|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
40-540 |
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: 590.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFS 119
Cdd:cd16030 4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 120 TIPQYFKENGYVTMSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTK---GQDGKLHANLLCPVDVADVPEGTLP 196
Cdd:cd16030 84 TLPQYFKENGYTTAGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKlcpGKKGGKGGGGGPAWEAADVPDEAYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 197 DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQ 276
Cdd:cd16030 162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 277 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRV 356
Cdd:cd16030 241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 357 PLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvelCREGQN 436
Cdd:cd16030 321 PLIIRAPGVTKP------------------------GKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 437 LQKHLQlhdleeEPDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikVMGYSIRTVDYRYTVWVgfdpseflaNFSDI 516
Cdd:cd16030 366 LVPLLK------NPSAKWKDA---AFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKV 411
|
490 500
....*....|....*....|....
gi 2202693044 517 HAGELYFVDSDPLQDHNVYNDSQH 540
Cdd:cd16030 412 GAEELYDHKNDPNEWKNLANDPEY 435
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
22-537 |
8.90e-93 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 289.09 E-value: 8.90e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 22 FCIALESAAQGNSATDALNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPD 100
Cdd:COG3119 7 LLLALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 101 TTRLYDFNSYWRVH-SGNFSTIPQYFKENGYVTMSVGKVFHpgissnHSDDYpyswsfppyhpssekyentkgqdgklha 179
Cdd:COG3119 87 RTGVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTDL---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 180 nllcpvdvadvpegtlpdkqSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdphvpdslp 259
Cdd:COG3119 133 --------------------LTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL----------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 260 PVAYNPWmdireredvqalnisvpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALG 339
Cdd:COG3119 182 PPNLAPR-------------------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 340 EHG-EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVP 418
Cdd:COG3119 243 EHGlRGGKGTLYEGGIRVPLIVRWPGKIKA------------------------GSVSDALVSLIDLLPTLLDLAGVPIP 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 419 PRCpipsfhvelcrEGQNLQKHLQlhdlEEEPDlfgnPRELIaYSQYPRPAdfpqwnsdkpslndikvMGYSIRTVDYRY 498
Cdd:COG3119 299 EDL-----------DGRSLLPLLT----GEKAE----WRDYL-YWEYPRGG-----------------GNRAIRTGRWKL 341
|
490 500 510
....*....|....*....|....*....|....*....
gi 2202693044 499 TVWVGFDPSEflanfsdihagELYFVDSDPLQDHNVYND 537
Cdd:COG3119 342 IRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
40-548 |
1.25e-65 |
|
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: 217.76 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFS 119
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 120 TIPQYFKENGYVTMSVGKVFHPGissnhsdDYPYSWSFPPYHPSSEKYENTKGQDgklhanllcpvDVADVPEGTLPDKq 199
Cdd:cd16027 82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYAS-----------NAADFLNRAKKGQ- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 200 steeairllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapDPHVPDsLPPVaynpwmdireREDVQAln 279
Cdd:cd16027 143 -----------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKV--PPYLPD-TPEV----------REDLAD-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 280 isvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGehgeWAKYSNFDVATRVPLM 359
Cdd:cd16027 191 -------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGLRVPLI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 360 LYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvELcrEGQNLqk 439
Cdd:cd16027 248 VRWPGKIKP------------------------GSVSDALVSFIDLAPTLLDLAGIEPPE---------YL--QGRSF-- 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 440 hlqLHDLEEEPDlfgNPRELIaYSQYPRpadfpqwnsdkpslNDIKVMGY-SIRTVDYRYTVwvgfdpseflaNFSDIha 518
Cdd:cd16027 291 ---LPLLKGEKD---PGRDYV-FAERDR--------------HDETYDPIrSVRTGRYKYIR-----------NYMPE-- 336
|
490 500 510
....*....|....*....|....*....|
gi 2202693044 519 gELYFVDSDPLQDHNVYNDSQHGGLLHSLR 548
Cdd:cd16027 337 -ELYDLKNDPDELNNLADDPEYAEVLEELR 365
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
40-548 |
1.52e-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: 213.93 E-value: 1.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNf 118
Cdd:cd16031 4 NIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFDASQP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 sTIPQYFKENGYVTMSVGKvFHPGISSNHSD---DYPYSWS-----FPPYHPSSEKYENTKGqdgklHANLLCpvdvadv 190
Cdd:cd16031 83 -TYPKLLRKAGYQTAFIGK-WHLGSGGDLPPpgfDYWVSFPgqgsyYDPEFIENGKRVGQKG-----YVTDII------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 191 pegtlpdkqsTEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENI----TLAPDPHvpDSLPPVAYNPW 266
Cdd:cd16031 149 ----------TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIpepeTFDDDDY--AGRPEWAREQR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 267 MDIREREDVQALNisvpygpiPEDFQRKIRQsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGeWA- 345
Cdd:cd16031 216 NRIRGVLDGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFd 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 346 KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCpips 425
Cdd:cd16031 286 KRLMYEESIRVPLIIRDPRLIKA------------------------GTVVDALVLNIDFAPTILDLAGVPIPEDM---- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 426 fhvelcrEGQNLQKHLQLHDLEEEPDLFgnpreLIAYSQYPRPADFPQWnsdkpslndikvmgYSIRTVDYRYTVWVGFD 505
Cdd:cd16031 338 -------QGRSLLPLLEGEKPVDWRKEF-----YYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYYGVW 391
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2202693044 506 PSEflanfsdihagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 548
Cdd:cd16031 392 DEE-----------ELYDLKKDPLELNNLANDPEYAEVLKELR 423
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-548 |
2.85e-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: 212.85 E-value: 2.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY----DFNSYWRVH 114
Cdd:cd16033 2 NILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 115 SGNFSTIPQYFKENGYVTMSVGKvFHPGISSNhsddyPYSWSFPPYHPssekYENTKgqdgklhanllcpvdvadvpEGT 194
Cdd:cd16033 82 PPGVETFSEDLREAGYRNGYVGK-WHVGPEET-----PLDYGFDEYLP----VETTI--------------------EYF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 195 LpdkqsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPHVPDSLPPVAYNpwmDIRERED 274
Cdd:cd16033 132 L-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYR---RERKRWG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 275 VQALNisvpygpipEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSNFDVA 353
Cdd:cd16033 204 VDTED---------EEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKgPFMYEET 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 354 TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrE 433
Cdd:cd16033 275 YRIPLIIKWPGVIAA------------------------GQVVDEFVSLLDLAPTILDLAGVDVPPKV-----------D 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 434 GQNLQKHLqlhdLEEEPDlfgNPRELIaysqyprpadFPQWNSdkpslNDIKVMGYSIRTVDYRYtVWVGFDpseflanf 513
Cdd:cd16033 320 GRSLLPLL----RGEQPE---DWRDEV----------VTEYNG-----HEFYLPQRMVRTDRYKY-VFNGFD-------- 368
|
490 500 510
....*....|....*....|....*....|....*
gi 2202693044 514 sdihAGELYFVDSDPLQDHNVYNDSQHGGLLHSLR 548
Cdd:cd16033 369 ----IDELYDLESDPYELNNLIDDPEYEEILREMR 399
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
40-418 |
2.84e-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: 196.50 E-value: 2.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16022 2 NILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 STIPQYFKENGYVTMSVGKvfhpgissNHsddypyswsfppyhpssekyentkgqdgklhanllcpvdvadvpegtlpdk 198
Cdd:cd16022 82 PTLAELLKEAGYRTALIGK--------WH--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 199 qstEEAIRLLEKMKTSAsPFFLAVGYHKPHIPFRypkefqklyplenitlapdphvpdslppvaynpwmdireredvqal 278
Cdd:cd16022 103 ---DEAIDFIERRDKDK-PFFLYVSFNAPHPPFA---------------------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 279 nisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE-WAKYSNFDVATRVP 357
Cdd:cd16022 133 --------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGIRVP 192
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2202693044 358 LMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVP 418
Cdd:cd16022 193 FIVRWPGKIP------------------------AGQVSDALVSLLDLLPTLLDLAGIEPP 229
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-533 |
4.52e-59 |
|
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: 201.26 E-value: 4.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHSGNF 118
Cdd:cd16034 3 NILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG-ND--VPLPPDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 STIPQYFKENGYVTMSVGKvFHpgISSNHSDDYPYSWSFPP-----------------YHPSSEKYENTkgqdgklhanl 181
Cdd:cd16034 80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDDD----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 182 lcpvDVADVPEGTLPDKQsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDphvpdslpp 260
Cdd:cd16034 146 ----GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN--------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 261 vaynpwmdireredvqalnisVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGE 340
Cdd:cd16034 212 ---------------------VPEDKKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 341 HGEWAKYSNFDVATRVPLMLYVPGRtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPPr 420
Cdd:cd16034 271 HGLMNKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPIPD- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 421 cpipsfhvelCREGQNLQKHLqlhdLEEEPDLFGNpreliAYSQYPRPadFPQWNSDKPSLNDIkvmgysIRTVDYRYTV 500
Cdd:cd16034 326 ----------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVP--FGGGSARDGGEWRG------VRTDRYTYVR 378
|
490 500 510
....*....|....*....|....*....|....*
gi 2202693044 501 WVGfdpseflanfsdihaGELYFVD--SDPLQDHN 533
Cdd:cd16034 379 DKN---------------GPWLLFDneKDPYQLNN 398
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-528 |
4.86e-59 |
|
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: 198.92 E-value: 4.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhSGNF 118
Cdd:cd16037 2 NILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPY---DGDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 STIPQYFKENGYVTMSVGKVFHPGISSNHSDDYpyswsfppyhpssekyentkgqdgklhanllcpvdvadvpegtlpDK 198
Cdd:cd16037 79 PSWGHALRAAGYETVLIGKLHFRGEDQRHGFRY---------------------------------------------DR 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 199 QSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredvqal 278
Cdd:cd16037 114 DVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY------------------------------------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 279 nisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPL 358
Cdd:cd16037 157 -------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVRVPM 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 359 MLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPipsfhvelcreGQNLQ 438
Cdd:cd16037 224 IISGPGIP-------------------------AGKRVKTPVSLVDLAPTILEAAGAPPPPDLD-----------GRSLL 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 439 khlqlhDLEEEPDlfgnPRELIAYSQYprpadfpqwnsdkpSLNDIKVMGYSIRTVDYRYTVWVGFDPseflanfsdiha 518
Cdd:cd16037 268 ------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP------------ 311
|
490
....*....|
gi 2202693044 519 gELYFVDSDP 528
Cdd:cd16037 312 -QLFDLENDP 320
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-457 |
2.83e-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: 198.17 E-value: 2.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQ----QAVCAPSRVSFLTGRrpdttrlydfnSYWRVH 114
Cdd:cd16155 4 NILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR-----------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 115 SGNFS-------TIPQYFKENGYVTMSVGKvfhpgissnhsddypysWsfppyhpssekyentkgqdgklHanllcpVDV 187
Cdd:cd16155 73 EGGKAaipsddkTWPETFKKAGYRTFATGK-----------------W----------------------H------NGF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 188 ADvpegtlpdkqsteEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPdsLPPVAyNPWM 267
Cdd:cd16155 108 AD-------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL-PENFLP--QHPFD-NGEG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 268 DIRereDVQALnisvPYGPIPEDFQRKIRQsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKY 347
Cdd:cd16155 171 TVR---DEQLA----PFPRTPEAVRQHLAE-YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLMGKQ 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 348 SNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIPSF- 426
Cdd:cd16155 243 NLYEHSMRVPLIISGPG-------------------------IPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLl 297
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2202693044 427 ----------HVELCREGQNLQ-----------------KHLQLHDLEEEP----DLFGNPR 457
Cdd:cd16155 298 pvirgekkavRDTLYGAYRDGQrairddrwkliiyvpgvKRTQLFDLKKDPdelnNLADEPE 359
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
40-419 |
2.19e-55 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 193.73 E-value: 2.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHSGN 117
Cdd:PRK13759 8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 118 FS-TIPQYFKENGYVTMSVGKV-FHP-----GISSNHSDDyPYSWSFPPYHPSSEKY---------ENTKGQDGKL-HAN 180
Cdd:PRK13759 84 YKnTLPQEFRDAGYYTQCIGKMhVFPqrnllGFHNVLLHD-GYLHSGRNEDKSQFDFvsdylawlrEKAPGKDPDLtDIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 181 LLCPVDVA---DVPEGTLPDKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPHVPDs 257
Cdd:PRK13759 163 WDCNSWVArpwDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 258 lppvaynpWmDIREREDVQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA 337
Cdd:PRK13759 238 --------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 338 LGEHGEWAKYSNFDVATRVPLMLYVPGRTAPLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 417
Cdd:PRK13759 309 LGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGN---------------------RGTVIDQVVELRDIMPTLLDLAGGTI 367
|
..
gi 2202693044 418 PP 419
Cdd:PRK13759 368 PD 369
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-420 |
1.91e-51 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 176.97 E-value: 1.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 39 LNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPdttrlydfnSYWRVHSG- 116
Cdd:cd16148 1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP---------FYHGVWGGp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 ---NFSTIPQYFKENGYVTMsvgkvfhpGISSNhsddyPYSWSFPPYHPSSEKYENTKGQDGklhanllcpvdvADVPEG 193
Cdd:cd16148 72 lepDDPTLAEILRKAGYYTA--------AVSSN-----PHLFGGPGFDRGFDTFEDFRGQEG------------DPGEEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 194 TLPDKQSTEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapDphvpdslppvaynpwmdirere 273
Cdd:cd16148 127 DERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-----------------D---------------------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 274 dvqalnisvpygpipedfqrkirqsyfASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSNF-D 351
Cdd:cd16148 167 ---------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSNLyD 219
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2202693044 352 VATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 420
Cdd:cd16148 220 EQLHVPLIIRWPGKE-------------------------PGKRVDALVSHIDIAPTLLDLLGVEPPDY 263
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-548 |
4.40e-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: 177.81 E-value: 4.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16150 2 NIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 StipQYFKENGYVTMSVGKvfhpgissnhSDDYPYSWSFPPYhpssekyentkgqdgklhanllCPVDVADVpegtlpdk 198
Cdd:cd16150 82 L---KTLKDAGYHVAWAGK----------NDDLPGEFAAEAY----------------------CDSDEACV-------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 199 qstEEAIRLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPdPHVPDSLPPVAYNPWMDIREREDVQAL 278
Cdd:cd16150 119 ---RTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLRAKGKPSMLEGIEKQGLDRW 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 279 NisvpygpipEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN-F-DVATRV 356
Cdd:cd16150 191 S---------EERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCLTRV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 357 PLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPrcpiPSFHVELCRegqn 436
Cdd:cd16150 262 PLIIKPPGGP-------------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THFGRSLLP---- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 437 lqkhlQLHDLEEEPD---------LFGNPReliAYSQYPRPADFPQWNS---DKPSLNDIKVMgysIRTVDYRYtVWVGF 504
Cdd:cd16150 309 -----VLAGETEEHRdavfseggrLHGEEQ---AMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VYRLY 376
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2202693044 505 DPSeflanfsdihagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 548
Cdd:cd16150 377 EPD------------ELYDLEADPLELHNLIGDPAYAEIIAEMK 408
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
39-422 |
5.24e-50 |
|
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: 175.07 E-value: 5.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 39 LNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhSGN 117
Cdd:cd16032 1 PNILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEF---PAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 118 FSTIPQYFKENGYVTMSVGKVFHPGISSNHSDDYpyswsfppyhpssekyentkgqdgklhanllcpvdvadvpegtlpD 197
Cdd:cd16032 78 IPTFAHYLRAAGYRTALSGKMHFVGPDQLHGFDY---------------------------------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 198 KQSTEEAIRLLEKMKTSAS--PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredv 275
Cdd:cd16032 113 EEVAFKAVQKLYDLARGEDgrPFFLTVSFTHPHDPYVIPQEYWDLY---------------------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 276 qalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATR 355
Cdd:cd16032 159 ----------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSAR 222
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2202693044 356 VPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAGLPVPPRCP 422
Cdd:cd16032 223 VPLIISAPGRFAP-------------------------RRVAEPVSLVDLLPTLVDLAGGGTAPHVP 264
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-417 |
1.21e-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: 172.56 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRP-SLGCYGDKL----------VRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFN 108
Cdd:cd16153 3 NILWIITDDQRVdSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 109 SYWRVHSGNFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypyswsfppyhpssEKYENtkgqdgklhanllcPVDVA 188
Cdd:cd16153 83 AAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA--------------FQRYL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 189 DVPEgtlpdkQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdphvpdslppvaynpwmd 268
Cdd:cd16153 122 KNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 269 iREREDvqalnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAH---NTIIAFTSDHGWALGEHGEWA 345
Cdd:cd16153 165 -RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGILA 219
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2202693044 346 KYSNFDVATRVPLMLYVPGRtaplpaagqKLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 417
Cdd:cd16153 220 KFTFWPQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
40-419 |
6.06e-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: 6.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16144 2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 S---------------TIPQYFKENGYVTMSVGKvFHPGISSNHS-DDYPYSWSFPPY---HPSSEKYENTKGqdgklha 179
Cdd:cd16144 82 KlipppsttrlpleevTIAEALKDAGYATAHFGK-WHLGGEGGYGpEDQGFDVNIGGTgngGPPSYYFPPGKP------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 180 nllcPVDVADVPEGTLPDKQSTEEAIRLLEkmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslp 259
Cdd:cd16144 154 ----NPDLEDGPEGEYLTDRLTDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKY------------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 260 pvaynpwmdireredvqalnisvpYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALG 339
Cdd:cd16144 210 ------------------------EKKKKGLRKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNG-GLS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 340 EHGEWA---------KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLA 410
Cdd:cd16144 265 TRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIKP------------------------GSVSDVPVIGTDLYPTFL 320
|
....*....
gi 2202693044 411 GLAGLPVPP 419
Cdd:cd16144 321 ELAGGPLPP 329
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
40-506 |
1.96e-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: 168.59 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFN--SYW----- 111
Cdd:cd16028 2 NVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR-------YLMNhrSVWngtpl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 112 RVHsgnFSTIPQYFKENGYVTMSVGK---VFHP-GISSNHsddyPYSWSfppYHPSSEKYEntkgqdgklhanllcPVDV 187
Cdd:cd16028 75 DAR---HLTLALELRKAGYDPALFGYtdtSPDPrGLAPLD----PRLLS---YELAMPGFD---------------PVDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 188 ADvpegTLPDKQS-----TEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDPHVPDSLP 259
Cdd:cd16028 130 LD----EYPAEDSdtaflTDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQH 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 260 PVaYNPWMDIREREDVQALNIsvPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALG 339
Cdd:cd16028 204 PL-LAAFLERIESLSFSPGAA--NAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 340 EHGEWAKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfDPASdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPP 419
Cdd:cd16028 281 DHWLWGKDGFFDQAYRVPLIVRDPRREA----------------DATR-----GQVVDAFTESVDVMPTILDWLGGEIPH 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 420 RCpipsfhvelcrEGQNLQKHLQlhdlEEEPdlfGNPRELIAYSQYPRPADFPQW------NSDKPSLNdikvmgySIRT 493
Cdd:cd16028 340 QC-----------DGRSLLPLLA----GAQP---SDWRDAVHYEYDFRDVSTRRPqealglSPDECSLA-------VIRD 394
|
490
....*....|...
gi 2202693044 494 VDYRYTVWVGFDP 506
Cdd:cd16028 395 ERWKYVHFAALPP 407
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
40-537 |
3.82e-45 |
|
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: 164.26 E-value: 3.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNaFAQQAVCAPSRVSFLTGRRPDTTRLydfnsyWRVHSG-- 116
Cdd:cd16146 2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGV------WHTILGre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 ----NFSTIPQYFKENGYVTMSVGKvFHPGissnhsDDYPY----------------SWSFPPYHPSSEKYENTKGQDGK 176
Cdd:cd16146 75 rmrlDETTLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 177 LHANllcpvdvadvpEGTLPDKQsTEEAIRLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpd 256
Cdd:cd16146 148 FVKT-----------EGYCTDVF-FDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPYK-------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 257 slppvaynpwmDIREREDVQAlnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGW 336
Cdd:cd16146 200 -----------DMGLDDKLAA---------------------FYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 337 ALGEHGEW------AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLA 410
Cdd:cd16146 248 AGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKILA------------------------GKDVDTLTAHIDLLPTLL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 411 GLAGLPVPPRCPIpsfhvelcrEGQNLQKHLQlHDLEEEPDlfgnpRELIAYSQYPRPADFPQWNSdkpslndikvmgyS 490
Cdd:cd16146 304 DLCGVKLPEGIKL---------DGRSLLPLLK-GESDPWPE-----RTLFTHSGRWPPPPKKKRNA-------------A 355
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2202693044 491 IRTVDYRYtVWVGFDPSeflanfsdihagELYFVDSDPLQDHNVYND 537
Cdd:cd16146 356 VRTGRWRL-VSPKGFQP------------ELYDIENDPGEENDVADE 389
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-423 |
8.05e-44 |
|
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: 160.42 E-value: 8.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16026 3 NIVVILADDLGYGdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 -NFSTIPQYFKENGYVTMSVGKvFHPGISS-----NHSDDY----PYS---WSFPPYHPSSEKYENTKGQDGKLHANllc 183
Cdd:cd16026 83 pDEITIAEVLKKAGYRTALVGK-WHLGHQPeflptRHGFDEyfgiPYSndmWPFPLYRNDPPGPLPPLMENEEVIEQ--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 184 PVDVADVPegtlpdKQSTEEAIRLLEKMKTsaSPFFLAVGYHKPHIPfrypkefqkLYPlenitlapdphvpdslppvay 263
Cdd:cd16026 159 PADQSSLT------QRYTDEAVDFIERNKD--QPFFLYLAHTMPHVP---------LFA--------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 264 npwmdireredvqalnisvpygpiPEDFQ-RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHG 342
Cdd:cd16026 201 ------------------------SEKFKgRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 343 EW--------AKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAG 414
Cdd:cd16026 257 HGgsagplrgGKGTTWEGGVRVPFIAWWPGVIP------------------------AGTVSDELASTMDLLPTLAALAG 312
|
....*....
gi 2202693044 415 LPVPPRCPI 423
Cdd:cd16026 313 APLPEDRVI 321
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-426 |
5.79e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 148.54 E-value: 5.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRV----- 113
Cdd:cd16149 2 NILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHgktkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 114 ---HSGNFSTIPQYFKENGYVTMSVGKvFHPGissnhsddypyswsfppyhpssekyentkgqdgklhanllcpvdvadv 190
Cdd:cd16149 82 pegYLEGQTTLPEVLQDAGYRCGLSGK-WHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 191 pegtlpdkqstEEAIRLLEKMKTSASPFFLAVGYHKPHipfrypkefqklyplenitlapdphvpdslppvayNPWmdir 270
Cdd:cd16149 113 -----------DDAADFLRRRAEAEKPFFLSVNYTAPH-----------------------------------SPW---- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 271 eredvqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK---- 346
Cdd:cd16149 143 ---------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngt 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 347 --YSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVP--PRCP 422
Cdd:cd16149 196 fpLNMYDNSVKVPFIIRWPGVVPA------------------------GRVVDSLVSAYDFFPTLLELAGVDPPadPRLP 251
|
....
gi 2202693044 423 IPSF 426
Cdd:cd16149 252 GRSF 255
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
40-420 |
1.25e-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: 151.98 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY---WRVHS 115
Cdd:cd16145 2 NIIFILADDLGYGdLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPggqDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 116 GNfSTIPQYFKENGYVTMSVGK-----VFHPGISSNHSDDYPYSWS--------FPPYhpsseKYENTKGQDgklHANLL 182
Cdd:cd16145 82 DD-VTLAEVLKKAGYATAAFGKwglggPGTPGHPTKQGFDYFYGYLdqvhahnyYPEY-----LWRNGEKVP---LPNNV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 183 CPVDVADVPEGTLPDKQS----TEEAIRLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDPHVPDSL 258
Cdd:cd16145 153 IPPLDEGNNAGGGGGTYShdlfTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYKYKPKDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 259 PPVAYNPWmdireredvqalnisvpygpipedfqRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwAL 338
Cdd:cd16145 219 GIYAYLPW--------------------------PQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG-PH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 339 GEHGEWAKYSNFDVA--------------TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVS 404
Cdd:cd16145 272 SEGGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPGKIPA------------------------GSVSDHPSAFWD 327
|
410
....*....|....*.
gi 2202693044 405 LFPTLAGLAGLPVPPR 420
Cdd:cd16145 328 FMPTLADLAGAEPPED 343
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-533 |
3.66e-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: 141.58 E-value: 3.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAqQAVCAPSRVSFLTGRRPDTTrlYDFNSYWrvHSGNf 118
Cdd:cd16151 2 NIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRN--YVVFGYL--DPKQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 STIPQYFKENGYVTMSVGKvfhPGISSNHSD-DYPY-----SWSFPPYHPSSEKYENTKGQDGKLHANllcpVDVADVPE 192
Cdd:cd16151 76 KTFGHLLKDAGYATAIAGK---WQLGGGRGDgDYPHefgfdEYCLWQLTETGEKYSRPATPTFNIRNG----KLLETTEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 193 GTLPDkQSTEEAIRLLEKMKtsASPFFLavgYhkphipfrYPkefqklyplenITLAPDPHV--PDSLppvaynPWMDIR 270
Cdd:cd16151 149 DYGPD-LFADFLIDFIERNK--DQPFFA---Y--------YP-----------MVLVHDPFVptPDSP------DWDPDD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 271 ERedvqalnisvpygpipedfqRKIRQSYF-ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW----- 344
Cdd:cd16151 198 KR--------------------KKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTngrev 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 345 --AKYSNFDVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSLFPTLAGLAGLPVPPRCP 422
Cdd:cd16151 258 rgGKGKTTDAGTHVPLIVNWPGLI------------------------PAGGVSDDLVDFSDFLPTLAELAGAPLPEDYP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 423 IpsfhvelcrEGQNLQkhlqlhdleeePDLFGNP----RELIAYsqYPRpadfPQWNSDKPslndikvmgYSIRTVDYRY 498
Cdd:cd16151 314 L---------DGRSFA-----------PQLLGKTgsprREWIYW--YYR----NPHKKFGS---------RFVRTKRYKL 358
|
490 500 510
....*....|....*....|....*....|....*
gi 2202693044 499 tvwvgfdpseflanFSDihaGELYFVDSDPLQDHN 533
Cdd:cd16151 359 --------------YAD---GRFFDLREDPLEKNP 376
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
40-415 |
2.39e-36 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 137.17 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNsywRVHSGN- 117
Cdd:pfam00884 2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVST---PVGLPRt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 118 FSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDYPYSWSFPPYHPSSEKYENTKGQDGklhanlLCPVDVADvpegtlpD 197
Cdd:pfam00884 79 EPSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPY------NCSGGGVS-------D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 198 KQSTEEAIRLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpdslppvaynpwmdireredvqa 277
Cdd:pfam00884 145 EALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA----------------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 278 lnISVPYGpipeDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA---- 353
Cdd:pfam00884 187 --TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApegg 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2202693044 354 TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 415
Cdd:pfam00884 261 YRVPLLIWSPGGKAK------------------------GQKSEALVSHVDLFPTILDLAGI 298
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
40-423 |
2.56e-35 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 136.53 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQaVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16029 2 HIVFILADDLGWNdVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILAGEPYGlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 -NFSTIPQYFKENGYVTMSVGKvFHPGIssnhsddypYSWSFPP----------YHPSSEKYENTKGQDGKLHANLLCPV 185
Cdd:cd16029 81 lNETLLPQYLKELGYATHLVGK-WHLGF---------YTWEYTPtnrgfdsfygYYGGAEDYYTHTSGGANDYGNDDLRD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 186 DVADVPEGTlpDKQST----EEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlAPDPHVPDslppv 261
Cdd:cd16029 151 NEEPAWDYN--GTYSTdlftDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE------DKFAHIKD----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 262 aynpwmdireredvqalnisvpygpipedfqrKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALGEH 341
Cdd:cd16029 217 --------------------------------EDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG-GPTGG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 342 GEWA--------KYSNFDVATRVPLMLYVPGRTaplPAAGQKlfpYRDPFDpASDWmdagrhtedlvelvslFPTLAGLA 413
Cdd:cd16029 264 GDGGsnyplrggKNTLWEGGVRVPAFVWSPLLP---PKRGTV---SDGLMH-VTDW----------------LPTLLSLA 320
|
410
....*....|
gi 2202693044 414 GLPVPPRCPI 423
Cdd:cd16029 321 GGDPDDLPPL 330
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-548 |
3.62e-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: 133.12 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHSGNF 118
Cdd:cd16152 3 NVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFR-NG--IPLPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 STIPQYFKENGYVTMSVGKvfhpgissnhsddypysWSFPPYHpssekyentkgqdgklhanllcpVDVAdvpegtlpdk 198
Cdd:cd16152 80 KTLAHYFRDAGYETGYVGK-----------------WHLAGYR-----------------------VDAL---------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 199 qsTEEAIRLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYplenitlaPDPHVPdslppvaynpwmdirerE 273
Cdd:cd16152 110 --TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERF--------ANFWVP-----------------P 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 274 DVQALnisvpygpiPEDFQRKIrQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHgwalGEH-----GEWaKYS 348
Cdd:cd16152 162 DLAAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY-KRS 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 349 NFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPprcpiPSFHv 428
Cdd:cd16152 227 CHESSIRVPLVIYGPG-------------------------FNGGGRVEELVSLIDLPPTLLDAAGIDVP-----EEMQ- 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 429 elcreGQNLQKhlqlhDLEEEPDlfgnPRELIAYSQyprpadfpqwnsdkpsLNDIKVmGYSIRTVDYRYTVwVGFDPSE 508
Cdd:cd16152 276 -----GRSLLP-----LVDGKVE----DWRNEVFIQ----------------ISESQV-GRAIRTDRWKYSV-AAPDKDG 323
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2202693044 509 FLANFSDIHAGE-LYFVDSDPLQDHNVYNDSQHGGLLHSLR 548
Cdd:cd16152 324 WKDSGSDVYVEDyLYDLEADPYELVNLIGRPEYREVAAELR 364
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
40-419 |
4.95e-34 |
|
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: 133.06 E-value: 4.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPSLGCYGD--KLVRspnidQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPD----TTRLYDFNSYWRV 113
Cdd:cd16147 3 NIVLILTDDQDVELGSMDPmpKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHnhgvTNNSPPGGGYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 114 HSGNF--STIPQYFKENGYVTMSVGKVFHpGISSNHSDDYP---YSWSFPPYHPSseKYENTKGQDGKLHanllcpVDVA 188
Cdd:cd16147 78 WQNGLerSTLPVWLQEAGYRTAYAGKYLN-GYGVPGGVSYVppgWDEWDGLVGNS--TYYNYTLSNGGNG------KHGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 189 DVPEGTLPDKqSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAPDPHVPDslPPVAYNP-Wm 267
Cdd:cd16147 149 SYPGDYLTDV-IANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPRPPPNN--PDVSDKPhW- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 268 dIREREDVQALNISVpygpIPEDFQRKIR--QSyfasvsyLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHG-EW 344
Cdd:cd16147 223 -LRRLPPLNPTQIAY----IDELYRKRLRtlQS-------VDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRlPP 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2202693044 345 AKYSNFDVATRVPLMLYVPGrtapLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 419
Cdd:cd16147 291 GKRTPYEEDIRVPLLVRGPG----IP---------------------AGVTVDQLVSNIDLAPTILDLAGAPPPS 340
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
40-419 |
2.20e-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: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTtrlydfNSYWR---VHS 115
Cdd:cd16156 2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT------NGSWTncmALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 116 GNFSTIPQYFKENGYVTMSVGKVfhpgissnHSD--DY------PYSWSfPPYHPSSEKY-ENTKGQDGKLHANLLCPVD 186
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKW--------HLDggDYfgngicPQGWD-PDYWYDMRNYlDELTEEERRKSRRGLTSLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 187 VADVPEGTLPDKQSTEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplENITLAPDPHVPDSLP--PVAYN 264
Cdd:cd16156 147 AEGIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLHQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 265 PWMDIREREDVQALNISVPYgpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLrlAHNTIIAFTSDHGWALGEHGEW 344
Cdd:cd16156 223 LWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHKLW 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2202693044 345 AK-YSNFDVATRVPLMLYVPGRtapLPAAGQKLFPyrdpfdpasdwmdagrhtedlVELVSLFPTLAGLAGLPVPP 419
Cdd:cd16156 287 AKgPAVYDEITNIPLIIRGKGG---EKAGTVTDTP---------------------VSHIDLAPTILDYAGIPQPK 338
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
40-418 |
2.49e-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: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRP-SLGCYGDK-LVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNsyWRVHSG- 116
Cdd:cd16143 2 NIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV--LGGFSPp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 ----NFSTIPQYFKENGYVTMSVGKvFHPGIssnhsdDYPYSWSFPPYHPSSEKYENTKG-QDGklhanllcPVDV---- 187
Cdd:cd16143 80 liepDRVTLAKMLKQAGYRTAMVGK-WHLGL------DWKKKDGKKAATGTGKDVDYSKPiKGG--------PLDHgfdy 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 188 ------ADVpegtlpDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapdphvpdslppv 261
Cdd:cd16143 145 yfgipaSEV------LPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQG---------------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 262 aynpwmdireredVQALNisvPYGpipeDFqrkIRQsyfasvsyLDTQVGHVLSALDDLRLAHNTIIAFTSDHG------ 335
Cdd:cd16143 197 -------------KSGAG---PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyad 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 336 -WALGEHGEWA-------KYSNFDVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSLFP 407
Cdd:cd16143 246 yKELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKI------------------------PAGSVSDQLVSLTDLFA 301
|
410
....*....|.
gi 2202693044 408 TLAGLAGLPVP 418
Cdd:cd16143 302 TLAAIVGQKLP 312
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
40-419 |
2.10e-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: 122.26 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVR---SPNIDQLASHSVLFQNAFAQQAvCAPSRVSFLTGRRPdttrlydfnsywrVHS 115
Cdd:cd16142 2 NILVILGDDIGWGdLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP-------------IRT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 116 GNFS---------------TIPQYFKENGYVTMSVGKvfhpgissNHSDDYPYSWsfppyhpssekyentkgqdgklhan 180
Cdd:cd16142 68 GLTTvglpgspgglppwepTLAELLKDAGYATAQFGK--------WHLGDEDGRL------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 181 llcPVDVA-DVPEGTLP---DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpd 256
Cdd:cd16142 115 ---PTDHGfDEFYGNLYhtiDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS-------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 257 slppvAYNPWMDireredvqalnisvpygpipedfqrkirqsyfaSVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG- 335
Cdd:cd16142 178 -----GKGKYAD---------------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGp 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 336 ----WALGEHGEW--AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTL 409
Cdd:cd16142 220 eqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGKIKP------------------------GRVSNEIVSHLDWFPTL 275
|
410
....*....|
gi 2202693044 410 AGLAGLPVPP 419
Cdd:cd16142 276 AALAGAPDPK 285
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
40-418 |
6.81e-29 |
|
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: 118.31 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDkLVRSPNIDQLASHSVLFQNaFAQQAVCAPSRVSFLTGRRP-------DTTRLYDFNSYW 111
Cdd:cd16025 4 NILLILADDLGFSdLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHhqvgmgtMAELATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 112 RVHSGNFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypysW--SFPPYHpSSEKYentkgqdgklhanllcpvdvad 189
Cdd:cd16025 82 GYLPDSAATIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL---------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 190 vpegtlpdkqsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LYPlE 244
Cdd:cd16025 122 -----------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLIP-A 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 245 NITLAPDPH-VP--DSLPPvaynpwmdirEREDVQALNISVpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLR 321
Cdd:cd16025 190 DTKLTPRPPgVPawDSLSP----------EEKKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKELG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 322 LAHNTIIAFTSDHGwALGEHGeWAKYSNfdvaTrvPLMLYvpgrtaplpaagqKLFPY----RDPF--DPASDWMDAGRH 395
Cdd:cd16025 244 ELDNTLIIFLSDNG-ASAEPG-WANASN----T--PFRLY-------------KQASHeggiRTPLivSWPKGIKAKGGI 302
|
410 420
....*....|....*....|...
gi 2202693044 396 TEDLVELVSLFPTLAGLAGLPVP 418
Cdd:cd16025 303 RHQFAHVIDIAPTILELAGVEYP 325
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-420 |
1.21e-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: 113.07 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYD-FNSYWRVH-SG 116
Cdd:cd16035 2 NILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLlSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 NFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypysWsfppyHPSSekyentkgqdgklHANllcpvdvadvpEGTLP 196
Cdd:cd16035 82 DVPTLGHMLRAAGYYTAYKGK-----------------W-----HLSG-------------AAG-----------GGYKR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 197 DKQSTEEAIRLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdphvpdslppvaynpwmdirere 273
Cdd:cd16035 116 DPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH--------------------------------------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 274 DVQalnisvpYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN-FDV 352
Cdd:cd16035 151 DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNaYEE 223
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2202693044 353 ATRVPLMLYVPGrtaplpaagqkLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 420
Cdd:cd16035 224 ALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGVDAEAR 267
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
40-419 |
6.74e-25 |
|
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: 106.09 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPSLGCY-GDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRlyDFNSYWRVHSgNF 118
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE--SWNNYKGLDP-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 STIPQYFKENGYVTMSVGKVFHpgISSNHS-DDYPYSWSfppyhpssEKYENTKGQDGKLHANLLCPVDVADVpegTLPD 197
Cdd:cd16171 79 PTWMDRLEKHGYHTQKYGKLDY--TSGHHSvSNRVEAWT--------RDVPFLLRQEGRPTVNLVGDRSTVRV---MLKD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 198 KQSTEEAIRLLEKMKTSAS-PFFLAVGYHKPHiPFRYPkefqklypleniTLAPDphvpdslppvaynpwmdireredvq 276
Cdd:cd16171 146 WQNTDKAVHWIRKEAPNLTqPFALYLGLNLPH-PYPSP------------SMGEN------------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 277 alnisvpYGPIpedfqRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRV 356
Cdd:cd16171 188 -------FGSI-----RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGSSHV 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2202693044 357 PLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPP 419
Cdd:cd16171 256 PLLIMGPG-------------------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
40-418 |
3.85e-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: 105.83 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY----WRVH 114
Cdd:cd16159 3 NIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMrvilFTAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 115 SG----NFSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDYpyswsfpPYHPSSEKYENTKGqdgklhanllcpvdvadV 190
Cdd:cd16159 83 SGglppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDF-------CHHPLNHGFDYFYG-----------------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 191 PEGTLPDKQSTEEAI--RLLEKMKTSASPF------FLAVGYHKPHIPFRY--------------PKEFQKLYPLENITL 248
Cdd:cd16159 138 PLTNLKDCGDGSNGEydLSFDPLFPLLTAFvlitalTIFLLLYLGAVSKRFfvfllilsllfislFFLLLITNRYFNCIL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 249 APDPHV---PDSLPPVAY------NPWMDIRERED----VQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLS 315
Cdd:cd16159 218 MRNHEVveqPMSLENLTQrltkeaISFLERNKERPfllvMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 316 ALDDLRLAHNTIIAFTSDHGWAL------GEHGEW-------AKYSNFDVATRVPLMLYVPGRTAPlpaaGQKLfpyrdp 382
Cdd:cd16159 298 ALDELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGVIPP----GSVI------ 367
|
410 420 430
....*....|....*....|....*....|....*.
gi 2202693044 383 fDPASDWMDagrhtedlvelvsLFPTLAGLAGLPVP 418
Cdd:cd16159 368 -DEPTSLMD-------------IFPTVAALAGAPLP 389
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
40-418 |
9.61e-21 |
|
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: 95.20 E-value: 9.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16158 3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 -NFSTIPQYFKENGYVTMSVGKvFHPGISSNHS--------DDY---PYSWSFPPYHPSSEKYENTKGQDGKLHANLLCP 184
Cdd:cd16158 83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNGTylpthqgfDHYlgiPYSHDQGPCQNLTCFPPNIPCFGGCDQGEVPCP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 185 VDVADVPEGTLPD-----KQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdphvpdslp 259
Cdd:cd16158 162 LFYNESIVQQPVDlltleERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFA--------------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 260 pvaynpwmdireredvqalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL- 338
Cdd:cd16158 221 --------------------------------GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTm 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 339 -----GEHG--EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRhTEDLVELVSLFPTLAG 411
Cdd:cd16158 269 rksrgGNAGllKCGKGTTYEGGVREPAIAYWPGRIKP------------------------GV-THELASTLDILPTIAK 323
|
....*..
gi 2202693044 412 LAGLPVP 418
Cdd:cd16158 324 LAGAPLP 330
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-418 |
3.31e-19 |
|
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: 90.60 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSywrvHSGNF 118
Cdd:cd16157 3 NIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA----HARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 119 ST--------------IPQYFKENGYVTMSVGK-------VFHPgisSNHSDDYPY---SWSFPPY----HPSSEKYENT 170
Cdd:cd16157 79 YTpqnivggipdseilLPELLKKAGYRNKIVGKwhlghrpQYHP---LKHGFDEWFgapNCHFGPYdnkaYPNIPVYRDW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 171 KGQdGKLHANLlcPVDVADvPEGTLpDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPfrypkefqkLYplenitlap 250
Cdd:cd16157 156 EMI-GRYYEEF--KIDKKT-GESNL-TQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAP---------VY--------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 251 dphvpdslppvAYNPWMDIREREdvqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAF 330
Cdd:cd16157 213 -----------ASKPFLGTSQRG------------------------LYGDAVMELDSSVGKILESLKSLGIENNTFVFF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 331 TSDHGWAL-------GEHGEW--AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVE 401
Cdd:cd16157 258 SSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGHIKP------------------------GQVSHQLGS 313
|
410
....*....|....*..
gi 2202693044 402 LVSLFPTLAGLAGLPVP 418
Cdd:cd16157 314 LMDLFTTSLALAGLPIP 330
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
40-419 |
4.13e-19 |
|
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: 89.45 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLR-PSLGCYGDKLVR-SPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVHSG- 116
Cdd:cd16161 3 NFLLLFADDLGwGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH-NFLPTSVGGl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 --NFSTIPQYFKENGYVTMSVGKvFHPGISSNhsddypyswsfppYHPSSEKYENTKGqdgklhanllcpvdvadVP--- 191
Cdd:cd16161 82 plNETTLAEVLRQAGYATGMIGK-WHLGQREA-------------YLPNSRGFDYYFG-----------------IPfsh 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 192 EGTLPDKQStEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPkefqklyplenitlaPDPHVPDSlppvaynpwmdire 271
Cdd:cd16161 131 DSSLADRYA-QFATDFIQRASAKDRPFFLYAALAHVHVPLANL---------------PRFQSPTS-------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 272 redvqalnISVPYGpipedfqrkirqsyfASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG-WALG-------EHGE 343
Cdd:cd16161 181 --------GRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpGTGD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 344 W--------AKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGL 415
Cdd:cd16161 238 WqgnlggsvAKASTWEGGHREPAIVYWPGRIP------------------------ANSTSAALVSTLDIFPTVVALAGA 293
|
....
gi 2202693044 416 PVPP 419
Cdd:cd16161 294 SLPP 297
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-419 |
8.42e-19 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 89.71 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 28 SAAQGNSATDALNILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGrrpdttrLYD 106
Cdd:COG1368 224 PTPNPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-------LPP 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 107 FNS---YWRVHSGNFSTIPQYFKENGYVTMsvgkVFHPGissnhsddYPYSWSFPPYHPsSEKYENTKGQDgklhanllc 183
Cdd:COG1368 297 LPGgspYKRPGQNNFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYK-NLGFDEFYDRE--------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 184 pvDVADVPEGT--LPDKQSTEEAIRLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITLapdphvpds 257
Cdd:COG1368 355 --DFDDPFDGGwgVSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL--------- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 258 lppvaynpwmdireredvqalnisvpygpipedfqrkirQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwa 337
Cdd:COG1368 417 ---------------------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG-- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 338 lGEHGEWAKYSNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPV 417
Cdd:COG1368 456 -PRSPGKTDYENPLERYRVPLLIYSPG-------------------------LKKPKVIDTVGSQIDIAPTLLDLLGIDY 509
|
..
gi 2202693044 418 PP 419
Cdd:COG1368 510 PS 511
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
40-414 |
2.97e-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: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRpslgcYGDKLV-------RSPnIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY--DFNSY 110
Cdd:cd16160 3 NIVLFFADDMG-----YGDLASyghptqeRGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 111 WRVHSG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDypyswsfpPYHPSSEKYENTKGQDGKLHANLLC---- 183
Cdd:cd16160 77 PWDIGGlpkTEVTMAEALKEAGYTTGMVGK-WHLGINENNHSD--------GAHLPSHHGFDFVGTNLPFTNSWACddtg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 184 -PVDVADVPEGTLPDK-QSTEEAIR---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyplenitla 249
Cdd:cd16160 148 rHVDFPDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK----------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 250 pdphvpdslppvaynpwmdireredvqalNISVpygpipedfqrkiRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIA 329
Cdd:cd16160 217 -----------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVF 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 330 FTSDHGWAL---GEHGEWA-----KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVE 401
Cdd:cd16160 255 FLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTIKP-------------------------RVSHEVVS 309
|
410
....*....|...
gi 2202693044 402 LVSLFPTLAGLAG 414
Cdd:cd16160 310 TMDIFPTFVDLAG 322
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
40-414 |
4.95e-16 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 78.49 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVC--APSRVSFLTGRRPDTTRLYDFNSYwrvHSG 116
Cdd:cd16015 2 NVIVILLESFsDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPPLPLGSGSYTLY---KLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 NFSTIPQYFKENGYVTMSvgkvFHPGissnhsddYPYSWSFPPYHPSsEKYENTKGQDGKlhanllcPVDVADVPEGTLP 196
Cdd:cd16015 79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPN-LGFDEFYDLEDF-------PDDEKETNGWGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 197 DKQSTEEAIRLLEKMKtsASPFFLAVgyhkphipfrypkefqklyplenITLapDPHVPDSLPPVAYNPwmdireredvq 276
Cdd:cd16015 139 DESLFDQALEELEELK--KKPFFIFL-----------------------VTM--SNHGPYDLPEEKKDE----------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 277 alnisvpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDvATRV 356
Cdd:cd16015 181 ---------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLD-LYRT 250
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2202693044 357 PLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAG 414
Cdd:cd16015 251 PLLIYSPGLKKP-------------------------KKIDRVGSQIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-418 |
5.38e-13 |
|
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: 70.46 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDL-RPSLGCY--GDKLVRSPNIDQLASHSVLFQNAFAqQAVCAPSRVSFLTGRrpdttrlYDFN----SYWR 112
Cdd:cd16154 2 NILLIIADDQgLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGK-------YGFRtgvlAVPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 113 VHSGNFSTIPQYFKEN----GYVTMSVGKvFHPGISSNHsddypyswsfPPYHPSSEKYENTKGQDGKLHANLLCPVDVA 188
Cdd:cd16154 74 ELLLSEETLLQLLIKDattaGYSSAVIGK-WHLGGNDNS----------PNNPGGIPYYAGILGGGVQDYYNWNLTNNGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 189 DVPEGTLPDKQSTEEAIRLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDphvpdsLPPVAYNPw 266
Cdd:cd16154 143 TTNSTEYATTKLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGD------SADIEANP- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 267 mdireredvqalnisvpygpipedfqrkiRQSYFASVSYLDTQVGHVLSALDDLRLAhNTIIAFTSDHG--------WAL 338
Cdd:cd16154 206 -----------------------------RPYYLAAIEAMDTEIGRLLASIDEEERE-NTIIIFIGDNGtpgqvvdlPYT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 339 GEHgewAKYSNFDVATRVPLMlyvpgrtaplpAAGQKLfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVP 418
Cdd:cd16154 256 RNH---AKGSLYEGGINVPLI-----------VSGAGV-------------ERANERESALVNATDLYATIAELAGVDAA 308
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
40-413 |
5.72e-13 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 68.60 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQnAFAQQAVC--APSRVSFLTGRRPDttrlydfnsywrvhsg 116
Cdd:cd00016 2 HVVLIVLDGLGADdLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTssAPNHAALLTGAYPT---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 117 nfstipqyfkENGYVTMSVGKVFHPGISSNHSDDYPyswSFPpyhpssekyentkgqdgklhanllcpvdvadvpeGTLP 196
Cdd:cd00016 65 ----------LHGYTGNGSADPELPSRAAGKDEDGP---TIP----------------------------------ELLK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 197 DKQSTEEAIRLLE--KMKTSASPFFLAVGYHKPHIPFrypkefqklyplenitlapdpHVPDSLPPvaynpwmdirered 274
Cdd:cd00016 98 QAGYRTGVIGLLKaiDETSKEKPFVLFLHFDGPDGPG---------------------HAYGPNTP-------------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 275 vqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYS----NF 350
Cdd:cd00016 143 -----------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgkadKS 199
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2202693044 351 DVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLA 413
Cdd:cd00016 200 HTGMRVPFIAYGPG-------------------------VKKGGVKHELISQYDIAPTLADLL 237
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
197-367 |
3.72e-12 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 68.78 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 197 DKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIpFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredvQ 276
Cdd:COG3083 363 DRQITAQWLQWLDQ-RDSDRPWFSYLFLDAPHA-YSFPADYPKPF----------------------------------Q 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 277 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE--WAKYSNF-DVA 353
Cdd:COG3083 407 PSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFsRYQ 486
|
170
....*....|....
gi 2202693044 354 TRVPLMLYVPGRTA 367
Cdd:COG3083 487 LQVPLVIHWPGTPP 500
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
301-364 |
2.54e-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: 2.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2202693044 301 ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA-LGEHGewakYSNFDVATRVPLMLYVPG 364
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
228-415 |
3.32e-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: 42.61 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 228 HIPF--RYPKEFQKLYPlenitlapdphvpdslppvaynpwmdireredvqalnisVPYGPIPEDFQRKIRQSYFASVSY 305
Cdd:cd16017 154 HGPYydRYPEEFAKFTP---------------------------------------DCDNELQSCSKEELINAYDNSILY 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 306 LDTQVGHVLSALDdlRLAHNTIIAFTSDHGWALGEHGEW--AKYSNFDVATRVPLMLYVPGRTAPLPAAGQKLFPYRDPF 383
Cdd:cd16017 195 TDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENGLYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPF 272
|
170 180 190
....*....|....*....|....*....|..
gi 2202693044 384 DpaSDWmdagrhtedlvelvsLFPTLAGLAGL 415
Cdd:cd16017 273 S--HDN---------------LFHTLLGLLGI 287
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
19-112 |
4.40e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 39.35 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2202693044 19 LGSFCIALESAAQGNSATDALNILLIIVDDLRPslgcygDKLVR--SPNIDQLASHSVLFQNAfaqQAVC----APSRVS 92
Cdd:COG1524 4 GLSLLLASLLAAAAAAAPPAKKVVLILVDGLRA------DLLERahAPNLAALAARGVYARPL---TSVFpsttAPAHTT 74
|
90 100
....*....|....*....|
gi 2202693044 93 FLTGRRPDTTRLYDFNSYWR 112
Cdd:COG1524 75 LLTGLYPGEHGIVGNGWYDP 94
|
|
| |
