|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
24-495 |
0e+00 |
|
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: 539.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLRPVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWRTFTGN 103
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 104 FTTLPQYFKEHGYYTYSCGKVFHPGLSsnNTDDYPLSWSAPAFRPRTEQFMNSPVCPDKEGILRKNLICPVELQTQPYKT 183
Cdd:cd16030 82 AVTLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 184 LPDIESVAEALRFVGSRSrHSQEPFFLAMGFHKPHINFRFPRQFLSRFNLSQFynYTEDSLKPPDMPAVAWNPYTDVRAR 263
Cdd:cd16030 160 YPDGKVADEAIEQLRKLK-DSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESI--PLPNPFDPIDLPEVAWNDLDDLPKY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 264 DDFKHSNISFPYGPISPLQAAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEWAKYSNFEV 339
Cdd:cd16030 237 GDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEelglADNTIVVLWSDHGWHLGEHGHWGKHTLFEE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 340 ALRVPLIIRSPQFPVAQTKyYHGITELLDVFPTLVDLAGLPKLDkcqssqeltCGEGKSLYHQLMGLGRADEHVALSQYP 419
Cdd:cd16030 317 ATRVPLIIRAPGVTKPGKV-TDALVELVDIYPTLAELAGLPAPP---------CLEGKSLVPLLKNPSAKWKDAAFSQYP 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24656835 420 RPgmlptkhpnsdkpklrniKIMGYSLRTDIYRYTMWvrfhaqnfsRDWHDVYGEELYDHRLDSGEELNLMPLPQF 495
Cdd:cd16030 387 RP------------------SIMGYSIRTERYRYTEW---------VDFDKVGAEELYDHKNDPNEWKNLANDPEY 435
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
5-508 |
2.86e-72 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 234.77 E-value: 2.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 5 RLLLSLMMPVLLDAAAPPRRPNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGR 83
Cdd:COG3119 4 LLLLLLALLAAAAAAAAAKRPNILFILADDLGYgDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 84 RPDTLHLYDF-YSYWRTFTGNFTTLPQYFKEHGYYTYSCGKVFHpglssNNTDDYplswsapafrprteqfmnspvcpdk 162
Cdd:COG3119 84 YPHRTGVTDNgEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-----YLTDLL------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 163 egilrknlicpvelqtqpyktlpdiesVAEALRFVGSRSRHSQePFFLAMGFHKPHINFRFPRQFLSRfnlsqfynYTED 242
Cdd:COG3119 134 ---------------------------TDKAIDFLERQADKDK-PFFLYLAFNAPHAPYQAPEEYLDK--------YDGK 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 243 SLKPPDmpavawnpytdvrarddfkhsniSFPYGPISPLQAAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVAL 318
Cdd:COG3119 178 DIPLPP-----------------------NLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEelglADNTIVVFT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 319 GDHGWSLGEHA-EWAKYSNFEVALRVPLIIRSPQFPVAQTKyYHGITELLDVFPTLVDLAGLPKLDKCQssqeltcgeGK 397
Cdd:COG3119 235 SDNGPSLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIKAGSV-SDALVSLIDLLPTLLDLAGVPIPEDLD---------GR 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 398 SLYHQLMGLGRADEHVALSQYPRPGmlptkhpnsdkpklrnikiMGYSLRTDIYRYTmwvrfhaqnfsRDWHDVYGEELY 477
Cdd:COG3119 305 SLLPLLTGEKAEWRDYLYWEYPRGG-------------------GNRAIRTGRWKLI-----------RYYDDDGPWELY 354
|
490 500 510
....*....|....*....|....*....|.
gi 24656835 478 DHRLDSGEELNLmpLPQFDDVRQRLRRRLME 508
Cdd:COG3119 355 DLKNDPGETNNL--AADYPEVVAELRALLEA 383
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
25-508 |
1.58e-51 |
|
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: 179.63 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRPVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWRTFTGNF 104
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 105 TTLPQYFKEHGYYTYSCGKVFHPGLSSNNTDDYPLSWSAPAFRPRTEqfmnspvcpdkegilrknlicpvelqtqpyktl 184
Cdd:cd16027 81 KTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWDY--------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 185 pdiesVAEALRFVgsRSRHSQEPFFLAMGFHKPHINFRFPRQFLSRFNLSQ-----FYnytedslkpPDMPAVawnpytd 259
Cdd:cd16027 128 -----ASNAADFL--NRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKvkvppYL---------PDTPEV------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 260 vraRDDFkhsnisfpygpisplqaAQirqsYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGehaeWAKYS 335
Cdd:cd16027 185 ---REDL-----------------AD----YYDEIERLDQQVGEILDELEedglLDNTIVIFTSDHGMPFP----RAKGT 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 336 NFEVALRVPLIIRSPQFPVAQTKyYHGITELLDVFPTLVDLAGLPKLDKCQssqeltcgeGKSLYHQLMGLGRADEHVAL 415
Cdd:cd16027 237 LYDSGLRVPLIVRWPGKIKPGSV-SDALVSFIDLAPTLLDLAGIEPPEYLQ---------GRSFLPLLKGEKDPGRDYVF 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 416 SQYprpgmlpTKHPnsdkpklrnikIMGY---SLRTDIYRYtmwVRfhaqNFsrdwhdvYGEELYDHRLDSGEELNLMPL 492
Cdd:cd16027 307 AER-------DRHD-----------ETYDpirSVRTGRYKY---IR----NY-------MPEELYDLKNDPDELNNLADD 354
|
490
....*....|....*.
gi 24656835 493 PQFDDVRQRLRRRLME 508
Cdd:cd16027 355 PEYAEVLEELRAALDA 370
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
25-386 |
6.73e-47 |
|
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: 162.99 E-value: 6.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWRTFTGN 103
Cdd:cd16022 1 PNILLIMTDDLGYdDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 104 FTTLPQYFKEHGYYTYSCGKvFHpglssnntddyplswsapafrprteqfmnspvcpdkegilrknlicpvelqtqpykt 183
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGK-WH--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 184 lpdiesvAEALRFVgsRSRHSQEPFFLAMGFHKPHinfrfprqflsrfnlsqfynytedslkppdmpavawNPYTdvrar 263
Cdd:cd16022 103 -------DEAIDFI--ERRDKDKPFFLYVSFNAPH------------------------------------PPFA----- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 264 ddfkhsnisfpygpisplqaaqirqsYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAE-WAKYSNFE 338
Cdd:cd16022 133 --------------------------YYAMVSAIDDQIGRILDALEelglLDNTLIVFTSDHGDMLGDHGLrGKKGSLYE 186
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24656835 339 VALRVPLIIRSPQFPVAQTKyYHGITELLDVFPTLVDLAGLPKLDKCQ 386
Cdd:cd16022 187 GGIRVPFIVRWPGKIPAGQV-SDALVSLLDLLPTLLDLAGIEPPEGLD 233
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-418 |
2.59e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 161.56 E-value: 2.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWRtftGN 103
Cdd:cd16037 1 PNILIIMSDEHNPdAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYD---GD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 104 FTTLPQYFKEHGYYTYSCGKVFHPGLSSNNTDDYplswsapafrprteqfmnspvcpdkegilrknlicpvelqtqpykt 183
Cdd:cd16037 78 VPSWGHALRAAGYETVLIGKLHFRGEDQRHGFRY---------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 184 lpDIESVAEALRFVGSRSRHsQEPFFLAMGFHKPHINFRFPRQFLSRFnlsqfynytedslkppdmpavawnpytdVRAr 263
Cdd:cd16037 112 --DRDVTEAAVDWLREEAAD-DKPWFLFVGFVAPHFPLIAPQEFYDLY----------------------------VRR- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 264 ddfkhsnisfpygpisplqaaqIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEWAKYSNFEV 339
Cdd:cd16037 160 ----------------------ARAAYYGLVEFLDENIGRVLDALEelglLDNTLIIYTSDHGDMLGERGLWGKSTMYEE 217
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24656835 340 ALRVPLIIRSPQFPVAQTKyyHGITELLDVFPTLVDLAGLPKLDKCQssqeltcgeGKSLYhQLMGLGRADEHVALSQY 418
Cdd:cd16037 218 SVRVPMIISGPGIPAGKRV--KTPVSLVDLAPTILEAAGAPPPPDLD---------GRSLL-PLAEGPDDPDRVVFSEY 284
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
23-509 |
4.43e-45 |
|
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: 163.85 E-value: 4.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 23 RRPNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSywRTFT 101
Cdd:cd16031 1 KRPNIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG--PLFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 102 GNFTTLPQYFKEHGYYTYSCGKvFHPGLSSNNTD---DYplsWSapAFRPRTEQFMNspvcpdkegilrKNLICPVELQT 178
Cdd:cd16031 79 ASQPTYPKLLRKAGYQTAFIGK-WHLGSGGDLPPpgfDY---WV--SFPGQGSYYDP------------EFIENGKRVGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 179 QPYKTlpDIeSVAEALRFVgsRSRHSQEPFFLAMGFHKPHINFRFPRQFlsrfnlsqFYNYTEDSLKPpdmPAVAWNPYT 258
Cdd:cd16031 141 KGYVT--DI-ITDKALDFL--KERDKDKPFCLSLSFKAPHRPFTPAPRH--------RGLYEDVTIPE---PETFDDDDY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 259 D-----VRARDDFKHSNISFPYGPISPLQAAQIRqsYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHA 329
Cdd:cd16031 205 AgrpewAREQRNRIRGVLDGRFDTPEKYQRYMKD--YLRTVTGVDDNVGRILDYLEeqglADNTIIIYTSDNGFFLGEHG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 330 eWA-KYSNFEVALRVPLIIRSP-QFPVAQTkyyhgITEL---LDVFPTLVDLAGLPKLDKCQssqeltcgeGKSLYHQLM 404
Cdd:cd16031 283 -LFdKRLMYEESIRVPLIIRDPrLIKAGTV-----VDALvlnIDFAPTILDLAGVPIPEDMQ---------GRSLLPLLE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 405 GLGRAD-EHVALSQYPrpgMLPTKHpnsdkpklRNIKIMGysLRTDIYRYTMWvrfhaqnfsrdWHDVYGEELYDHRLDS 483
Cdd:cd16031 348 GEKPVDwRKEFYYEYY---EEPNFH--------NVPTHEG--VRTERYKYIYY-----------YGVWDEEELYDLKKDP 403
|
490 500
....*....|....*....|....*.
gi 24656835 484 GEELNLMPLPQFDDVRQRLRRRLMEM 509
Cdd:cd16031 404 LELNNLANDPEYAEVLKELRKRLEEL 429
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-508 |
1.09e-42 |
|
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: 156.61 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTlH-----LYDFYSYWR 98
Cdd:cd16033 1 PNILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHE-HgvlnnVENAGAYSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 99 TFTGNFTTLPQYFKEHGYYTYSCGKvFHPGlSSNNTDDYplswsapafrprteqfmnspvcpDKEGILrknlicPVElQT 178
Cdd:cd16033 80 GLPPGVETFSEDLREAGYRNGYVGK-WHVG-PEETPLDY-----------------------GFDEYL------PVE-TT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 179 QPYKTlpdiesVAEALRFVgSRSRHSQEPFFLAMGFHKPHINFRFPRQFLSRfnlsqfynYTEDSLKPP--------DMP 250
Cdd:cd16033 128 IEYFL------ADRAIEML-EELAADDKPFFLRVNFWGPHDPYIPPEPYLDM--------YDPEDIPLPesfaddfeDKP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 251 AVAWNpYTDVRARDDFKHSNIsfpygpisplqaAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLG 326
Cdd:cd16033 193 YIYRR-ERKRWGVDTEDEEDW------------KEIIAHYWGYITLIDDAIGRILDALEelglADDTLVIFTSDHGDALG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 327 EHAEWAK-YSNFEVALRVPLIIRSPQFPVAQTKyYHGITELLDVFPTLVDLAGLPKLDKCQssqeltcgeGKSLYHQLMG 405
Cdd:cd16033 260 AHRLWDKgPFMYEETYRIPLIIKWPGVIAAGQV-VDEFVSLLDLAPTILDLAGVDVPPKVD---------GRSLLPLLRG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 406 LGRAD---EHVAlsQYprpgmlptkhpNSDKPKLRNikimgYSLRTDIYRYTmwvrFHAqnFSRDwhdvygeELYDHRLD 482
Cdd:cd16033 330 EQPEDwrdEVVT--EY-----------NGHEFYLPQ-----RMVRTDRYKYV----FNG--FDID-------ELYDLESD 378
|
490 500
....*....|....*....|....*.
gi 24656835 483 SGEELNLMPLPQFDDVRQRLRRRLME 508
Cdd:cd16033 379 PYELNNLIDDPEYEEILREMRTRLYE 404
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-399 |
1.06e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 145.00 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPdTLHlydfYSYWRTFTGN 103
Cdd:cd16148 1 MNVILIVIDSLRAdHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-FYH----GVWGGPLEPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 104 FTTLPQYFKEHGYYTYscgkvfhpGLSSNntddyPLSWSAPAFRPRTEQFMNSPvcpdkegilrknlicPVELQTQPYKT 183
Cdd:cd16148 76 DPTLAEILRKAGYYTA--------AVSSN-----PHLFGGPGFDRGFDTFEDFR---------------GQEGDPGEEGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 184 LPDIESVAEALRFVgsRSRHSQEPFFLamgfhkpHINFrfprqflsrfnlsqfynytedslkppdmpavaWNPytdvrar 263
Cdd:cd16148 128 ERAERVTDRALEWL--DRNADDDPFFL-------FLHY--------------------------------FDP------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 264 ddfkHSnisfPYGpisplqaaqirqsYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEWAK-YSNF- 337
Cdd:cd16148 160 ----HE----PYL-------------YDAEVRYVDEQIGRLLDKLKelglLEDTLVIVTSDHGEEFGEHGLYWGhGSNLy 218
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24656835 338 EVALRVPLIIRSPQFPVAQTkyYHGITELLDVFPTLVDLAGLPKLDKCQssqeltcgeGKSL 399
Cdd:cd16148 219 DEQLHVPLIIRWPGKEPGKR--VDALVSHIDIAPTLLDLLGVEPPDYSD---------GRSL 269
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
25-418 |
2.39e-39 |
|
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: 145.41 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYwrtFTGN 103
Cdd:cd16032 1 PNILLIMADQLTAaALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAE---FPAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 104 FTTLPQYFKEHGYYTYSCGKVfHpglssnntddyplswsapafrprteqFmnspVCPDKegilrknlicpveLQTQPYkt 183
Cdd:cd16032 78 IPTFAHYLRAAGYRTALSGKM-H--------------------------F----VGPDQ-------------LHGFDY-- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 184 lpDIESVAEALRFVGSRSR-HSQEPFFLAMGFHKPHINFRFPRQFlsrfnlsqfynytedslkppdmpavaWNPYtdVRA 262
Cdd:cd16032 112 --DEEVAFKAVQKLYDLARgEDGRPFFLTVSFTHPHDPYVIPQEY--------------------------WDLY--VRR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 263 rddfkhsnisfpygpisplqaaqIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEWAKYSNFE 338
Cdd:cd16032 162 -----------------------ARRAYYGMVSYVDDKVGQLLDTLErtglADDTIVIFTSDHGDMLGERGLWYKMSFFE 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 339 VALRVPLIIRSPQFPVAqtkyyHGITE---LLDVFPTLVDLAGlpkldkCQSSQELTCGEGKSLYHQLMGLGRADEHVAL 415
Cdd:cd16032 219 GSARVPLIISAPGRFAP-----RRVAEpvsLVDLLPTLVDLAG------GGTAPHVPPLDGRSLLPLLEGGDSGGEDEVI 287
|
...
gi 24656835 416 SQY 418
Cdd:cd16032 288 SEY 290
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-507 |
7.73e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 145.40 E-value: 7.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 23 RRPNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQS----LCAPSRNSLLTGRrpdtlhlydfySYW 97
Cdd:cd16155 1 KKPNILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTGR-----------TLF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 98 RTFTGNF-------TTLPQYFKEHGYYTYSCGKvFHPGLssnnTDDyplswsapafrprteqfmnspvcpdkegilrknl 170
Cdd:cd16155 70 HAPEGGKaaipsddKTWPETFKKAGYRTFATGK-WHNGF----ADA---------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 171 icpvelqtqpyktlpdiesvaeALRFVGSRSRHSQePFFLAMGFHKPHInfrfPRQ----FLSRfnlsqfynYTEDSLKP 246
Cdd:cd16155 111 ----------------------AIEFLEEYKDGDK-PFFMYVAFTAPHD----PRQappeYLDM--------YPPETIPL 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 247 PDMPAVAwNPY--TDVRARDDFKHSNisfpygPISPLQAAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGD 320
Cdd:cd16155 156 PENFLPQ-HPFdnGEGTVRDEQLAPF------PRTPEAVRQHLAEYYAMITHLDAQIGRILDALEasgeLDNTIIVFTSD 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 321 HGWSLGEHAEWAKYSNFEVALRVPLIIRSPQFPVAQTkyYHGITELLDVFPTLVDLAGLPKLDKCQ--SSQELTCGEGKS 398
Cdd:cd16155 229 HGLAVGSHGLMGKQNLYEHSMRVPLIISGPGIPKGKR--RDALVYLQDVFPTLCELAGIEIPESVEgkSLLPVIRGEKKA 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 399 LYHQLMGlgradehvALSQYPRPGMlptkhpnSDKPKLrnikimgyslrtDIYRytmwvrfhaqnfsrdwHDVYGEELYD 478
Cdd:cd16155 307 VRDTLYG--------AYRDGQRAIR-------DDRWKL------------IIYV----------------PGVKRTQLFD 343
|
490 500
....*....|....*....|....*....
gi 24656835 479 HRLDSGEELNLMPLPQFDDVRQRLRRRLM 507
Cdd:cd16155 344 LKKDPDELNNLADEPEYQERLKKLLAELK 372
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
19-508 |
1.33e-37 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 144.43 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 19 AAPPRRPNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTlhlYDFYSYW 97
Cdd:PRK13759 1 MVQTKKPNIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWH---HGRVGYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 98 RTFTGNFT-TLPQYFKEHGYYTYSCGKV-FHP------------------------GLSSNNTDDYpLSWsapaFRprtE 151
Cdd:PRK13759 78 DVVPWNYKnTLPQEFRDAGYYTQCIGKMhVFPqrnllgfhnvllhdgylhsgrnedKSQFDFVSDY-LAW----LR---E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 152 QFMNSPvcPDKEGI-LRKNlicpvELQTQPYKTL----PDIESVAEALRFVgsRSRHSQEPFFLAMGFHKPHINFRFPRQ 226
Cdd:PRK13759 150 KAPGKD--PDLTDIgWDCN-----SWVARPWDLEerlhPTNWVGSESIEFL--RRRDPTKPFFLKMSFARPHSPYDPPKR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 227 FLSRFNLSQFYNytedslkppdmPAVAWNPYTdvrARDDFKHSNISFPYGPISPLQAAQIRQSYYASVSYVDDLFGKLIG 306
Cdd:PRK13759 221 YFDMYKDADIPD-----------PHIGDWEYA---EDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 307 GLD----LDETVVVALGDHGWSLGEHAEWAKYSNFEVALRVPLIIRSP--QFPVAQTKYYHGITELLDVFPTLVDLAGLP 380
Cdd:PRK13759 287 ALKefglLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPggLLAGNRGTVIDQVVELRDIMPTLLDLAGGT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 381 KLDKCqssqeltcgEGKSLYhqlmglgradeHVALSQYPRPgmlptkhpnsdKPKLRNIKIMGYS----LRTDIYRYtMW 456
Cdd:PRK13759 367 IPDDV---------DGRSLK-----------NLIFGQYEGW-----------RPYLHGEHALGYSsdnyLTDGKWKY-IW 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24656835 457 vrfhaqnFSRDWHdvygEELYDHRLDSGEELNLMPLPQFDDVRQRLRRRLME 508
Cdd:PRK13759 415 -------FSQTGE----EQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVD 455
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-506 |
1.71e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 142.76 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTL-HlydfysywRTFTG 102
Cdd:cd16150 1 PNIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNgH--------RTLHH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 103 -------NFTtlpQYFKEHGYYTYSCGKvfhpglssnnTDDYPlswsapafrprtEQFMNSPVCpdkegilrknlicpve 175
Cdd:cd16150 73 llrpdepNLL---KTLKDAGYHVAWAGK----------NDDLP------------GEFAAEAYC---------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 176 lqtqpyktLPDIESVAEALRFVgsRSRHSQEPFFLAMGFHKPHINFRFPRQFLSRfnlsqfynYTEDSLKPPDMPAVAWN 255
Cdd:cd16150 112 --------DSDEACVRTAIDWL--RNRRPDKPFCLYLPLIFPHPPYGVEEPWFSM--------IDREKLPPRRPPGLRAK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 256 PYTDVRARDDFKHSNisfpygPISPLQAAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEW 331
Cdd:cd16150 174 GKPSMLEGIEKQGLD------RWSEERWRELRATYLGMVSRLDHQFGRLLEALKetglYDDTAVFFFSDHGDYTGDYGLV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 332 AKYSN-FE-VALRVPLIIRSPQFPVAQTkyYHGITELLDVFPTLVDLAGLPkLDKCQSsqeltcgeGKSLYHQLMGLGRA 409
Cdd:cd16150 248 EKWPNtFEdCLTRVPLIIKPPGGPAGGV--SDALVELVDIPPTLLDLAGIP-LSHTHF--------GRSLLPVLAGETEE 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 410 DEHVALSQYPR----PGMLPTKHPNSDKPKLRNIKIMGYSLRTdiyRYTMwVRfhaqnfSRDWHDVY----GEELYDHRL 481
Cdd:cd16150 317 HRDAVFSEGGRlhgeEQAMEGGHGPYDLKWPRLLQQEEPPEHT---KAVM-IR------TRRYKYVYrlyePDELYDLEA 386
|
490 500
....*....|....*....|....*
gi 24656835 482 DSGEELNLMPLPQFDDVRQRLRRRL 506
Cdd:cd16150 387 DPLELHNLIGDPAYAEIIAEMKQRL 411
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-456 |
2.10e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 139.24 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWRTftg 102
Cdd:cd16034 1 KPNILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 103 NFTTLPQYFKEHGYYTYSCGKvFHPGLSSNNTDDYPLSWSAPAFR---------PRTEQFMNSPVCPDKegilrknlicP 173
Cdd:cd16034 78 DAPTIADVLKDAGYRTGYIGK-WHLDGPERNDGRADDYTPPPERRhgfdywkgyECNHDHNNPHYYDDD----------G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 174 VELQTQPYKtlPDIESvAEALRFVGSRSrHSQEPFFLAMGFHKPH-INFRFPRQFLSRFNLsqfynytEDSLKPPDMPAv 252
Cdd:cd16034 147 KRIYIKGYS--PDAET-DLAIEYLENQA-DKDKPFALVLSWNPPHdPYTTAPEEYLDMYDP-------KKLLLRPNVPE- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 253 awnpytDVRARDDFKHsnisfpygpisplqaaQIRQsYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEH 328
Cdd:cd16034 215 ------DKKEEAGLRE----------------DLRG-YYAMITALDDNIGRLLDALKelglLENTIVVFTSDHGDMLGSH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 329 AEWAKYSNFEVALRVPLIIRSPqFPVAQTKYYHGITELLDVFPTLVDLAGLPKLDKCqssqeltcgEGKSLYHQLMGLGR 408
Cdd:cd16034 272 GLMNKQVPYEESIRVPFIIRYP-GKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTV---------EGRDLSPLLLGGKD 341
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 24656835 409 ADEHVALSQYPRPGMlptKHPNSDKPKLRNIkimgyslRTDIYRYTMW 456
Cdd:cd16034 342 DEPDSVLLQCFVPFG---GGSARDGGEWRGV-------RTDRYTYVRD 379
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
25-379 |
4.75e-35 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 132.93 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDfySYWRTFTGN 103
Cdd:pfam00884 1 PNVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYV--STPVGLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 104 FTTLPQYFKEHGYYTYscgkVFHPGLSSNNTDDYPLSWSAPAFRPRTEQFMNSPVCPDKEGILrknlicpvelqtqPYKT 183
Cdd:pfam00884 79 EPSLPDLLKRAGYNTG----AIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC-------------SGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 184 LPDIESVAEALRFVGSRSRhsqePFFLAMGFHKPHINFRFPRQFLSRFnlSQFYNYTEDslkppdmpavawnpytdvrar 263
Cdd:pfam00884 142 VSDEALLDEALEFLDNNDK----PFFLVLHTLGSHGPPYYPDRYPEKY--ATFKPSSCS--------------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 264 ddfkhsnisfpygpisplqAAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEWAKYSNFEV 339
Cdd:pfam00884 195 -------------------EEQLLNSYDNTLLYTDDAIGRVLDKLEenglLDNTLVVYTSDHGESLGEGGGYLHGGKYDN 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24656835 340 A----LRVPLIIRSPQFPVAQTKyYHGITELLDVFPTLVDLAGL 379
Cdd:pfam00884 256 ApeggYRVPLLIWSPGGKAKGQK-SEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-380 |
7.40e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 129.42 E-value: 7.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLRP-VIGAYGDTLA----------STPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYD 92
Cdd:cd16153 1 KPNILWIITDDQRVdSLSCYNNAHTgksesrlgyvESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 93 FYSYWRTFTGNFTTLPQYFKEHGYYTYSCGKVFHpglssnntddyplswsapafrprtEQFMNspvcpdkegiLRKNLIC 172
Cdd:cd16153 81 FEAAHPALDHGLPTFPEVLKKAGYQTASFGKSHL------------------------EAFQR----------YLKNANQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 173 PVELQTQPYKTLPDiesvaealrfvgsrsrhSQEPFFLAMGFHKPHinfrfprqflsrfnlsqfynytedslkPPDMPAV 252
Cdd:cd16153 127 SYKSFWGKIAKGAD-----------------SDKPFFVRLSFLQPH---------------------------TPVLPPK 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 253 AWnpytdvRARDDfkhsnisfpygpisplqaaqirqsYYASVSYVDDLFGKLIGGLDL-------DETVVVALGDHGWSL 325
Cdd:cd16153 163 EF------RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAyslkqdrDYTIVYVTGDHGWHL 212
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24656835 326 GEHAEWAKYSNFEVALRVPLIIRSP-QFPVAQTKYYHGITELLDVFPTLVDLAGLP 380
Cdd:cd16153 213 GEQGILAKFTFWPQSHRVPLIVVSSdKLKAPAGKVRHDFVEFVDLAPTLLAAAGVD 268
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
25-508 |
3.71e-33 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 131.23 E-value: 3.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRrpdtlHLYDFYSYWRTF--T 101
Cdd:cd16028 1 RNVLFITADQWRaDCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR-----YLMNHRSVWNGTplD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 102 GNFTTLPQYFKEHGYYTYSCGK---VFHP-GLSSNntDDYPLSW--SAPAFRPrteqfmnspVCPDKEgilrknliCPVE 175
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYtdtSPDPrGLAPL--DPRLLSYelAMPGFDP---------VDRLDE--------YPAE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 176 LQTQPYKTlpdiesvAEALRFVGSRSrhsQEPFFLAMGFHKPHINFRFPRQflsrfnlsqfYN--YTEDSLKPPDM---- 249
Cdd:cd16028 137 DSDTAFLT-------DRAIEYLDERQ---DEPWFLHLSYIRPHPPFVAPAP----------YHalYDPADVPPPIRaesl 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 250 -------PAVAWnpYTDVRARDDFKHSniSFPYGPISPLQAAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVAL 318
Cdd:cd16028 197 aaeaaqhPLLAA--FLERIESLSFSPG--AANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKetgqWDDTLIVFT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 319 GDHGWSLGEHAEWAKYSNFEVALRVPLIIRSPQFPVAQTKYY--HGITELLDVFPTLVDLAGLPKLDKCQssqeltcgeG 396
Cdd:cd16028 273 SDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRREADATRGQvvDAFTESVDVMPTILDWLGGEIPHQCD---------G 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 397 KSLYHQLMGLGRADEHVALSQYPRPGMLPTKHPNSdkpklrnikimgySLRTDIYRYTMWVRfhaqnFSRDWHDVYGEE- 475
Cdd:cd16028 344 RSLLPLLAGAQPSDWRDAVHYEYDFRDVSTRRPQE-------------ALGLSPDECSLAVI-----RDERWKYVHFAAl 405
|
490 500 510
....*....|....*....|....*....|....*.
gi 24656835 476 ---LYDHRLDSGEELNLMPLPQFDDVRQRLRRRLME 508
Cdd:cd16028 406 pplLFDLKNDPGELRDLAADPAYAAVVLRYAQKLLS 441
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
25-506 |
1.59e-28 |
|
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: 117.27 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLrpvigAYGD------TLASTPYLDNFARGSHIFTRVYsQQSLCAPSRNSLLTGRrpdtlhlydfYSY-- 96
Cdd:cd16146 1 PNVILILTDDQ-----GYGDlgfhgnPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGR----------YPFrt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 97 --WRTFTG------NFTTLPQYFKEHGYYTYSCGKvFHPGlssnntDDYPlswsapaFRPR----TEQFMN--------- 155
Cdd:cd16146 65 gvWHTILGrermrlDETTLAEVFKDAGYRTGIFGK-WHLG------DNYP-------YRPQdrgfDEVLGHggggigqyp 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 156 SPVCPD-KEGILRKNlicPVELQTQPYKT--LPDiesvaEALRFVgsrSRHSQEPFFLAMGFHKPHINFRFPRQFlsrfn 232
Cdd:cd16146 131 DYWGNDyFDDTYYHN---GKFVKTEGYCTdvFFD-----EAIDFI---EENKDKPFFAYLATNAPHGPLQVPDKY----- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 233 lsqfynytedslkppdmpavaWNPYTDVRARDDfkhsnisfpygpisplqaaqiRQSYYASVSYVDDLFGKLIGGLD--- 309
Cdd:cd16146 195 ---------------------LDPYKDMGLDDK---------------------LAAFYGMIENIDDNVGRLLAKLKelg 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 310 -LDETVVVALGDHGWSLGEHAEW------AKYSNFEVALRVPLIIRSP-QFPVAQTKyyHGITELLDVFPTLVDLAGLP- 380
Cdd:cd16146 233 lEENTIVIFMSDNGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPgKILAGKDV--DTLTAHIDLLPTLLDLCGVKl 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 381 ----KLDkcqssqeltcgeGKSLYHQLMGLGRA-DEHVALSQYPRPGMLPTKHPNSdkpklrnikimgySLRTDIYRYTm 455
Cdd:cd16146 311 pegiKLD------------GRSLLPLLKGESDPwPERTLFTHSGRWPPPPKKKRNA-------------AVRTGRWRLV- 364
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24656835 456 wvrfhaqnfsrdWHDVYGEELYDHRLDSGEELNLmpLPQFDDVRQRLRRRL 506
Cdd:cd16146 365 ------------SPKGFQPELYDIENDPGEENDV--ADEHPEVVKRLKAAY 401
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-508 |
1.61e-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: 293763 [Multi-domain] Cd Length: 421 Bit Score: 117.26 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDL-RPVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWRTFTGN 103
Cdd:cd16144 1 PNIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 104 F---------------TTLPQYFKEHGYYTYSCGKvFHPGlssNNTDDYPLS----WSAPAFRprteqfMNSPVCPDKEG 164
Cdd:cd16144 81 TklipppsttrlpleeVTIAEALKDAGYATAHFGK-WHLG---GEGGYGPEDqgfdVNIGGTG------NGGPPSYYFPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 165 ILRKNLicPVELQTQPYKTlpdiESVA-EALRFVgsrSRHSQEPFFLAMGFHKPHINFRFPRQFLSRfnlsqfynyteds 243
Cdd:cd16144 151 GKPNPD--LEDGPEGEYLT----DRLTdEAIDFI---EQNKDKPFFLYLSHYAVHTPIQARPELIEK------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 244 lkppdmpavawnpYTDVRARDDFKHSNIsfpygpisplqaaqirqsYYAS-VSYVDDLFGKLIGGLD----LDETVVVAL 318
Cdd:cd16144 209 -------------YEKKKKGLRKGQKNP------------------VYAAmIESLDESVGRILDALEelglADNTLVIFT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 319 GDHGwSLGEHAEWA---------KYSNFEVALRVPLIIRSPQFPVAQTK---YYHGItellDVFPTLVDLAGLPKldkcQ 386
Cdd:cd16144 258 SDNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIKPGSVsdvPVIGT----DLYPTFLELAGGPL----P 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 387 SSQELtcgEGKSLYHQLMGlgraDEhvalSQYPRPGML---PTKHPNSDKPklrnikimGYSLRTDIYRYtmwVRFHAQN 463
Cdd:cd16144 329 PPQHL---DGVSLVPLLKG----GE----ADLPRRALFwhfPHYHGQGGRP--------ASAIRKGDWKL---IEFYEDG 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24656835 464 fsrdwhdvyGEELYDHRLDSGEELNL---MPlpqfdDVRQRLRRRLME 508
Cdd:cd16144 387 ---------RVELYNLKNDIGETNNLaaeMP-----EKAAELKKKLDA 420
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-380 |
5.12e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 106.55 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWR----- 98
Cdd:cd16149 1 PNILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGShgktk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 99 ---TFTGNFTTLPQYFKEHGYYTYSCGKvFHPGlssnntddyplswsapafrprteqfmnspvcpdkegilrknlicpve 175
Cdd:cd16149 81 kpeGYLEGQTTLPEVLQDAGYRCGLSGK-WHLG----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 176 lqtqpyktlpdiesvAEALRFVgSRSRHSQEPFFLAMGFHKPHinfrfprqflsrfnlsqfynytedslkppdmpavawn 255
Cdd:cd16149 113 ---------------DDAADFL-RRRAEAEKPFFLSVNYTAPH------------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 256 pytdvrarddfkhsnisfpygpiSPLQaaqirqsYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEW 331
Cdd:cd16149 140 -----------------------SPWG-------YFAAVTGVDRNVGRLLDELEelglTENTLVIFTSDNGFNMGHHGIW 189
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24656835 332 AK------YSNFEVALRVPLIIRSPqfpvAQTKYYHGITEL---LDVFPTLVDLAGLP 380
Cdd:cd16149 190 GKgngtfpLNMYDNSVKVPFIIRWP----GVVPAGRVVDSLvsaYDFFPTLLELAGVD 243
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-508 |
3.73e-24 |
|
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: 103.85 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPdtlhlydfysywrTFTG 102
Cdd:cd16152 1 KPNVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYP-------------TETG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 103 NF----------TTLPQYFKEHGYYTYSCGKvfhpglssnntddyplsWSAPAFRprteqfmnspvcpdkegilrknlic 172
Cdd:cd16152 68 CFrngiplpadeKTLAHYFRDAGYETGYVGK-----------------WHLAGYR------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 173 pVELQTQpyktlpdiesvaEALRFVgsRSRHSQEPFFLAMGFHKPHI-----NFRFPRQFLSRFnlsqfynytedslKPP 247
Cdd:cd16152 106 -VDALTD------------FAIDYL--DNRQKDKPFFLFLSYLEPHHqndrdRYVAPEGSAERF-------------ANF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 248 DMPAvawnpytDVRARddfkhsnisfpygpisPLQAAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHgw 323
Cdd:cd16152 158 WVPP-------DLAAL----------------PGDWAEELPDYLGCCERLDENVGRIRDALKelglYDNTIIVFTSDH-- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 324 slGEH-----AEWaKYSNFEVALRVPLIIRSPQFpvAQTKYYHGITELLDVFPTLVDLAGLPKLDKCQssqeltcgeGKS 398
Cdd:cd16152 213 --GCHfrtrnAEY-KRSCHESSIRVPLVIYGPGF--NGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQ---------GRS 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 399 LYHQLMGLGRADEHVALSQyprpgmlptkhpnsdkpklrnIK--IMGYSLRTDiyRYTMWVRFHAQNFSRD-WHDVYGEE 475
Cdd:cd16152 279 LLPLVDGKVEDWRNEVFIQ---------------------ISesQVGRAIRTD--RWKYSVAAPDKDGWKDsGSDVYVED 335
|
490 500 510
....*....|....*....|....*....|....
gi 24656835 476 -LYDHRLDSGEELNLMPLPQFDDVRQRLRRRLME 508
Cdd:cd16152 336 yLYDLEADPYELVNLIGRPEYREVAAELRERLLA 369
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
24-380 |
6.04e-24 |
|
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: 103.78 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLRPVIGAYgDTLASTPyldnfargSHI------FTRVYSQQSLCAPSRNSLLTGRRP------DTLHLY 91
Cdd:cd16147 1 RPNIVLILTDDQDVELGSM-DPMPKTK--------KLLadqgttFTNAFVTTPLCCPSRASILTGQYAhnhgvtNNSPPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 92 DFYSYWRTFTGNFTTLPQYFKEHGYYTYSCGKVFHPGLSSNNTDDYPLSWSAPAFrprteqfmnsPVCPDKEGilrkNLI 171
Cdd:cd16147 72 GGYPKFWQNGLERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPPGWDEWDG----------LVGNSTYY----NYT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 172 CPVELQTQPYKT-----LPDIesVAE-ALRFVgSRSRHSQEPFFLAMGFHKPHINFRFPRQFLSRF-NLSQFYNYTEDSL 244
Cdd:cd16147 138 LSNGGNGKHGVSypgdyLTDV--IANkALDFL-RRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFpNVTAPPRPPPNNP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 245 KPPDMPAvaWnpytdVRARddfkhsnisfpyGPISPLQAAQIRQSYYA---SVSYVDDLFGKLIGGLD----LDETVVVA 317
Cdd:cd16147 215 DVSDKPH--W-----LRRL------------PPLNPTQIAYIDELYRKrlrTLQSVDDLVERLVNTLEatgqLDNTYIIY 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24656835 318 LGDHGWSLGEHA-EWAKYSNFEVALRVPLIIRSPQFPVAQTKyyHGITELLDVFPTLVDLAGLP 380
Cdd:cd16147 276 TSDNGYHLGQHRlPPGKRTPYEEDIRVPLLVRGPGIPAGVTV--DQLVSNIDLAPTILDLAGAP 337
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
24-380 |
4.55e-23 |
|
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: 101.10 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLrp-vIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWRTFTG 102
Cdd:cd16026 1 KPNIVVILADDLgygdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 103 ---NFTTLPQYFKEHGYYTYSCGKvFHPGlssnntddyplswSAPAFRPRTEQF--------MNSPVCPDKEG----ILR 167
Cdd:cd16026 81 lppDEITIAEVLKKAGYRTALVGK-WHLG-------------HQPEFLPTRHGFdeyfgipySNDMWPFPLYRndppGPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 168 KNLICPVELQTQPyktlPDIES-----VAEALRFVgsrSRHSQEPFFLAMGFHKPHINFRFPRQFLSRfnlsqfynyted 242
Cdd:cd16026 147 PPLMENEEVIEQP----ADQSSltqryTDEAVDFI---ERNKDQPFFLYLAHTMPHVPLFASEKFKGR------------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 243 slkppdmpaVAWNPYTDVrarddfkhsnisfpygpisplqaaqirqsyyasVSYVDDLFGKLIGGLD----LDETVVVAL 318
Cdd:cd16026 208 ---------SGAGLYGDV---------------------------------VEELDWSVGRILDALKelglEENTLVIFT 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24656835 319 GDHGWSLGEHAEW--------AKYSNFEVALRVPLIIRSP-QFPVAQTkyYHGITELLDVFPTLVDLAGLP 380
Cdd:cd16026 246 SDNGPWLEYGGHGgsagplrgGKGTTWEGGVRVPFIAWWPgVIPAGTV--SDELASTMDLLPTLAALAGAP 314
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
25-383 |
4.58e-23 |
|
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: 101.09 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLrpviGaYGD------TLASTPYLDNFARGSHIFTRVYSQQSlCAPSRNSLLTGRRPDTLHLYDFYSYWR 98
Cdd:cd16029 1 PHIVFILADDL----G-WNDvgfhgsDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGMQHGVILAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 99 TFTG---NFTTLPQYFKEHGYYTYSCGKvFHPGLSS-----------------NNTDDY--PLSWSAPAFRPRTEQFMNS 156
Cdd:cd16029 75 EPYGlplNETLLPQYLKELGYATHLVGK-WHLGFYTweytptnrgfdsfygyyGGAEDYytHTSGGANDYGNDDLRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 157 PVcPDKEGilrknlicpvELQTQPYKtlpdiesvAEALRFVgsRSRHSQEPFFLAMGFHKPHinfrFPRQFLSRFnlSQF 236
Cdd:cd16029 154 PA-WDYNG----------TYSTDLFT--------DRAVDII--ENHDPSKPLFLYLAFQAVH----APLQVPPEY--ADP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 237 YNYTEDSLKPPDmpavawnpytdvrarddfkhsnisfpygpisplqaaqiRQSYYASVSYVDDLFGKLIGGLD----LDE 312
Cdd:cd16029 207 YEDKFAHIKDED--------------------------------------RRTYAAMVSALDESVGNVVDALKakgmLDN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 313 TVVVALGDHGwslGEHAE------W----AKYSNFEVALRVPLIIRSPQFPVAQTKYYHGITELLDVFPTLVDLAG---- 378
Cdd:cd16029 249 TLIVFTSDNG---GPTGGgdggsnYplrgGKNTLWEGGVRVPAFVWSPLLPPKRGTVSDGLMHVTDWLPTLLSLAGgdpd 325
|
....*.
gi 24656835 379 -LPKLD 383
Cdd:cd16029 326 dLPPLD 331
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-422 |
6.76e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 100.37 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSqQSLCAPSRNSLLTGRrpdtlhlYDFYSYWRTFT-- 101
Cdd:cd16151 1 PNIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGK-------YNFRNYVVFGYld 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 102 GNFTTLPQYFKEHGYYTYSCGKvfhPGLSSNNT----------DDYPLsWSAPAfRPRTEQFMNSPVCPDKEGILRKnli 171
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGK---WQLGGGRGdgdyphefgfDEYCL-WQLTE-TGEKYSRPATPTFNIRNGKLLE--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 172 cpvelqTQPYKTLPDIEsVAEALRFVgsrSRHSQEPFFL--AMGF-HKPHINFrfprqflsrfnlsqfynytedslkpPD 248
Cdd:cd16151 145 ------TTEGDYGPDLF-ADFLIDFI---ERNKDQPFFAyyPMVLvHDPFVPT-------------------------PD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 249 MPavAWNPYTDVRARDDFKHSnisfpygpisplqaaqirqsyyASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWS 324
Cdd:cd16151 190 SP--DWDPDDKRKKDDPEYFP----------------------DMVAYMDKLVGKLVDKLEelglRENTIIIFTGDNGTH 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 325 LGEHAEW-------AKYSNFEVALRVPLIIRSPQFpVAQTKYYHGITELLDVFPTLVDLAGLPKLDKCQssqeltcGEGK 397
Cdd:cd16151 246 RPITSRTngrevrgGKGKTTDAGTHVPLIVNWPGL-IPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYP-------LDGR 317
|
410 420
....*....|....*....|....*
gi 24656835 398 SLYHQLMGLGRADEHVALSQYPRPG 422
Cdd:cd16151 318 SFAPQLLGKTGSPRREWIYWYYRNP 342
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-412 |
6.97e-23 |
|
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: 100.75 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWR--TFT 101
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGqdPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 102 GNFTTLPQYFKEHGYYTYSCGKVfhpGLSSNNTDDYPLS--WS----------APAFRPrTEQFMNspvcpDKEGILRKN 169
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKW---GLGGPGTPGHPTKqgFDyfygyldqvhAHNYYP-EYLWRN-----GEKVPLPNN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 170 LICPVELQ--TQPYKTL--PDIeSVAEALRFVgsrSRHSQEPFFLAMGFHKPHINFRFPRQflsrfnlsqfynyTEDSLK 245
Cdd:cd16145 152 VIPPLDEGnnAGGGGGTysHDL-FTDEALDFI---RENKDKPFFLYLAYTLPHAPLQVPDD-------------GPYKYK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 246 PPDMPAVAWNPYTDVRARddfkhsnisfpygpisplqaaqirqsYYASVSYVDDLFGKLIG---GLDLDE-TVVVALGDH 321
Cdd:cd16145 215 PKDPGIYAYLPWPQPEKA--------------------------YAAMVTRLDRDVGRILAllkELGIDEnTLVVFTSDN 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 322 GWSLgEHAEWA--------------KYSNFEVALRVPLIIRSP-QFPVAQTKYYhgITELLDVFPTLVDLAGLP---KLD 383
Cdd:cd16145 269 GPHS-EGGSEHdpdffdsngplrgyKRSLYEGGIRVPFIARWPgKIPAGSVSDH--PSAFWDFMPTLADLAGAEppeDID 345
|
410 420
....*....|....*....|....*....
gi 24656835 384 kcqssqeltcgeGKSLYHQLMGLGRADEH 412
Cdd:cd16145 346 ------------GISLLPTLLGKPQQQQH 362
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
25-508 |
2.62e-22 |
|
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: 99.76 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPdtlHLYDFYSYWRTFTGN 103
Cdd:cd16156 1 KQFIFIMTDTQRwDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYP---HTNGSWTNCMALGDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 104 FTTLPQYFKEHGYYTYSCGKVFHPGlssnntDDY------PLSWSaPAFRPRTEQFMNSpvCPDKEGILRKNLicpvelQ 177
Cdd:cd16156 78 VKTIGQRLSDNGIHTAYIGKWHLDG------GDYfgngicPQGWD-PDYWYDMRNYLDE--LTEEERRKSRRG------L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 178 TQPYKtlpdiESVAE-----------ALRFVgsrSRHSQEPFFLAMGFHKPHINFRFPRQFLS-----RFNLSQFYNyte 241
Cdd:cd16156 143 TSLEA-----EGIKEeftyghrctnrALDFI---EKHKDEDFFLVVSYDEPHHPFLCPKPYASmykdfEFPKGENAY--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 242 DSL--KPPDMPAVAWNPYTDVRARDDFKHsnisfpygpisplqaaqirQSYYASVSYVDDLFGKLIGGLD--LDETVVVA 317
Cdd:cd16156 212 DDLenKPLHQRLWAGAKPHEDGDKGTIKH-------------------PLYFGCNSFVDYEIGRVLDAADeiAEDAWVIY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 318 LGDHGWSLGEHAEWAK-YSNFEVALRVPLIIRSPQFPVAQTKYYHGITeLLDVFPTLVDLAGLPKLDKCQSS---QELTC 393
Cdd:cd16156 273 TSDHGDMLGAHKLWAKgPAVYDEITNIPLIIRGKGGEKAGTVTDTPVS-HIDLAPTILDYAGIPQPKVLEGEsilATIED 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 394 GEGKSLYHQLMGLGRAD-EHVALSqyprpGMLPTKHPNSDKPKLrNIKIMGyslrTDiyrytmwvrfhaqnfsrdwhdvy 472
Cdd:cd16156 352 PEIPENRGVFVEFGRYEvDHDGFG-----GFQPVRCVVDGRYKL-VINLLS----TD----------------------- 398
|
490 500 510
....*....|....*....|....*....|....*.
gi 24656835 473 geELYDHRLDSGEELNLMPLPQFDDVRQRLRRRLME 508
Cdd:cd16156 399 --ELYDLEKDPYEMHNLIDDPDYADVRDQLHDELLD 432
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
24-380 |
7.11e-20 |
|
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: 91.74 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLRP-VIGAYGdTLASTPYLDNFARGSHIFTRVYSQqSLCAPSRNSLLTGRRP-------DTLHLYDFYS 95
Cdd:cd16025 2 RPNILLILADDLGFsDLGCFG-GEIPTPNLDALAAEGLRFTNFHTT-ALCSPTRAALLTGRNHhqvgmgtMAELATGKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 96 YWRTFTGNFTTLPQYFKEHGYYTYSCGKvFHpglssNNTDDYPLSwsapafrprteqfmnspvcpdkegilrknlicpve 175
Cdd:cd16025 80 YEGYLPDSAATIAEVLKDAGYHTYMSGK-WH-----LGPDDYYST----------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 176 lqtqpyKTLPDiesvaEALRFVGSRsRHSQEPFFLAMGFHKPHINFRFPRQFLSRFnLSQF---YN-YTEDSLK------ 245
Cdd:cd16025 119 ------DDLTD-----KAIEYIDEQ-KAPDKPFFLYLAFGAPHAPLQAPKEWIDKY-KGKYdagWDaLREERLErqkelg 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 246 --PPDMPAVAWNPytDVRARDDfkhsnisfpygpISP-LQAAQIRQ--SYYASVSYVDDLFGKLIGGLD----LDETVVV 316
Cdd:cd16025 186 liPADTKLTPRPP--GVPAWDS------------LSPeEKKLEARRmeVYAAMVEHMDQQIGRLIDYLKelgeLDNTLII 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24656835 317 ALGDHGWSlGEHAeWA----------KYSNFEVALRVPLIIRSPQFPVAQTKYYHGITELLDVFPTLVDLAGLP 380
Cdd:cd16025 252 FLSDNGAS-AEPG-WAnasntpfrlyKQASHEGGIRTPLIVSWPKGIKAKGGIRHQFAHVIDIAPTILELAGVE 323
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-384 |
7.86e-20 |
|
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: 91.06 E-value: 7.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDlrpV----IGAYGDTL---ASTPYLDNFARGSHIFTRVYSQQSlCAPSRNSLLTGRRPdtlhlydfysyw 97
Cdd:cd16142 1 PNILVILGDD---IgwgdLGCYGGGIgrgAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 98 rTFTGNFT---------------TLPQYFKEHGYYTYSCGKvFHPGlssnntddyplswSAPAFRPrTEQ-FmnspvcpD 161
Cdd:cd16142 65 -IRTGLTTvglpgspgglppwepTLAELLKDAGYATAQFGK-WHLG-------------DEDGRLP-TDHgF-------D 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 162 K-EGILRKNLicpvelqtqpyktlpDIESVAEALRFVGsRSRHSQEPFFLAMGFHKPHinfrfprqflsrfnlsqfynyt 240
Cdd:cd16142 122 EfYGNLYHTI---------------DEEIVDKAIDFIK-RNAKADKPFFLYVNFTKMH---------------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 241 edslkPPDMPavawnpytdvraRDDFKHSNisfpygpisplqaaqIRQSYYA-SVSYVDDLFGKLIGGLD----LDETVV 315
Cdd:cd16142 164 -----FPTLP------------SPEFEGKS---------------SGKGKYAdSMVELDDHVGQILDALDelgiADNTIV 211
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24656835 316 VALGDHGwslGEHAEW----------AKYSNFEVALRVPLIIRSPQFPVAQTKyYHGITELLDVFPTLVDLAGLPKLDK 384
Cdd:cd16142 212 IFTTDNG---PEQDVWpdggytpfrgEKGTTWEGGVRVPAIVRWPGKIKPGRV-SNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
25-453 |
9.62e-20 |
|
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: 90.68 E-value: 9.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFD--DLRpVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPdtlHLYDFYSYWRTFTG 102
Cdd:cd16171 1 PNVVMVMSDsfDGR-LTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT---HLTESWNNYKGLDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 103 NFTTLPQYFKEHGYYTYSCGKVFHpglssnNTDDYPLSwsapafrPRTEQFM-NSPVCPDKEGILRKNLicpVELQTQPY 181
Cdd:cd16171 77 NYPTWMDRLEKHGYHTQKYGKLDY------TSGHHSVS-------NRVEAWTrDVPFLLRQEGRPTVNL---VGDRSTVR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 182 KTLPDIESVAEALRFVGSRSRHSQEPFFLAMGFHKPHinfrfprqflsrfnlsqfynytedslkppdmpavawnPYTDVR 261
Cdd:cd16171 141 VMLKDWQNTDKAVHWIRKEAPNLTQPFALYLGLNLPH-------------------------------------PYPSPS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 262 ARDDFkhsnisfpyGPISplqaaQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEWAKYSNF 337
Cdd:cd16171 184 MGENF---------GSIR-----NIRAFYYAMCAETDAMLGEIISALKdtglLDKTYVFFTSDHGELAMEHRQFYKMSMY 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 338 EVALRVPLIIRSPQFPVAQTkyYHGITELLDVFPTLVDLAGLPKLdkcqssqeltcgEGKSLYHQLMGLGRADEHVALSQ 417
Cdd:cd16171 250 EGSSHVPLLIMGPGIKAGQQ--VSDVVSLVDIYPTMLDIAGVPQP------------QNLSGYSLLPLLSESSIKESPSR 315
|
410 420 430
....*....|....*....|....*....|....*.
gi 24656835 418 YPRPGMLPTKHPNSdkpklrNIKIMGYSLRTDIYRY 453
Cdd:cd16171 316 VPHPDWVLSEFHGC------NVNASTYMLRTNSWKY 345
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-417 |
5.46e-18 |
|
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: 85.72 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLRP-VIGAYGDT-LASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPdtlhlydfysyWRT--- 99
Cdd:cd16143 1 PNIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYP-----------WRSrlk 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 100 -----------FTGNFTTLPQYFKEHGYYTYSCGKvFHPGLssnntdDYPLSWSAPAFRPRTEQF-MNSPVcpdKEGilr 167
Cdd:cd16143 70 ggvlggfspplIEPDRVTLAKMLKQAGYRTAMVGK-WHLGL------DWKKKDGKKAATGTGKDVdYSKPI---KGG--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 168 knlicPVELQTQPYKTLPDIES----VAEALRFVGSRSRhSQEPFFLAMGFHKPHInfrfprqflsrfnlsqfynyteds 243
Cdd:cd16143 137 -----PLDHGFDYYFGIPASEVlptlTDKAVEFIDQHAK-KDKPFFLYFALPAPHT------------------------ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 244 lkpPDMPAVAWNPYTDVRARDDFkhsnisfpygpisplqaaqIRQsyyasvsyVDDLFGKLIGGLD----LDETVVVALG 319
Cdd:cd16143 187 ---PIVPSPEFQGKSGAGPYGDF-------------------VYE--------LDWVVGRILDALKelglAENTLVIFTS 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 320 DHGWSLGEHAEWA--------------KYSNFEVALRVPLIIRSP-QFPVAQTKyyHGITELLDVFPTLVDLAGLpKLDK 384
Cdd:cd16143 237 DNGPSPYADYKELekfghdpsgplrgmKADIYEGGHRVPFIVRWPgKIPAGSVS--DQLVSLTDLFATLAAIVGQ-KLPD 313
|
410 420 430
....*....|....*....|....*....|....
gi 24656835 385 cqssqelTCGE-GKSLYHQLMGLGRADEHVALSQ 417
Cdd:cd16143 314 -------NAAEdSFSFLPALLGPKKQEVRESLVH 340
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-420 |
9.74e-17 |
|
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: 81.10 E-value: 9.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRP------DTLHLYDFYsyw 97
Cdd:cd16035 1 PNILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPqqtgvtDTLGSPMQP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 98 rTFTGNFTTLPQYFKEHGYYTYSCGKvFHpgLSSnntddypLSWSAPAFRPRTeqfmnspvcpdkegilrknlicpvelq 177
Cdd:cd16035 78 -LLSPDVPTLGHMLRAAGYYTAYKGK-WH--LSG-------AAGGGYKRDPGI--------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 178 tqpyktlpdiesVAEALRFV--GSRSRHSQEPFFLAMGFHKPHinfrfprqflsrfnlsqfynyteDSLKPPDMPavawn 255
Cdd:cd16035 120 ------------AAQAVEWLreRGAKNADGKPWFLVVSLVNPH-----------------------DIMFPPDDE----- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 256 pyTDVRARDDFkhsnisfpygpisplqaaqirqsYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSLGEHAEW 331
Cdd:cd16035 160 --ERWRRFRNF-----------------------YYNLIRDVDRQIGRVLDALDasglADNTIVVFTSDHGEMGGAHGLR 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 332 AKYSN-FEVALRVPLIIRSPQ-FPVAQTKyyHGITELLDVFPTLVDLAGLPKLDKCQSSQELtcgEGKSLYHQLMGL-GR 408
Cdd:cd16035 215 GKGFNaYEEALHVPLIISHPDlFGTGQTT--DALTSHIDLLPTLLGLAGVDAEARATEAPPL---PGRDLSPLLTDAdAD 289
|
410
....*....|..
gi 24656835 409 ADEHVALSQYPR 420
Cdd:cd16035 290 AVRDGILFTYDR 301
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
25-378 |
1.05e-16 |
|
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: 80.42 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVI---FDDlrPVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRN--SLLTGRRPDTLHLYDFYSYwrt 99
Cdd:cd16015 1 PNVIVILlesFSD--PYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLY--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 100 FTGNFTTLPQYFKEHGYYTYScgkvFHPGLSSN-NTDD-YPL-----SWSAPAFrPRTEQFMNSPVCPDKEgILRKnlic 172
Cdd:cd16015 76 KLNPLPSLPSILKEQGYETIF----IHGGDASFyNRDSvYPNlgfdeFYDLEDF-PDDEKETNGWGVSDES-LFDQ---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 173 pvelqtqpykTLPDIESvaealrfvgsrsrHSQEPFF---LAMGFHKPhinfrfprqflsrfnlsqfYNYTEDSLKPPDM 249
Cdd:cd16015 146 ----------ALEELEE-------------LKKKPFFiflVTMSNHGP-------------------YDLPEEKKDEPLK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 250 PAVAWNPYTDvrarddfkhsnisfpygpisplqaaqirqsYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSL 325
Cdd:cd16015 184 VEEDKTELEN------------------------------YLNAIHYTDKALGEFIEKLKksglYENTIIVIYGDHLPSL 233
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24656835 326 GEHAEWAKYSNFEvALRVPLIIRSPqfPVAQTKYYHGITELLDVFPTLVDLAG 378
Cdd:cd16015 234 GSDYDETDEDPLD-LYRTPLLIYSP--GLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
24-380 |
3.36e-16 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 81.18 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPD----TLHLYDFYSYWR 98
Cdd:cd16159 1 KPNIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIrsgmASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 99 TFTG----NFTTLPQYFKEHGYYTYSCGKvFHPGLSSNNTDD---------------YPL------------SWSAPAFR 147
Cdd:cd16159 81 ASSGglppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDfchhplnhgfdyfygLPLtnlkdcgdgsngEYDLSFDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 148 PRTEQFMNSPVCP------DKEGILRKN-----LICPV------------------------ELQTQPYkTLPDIES--V 190
Cdd:cd16159 160 LFPLLTAFVLITAltifllLYLGAVSKRffvflLILSLlfislfflllitnryfncilmrnhEVVEQPM-SLENLTQrlT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 191 AEALRFVgsrSRHSQEPFFLAMGFHKPHinfrfprqflsrfnlsqfynytedslkppdmpavawnpyTDVRARDDFKHSN 270
Cdd:cd16159 239 KEAISFL---ERNKERPFLLVMSFLHVH---------------------------------------TALFTSKKFKGRS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 271 ISFPYGpisplqaaqirqsyyASVSYVDDLFGKLIGGLD----LDETVVVALGDHGWSL------GEHAEW-------AK 333
Cdd:cd16159 277 KHGRYG---------------DNVEEMDWSVGQILDALDelglKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKK 341
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 24656835 334 YSNFEVALRVPLIIRSPQFPVAQTKYYHGiTELLDVFPTLVDLAGLP 380
Cdd:cd16159 342 MGGWEGGIRVPTIVRWPGVIPPGSVIDEP-TSLMDIFPTVAALAGAP 387
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
24-378 |
7.10e-16 |
|
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: 79.78 E-value: 7.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLrpvigAYGDtLASTPY-------LDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLY--DFY 94
Cdd:cd16160 1 KPNIVLFFADDM-----GYGD-LASYGHptqergpIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggTRV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 95 SYWRTFTG---NFTTLPQYFKEHGYYTYSCGKvFHPGLSSNNTDD-YPLswsaPAFR---------PrteqFMNSPVCPD 161
Cdd:cd16160 75 FLPWDIGGlpkTEVTMAEALKEAGYTTGMVGK-WHLGINENNHSDgAHL----PSHHgfdfvgtnlP----FTNSWACDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 162 -KEGILRKNLI-CPV----ELQTQP--YKTLPDiESVAEALRFVGSRsrhSQEPFFLAMGFHKPHINfrfprQFlsrfnl 233
Cdd:cd16160 146 tGRHVDFPDRSaCFLyyndTIVEQPiqHEHLTE-TLVGDAKSFIEDN---QENPFFLYFSFPQTHTP-----LF------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 234 sqfynytedslkppdmpavawnpytdvrARDDFKHSNISFPYGPisplqaaQIRQSYYASVSYVDDLFGKligGLDlDET 313
Cdd:cd16160 211 ----------------------------ASKRFKGKSKRGRYGD-------NINEMSWAVGEVLDTLVDT---GLD-QNT 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24656835 314 VVVALGDHgwslGEHAEW------------AKYSNFEVALRVPLIIRSPQfpVAQTKYYHGITELLDVFPTLVDLAG 378
Cdd:cd16160 252 LVFFLSDH----GPHVEYcleggstgglkgGKGNSWEGGIRVPFIAYWPG--TIKPRVSHEVVSTMDIFPTFVDLAG 322
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
17-380 |
4.16e-15 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 77.77 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 17 DAAAPPRRPNVVMVI---FDDlrPVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGrRPDTLHLYDF 93
Cdd:COG1368 227 NPFGPAKKPNVVVILlesFSD--FFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-LPPLPGGSPY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 94 YSYWRTftgNFTTLPQYFKEHGYYTYscgkVFHPGLSSnntddyplswsapafrprteqFMNspvcpdkegilRKNlicp 173
Cdd:COG1368 304 KRPGQN---NFPSLPSILKKQGYETS----FFHGGDGS---------------------FWN-----------RDS---- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 174 velqtqpyktlpdiesvaealrfvgsrsrhsqepFFLAMGFHkpHINFR--FPRQFLSRFNLS--QFYNYTEDSLKPPDM 249
Cdd:COG1368 341 ----------------------------------FYKNLGFD--EFYDRedFDDPFDGGWGVSdeDLFDKALEELEKLKK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 250 PAVAW-------NPYT---DVRARDDFKHSNIsfpygpisplqaaqirQSYYASVSYVDDLFGKLIGGLD----LDETVV 315
Cdd:COG1368 385 PFFAFlitlsnhGPYTlpeEDKKIPDYGKTTL----------------NNYLNAVRYADQALGEFIEKLKksgwYDNTIF 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24656835 316 VALGDH-GWSLGEHAEWAKYSNFevalRVPLIIRSPqfPVAQTKYYHGITELLDVFPTLVDLAGLP 380
Cdd:COG1368 449 VIYGDHgPRSPGKTDYENPLERY----RVPLLIYSP--GLKKPKVIDTVGSQIDIAPTLLDLLGID 508
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
24-380 |
1.32e-13 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 72.88 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLR-PVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRP-------DTLHLYDFYS 95
Cdd:cd16157 1 KPNIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPirngfytTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 96 YWRTFTG---NFTTLPQYFKEHGYYTYSCGKvFHPGlssNNTDDYPLS-----W-SAPA--FRPRTEQFM-NSPVCPDKE 163
Cdd:cd16157 81 PQNIVGGipdSEILLPELLKKAGYRNKIVGK-WHLG---HRPQYHPLKhgfdeWfGAPNchFGPYDNKAYpNIPVYRDWE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 164 GILRKNLICPVELQ------TQPYktlpdiesVAEALRFVgSRSRHSQEPFFLamgfhkphinfrfprqflsrfnlsqfy 237
Cdd:cd16157 157 MIGRYYEEFKIDKKtgesnlTQIY--------LQEALEFI-EKQHDAQKPFFL--------------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 238 nytedslkppdmpavAWNPytdvrardDFKHSnisfPYGPISPLQAAQIRQSYYASVSYVDDLFGKLIGGLDL----DET 313
Cdd:cd16157 201 ---------------YWAP--------DATHA----PVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSlgieNNT 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24656835 314 VVVALGDHGWSLGEHAEW---------AKYSNFEVALRVPLIIRSPQfPVAQTKYYHGITELLDVFPTLVDLAGLP 380
Cdd:cd16157 254 FVFFSSDNGAALISAPEQggsngpflcGKQTTFEGGMREPAIAWWPG-HIKPGQVSHQLGSLMDLFTTSLALAGLP 328
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
24-380 |
4.34e-13 |
|
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: 70.96 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 24 RPNVVMVIFDDLrpvigAYGD-------TLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDfySY 96
Cdd:cd16161 1 KPNFLLLFADDL-----GWGDlganwapNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH--NF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 97 WRTFTG----NFTTLPQYFKEHGYYTYSCGKvFHPGlssnNTDDYplswsAPAFRPRTEQFmnspvcpdkeGIlrknlic 172
Cdd:cd16161 74 LPTSVGglplNETTLAEVLRQAGYATGMIGK-WHLG----QREAY-----LPNSRGFDYYF----------GI------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 173 pvelqtqPYK---TLPDiESVAEALRFVGsRSRHSQEPFFLAMGFHKPHInfrfPRQFLSRFNLSqfynytedslkppdm 249
Cdd:cd16161 127 -------PFShdsSLAD-RYAQFATDFIQ-RASAKDRPFFLYAALAHVHV----PLANLPRFQSP--------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 250 pavawnpytdvrarddfkhSNISFPYGpisplqaaqirqsyyASVSYVDDLFGKLIGGLD----LDETVVVALGDHG-WS 324
Cdd:cd16161 179 -------------------TSGRGPYG---------------DALQEMDDLVGQIMDAVKhaglKDNTLTWFTSDNGpWE 224
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24656835 325 LGE-------HAEW--------AKYSNFEVALRVPLIIRSP-QFPVAQTKYyhGITELLDVFPTLVDLAGLP 380
Cdd:cd16161 225 VKCelavgpgTGDWqgnlggsvAKASTWEGGHREPAIVYWPgRIPANSTSA--ALVSTLDIFPTVVALAGAS 294
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
16-373 |
4.12e-12 |
|
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: 68.39 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 16 LDAAAPPRRPNVVMVIFDDLRpvigayGDTL--ASTPYLDNFARGSHIFTRVYSqqslcapSRNSLLTGrrpdtlhLYD- 92
Cdd:COG3083 236 LQFSDPAKPPNILLIVVDSLR------ADMLdpEVMPNLYAFAQRSLRFTNHYS-------SGNSTRAG-------LFGl 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 93 FYS----YWRTFTGNFTT--LPQYFKEHGYytyscgkvfhpglssnntdDYPLSWSAPafrprteqfMNSPvcPDKEGIL 166
Cdd:COG3083 296 FYGlpgnYWDSILAERTPpvLIDALQQQGY-------------------QFGLFSSAG---------FNSP--LFRQTIF 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 167 RKnlICPVELQTQPYKTLPDIESVAEALRFVGSRSrhSQEPFFLamgfhkphinfrfprqFLsrfnlsqFYNYTEDSLKP 246
Cdd:COG3083 346 SD--VSLPRLHTPGGPAQRDRQITAQWLQWLDQRD--SDRPWFS----------------YL-------FLDAPHAYSFP 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 247 PDMPAVawnpytdvrarddFKHSNISFPYGPISPLQAAQIRQSYYASVSYVDDLFGKLIGGLD----LDETVVVALGDHG 322
Cdd:COG3083 399 ADYPKP-------------FQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEqrglLENTIVIITADHG 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24656835 323 WSLGEHAE--WAKYSNF-EVALRVPLIIRSPQFPvAQTkyYHGITELLDVFPTL 373
Cdd:COG3083 466 EEFNENGQnyWGHNSNFsRYQLQVPLVIHWPGTP-PQV--ISKLTSHLDIVPTL 516
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
25-134 |
3.27e-11 |
|
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: 65.54 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDL-RPVIGAYGDTLASTPYLDNFARGSHIFTRVYSQQSLCAPSRNSLLTGRRPDTLHLYDFYSYWRTFTG- 102
Cdd:cd16158 2 PNIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGl 81
|
90 100 110
....*....|....*....|....*....|....
gi 24656835 103 --NFTTLPQYFKEHGYYTYSCGKvFHPGLSSNNT 134
Cdd:cd16158 82 plNETTIAEVLKTVGYQTAMVGK-WHLGVGLNGT 114
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-378 |
5.34e-09 |
|
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: 58.13 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 25 PNVVMVIFDDLrpviG-------AYGDTLASTPYLDNFARGSHIFTRVYSQqSLCAPSRNSLLTGRR---------PDTL 88
Cdd:cd16154 1 PNILLIIADDQ----GldssaqySLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYgfrtgvlavPDEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 89 HLydfysywrtftgNFTTLPQYFKE----HGYYTYSCGKvFHPGLSSNNtddyplswsapafrprteqFMNSPVCPDKEG 164
Cdd:cd16154 76 LL------------SEETLLQLLIKdattAGYSSAVIGK-WHLGGNDNS-------------------PNNPGGIPYYAG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 165 ILRKNLicpvelqtQPY----KTLPDI----------ESVAEALRFVGSRSrhsqEPFFLAMGFHKPHINFRFPRQFLSR 230
Cdd:cd16154 124 ILGGGV--------QDYynwnLTNNGQttnsteyattKLTNLAIDWIDQQT----KPWFLWLAYNAPHTPFHLPPAELHS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 231 FNLSqfynytedslkpPDMPAVAWNPytdvrarddfkhsnisfpygpisplqaaqiRQSYYASVSYVDDLFGKLIGGLD- 309
Cdd:cd16154 192 RSLL------------GDSADIEANP------------------------------RPYYLAAIEAMDTEIGRLLASIDe 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 310 --LDETVVVALGDHG--------WSLGEHaewAKYSNFEVALRVPLIIRS---PQFPVAQTKYYHGItellDVFPTLVDL 376
Cdd:cd16154 230 eeRENTIIIFIGDNGtpgqvvdlPYTRNH---AKGSLYEGGINVPLIVSGagvERANERESALVNAT----DLYATIAEL 302
|
..
gi 24656835 377 AG 378
Cdd:cd16154 303 AG 304
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
287-377 |
1.85e-08 |
|
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: 55.12 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 287 RQSYYASVSYVDDLFGKLIGGL----DLDETVVVALGDHGWSLGEHAEWAKYS----NFEVALRVPLIIRSPQFPVAQTK 358
Cdd:cd00016 141 TPEYYDAVEEIDERIGKVLDALkkagDADDTVIIVTADHGGIDKGHGGDPKADgkadKSHTGMRVPFIAYGPGVKKGGVK 220
|
90
....*....|....*....
gi 24656835 359 yyHGITELLDVFPTLVDLA 377
Cdd:cd00016 221 --HELISQYDIAPTLADLL 237
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
5-322 |
5.97e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 51.67 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 5 RLLLSLMMPVLLDA--AAPPRRPNVVMVIFDDLRPvigaygDTL--ASTPYLDNFARGSHIFTRVYSQQ-SLCAPSRNSL 79
Cdd:COG1524 2 KRGLSLLLASLLAAaaAAAPPAKKVVLILVDGLRA------DLLerAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 80 LTGRRPDtlhlydfysywrtftgnfttlpqyfkEHGyytyscgkVFHpglssnntddyplswsapafrprteqfmNSPVC 159
Cdd:COG1524 76 LTGLYPG--------------------------EHG--------IVG----------------------------NGWYD 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 160 PDKEGILrkNLICPVELQTQPYKTLPdIESVAEALRFVGSRSRHSQEPFFLAMGFhkphINFRFPRQFLSRFNLSQFYNY 239
Cdd:COG1524 94 PELGRVV--NSLSWVEDGFGSNSLLP-VPTIFERARAAGLTTAAVFWPSFEGSGL----IDAARPYPYDGRKPLLGNPAA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 240 TEDSL---------KPPDMpAVAWNPYTdvrarDDFKHSnisfpYGPISPLQAAQIRQsyyasvsyVDDLFGKLIGGLD- 309
Cdd:COG1524 167 DRWIAaaalellreGRPDL-LLVYLPDL-----DYAGHR-----YGPDSPEYRAALRE--------VDAALGRLLDALKa 227
|
330
....*....|....*.
gi 24656835 310 ---LDETVVVALGDHG 322
Cdd:COG1524 228 rglYEGTLVIVTADHG 243
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
264-378 |
1.21e-05 |
|
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: 46.81 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 264 DDFKHSnisfpYGPISPlqaaQIRQSyyasVSYVDDLFGKLIGGLD----LDETVVVALGDHGWS-LGEHAewakYSNFE 338
Cdd:cd16018 168 DSAGHK-----YGPDSP----EVNEA----LKRVDRRLGYLIEALKerglLDDTNIIVVSDHGMTdVGTHG----YDNEL 230
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 24656835 339 VALRVPLIIRSPQFPVaqtKYYHGITELLDVFPTLVDLAG 378
Cdd:cd16018 231 PDMRAIFIARGPAFKK---GKKLGPFRNVDIYPLMCNLLG 267
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
23-379 |
4.93e-05 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 45.31 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 23 RRPNVVMVIFDDLRPV-IGAYGDTLASTPYLDNFARGSHIFTRVYSqqslCAPS-RNSLltgrrPDTLHLYDFYSYWRTF 100
Cdd:cd16017 1 KPKNVVLVIGESARRDhMSLYGYPRDTTPFLSKLKKNLIVFDNVIS----CGTStAVSL-----PCMLSFANRENYDRAY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 101 tgNFTTLPQYFKEHGYYTY------SCGKVFHPGLSSNNTDDYPLSwsapafrprtEQFMNSPVCPDkeGILrknlicpv 174
Cdd:cd16017 72 --YQENLIDLAKKAGYKTYwisnqgGCGGYDTRISAIAKIETVFTN----------KGSCNSSNCYD--EAL-------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 175 elqtqpyktLPDIESVAEAlrfvgsrsrhSQEPFFLA---MGFHKPHINfRFPRQFlSRFnlsqfynytedslkppdmpa 251
Cdd:cd16017 130 ---------LPLLDEALAD----------SSKKKLIVlhlMGSHGPYYD-RYPEEF-AKF-------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656835 252 vawNPYTDVRARDDFKhsnisfpygpisplqaAQIRQSYYASVSYVDDLFGKLIGGL--DLDETVVVALGDHGWSLGEHA 329
Cdd:cd16017 169 ---TPDCDNELQSCSK----------------EELINAYDNSILYTDYVLSQIIERLkkKDKDAALIYFSDHGESLGENG 229
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24656835 330 EW--AKYSNFEVALRVPLIIRSP-----QFPVAQ------TKYYHgitelLDVFPTLVDLAGL 379
Cdd:cd16017 230 LYlhGAPYAPKEQYHVPFIIWSSdsykqRYPVERlrankdRPFSH-----DNLFHTLLGLLGI 287
|
|
| |
