cd16149 81 kpeGYLEGQ--TTLPEVLQDAG-YRCGLSGK----------------------W----------------------H--- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 240 ysedyltdvLANISIDFLE-NKSNRRPFFMMVSTPAPHSPWtaapQYESSFSnvkaprdpnfnihgkdkhwlirqaktpm 318
Cdd:cd16149 111 ---------LGDDAADFLRrRAEAEKPFFLSVNYTAPHSPW----GYFAAVT---------------------------- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 319 tnssvefldnayrkrwrtllSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSL--------PMDkrqLYEFDIR 390
Cdd:cd16149 150 --------------------GVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIwgkgngtfPLN---MYDNSVK 206
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1515217839 391 VPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGY-NVNETKMDGMSFLP 439
Cdd:cd16149 207 VPFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVdPPADPRLPGRSFAD 257
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
88-458 |
7.89e-35 |
|
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: 137.01 E-value: 7.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL--DVSIGGMIPLVKTKKLigDA----GITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCss 161
Cdd:cd16028 1 RNVLFITADQWraDCLSCLGHPLVKTPNL--DRlaaeGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 tawqktqEPDSFPAFLQKHGtYQTFFAGKylNEYGSKKAG---------GVEHVPPGWDHWFALErnskYYnytlsvngR 232
Cdd:cd16028 77 -------RHLTLALELRKAG-YDPALFGY--TDTSPDPRGlapldprllSYELAMPGFDPVDRLD----EY--------P 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 233 AQrhgqnYSED-YLTDVLanisIDFLENKSNRrPFFMMVSTPAPHSPWTAAPQYESSF--SNVKAP-RDPNFNIHGKD-- 306
Cdd:cd16028 135 AE-----DSDTaFLTDRA----IEYLDERQDE-PWFLHLSYIRPHPPFVAPAPYHALYdpADVPPPiRAESLAAEAAQhp 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 307 --KHWLIRQAKTP--MTNSSVEFLDNAYRKRWRT----LLS-VDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSL 377
Cdd:cd16028 205 llAAFLERIESLSfsPGAANAADLDDEEVAQMRAtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 378 pMDKRQLYEFDIRVPLLVRGP----DIKPNQTSSLLVANVDLGPTILDIAGYNVNEtKMDGMSFLPIMIGkGNSSTWRSD 453
Cdd:cd16028 285 -WGKDGFFDQAYRVPLIVRDPrreaDATRGQVVDAFTESVDVMPTILDWLGGEIPH-QCDGRSLLPLLAG-AQPSDWRDA 361
|
....*
gi 1515217839 454 VLVEY 458
Cdd:cd16028 362 VHYEY 366
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
88-463 |
1.24e-34 |
|
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: 133.47 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDLDVSIGGM--IPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSsta 163
Cdd:cd16032 1 PNILLIMADQLTAAALPAygNTVVKTPNLdrLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPAD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 164 wqktqEPdSFPAFLQKHGtYQTFFAGKYlneygskkaggvehvppgwdHWFalernskyynytlsvnGRAQRHGQNYSED 243
Cdd:cd16032 78 -----IP-TFAHYLRAAG-YRTALSGKM--------------------HFV----------------GPDQLHGFDYDEE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 244 -------YLTDvlanisidfLENKSNRRPFFMMVSTPAPHSPWTAAPQYEssfsnvkaprdpnfnihgkdkHWLIRQAkt 316
Cdd:cd16032 115 vafkavqKLYD---------LARGEDGRPFFLTVSFTHPHDPYVIPQEYW---------------------DLYVRRA-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 317 pmtnssvefldnayRKRWRTLLS-VDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLPMdKRQLYEFDIRVPLLV 395
Cdd:cd16032 163 --------------RRAYYGMVSyVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWY-KMSFFEGSARVPLII 227
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 396 RGPDIKPNQTSSLLVANVDLGPTILDIAGYNVNE--TKMDGMSFLPIMigKGNSSTWRSDVLVEYEGEGS 463
Cdd:cd16032 228 SAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPhvPPLDGRSLLPLL--EGGDSGGEDEVISEYLAEGA 295
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
88-458 |
4.74e-32 |
|
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: 127.67 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSIGGmIPLVKT---KKLIGDaGITFTNTFVAsPLCCPSRASILTGKYPHNH---HVVNNTLEGN 158
Cdd:cd16029 1 PHIVFILADDLgwnDVGFHG-SDQIKTpnlDALAAD-GVILNNYYVQ-PICTPSRAALMTGRYPIHTgmqHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 159 CSSTawqktqEPDSFPAFLQKHGtYQTFFAGKYLNEYGSKkaggvEHVPP--GWDHWFA-LERNSKYYNYTLS---VNGR 232
Cdd:cd16029 78 GLPL------NETLLPQYLKELG-YATHLVGKWHLGFYTW-----EYTPTnrGFDSFYGyYGGAEDYYTHTSGganDYGN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 233 AQRHGQN-----YSEDYLTDVLANISIDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYessfsnvkAPRDPNFNIHGKDK 307
Cdd:cd16029 146 DDLRDNEepawdYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEY--------ADPYEDKFAHIKDE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 308 HwliRQAKTPMtnssvefldnayrkrwrtLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSL----PM--DK 381
Cdd:cd16029 218 D---RRTYAAM------------------VSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsnyPLrgGK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 382 RQLYEFDIRVPLLVRGPDIKPN--QTSSLLVANVDLGPTILDIAGYNVNET-KMDGMSFLPiMIGKGNSSTwRSDVLVEY 458
Cdd:cd16029 277 NTLWEGGVRVPAFVWSPLLPPKrgTVSDGLMHVTDWLPTLLSLAGGDPDDLpPLDGVDQWD-ALSGGAPSP-RTEILLNI 354
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
87-451 |
5.74e-31 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 126.32 E-value: 5.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL--D-VSIGGMiPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVnntleGNCSS 161
Cdd:PRK13759 6 KPNIILIMVDQMrgDcLGCNGN-KAVETPNLdmLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV-----GYGDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TAWQKTQEpdsFPAFLQKHGtYQTFFAGKYlneygskkaggvehvppgwdHWFAlERNSKYYNYTL-----SVNGRAQRH 236
Cdd:PRK13759 80 VPWNYKNT---LPQEFRDAG-YYTQCIGKM--------------------HVFP-QRNLLGFHNVLlhdgyLHSGRNEDK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 237 GQ-NYSEDYL-------------------------------------TDVLANISIDFLENKSNRRPFFMMVSTPAPHSP 278
Cdd:PRK13759 135 SQfDFVSDYLawlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 279 WTAAPQYESSFSNVKAPRDPNFNIHGKDKHWLIRQAKT-PMTNSSVEFLDNAYRKRWRTLLSVDDLVEKVVKKLEVRGEL 357
Cdd:PRK13759 215 YDPPKRYFDMYKDADIPDPHIGDWEYAEDQDPEGGSIDaLRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 358 SNTYIIFTSDNGYHTGQFSLpMDKRQLYEFDIRVPLLVRGPD--IKPNQTSSL--LVANVDLGPTILDIAGYNVNETkMD 433
Cdd:PRK13759 295 DNTIILFVSDHGDMLGDHYL-FRKGYPYEGSAHIPFIIYDPGglLAGNRGTVIdqVVELRDIMPTLLDLAGGTIPDD-VD 372
|
410
....*....|....*...
gi 1515217839 434 GMSFLPIMigKGNSSTWR 451
Cdd:PRK13759 373 GRSLKNLI--FGQYEGWR 388
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
88-547 |
1.07e-30 |
|
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: 125.19 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTD----DLDVSIGGmiPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPH-NHHVVNNTLEGNCS 160
Cdd:cd16156 1 KQFIFIMTDtqrwDMVGCYGN--KAMKTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHtNGSWTNCMALGDNV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 161 STAWQKtqepdsfpafLQKHGtYQTFFAGKYLNEYGSKKAGGVehVPPGWD--HWFALeRNskYYNYTLSVNGRAQRHGQ 238
Cdd:cd16156 79 KTIGQR----------LSDNG-IHTAYIGKWHLDGGDYFGNGI--CPQGWDpdYWYDM-RN--YLDELTEEERRKSRRGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 239 N--YSEDYLTDV-----LANISIDFLENKSNrRPFFMMVSTPAPHSPWTAAPQYESSFSNVKAPRDPNF--NIHGKDKH- 308
Cdd:cd16156 143 TslEAEGIKEEFtyghrCTNRALDFIEKHKD-EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPLHq 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 309 --W---LIRQAKTPMTNSSVEFLD-NAYrkrwrtllsVDDLVEKVVKKleVRGELSNTYIIFTSDNGYHTGQFSLPMDKR 382
Cdd:cd16156 222 rlWagaKPHEDGDKGTIKHPLYFGcNSF---------VDYEIGRVLDA--ADEIAEDAWVIYTSDHGDMLGAHKLWAKGP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 383 QLYEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGynVNETKM-DGMSFLPIMIGKGNSStwRSDVLVE--- 457
Cdd:cd16156 291 AVYDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVlEGESILATIEDPEIPE--NRGVFVEfgr 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 458 YEgegsnisdpacpllgpgvsecfpdcVCEDSYNNtYACVRtvsqaanlqyCEFDDNEVFV-------EVYNLTADPFQL 530
Cdd:cd16156 367 YE-------------------------VDHDGFGG-FQPVR----------CVVDGRYKLVinllstdELYDLEKDPYEM 410
|
490 500
....*....|....*....|....*.
gi 1515217839 531 SN---------IAKSIDQEVLEKMNH 547
Cdd:cd16156 411 HNliddpdyadVRDQLHDELLDYMNE 436
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
88-463 |
6.67e-28 |
|
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: 115.32 E-value: 6.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSI--GGMIPLVKTKKL--IGDAGITFTNtFVASPLCCPSRASILTGKYPhNHHvvnntlegNCS 160
Cdd:cd16142 1 PNILVILGDDIgwgDLGCygGGIGRGAPTPNIdrLAKEGLRFTS-FYVEPSCTPGRAAFITGRHP-IRT--------GLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 161 STAWQKTQ------EPdSFPAFLQKHGtYQTFFAGKylNEYGSKKaggvEHVPP--GWDHWFAlernskYYNYTLsvngr 232
Cdd:cd16142 71 TVGLPGSPgglppwEP-TLAELLKDAG-YATAQFGK--WHLGDED----GRLPTdhGFDEFYG------NLYHTI----- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 233 aqrhgqnysEDYLTDVlaniSIDFL-ENKSNRRPFFMMVSTPAPHSPWTAAPQYEssfsnvkaprdpnfnihGKDKHWli 311
Cdd:cd16142 132 ---------DEEIVDK----AIDFIkRNAKADKPFFLYVNFTKMHFPTLPSPEFE-----------------GKSSGK-- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 312 rqaktpmtnssVEFLDnayrkrwrTLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHtgQFSLPM--------DKRQ 383
Cdd:cd16142 180 -----------GKYAD--------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGPE--QDVWPDggytpfrgEKGT 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 384 LYEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAG-------YNVNETKMDGMSFLPIMIGKGNSStwRSDVL 455
Cdd:cd16142 239 TWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGapdpkdkLLGKDRHIDGVDQSPFLLGKSEKS--RRSEF 316
|
....*...
gi 1515217839 456 VeYEGEGS 463
Cdd:cd16142 317 F-YFGEGE 323
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
88-459 |
1.70e-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: 107.29 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDD---LDVSIGGMIPL-VKTKKLIGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTlegncsSTA 163
Cdd:cd16035 1 PNILLILTDQeryPPPWPAGWAALnLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTL------GSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 164 WQKTQEPDsFP---AFLQKHGtYQTFFAGKylneygskkaggvehvppgWdHwfalernskyynytLSvngRAQRHGQNY 240
Cdd:cd16035 75 MQPLLSPD-VPtlgHMLRAAG-YYTAYKGK-------------------W-H--------------LS---GAAGGGYKR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 241 SEDYltdvlANISIDFLENK----SNRRPFFMMVSTPAPH---SPWTAAPQYEssfsnvkapRDPNFnihgkdKHWLIRQ 313
Cdd:cd16035 116 DPGI-----AAQAVEWLRERgaknADGKPWFLVVSLVNPHdimFPPDDEERWR---------RFRNF------YYNLIRD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 314 aktpmtnssvefldnayrkrwrtllsVDDLVEKVVKKLEVRGELSNTYIIFTSDNG----YHTGqfslpmdKRQ---LYE 386
Cdd:cd16035 176 --------------------------VDRQIGRVLDALDASGLADNTIVVFTSDHGemggAHGL-------RGKgfnAYE 222
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515217839 387 FDIRVPLLVRGPDIKPN-QTSSLLVANVDLGPTILDIAGYNVNETKMD-----GMSFLPIMIGKGNSSTwRSDVLVEYE 459
Cdd:cd16035 223 EALHVPLIISHPDLFGTgQTTDALTSHIDLLPTLLGLAGVDAEARATEapplpGRDLSPLLTDADADAV-RDGILFTYD 300
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
87-447 |
1.65e-24 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 106.75 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDLDV----SIG------GMIPLVKTKkligdaGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNntle 156
Cdd:cd16160 1 KPNIVLFFADDMGYgdlaSYGhptqerGPIDDMAAE------GIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 157 GNCSSTAWQKTQEPDS---FPAFLQKHGtYQTFFAGKY---LNEYGS-------KKAG--GVEHVPPGWDHWFAleRNSK 221
Cdd:cd16160 71 GTRVFLPWDIGGLPKTevtMAEALKEAG-YTTGMVGKWhlgINENNHsdgahlpSHHGfdFVGTNLPFTNSWAC--DDTG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 222 -------------YYNYTLSvngraqrhGQNYSEDYLTDVLANISIDFLENKSNrRPFFMMVSTPAPHSPWTAAPQYess 288
Cdd:cd16160 148 rhvdfpdrsacflYYNDTIV--------EQPIQHEHLTETLVGDAKSFIEDNQE-NPFFLYFSFPQTHTPLFASKRF--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 289 fsnvkaprdpnfnihgkdkhwlirqaktpmTNSSV--EFLDNAYRKRWRtllsvddlVEKVVKKLEVRGELSNTYIIFTS 366
Cdd:cd16160 216 ------------------------------KGKSKrgRYGDNINEMSWA--------VGEVLDTLVDTGLDQNTLVFFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 367 DNGYH-----TGQFSLPMD--KRQLYEFDIRVPLLVRGPDIKPNQTSSLLVANVDLGPTILDIAGYNVNE-TKMDGMSFL 438
Cdd:cd16160 258 DHGPHveyclEGGSTGGLKggKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTdRIYDGLSIT 337
|
....*....
gi 1515217839 439 PIMIGKGNS 447
Cdd:cd16160 338 DLLLGEADS 346
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
87-436 |
2.24e-23 |
|
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: 100.14 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDLDV-SIG--GMIPLVKTKKLIG-------DA----GITFTNTFVASPLCCPSRASILTGKYPHNHHVVN 152
Cdd:cd16153 1 KPNILWIITDDQRVdSLScyNNAHTGKSESRLGyvespniDAlaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 153 NtlEGncsstAWQKTQE-PDSFPAFLQKHGtYQTFFAGKylneygskkaggvEHVPPgwdhwFALERNSKYYNYTLSVNG 231
Cdd:cd16153 81 F--EA-----AHPALDHgLPTFPEVLKKAG-YQTASFGK-------------SHLEA-----FQRYLKNANQSYKSFWGK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 232 RAQrhgqnysedyltdvlanisidfleNKSNRRPFFMMVSTPAPHSPWTAAPQYESSFsnvkaprdpnfnihgkDKHWLI 311
Cdd:cd16153 135 IAK------------------------GADSDKPFFVRLSFLQPHTPVLPPKEFRDRF----------------DYYAFC 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 312 rqaktpmtnssvefldnAYrkrwrtllsVDDLVEKVVKKLEVRGELS---NTYIIFTSDNGYHTGQFSLpMDKRQLYEFD 388
Cdd:cd16153 175 -----------------AY---------GDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGI-LAKFTFWPQS 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1515217839 389 IRVPLLVRGPDIKP---NQTSSLLVANVDLGPTILDIAGYNVNETK-MDGMS 436
Cdd:cd16153 228 HRVPLIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDVDAPDyLDGRD 279
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
87-444 |
1.49e-21 |
|
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: 97.92 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL---DVSIGGMiPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYP-------HNHHVVNNT 154
Cdd:cd16157 1 KPNIILMLMDDMgwgDLGVFGE-PSRETPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPirngfytTNAHARNAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 155 LEGNCSSTAwqktqePDS---FPAFLQKHGtYQTFFAGKYlneygskKAGGVEHVPP---GWDHWFALER-------NSK 221
Cdd:cd16157 80 TPQNIVGGI------PDSeilLPELLKKAG-YRNKIVGKW-------HLGHRPQYHPlkhGFDEWFGAPNchfgpydNKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 222 YYNYTLSVN----GRAQRH---GQNYSEDYLTDVLANISIDFLENKSNR-RPFFMMVSTPAPHSPWTAAPQYEssfsnvk 293
Cdd:cd16157 146 YPNIPVYRDwemiGRYYEEfkiDKKTGESNLTQIYLQEALEFIEKQHDAqKPFFLYWAPDATHAPVYASKPFL------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 294 aprdpnfnihGKDKHWLIRQAktpmtnssvefldnayrkrwrtLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTg 373
Cdd:cd16157 219 ----------GTSQRGLYGDA----------------------VMELDSSVGKILESLKSLGIENNTFVFFSSDNGAAL- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 374 qFSLPMD----------KRQLYEFDIRVPLLVRGP-DIKPNQTSSLLVANVDLGPTILDIAGYNV-NETKMDGMSFLPIM 441
Cdd:cd16157 266 -ISAPEQggsngpflcgKQTTFEGGMREPAIAWWPgHIKPGQVSHQLGSLMDLFTTSLALAGLPIpSDRAIDGIDLLPVL 344
|
...
gi 1515217839 442 IGK 444
Cdd:cd16157 345 LNG 347
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
87-443 |
2.88e-21 |
|
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: 96.00 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL---DVSIGGMIPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSS 161
Cdd:cd16161 1 KPNFLLLFADDLgwgDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TAWQKTQEPDSfpafLQKHGtYQTFFAGKYlnEYGSKKAggveHVPpgwdhwfalerNSKYYNYTLsvngraqrhGQNYS 241
Cdd:cd16161 81 LPLNETTLAEV----LRQAG-YATGMIGKW--HLGQREA----YLP-----------NSRGFDYYF---------GIPFS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 242 ED-YLTDVLANISIDFLENKSNR-RPFFMMVSTPAPHSPWTAAPQYESSFSnvkaprdpnfnihgkdkhwlirqAKTPMT 319
Cdd:cd16161 130 HDsSLADRYAQFATDFIQRASAKdRPFFLYAALAHVHVPLANLPRFQSPTS-----------------------GRGPYG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 320 NssvefldnayrkrwrTLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDNG-------YHTGQFSLPMDKRQ--------L 384
Cdd:cd16161 187 D---------------ALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkceLAVGPGTGDWQGNLggsvakasT 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1515217839 385 YEFDIRVPLLVRGPD-IKPNQTSSLLVANVDLGPTILDIAGYNVNETKM-DGMSFLPIMIG 443
Cdd:cd16161 252 WEGGHREPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGRIyDGKDLSPVLFG 312
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
88-466 |
6.81e-21 |
|
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: 94.53 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDLDVSIGGMiPLVKTKKL-----IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST 162
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFR-PGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 163 AWQKTqepdsfpafLQKHGtYQTFFAGKYlnEYGSkkagGVEHVPPGWDHWfalernSKYYNYTLSVNGR-------AQR 235
Cdd:cd16171 80 TWMDR---------LEKHG-YHTQKYGKL--DYTS----GHHSVSNRVEAW------TRDVPFLLRQEGRptvnlvgDRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 236 HGQNYSEDYLTDVLANISIDFlENKSNRRPFFMMVSTPAPHsPWTAapqyESSFSNVKAPRDpnfnihgkdkhwlIRQAK 315
Cdd:cd16171 138 TVRVMLKDWQNTDKAVHWIRK-EAPNLTQPFALYLGLNLPH-PYPS----PSMGENFGSIRN-------------IRAFY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 316 TPMTNSSvefldnayrkrwrtllsvDDLVEKVVKKLEVRGELSNTYIIFTSDNGyhtgqfSLPMDKRQ-----LYEFDIR 390
Cdd:cd16171 199 YAMCAET------------------DAMLGEIISALKDTGLLDKTYVFFTSDHG------ELAMEHRQfykmsMYEGSSH 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 391 VPLLVRGPDIKPNQTSSLLVANVDLGPTILDIAGYNVNETkMDGMSFLPIMIGKGNSSTWRSD-----VLVEYEGEGSNI 465
Cdd:cd16171 255 VPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN-LSGYSLLPLLSESSIKESPSRVphpdwVLSEFHGCNVNA 333
|
.
gi 1515217839 466 S 466
Cdd:cd16171 334 S 334
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
88-447 |
8.76e-17 |
|
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: 83.26 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSIGGMiPLVKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST 162
Cdd:cd16158 2 PNIVLLFADDLgygDLGCYGH-PSSSTPNLdrLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 163 AwqkTQEPDSFPAFLQKHGtYQTFFAGKYLNEYGSKKAggveHVPP--GWDHWFALErnskyynYTlsvngRAQRHGQNY 240
Cdd:cd16158 81 L---PLNETTIAEVLKTVG-YQTAMVGKWHLGVGLNGT----YLPThqGFDHYLGIP-------YS-----HDQGPCQNL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 241 S------------EDYLTDV--LANISI-----DFL---------------ENKSNRRPFFMMVSTPAPHSPWTAAPQYE 286
Cdd:cd16158 141 TcfppnipcfggcDQGEVPCplFYNESIvqqpvDLLtleeryakfakdfiaDNAKEGKPFFLYYASHHTHYPQFAGQKFA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 287 SsfsnvKAPRDPnfnihgkdkhwlirqaktpmtnssveFLDnayrkrwrTLLSVDDLVEKVVKKLEVRGELSNTYIIFTS 366
Cdd:cd16158 221 G-----RSSRGP--------------------------FGD--------ALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 367 DNGYHTGQFS-------LPMDKRQLYEFDIRVPLLVRGPD-IKPNQTSSlLVANVDLGPTILDIAGYNVNETKMDGMSFL 438
Cdd:cd16158 262 DNGPSTMRKSrggnaglLKCGKGTTYEGGVREPAIAYWPGrIKPGVTHE-LASTLDILPTIAKLAGAPLPNVTLDGVDMS 340
|
....*....
gi 1515217839 439 PIMIGKGNS 447
Cdd:cd16158 341 PILFEQGKS 349
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
87-448 |
1.93e-16 |
|
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: 82.34 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLILTDDL---DVSIGGMIPLvKTKKL--IGDAGITFTNTFVASPLCCPSRASILTGKYP-------HNHHVVNNt 154
Cdd:cd16159 1 KPNIVLFMADDLgigDVGCFGNDTI-RTPNIdrLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirsgmasSHGMRVIL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 155 legNCSSTAWQKTQEPdSFPAFLQKHGtYQTFFAGKY-------------------------------LNEYGSKKAGGV 203
Cdd:cd16159 79 ---FTASSGGLPPNET-TFAEVLKQQG-YSTALIGKWhlglhcesrndfchhplnhgfdyfyglpltnLKDCGDGSNGEY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 204 EHVPPGWDH----------------------------------------WFALERNSKYYNYTLSVNGRAQRhgQNYSED 243
Cdd:cd16159 154 DLSFDPLFPlltafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHEVVE--QPMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 244 YLTDVLANISIDFLENKSnRRPFFMMVSTPAPHSPWTAAPQYEssfsnvkaprdpnfnihGKDKHWLIRQAktpmtnssV 323
Cdd:cd16159 232 NLTQRLTKEAISFLERNK-ERPFLLVMSFLHVHTALFTSKKFK-----------------GRSKHGRYGDN--------V 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 324 EFLDnayrkrWRtllsvddlVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQFSLPMD------------KRQLYEFDIRV 391
Cdd:cd16159 286 EEMD------WS--------VGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEygggnggiyggkKMGGWEGGIRV 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1515217839 392 PLLVRGP-DIKPNQTSSLLVANVDLGPTILDIAGYNV-NETKMDGMSFLPIMIGKGNSS 448
Cdd:cd16159 352 PTIVRWPgVIPPGSVIDEPTSLMDIFPTVAALAGAPLpSDRIIDGRDLMPLLTGQEKRS 410
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
88-423 |
5.18e-16 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 77.85 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLILTDDL---DVSIGGM-IPLVKTKKLIGDAGITFtNTFVASPLC--CPSRASILTGKYPHNHHVVNNtlegncss 161
Cdd:cd00016 1 KHVVLIVLDGLgadDLGKAGNpAPTTPNLKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGN-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 tAWQKTQEPDSFpafLQKHGTYQTFFagKYLneygsKKAGGvehvppGWDhWFALErnskyynytlsvngraqrhgqnys 241
Cdd:cd00016 72 -GSADPELPSRA---AGKDEDGPTIP--ELL-----KQAGY------RTG-VIGLL------------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 242 edyltdvlanisiDFLENKSNRRPFFMMVSTPAPHSPWTA-APQYESSFSNVKAprdpnfnihgkdkhwlirqaktpmtn 320
Cdd:cd00016 110 -------------KAIDETSKEKPFVLFLHFDGPDGPGHAyGPNTPEYYDAVEE-------------------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 321 ssvefldnayrkrwrtllsVDDLVEKVVKKLEVRGELSNTYIIFTSDNG---YHTGQFSLPMDKRQLYEFDIRVPLLVRG 397
Cdd:cd00016 151 -------------------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYG 211
|
330 340
....*....|....*....|....*.
gi 1515217839 398 PDIKPNQTSSLLVANVDLGPTILDIA 423
Cdd:cd00016 212 PGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
88-424 |
2.27e-10 |
|
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: 61.93 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 88 PNIVLIL-----TDDLDVSIGGMIPLVKTKKLIGDaGITFTNTFVASPLCCPSRA--SILTGKYPhnhhvvnntLEGNCS 160
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKE-GLYFGNFYSPGFGGGTANGefEVLTGLPP---------LPLGSG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 161 STAWQKTQEPDSFPAFLQKHGtYQTFFAGKYLNEYGSK----KAGGVEHVppgWDhwfalernSKYYNYTlsvngraqrh 236
Cdd:cd16015 71 SYTLYKLNPLPSLPSILKEQG-YETIFIHGGDASFYNRdsvyPNLGFDEF---YD--------LEDFPDD---------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 237 GQNYSEDYLTD-VLANISIDFLENKSNRrPFFMMVSTPAPHSPWTaapqyessfsnVKAPRDPNFNIHGKDKHWLIRQAk 315
Cdd:cd16015 129 EKETNGWGVSDeSLFDQALEELEELKKK-PFFIFLVTMSNHGPYD-----------LPEEKKDEPLKVEEDKTELENYL- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 316 tpmtnSSVEFLDNAyrkrwrtllsvddlVEKVVKKLEVRGELSNTYIIFTSDngyHTGQFSLPMDKRQLYEFDI-RVPLL 394
Cdd:cd16015 196 -----NAIHYTDKA--------------LGEFIEKLKKSGLYENTIIVIYGD---HLPSLGSDYDETDEDPLDLyRTPLL 253
|
330 340 350
....*....|....*....|....*....|
gi 1515217839 395 VRGPDIKPNQTSSLLVANVDLGPTILDIAG 424
Cdd:cd16015 254 IYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
87-438 |
1.14e-09 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 61.21 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 87 RPNIVLIL-----TDDLDVSIGGMIPLVKTKKLIGDaGITFTNTFVASPLCCPSRASILTGKYPhnhhvvnnTLEGNCSS 161
Cdd:COG1368 234 KPNVVVILlesfsDFFIGALGNGKDVTPFLDSLAKE-SLYFGNFYSQGGRTSRGEFAVLTGLPP--------LPGGSPYK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 162 TAWQKTQEpdSFPAFLQKHGtYQTFFagkylneygskkaggvehvppgwdhwfalernskYYNYTLSVNGRAQRHGQN-- 239
Cdd:COG1368 305 RPGQNNFP--SLPSILKKQG-YETSF----------------------------------FHGGDGSFWNRDSFYKNLgf 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 240 ---YSEDYLTDVLANI-----------SIDFLENKSnrRPFFMMVSTPAPHSPWTAaPQYESSFSnvkaprdpnfnihgk 305
Cdd:COG1368 348 defYDREDFDDPFDGGwgvsdedlfdkALEELEKLK--KPFFAFLITLSNHGPYTL-PEEDKKIP--------------- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 306 dkhwlirqaktpmtnssvEFLDNAYRKRWRTLLSVDDLVEKVVKKLEVRGELSNTYIIFTSDngyHTGqfslPMDKRQLY 385
Cdd:COG1368 410 ------------------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGD---HGP----RSPGKTDY 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1515217839 386 EFDI---RVPLLVRGPDIKPNQTSSLLVANVDLGPTILDIAGYNVNETKMDGMSFL 438
Cdd:COG1368 465 ENPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLL 520
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
133-424 |
2.17e-09 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 58.75 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 133 CPSRASILTGKYPHNHHVVNNTLegncsstaWQ-KTQEPDSFPAFLQKHGTYQ--TFFagkYLNEYGSKKAGGVehvppg 209
Cdd:cd16018 47 FPNHYSIVTGLYPESHGIVGNYF--------YDpKTNEEFSDSDWVWDPWWIGgePIW---VTAEKAGLKTASY------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 210 wdHWFALERNSKYYNYTLSVNGRaqrHGQNYSEDYLTDVLANISIDFLENksnRRPFFMMVSTPAP----HspwtaapQY 285
Cdd:cd16018 110 --FWPGSEVAIIGYNPTPIPLGG---YWQPYNDSFPFEERVDTILEWLDL---ERPDLILLYFEEPdsagH-------KY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 286 essfsnvkAPRDPNFNihgkdkhwlirqaktpmtnssvefldNAYRKrwrtllsVDDLVEKVVKKLEVRGELSNTYIIFT 365
Cdd:cd16018 175 --------GPDSPEVN--------------------------EALKR-------VDRRLGYLIEALKERGLLDDTNIIVV 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1515217839 366 SDNGYHT----GQFSlpmdkrqlYEFDIRVPLLVRGPDIKPNQTSSLLvANVDLGPTILDIAG 424
Cdd:cd16018 214 SDHGMTDvgthGYDN--------ELPDMRAIFIARGPAFKKGKKLGPF-RNVDIYPLMCNLLG 267
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
133-369 |
9.46e-05 |
|
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: 44.72 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 133 CPSRASILTGKYPHNHHVVNNTL---EGNCSSTAWQKTQEpdsFPAFLQKHGTYQT-----FFAGKYLNEYGSKKAGGVE 204
Cdd:pfam01663 45 FPNHYTLVTGLYPGSHGIVGNTFydpKTGEYLVFVISDPE---DPRWWQGEPIWDTaakagVRAAALFWPGSEVDYSTYY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 205 HVPPGWDHwfalernsKYYNYTLSVNGRAqrhGQNYSEDYLTDVLANISIDflenksnrRPFFMMVSTPAPhspwtaapq 284
Cdd:pfam01663 122 GTPPRYLK--------DDYNNSVPFEDRV---DTAVLQTWLDLPFADVAAE--------RPDLLLVYLEEP--------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 285 yeSSFSNVKAPRDPNFNihgkdkhwlirqaktpmtnssvefldNAYRKrwrtllsVDDLVEKVVKKLEVRGELSNTYIIF 364
Cdd:pfam01663 174 --DYAGHRYGPDSPEVE--------------------------DALRR-------VDRAIGDLLEALDERGLFEDTNVIV 218
|
....*
gi 1515217839 365 TSDNG 369
Cdd:pfam01663 219 VSDHG 223
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
324-426 |
3.63e-03 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 39.43 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515217839 324 EFLdNAYRKR------WRTLLS---------VDDLVEKVVKKLEVRGELSNTYIIFTSDNGYHTGQF----------SLP 378
Cdd:cd16021 155 DFI-EAYKDRpkfsffWLSELThdylnglslADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIretlqgkleeRLP 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1515217839 379 MdkrqLYefdIRVP--LLVRGPDIKPN--QTSSLLVANVDLGPTILDIAGYN 426
Cdd:cd16021 234 F----LS---ISLPkwFREKYPEAVANlkKNSNRLTTPFDLHATLLDILNLQ 278
|
|
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