|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
38-487 |
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: 608.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDQDAELGGMTPLKKTKALIGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKAWQK 117
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 118 IQEPYTFPAILKSvCGYQTFFAGKYLNEYGAPdaGGLEHIPLGWSYWYALEKNSKYYNYTLSiNGKARKHGENYSVDYLT 197
Cdd:cd16147 81 GLERSTLPVWLQE-AGYRTAYAGKYLNGYGVP--GGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 198 DVLANLSLDFLDY-KSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNV--IAPRNKNFNIHGTNKHWLIRQAKTPMTnsSI 274
Cdd:cd16147 157 DVIANKALDFLRRaAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVtaPPRPPPNNPDVSDKPHWLRRLPPLNPT--QI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 275 RFLDDAFRRRWQTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIKPN 354
Cdd:cd16147 235 AYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 355 QTSKMLVSNIDLGPTILDLAGYDLnKTQMDGMSllpilkgdrnltwrsdvlveyqgegrnvtdptcpslspgvsqcfpdc 434
Cdd:cd16147 315 VTVDQLVSNIDLAPTILDLAGAPP-PSDMDGRS----------------------------------------------- 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 29789239 435 vCEDAYNNTYACVRTLSSLWNLQYCEFDdqEVFVEVYNITADPDQITNIAKSI 487
Cdd:cd16147 347 -CGDSNNNTYKCVRTVDDTYNLLYFEWC--TGFRELYDLTTDPYQLTNLAGDL 396
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
37-502 |
2.05e-99 |
|
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: 307.15 E-value: 2.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 37 RRPNVLLLLTDDQ--DAeLGGMT-PLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNtlEGNcS 111
Cdd:cd16031 1 KRPNIIFILTDDHryDA-LGCYGnPIVKTPNIdrLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDN--NGP-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 112 SKAWQKiqepyTFPAILKSVcGYQTFFAGKylneYGAPDAGGLEhiPLGWSYWYALEKNSKYYNYTLSINGKARKHGEny 191
Cdd:cd16031 77 FDASQP-----TYPKLLRKA-GYQTAFIGK----WHLGSGGDLP--PPGFDYWVSFPGQGSYYDPEFIENGKRVGQKG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 192 svdYLTDVLANLSLDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAPRNKNFNI-HGTNK-HWLiRQAKtpm 269
Cdd:cd16031 143 ---YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDDdDYAGRpEWA-REQR--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 270 tNSSIRFLDDAFRRRW----------QTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLpIDKRQLYEFD 339
Cdd:cd16031 216 -NRIRGVLDGRFDTPEkyqrymkdylRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGL-FDKRLMYEES 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 340 IKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKtQMDGMSLLPILKGDRNLTWRSDVLVEYQGEGrnvtdp 418
Cdd:cd16031 294 IRVPLIIRDPRlIKAGTVVDALVLNIDFAPTILDLAGVPIPE-DMQGRSLLPLLEGEKPVDWRKEFYYEYYEEP------ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 419 tcpslspgvsqcfpdcvcedAYNNTYAC--VRTlsSLWNL-QYCEFDDQEvfvEVYNITADPDQITNIAKsiDPE---LL 492
Cdd:cd16031 367 --------------------NFHNVPTHegVRT--ERYKYiYYYGVWDEE---ELYDLKKDPLELNNLAN--DPEyaeVL 419
|
490
....*....|
gi 29789239 493 GKMNYRLMML 502
Cdd:cd16031 420 KELRKRLEEL 429
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
35-495 |
1.71e-87 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 275.22 E-value: 1.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 35 AARRPNVLLLLTDDQDA-ELG--GMTPLKkTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGN 109
Cdd:COG3119 20 AAKRPNILFILADDLGYgDLGcyGNPLIK-TPNIdrLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 110 CSSKAWQKiqepyTFPAILKSVcGYQTFFAGKYlneygapdaggleHIplgwsywyaleknskyynytlsingkarkhge 189
Cdd:COG3119 99 GGLPPDEP-----TLAELLKEA-GYRTALFGKW-------------HL-------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 190 nysvdYLTDVLANLSLDFLD-YKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAPRNKNFNIHGTNKHWLIRqaktp 268
Cdd:COG3119 128 -----YLTDLLTDKAIDFLErQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPNLAPRDLTEEELRR----- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 269 mtnssirflddAFRRRWQTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRG 348
Cdd:COG3119 198 -----------ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRW 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 349 PG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKTqMDGMSLLPILKGDRNlTWRSDVLVEYQGEGRNvtdptcpslspgv 427
Cdd:COG3119 267 PGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPED-LDGRSLLPLLTGEKA-EWRDYLYWEYPRGGGN------------- 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789239 428 sqcfpdcvcedaynntyACVRTlsslWNLQYCEFDDQEVFVEVYNITADPDQITNIAKSiDPELLGKM 495
Cdd:COG3119 332 -----------------RAIRT----GRWKLIRYYDDDGPWELYDLKNDPGETNNLAAD-YPEVVAEL 377
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
39-400 |
2.59e-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: 213.17 E-value: 2.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDD---QDAELGGM----TP----LKKtkaligeKGMTFSSAYVPSALCCPSRASILTGKYPHNHHvVNNTLE 107
Cdd:cd16144 1 PNIVLILVDDlgwADLGCYGSkfyeTPnidrLAK-------EGMRFTQAYAAAPVCSPSRASILTGQYPARLG-ITDVIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 108 GNCSSKAWQKIQEPY----------TFPAILKSvCGYQTFFAGKY---LNEYGAP--------DAGGLEHIPLGWSYWYa 166
Cdd:cd16144 73 GRRGPPDNTKLIPPPsttrlpleevTIAEALKD-AGYATAHFGKWhlgGEGGYGPedqgfdvnIGGTGNGGPPSYYFPP- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 167 leknsKYYNYTLSINGKArkhgenysvDYLTDVLANLSLDFLDyKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAP 246
Cdd:cd16144 151 -----GKPNPDLEDGPEG---------EYLTDRLTDEAIDFIE-QNKDKPFFLYLSHYAVHTPIQARPELIEKYEKKKKG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 247 RNKnfnihgtnKHWLIRQAktpmtnssirflddafrrrwqTLL-SVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQ 325
Cdd:cd16144 216 LRK--------GQKNPVYA---------------------AMIeSLDESVGRILDALEELGLADNTLVIFTSDNGGLSTR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 326 FSLPID-------KRQLYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQ-MDGMSLLPILKGD- 395
Cdd:cd16144 267 GGPPTSnaplrggKGSLYEGGIRVPLIVRWPGvIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQhLDGVSLVPLLKGGe 346
|
410
....*....|
gi 29789239 396 -----RNLTW 400
Cdd:cd16144 347 adlprRALFW 356
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
39-387 |
9.91e-63 |
|
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: 205.36 E-value: 9.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAELGGMT--PLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKa 114
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYgnPDIKTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 wqkiqEPYTFPAILKSVcGYQTFFAGKylneygapdagglehiplgwsyWyaleknskyynytlsingkarkHGEnysvd 194
Cdd:cd16022 80 -----DEPTLAELLKEA-GYRTALIGK----------------------W----------------------HDE----- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 195 yltdvlanlSLDFLDYKSNSEPFFMMISTPAPHSPWTAApqyqkafqnviaprnknfnihgtnkhwlirqaktpmtnSSI 274
Cdd:cd16022 105 ---------AIDFIERRDKDKPFFLYVSFNAPHPPFAYY--------------------------------------AMV 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 275 RFLDDAFRRrwqtllsvddlvekLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPG-IKP 353
Cdd:cd16022 138 SAIDDQIGR--------------ILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGkIPA 203
|
330 340 350
....*....|....*....|....*....|....
gi 29789239 354 NQTSKMLVSNIDLGPTILDLAGYDLNKTqMDGMS 387
Cdd:cd16022 204 GQVSDALVSLLDLLPTLLDLAGIEPPEG-LDGRS 236
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
39-376 |
1.09e-60 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 202.27 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQ---DAELGG----MTPLKKTKAligEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLegncs 111
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLYGyprpTTPFLDRLA---EEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 112 skaWQKIQEPYTFPAILKSVcGYQTFFAGKYL---NEYGAPDAGGLEHIpLGWSYWYALEKNSKYYNYTLSINGkarkhg 188
Cdd:pfam00884 73 ---VGLPRTEPSLPDLLKRA-GYNTGAIGKWHlgwYNNQSPCNLGFDKF-FGRNTGSDLYADPPDVPYNCSGGG------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 189 enysvdYLTDVLANLSLDFLDykSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNViaprnknfnihgtnkhwlirqaktp 268
Cdd:pfam00884 142 ------VSDEALLDEALEFLD--NNDKPFFLVLHTLGSHGPPYYPDRYPEKYATF------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 269 mtNSSIRFLDDAFRRRWQTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPID---KRQLYEFDIKVPLL 345
Cdd:pfam00884 189 --KPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHggkYDNAPEGGYRVPLL 266
|
330 340 350
....*....|....*....|....*....|..
gi 29789239 346 VRGPG-IKPNQTSKMLVSNIDLGPTILDLAGY 376
Cdd:pfam00884 267 IWSPGgKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
39-490 |
2.34e-60 |
|
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: 203.89 E-value: 2.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAELGG-MTPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNhhvvnNTLEGNCSSKAW 115
Cdd:cd16027 1 PNILWIIADDLSPDLGGyGGNVVKTPNLdrLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQ-----NGAHGLRSRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 116 --QKIQepyTFPAILKSVcGYQTFFAGKylneygapdagglehiplgwsywyaleknsKYYNYTLSINGKARKHGENYSV 193
Cdd:cd16027 76 lpDGVK---TLPELLREA-GYYTGLIGK------------------------------THYNPDAVFPFDDEMRGPDDGG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 194 DYLTDVLANlSLDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQKAF--QNVIAPRNknfnihgtnkhwlirQAKTPMTn 271
Cdd:cd16027 122 RNAWDYASN-AADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYdpEKVKVPPY---------------LPDTPEV- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 272 ssiRfldDAFRRRWQTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYhtgqfSLPIDKRQLYEFDIKVPLLVRGPG- 350
Cdd:cd16027 185 ---R---EDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGk 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 351 IKPNQTSKMLVSNIDLGPTILDLAGYDLNKtQMDGMSLLPILKGDrNLTWRSDVLVEYqgegrnvtdptcpslspgvsqc 430
Cdd:cd16027 254 IKPGSVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLLKGE-KDPGRDYVFAER---------------------- 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789239 431 fpdcvceDAYNNTYACVRTLSS-----LWNLQYcefddqevfVEVYNITADPDQITNIAKsiDPE 490
Cdd:cd16027 310 -------DRHDETYDPIRSVRTgrykyIRNYMP---------EELYDLKNDPDELNNLAD--DPE 356
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-490 |
1.69e-58 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 200.14 E-value: 1.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQ--DAELGGMTPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKA 114
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 WQKIQEpyTFPAILKSVcGYQTFFAGKYlneYGAPDAGGLEHiplGWSYWyaleknskyynytlsingkarkHGENYSVD 194
Cdd:cd16033 81 LPPGVE--TFSEDLREA-GYRNGYVGKW---HVGPEETPLDY---GFDEY----------------------LPVETTIE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 195 YLtdvLANLSLDFL-DYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAPRNKNFNIHGTNKHWLIRQAKTPMTnss 273
Cdd:cd16033 130 YF---LADRAIEMLeELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYRRERKRWG--- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 274 irfLDDAFRRRWQTLLS--------VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLpIDKRQ-LYEFDIKVPL 344
Cdd:cd16033 204 ---VDTEDEEDWKEIIAhywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRL-WDKGPfMYEETYRIPL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 345 LVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYD-LNKTqmDGMSLLPILKGDRNLTWRSDVLVEYQGEGrnvtdptcps 422
Cdd:cd16033 280 IIKWPGvIAAGQVVDEFVSLLDLAPTILDLAGVDvPPKV--DGRSLLPLLRGEQPEDWRDEVVTEYNGHE---------- 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789239 423 lSPGVSQcfpdcvcedaynntyaCVRTLSslWNLQYCEFDdqevFVEVYNITADPDQITNIAKsiDPE 490
Cdd:cd16033 348 -FYLPQR----------------MVRTDR--YKYVFNGFD----IDELYDLESDPYELNNLID--DPE 390
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-483 |
2.42e-58 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 199.33 E-value: 2.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDD---QDAELGGMTPLKkTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNN--TLEgnc 110
Cdd:cd16034 1 KPNILFIFADQhraQALGCAGDDPVK-TPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNdvPLP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 111 sskawqkiQEPYTFPAILKSVcGYQTFFAGKY-LNEYGAPDAGGLEHIP-----LGWSYWYALEKNSKYYNYTLSINGKA 184
Cdd:cd16034 77 --------PDAPTIADVLKDA-GYRTGYIGKWhLDGPERNDGRADDYTPpperrHGFDYWKGYECNHDHNNPHYYDDDGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 185 RKHGENYSVDYLTDVLanlsLDFLD-YKSNSEPFFMMISTPAPHSPWTAAPQ-YQKAFQnviaprnknfnihgtNKHWLI 262
Cdd:cd16034 148 RIYIKGYSPDAETDLA----IEYLEnQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYD---------------PKKLLL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 263 RQaktpmtNSSIRFLDDAFRRRWQT-----LLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNG---YHTGQFSlpidKRQ 334
Cdd:cd16034 209 RP------NVPEDKKEEAGLREDLRgyyamITALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMN----KQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 335 LYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKTqMDGMSLLPILKGDRNLTWRSDVLVEYQGEGR 413
Cdd:cd16034 279 PYEESIRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT-VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGG 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789239 414 NvtdptcpslspgvsqcfpdcvcEDAYNNTYACVRTlsslwnLQY---CEFDDQEVFvevYNITADPDQITNI 483
Cdd:cd16034 358 G----------------------SARDGGEWRGVRT------DRYtyvRDKNGPWLL---FDNEKDPYQLNNL 399
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
38-490 |
1.94e-48 |
|
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: 173.53 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDQDAELGGM------TP----LKKtkaligeKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNtle 107
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYgghpakTPnidrLAA-------RGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDN--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 108 gncsSKAWQKIQEPY-TFPAILKSVcGYQTFFAGK---YLNEYGAPDagglehiPLGWSYWYALEKNSKYYNYTLSINGK 183
Cdd:cd16030 72 ----NSYFRKVAPDAvTLPQYFKEN-GYTTAGVGKifhPGIPDGDDD-------PASWDEPPNPPGPEKYPPGKLCPGKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 184 ARKHGENYSV------------DYLTdvlANLSLDFLDYKSNS-EPFFMMISTPAPHSPWTAAPQYQKAFqnviaPRNKN 250
Cdd:cd16030 140 GGKGGGGGPAweaadvpdeaypDGKV---ADEAIEQLRKLKDSdKPFFLAVGFYKPHLPFVAPKKYFDLY-----PLESI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 251 FNIHGTNKHWLIRQAKTPMTNssIRFLDDAFRR------------RWQTLLS--------VDDLVEKLVKRLDSTGELDN 310
Cdd:cd16030 212 PLPNPFDPIDLPEVAWNDLDD--LPKYGDIPALnpgdpkgplpdeQARELRQayyasvsyVDAQVGRVLDALEELGLADN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 311 TYIFYTSDNGYH---TGQFSlpidKRQLYEFDIKVPLLVRGPGIK-PNQTSKMLVSNIDLGPTILDLAGYDLNKtQMDGM 386
Cdd:cd16030 290 TIVVLWSDHGWHlgeHGHWG----KHTLFEEATRVPLIIRAPGVTkPGKVTDALVELVDIYPTLAELAGLPAPP-CLEGK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 387 SLLPILKgDRNLTWRSDVLVEYQGEGRNvtdptcpslspGVSqcfpdcvcedaynntyacVRTlsSLWNL-QYCEFDDqE 465
Cdd:cd16030 365 SLVPLLK-NPSAKWKDAAFSQYPRPSIM-----------GYS------------------IRT--ERYRYtEWVDFDK-V 411
|
490 500
....*....|....*....|....*
gi 29789239 466 VFVEVYNITADPDQITNIAKsiDPE 490
Cdd:cd16030 412 GAEELYDHKNDPNEWKNLAN--DPE 434
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
39-495 |
2.16e-48 |
|
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: 172.73 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAELGGMT--PLKKTKAL--IGEKGMTFSSAYVpSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKa 114
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHgnPILKTPNLdrLAAESVRFTNFHV-SPVCAPTRAALLTGRYPFRTGVWHTILGRERMRL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 wqkiqEPYTFPAILKSVcGYQTFFAGKYLN--EYG-APDAGGLE--------HIPLGWSYWyalekNSKYYNYTLSINGK 183
Cdd:cd16146 79 -----DETTLAEVFKDA-GYRTGIFGKWHLgdNYPyRPQDRGFDevlghgggGIGQYPDYW-----GNDYFDDTYYHNGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 184 ARKH-GenysvdYLTDVLANLSLDFLDyKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNvIAPRNKNFNIHGtnkhwli 262
Cdd:cd16146 148 FVKTeG------YCTDVFFDEAIDFIE-ENKDKPFFAYLATNAPHGPLQVPDKYLDPYKD-MGLDDKLAAFYG------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 263 rqaktpM-TNssirflddafrrrwqtllsVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGqfslpIDKR-------- 333
Cdd:cd16146 213 ------MiEN-------------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGG-----VPKRfnagmrgk 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 334 --QLYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKT-QMDGMSLLPILKGDrNLTWRSDVLVEYQ 409
Cdd:cd16146 263 kgSVYEGGHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGiKLDGRSLLPLLKGE-SDPWPERTLFTHS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 410 GEGRNVTDPTCPSlspGVsqcfpdcvcedaYNNTYACVRTLSSLWNLqycefddqevfvevYNITADPDQITNIAKSIdP 489
Cdd:cd16146 342 GRWPPPPKKKRNA---AV------------RTGRWRLVSPKGFQPEL--------------YDIENDPGEENDVADEH-P 391
|
....*.
gi 29789239 490 ELLGKM 495
Cdd:cd16146 392 EVVKRL 397
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-417 |
6.22e-47 |
|
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: 167.74 E-value: 6.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 37 RRPNVLLLLTDDQDAE----LGGM---TP-LKKtkaLIGEkGMTFSSAYVP----SALCCPSRASILTGKYphnhhvVNN 104
Cdd:cd16155 1 KKPNILFILADDQRADtigaLGNPeiqTPnLDR---LARR-GTSFTNAYNMggwsGAVCVPSRAMLMTGRT------LFH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 105 TLEGNCSSKAwqkiQEPYTFPAILKSVcGYQTFFAGKYLNEYgapdagglehiplgwsywyaleknskyynytlsingka 184
Cdd:cd16155 71 APEGGKAAIP----SDDKTWPETFKKA-GYRTFATGKWHNGF-------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 185 rkhgenysvdyltdvlANLSLDFL-DYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAPRNKNF-------NIHGT 256
Cdd:cd16155 108 ----------------ADAAIEFLeEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENFlpqhpfdNGEGT 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 257 NKHWLIrqAKTPMTNSSIRflddAFRRRWQTLLS-VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLpIDKRQL 335
Cdd:cd16155 172 VRDEQL--APFPRTPEAVR----QHLAEYYAMIThLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGL-MGKQNL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 336 YEFDIKVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTqMDGMSLLPILKGDrNLTWRSDVLVEYQGEGRNV 415
Cdd:cd16155 245 YEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPES-VEGKSLLPVIRGE-KKAVRDTLYGAYRDGQRAI 322
|
..
gi 29789239 416 TD 417
Cdd:cd16155 323 RD 324
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
39-395 |
3.23e-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: 161.21 E-value: 3.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDqdaeLG-------GMTPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGN 109
Cdd:cd16143 1 PNIVIILADD----LGygdiscyNPDSKIPTPNIdrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 110 CSSkawqkIQEP--YTFPAILKSVcGYQTFFAGKYlneygapdaggleHipLGWSyWYALEKNSKYYNYTLSIN-GKARK 186
Cdd:cd16143 77 SPP-----LIEPdrVTLAKMLKQA-GYRTAMVGKW-------------H--LGLD-WKKKDGKKAATGTGKDVDySKPIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 187 HGEN-YSVDY--------LTDVLANLSLDFLD-YKSNSEPFFMMISTPAPHSPWTAAPQYQKafqnviaprNKNFNIHGt 256
Cdd:cd16143 135 GGPLdHGFDYyfgipaseVLPTLTDKAVEFIDqHAKKDKPFFLYFALPAPHTPIVPSPEFQG---------KSGAGPYG- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 257 nkhwlirqaktpmtnssirfldDAfrrrwqtLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNG---YHTGQFSLPID-- 331
Cdd:cd16143 205 ----------------------DF-------VYELDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhd 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789239 332 --------KRQLYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQ-MDGMSLLPILKGD 395
Cdd:cd16143 256 psgplrgmKADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAaEDSFSFLPALLGP 329
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
39-400 |
1.24e-43 |
|
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: 160.07 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDqdaeLG-GMT-----PLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKyphnhHVVNNTLEGNC 110
Cdd:cd16145 1 PNIIFILADD----LGyGDLgcygqKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL-----HTGHTRVRGNS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 111 SSKAWQKIQEPY-TFPAILKSVcGYQTFFAGKYlnEYGAPDAGGLEHiPLGWSYWYA--------------LEKNSK--- 172
Cdd:cd16145 72 EPGGQDPLPPDDvTLAEVLKKA-GYATAAFGKW--GLGGPGTPGHPT-KQGFDYFYGyldqvhahnyypeyLWRNGEkvp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 173 ---YYNYTLSINGKARKHGENYSvdylTDVLANLSLDFLDyKSNSEPFFMMISTPAPHSPWtAAPQYQKAFQNVIAPRnk 249
Cdd:cd16145 148 lpnNVIPPLDEGNNAGGGGGTYS----HDLFTDEALDFIR-ENKDKPFFLYLAYTLPHAPL-QVPDDGPYKYKPKDPG-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 250 nfniHGTNKHWlirqaktpmtnssirfldDAFRRRWQTLLS-VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHT-GQFS 327
Cdd:cd16145 220 ----IYAYLPW------------------PQPEKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeGGSE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 328 LPID-----------KRQLYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLnKTQMDGMSLLPILKG- 394
Cdd:cd16145 278 HDPDffdsngplrgyKRSLYEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEP-PEDIDGISLLPTLLGk 356
|
410
....*....|.
gi 29789239 395 -----DRNLTW 400
Cdd:cd16145 357 pqqqqHDYLYW 367
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-415 |
3.47e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 148.07 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAELGGMT--PLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNtlegncsSKA 114
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYghPVVRTPNLdrLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDN-------ADP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 WQKiqEPYTFPAILKSVcGYQTFFAGKylneygapdagglehiplgwsywyaleknskyynytLSINGKARKHGENYsvd 194
Cdd:cd16037 74 YDG--DVPSWGHALRAA-GYETVLIGK------------------------------------LHFRGEDQRHGFRY--- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 195 ylTDVLANLSLDFL-DYKSNSEPFFMMISTPAPHSPWTAAPQyqkafqnviaprnknfnihgtnkHWlirqaktpmtnss 273
Cdd:cd16037 112 --DRDVTEAAVDWLrEEAADDKPWFLFVGFVAPHFPLIAPQE-----------------------FY------------- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 274 irfldDAFRRRWQT----LLS-VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLpIDKRQLYEFDIKVPLLVRG 348
Cdd:cd16037 154 -----DLYVRRARAayygLVEfLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGL-WGKSTMYEESVRVPMIISG 227
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789239 349 PGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQmDGMSLLPILKGDRNltWRSDVLVEYQGEGRNV 415
Cdd:cd16037 228 PGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-DGRSLLPLAEGPDD--PDRVVFSEYHAHGSPS 291
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
39-408 |
7.67e-40 |
|
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: 150.49 E-value: 7.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAE-LGGM-TPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCsska 114
Cdd:cd16028 1 RNVLFITADQWRADcLSCLgHPLVKTPNLdrLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 wqkiQEPyTFPAILKSVcGYQTFFAGKylNEYGAPDAGGLEHIPLGWSYWYALEKnskyYNYTLSINGKARKHGEnysVD 194
Cdd:cd16028 77 ----RHL-TLALELRKA-GYDPALFGY--TDTSPDPRGLAPLDPRLLSYELAMPG----FDPVDRLDEYPAEDSD---TA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 195 YLTDVLanlsLDFLDYKSNsEPFFMMISTPAPHSPWTAAPQYQKAFQN-VIAPRNKNFN------IHGTNKHWLIRQAKT 267
Cdd:cd16028 142 FLTDRA----IEYLDERQD-EPWFLHLSYIRPHPPFVAPAPYHALYDPaDVPPPIRAESlaaeaaQHPLLAAFLERIESL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 268 P--MTNSSIRFLDDAFRRRWQT----LLS-VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLpIDKRQLYEFDI 340
Cdd:cd16028 217 SfsPGAANAADLDDEEVAQMRAtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWL-WGKDGFFDQAY 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789239 341 KVPLLVRGPGIKPNQTSKMLVSN----IDLGPTILDLAGYDLnKTQMDGMSLLPILKGDRNLTWRSDVLVEY 408
Cdd:cd16028 296 RVPLIVRDPRREADATRGQVVDAftesVDVMPTILDWLGGEI-PHQCDGRSLLPLLAGAQPSDWRDAVHYEY 366
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-394 |
9.66e-38 |
|
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: 142.74 E-value: 9.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAE-LGGMTPLK-KTKAL--IGEKGMTFSSAYVpSALCCPSRASILTGKYPHNHHVVNNTLEgncsska 114
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYGGESyKTPNIdaLAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRNYVVFGYLD------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 wqkiQEPYTFPAILKSVcGYQTFFAGKY-LNEYGapdaGGLEHIP-LG---WSYWYALEKNSKYYNYTLSI----NGKAR 185
Cdd:cd16151 73 ----PKQKTFGHLLKDA-GYATAIAGKWqLGGGR----GDGDYPHeFGfdeYCLWQLTETGEKYSRPATPTfnirNGKLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 186 KHGENysvDYLTDVLANLSLDFLDYKSNsEPFFMMISTPAPHSPWTAAPQyqkafqnviaPRNKNFNIHGTNKHWlirqa 265
Cdd:cd16151 144 ETTEG---DYGPDLFADFLIDFIERNKD-QPFFAYYPMVLVHDPFVPTPD----------SPDWDPDDKRKKDDP----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 266 ktpmtnssIRFLDdafrrrwqTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPID------KRQLYEFD 339
Cdd:cd16151 205 --------EYFPD--------MVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTNGrevrggKGKTTDAG 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 29789239 340 IKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDL-NKTQMDGMSLLPILKG 394
Cdd:cd16151 269 THVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLpEDYPLDGRSFAPQLLG 325
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-407 |
3.73e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 138.52 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDQDAELGGM--TPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEgncssk 113
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCygQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 114 awqkiqepytFPAILKSVcgyqtffaGKYLNEYGapdagglehiplgwsYWYAleknskyynYTlsinGKArkHGENYSV 193
Cdd:cd16152 75 ----------LPADEKTL--------AHYFRDAG---------------YETG---------YV----GKW--HLAGYRV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 194 DYLTDvlanLSLDFLDYKSNSEPFFMMISTPAPHspwtaapqYQKAFQNVIAP-----RNKNFNIhgtnkhwlirqaktP 268
Cdd:cd16152 107 DALTD----FAIDYLDNRQKDKPFFLFLSYLEPH--------HQNDRDRYVAPegsaeRFANFWV--------------P 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 269 mtnssirflDD--AFRRRWQTLL--------SVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYH----TGQFslpidKRQ 334
Cdd:cd16152 161 ---------PDlaALPGDWAEELpdylgcceRLDENVGRIRDALKELGLYDNTIIVFTSDHGCHfrtrNAEY-----KRS 226
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789239 335 LYEFDIKVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTqMDGMSLLPILKGDRNlTWRSDVLVE 407
Cdd:cd16152 227 CHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEE-MQGRSLLPLVDGKVE-DWRNEVFIQ 297
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
39-412 |
7.38e-35 |
|
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: 133.86 E-value: 7.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAEL---GGMTPLK--KTKALIgEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSsk 113
Cdd:cd16032 1 PNILLIMADQLTAAAlpaYGNTVVKtpNLDRLA-ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPAD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 114 awqkiqEPyTFPAILKSVcGYQTFFAGKYlnEYGAPDagglehiplgwsywyaleknskyynytlsingkaRKHGENY-- 191
Cdd:cd16032 78 ------IP-TFAHYLRAA-GYRTALSGKM--HFVGPD----------------------------------QLHGFDYde 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 192 -----SVDYLTDvlanlsldfLDYKSNSEPFFMMISTPAPHSPWTAAPQYQkafqnviaprnknfnihgtnkHWLIRQAk 266
Cdd:cd16032 114 evafkAVQKLYD---------LARGEDGRPFFLTVSFTHPHDPYVIPQEYW---------------------DLYVRRA- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 267 tpmtnssirflddafRRRWQTLLS-VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPIdKRQLYEFDIKVPLL 345
Cdd:cd16032 163 ---------------RRAYYGMVSyVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWY-KMSFFEGSARVPLI 226
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789239 346 VRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNK--TQMDGMSLLPILKGDRNLtWRSDVLVEYQGEG 412
Cdd:cd16032 227 ISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPhvPPLDGRSLLPLLEGGDSG-GEDEVISEYLAEG 294
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-397 |
1.06e-33 |
|
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: 132.30 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDQ---DAELGGmTPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPH---NHHVVNNTlegn 109
Cdd:cd16026 1 KPNIVVILADDLgygDLGCYG-SPLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVrvgLPGVVGPP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 110 csskaWQKI---QEPYTFPAILKSvCGYQTFFAGKYlneygapDAGGL-EHIPL--GWSYWYAL-----EKNSKYYNYTL 178
Cdd:cd16026 76 -----GSKGglpPDEITIAEVLKK-AGYRTALVGKW-------HLGHQpEFLPTrhGFDEYFGIpysndMWPFPLYRNDP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 179 SINGKARkhGENYSVDYLTDVLANLSLDFLD------YKSNSEPFFMMISTPAPHSPWTAAPqyqkafqnviaprnknfn 252
Cdd:cd16026 143 PGPLPPL--MENEEVIEQPADQSSLTQRYTDeavdfiERNKDQPFFLYLAHTMPHVPLFASE------------------ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 253 ihgtnkhwlirqaktpmtnssirflDDAFRRRWQ----TLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNG-----YHT 323
Cdd:cd16026 203 -------------------------KFKGRSGAGlygdVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwleyGGH 257
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789239 324 GQFSLPID--KRQLYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQM-DGMSLLPILKGDRN 397
Cdd:cd16026 258 GGSAGPLRggKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDRViDGKDISPLLLGGSK 335
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-505 |
4.65e-33 |
|
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: 130.82 E-value: 4.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAE-LGGM-TPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHnhhvVNntleGNCSSKA 114
Cdd:cd16150 1 PNIVIFVADQLRADsLGHLgNPAAVTPNLdaLAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPH----VN----GHRTLHH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 WQKIQEPyTFPAILKSVcGYQTFFAGK--YLNEYGAPDAgglehiplgwsywyaleknskyynYTLSingkarkhgenys 192
Cdd:cd16150 73 LLRPDEP-NLLKTLKDA-GYHVAWAGKndDLPGEFAAEA------------------------YCDS------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 193 vDYLTdvlANLSLDFLDYKSNSEPFFMMISTPAPHSPWTA-APQYQKAFQNVIAPRNKNFNIHGTNKHWLIRqaktpMTN 271
Cdd:cd16150 114 -DEAC---VRTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVeEPWFSMIDREKLPPRRPPGLRAKGKPSMLEG-----IEK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 272 SSIRFLDDAfrrRWQTLLSV--------DDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLpIDKRQ--LYEFDIK 341
Cdd:cd16150 185 QGLDRWSEE---RWRELRATylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGL-VEKWPntFEDCLTR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 342 VPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQMdGMSLLPILKGDRnLTWRSDVLVEyqGeGRNVTDPTCP 421
Cdd:cd16150 261 VPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGET-EEHRDAVFSE--G-GRLHGEEQAM 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 422 SLSPGVSQCFPDC--VCEDAYNNTYAC-VRTLSslWNLQYCEFDDQevfvEVYNITADPDQITNIAKsiDP---ELLGKM 495
Cdd:cd16150 336 EGGHGPYDLKWPRllQQEEPPEHTKAVmIRTRR--YKYVYRLYEPD----ELYDLEADPLELHNLIG--DPayaEIIAEM 407
|
490
....*....|..
gi 29789239 496 NYRLM--MLQSC 505
Cdd:cd16150 408 KQRLLrwMVETS 419
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
38-395 |
1.12e-32 |
|
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: 129.10 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDqdaeLG----GM------TP-LKKtkalIGEKGMTFSSAYVpSALCCPSRASILTGkypHNHHVVNNtl 106
Cdd:cd16025 2 RPNILLILADD----LGfsdlGCfggeipTPnLDA----LAAEGLRFTNFHT-TALCSPTRAALLTG---RNHHQVGM-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 107 eGNCSskAWQKIQEPY---------TFPAILKSVcGYQTFFAGKYlneygapdaggleHipLGwsywyaleknskyynyt 177
Cdd:cd16025 68 -GTMA--ELATGKPGYegylpdsaaTIAEVLKDA-GYHTYMSGKW-------------H--LG----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 178 lsingkarkhGENYsvdYLTDVLANLSLDFLD-YKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQ-------NVIapRNK 249
Cdd:cd16025 112 ----------PDDY---YSTDDLTDKAIEYIDeQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKgkydagwDAL--REE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 250 NFNihgtnkhwliRQ-------AKTPMT--NSSIRFLDD--AFRRRWQTLL---------SVDDLVEKLVKRLDSTGELD 309
Cdd:cd16025 177 RLE----------RQkelglipADTKLTprPPGVPAWDSlsPEEKKLEARRmevyaamveHMDQQIGRLIDYLKELGELD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 310 NTYIFYTSDNG--YHTG--QFS---LPIDKRQLYEFDIKVPLLVRGPG--IKPNQTSKMLVSNIDLGPTILDLAGYDLNK 380
Cdd:cd16025 247 NTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKgiKAKGGIRHQFAHVIDIAPTILELAGVEYPK 326
|
410 420
....*....|....*....|..
gi 29789239 381 T-------QMDGMSLLPILKGD 395
Cdd:cd16025 327 TvngvpqlPLDGVSLLPTLDGA 348
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
68-390 |
2.22e-32 |
|
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: 125.35 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 68 EKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEgncsskawqkiQEPYTFPAILKSVcGYQTFfagkylneyG 147
Cdd:cd16148 34 AEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLE-----------PDDPTLAEILRKA-GYYTA---------A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 148 APDAGgleHIPLGWSYWyaleknsKYYNYTLSINGKARKHGEN--YSVDYLTDVLanlsLDFLDYKSNSEPFFMMISTPA 225
Cdd:cd16148 93 VSSNP---HLFGGPGFD-------RGFDTFEDFRGQEGDPGEEgdERAERVTDRA----LEWLDRNADDDPFFLFLHYFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 226 PHSPWtaapQYQkafqnviaprnknfnihgtnkhwlirqaktpmtnSSIRFlddafrrrwqtllsVDDLVEKLVKRLDST 305
Cdd:cd16148 159 PHEPY----LYD----------------------------------AEVRY--------------VDEQIGRLLDKLKEL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 306 GELDNTYIFYTSDNG--------YHTGQFSLpidkrqlYEFDIKVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYD 377
Cdd:cd16148 187 GLLEDTLVIVTSDHGeefgehglYWGHGSNL-------YDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVE 259
|
330
....*....|...
gi 29789239 378 LNKTqMDGMSLLP 390
Cdd:cd16148 260 PPDY-SDGRSLLP 271
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-378 |
4.03e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 121.19 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDA-ELGG-MTPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNcssKA 114
Cdd:cd16149 1 PNILFILTDDQGPwALGCyGNSEAVTPNLdrLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGS---HG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 WQKIQEPY-----TFPAILKSVcGYQTFFAGKYlneygapdaggleHIplgwsywyaleknskyynytlsingkarkhGE 189
Cdd:cd16149 78 KTKKPEGYlegqtTLPEVLQDA-GYRCGLSGKW-------------HL------------------------------GD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 190 NysvdyltdvlanlSLDFL-DYKSNSEPFFMMISTPAPHSPWtaapQYQKAfqnviaprnknfnihgtnkhwlirqaktp 268
Cdd:cd16149 114 D-------------AADFLrRRAEAEKPFFLSVNYTAPHSPW----GYFAA----------------------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 269 mtnssirflddafrrrwqtLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQ----------FSLpidkrQLYEF 338
Cdd:cd16149 148 -------------------VTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHhgiwgkgngtFPL-----NMYDN 203
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 29789239 339 DIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDL 378
Cdd:cd16149 204 SVKVPFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDP 244
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
39-408 |
1.37e-28 |
|
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: 118.64 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAE-LGGMTPLK-KTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNhhvvnNTLEGNCSSKA 114
Cdd:cd16156 1 KQFIFIMTDTQRWDmVGCYGNKAmKTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT-----NGSWTNCMALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 115 wQKIQepyTFPAILKSVcGYQTFFAGKYLNEYGapDAGGLEHIPLGW--SYWYALEknskyyNY---------TLSINGK 183
Cdd:cd16156 76 -DNVK---TIGQRLSDN-GIHTAYIGKWHLDGG--DYFGNGICPQGWdpDYWYDMR------NYldelteeerRKSRRGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 184 ARKHGENYSVDY-LTDVLANLSLDFLDyKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAPRNKNFNIHGTNKHWLI 262
Cdd:cd16156 143 TSLEAEGIKEEFtYGHRCTNRALDFIE-KHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAYDDLENKPLHQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 263 RQAKTPMtnssiRFLD-DAFRRRWQTLLS----VDDLVEKLVKRLDSTGEldNTYIFYTSDNGYHTGQFSLPIDKRQLYE 337
Cdd:cd16156 222 RLWAGAK-----PHEDgDKGTIKHPLYFGcnsfVDYEIGRVLDAADEIAE--DAWVIYTSDHGDMLGAHKLWAKGPAVYD 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789239 338 FDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKtQMDGMSLLPILKgDRNLTWRSDVLVEY 408
Cdd:cd16156 295 EITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPK-VLEGESILATIE-DPEIPENRGVFVEF 364
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-408 |
1.61e-28 |
|
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: 115.38 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQ-----------DAELGGMTPLKKTkaligekGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTle 107
Cdd:cd16035 1 PNILLILTDQErypppwpagwaALNLPARERLAAN-------GLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 108 gncsSKAWQKiQEPYTFPAI---LKSVcGYQTFFAGKylneygapdagglehiplgwsyWYALEKNSKYYNYTLSINGKA 184
Cdd:cd16035 72 ----GSPMQP-LLSPDVPTLghmLRAA-GYYTAYKGK----------------------WHLSGAAGGGYKRDPGIAAQA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 185 rkhgenysVDYLTDVLANlsldfldyKSNSEPFFMMISTPAPH---SPWTAAPQYQkafqnviapRNKNFnihgtnKHWL 261
Cdd:cd16035 124 --------VEWLRERGAK--------NADGKPWFLVVSLVNPHdimFPPDDEERWR---------RFRNF------YYNL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 262 IRQaktpmtnssirflddafrrrwqtllsVDDLVEKLVKRLDSTGELDNTYIFYTSDNG----YHTGqfslpidKRQ--- 334
Cdd:cd16035 173 IRD--------------------------VDRQIGRVLDALDASGLADNTIVVFTSDHGemggAHGL-------RGKgfn 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 335 LYEFDIKVPLLVRGPGIKPN-QTSKMLVSNIDLGPTILDLAGYDLNKTQMD-----GMSLLPILKGDRNLTWRSDVLVEY 408
Cdd:cd16035 220 AYEEALHVPLIISHPDLFGTgQTTDALTSHIDLLPTLLGLAGVDAEARATEapplpGRDLSPLLTDADADAVRDGILFTY 299
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
39-396 |
1.80e-28 |
|
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: 116.88 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQ---DAELGGmTPLKKT---KALIGEkGMTFSSAYVpSALCCPSRASILTGKYPHNH---HVVNNTLEGN 109
Cdd:cd16029 1 PHIVFILADDLgwnDVGFHG-SDQIKTpnlDALAAD-GVILNNYYV-QPICTPSRAALMTGRYPIHTgmqHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 110 CSSKawqkiqEPYTFPAILKSvCGYQTFFAGKYLNEYGAPdagglEHIPLG----------------WSYWYALEKNskY 173
Cdd:cd16029 78 GLPL------NETLLPQYLKE-LGYATHLVGKWHLGFYTW-----EYTPTNrgfdsfygyyggaedyYTHTSGGAND--Y 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 174 YNYTLSINGKARKHGENysvDYLTDVLANLSLDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAprnknfNI 253
Cdd:cd16029 144 GNDDLRDNEEPAWDYNG---TYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFA------HI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 254 HGTNkhwlirqaktpmtnssirflddafRRRWQTLLS-VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSL---- 328
Cdd:cd16029 215 KDED------------------------RRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsny 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789239 329 PI--DKRQLYEFDIKVPLLVRGPGIKPN--QTSKMLVSNIDLGPTILDLAGYDLN-KTQMDGMSLLPILKGDR 396
Cdd:cd16029 271 PLrgGKNTLWEGGVRVPAFVWSPLLPPKrgTVSDGLMHVTDWLPTLLSLAGGDPDdLPPLDGVDQWDALSGGA 343
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-413 |
4.54e-28 |
|
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: 115.52 E-value: 4.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQ----DAELGGMTPLKKTKAL--IGEKGMTFSSAYVPSAlCCPSRASILTGKYPHNHHVvnNTLEGNCSS 112
Cdd:cd16154 1 PNILLIIADDQgldsSAQYSLSSDLPVTPTLdsLANSGIVFDNLWATPA-CSPTRATILTGKYGFRTGV--LAVPDELLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 113 kawqkiqEPYTFPAILKS---VCGYQTFFAGKYL---NEYGAPDAGGLEHiplgwsYWYALEKN-SKYYNYTLSINGKAR 185
Cdd:cd16154 78 -------SEETLLQLLIKdatTAGYSSAVIGKWHlggNDNSPNNPGGIPY------YAGILGGGvQDYYNWNLTNNGQTT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 186 KHGEnysvdYLTDVLANLSLDFLDykSNSEPFFMMISTPAPHSPWTAAPQyqkafqnviaprnknfNIHGTnkhwlirqa 265
Cdd:cd16154 145 NSTE-----YATTKLTNLAIDWID--QQTKPWFLWLAYNAPHTPFHLPPA----------------ELHSR--------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 266 ktpmTNSSIRFLDDAFRRRW--QTLLSVDDLVEKLVKRLDSTgELDNTYIFYTSDNGyhT-GQ-----FSLPIDKRQLYE 337
Cdd:cd16154 193 ----SLLGDSADIEANPRPYylAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNG--TpGQvvdlpYTRNHAKGSLYE 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789239 338 FDIKVPLLVRGPGI-KPNQTSKMLVSNIDLGPTILDLAGYDLNKtQMDGMSLLPILKgDRNLTWRSDVLVEYQGEGR 413
Cdd:cd16154 266 GGINVPLIVSGAGVeRANERESALVNATDLYATIAELAGVDAAE-IHDSVSFKPLLS-DVNASTRQYNYTEYESPTT 340
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
38-392 |
3.16e-27 |
|
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: 114.45 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDQD----AELGGMTPLKKTKALIGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNntleGNCSSK 113
Cdd:cd16160 1 KPNIVLFFADDMGygdlASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG----GTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 114 AWQKIQEPY---TFPAILKSVcGYQTFFAGKY---LNEYGAPDAGGLEH----------IPLG-------WSYWYALEKN 170
Cdd:cd16160 77 PWDIGGLPKtevTMAEALKEA-GYTTGMVGKWhlgINENNHSDGAHLPShhgfdfvgtnLPFTnswacddTGRHVDFPDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 171 SK---YYNYTlsINGKARKHgenysvDYLTDVLANLSLDFLdYKSNSEPFFMMISTPAPHSPWTAAPQYQkafqnviapr 247
Cdd:cd16160 156 SAcflYYNDT--IVEQPIQH------EHLTETLVGDAKSFI-EDNQENPFFLYFSFPQTHTPLFASKRFK---------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 248 nknfnihgtnkhwlirqaktpmtNSSIR--FLDDAFRRRWQtllsvddlVEKLVKRLDSTGELDNTYIFYTSDNGYH--- 322
Cdd:cd16160 217 -----------------------GKSKRgrYGDNINEMSWA--------VGEVLDTLVDTGLDQNTLVFFLSDHGPHvey 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789239 323 --TGQFSLPID--KRQLYEFDIKVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDL-NKTQMDGMSLLPIL 392
Cdd:cd16160 266 clEGGSTGGLKggKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLpTDRIYDGLSITDLL 340
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
38-401 |
7.07e-26 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 110.91 E-value: 7.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDQDAE-LGGM-TPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNntlEGNCSSK 113
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgNKAVETPNLdmLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG---YGDVVPW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 114 AWqkiqePYTFPAILKSVcGYQTFFAGKyLNEYGAPDAGGLEHIPL--GWS------------------YWY---ALEKN 170
Cdd:PRK13759 83 NY-----KNTLPQEFRDA-GYYTQCIGK-MHVFPQRNLLGFHNVLLhdGYLhsgrnedksqfdfvsdylAWLrekAPGKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 171 SKYYNYTLSING-KAR--KHGENYsvdYLTDVLANLSLDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAPr 247
Cdd:PRK13759 156 PDLTDIGWDCNSwVARpwDLEERL---HPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADIP- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 248 nkNFNIHGTNKHW-LIRQAKTPMTnSSIRFLDDAFRRRWQTLLS----VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYH 322
Cdd:PRK13759 232 --DPHIGDWEYAEdQDPEGGSIDA-LRGNLGEEYARRARAAYYGlithIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 323 TGQFSLpIDKRQLYEFDIKVPLLVRGPG--IKPN--QTSKMLVSNIDLGPTILDLAGYDLNKTqMDGMSLLPILKGDRNl 398
Cdd:PRK13759 309 LGDHYL-FRKGYPYEGSAHIPFIIYDPGglLAGNrgTVIDQVVELRDIMPTLLDLAGGTIPDD-VDGRSLKNLIFGQYE- 385
|
...
gi 29789239 399 TWR 401
Cdd:PRK13759 386 GWR 388
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
39-395 |
6.02e-24 |
|
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: 103.38 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDD----------QDAELGGMTP-LKKtkalIGEKGMTFSSAYV-PSalCCPSRASILTGKYPhNHHvvnntl 106
Cdd:cd16142 1 PNILVILGDDigwgdlgcygGGIGRGAPTPnIDR----LAKEGLRFTSFYVePS--CTPGRAAFITGRHP-IRT------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 107 egNCSSKAWQKI-----QEPYTFPAILKSVcGYQTFFAGKylNEYGAPDagglEHIPL--GWSYWYAleknskYYNYTLs 179
Cdd:cd16142 68 --GLTTVGLPGSpgglpPWEPTLAELLKDA-GYATAQFGK--WHLGDED----GRLPTdhGFDEFYG------NLYHTI- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 180 ingkarkhgENYSVDYltdvlanlSLDFLD-YKSNSEPFFMMISTPAPHSPWTAAPQYQkafqnviaprnknfnihGTNK 258
Cdd:cd16142 132 ---------DEEIVDK--------AIDFIKrNAKADKPFFLYVNFTKMHFPTLPSPEFE-----------------GKSS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 259 HWlirqaktpmtnssIRFLDdafrrrwqTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHtgQFSLPI-------- 330
Cdd:cd16142 178 GK-------------GKYAD--------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGPE--QDVWPDggytpfrg 234
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789239 331 DKRQLYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDL-------NKTQMDGMSLLPILKGD 395
Cdd:cd16142 235 EKGTTWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDpkdkllgKDRHIDGVDQSPFLLGK 307
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
38-394 |
1.36e-23 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 102.55 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDD---QDAELGGMTPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYPhnhhvVNNTLEGNCSS 112
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLG-----LRNGVGHNFLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 113 KAWQKIQ-EPYTFPAILKSVcGYQTFFAGKY-LNEYGApdaggleHIPlgwsywyalekNSKYYNYTLSINgkarkhgen 190
Cdd:cd16161 76 TSVGGLPlNETTLAEVLRQA-GYATGMIGKWhLGQREA-------YLP-----------NSRGFDYYFGIP--------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 191 YSVD-YLTDVLANLSLDFLDYKSNS-EPFFMMISTPAPHSPWTAAPQYQkafqnviaprnknfnihgtnkhwlirqaktP 268
Cdd:cd16161 128 FSHDsSLADRYAQFATDFIQRASAKdRPFFLYAALAHVHVPLANLPRFQ------------------------------S 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 269 MTNSSIRFLDdafrrrwqTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNG---------------YHTGQFSLPIDKR 333
Cdd:cd16161 178 PTSGRGPYGD--------ALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelavgpgtgDWQGNLGGSVAKA 249
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789239 334 QLYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQM-DGMSLLPILKG 394
Cdd:cd16161 250 STWEGGHREPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGRIyDGKDLSPVLFG 312
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-388 |
1.54e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 97.45 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDQDAE----LGGMTPLKKTKAL----------IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVN 103
Cdd:cd16153 1 KPNILWIITDDQRVDslscYNNAHTGKSESRLgyvespnidaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 104 NtlegncsSKAWQKIQEPY-TFPAILKsVCGYQTFFAGKylneygapdagglEHIplgwsYWYALEKNSKYYNYTLSING 182
Cdd:cd16153 81 F-------EAAHPALDHGLpTFPEVLK-KAGYQTASFGK-------------SHL-----EAFQRYLKNANQSYKSFWGK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 183 KARKhgenysvdyltdvlanlsldfldyKSNSEPFFMMISTPAPHSPwtaapqyqkafqnVIAPrnknfnihgtnKHWli 262
Cdd:cd16153 135 IAKG------------------------ADSDKPFFVRLSFLQPHTP-------------VLPP-----------KEF-- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 263 RQaktpmtnssiRFLDDAFrrrwqtLLSVDDLVEKLVKRLDSTGEL---DNTYIFYTSDNGYHTGQFSLpIDKRQLYEFD 339
Cdd:cd16153 165 RD----------RFDYYAF------CAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGI-LAKFTFWPQS 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 29789239 340 IKVPLLVRGPGIKPNQTSKM---LVSNIDLGPTILDLAGYDLNK-TQMDGMSL 388
Cdd:cd16153 228 HRVPLIVVSSDKLKAPAGKVrhdFVEFVDLAPTLLAAAGVDVDApDYLDGRDL 280
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-397 |
2.93e-22 |
|
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: 99.85 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDQD-AELGGM-TPLKKTKAL--IGEKGMTFSSAYVPSALCCPSRASILTGKYP-HNHHVVNNTLEGNcsS 112
Cdd:cd16157 1 KPNIILMLMDDMGwGDLGVFgEPSRETPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPiRNGFYTTNAHARN--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 113 KAWQKI-----QEPYTFPAILKSVcGYQTFFAGKY--------------LNE--------YGAPDAGGLEHIPLgWSYWy 165
Cdd:cd16157 79 YTPQNIvggipDSEILLPELLKKA-GYRNKIVGKWhlghrpqyhplkhgFDEwfgapnchFGPYDNKAYPNIPV-YRDW- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 166 alEKNSKYYNyTLSINgkaRKHGENYsvdyLTDVLANLSLDFLDYKSNS-EPFFMMISTPAPHSPWTAAPQYQkafqnvi 244
Cdd:cd16157 156 --EMIGRYYE-EFKID---KKTGESN----LTQIYLQEALEFIEKQHDAqKPFFLYWAPDATHAPVYASKPFL------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 245 aprnknfnihGTNKHWLIRQAktpmtnssIRFLDDAfrrrwqtllsvddlVEKLVKRLDSTGELDNTYIFYTSDNGYHTg 324
Cdd:cd16157 219 ----------GTSQRGLYGDA--------VMELDSS--------------VGKILESLKSLGIENNTFVFFSSDNGAAL- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 325 qFSLPID----------KRQLYEFDIKVPLLVRGPG-IKPNQTSKMLVSNIDLGPTILDLAGYDLNK-TQMDGMSLLPIL 392
Cdd:cd16157 266 -ISAPEQggsngpflcgKQTTFEGGMREPAIAWWPGhIKPGQVSHQLGSLMDLFTTSLALAGLPIPSdRAIDGIDLLPVL 344
|
....*
gi 29789239 393 KGDRN 397
Cdd:cd16157 345 LNGKE 349
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
39-392 |
5.56e-20 |
|
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: 92.89 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQD-AELG------GMTP-LKKTKAligeKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNc 110
Cdd:cd16158 2 PNIVLLFADDLGyGDLGcyghpsSSTPnLDRLAA----NGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 111 sSKAWQKIQEpYTFPAILKSVcGYQTFFAGKYlneygapdaggleHIPLGwsywyaleKNSKYynytLSIN-GKARKHGE 189
Cdd:cd16158 77 -SRGGLPLNE-TTIAEVLKTV-GYQTAMVGKW-------------HLGVG--------LNGTY----LPTHqGFDHYLGI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 190 NYSVDY-----LTDVLANLSLDFL--DYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAP---RNKNFNIHGTNKH 259
Cdd:cd16158 129 PYSHDQgpcqnLTCFPPNIPCFGGcdQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADnakEGKPFFLYYASHH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 260 WLIRQ-AKTPMTNSSIR--FLDdafrrrwqTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFS-------LP 329
Cdd:cd16158 209 THYPQfAGQKFAGRSSRgpFGD--------ALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSrggnaglLK 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789239 330 IDKRQLYEFDIKVPLLVRGPG-IKPNQTSKmLVSNIDLGPTILDLAGYDLNKTQMDGMSLLPIL 392
Cdd:cd16158 281 CGKGTTYEGGVREPAIAYWPGrIKPGVTHE-LASTLDILPTIAKLAGAPLPNVTLDGVDMSPIL 343
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
39-392 |
2.96e-17 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 83.36 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDDQDAELGGMtPLKKTKAL-----IGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSK 113
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFR-PGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 114 AWQKIQEPYtfpailksvcGYQTffagkylNEYGAPDAGGLEHiplgwSYWYALEKNSKYYNYTLSINGK-------ARK 186
Cdd:cd16171 80 TWMDRLEKH----------GYHT-------QKYGKLDYTSGHH-----SVSNRVEAWTRDVPFLLRQEGRptvnlvgDRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 187 HGENYSVDY-LTDVLANLSLDflDYKSNSEPFFMMISTPAPHsPWtAAPQYQKAFQNViapRNknfnihgtnkhwlIRQA 265
Cdd:cd16171 138 TVRVMLKDWqNTDKAVHWIRK--EAPNLTQPFALYLGLNLPH-PY-PSPSMGENFGSI---RN-------------IRAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 266 KTPMTNSSirflddafrrrwqtllsvDDLVEKLVKRLDSTGELDNTYIFYTSDNGyhtgqfSLPIDKRQ-----LYEFDI 340
Cdd:cd16171 198 YYAMCAET------------------DAMLGEIISALKDTGLLDKTYVFFTSDHG------ELAMEHRQfykmsMYEGSS 253
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 29789239 341 KVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTqMDGMSLLPIL 392
Cdd:cd16171 254 HVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN-LSGYSLLPLL 304
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
38-394 |
4.59e-17 |
|
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: 84.26 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 38 RPNVLLLLTDDqdaeLG-------GMTPLKKTKA-LIGEKGMTFSSAYVPSALCCPSRASILTGKYP------HNHHVVN 103
Cdd:cd16159 1 KPNIVLFMADD----LGigdvgcfGNDTIRTPNIdRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirsgmaSSHGMRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 104 NTLEGNCSSKAWQKIqepyTFPAILKSVcGYQTFFAGKYLNEYGAPDAGGLEHIPL--GWSYwyaleknskYYNYTLSiN 181
Cdd:cd16159 77 ILFTASSGGLPPNET----TFAEVLKQQ-GYSTALIGKWHLGLHCESRNDFCHHPLnhGFDY---------FYGLPLT-N 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 182 GKARKHGENYSVDYLTD---------VLANLSLDFLDYKSNSEP----FFMMISTPAPHSPWTAAPQYQKAFqNVIAPRN 248
Cdd:cd16159 142 LKDCGDGSNGEYDLSFDplfplltafVLITALTIFLLLYLGAVSkrffVFLLILSLLFISLFFLLLITNRYF-NCILMRN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 249 knfnihgtnkHWLIRQaktPM---------TNSSIRFLDDAFRRRWQTLLS----------------------------- 290
Cdd:cd16159 221 ----------HEVVEQ---PMslenltqrlTKEAISFLERNKERPFLLVMSflhvhtalftskkfkgrskhgrygdnvee 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 291 VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQfslpIDKRQLYE--------------FD--IKVPLLVRGPG-IKP 353
Cdd:cd16159 288 MDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEE----ISVGGEYGggnggiyggkkmggWEggIRVPTIVRWPGvIPP 363
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 29789239 354 NQTSKMLVSNIDLGPTILDLAGYDL-NKTQMDGMSLLPILKG 394
Cdd:cd16159 364 GSVIDEPTSLMDIFPTVAALAGAPLpSDRIIDGRDLMPLLTG 405
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
39-375 |
1.47e-14 |
|
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: 74.26 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLL-----TDDQDAELGGMTPLKKTKALIgEKGMTFSSAYVPSALCCPSRA--SILTGKYPhnhhvvnntLEGNCS 111
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLA-KEGLYFGNFYSPGFGGGTANGefEVLTGLPP---------LPLGSG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 112 SKAWQKIQEPYTFPAILKSvCGYQTFFAgkylneYGapdagglehiplGWSYWYALEKNSKYYNYTLSINGKA-RKHGEN 190
Cdd:cd16015 71 SYTLYKLNPLPSLPSILKE-QGYETIFI------HG------------GDASFYNRDSVYPNLGFDEFYDLEDfPDDEKE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 191 YSVDYLTD-VLANLSLDFLDyKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAPRNKNFNIHgtnkhwlirqaktpm 269
Cdd:cd16015 132 TNGWGVSDeSLFDQALEELE-ELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTELENYL--------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 270 tnSSIRFLDDAFrrrwqtllsvddlvEKLVKRLDSTGELDNTYIFYTSDngyHTGQFSLPIDKRQLYEFDI-KVPLLVRG 348
Cdd:cd16015 196 --NAIHYTDKAL--------------GEFIEKLKKSGLYENTIIVIYGD---HLPSLGSDYDETDEDPLDLyRTPLLIYS 256
|
330 340
....*....|....*....|....*..
gi 29789239 349 PGIKPNQTSKMLVSNIDLGPTILDLAG 375
Cdd:cd16015 257 PGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
34-389 |
5.72e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 74.69 E-value: 5.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 34 GAARRPNVLLL----LTD---DQDAELGGMTP-LKKtkalIGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNT 105
Cdd:COG1368 230 GPAKKPNVVVIllesFSDffiGALGNGKDVTPfLDS----LAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 106 LEGNcsskawqkiqEPYTFPAILKSVcGYQTFFAgkylneYGapdagglehiplGWSYWYALEKNSKY--YNYTLSINGK 183
Cdd:COG1368 306 PGQN----------NFPSLPSILKKQ-GYETSFF------HG------------GDGSFWNRDSFYKNlgFDEFYDREDF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 184 ARKHGENYSV-DyltDVLANLSLDFLDykSNSEPFFMMISTPAPHSPWTAAPQYQKafqnviaprnknfnIHGTNKHWLI 262
Cdd:COG1368 357 DDPFDGGWGVsD---EDLFDKALEELE--KLKKPFFAFLITLSNHGPYTLPEEDKK--------------IPDYGKTTLN 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 263 RQAKTpmtnssIRFLDDAfrrrwqtllsvddlVEKLVKRLDSTGELDNTYIFYTSDngyHTGqfslPIDKRQLYEFDI-- 340
Cdd:COG1368 418 NYLNA------VRYADQA--------------LGEFIEKLKKSGWYDNTIFVIYGD---HGP----RSPGKTDYENPLer 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 29789239 341 -KVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQMDGMSLL 389
Cdd:COG1368 471 yRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLL 520
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
39-374 |
5.70e-13 |
|
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: 68.60 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 39 PNVLLLLTDD-QDAELGGMTPLKKTKALIGEKGMTFSSAYV----PSALCCPSRASILTGKYPHNHhvvnntlegncssk 113
Cdd:cd00016 1 KHVVLIVLDGlGADDLGKAGNPAPTTPNLKRLASEGATFNFrsvsPPTSSAPNHAALLTGAYPTLH-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 114 awqkiqePYTFPailksvcgyqtffaGKYLNEYGAPDAGGLEHIPlgwsywyaleknskyynytlSINGKARKHGenysv 193
Cdd:cd00016 67 -------GYTGN--------------GSADPELPSRAAGKDEDGP--------------------TIPELLKQAG----- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 194 dYLTDVLANLslDFLDYKSNSEPFFMMISTPAPHSPWtaapqyqkafqnviaprnknfnihgtnkhwlirQAKTPMTNSS 273
Cdd:cd00016 101 -YRTGVIGLL--KAIDETSKEKPFVLFLHFDGPDGPG---------------------------------HAYGPNTPEY 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 274 IrflddafrrrwQTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNG---YHTGQFSLPIDKRQLYEFDIKVPLLVRGPG 350
Cdd:cd00016 145 Y-----------DAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPG 213
|
330 340
....*....|....*....|....
gi 29789239 351 IKPNQTSKMLVSNIDLGPTILDLA 374
Cdd:cd00016 214 VKKGGVKHELISQYDIAPTLADLL 237
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
205-371 |
1.41e-07 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 54.14 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 205 LDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNviaprnKNFNIHGTNKHwlirqaktpmtnssirFLDDAFRRR 284
Cdd:COG3083 371 LQWLDQRDSDRPWFSYLFLDAPHAYSFPADYPKPFQPS------EDCNYLALDNE----------------SDPTPFKNR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 285 WQT-LLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGY-----------HTGQFSlpidkrqlyEFDIKVPLLVRGPGIK 352
Cdd:COG3083 429 YRNaVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS---------RYQLQVPLVIHWPGTP 499
|
170
....*....|....*....
gi 29789239 353 PNQTSKMlVSNIDLGPTIL 371
Cdd:COG3083 500 PQVISKL-TSHLDIVPTLM 517
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
84-375 |
6.96e-06 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 47.96 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 84 CPSRASILTGKYPHNHHVVNNTLegncsskaWQ-KIQEPYTFPAilksvcgyqTFFAGKYlneYGAPdagglehiPLgws 162
Cdd:cd16018 47 FPNHYSIVTGLYPESHGIVGNYF--------YDpKTNEEFSDSD---------WVWDPWW---IGGE--------PI--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 163 yWYALEKNS-------------KYYNYTLSINGKARKHGENYSVDYLTDVLANLsldfLDYKSNSEPFFMMISTPAP--- 226
Cdd:cd16018 96 -WVTAEKAGlktasyfwpgsevAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTI----LEWLDLERPDLILLYFEEPdsa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 227 -HSpwtaapqyqkafqnviaprnknfniHGTNKHwlirqaktpmtnssirflddafrRRWQTLLSVDDLVEKLVKRLDST 305
Cdd:cd16018 171 gHK-------------------------YGPDSP-----------------------EVNEALKRVDRRLGYLIEALKER 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789239 306 GELDNTYIFYTSDNGYHT----GQFSlpidkrqlYEFDIKVPLLVRGPGIKPNQTSKMLvSNIDLGPTILDLAG 375
Cdd:cd16018 203 GLLDDTNIIVVSDHGMTDvgthGYDN--------ELPDMRAIFIARGPAFKKGKKLGPF-RNVDIYPLMCNLLG 267
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
35-375 |
3.57e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 42.81 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 35 AARRPNVLLLLTDdqdaelgGMTP--LKKT-----KALIgEKGMTFSSAY--VPSaLCCPSRASILTGKYPHNHHVVNNT 105
Cdd:COG1524 20 APPAKKVVLILVD-------GLRAdlLERAhapnlAALA-ARGVYARPLTsvFPS-TTAPAHTTLLTGLYPGEHGIVGNG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 106 LEGNCSSKAWQKIQEPYTFPAILKSVcGYQTFFagkylnEYgAPDAGglehIPLGWSYWYALEkNSKYYNYTL--SINGK 183
Cdd:COG1524 91 WYDPELGRVVNSLSWVEDGFGSNSLL-PVPTIF------ER-ARAAG----LTTAAVFWPSFE-GSGLIDAARpyPYDGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 184 ARKHGENYSVDYLTDVLANLSldfldykSNSEPFFMMISTPAP------HSPwtAAPQYQKAFQNV---IA--------- 245
Cdd:COG1524 158 KPLLGNPAADRWIAAAALELL-------REGRPDLLLVYLPDLdyaghrYGP--DSPEYRAALREVdaaLGrlldalkar 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 246 PRNKNFNI-----HG---TNKHWLIRQAKT----PMTNSSIRFL------DDAFRRRWQTLLSVDDLVEKLVKRLDST-- 305
Cdd:COG1524 229 GLYEGTLVivtadHGmvdVPPDIDLNRLRLagllAVRAGESAHLylkdgaDAEVRALLGLPARVLTREELAAGHFGPHri 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789239 306 GEL----DNTYIFYTSDNGYHtGqfSLPIDKRQlyefdikVPLLVRGPGIKPNqtskmlVSNIDLGPTILDLAG 375
Cdd:COG1524 309 GDLvlvaKPGWALDAPLKGSH-G--GLPDEEMR-------VPLLASGPGFRPG------VRNVDVAPTIARLLG 366
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
287-377 |
1.28e-03 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 41.07 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 287 TLLSVDDLVEKLVKRLDSTGEldNTYIFYTSDNG---YHTGQF--SLPIDKRQLYEfdikVPLLV--------RGPGIKP 353
Cdd:cd16017 191 SILYTDYVLSQIIERLKKKDK--DAALIYFSDHGeslGENGLYlhGAPYAPKEQYH----VPFIIwssdsykqRYPVERL 264
|
90 100
....*....|....*....|....
gi 29789239 354 NQTSKMLVSNIDLGPTILDLAGYD 377
Cdd:cd16017 265 RANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
76-105 |
3.11e-03 |
|
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: 40.10 E-value: 3.11e-03
10 20 30
....*....|....*....|....*....|
gi 29789239 76 AYVPSaLCCPSRASILTGKYPHNHHVVNNT 105
Cdd:pfam01663 38 PVFPT-LTFPNHYTLVTGLYPGSHGIVGNT 66
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
285-377 |
5.49e-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: 39.04 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789239 285 WQTLLS---------VDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQF----------SLPIdkrqLYefdIKVP-- 343
Cdd:cd16021 170 WLSELThdylnglslADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIretlqgkleeRLPF----LS---ISLPkw 242
|
90 100 110
....*....|....*....|....*....|....*.
gi 29789239 344 LLVRGPGIKPN--QTSKMLVSNIDLGPTILDLAGYD 377
Cdd:cd16021 243 FREKYPEAVANlkKNSNRLTTPFDLHATLLDILNLQ 278
|
|
| |
