|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
40-543 |
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: 598.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFS 119
Cdd:cd16030 4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 120 TIPQYFKENGYVTMSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLP 199
Cdd:cd16030 84 TLPQYFKENGYTTAGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 200 DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQ 279
Cdd:cd16030 162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 280 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRV 359
Cdd:cd16030 241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 360 PLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvelCREGQN 439
Cdd:cd16030 321 PLIIRAPGVTKP------------------------GKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 440 LQKHLQlhdleeEPDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikVMGYSIRTVDYRYTVWVgfdpseflaNFSDI 519
Cdd:cd16030 366 LVPLLK------NPSAKWKDA---AFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKV 411
|
490 500
....*....|....*....|....
gi 84781812 520 HAGELYFVDSDPLQDHNVYNDSQH 543
Cdd:cd16030 412 GAEELYDHKNDPNEWKNLANDPEY 435
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
22-540 |
1.82e-92 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 288.32 E-value: 1.82e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 22 FCIALESAAQGNSATDALNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPD 100
Cdd:COG3119 7 LLLALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 101 TTRLYDFNSYWRVH-SGNFSTIPQYFKENGYVTMSVGKVFHpgissnHSDDYpyswsfppyhpssekyentktckgqdgk 179
Cdd:COG3119 87 RTGVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTDL---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 180 lhanllcpvdvadvpegtlpdkqSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdphvpd 259
Cdd:COG3119 133 -----------------------LTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL-------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 260 slpPVAYNPWmdireredvqalnisvpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGW 339
Cdd:COG3119 182 ---PPNLAPR-------------------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 340 ALGEHG-EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 418
Cdd:COG3119 240 SLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIKA------------------------GSVSDALVSLIDLLPTLLDLAGV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 419 PVPPRCpipsfhvelcrEGQNLQKHLQlhdlEEEPDlfgnPRELIaYSQYPRPAdfpqwnsdkpslndikvMGYSIRTVD 498
Cdd:COG3119 296 PIPEDL-----------DGRSLLPLLT----GEKAE----WRDYL-YWEYPRGG-----------------GNRAIRTGR 338
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 84781812 499 YRYTVWVGFDPSEflanfsdihagELYFVDSDPLQDHNVYND 540
Cdd:COG3119 339 WKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
40-551 |
1.18e-66 |
|
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: 220.46 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFS 119
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 120 TIPQYFKENGYVTMSVGKVFHPGissnhsdDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANllcpvdvadvpegtlP 199
Cdd:cd16027 82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRA---------------K 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 200 DKQsteeairllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapDPHVPDsLPPVaynpwmdireREDVQ 279
Cdd:cd16027 140 KGQ-----------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKV--PPYLPD-TPEV----------REDLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 280 AlnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGehgeWAKYSNFDVATRV 359
Cdd:cd16027 190 D---------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGLRV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 360 PLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvELcrEGQN 439
Cdd:cd16027 245 PLIVRWPGKIKP------------------------GSVSDALVSFIDLAPTLLDLAGIEPPE---------YL--QGRS 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 440 LqkhlqLHDLEEEPDlfgNPRELIaYSQYPRpadfpqwnsdkpslNDIKVMGY-SIRTVDYRYTVwvgfdpseflaNFSD 518
Cdd:cd16027 290 F-----LPLLKGEKD---PGRDYV-FAERDR--------------HDETYDPIrSVRTGRYKYIR-----------NYMP 335
|
490 500 510
....*....|....*....|....*....|...
gi 84781812 519 IhagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16027 336 E---ELYDLKNDPDELNNLADDPEYAEVLEELR 365
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-551 |
6.48e-63 |
|
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: 212.08 E-value: 6.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY----DFNSYWRVH 114
Cdd:cd16033 2 NILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 115 SGNFSTIPQYFKENGYVTMSVGKvFHPGISSNhsddyPYSWSFPPYHPssekYENTKtckgqdgklhanllcpvdvadvp 194
Cdd:cd16033 82 PPGVETFSEDLREAGYRNGYVGK-WHVGPEET-----PLDYGFDEYLP----VETTI----------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 195 EGTLpdkqsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPHVPDSLPPVAYNpwmDIRE 274
Cdd:cd16033 129 EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYR---RERK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 275 REDVQALNisvpygpipEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSNF 353
Cdd:cd16033 201 RWGVDTED---------EEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKgPFMY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 354 DVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCpipsfhvel 433
Cdd:cd16033 272 EETYRIPLIIKWPGVIAA------------------------GQVVDEFVSLLDLAPTILDLAGVDVPPKV--------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 434 crEGQNLQKHLqlhdLEEEPDlfgNPRELIaysqyprpadFPQWNSdkpslNDIKVMGYSIRTVDYRYtVWVGFDpsefl 513
Cdd:cd16033 319 --DGRSLLPLL----RGEQPE---DWRDEV----------VTEYNG-----HEFYLPQRMVRTDRYKY-VFNGFD----- 368
|
490 500 510
....*....|....*....|....*....|....*...
gi 84781812 514 anfsdihAGELYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16033 369 -------IDELYDLESDPYELNNLIDDPEYEEILREMR 399
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
40-551 |
6.55e-63 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 212.39 E-value: 6.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNf 118
Cdd:cd16031 4 NIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFDASQP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 sTIPQYFKENGYVTMSVGKvFHPGISSNHSD---DYPYSWS-----FPPYHPSSEKYentktcKGQDGklHANLLCpvdv 190
Cdd:cd16031 83 -TYPKLLRKAGYQTAFIGK-WHLGSGGDLPPpgfDYWVSFPgqgsyYDPEFIENGKR------VGQKG--YVTDII---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 191 advpegtlpdkqsTEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENI----TLAPDPHvpDSLPPVAY 266
Cdd:cd16031 149 -------------TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIpepeTFDDDDY--AGRPEWAR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 267 NPWMDIREREDVQALNisvpygpiPEDFQRKIRQsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGe 346
Cdd:cd16031 213 EQRNRIRGVLDGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 347 WA-KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCp 425
Cdd:cd16031 283 LFdKRLMYEESIRVPLIIRDPRLIKA------------------------GTVVDALVLNIDFAPTILDLAGVPIPEDM- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 426 ipsfhvelcrEGQNLQKHLQLHDLEEEPDLFgnpreLIAYSQYPRPADFPQWnsdkpslndikvmgYSIRTVDYRYTVWV 505
Cdd:cd16031 338 ----------QGRSLLPLLEGEKPVDWRKEF-----YYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYY 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 84781812 506 GFDPSEflanfsdihagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16031 389 GVWDEE-----------ELYDLKKDPLELNNLANDPEYAEVLKELR 423
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
40-421 |
6.26e-59 |
|
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: 195.73 E-value: 6.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16022 2 NILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 STIPQYFKENGYVTMSVGKvfhpgissNHsddypyswsfppyhpssekyentktckgqdgklhanllcpvdvadvpegtl 198
Cdd:cd16022 82 PTLAELLKEAGYRTALIGK--------WH--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 199 pdkqstEEAIRLLEKMKTSAsPFFLAVGYHKPHIPFRypkefqklyplenitlapdphvpdslppvaynpwmdireredv 278
Cdd:cd16022 103 ------DEAIDFIERRDKDK-PFFLYVSFNAPHPPFA------------------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 279 qalnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE-WAKYSNFDVAT 357
Cdd:cd16022 133 -----------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGI 189
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84781812 358 RVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVP 421
Cdd:cd16022 190 RVPFIVRWPGKIP------------------------AGQVSDALVSLLDLLPTLLDLAGIEPP 229
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-536 |
1.00e-58 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 200.49 E-value: 1.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHSGNF 118
Cdd:cd16034 3 NILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG-ND--VPLPPDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 STIPQYFKENGYVTMSVGKvFHpgISSNHSDDYPYSWSFPP-----------------YHPSSEKYENTktckgqdgklh 181
Cdd:cd16034 80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDDD----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 182 anllcpvDVADVPEGTLPDKQsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDphvpds 260
Cdd:cd16034 146 -------GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 261 lppvaynpwmdireredvqalnisVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA 340
Cdd:cd16034 212 ------------------------VPEDKKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 341 LGEHGEWAKYSNFDVATRVPLMLYVPGRtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:cd16034 268 LGSHGLMNKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPI 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 421 PPrcpipsfhvelCREGQNLQKHLqlhdLEEEPDLFGNpreliAYSQYPRPadFPQWNSDKPSLNDIkvmgysIRTVDYR 500
Cdd:cd16034 324 PD-----------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVP--FGGGSARDGGEWRG------VRTDRYT 375
|
490 500 510
....*....|....*....|....*....|....*...
gi 84781812 501 YTVWVGfdpseflanfsdihaGELYFVD--SDPLQDHN 536
Cdd:cd16034 376 YVRDKN---------------GPWLLFDneKDPYQLNN 398
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-531 |
1.08e-58 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 197.77 E-value: 1.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhSGNF 118
Cdd:cd16037 2 NILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPY---DGDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 STIPQYFKENGYVTMSVGKVFHPGISSNHSDDYpyswsfppyhpssekyentktckgqdgklhanllcpvdvadvpegtl 198
Cdd:cd16037 79 PSWGHALRAAGYETVLIGKLHFRGEDQRHGFRY----------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 199 pDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredv 278
Cdd:cd16037 112 -DRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY---------------------------------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 279 qalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATR 358
Cdd:cd16037 157 ----------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVR 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 359 VPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPipsfhvelcreGQ 438
Cdd:cd16037 221 VPMIISGPGIP-------------------------AGKRVKTPVSLVDLAPTILEAAGAPPPPDLD-----------GR 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 439 NLQkhlqlhDLEEEPDlfgnPRELIAYSQYprpadfpqwnsdkpSLNDIKVMGYSIRTVDYRYTVWVGFDPseflanfsd 518
Cdd:cd16037 265 SLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP--------- 311
|
490
....*....|...
gi 84781812 519 ihagELYFVDSDP 531
Cdd:cd16037 312 ----QLFDLENDP 320
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-460 |
6.32e-58 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 197.40 E-value: 6.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQ----QAVCAPSRVSFLTGRrpdttrlydfnSYWRVH 114
Cdd:cd16155 4 NILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR-----------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 115 SGNFS-------TIPQYFKENGYVTMSVGKvfhpgissnhsddypysWsfppyhpssekyentktckgqdgklHanllcp 187
Cdd:cd16155 73 EGGKAaipsddkTWPETFKKAGYRTFATGK-----------------W-------------------------H------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 188 VDVADvpegtlpdkqsteEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPdsLPPVAyN 267
Cdd:cd16155 105 NGFAD-------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL-PENFLP--QHPFD-N 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 268 PWMDIRereDVQALnisvPYGPIPEDFQRKIRQsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW 347
Cdd:cd16155 168 GEGTVR---DEQLA----PFPRTPEAVRQHLAE-YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 348 AKYSNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIP 427
Cdd:cd16155 240 GKQNLYEHSMRVPLIISGPG-------------------------IPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGK 294
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84781812 428 SF-----------HVELCREGQNLQ-----------------KHLQLHDLEEEP----DLFGNPR 460
Cdd:cd16155 295 SLlpvirgekkavRDTLYGAYRDGQrairddrwkliiyvpgvKRTQLFDLKKDPdelnNLADEPE 359
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
40-422 |
1.68e-54 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 191.42 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHSGN 117
Cdd:PRK13759 8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 118 FS-TIPQYFKENGYVTMSVGKV-FHP-----GISSNHSDDyPYSWSFPPYHPSSEKY--ENTKTCKGQDGKLHANLL--- 185
Cdd:PRK13759 84 YKnTLPQEFRDAGYYTQCIGKMhVFPqrnllGFHNVLLHD-GYLHSGRNEDKSQFDFvsDYLAWLREKAPGKDPDLTdig 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 186 --CPVDVA---DVPEGTLPDKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPHVPDs 260
Cdd:PRK13759 163 wdCNSWVArpwDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 261 lppvaynpWmDIREREDVQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA 340
Cdd:PRK13759 238 --------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 341 LGEHGEWAKYSNFDVATRVPLMLYVPGRTAPLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:PRK13759 309 LGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGN---------------------RGTVIDQVVELRDIMPTLLDLAGGTI 367
|
..
gi 84781812 421 PP 422
Cdd:PRK13759 368 PD 369
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-551 |
9.73e-50 |
|
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: 177.04 E-value: 9.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16150 2 NIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 StipQYFKENGYVTMSVGKvfhpgissnhSDDYPYSWSFPPYhpssekyentktckgqdgklhanllCPVDVADVpegtl 198
Cdd:cd16150 82 L---KTLKDAGYHVAWAGK----------NDDLPGEFAAEAY-------------------------CDSDEACV----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 199 pdkqstEEAIRLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPdPHVPDSLPPVAYNPWMDIREREDV 278
Cdd:cd16150 119 ------RTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLRAKGKPSMLEGIEKQGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 279 QALNisvpygpipEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN-F-DVA 356
Cdd:cd16150 188 DRWS---------EERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 357 TRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPrcpiPSFHVELCRe 436
Cdd:cd16150 259 TRVPLIIKPPGGP-------------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THFGRSLLP- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 437 gqnlqkhlQLHDLEEEPD---------LFGNPReliAYSQYPRPADFPQWNS---DKPSLNDIKVMgysIRTVDYRYtVW 504
Cdd:cd16150 309 --------VLAGETEEHRdavfseggrLHGEEQ---AMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VY 373
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 84781812 505 VGFDPSeflanfsdihagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16150 374 RLYEPD------------ELYDLEADPLELHNLIGDPAYAEIIAEMK 408
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
39-425 |
1.06e-49 |
|
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: 174.30 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 39 LNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhSGN 117
Cdd:cd16032 1 PNILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEF---PAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 118 FSTIPQYFKENGYVTMSVGKVFHPGISSNHSDDYpyswsfppyhpssekyentktckgqdgklhanllcpvdvadvpegt 197
Cdd:cd16032 78 IPTFAHYLRAAGYRTALSGKMHFVGPDQLHGFDY---------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 198 lpDKQSTEEAIRLLEKMKTSAS--PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdirer 275
Cdd:cd16032 112 --DEEVAFKAVQKLYDLARGEDgrPFFLTVSFTHPHDPYVIPQEYWDLY------------------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 276 edvqalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDV 355
Cdd:cd16032 159 -------------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEG 219
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 356 ATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAGLPVPPRCP 425
Cdd:cd16032 220 SARVPLIISAPGRFAP-------------------------RRVAEPVSLVDLLPTLVDLAGGGTAPHVP 264
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-423 |
1.53e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 171.96 E-value: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 39 LNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPdttrlydfnSYWRVHSG- 116
Cdd:cd16148 1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP---------FYHGVWGGp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 ---NFSTIPQYFKENGYVTMsvgkvfhpGISSNhsddyPYSWSFPPYHPSSEKYENTktcKGQDGklhanllcpvdvADV 193
Cdd:cd16148 72 lepDDPTLAEILRKAGYYTA--------AVSSN-----PHLFGGPGFDRGFDTFEDF---RGQEG------------DPG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 194 PEGTLPDKQSTEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapDphvpdslppvaynpwmdir 273
Cdd:cd16148 124 EEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-----------------D------------------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 274 eredvqalnisvpygpipedfqrkirqsyfASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSN 352
Cdd:cd16148 167 ------------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSN 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84781812 353 F-DVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 423
Cdd:cd16148 217 LyDEQLHVPLIIRWPGKE-------------------------PGKRVDALVSHIDIAPTLLDLLGVEPPDY 263
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-420 |
2.72e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 171.79 E-value: 2.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRP-SLGCYGDKL----------VRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFN 108
Cdd:cd16153 3 NILWIITDDQRVdSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 109 SYWRVHSGNFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypyswsfppyhpssEKYENtktckgqdgklhanllcPV 188
Cdd:cd16153 83 AAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA-----------------FQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 189 DVADVPEgtlpdkQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdphvpdslppvaynp 268
Cdd:cd16153 119 RYLKNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 269 wmdiREREDvqalnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAH---NTIIAFTSDHGWALGEHG 345
Cdd:cd16153 165 ----RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQG 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84781812 346 EWAKYSNFDVATRVPLMLYVPGRtaplpaagqKLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:cd16153 217 ILAKFTFWPQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
40-422 |
6.01e-48 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 171.96 E-value: 6.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16144 2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 S---------------TIPQYFKENGYVTMSVGKvFHPGISSNHS-DDYPYSWSF-------PPYHPSSEKYENTKTCKG 175
Cdd:cd16144 82 KlipppsttrlpleevTIAEALKDAGYATAHFGK-WHLGGEGGYGpEDQGFDVNIggtgnggPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 176 QDGKlhanllcpvdvadvpegTLPDKqSTEEAIRLLEkmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdp 255
Cdd:cd16144 161 PEGE-----------------YLTDR-LTDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKY----------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 256 hvpdslppvaynpwmdireredvqalnisvpYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTS 335
Cdd:cd16144 210 -------------------------------EKKKKGLRKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTS 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 336 DHGwALGEHGEWA---------KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELV 406
Cdd:cd16144 259 DNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIKP------------------------GSVSDVPVIGT 313
|
410
....*....|....*.
gi 84781812 407 SLFPTLAGLAGLPVPP 422
Cdd:cd16144 314 DLYPTFLELAGGPLPP 329
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
40-509 |
4.02e-46 |
|
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: 167.82 E-value: 4.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFN--SYW----- 111
Cdd:cd16028 2 NVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR-------YLMNhrSVWngtpl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 112 RVHsgnFSTIPQYFKENGYVTMSVGK---VFHP-GISSNHsddyPYSWSfppYHPSSEKYEntktckgqdgklhanllcP 187
Cdd:cd16028 75 DAR---HLTLALELRKAGYDPALFGYtdtSPDPrGLAPLD----PRLLS---YELAMPGFD------------------P 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 188 VDVADvpegTLPDKQS-----TEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDPHVPD 259
Cdd:cd16028 127 VDRLD----EYPAEDSdtaflTDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 260 SLPPVaYNPWMDIREREDVQALNIsvPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGW 339
Cdd:cd16028 201 AQHPL-LAAFLERIESLSFSPGAA--NAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 340 ALGEHGEWAKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfDPASdwmdaGRHTEDLVELVSLFPTLAGLAGLP 419
Cdd:cd16028 278 QLGDHWLWGKDGFFDQAYRVPLIVRDPRREA----------------DATR-----GQVVDAFTESVDVMPTILDWLGGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 420 VPPRCpipsfhvelcrEGQNLQKHLQlhdlEEEPdlfGNPRELIAYSQYPRPADFPQW------NSDKPSLNdikvmgyS 493
Cdd:cd16028 337 IPHQC-----------DGRSLLPLLA----GAQP---SDWRDAVHYEYDFRDVSTRRPqealglSPDECSLA-------V 391
|
490
....*....|....*.
gi 84781812 494 IRTVDYRYTVWVGFDP 509
Cdd:cd16028 392 IRDERWKYVHFAALPP 407
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
40-540 |
1.24e-43 |
|
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: 160.02 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNaFAQQAVCAPSRVSFLTGRRPDTTRLydfnsyWRVHSG-- 116
Cdd:cd16146 2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGV------WHTILGre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 ----NFSTIPQYFKENGYVTMSVGKvFHPGissnhsDDYPY----------------SWSFPPYHPSSEKYENTKTCKGQ 176
Cdd:cd16146 75 rmrlDETTLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 177 DGKLhanllcpvdvadvpEGTLPDKQsTEEAIRLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdph 256
Cdd:cd16146 148 FVKT--------------EGYCTDVF-FDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPYK----------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 257 vpdslppvaynpwmDIREREDVQAlnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSD 336
Cdd:cd16146 200 --------------DMGLDDKLAA---------------------FYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSD 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 337 HGWALGEHGEW------AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFP 410
Cdd:cd16146 245 NGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKILA------------------------GKDVDTLTAHIDLLP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 411 TLAGLAGLPVPPRCPIpsfhvelcrEGQNLQKHLQlHDLEEEPDlfgnpRELIAYSQYPRPADFPQWNSdkpslndikvm 490
Cdd:cd16146 301 TLLDLCGVKLPEGIKL---------DGRSLLPLLK-GESDPWPE-----RTLFTHSGRWPPPPKKKRNA----------- 354
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 84781812 491 gySIRTVDYRYtVWVGFDPSeflanfsdihagELYFVDSDPLQDHNVYND 540
Cdd:cd16146 355 --AVRTGRWRL-VSPKGFQP------------ELYDIENDPGEENDVADE 389
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-421 |
3.12e-43 |
|
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: 158.88 E-value: 3.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16026 3 NIVVILADDLGYGdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 -NFSTIPQYFKENGYVTMSVGKvFHPGISS-----NHSDDY----PYS---WSFPPYHPSSEkyentktckGQDGKLHAN 183
Cdd:cd16026 83 pDEITIAEVLKKAGYRTALVGK-WHLGHQPeflptRHGFDEyfgiPYSndmWPFPLYRNDPP---------GPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 184 LLCPVDVADVPEGTlpdKQSTEEAIRLLEKMKTsaSPFFLAVGYHKPHIPfrypkefqkLYPlenitlapdphvpdslpp 263
Cdd:cd16026 153 EEVIEQPADQSSLT---QRYTDEAVDFIERNKD--QPFFLYLAHTMPHVP---------LFA------------------ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 264 vaynpwmdireredvqalnisvpygpiPEDFQ-RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALG 342
Cdd:cd16026 201 ---------------------------SEKFKgRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 343 EHGEW--------AKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAG 414
Cdd:cd16026 254 YGGHGgsagplrgGKGTTWEGGVRVPFIAWWPGVIP------------------------AGTVSDELASTMDLLPTLAA 309
|
....*..
gi 84781812 415 LAGLPVP 421
Cdd:cd16026 310 LAGAPLP 316
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-429 |
1.25e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 147.77 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRV----- 113
Cdd:cd16149 2 NILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHgktkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 114 ---HSGNFSTIPQYFKENGYVTMSVGKvFHPGissnhsddypyswsfppyhpssekyentktckgqdgklhanllcpvdv 190
Cdd:cd16149 82 pegYLEGQTTLPEVLQDAGYRCGLSGK-WHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 191 advpegtlpdkqstEEAIRLLEKMKTSASPFFLAVGYHKPHipfrypkefqklyplenitlapdphvpdslppvayNPWm 270
Cdd:cd16149 113 --------------DDAADFLRRRAEAEKPFFLSVNYTAPH-----------------------------------SPW- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 271 direredvqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK- 349
Cdd:cd16149 143 ------------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKg 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 350 -----YSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVP--P 422
Cdd:cd16149 193 ngtfpLNMYDNSVKVPFIIRWPGVVPA------------------------GRVVDSLVSAYDFFPTLLELAGVDPPadP 248
|
....*..
gi 84781812 423 RCPIPSF 429
Cdd:cd16149 249 RLPGRSF 255
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
40-423 |
1.62e-40 |
|
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: 151.59 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY---WRVHS 115
Cdd:cd16145 2 NIIFILADDLGYGdLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPggqDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 116 GNfSTIPQYFKENGYVTMSVGK-----VFHPGISSNHSDDYPYSWS--------FPPYhpsseKYENTKTcKGQDGKLHA 182
Cdd:cd16145 82 DD-VTLAEVLKKAGYATAAFGKwglggPGTPGHPTKQGFDYFYGYLdqvhahnyYPEY-----LWRNGEK-VPLPNNVIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 183 NLLCPVDVADVPEGTLPDKqSTEEAIRLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDPHVPDSLP 262
Cdd:cd16145 155 PLDEGNNAGGGGGTYSHDL-FTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYKYKPKDPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 263 PVAYNPWmdireredvqalnisvpygpipedfqRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALG 342
Cdd:cd16145 220 IYAYLPW--------------------------PQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG-PHS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 343 EHGEWAKYSNFDVA--------------TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSL 408
Cdd:cd16145 273 EGGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPGKIPA------------------------GSVSDHPSAFWDF 328
|
410
....*....|....*
gi 84781812 409 FPTLAGLAGLPVPPR 423
Cdd:cd16145 329 MPTLADLAGAEPPED 343
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
40-418 |
6.64e-37 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 138.71 E-value: 6.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNsywRVHSGN- 117
Cdd:pfam00884 2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVST---PVGLPRt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 118 FSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDYPYSWSFPPYHPSSEKYENTKTCKGQDgklhanllcpvdvadvPEGT 197
Cdd:pfam00884 79 EPSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------SGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 198 LPDKQSTEEAIRLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpdslppvaynpwmdirered 277
Cdd:pfam00884 142 VSDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA-------------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 278 vqalnISVPYGpipeDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA- 356
Cdd:pfam00884 187 -----TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNAp 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84781812 357 ---TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 418
Cdd:pfam00884 258 eggYRVPLLIWSPGGKAK------------------------GQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-536 |
7.32e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 140.43 E-value: 7.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAqQAVCAPSRVSFLTGRRPDTTrlYDFNSYWrvHSGNf 118
Cdd:cd16151 2 NIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRN--YVVFGYL--DPKQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 STIPQYFKENGYVTMSVGKvfhPGISSNHSD-DYPY-----SWSFPPYHPSSEKYENTKTCKG--QDGKLhanllcpvdV 190
Cdd:cd16151 76 KTFGHLLKDAGYATAIAGK---WQLGGGRGDgDYPHefgfdEYCLWQLTETGEKYSRPATPTFniRNGKL---------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 191 ADVPEGTLPDkQSTEEAIRLLEKMKtsASPFFLavgYhkphipfrYPkefqklyplenITLAPDPHV--PDSLppvaynP 268
Cdd:cd16151 144 ETTEGDYGPD-LFADFLIDFIERNK--DQPFFA---Y--------YP-----------MVLVHDPFVptPDSP------D 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 269 WMDIRERedvqalnisvpygpipedfqRKIRQSYF-ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW 347
Cdd:cd16151 193 WDPDDKR--------------------KKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 348 -------AKYSNFDVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:cd16151 253 ngrevrgGKGKTTDAGTHVPLIVNWPGLI------------------------PAGGVSDDLVDFSDFLPTLAELAGAPL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 421 PPRCPIpsfhvelcrEGQNLQkhlqlhdleeePDLFGNP----RELIAYsqYPRpadfPQWNSDKPslndikvmgYSIRT 496
Cdd:cd16151 309 PEDYPL---------DGRSFA-----------PQLLGKTgsprREWIYW--YYR----NPHKKFGS---------RFVRT 353
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 84781812 497 VDYRYtvwvgfdpseflanFSDihaGELYFVDSDPLQDHN 536
Cdd:cd16151 354 KRYKL--------------YAD---GRFFDLREDPLEKNP 376
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
40-426 |
1.84e-35 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 136.91 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQaVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16029 2 HIVFILADDLGWNdVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILAGEPYGlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 -NFSTIPQYFKENGYVTMSVGKvFHPGIssnhsddypYSWSFPP----------YHPSSEKYENTKTCKGQDgklhanll 185
Cdd:cd16029 81 lNETLLPQYLKELGYATHLVGK-WHLGF---------YTWEYTPtnrgfdsfygYYGGAEDYYTHTSGGAND-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 186 CPVDVADVPEGTLPDKQS-------TEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlAPDPHVP 258
Cdd:cd16029 143 YGNDDLRDNEEPAWDYNGtystdlfTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE------DKFAHIK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 259 DslppvaynpwmdireredvqalnisvpygpipedfqrKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG 338
Cdd:cd16029 216 D-------------------------------------EDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 339 wALGEHGEWA--------KYSNFDVATRVPLMLYVPGRTaplPAAGQKlfpYRDPFDpASDWmdagrhtedlvelvslFP 410
Cdd:cd16029 259 -GPTGGGDGGsnyplrggKNTLWEGGVRVPAFVWSPLLP---PKRGTV---SDGLMH-VTDW----------------LP 314
|
410
....*....|....*.
gi 84781812 411 TLAGLAGLPVPPRCPI 426
Cdd:cd16029 315 TLLSLAGGDPDDLPPL 330
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
40-422 |
8.70e-35 |
|
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: 135.37 E-value: 8.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPSLGCYGD--KLVRspnidQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPD----TTRLYDFNSYWRV 113
Cdd:cd16147 3 NIVLILTDDQDVELGSMDPmpKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHnhgvTNNSPPGGGYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 114 HSGNF--STIPQYFKENGYVTMSVGKVFHpGISSNHSDDYP---YSWSFPPYHPSseKYENTKTCKGQDGKLHANLlcpv 188
Cdd:cd16147 78 WQNGLerSTLPVWLQEAGYRTAYAGKYLN-GYGVPGGVSYVppgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVSY---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 189 dvadvPEGTLPDKqSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAPDPHVPDslPPVAYNP 268
Cdd:cd16147 151 -----PGDYLTDV-IANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPRPPPNN--PDVSDKP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 269 -WmdIREREDVQALNISVpygpIPEDFQRKIR--QSyfasvsyLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHG 345
Cdd:cd16147 221 hW--LRRLPPLNPTQIAY----IDELYRKRLRtlQS-------VDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHR 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84781812 346 -EWAKYSNFDVATRVPLMLYVPGrtapLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 422
Cdd:cd16147 288 lPPGKRTPYEEDIRVPLLVRGPG----IP---------------------AGVTVDQLVSNIDLAPTILDLAGAPPPS 340
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-551 |
9.62e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 131.97 E-value: 9.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHSGNF 118
Cdd:cd16152 3 NVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFR-NG--IPLPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 STIPQYFKENGYVTMSVGKvfhpgissnhsddypysWSFPPYHpssekyentktckgqdgklhanllcpVDVAdvpegtl 198
Cdd:cd16152 80 KTLAHYFRDAGYETGYVGK-----------------WHLAGYR--------------------------VDAL------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 199 pdkqsTEEAIRLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYplenitlaPDPHVPdslppvaynpwmdir 273
Cdd:cd16152 110 -----TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERF--------ANFWVP--------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 274 erEDVQALnisvpygpiPEDFQRKIrQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHgwalGEH-----GEWa 348
Cdd:cd16152 161 --PDLAAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 349 KYSNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPprcpiPS 428
Cdd:cd16152 224 KRSCHESSIRVPLVIYGPG-------------------------FNGGGRVEELVSLIDLPPTLLDAAGIDVP-----EE 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 429 FHvelcreGQNLQKhlqlhDLEEEPDlfgnPRELIAYSQyprpadfpqwnsdkpsLNDIKVmGYSIRTVDYRYTVwVGFD 508
Cdd:cd16152 274 MQ------GRSLLP-----LVDGKVE----DWRNEVFIQ----------------ISESQV-GRAIRTDRWKYSV-AAPD 320
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 84781812 509 PSEFLANFSDIHAGE-LYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16152 321 KDGWKDSGSDVYVEDyLYDLEADPYELVNLIGRPEYREVAAELR 364
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
40-421 |
2.11e-33 |
|
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: 131.17 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRP-SLGCYGDK-LVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNsyWRVHSG- 116
Cdd:cd16143 2 NIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV--LGGFSPp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 ----NFSTIPQYFKENGYVTMSVGKvFHPGIssnhsdDYPYSWSFPPYHPSSEKYENTKTCKgqDGklhanllcPVDV-- 190
Cdd:cd16143 80 liepDRVTLAKMLKQAGYRTAMVGK-WHLGL------DWKKKDGKKAATGTGKDVDYSKPIK--GG--------PLDHgf 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 191 --------ADVpegtlpDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapdphvpdslp 262
Cdd:cd16143 143 dyyfgipaSEV------LPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQG-------------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 263 pvaynpwmdireredVQALNisvPYGpipeDFqrkIRQsyfasvsyLDTQVGHVLSALDDLRLAHNTIIAFTSDHG---- 338
Cdd:cd16143 197 ---------------KSGAG---PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspy 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 339 ---WALGEHGEWA-------KYSNFDVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSL 408
Cdd:cd16143 244 adyKELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKI------------------------PAGSVSDQLVSLTDL 299
|
410
....*....|...
gi 84781812 409 FPTLAGLAGLPVP 421
Cdd:cd16143 300 FATLAAIVGQKLP 312
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
40-422 |
2.60e-33 |
|
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: 132.51 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTtrlydfNSYWR---VHS 115
Cdd:cd16156 2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT------NGSWTncmALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 116 GNFSTIPQYFKENGYVTMSVGKVfhpgissnHSD--DY------PYSWSfPPYHPSSEKYENTKTckGQDGKLHANLLCP 187
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKW--------HLDggDYfgngicPQGWD-PDYWYDMRNYLDELT--EEERRKSRRGLTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 188 VDVADVPEGTLPDKQSTEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplENITLAPDPHVPDSLP--PVA 265
Cdd:cd16156 145 LEAEGIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 266 YNPWMDIREREDVQALNISVPYgpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLrlAHNTIIAFTSDHGWALGEHG 345
Cdd:cd16156 221 QRLWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHK 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84781812 346 EWAK-YSNFDVATRVPLMLYVPGRtapLPAAGQKLFPyrdpfdpasdwmdagrhtedlVELVSLFPTLAGLAGLPVPP 422
Cdd:cd16156 285 LWAKgPAVYDEITNIPLIIRGKGG---EKAGTVTDTP---------------------VSHIDLAPTILDYAGIPQPK 338
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
40-422 |
3.93e-30 |
|
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: 121.49 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVR---SPNIDQLASHSVLFQNAFAQQAvCAPSRVSFLTGRRPdttrlydfnsywrVHS 115
Cdd:cd16142 2 NILVILGDDIGWGdLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP-------------IRT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 116 GNFS---------------TIPQYFKENGYVTMSVGKvfhpgissNHSDDYPYSWsfppyhpssekyentktckgqdgkl 180
Cdd:cd16142 68 GLTTvglpgspgglppwepTLAELLKDAGYATAQFGK--------WHLGDEDGRL------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 181 hanllcPVDVA-DVPEGTLP---DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdph 256
Cdd:cd16142 115 ------PTDHGfDEFYGNLYhtiDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS----------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 257 vpdslppvAYNPWMDireredvqalnisvpygpipedfqrkirqsyfaSVSYLDTQVGHVLSALDDLRLAHNTIIAFTSD 336
Cdd:cd16142 178 --------GKGKYAD---------------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTD 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 337 HG-----WALGEHGEW--AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLF 409
Cdd:cd16142 217 NGpeqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGKIKP------------------------GRVSNEIVSHLDWF 272
|
410
....*....|...
gi 84781812 410 PTLAGLAGLPVPP 422
Cdd:cd16142 273 PTLAALAGAPDPK 285
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
40-421 |
1.32e-28 |
|
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: 117.54 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDkLVRSPNIDQLASHSVLFQNaFAQQAVCAPSRVSFLTGRRP-------DTTRLYDFNSYW 111
Cdd:cd16025 4 NILLILADDLGFSdLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHhqvgmgtMAELATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 112 RVHSGNFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypysW--SFPPYHpSSEKYentktckgqdgklhanllcpvd 189
Cdd:cd16025 82 GYLPDSAATIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL---------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 190 vadvpegtlpdkqsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LY 244
Cdd:cd16025 122 --------------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 245 PlENITLAPDPH-VP--DSLPPvaynpwmdirEREDVQALNISVpygpipedfqrkirqsYFASVSYLDTQVGHVLSALD 321
Cdd:cd16025 188 P-ADTKLTPRPPgVPawDSLSP----------EEKKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLK 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 322 DLRLAHNTIIAFTSDHGwALGEHGeWAKYSNfdvaTrvPLMLYvpgrtaplpaagqKLFPY----RDPF--DPASDWMDA 395
Cdd:cd16025 241 ELGELDNTLIIFLSDNG-ASAEPG-WANASN----T--PFRLY-------------KQASHeggiRTPLivSWPKGIKAK 299
|
410 420
....*....|....*....|....*.
gi 84781812 396 GRHTEDLVELVSLFPTLAGLAGLPVP 421
Cdd:cd16025 300 GGIRHQFAHVIDIAPTILELAGVEYP 325
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-423 |
2.51e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 112.30 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYD-FNSYWRVH-SG 116
Cdd:cd16035 2 NILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLlSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 NFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypysWsfppyHPSSekyentktckgqdgklHANllcpvdvadvpEG 196
Cdd:cd16035 82 DVPTLGHMLRAAGYYTAYKGK-----------------W-----HLSG----------------AAG-----------GG 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 197 TLPDKQSTEEAIRLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdphvpdslppvaynpwmdir 273
Cdd:cd16035 113 YKRDPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH------------------------------------------ 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 274 ereDVQalnisvpYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN- 352
Cdd:cd16035 151 ---DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNa 220
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84781812 353 FDVATRVPLMLYVPGrtaplpaagqkLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 423
Cdd:cd16035 221 YEEALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGVDAEAR 267
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
40-422 |
1.43e-24 |
|
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: 105.32 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPSLGCY-GDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRlyDFNSYWRVHSgNF 118
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE--SWNNYKGLDP-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 STIPQYFKENGYVTMSVGKVFHpgISSNHS-DDYPYSWSfppyhpssekyENTKTCKGQDGKLHANLLCPVDVADVpegT 197
Cdd:cd16171 79 PTWMDRLEKHGYHTQKYGKLDY--TSGHHSvSNRVEAWT-----------RDVPFLLRQEGRPTVNLVGDRSTVRV---M 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 198 LPDKQSTEEAIRLLEKMKTSAS-PFFLAVGYHKPHiPFRYPkefqklypleniTLAPDphvpdslppvaynpwmdirere 276
Cdd:cd16171 143 LKDWQNTDKAVHWIRKEAPNLTqPFALYLGLNLPH-PYPSP------------SMGEN---------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 277 dvqalnisvpYGPIpedfqRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA 356
Cdd:cd16171 188 ----------FGSI-----RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGS 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84781812 357 TRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPP 422
Cdd:cd16171 253 SHVPLLIMGPG-------------------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
40-421 |
2.46e-24 |
|
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: 106.60 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY----WRVH 114
Cdd:cd16159 3 NIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMrvilFTAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 115 SG----NFSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDYpyswsfpPYHPSSEKYE--------NTKTCkgQDGKLHA 182
Cdd:cd16159 83 SGglppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDF-------CHHPLNHGFDyfyglpltNLKDC--GDGSNGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 183 NLLCPVDVADVPEGTLPDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPL--ENITLAPDPHVPDS 260
Cdd:cd16159 153 YDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCIlmRNHEVVEQPMSLEN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 261 LPP---VAYNPWMDIRERED----VQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAF 333
Cdd:cd16159 233 LTQrltKEAISFLERNKERPfllvMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 334 TSDHGWAL------GEHGEW-------AKYSNFDVATRVPLMLYVPGRTAPlpaaGQKLfpyrdpfDPASDWMDagrhte 400
Cdd:cd16159 313 TSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGVIPP----GSVI-------DEPTSLMD------ 375
|
410 420
....*....|....*....|.
gi 84781812 401 dlvelvsLFPTLAGLAGLPVP 421
Cdd:cd16159 376 -------IFPTVAALAGAPLP 389
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
40-421 |
4.33e-20 |
|
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 93.28 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16158 3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 -NFSTIPQYFKENGYVTMSVGKvFHPGISSNHS--------DDY---PYSWSFPPYHPSSEKYENTKTCKGQDGKLhanL 184
Cdd:cd16158 83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNGTylpthqgfDHYlgiPYSHDQGPCQNLTCFPPNIPCFGGCDQGE---V 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 185 LCPVDVADVPEGTLPD-----KQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdphvpd 259
Cdd:cd16158 159 PCPLFYNESIVQQPVDlltleERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFA------------------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 260 slppvaynpwmdireredvqalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGW 339
Cdd:cd16158 221 -----------------------------------GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 340 AL------GEHG--EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRhTEDLVELVSLFPT 411
Cdd:cd16158 266 STmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPGRIKP------------------------GV-THELASTLDILPT 320
|
410
....*....|
gi 84781812 412 LAGLAGLPVP 421
Cdd:cd16158 321 IAKLAGAPLP 330
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-421 |
1.10e-18 |
|
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: 88.68 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSywrvHSGNF 118
Cdd:cd16157 3 NIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA----HARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 119 ST--------------IPQYFKENGYVTMSVGKvFHPGissnHSddypyswsfPPYHP---SSEKYENTKTC--KGQDGK 179
Cdd:cd16157 79 YTpqnivggipdseilLPELLKKAGYRNKIVGK-WHLG----HR---------PQYHPlkhGFDEWFGAPNChfGPYDNK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 180 LHANLlcPVDVADVPEGTLPDKQS--------------TEEAIRLLEKMKTSASPFFLAVGYHKPHIPfrypkefqkLYp 245
Cdd:cd16157 145 AYPNI--PVYRDWEMIGRYYEEFKidkktgesnltqiyLQEALEFIEKQHDAQKPFFLYWAPDATHAP---------VY- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 246 lenitlapdphvpdslppvAYNPWMDIREREdvqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRL 325
Cdd:cd16157 213 -------------------ASKPFLGTSQRG------------------------LYGDAVMELDSSVGKILESLKSLGI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 326 AHNTIIAFTSDHGWAL-------GEHGEW--AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaG 396
Cdd:cd16157 250 ENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGHIKP------------------------G 305
|
410 420
....*....|....*....|....*
gi 84781812 397 RHTEDLVELVSLFPTLAGLAGLPVP 421
Cdd:cd16157 306 QVSHQLGSLMDLFTTSLALAGLPIP 330
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
40-422 |
2.24e-18 |
|
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: 87.14 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLR-PSLGCYGDKLVR-SPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVHSG- 116
Cdd:cd16161 3 NFLLLFADDLGwGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH-NFLPTSVGGl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 --NFSTIPQYFKENGYVTMSVGKvFHPGISSNhsddypyswsfppYHPSSekyentktcKGQDGKLHANLLCPVDVADvp 194
Cdd:cd16161 82 plNETTLAEVLRQAGYATGMIGK-WHLGQREA-------------YLPNS---------RGFDYYFGIPFSHDSSLAD-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 195 egtlpdkQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPkefqklyplenitlaPDPHVPDSlppvaynpwmdire 274
Cdd:cd16161 137 -------RYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANL---------------PRFQSPTS-------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 275 redvqalnISVPYGpipedfqrkirqsyfASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG-WALG-------EHGE 346
Cdd:cd16161 181 --------GRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpGTGD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 347 W--------AKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGL 418
Cdd:cd16161 238 WqgnlggsvAKASTWEGGHREPAIVYWPGRIP------------------------ANSTSAALVSTLDIFPTVVALAGA 293
|
....
gi 84781812 419 PVPP 422
Cdd:cd16161 294 SLPP 297
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
40-417 |
2.67e-18 |
|
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: 87.49 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRpslgcYGDKLV-------RSPnIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY--DFNSY 110
Cdd:cd16160 3 NIVLFFADDMG-----YGDLASyghptqeRGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 111 WRVHSG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDypySWSFPPYH---------PssekYENTKTCkgQDG 178
Cdd:cd16160 77 PWDIGGlpkTEVTMAEALKEAGYTTGMVGK-WHLGINENNHSD---GAHLPSHHgfdfvgtnlP----FTNSWAC--DDT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 179 KLHanllcpVDVADVPEGTLPDK-QSTEEAIR---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyp 245
Cdd:cd16160 147 GRH------VDFPDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 246 lenitlapdphvpdslppvaynpwmdireredvqalNISVpygpipedfqrkiRQSYFASVSYLDTQVGHVLSALDDLRL 325
Cdd:cd16160 217 ------------------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 326 AHNTIIAFTSDHGWAL---GEHGEWA-----KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagR 397
Cdd:cd16160 248 DQNTLVFFLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTIKP-------------------------R 302
|
410 420
....*....|....*....|
gi 84781812 398 HTEDLVELVSLFPTLAGLAG 417
Cdd:cd16160 303 VSHEVVSTMDIFPTFVDLAG 322
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-422 |
2.99e-17 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 85.09 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 28 SAAQGNSATDALNILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGrrpdttrLYD 106
Cdd:COG1368 224 PTPNPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-------LPP 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 107 FNS---YWRVHSGNFSTIPQYFKENGYVTMsvgkVFHPGissnhsddYPYSWSFPPYHPSsEKYENTKtckGQDgklhan 183
Cdd:COG1368 297 LPGgspYKRPGQNNFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYKN-LGFDEFY---DRE------ 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 184 llcpvDVADVPEGT--LPDKQSTEEAIRLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITLapdphv 257
Cdd:COG1368 355 -----DFDDPFDGGwgVSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL------ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 258 pdslppvaynpwmdireredvqalnisvpygpipedfqrkirQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDH 337
Cdd:COG1368 417 ------------------------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDH 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 338 GwalGEHGEWAKYSNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAG 417
Cdd:COG1368 455 G---PRSPGKTDYENPLERYRVPLLIYSPG-------------------------LKKPKVIDTVGSQIDIAPTLLDLLG 506
|
....*
gi 84781812 418 LPVPP 422
Cdd:COG1368 507 IDYPS 511
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
40-417 |
1.70e-15 |
|
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: 76.95 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVC--APSRVSFLTGRRPDTTRLYDFNSYwrvHSG 116
Cdd:cd16015 2 NVIVILLESFsDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPPLPLGSGSYTLY---KLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 NFSTIPQYFKENGYVTMSvgkvFHPGissnhsddYPYSWSFPPYHP--------SSEKYENTKTCKGQDGklhanllcpv 188
Cdd:cd16015 79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPnlgfdefyDLEDFPDDEKETNGWG---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 189 dvadvpegtLPDKQSTEEAIRLLEKMKtsASPFFLAVgyhkphipfrypkefqklyplenITLapDPHVPDSLPPVAYNP 268
Cdd:cd16015 137 ---------VSDESLFDQALEELEELK--KKPFFIFL-----------------------VTM--SNHGPYDLPEEKKDE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 269 wmdireredvqalnisvpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWA 348
Cdd:cd16015 181 --------------------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDET 240
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84781812 349 KYSNFDvATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAG 417
Cdd:cd16015 241 DEDPLD-LYRTPLLIYSPGLKKP-------------------------KKIDRVGSQIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-421 |
2.48e-14 |
|
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: 74.69 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDL-RPSLGCY--GDKLVRSPNIDQLASHSVLFQNAFAqQAVCAPSRVSFLTGRrpdttrlYDFN----SYWR 112
Cdd:cd16154 2 NILLIIADDQgLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGK-------YGFRtgvlAVPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 113 VHSGNFSTIPQYFKEN----GYVTMSVGKvFHPGISSNHSDDYPYSWSFPPYHPS--SEKYENTKTCKGQdgklhanllc 186
Cdd:cd16154 74 ELLLSEETLLQLLIKDattaGYSSAVIGK-WHLGGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQ---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 187 pvdvaDVPEGTLPDKQSTEEAIRLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDphvpdsLPPV 264
Cdd:cd16154 143 -----TTNSTEYATTKLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGD------SADI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 265 AYNPwmdireredvqalnisvpygpipedfqrkiRQSYFASVSYLDTQVGHVLSALDDLRLAhNTIIAFTSDHG------ 338
Cdd:cd16154 202 EANP------------------------------RPYYLAAIEAMDTEIGRLLASIDEEERE-NTIIIFIGDNGtpgqvv 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 339 --WALGEHgewAKYSNFDVATRVPLMlyvpgrtaplpAAGQKLfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLA 416
Cdd:cd16154 251 dlPYTRNH---AKGSLYEGGINVPLI-----------VSGAGV-------------ERANERESALVNATDLYATIAELA 303
|
....*
gi 84781812 417 GLPVP 421
Cdd:cd16154 304 GVDAA 308
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
40-416 |
9.48e-13 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 67.83 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQnAFAQQAVC--APSRVSFLTGRRPDttrlydfnsywrvhsg 116
Cdd:cd00016 2 HVVLIVLDGLGADdLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTssAPNHAALLTGAYPT---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 117 nfstipqyfkENGYVTMSVGKVFHPGISSNHSDDYPyswSFPpyhpssekyentktckgqdgklhanllcpvdvadvpeG 196
Cdd:cd00016 65 ----------LHGYTGNGSADPELPSRAAGKDEDGP---TIP-------------------------------------E 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 197 TLPDKQSTEEAIRLLE--KMKTSASPFFLAVGYHKPHIPFrypkefqklyplenitlapdpHVPDSLPPvaynpwmdire 274
Cdd:cd00016 95 LLKQAGYRTGVIGLLKaiDETSKEKPFVLFLHFDGPDGPG---------------------HAYGPNTP----------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 275 redvqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYS--- 351
Cdd:cd00016 143 --------------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgka 196
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84781812 352 -NFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLA 416
Cdd:cd00016 197 dKSHTGMRVPFIAYGPG-------------------------VKKGGVKHELISQYDIAPTLADLL 237
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
200-370 |
3.27e-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: 69.16 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 200 DKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIpFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredvQ 279
Cdd:COG3083 363 DRQITAQWLQWLDQ-RDSDRPWFSYLFLDAPHA-YSFPADYPKPF----------------------------------Q 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 280 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE--WAKYSNF-DVA 356
Cdd:COG3083 407 PSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFsRYQ 486
|
170
....*....|....
gi 84781812 357 TRVPLMLYVPGRTA 370
Cdd:COG3083 487 LQVPLVIHWPGTPP 500
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
40-418 |
2.03e-04 |
|
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: 43.38 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAqqavCAPS-RVS---FLTGR-RPDTTRLYDFNSywrv 113
Cdd:cd16017 4 NVVLVIGESARRDhMSLYGYPRDTTPFLSKLKKNLIVFDNVIS----CGTStAVSlpcMLSFAnRENYDRAYYQEN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 114 hsgnfstIPQYFKENGYvtmsvgKVFHpgISsNHSDDYPYSWSFPPYHPSSEKYENTKTCKGQ---DGKLhanllcpvdv 190
Cdd:cd16017 76 -------LIDLAKKAGY------KTYW--IS-NQGGCGGYDTRISAIAKIETVFTNKGSCNSSncyDEAL---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 191 advpegtLPDkqsteeairLLEKMKTSASPFFLAV---GyhkPHIPF--RYPKEFQKLYPlenitlapdphvpdslppva 265
Cdd:cd16017 130 -------LPL---------LDEALADSSKKKLIVLhlmG---SHGPYydRYPEEFAKFTP-------------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 266 ynpwmdireredvqalnisVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDdlRLAHNTIIAFTSDHGWALGEHG 345
Cdd:cd16017 171 -------------------DCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENG 229
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84781812 346 EW--AKYSNFDVATRVPLMLYVPGRTAPLPAAGQKLFPYRDPFDpaSDWmdagrhtedlvelvsLFPTLAGLAGL 418
Cdd:cd16017 230 LYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPFS--HDN---------------LFHTLLGLLGI 287
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
304-367 |
2.36e-04 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 42.96 E-value: 2.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84781812 304 ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA-LGEHGewakYSNFDVATRVPLMLYVPG 367
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
19-112 |
3.96e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 39.73 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84781812 19 LGSFCIALESAAQGNSATDALNILLIIVDDLRPslgcygDKLVR--SPNIDQLASHSVLFQNAfaqQAVC----APSRVS 92
Cdd:COG1524 4 GLSLLLASLLAAAAAAAPPAKKVVLILVDGLRA------DLLERahAPNLAALAARGVYARPL---TSVFpsttAPAHTT 74
|
90 100
....*....|....*....|
gi 84781812 93 FLTGRRPDTTRLYDFNSYWR 112
Cdd:COG1524 75 LLTGLYPGEHGIVGNGWYDP 94
|
|
| |
