|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
29-478 |
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: 619.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDLDIAIGGLSPLNKTKKLIGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEGNCSSKAWQK 108
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 109 SEEATTFPSLLKAnAGYQTFFAGKYLNQYGhaEAGGVEHVPPGWNYWVGLEKNSKYYNYTLSvNGKAQKHGADYNKDYLT 188
Cdd:cd16147 81 GLERSTLPVWLQE-AGYRTAYAGKYLNGYG--VPGGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 189 DVLANMSLDFL-QHKSNYQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDPNFN--IHGKDKHWLIRQAKTPMTnsSV 265
Cdd:cd16147 157 DVIANKALDFLrRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPPPNnpDVSDKPHWLRRLPPLNPT--QI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 266 QFLDDAFRKRWRTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLPLDKRQLYEFDIKVPLMVRGPNIKPN 345
Cdd:cd16147 235 AYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 346 QTSQMLVANVDLGPTMLDIAGLDVnKTQMDGMSflpimegkmnsswrtdilveyegegsnvsdpacpllgpgvsecfpdc 425
Cdd:cd16147 315 VTVDQLVSNIDLAPTILDLAGAPP-PSDMDGRS----------------------------------------------- 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1771637665 426 vCEDSYNNTYACVRTVAPSANLQYCEFDDNevFVEVYNVTADPFQLTNIAKSI 478
Cdd:cd16147 347 -CGDSNNNTYKCVRTVDDTYNLLYFEWCTG--FRELYDLTTDPYQLTNLAGDL 396
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
28-493 |
2.52e-106 |
|
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: 324.87 E-value: 2.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 28 RRPNIVLILTDDL--DiAIGGL-SPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNtlEGNcS 102
Cdd:cd16031 1 KRPNIIFILTDDHryD-ALGCYgNPIVKTPNIdrLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDN--NGP-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 SKAWQKseeatTFPSLLKAnAGYQTFFAGKYlnqygHAEAGGvEHVPPGWNYWVGLEKNSKYYNYTLSVNGKAQKHgady 182
Cdd:cd16031 77 FDASQP-----TYPKLLRK-AGYQTAFIGKW-----HLGSGG-DLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 183 nKDYLTDVLANMSLDFLQHKSNYQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDPNFNI---HGKDKhWLiRQAKtp 259
Cdd:cd16031 141 -KGYVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDDddyAGRPE-WA-REQR-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 260 mtNSSVQFLDDAFRKRW----------RTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLpLDKRQLYEF 329
Cdd:cd16031 216 --NRIRGVLDGRFDTPEkyqrymkdylRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGL-FDKRLMYEE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 330 DIKVPLMVRGP-NIKPNQTSQMLVANVDLGPTMLDIAGLDVNKtQMDGMSFLPIMEGKMNSSWRTDILVEYEGEGsnvsd 408
Cdd:cd16031 293 SIRVPLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPE-DMQGRSLLPLLEGEKPVDWRKEFYYEYYEEP----- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 409 pacpllgpgvsecfpdcvcedSYNNTYAC--VRTvapsANLQYCEFDDNEVFVEVYNVTADPFQLTNIAKSID-QEILEK 485
Cdd:cd16031 367 ---------------------NFHNVPTHegVRT----ERYKYIYYYGVWDEEELYDLKKDPLELNNLANDPEyAEVLKE 421
|
....*...
gi 1771637665 486 MNHRLMML 493
Cdd:cd16031 422 LRKRLEEL 429
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
10-490 |
1.27e-97 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 301.03 E-value: 1.27e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 10 FLLICVTLCSSAVFAASYRRPNIVLILTDDL---DIAIGGlSPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTG 84
Cdd:COG3119 4 LLLLLLALLAAAAAAAAAKRPNILFILADDLgygDLGCYG-NPLIKTPNIdrLAAEGVRFTNAYVTSPVCSPSRASLLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 85 KYPHNHHVINNTLEGNcsskaWQKSEEATTFPSLLKAnAGYQTFFAGKYlnqyghaeaggveHVppgwnywvgleknsky 164
Cdd:COG3119 83 RYPHRTGVTDNGEGYN-----GGLPPDEPTLAELLKE-AGYRTALFGKW-------------HL---------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 165 ynytlsvngkaqkhgadynkdYLTDVLANMSLDFL-QHKSNYQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDPNFN 243
Cdd:COG3119 128 ---------------------YLTDLLTDKAIDFLeRQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPNLA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 244 IHGKDKHWLIRqaktpmtnssvqflddAFRKRWRTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLPLDK 323
Cdd:COG3119 187 PRDLTEEELRR----------------ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGK 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 324 RQLYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKTqMDGMSFLPIMEGKmNSSWRTDILVEYEGE 402
Cdd:COG3119 251 GTLYEGGIRVPLIVRWPGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPED-LDGRSLLPLLTGE-KAEWRDYLYWEYPRG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 403 GSNVSdpacpllgpgvsecfpdcvcedsynntyacVRTvapsANLQYCEFDDNEVFVEVYNVTADPFQLTNIAKSiDQEI 482
Cdd:COG3119 329 GGNRA------------------------------IRT----GRWKLIRYYDDDGPWELYDLKNDPGETNNLAAD-YPEV 373
|
....*...
gi 1771637665 483 LEKMNHRL 490
Cdd:COG3119 374 VAELRALL 381
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-386 |
9.56e-68 |
|
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: 224.34 E-value: 9.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL---DIAIGGlSPLNKTKKLigDA----GISFTNAFVASPLCCPSRASILTGKYPHNHH---VINNTLEG 99
Cdd:cd16144 1 PNIVLILVDDLgwaDLGCYG-SKFYETPNI--DRlakeGMRFTQAYAAAPVCSPSRASILTGQYPARLGitdVIPGRRGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 100 NCSSK------AWQKSEEATTFPSLLKaNAGYQTFFAGKY----------LNQ-YGHAEAGGVEHVPPGWNYWVGLEKNS 162
Cdd:cd16144 78 PDNTKlipppsTTRLPLEEVTIAEALK-DAGYATAHFGKWhlggeggygpEDQgFDVNIGGTGNGGPPSYYFPPGKPNPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 163 KYYnytlsvngkaqkhgaDYNKDYLTDVLANMSLDFL-QHKSnyQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPrdpn 241
Cdd:cd16144 157 LED---------------GPEGEYLTDRLTDEAIDFIeQNKD--KPFFLYLSHYAVHTPIQARPELIEKYEKKKKG---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 242 fnihGKDKHWLIRQAktpmtnssvqflddafrkrwrTLL-SVDDLVEKIVKRLEVRGELDNTYIFFTSDNG---YHTGQF 317
Cdd:cd16144 216 ----LRKGQKNPVYA---------------------AMIeSLDESVGRILDALEELGLADNTLVIFTSDNGglsTRGGPP 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771637665 318 S--LPLD--KRQLYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKTQ-MDGMSFLPIMEGK 386
Cdd:cd16144 271 TsnAPLRggKGSLYEGGIRVPLIVRWPGvIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQhLDGVSLVPLLKGG 345
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
30-490 |
3.55e-67 |
|
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: 221.61 E-value: 3.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL---DIAIGGlsPLNKTKKLigDA----GISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTlegncs 102
Cdd:cd16027 1 PNILWIIADDLspdLGGYGG--NVVKTPNL--DRlaaeGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 SKAWQKSEEATTFPSLLKAnAGYQTFFAGKYlnqyghaeaggveHVPPGWNYWvgleknskyynytlsvnGKAQKHGADY 182
Cdd:cd16027 71 SRGFPLPDGVKTLPELLRE-AGYYTGLIGKT-------------HYNPDAVFP-----------------FDDEMRGPDD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 183 NKDYLTDVLANmSLDFLQHKSNYQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDPNFnihgkdkhwlirqAKTPMTn 262
Cdd:cd16027 120 GGRNAWDYASN-AADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYL-------------PDTPEV- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 263 ssvqflddafRKRW----RTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYhtgqfSLPLDKRQLYEFDIKVPLMVR 338
Cdd:cd16027 185 ----------REDLadyyDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 339 GPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKtQMDGMSFLPIMEGKmNSSWRTDILVEYEGEGsnvsdpacpllgpg 417
Cdd:cd16027 250 WPGkIKPGSVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLLKGE-KDPGRDYVFAERDRHD-------------- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 418 vsecfpdcvcedsynNTYACVRTVapsanlqyceFDD------NEVFVEVYNVTADPFQLTNIAKSID-QEILEKMNHRL 490
Cdd:cd16027 314 ---------------ETYDPIRSV----------RTGrykyirNYMPEELYDLKNDPDELNNLADDPEyAEVLEELRAAL 368
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
30-378 |
1.35e-66 |
|
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: 215.38 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL---DIAIGGlSPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEGNCSSk 104
Cdd:cd16022 1 PNILLIMTDDLgydDLGCYG-NPDIKTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 105 awqksEEATTFPSLLKAnAGYQTFFAGKYlnqygHAEAggvehvppgwnywvgleknskyynytlsvngkaqkhgadynk 184
Cdd:cd16022 79 -----PDEPTLAELLKE-AGYRTALIGKW-----HDEA------------------------------------------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 185 dyltdvlanmsLDFLQHKSNYQPFFMMVSTPAPHSPWTaapqYqnsfnntkaprdpnfnihgkdkhwlirqaktpmtnss 264
Cdd:cd16022 106 -----------IDFIERRDKDKPFFLYVSFNAPHPPFA----Y------------------------------------- 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 265 vqflddafrkrWRTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLPLDKRQLYEFDIKVPLMVRGPN-IK 343
Cdd:cd16022 134 -----------YAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGkIP 202
|
330 340 350
....*....|....*....|....*....|....*
gi 1771637665 344 PNQTSQMLVANVDLGPTMLDIAGLDVNKTqMDGMS 378
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPPEG-LDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-474 |
6.01e-62 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 208.58 E-value: 6.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDL---DIAIGGLSPLnKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVInntleGNCss 103
Cdd:cd16034 1 KPNILFIFADQHraqALGCAGDDPV-KTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-----GND-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 104 kaWQKSEEATTFPSLLKAnAGYQTFFAGKY-LnqYGHAEAGGV---EHVPP----GWNYWVGLEKNSKYYNYTLSVNGKA 175
Cdd:cd16034 73 --VPLPPDAPTIADVLKD-AGYRTGYIGKWhL--DGPERNDGRaddYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 176 QKHGADYNKDYLTDVLanmsLDFL-QHKSNYQPFFMMVSTPAPHSPWTAAPQ-YQNSFNNTKAPRDPNFNIHGKDKHWLI 253
Cdd:cd16034 148 RIYIKGYSPDAETDLA----IEYLeNQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLLRPNVPEDKKEEAGLR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 254 RQAKTPMTNSSvqflddafrkrwrtllSVDDLVEKIVKRLEVRGELDNTYIFFTSDNG---YHTGQFSlpldKRQLYEFD 330
Cdd:cd16034 224 EDLRGYYAMIT----------------ALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMN----KQVPYEES 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 331 IKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKTqMDGMSFLPIMEGKmnsswrtdilveyEGEGSNVSDP 409
Cdd:cd16034 284 IRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT-VEGRDLSPLLLGG-------------KDDEPDSVLL 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771637665 410 ACPllgpgvsecFPDCVCEDSYNNTYACVRTVapsanlQY---CEFDDNEVFvevYNVTADPFQLTNI 474
Cdd:cd16034 350 QCF---------VPFGGGSARDGGEWRGVRTD------RYtyvRDKNGPWLL---FDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-490 |
3.85e-60 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 203.99 E-value: 3.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTD----DLdIAIGGlSPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEGNCSS 103
Cdd:cd16033 1 PNILFIMTDqqryDT-LGCYG-NPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 104 KAWQksEEATTFPSLLKAnAGYQTFFAGKYlnqygHAeagGVEHVPP--GWNYWVGLEKNSKYYnytlsvngkaqkhgad 181
Cdd:cd16033 79 RGLP--PGVETFSEDLRE-AGYRNGYVGKW-----HV---GPEETPLdyGFDEYLPVETTIEYF---------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 182 ynkdyltdvLANMSLDFL-QHKSNYQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDPNFNIHGKDKHWLIRQAKTPM 260
Cdd:cd16033 132 ---------LADRAIEMLeELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYRRERKRW 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 261 TnssvqfLDDAFRKRWRTLLS--------VDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLpLDKRQ-LYEFDI 331
Cdd:cd16033 203 G------VDTEDEEDWKEIIAhywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRL-WDKGPfMYEETY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 332 KVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKTqMDGMSFLPIMEGKMNSSWRTDILVEYEGEGSnvsdpa 410
Cdd:cd16033 276 RIPLIIKWPGvIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK-VDGRSLLPLLRGEQPEDWRDEVVTEYNGHEF------ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 411 cpllgpgvsecfpdcvcedsynntYACVRTVapsanlqyceFDDNEVFV-------EVYNVTADPFQLTN-IAKSIDQEI 482
Cdd:cd16033 349 ------------------------YLPQRMV----------RTDRYKYVfngfdidELYDLESDPYELNNlIDDPEYEEI 394
|
....*...
gi 1771637665 483 LEKMNHRL 490
Cdd:cd16033 395 LREMRTRL 402
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
30-486 |
1.43e-58 |
|
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: 199.70 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL---DIAIGGlSPLNKTKKL--IGDAGISFTNaFVASPLCCPSRASILTGKYPHNHHVINNTLEGNcssk 104
Cdd:cd16146 1 PNVILILTDDQgygDLGFHG-NPILKTPNLdrLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWHTILGRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 105 awQKSEEATTFPSLLKANaGYQTFFAGK--------YLNQ-------YGHAeAGGVEHVPPGWnywvglekNSKYYNYTL 169
Cdd:cd16146 75 --RMRLDETTLAEVFKDA-GYRTGIFGKwhlgdnypYRPQdrgfdevLGHG-GGGIGQYPDYW--------GNDYFDDTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 170 SVNGKAQKHgadynKDYLTDVLANMSLDFLQHKSNyQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPrDPNFNIHGKdk 249
Cdd:cd16146 143 YHNGKFVKT-----EGYCTDVFFDEAIDFIEENKD-KPFFAYLATNAPHGPLQVPDKYLDPYKDMGLD-DKLAAFYGM-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 250 hwlirqaktpMTNssvqflddafrkrwrtllsVDDLVEKIVKRLEVRGELDNTYIFFTSDNG---YHTGQFSLPL--DKR 324
Cdd:cd16146 214 ----------IEN-------------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGpagGVPKRFNAGMrgKKG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 325 QLYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKT-QMDGMSFLPIMEGKmNSSWRTDILVEYEGE 402
Cdd:cd16146 265 SVYEGGHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGiKLDGRSLLPLLKGE-SDPWPERTLFTHSGR 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 403 GSNVSDPACPllgpgvsecfpdCVCedsYNNTYacvRTVAPSANLQycefddnevfvEVYNVTADPFQLTNIAKSIdQEI 482
Cdd:cd16146 344 WPPPPKKKRN------------AAV---RTGRW---RLVSPKGFQP-----------ELYDIENDPGEENDVADEH-PEV 393
|
....
gi 1771637665 483 LEKM 486
Cdd:cd16146 394 VKRL 397
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
30-367 |
7.82e-58 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 194.56 E-value: 7.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLDI----AIGGLSPLNKTKKLIGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLegncsska 105
Cdd:pfam00884 1 PNVVLVLGESLRApdlgLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 106 WQKSEEATTFPSLLKAnAGYQTFFAGKYLNqyGHAEAGGVEHVppGWNYWVGLEKNSKYYNYTLSVNGKAQkhgadyNKD 185
Cdd:pfam00884 73 VGLPRTEPSLPDLLKR-AGYNTGAIGKWHL--GWYNNQSPCNL--GFDKFFGRNTGSDLYADPPDVPYNCS------GGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 186 YLTDVLANMSLDFLQHKSnyQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAprdpnfnihgkdkhwlirqaktpmtnsSV 265
Cdd:pfam00884 142 VSDEALLDEALEFLDNND--KPFFLVLHTLGSHGPPYYPDRYPEKYATFKP---------------------------SS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 266 QFLDDAFRKRWRTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLPLD---KRQLYEFDIKVPLMVRGP-N 341
Cdd:pfam00884 193 CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHggkYDNAPEGGYRVPLLIWSPgG 272
|
330 340
....*....|....*....|....*.
gi 1771637665 342 IKPNQTSQMLVANVDLGPTMLDIAGL 367
Cdd:pfam00884 273 KAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
29-476 |
4.04e-54 |
|
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: 188.55 E-value: 4.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDLDIAIGGL-SPLNKTKKLigDA----GISFTNAFVASPLCCPSRASILTGKYPHNHHVINNtlegncSS 103
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYgGHPAKTPNI--DRlaarGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDN------NS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 104 KAWQKSEEATTFPSLLKaNAGYQTFFAGK-YlnqygHAEAGGVEHVPPGWNYWVGLEKNSKYYNYTLSVNGKAQKHGADY 182
Cdd:cd16030 74 YFRKVAPDAVTLPQYFK-ENGYTTAGVGKiF-----HPGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 183 N------------KDYLTdvlANMSLDFL-QHKSNYQPFFMMVSTPAPHSPWTaAPQ-----YQNSFNNTKAPRDPNF-- 242
Cdd:cd16030 148 PaweaadvpdeayPDGKV---ADEAIEQLrKLKDSDKPFFLAVGFYKPHLPFV-APKkyfdlYPLESIPLPNPFDPIDlp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 243 NIHGKDKHWLIRQAKTPMTNSSVQF--LDDAFrkrWRTLLS--------VDDLVEKIVKRLEVRGELDNTYIFFTSDNGY 312
Cdd:cd16030 224 EVAWNDLDDLPKYGDIPALNPGDPKgpLPDEQ---ARELRQayyasvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 313 H---TGQFSlpldKRQLYEFDIKVPLMVRGPNIK-PNQTSQMLVANVDLGPTMLDIAGLDVNKtQMDGMSFLPIMEGKmN 388
Cdd:cd16030 301 HlgeHGHWG----KHTLFEEATRVPLIIRAPGVTkPGKVTDALVELVDIYPTLAELAGLPAPP-CLEGKSLVPLLKNP-S 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 389 SSWRTDILVEYegegsnvsdPACPLLGpgvsecfpdcvcedsynntYAcVRTvapsANLQYCEF--DDNEVFVEVYNVTA 466
Cdd:cd16030 375 AKWKDAAFSQY---------PRPSIMG-------------------YS-IRT----ERYRYTEWvdFDKVGAEELYDHKN 421
|
490
....*....|
gi 1771637665 467 DPFQLTNIAK 476
Cdd:cd16030 422 DPNEWKNLAN 431
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-386 |
4.57e-52 |
|
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: 182.79 E-value: 4.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLdiAIGGLS----PLNKTKKLigDA----GISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEGNc 101
Cdd:cd16145 1 PNIIFILADDL--GYGDLGcygqKKIKTPNL--DRlaaeGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 102 sskAWQKSEEATTFPSLLKaNAGYQTFFAGKY-LNQYGHAEAggvehvpP---GWNYWVG--------------LEKNSK 163
Cdd:cd16145 76 ---QDPLPPDDVTLAEVLK-KAGYATAAFGKWgLGGPGTPGH-------PtkqGFDYFYGyldqvhahnyypeyLWRNGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 164 ---YYNYTLSVNGKAQkHGADYNKDYLTDVLANMSLDFLQ-HKSnyQPFFMMVSTPAPHSPWtAAPQyqnsfnntkapRD 239
Cdd:cd16145 145 kvpLPNNVIPPLDEGN-NAGGGGGTYSHDLFTDEALDFIReNKD--KPFFLYLAYTLPHAPL-QVPD-----------DG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 240 PNFNihgKDKHWLIRqaktpmtnsSVQFLDDAfRKRWRTLLS-VDDLVEKIVKRLEVRGELDNTYIFFTSDNGYH----- 313
Cdd:cd16145 210 PYKY---KPKDPGIY---------AYLPWPQP-EKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHseggs 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 314 --TGQF---SLPLD--KRQLYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVnKTQMDGMSFLPIMEG 385
Cdd:cd16145 277 ehDPDFfdsNGPLRgyKRSLYEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEP-PEDIDGISLLPTLLG 355
|
.
gi 1771637665 386 K 386
Cdd:cd16145 356 K 356
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-401 |
4.46e-51 |
|
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: 178.91 E-value: 4.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 28 RRPNIVLILTDDL---DIAIGGLSPLnKTKKLigDA----GISFTNAFVA---SP-LCCPSRASILTGKYphnhhviNNT 96
Cdd:cd16155 1 KKPNILFILADDQradTIGALGNPEI-QTPNL--DRlarrGTSFTNAYNMggwSGaVCVPSRAMLMTGRT-------LFH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 97 LEGNcssKAWQKSEEATTFPSLLKaNAGYQTFFAGKYLNQYghaeaggvehvppgwnywvgleknskyynytlsvngkaq 176
Cdd:cd16155 71 APEG---GKAAIPSDDKTWPETFK-KAGYRTFATGKWHNGF--------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 177 khgadynkdyltdvlANMSLDFLQHKSNY-QPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDPNF-NIHGKDKHWL-I 253
Cdd:cd16155 108 ---------------ADAAIEFLEEYKDGdKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENFlPQHPFDNGEGtV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 254 RQ---AKTPMTNSSVQflddAFRKRWRTLLS-VDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLpLDKRQLYEF 329
Cdd:cd16155 173 RDeqlAPFPRTPEAVR----QHLAEYYAMIThLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGL-MGKQNLYEH 247
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771637665 330 DIKVPLMVRGPNIKPNQTSQMLVANVDLGPTMLDIAGLDVNKTqMDGMSFLPIMEGKMNsSWRTDILVEYEG 401
Cdd:cd16155 248 SMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPES-VEGKSLLPVIRGEKK-AVRDTLYGAYRD 317
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-398 |
3.31e-50 |
|
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: 177.01 E-value: 3.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLdiAIGGLSPLNKTKKL-------IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEGNCS 102
Cdd:cd16143 1 PNIVIILADDL--GYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 SkawQKSEEATTFPSLLKaNAGYQTFFAGKYlnqyghaeaggveHVppGWN-YWVGLEKNSKYYNYTLSVNGKAQK---- 177
Cdd:cd16143 79 P---LIEPDRVTLAKMLK-QAGYRTAMVGKW-------------HL--GLDwKKKDGKKAATGTGKDVDYSKPIKGgpld 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 178 HGADY-----NKDYLtDVLANMSLDFL-QHKSNYQPFFMMVSTPAPHSPWTAAPQYQNSfnnTKAprdpnfNIHGkDkhw 251
Cdd:cd16143 140 HGFDYyfgipASEVL-PTLTDKAVEFIdQHAKKDKPFFLYFALPAPHTPIVPSPEFQGK---SGA------GPYG-D--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 252 LIRQaktpmtnssvqflddafrkrwrtllsVDDLVEKIVKRLEVRGELDNTYIFFTSDNG---YHTGQFSLPLD------ 322
Cdd:cd16143 206 FVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgp 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 323 ----KRQLYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKTQ-MDGMSFLPIMEGKMNSSWRTDIL 396
Cdd:cd16143 260 lrgmKADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAaEDSFSFLPALLGPKKQEVRESLV 339
|
..
gi 1771637665 397 VE 398
Cdd:cd16143 340 HH 341
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-392 |
3.62e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 173.94 E-value: 3.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLDI----AIGGLSplNKTKKL--IGDAGISFTNAFvASPLCCPSRASILTGKYPHNHHVINNTLEgncss 103
Cdd:cd16151 1 PNIILIMADDLGYecigCYGGES--YKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLD----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 104 kawqKSEeaTTFPSLLKaNAGYQTFFAGKY-LNQYGHAEAGGVEHvppGWN-Y--WVGLEKNSKYYNYTLSVNGKAQKHG 179
Cdd:cd16151 73 ----PKQ--KTFGHLLK-DAGYATAIAGKWqLGGGRGDGDYPHEF---GFDeYclWQLTETGEKYSRPATPTFNIRNGKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 180 ADYNK-DYLTDVLANMSLDFLQHKSNyQPFFMMVSTPAPHSPWTAAPQ--YQNSFNNTKAPRDPNFnihgKDKhwlirqa 256
Cdd:cd16151 143 LETTEgDYGPDLFADFLIDFIERNKD-QPFFAYYPMVLVHDPFVPTPDspDWDPDDKRKKDDPEYF----PDM------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 257 ktpmtnssVQFLddafrkrwrtllsvDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLPLD------KRQLYEFD 330
Cdd:cd16151 211 --------VAYM--------------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTNGrevrggKGKTTDAG 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771637665 331 IKVPLMVRGP-NIKPNQTSQMLVANVDLGPTMLDIAGLDV-NKTQMDGMSFLPIMEGKMNSSWR 392
Cdd:cd16151 269 THVPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLpEDYPLDGRSFAPQLLGKTGSPRR 332
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-491 |
7.75e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 159.32 E-value: 7.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTD----DLDIAIGglSPLNKTKKLIGDA--GISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEgncs 102
Cdd:cd16152 1 KPNVIVFFTDqqrwDTLGCYG--QPLDLTPNLDALAeeGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 skawqKSEEATTFPSLLKaNAGYQTFFAGKylnqyghaeaggvehvppgwnyWvgleknskyynytlsvngkaqkHGADY 182
Cdd:cd16152 75 -----LPADEKTLAHYFR-DAGYETGYVGK----------------------W----------------------HLAGY 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 183 NKDYLTDvlanMSLDFLQHKSNYQPFFMMVSTPAPHspwtaapqYQNSFNNTKAPrdpnfniHG-KDKHwliRQAKTPmt 261
Cdd:cd16152 105 RVDALTD----FAIDYLDNRQKDKPFFLFLSYLEPH--------HQNDRDRYVAP-------EGsAERF---ANFWVP-- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 262 nssvqflDD--AFRKRWRTLL--------SVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYH----TGQFslpldKRQLY 327
Cdd:cd16152 161 -------PDlaALPGDWAEELpdylgcceRLDENVGRIRDALKELGLYDNTIIVFTSDHGCHfrtrNAEY-----KRSCH 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 328 EFDIKVPLMVRGPNIKPNQTSQMLVANVDLGPTMLDIAGLDVNKTqMDGMSFLPIMEGKMNsSWRTDILVEyegegsnvs 407
Cdd:cd16152 229 ESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEE-MQGRSLLPLVDGKVE-DWRNEVFIQ--------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 408 dpacpllgpgVSECFpdcvcedsynnTYACVRT-------VAPSANLQYCEFDDneVFVE--VYNVTADPFQLTNIAKSI 478
Cdd:cd16152 298 ----------ISESQ-----------VGRAIRTdrwkysvAAPDKDGWKDSGSD--VYVEdyLYDLEADPYELVNLIGRP 354
|
490
....*....|....
gi 1771637665 479 D-QEILEKMNHRLM 491
Cdd:cd16152 355 EyREVAAELRERLL 368
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-406 |
3.34e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 150.77 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLDIAIGGLS--PLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNtlegncsSKA 105
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYghPVVRTPNLdrLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDN-------ADP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 106 WQKseEATTFPSLLkANAGYQTFFAGKylnqyghaeaggvehvppgwnywvgleknskyynytLSVNGKAQKHGADYNKD 185
Cdd:cd16037 74 YDG--DVPSWGHAL-RAAGYETVLIGK------------------------------------LHFRGEDQRHGFRYDRD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 186 yltdvLANMSLDFLQ-HKSNYQPFFMMVSTPAPHSPWTAAPQyqnsfnntkaprdpnfnihgkdkHWlirqaktpmtnss 264
Cdd:cd16037 115 -----VTEAAVDWLReEAADDKPWFLFVGFVAPHFPLIAPQE-----------------------FY------------- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 265 vqfldDAFRKRWRT----LLS-VDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLpLDKRQLYEFDIKVPLMVRG 339
Cdd:cd16037 154 -----DLYVRRARAayygLVEfLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGL-WGKSTMYEESVRVPMIISG 227
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771637665 340 PNIKPNQTSQMLVANVDLGPTMLDIAGLDVNKTQmDGMSFLPIMEGkmNSSWRTDILVEYEGEGSNV 406
Cdd:cd16037 228 PGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-DGRSLLPLAEG--PDDPDRVVFSEYHAHGSPS 291
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-390 |
4.46e-41 |
|
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: 152.33 E-value: 4.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDL---DIAIGGlSPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYP--------HNHHVINN 95
Cdd:cd16026 1 KPNIVVILADDLgygDLGCYG-SPLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPvrvglpgvVGPPGSKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 96 TLegncsskawqkSEEATTFPSLLKaNAGYQTFFAGKY-LnqyGHAEaggvEHVPP--GWNYWVGL----------EKNS 162
Cdd:cd16026 80 GL-----------PPDEITIAEVLK-KAGYRTALVGKWhL---GHQP----EFLPTrhGFDEYFGIpysndmwpfpLYRN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 163 KYYNYTLSVNGKAQKHGADYNKDYLTDVLANMSLDFLQHKSNyQPFFMMVSTPAPHSPWTAAPQYQnsfnntkaprdpnf 242
Cdd:cd16026 141 DPPGPLPPLMENEEVIEQPADQSSLTQRYTDEAVDFIERNKD-QPFFLYLAHTMPHVPLFASEKFK-------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 243 nihGKDKHWLIRQAktpmtnssVQFLDDAfrkrwrtllsvddlVEKIVKRLEVRGELDNTYIFFTSDNG-----YHTGQF 317
Cdd:cd16026 206 ---GRSGAGLYGDV--------VEELDWS--------------VGRILDALKELGLEENTLVIFTSDNGpwleyGGHGGS 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771637665 318 SLPLD--KRQLYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKTQM-DGMSFLPIMEGKMNSS 390
Cdd:cd16026 261 AGPLRggKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDRViDGKDISPLLLGGSKSP 337
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-496 |
7.00e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 152.39 E-value: 7.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL--DiAIGGL-SPLNKTKKLigDA----GISFTNAFVASPLCCPSRASILTGKYPHNHhvinntleGNCS 102
Cdd:cd16150 1 PNIVIFVADQLraD-SLGHLgNPAAVTPNL--DAlaaeGVRFSNAYCQNPVCSPSRCSFLTGWYPHVN--------GHRT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 SKAWQKSEEattfPSLLKA--NAGYQTFFAGK--YLNQYGHAEAggvehvppgwnywvgleknskyynYTLSvngkaqkh 178
Cdd:cd16150 70 LHHLLRPDE----PNLLKTlkDAGYHVAWAGKndDLPGEFAAEA------------------------YCDS-------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 179 gadynkDYLTdvlANMSLDFLQHKSNYQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAP-RDPNFNIHGKDKHWLIRQAK 257
Cdd:cd16150 114 ------DEAC---VRTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPpRRPPGLRAKGKPSMLEGIEK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 258 tpmtnssvQFLDDAFRKRWRTLLSV--------DDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLpLDKRQ--LY 327
Cdd:cd16150 185 --------QGLDRWSEERWRELRATylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGL-VEKWPntFE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 328 EFDIKVPLMVRGPNIKPNQTSQMLVANVDLGPTMLDIAGLDVNKTQMdGMSFLPIMEGKmnsswrTDILVEY---EGeGS 404
Cdd:cd16150 256 DCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGE------TEEHRDAvfsEG-GR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 405 NVSDPAC--------PLLGPGVSECF-PDCVCE----DSYNNTYAcVRTVAPSanlqycefddnevfvEVYNVTADPFQL 471
Cdd:cd16150 328 LHGEEQAmegghgpyDLKWPRLLQQEePPEHTKavmiRTRRYKYV-YRLYEPD---------------ELYDLEADPLEL 391
|
490 500
....*....|....*....|....*...
gi 1771637665 472 TNIAKSID-QEILEKMNHRLM--MLQSC 496
Cdd:cd16150 392 HNLIGDPAyAEIIAEMKQRLLrwMVETS 419
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
29-401 |
9.13e-39 |
|
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: 146.05 E-value: 9.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDL---DI-AIGGLSP---LNKtkklIGDAGISFTNaFVASPLCCPSRASILTGKYPHNHHVinntleGNC 101
Cdd:cd16025 2 RPNILLILADDLgfsDLgCFGGEIPtpnLDA----LAAEGLRFTN-FHTTALCSPTRAALLTGRNHHQVGM------GTM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 102 SSKAWQK-------SEEATTFPSLLKANaGYQTFFAGKYlnqyghaeaggveHVPPgwnywvgleknskyynytlsvngk 174
Cdd:cd16025 71 AELATGKpgyegylPDSAATIAEVLKDA-GYHTYMSGKW-------------HLGP------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 175 aqkhgADYnkdYLTDVLANMSLDFL-QHKSNYQPFFMMVSTPAPHSPWTAAPQY----------------QNSFNNTKA- 236
Cdd:cd16025 113 -----DDY---YSTDDLTDKAIEYIdEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalrEERLERQKEl 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 237 ----------PRDPNfnihgkDKHWlirqaktpmtNSsvqfLDDAFRKRWRTLLSV--------DDLVEKIVKRLEVRGE 298
Cdd:cd16025 185 glipadtkltPRPPG------VPAW----------DS----LSPEEKKLEARRMEVyaamvehmDQQIGRLIDYLKELGE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 299 LDNTYIFFTSDNG--YHTG--QFS---LPLDKRQLYEFDIKVPLMVRGPN--IKPNQTSQMLVANVDLGPTMLDIAGLDV 369
Cdd:cd16025 245 LDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKgiKAKGGIRHQFAHVIDIAPTILELAGVEY 324
|
410 420 430
....*....|....*....|....*....|....*....
gi 1771637665 370 NKT-------QMDGMSFLPIMEGKMNSSWRTDILVEYEG 401
Cdd:cd16025 325 PKTvngvpqlPLDGVSLLPTLDGAAAPSRRRTQYFELFG 363
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
30-404 |
1.42e-36 |
|
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: 138.10 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLD---IAIGGLSPLnKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNtlegncssk 104
Cdd:cd16032 1 PNILLIMADQLTaaaLPAYGNTVV-KTPNLdrLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDN--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 105 AWQKSEEATTFPSLLKAnAGYQTFFAGKYlnqyghaeaggveHvppgwnyWVGLEknskyynytlsvngkaQKHGADYNK 184
Cdd:cd16032 71 AAEFPADIPTFAHYLRA-AGYRTALSGKM-------------H-------FVGPD----------------QLHGFDYDE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 185 DylTDVLANMSLDFLQHKSNYQPFFMMVSTPAPHSPWTAAPQYQNsfnntkaprdpnfnihgkdkhWLIRQAktpmtnss 264
Cdd:cd16032 114 E--VAFKAVQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQEYWD---------------------LYVRRA-------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 265 vqflddafRKRWRTLLS-VDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLPLdKRQLYEFDIKVPLMVRGPNIK 343
Cdd:cd16032 163 --------RRAYYGMVSyVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWY-KMSFFEGSARVPLIISAPGRF 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771637665 344 PNQTSQMLVANVDLGPTMLDIAGLDVNK--TQMDGMSFLPIMEGKmNSSWRTDILVEYEGEGS 404
Cdd:cd16032 234 APRRVAEPVSLVDLLPTLVDLAGGGTAPhvPPLDGRSLLPLLEGG-DSGGEDEVISEYLAEGA 295
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
30-399 |
2.65e-36 |
|
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: 140.47 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL--DIAIGGLSPLNKTKKLigDA----GISFTNAFVASPLCCPSRASILTGKYPHNHHVINNT--Legnc 101
Cdd:cd16028 1 RNVLFITADQWraDCLSCLGHPLVKTPNL--DRlaaeGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGtpL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 102 sskawqkSEEATTFPSLLKAnAGYQTFFAGK---YLNQYGHAEAG----GVEHVPPGWNYWVGLEknskYYnytlsvngK 174
Cdd:cd16028 75 -------DARHLTLALELRK-AGYDPALFGYtdtSPDPRGLAPLDprllSYELAMPGFDPVDRLD----EY--------P 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 175 AQkhgaDYNKDYLTDVLanmsLDFLQHKSNyQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAP---RDPNFNIHGKD--- 248
Cdd:cd16028 135 AE----DSDTAFLTDRA----IEYLDERQD-EPWFLHLSYIRPHPPFVAPAPYHALYDPADVPppiRAESLAAEAAQhpl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 249 -KHWLIRQAKTP--MTNSSVQFLDDAFRKRWRT----LLS-VDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLp 320
Cdd:cd16028 206 lAAFLERIESLSfsPGAANAADLDDEEVAQMRAtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWL- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 321 LDKRQLYEFDIKVPLMVRGPNIKPNQTSQMLVAN----VDLGPTMLDIAGLDVnKTQMDGMSFLPIMEGKMNSSWRTDIL 396
Cdd:cd16028 285 WGKDGFFDQAYRVPLIVRDPRREADATRGQVVDAftesVDVMPTILDWLGGEI-PHQCDGRSLLPLLAGAQPSDWRDAVH 363
|
...
gi 1771637665 397 VEY 399
Cdd:cd16028 364 YEY 366
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
30-399 |
2.08e-35 |
|
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: 136.53 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL---DIAIGGlSPLNKT---KKLIGDaGISFTNAFVAsPLCCPSRASILTGKYPHN----HHVINNTlEG 99
Cdd:cd16029 1 PHIVFILADDLgwnDVGFHG-SDQIKTpnlDALAAD-GVILNNYYVQ-PICTPSRAALMTGRYPIHtgmqHGVILAG-EP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 100 NCSSKawqkseEATTFPSLLKAnAGYQTFFAGKYlnqygHAEAGGVEHVPPG----------------WNYWVGLEKNsk 163
Cdd:cd16029 77 YGLPL------NETLLPQYLKE-LGYATHLVGKW-----HLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSGGAND-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 164 YYNYTLSVNGKAqkhGADYNKDYLTDVLANMSLDFLQHKSNYQPFFMMVSTPAPHSPWTAAPQYqnsfnntkAPRDPNFN 243
Cdd:cd16029 143 YGNDDLRDNEEP---AWDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEY--------ADPYEDKF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 244 IHGKDKHwliRQAKTPMtnssvqflddafrkrwrtLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSL---- 319
Cdd:cd16029 212 AHIKDED---RRTYAAM------------------VSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsny 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 320 PL--DKRQLYEFDIKVPLMVRGPNIKPN--QTSQMLVANVDLGPTMLDIAGLDVN-KTQMDGMSFLPIMEGKmNSSWRTD 394
Cdd:cd16029 271 PLrgGKNTLWEGGVRVPAFVWSPLLPPKrgTVSDGLMHVTDWLPTLLSLAGGDPDdLPPLDGVDQWDALSGG-APSPRTE 349
|
....*
gi 1771637665 395 ILVEY 399
Cdd:cd16029 350 ILLNI 354
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-381 |
5.63e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 131.98 E-value: 5.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLDI-AIGGLSPLN-KTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHV---INNTLEGNcS 102
Cdd:cd16149 1 PNILFILTDDQGPwALGCYGNSEaVTPNLdrLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwIVEGSHGK-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 SKAWQKSEEATTFPSLLKaNAGYQTFFAGKylnqyghaeaggvehvppgWnywvgleknskyynytlsvngkaqkHGADY 182
Cdd:cd16149 80 KKPEGYLEGQTTLPEVLQ-DAGYRCGLSGK-------------------W-------------------------HLGDD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 183 NKDYLTDvlanmsldflQHKSNyQPFFMMVSTPAPHSPWtaapQYQNSfnntkaprdpnfnihgkdkhwlirqaktpmtn 262
Cdd:cd16149 115 AADFLRR----------RAEAE-KPFFLSVNYTAPHSPW----GYFAA-------------------------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 263 ssvqflddafrkrwrtLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSL--------PLDkrqLYEFDIKVP 334
Cdd:cd16149 148 ----------------VTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIwgkgngtfPLN---MYDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1771637665 335 LMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKTQ-MDGMSFLP 381
Cdd:cd16149 209 FIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPrLPGRSFAD 257
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-404 |
7.39e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 134.78 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLDI------AIGGLSPLNKTKKLIGDAGISFTNAFVAsPLCCPSRASILTGKYPHNHHVinNTLEGNCSS 103
Cdd:cd16154 1 PNILLIIADDQGLdssaqySLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGV--LAVPDELLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 104 kawqkseEATTFPSLLK---ANAGYQTFFAGKYL---NQYGHAEaggvehvPPGWNYWVG-LEKN-SKYYNYTLSVNGKA 175
Cdd:cd16154 78 -------SEETLLQLLIkdaTTAGYSSAVIGKWHlggNDNSPNN-------PGGIPYYAGiLGGGvQDYYNWNLTNNGQT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 176 QKHgadynKDYLTDVLANMSLDFLQHKSnyQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDpnfnihgkdkhwlIRQ 255
Cdd:cd16154 144 TNS-----TEYATTKLTNLAIDWIDQQT--KPWFLWLAYNAPHTPFHLPPAELHSRSLLGDSAD-------------IEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 256 AKTPMTNSSVQFLDDAFRkrwRTLLSVDDlvekivkrlevrGELDNTYIFFTSDNGyhT-GQ-----FSLPLDKRQLYEF 329
Cdd:cd16154 204 NPRPYYLAAIEAMDTEIG---RLLASIDE------------EERENTIIIFIGDNG--TpGQvvdlpYTRNHAKGSLYEG 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771637665 330 DIKVPLMVRGPNI-KPNQTSQMLVANVDLGPTMLDIAGLDVNKtQMDGMSFLPIMEGKmNSSWRTDILVEYEGEGS 404
Cdd:cd16154 267 GINVPLIVSGAGVeRANERESALVNATDLYATIAELAGVDAAE-IHDSVSFKPLLSDV-NASTRQYNYTEYESPTT 340
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-381 |
1.46e-34 |
|
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: 131.13 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL--DiAIG-GLSPLNKTKKLigDA----GISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEgncs 102
Cdd:cd16148 1 MNVILIVIDSLraD-HLGcYGYDRVTTPNL--DRlaaeGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 skawqksEEATTFPSLLKAnAGYQTFFAGkylnqyGHAeaggveHVPPGWNYWVGLEKNskyynytlsVNGKAQKHGADY 182
Cdd:cd16148 74 -------PDDPTLAEILRK-AGYYTAAVS------SNP------HLFGGPGFDRGFDTF---------EDFRGQEGDPGE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 183 NKDYLTDVLANMSLDFLQHKSNYQPFFMMVSTPAPHSPWtaapQYQNSfnntkaprdpnfnihgkdkhwlIRQaktpmtn 262
Cdd:cd16148 125 EGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEPY----LYDAE----------------------VRY------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 263 ssvqflddafrkrwrtllsVDDLVEKIVKRLEVRGELDNTYIFFTSDNG--------YHTGQFSLpldkrqlYEFDIKVP 334
Cdd:cd16148 172 -------------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGeefgehglYWGHGSNL-------YDEQLHVP 225
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1771637665 335 LMVRGPNIKPNQTSQMLVANVDLGPTMLDIAGLDVNKTqMDGMSFLP 381
Cdd:cd16148 226 LIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDY-SDGRSLLP 271
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-400 |
1.57e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 123.86 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDD---LDIAIGGLSPLN-KTKKLIGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTlegncsSKA 105
Cdd:cd16035 1 PNILLILTDQeryPPPWPAGWAALNlPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTL------GSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 106 WQkSEEATTFPSL---LKAnAGYQTFFAGKylnqyghaeaggvehvppgWNywvgleknskyynytLSvngKAQKHGADY 182
Cdd:cd16035 75 MQ-PLLSPDVPTLghmLRA-AGYYTAYKGK-------------------WH---------------LS---GAAGGGYKR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 183 NKDYltdvlANMSLDFLQHK----SNYQPFFMMVSTPAPH---SPWTAAPQYQnsfnntkapRDPNFnihgkdKHWLIRQ 255
Cdd:cd16035 116 DPGI-----AAQAVEWLRERgaknADGKPWFLVVSLVNPHdimFPPDDEERWR---------RFRNF------YYNLIRD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 256 aktpmtnssvqflddafrkrwrtllsVDDLVEKIVKRLEVRGELDNTYIFFTSDNG----YHTGqfslpldKRQ---LYE 328
Cdd:cd16035 176 --------------------------VDRQIGRVLDALDASGLADNTIVVFTSDHGemggAHGL-------RGKgfnAYE 222
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771637665 329 FDIKVPLMVRGPNIKPN-QTSQMLVANVDLGPTMLDIAGLDVNKTQMD-----GMSFLPIMEGKMNSSWRTDILVEYE 400
Cdd:cd16035 223 EALHVPLIISHPDLFGTgQTTDALTSHIDLLPTLLGLAGVDAEARATEapplpGRDLSPLLTDADADAVRDGILFTYD 300
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
30-488 |
1.29e-30 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 124.42 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDD--LDIaIGGLSPLN-KTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNhhvinNTLEGNCSSK 104
Cdd:cd16156 1 KQFIFIMTDTqrWDM-VGCYGNKAmKTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT-----NGSWTNCMAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 105 AwqksEEATTFPSLLKANaGYQTFFAGKYlnqygHAEAG---GVEHVPPGW--NYWVGLEknskyyNY---------TLS 170
Cdd:cd16156 75 G----DNVKTIGQRLSDN-GIHTAYIGKW-----HLDGGdyfGNGICPQGWdpDYWYDMR------NYldelteeerRKS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 171 VNGKA--QKHGADYNKDYLTDVlANMSLDFL-QHKSnyQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDPNF--NIH 245
Cdd:cd16156 139 RRGLTslEAEGIKEEFTYGHRC-TNRALDFIeKHKD--EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 246 GKDKHWLIRQAKTPMTNSsvqfldDAFRKRWRTLLSVDDLVEKIVKRL--EVRGELDNTYIFFTSDNGYHTGQFSLPLDK 323
Cdd:cd16156 216 NKPLHQRLWAGAKPHEDG------DKGTIKHPLYFGCNSFVDYEIGRVldAADEIAEDAWVIYTSDHGDMLGAHKLWAKG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 324 RQLYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKtQMDGMSFLPIMEGKmNSSWRTDILVE---Y 399
Cdd:cd16156 290 PAVYDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPK-VLEGESILATIEDP-EIPENRGVFVEfgrY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 400 EgegsnvsdpacpllgpgvsecfpdcVCEDSYNNtYACVRtvapsanlqyCEFDDNEVFV-------EVYNVTADPFQLT 472
Cdd:cd16156 368 E-------------------------VDHDGFGG-FQPVR----------CVVDGRYKLVinllstdELYDLEKDPYEMH 411
|
490 500
....*....|....*....|....*
gi 1771637665 473 N---------IAKSIDQEILEKMNH 488
Cdd:cd16156 412 NliddpdyadVRDQLHDELLDYMNE 436
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
29-399 |
5.77e-30 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 122.86 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDL--DiAIGGLS-PLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINntlEGNCSS 103
Cdd:PRK13759 6 KPNIILIMVDQMrgD-CLGCNGnKAVETPNLdmLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG---YGDVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 104 KAWQkseeaTTFPSLLKaNAGYQTFFAGKYlnqyghaeaggveHVPPgwnywvglEKNSKYYNYTLSVNGKA----QKHG 179
Cdd:PRK13759 82 WNYK-----NTLPQEFR-DAGYYTQCIGKM-------------HVFP--------QRNLLGFHNVLLHDGYLhsgrNEDK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 180 ADYN--KDYL-------------------------------------TDVLANMSLDFLQHKSNYQPFFMMVSTPAPHSP 220
Cdd:PRK13759 135 SQFDfvSDYLawlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 221 WTAAPQYQNSFNNTKAPRDPNFNIHGKDKHWLIRQAKT-PMTNSSVQFLDDAFRKRWRTLLSVDDLVEKIVKRLEVRGEL 299
Cdd:PRK13759 215 YDPPKRYFDMYKDADIPDPHIGDWEYAEDQDPEGGSIDaLRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 300 DNTYIFFTSDNGYHTGQFSLpLDKRQLYEFDIKVPLMVRGP----NIKPNQTSQMLVANVDLGPTMLDIAGLDVNKTqMD 375
Cdd:PRK13759 295 DNTIILFVSDHGDMLGDHYL-FRKGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD-VD 372
|
410 420
....*....|....*....|....
gi 1771637665 376 GMSFLPIMEGKmNSSWRTDILVEY 399
Cdd:PRK13759 373 GRSLKNLIFGQ-YEGWRPYLHGEH 395
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-402 |
2.23e-28 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 116.48 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL---DIAI--GGLSPLNKTKKL--IGDAGISFTNaFVASPLCCPSRASILTGKYPhNHHvinntlegNCS 102
Cdd:cd16142 1 PNILVILGDDIgwgDLGCygGGIGRGAPTPNIdrLAKEGLRFTS-FYVEPSCTPGRAAFITGRHP-IRT--------GLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 SKAWQKSE-----EATTFPSLLKAnAGYQTFFAGKylNQYGHAEaggvEHVPP--GWNYWVGleknskYYNYTLsvngka 175
Cdd:cd16142 71 TVGLPGSPgglppWEPTLAELLKD-AGYATAQFGK--WHLGDED----GRLPTdhGFDEFYG------NLYHTI------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 176 qkhgaDynkDYLTDvlanMSLDFL--QHKSNyQPFFMMVSTPAPHSPWTAAPQYQnsfnntkaprdpnfnihGKDKHWli 253
Cdd:cd16142 132 -----D---EEIVD----KAIDFIkrNAKAD-KPFFLYVNFTKMHFPTLPSPEFE-----------------GKSSGK-- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 254 rqaktpmtnssVQFLDdafrkrwrTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHtgQFSLPL--------DKRQ 325
Cdd:cd16142 180 -----------GKYAD--------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGPE--QDVWPDggytpfrgEKGT 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 326 LYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAG-------LDVNKTQMDGMSFLPIMEGKMNSSWRTDILV 397
Cdd:cd16142 239 TWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGapdpkdkLLGKDRHIDGVDQSPFLLGKSEKSRRSEFFY 318
|
....*
gi 1771637665 398 EYEGE 402
Cdd:cd16142 319 FGEGE 323
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
29-400 |
4.38e-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: 113.68 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDL---DIAIGGlSPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINntleGNCSS 103
Cdd:cd16160 1 KPNIVLFFADDMgygDLASYG-HPTQERGPIddMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG----GTRVF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 104 KAWQ-----KSEeaTTFPSLLKaNAGYQTFFAGKY---LNQYGHAEAGG---------VEHVPPGWNYW--------VGL 158
Cdd:cd16160 76 LPWDigglpKTE--VTMAEALK-EAGYTTGMVGKWhlgINENNHSDGAHlpshhgfdfVGTNLPFTNSWacddtgrhVDF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 159 EKNSK---YYNYTLSvngkAQKhgadYNKDYLTDVLANMSLDFLqHKSNYQPFFMMVSTPAPHSPWTAAPQYQNsfnntK 235
Cdd:cd16160 153 PDRSAcflYYNDTIV----EQP----IQHEHLTETLVGDAKSFI-EDNQENPFFLYFSFPQTHTPLFASKRFKG-----K 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 236 APRdpnfNIHGkdkhwlirqaktpmtnssvqflDDAFRKRWRtllsvddlVEKIVKRLEVRGELDNTYIFFTSDNGYH-- 313
Cdd:cd16160 219 SKR----GRYG----------------------DNINEMSWA--------VGEVLDTLVDTGLDQNTLVFFLSDHGPHve 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 314 ---TGQFSLPLD--KRQLYEFDIKVPLMVRGPNIKPNQTSQMLVANVDLGPTMLDIAGLDV-NKTQMDGMSFLPIMEGKm 387
Cdd:cd16160 265 yclEGGSTGGLKggKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLpTDRIYDGLSITDLLLGE- 343
|
410
....*....|...
gi 1771637665 388 NSSWRTDILVEYE 400
Cdd:cd16160 344 ADSPHDDILYYCC 356
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-378 |
9.22e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 109.77 E-value: 9.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDLDI----AIGGLSPLNKTKKLIG------DA----GISFTNAFVASPLCCPSRASILTGKYPHNHHVIN 94
Cdd:cd16153 1 KPNILWIITDDQRVdslsCYNNAHTGKSESRLGYvespniDAlaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 95 NtlegncsSKAWQKSEEAT-TFPSLLKAnAGYQTFFAGKylnqyghaeaggvEHVPPGWNYWvglekNSKYYNYTLSVNG 173
Cdd:cd16153 81 F-------EAAHPALDHGLpTFPEVLKK-AGYQTASFGK-------------SHLEAFQRYL-----KNANQSYKSFWGK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 174 KAQkhGADYNKdyltdvlanmsldflqhksnyqPFFMMVSTPAPHSPWTAAPQYQNSFnntkaprdpnfnihgkDKHwli 253
Cdd:cd16153 135 IAK--GADSDK----------------------PFFVRLSFLQPHTPVLPPKEFRDRF----------------DYY--- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 254 rqaktpmtnssvqflddAFrkrwrtLLSVDDLVEKIVKRLEVRGEL---DNTYIFFTSDNGYHTGQFSLpLDKRQLYEFD 330
Cdd:cd16153 172 -----------------AF------CAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGI-LAKFTFWPQS 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1771637665 331 IKVPLMVRGPNIKP---NQTSQMLVANVDLGPTMLDIAGLDVNK-TQMDGMS 378
Cdd:cd16153 228 HRVPLIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDVDApDYLDGRD 279
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
29-385 |
7.78e-24 |
|
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: 103.32 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDL---DIAIGGLSPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEGncSS 103
Cdd:cd16161 1 KPNFLLLFADDLgwgDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT--SV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 104 KAWQKSEeaTTFPSLLKaNAGYQTFFAGKYlnQYGHAEAggveHVPP--GWNYWVGLEknskyynYTlsvngkaqkhgad 181
Cdd:cd16161 79 GGLPLNE--TTLAEVLR-QAGYATGMIGKW--HLGQREA----YLPNsrGFDYYFGIP-------FS------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 182 yNKDYLTDVLANMSLDFLQHKSNY-QPFFMMVSTPAPHSPWTAAPQYQNSfnntkaprdpnfnihgkdkhwlirqaktpm 260
Cdd:cd16161 130 -HDSSLADRYAQFATDFIQRASAKdRPFFLYAALAHVHVPLANLPRFQSP------------------------------ 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 261 TNSSVQFLDdafrkrwrTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNG---------------YHTGQFSLPLDKRQ 325
Cdd:cd16161 179 TSGRGPYGD--------ALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelavgpgtgDWQGNLGGSVAKAS 250
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771637665 326 LYEFDIKVPLMVRGPN-IKPNQTSQMLVANVDLGPTMLDIAGLDVNKTQM-DGMSFLPIMEG 385
Cdd:cd16161 251 TWEGGHREPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGRIyDGKDLSPVLFG 312
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-386 |
8.67e-24 |
|
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: 104.09 E-value: 8.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDL---DIAIGGlSPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYP-------HNHHVINNT 96
Cdd:cd16157 1 KPNIILMLMDDMgwgDLGVFG-EPSRETPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPirngfytTNAHARNAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 97 LEGNCSSKAwqkSEEATTFPSLLKaNAGYQTFFAGKYlnQYGHAEaggvEHVP--PGWNYW-------VGLEKNSKYYNY 167
Cdd:cd16157 80 TPQNIVGGI---PDSEILLPELLK-KAGYRNKIVGKW--HLGHRP----QYHPlkHGFDEWfgapnchFGPYDNKAYPNI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 168 TLSVNGKAQ-KHGADYNKDY------LTDVLANMSLDFLQHKSNYQ-PFFMMVSTPAPHSPWTAAPQYQnsfnntkaprd 239
Cdd:cd16157 150 PVYRDWEMIgRYYEEFKIDKktgesnLTQIYLQEALEFIEKQHDAQkPFFLYWAPDATHAPVYASKPFL----------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 240 pnfnihGKDKHWLIRQAktpmtnssVQFLDDAfrkrwrtllsvddlVEKIVKRLEVRGELDNTYIFFTSDNGYHT----- 314
Cdd:cd16157 219 ------GTSQRGLYGDA--------VMELDSS--------------VGKILESLKSLGIENNTFVFFSSDNGAALisape 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771637665 315 -GQFSLPL--DKRQLYEFDIKVPLMVRGP-NIKPNQTSQMLVANVDLGPTMLDIAGLDVNK-TQMDGMSFLP-IMEGK 386
Cdd:cd16157 271 qGGSNGPFlcGKQTTFEGGMREPAIAWWPgHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSdRAIDGIDLLPvLLNGK 348
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
30-407 |
6.09e-21 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 94.53 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLDIAIGGLsPLNKTKKL-----IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINN--TLEGNcs 102
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFR-PGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNykGLDPN-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 skawqkseeATTFPSLLKANaGYQTFFAGKYLNQYG-HAEAGGVEhvppGWNYWVgleknskyyNYTLSVNGK------- 174
Cdd:cd16171 78 ---------YPTWMDRLEKH-GYHTQKYGKLDYTSGhHSVSNRVE----AWTRDV---------PFLLRQEGRptvnlvg 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 175 AQKHGADYNKDY-LTDVLANmsldFLQHKS-NY-QPFFMMVSTPAPHsPWtAAPQYQNSFNNTKAprdpnfnihgkdkhw 251
Cdd:cd16171 135 DRSTVRVMLKDWqNTDKAVH----WIRKEApNLtQPFALYLGLNLPH-PY-PSPSMGENFGSIRN--------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 252 lIRQAKTPMTNSSvqflddafrkrwrtllsvDDLVEKIVKRLEVRGELDNTYIFFTSDNGyhtgqfSLPLDKRQ-----L 326
Cdd:cd16171 194 -IRAFYYAMCAET------------------DAMLGEIISALKDTGLLDKTYVFFTSDHG------ELAMEHRQfykmsM 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 327 YEFDIKVPLMVRGPNIKPNQTSQMLVANVDLGPTMLDIAGLDVNKTqMDGMSFLPIMEGKMNS---------SWrtdILV 397
Cdd:cd16171 249 YEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN-LSGYSLLPLLSESSIKespsrvphpDW---VLS 324
|
410
....*....|
gi 1771637665 398 EYEGEGSNVS 407
Cdd:cd16171 325 EFHGCNVNAS 334
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
29-390 |
2.88e-18 |
|
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: 87.73 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 29 RPNIVLILTDDLDIA-IGGLSplNKTKK-----LIGDAGISFTNAFVASPLCCPSRASILTGKYP--------HNHHVIN 94
Cdd:cd16159 1 KPNIVLFMADDLGIGdVGCFG--NDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirsgmassHGMRVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 95 NTlegnCSSKAWQKSEeaTTFPSLLKaNAGYQTFFAGKY----------------LNQ-----YG----------HAEAG 143
Cdd:cd16159 79 FT----ASSGGLPPNE--TTFAEVLK-QQGYSTALIGKWhlglhcesrndfchhpLNHgfdyfYGlpltnlkdcgDGSNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 144 GVEHVPPGWNY----------------------------------------WVGLEKNSKYYNYTLSVNGKAQKHGADYn 183
Cdd:cd16159 152 EYDLSFDPLFPlltafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHEVVEQPMSL- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 184 kDYLTDVLANMSLDFLQHKSNyQPFFMMVSTPAPHSPWTAAPQYQnsfnntkaprdpnfnihGKDKHWLIRQAktpmtns 263
Cdd:cd16159 231 -ENLTQRLTKEAISFLERNKE-RPFLLVMSFLHVHTALFTSKKFK-----------------GRSKHGRYGDN------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 264 sVQFLDdafrkrWRtllsvddlVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQFSLPLD------------KRQLYEFDI 331
Cdd:cd16159 285 -VEEMD------WS--------VGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEygggnggiyggkKMGGWEGGI 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771637665 332 KVPLMVRGPN-IKPNQ-----TSQMlvanvDLGPTMLDIAGLDV-NKTQMDGMSFLPIMEGKMNSS 390
Cdd:cd16159 350 RVPTIVRWPGvIPPGSvidepTSLM-----DIFPTVAALAGAPLpSDRIIDGRDLMPLLTGQEKRS 410
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
30-383 |
9.65e-18 |
|
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: 85.96 E-value: 9.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDL---DIAIGGlSPLNKTKKL--IGDAGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLEGNcSSK 104
Cdd:cd16158 2 PNIVLLFADDLgygDLGCYG-HPSSSTPNLdrLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPG-SRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 105 AWQKSEeaTTFPSLLKANaGYQTFFAGKYlnQYGHAEAGgvEHVPP--GWNYWVGLE---------------KNSKYYN- 166
Cdd:cd16158 80 GLPLNE--TTIAEVLKTV-GYQTAMVGKW--HLGVGLNG--TYLPThqGFDHYLGIPyshdqgpcqnltcfpPNIPCFGg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 167 -------YTLSVNGKAQKHGADYNKdyLTDVLANMSLDFLQH--KSNyQPFFMMVSTPAPHSPWTAAPQYQNsfnntKAP 237
Cdd:cd16158 153 cdqgevpCPLFYNESIVQQPVDLLT--LEERYAKFAKDFIADnaKEG-KPFFLYYASHHTHYPQFAGQKFAG-----RSS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 238 RDPnfnihgkdkhwlirqaktpmtnssvqFLDdafrkrwrTLLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQF 317
Cdd:cd16158 225 RGP--------------------------FGD--------ALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRK 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771637665 318 S-------LPLDKRQLYEFDIKVPLMVRGPN-IKPNQTSQmLVANVDLGPTMLDIAGLDVNKTQMDGMSFLPIM 383
Cdd:cd16158 271 SrggnaglLKCGKGTTYEGGVREPAIAYWPGrIKPGVTHE-LASTLDILPTIAKLAGAPLPNVTLDGVDMSPIL 343
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
30-365 |
1.73e-14 |
|
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: 73.22 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLILTDDLdiaigGLSPLNKT---------KKLIGDAGISFtNAFVASPLC--CPSRASILTGKYPHNHHVINN--- 95
Cdd:cd00016 1 KHVVLIVLDGL-----GADDLGKAgnpapttpnLKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNgsa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 96 TLEGNCSSKAWQKSEeaTTFPSLLKAnAGYQTFfagkylnqyghaeaggvehvppgwnyWVGLeknskyynytlsvngka 175
Cdd:cd00016 75 DPELPSRAAGKDEDG--PTIPELLKQ-AGYRTG--------------------------VIGL----------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 176 qkhgadynkdyltdvlanmsLDFLQHKSNYQPFFMMVSTPAPHSPWTA-APQYQNSFNNTKAprdpnfnihgkdkhwlir 254
Cdd:cd00016 109 --------------------LKAIDETSKEKPFVLFLHFDGPDGPGHAyGPNTPEYYDAVEE------------------ 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 255 qaktpmtnssvqflddafrkrwrtllsVDDLVEKIVKRLEVRGELDNTYIFFTSDNG---YHTGQFSLPLDKRQLYEFDI 331
Cdd:cd00016 151 ---------------------------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGM 203
|
330 340 350
....*....|....*....|....*....|....
gi 1771637665 332 KVPLMVRGPNIKPNQTSQMLVANVDLGPTMLDIA 365
Cdd:cd00016 204 RVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
30-366 |
1.55e-12 |
|
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: 68.09 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 30 PNIVLIL-----TDDLDIAIGGLSPLNKTKKLIGDaGISFTNAFVASPLCCPSRA--SILTGKYPhnhhvinntLEGNCS 102
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKE-GLYFGNFYSPGFGGGTANGefEVLTGLPP---------LPLGSG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 103 SKAWQKSEEATTFPSLLKANaGYQTFFAgkylnqyghaeaggveHvpPGWNYWVGLEKNSKYYNYTLSVNGKA-QKHGAD 181
Cdd:cd16015 71 SYTLYKLNPLPSLPSILKEQ-GYETIFI----------------H--GGDASFYNRDSVYPNLGFDEFYDLEDfPDDEKE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 182 YNKDYLTD-VLANMSLDFLQHKSNyQPFFMMVSTPAPHSPWTAAPQYQNsfnntkaprdpNFNIHGKDKHWLIRQAktpm 260
Cdd:cd16015 132 TNGWGVSDeSLFDQALEELEELKK-KPFFIFLVTMSNHGPYDLPEEKKD-----------EPLKVEEDKTELENYL---- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 261 tnSSVQFLDDAFRkrwrtllsvdDLVEKivkrLEVRGELDNTYIFFTSDngyHTGQFSLPLDKRQLYEFDI-KVPLMVRG 339
Cdd:cd16015 196 --NAIHYTDKALG----------EFIEK----LKKSGLYENTIIVIYGD---HLPSLGSDYDETDEDPLDLyRTPLLIYS 256
|
330 340
....*....|....*....|....*..
gi 1771637665 340 PNIKPNQTSQMLVANVDLGPTMLDIAG 366
Cdd:cd16015 257 PGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
24-380 |
6.02e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 65.06 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 24 AASYRRPNIVLIL-----TDDLDIAIGGLSPLNKTKKLIGDaGISFTNAFVASPLCCPSRASILTGKYPHNHHVINNTLE 98
Cdd:COG1368 229 FGPAKKPNVVVILlesfsDFFIGALGNGKDVTPFLDSLAKE-SLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGSPYKRPG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 99 GNcsskawqkseEATTFPSLLKANaGYQTFFAgkylnqyghaeaggveHvpPGWNYWVGLEKNSKY--YNYTLSVNgkaq 176
Cdd:COG1368 308 QN----------NFPSLPSILKKQ-GYETSFF----------------H--GGDGSFWNRDSFYKNlgFDEFYDRE---- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 177 khgaDYNKDYLT------DVLANMSLDFLQHKSnyQPFFMMVSTPAPHSPWTAAPQYQNSFNNTKAPRDPNFNihgkdkh 250
Cdd:COG1368 355 ----DFDDPFDGgwgvsdEDLFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEEDKKIPDYGKTTLNNYLN------- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 251 wlirqaktpmtnsSVQFLDDAfrkrwrtllsvddlVEKIVKRLEVRGELDNTYIFFTSDngyHTGqfslPLDKRQLYEFD 330
Cdd:COG1368 422 -------------AVRYADQA--------------LGEFIEKLKKSGWYDNTIFVIYGD---HGP----RSPGKTDYENP 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1771637665 331 I---KVPLMVRGPNIKPNQTSQMLVANVDLGPTMLDIAGLDVNKTQMDGMSFL 380
Cdd:COG1368 468 LeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLL 520
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
75-366 |
2.54e-10 |
|
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: 61.06 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 75 CPSRASILTGKYPHNHHVINNTLegncsskaWQkseeattfPSLLKANAGYQTFFAGKYLNqyghaeaggvehVPPGWN- 153
Cdd:cd16018 47 FPNHYSIVTGLYPESHGIVGNYF--------YD--------PKTNEEFSDSDWVWDPWWIG------------GEPIWVt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 154 -----------YWVGLEKNSKYYNYTLSVNGKaqkhgadYNKDYLTDVLANMSLD-FLQHKSNYQPFFMMVSTPAP---- 217
Cdd:cd16018 99 aekaglktasyFWPGSEVAIIGYNPTPIPLGG-------YWQPYNDSFPFEERVDtILEWLDLERPDLILLYFEEPdsag 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 218 HspwtaapQYqnsfnntkAPRDPNFNihgkdkhwlirqaktpmtnssvqfldDAFRKrwrtllsVDDLVEKIVKRLEVRG 297
Cdd:cd16018 172 H-------KY--------GPDSPEVN--------------------------EALKR-------VDRRLGYLIEALKERG 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771637665 298 ELDNTYIFFTSDNGYHT----GQFSlpldkrqlYEFDIKVPLMVRGPNIKPNQTSQMLvANVDLGPTMLDIAG 366
Cdd:cd16018 204 LLDDTNIIVVSDHGMTDvgthGYDN--------ELPDMRAIFIARGPAFKKGKKLGPF-RNVDIYPLMCNLLG 267
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
196-362 |
1.17e-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: 54.53 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 196 LDFLQHKSNYQPFFMMVSTPAPHS---PWTAAPQYQNSFNNTKAPRDPNFNihgkdkhwlirqaktpmtnssvqflDDAF 272
Cdd:COG3083 371 LQWLDQRDSDRPWFSYLFLDAPHAysfPADYPKPFQPSEDCNYLALDNESD-------------------------PTPF 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 273 RKRWRT-LLSVDDLVEKIVKRLEVRGELDNTYIFFTSDNGY-----------HTGQFSlpldkrqlyEFDIKVPLMVRGP 340
Cdd:COG3083 426 KNRYRNaVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS---------RYQLQVPLVIHWP 496
|
170 180
....*....|....*....|..
gi 1771637665 341 NiKPNQTSQMLVANVDLGPTML 362
Cdd:COG3083 497 G-TPPQVISKLTSHLDIVPTLM 517
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
75-311 |
4.14e-04 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 42.79 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 75 CPSRASILTGKYPHNHHVINNTL---EGNCSSKAWQKSEEATTF--PSLLKANAGYQTFFAGKYLNQYGHAEAGGVEHVP 149
Cdd:pfam01663 45 FPNHYTLVTGLYPGSHGIVGNTFydpKTGEYLVFVISDPEDPRWwqGEPIWDTAAKAGVRAAALFWPGSEVDYSTYYGTP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 150 PGwnYWVgleknsKYYNYTLSVNGKAqkhGADYNKDYLTDVLANMSLDflqhksnyQPFFMMVSTPAPhspwtaapqyqN 229
Cdd:pfam01663 125 PR--YLK------DDYNNSVPFEDRV---DTAVLQTWLDLPFADVAAE--------RPDLLLVYLEEP-----------D 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 230 SFNNTKAPRDPNFNihgkdkhwlirqaktpmtnssvqfldDAFRKrwrtllsVDDLVEKIVKRLEVRGELDNTYIFFTSD 309
Cdd:pfam01663 175 YAGHRYGPDSPEVE--------------------------DALRR-------VDRAIGDLLEALDERGLFEDTNVIVVSD 221
|
..
gi 1771637665 310 NG 311
Cdd:pfam01663 222 HG 223
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
282-368 |
2.70e-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: 39.81 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771637665 282 VDDLVEKIVKRLEVRGELDNTYIFFTSDNGYHTGQF----------SLPLdkrqLYefdIKVP--LMVRGPNIKPN--QT 347
Cdd:cd16021 185 ADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIretlqgkleeRLPF----LS---ISLPkwFREKYPEAVANlkKN 257
|
90 100
....*....|....*....|.
gi 1771637665 348 SQMLVANVDLGPTMLDIAGLD 368
Cdd:cd16021 258 SNRLTTPFDLHATLLDILNLQ 278
|
|
| |
