|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
38-540 |
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: 600.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16030 4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 118 TIPQYFKENGYVTMSVGKVFHPGISsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLP 197
Cdd:cd16030 84 TLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 198 DKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPEVPDGLPPVAYNPWMDIRQREDVQ 277
Cdd:cd16030 162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 278 ALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHV 357
Cdd:cd16030 241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 358 PLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvpsfhvelCREGKN 437
Cdd:cd16030 321 PLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 438 LLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwnsdkpslkdikIMGYSIRTIDYRYTVWVgfnpdeflaNFS 515
Cdd:cd16030 366 LV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFD 409
|
490 500
....*....|....*....|....*
gi 2335187 516 DIHAGELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16030 410 KVGAEELYDHKNDPNEWKNLANDPE 434
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
22-538 |
8.01e-91 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 284.08 E-value: 8.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 22 VALGSETQANSTTDALNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT 100
Cdd:COG3119 9 LALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 101 RLYDFNSYWRVH-AGNFSTIPQYFKENGYVTMSVGKVFHpgissnHTDDspyswsfppyhpssekyentktcrgpdgELh 179
Cdd:COG3119 89 GVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTD----------------------------LL- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 180 anllcpvdvldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlapdpEVPDGL 259
Cdd:COG3119 134 ----------------------TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI------PLPPNL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 260 PPVAYNPWmdirqredvqalnisvpygpipvdFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWAL 339
Cdd:COG3119 186 APRDLTEE------------------------ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 340 GEHG-EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:COG3119 242 GEHGlRGGKGTLYEGGIRVPLIVRWPGKIK------------------------AGSVSDALVSLIDLLPTLLDLAGVPI 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 419 PPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPsdipqwnsdkpslkdikIMGYSIRTIDYR 498
Cdd:COG3119 298 PEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRG-----------------GGNRAIRTGRWK 340
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2335187 499 YTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYND 538
Cdd:COG3119 341 LIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-549 |
1.54e-60 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 205.53 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY----DFNSYWRVH 112
Cdd:cd16033 2 NILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 113 AGNFSTIPQYFKENGYVTMSVGKvFHPGissnhTDDSPYSWSFPPYHPssekYENTKtcrgpdgelhanllcpvdvldvp 192
Cdd:cd16033 82 PPGVETFSEDLREAGYRNGYVGK-WHVG-----PEETPLDYGFDEYLP----VETTI----------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 193 EGTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVP-DGLPPVAYNpwmdIR 271
Cdd:cd16033 129 EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDfEDKPYIYRR----ER 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 272 QREDVQALNISVpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAK-YSN 350
Cdd:cd16033 200 KRWGVDTEDEED---------WKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKgPFM 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 351 FDVATHVPLIFYVPGrtaslpeageklfpyldpfdsasqLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhve 430
Cdd:cd16033 271 YEETYRIPLIIKWPG------------------------VIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKV-------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 431 lcrEGKNLLKHFRfrdlEEDPylPGNPRELIAysqyprpsdipQWNSDKPSLkdikiMGYSIRTIDYRYTvwvgFNPdef 510
Cdd:cd16033 319 ---DGRSLLPLLR----GEQP--EDWRDEVVT-----------EYNGHEFYL-----PQRMVRTDRYKYV----FNG--- 366
|
490 500 510
....*....|....*....|....*....|....*....
gi 2335187 511 lanfSDIhaGELYFVDSDPLQDHNMYNDSQGGDLFQLLM 549
Cdd:cd16033 367 ----FDI--DELYDLESDPYELNNLIDDPEYEEILREMR 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
38-540 |
8.17e-59 |
|
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: 199.66 E-value: 8.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 118 TIPQYFKENGYVTMSVGKVFHPGissnhtdDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANllcpvdvldvpegtlP 197
Cdd:cd16027 82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRA---------------K 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 198 DKQsteqaiqllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAP----DPEVpdglppvaynpwmdirqR 273
Cdd:cd16027 140 KGQ-----------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPylpdTPEV-----------------R 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 274 EDVQAlnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGehgeWAKYSNFDV 353
Cdd:cd16027 186 EDLAD---------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDS 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 354 ATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvpsfhvELcr 433
Cdd:cd16027 241 GLRVPLIVRWPGKI------------------------KPGSVSDALVSFIDLAPTLLDLAGIEPPE---------YL-- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 434 EGKNLLkhfrfrDLEEDPYLPGNP-----RELIAYSQYP-RpsdipqwnsdkpslkdikimgySIRTIDYRYTvwvgFNP 507
Cdd:cd16027 286 QGRSFL------PLLKGEKDPGRDyvfaeRDRHDETYDPiR----------------------SVRTGRYKYI----RNY 333
|
490 500 510
....*....|....*....|....*....|...
gi 2335187 508 DEFlanfsdihagELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16027 334 MPE----------ELYDLKNDPDELNNLADDPE 356
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
38-419 |
1.10e-57 |
|
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: 192.27 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16022 2 NILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 STIPQYFKENGYVTMSVGKvfhpgissNHtddspyswsfppyhpssekyentktcrgpdgelhanllcpvdvldvpegtl 196
Cdd:cd16022 82 PTLAELLKEAGYRTALIGK--------WH--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 197 pdkqstEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRypkefqklyplenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:cd16022 103 ------DEAIDFIERRDKDK-PFFLYVSFNAPHPPFA------------------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 277 qalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGE-WAKYSNFDVAT 355
Cdd:cd16022 133 -----------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGI 189
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2335187 356 HVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16022 190 RVPFIVRWPGK------------------------IPAGQVSDALVSLLDLLPTLLDLAGIEPP 229
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-534 |
6.34e-57 |
|
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: 195.48 E-value: 6.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLydFNSYWRVHAgNF 116
Cdd:cd16034 3 NILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV--FGNDVPLPP-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 STIPQYFKENGYVTMSVGKvFHpgISSNHTDDSPYSWSFPP-----------------YHPSSEKYENTktcrgpdgelh 179
Cdd:cd16034 80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDDD----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 180 anllcpvDVLDVPEGTLPDKQsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDpevpdg 258
Cdd:cd16034 146 -------GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 259 lppvaynpwMDIRQREDVQAlnisvpygpipvdfQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWA 338
Cdd:cd16034 212 ---------VPEDKKEEAGL--------------REDLRG-YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 339 LGEHGEWAKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:cd16034 268 LGSHGLMNKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPI 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 419 PPrcpvpsfhvelCREGKNLLKHFrfrdLEEDPYLPGNpreliAYSQYPRPSDipQWNSDKPSLKDIkimgysIRTIDYR 498
Cdd:cd16034 324 PD-----------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVPFG--GGSARDGGEWRG------VRTDRYT 375
|
490 500 510
....*....|....*....|....*....|....*.
gi 2335187 499 YTVWVGfnpDEFLanfsdihageLYFVDSDPLQDHN 534
Cdd:cd16034 376 YVRDKN---GPWL----------LFDNEKDPYQLNN 398
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-529 |
4.42e-56 |
|
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: 190.83 E-value: 4.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhAGNF 116
Cdd:cd16037 2 NILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPY---DGDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 STIPQYFKENGYVTMSVGKvfhpgissnhtddspyswsfppyhpssekyentktcrgpdgeLHANllcpvdVLDVPEGTL 196
Cdd:cd16037 79 PSWGHALRAAGYETVLIGK------------------------------------------LHFR------GEDQRHGFR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 197 PDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:cd16037 111 YDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY---------------------------------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 277 qalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATH 356
Cdd:cd16037 157 ----------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVR 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 357 VPLIFYVPGRtaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPvpsfhvelcreGK 436
Cdd:cd16037 221 VPMIISGPGI-------------------------PAGKRVKTPVSLVDLAPTILEAAGAPPPPDLD-----------GR 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 437 NLLkhfrfrDLEEDPYlpgnPRELIAYSQYprpsdipqwnsdkpSLKDIKIMGYSIRTIDYRYTVWVGFNPdeflanfsd 516
Cdd:cd16037 265 SLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP--------- 311
|
490
....*....|...
gi 2335187 517 ihagELYFVDSDP 529
Cdd:cd16037 312 ----QLFDLENDP 320
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
38-548 |
2.19e-54 |
|
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: 189.66 E-value: 2.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRvhAGNF 116
Cdd:cd16031 4 NIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLF--DASQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 STIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENtKTCRGPDGEL-HANLLCpvdvldvpegt 195
Cdd:cd16031 82 PTYPKLLRKAGYQTAFIGK-WHLGSGGDLPPPGFDYWVSFPGQGSYYDPEF-IENGKRVGQKgYVTDII----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 196 lpdkqsTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAP--DPEVPDGLPPVAYNPWMDIRQR 273
Cdd:cd16031 149 ------TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPEtfDDDDYAGRPEWAREQRNRIRGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 274 EDVQALNisvpygpiPVDFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGeWA-KYSNFD 352
Cdd:cd16031 222 LDGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFdKRLMYE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 353 VATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelc 432
Cdd:cd16031 292 ESIRVPLIIRDPRLI------------------------KAGTVVDALVLNIDFAPTILDLAGVPIPEDM---------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 433 rEGKNLLKHFRFRDleedpylPGNPRE--LIAYSQYPRPSDIPQWnsdkpslkdikimgYSIRTIDYRYTVWVGFNPDEf 510
Cdd:cd16031 338 -QGRSLLPLLEGEK-------PVDWRKefYYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYYGVWDEE- 394
|
490 500 510
....*....|....*....|....*....|....*...
gi 2335187 511 lanfsdihagELYFVDSDPLQDHNMYNDSQGGDLFQLL 548
Cdd:cd16031 395 ----------ELYDLKKDPLELNNLANDPEYAEVLKEL 422
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-440 |
2.57e-53 |
|
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: 185.08 E-value: 2.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQ----QAVCAPSRVSFLTGRrpdttrlydfnSYWRVH 112
Cdd:cd16155 4 NILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR-----------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 113 AGNFS-------TIPQYFKENGYVTMSVGKvfhpgissNHTDdspyswsfppyhpssekyentktcrgpdgelHANllcp 185
Cdd:cd16155 73 EGGKAaipsddkTWPETFKKAGYRTFATGK--------WHNG-------------------------------FAD---- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 186 vdvldvpegtlpdkqsteQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdPEVPDGLPPVAyN 265
Cdd:cd16155 110 ------------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL---PENFLPQHPFD-N 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 266 PWMDIRqreDVQalnisvpYGPIPVDFQ--RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHG 343
Cdd:cd16155 168 GEGTVR---DEQ-------LAPFPRTPEavRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 344 EWAKYSNFDVATHVPLIFYVPGrtasLPeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPRCp 423
Cdd:cd16155 238 LMGKQNLYEHSMRVPLIISGPG----IP---------------------KGKRRDALVYLQDVFPTLCELAGIEIPESV- 291
|
410
....*....|....*..
gi 2335187 424 vpsfhvelcrEGKNLLK 440
Cdd:cd16155 292 ----------EGKSLLP 298
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
38-420 |
5.29e-52 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 184.87 E-value: 5.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHAGN 115
Cdd:PRK13759 8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 116 FS-TIPQYFKENGYVTMSVGKV-FHPGIS----SNHTDDSPYSWSFPPYHPSseKYENTKTCR--------GPDGEL--- 178
Cdd:PRK13759 84 YKnTLPQEFRDAGYYTQCIGKMhVFPQRNllgfHNVLLHDGYLHSGRNEDKS--QFDFVSDYLawlrekapGKDPDLtdi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 179 ----HANLLCPvdvLDVPEGTLPDKQSTEQAIQLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPE 254
Cdd:PRK13759 162 gwdcNSWVARP---WDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 255 VPDglppvaynpWmDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSD 334
Cdd:PRK13759 235 IGD---------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 335 HGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEageklfpyldpfdsasqlmepGRQSMDLVELVSLFPTLAGLA 414
Cdd:PRK13759 305 HGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNR---------------------GTVIDQVVELRDIMPTLLDLA 363
|
....*.
gi 2335187 415 GLQVPP 420
Cdd:PRK13759 364 GGTIPD 369
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-421 |
2.66e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 173.89 E-value: 2.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 37 LNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPdttrlydfnSYWRVHAG- 114
Cdd:cd16148 1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP---------FYHGVWGGp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 115 ---NFSTIPQYFKENGYVTMSVGkvfhpgissnhtdDSPYSWSFPPYHPSSEKYENTktcRGPDGElhanllcpvdvlDV 191
Cdd:cd16148 72 lepDDPTLAEILRKAGYYTAAVS-------------SNPHLFGGPGFDRGFDTFEDF---RGQEGD------------PG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 192 PEGTLPDKQSTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapDpevpdglppvaynpwmdir 271
Cdd:cd16148 124 EEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-----------------D------------------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 272 qredvqalnisvpygpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAK-YSN 350
Cdd:cd16148 167 ------------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSN 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2335187 351 F-DVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPR 421
Cdd:cd16148 217 LyDEQLHVPLIIRWPGK-------------------------EPGKRVDALVSHIDIAPTLLDLLGVEPPDY 263
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-418 |
5.79e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 171.02 E-value: 5.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRP-SLGCYGDKL----------VRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFN 106
Cdd:cd16153 3 NILWIITDDQRVdSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 107 SYWRVHAGNFSTIPQYFKENGYVTMSVGKvfhpgissnhtddspyswsfppyhpssEKYENtktcrgpdgelhanllcPV 186
Cdd:cd16153 83 AAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA-----------------FQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 187 DVLDVPEgtlpdkQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdpevpdglppvaynp 266
Cdd:cd16153 119 RYLKNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 267 wmdiRQREDvqalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLAN---STIIAFTSDHGWALGEHG 343
Cdd:cd16153 165 ----RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQG 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2335187 344 EWAKYSNFDVATHVPLIFYVPGRtaslpeageKLFPyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:cd16153 217 ILAKFTFWPQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
37-466 |
1.43e-48 |
|
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: 171.22 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 37 LNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfnsywrvHAGN 115
Cdd:cd16032 1 PNILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYD-------NAAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 116 FS----TIPQYFKENGYVTMSVGKVfhpgissnHtddspyswsFPpyhpssekyentktcrGPDgELHanllcpvdvldv 191
Cdd:cd16032 74 FPadipTFAHYLRAAGYRTALSGKM--------H---------FV----------------GPD-QLH------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 192 peGTLPDKQSTEQAIQLLEKMKTSAS--PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdpevpdglppvaynpwmd 269
Cdd:cd16032 108 --GFDYDEEVAFKAVQKLYDLARGEDgrPFFLTVSFTHPHDPYVIPQEYWDLY--------------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 270 irqredvqalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYS 349
Cdd:cd16032 159 -----------------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMS 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 350 NFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSmDLVELVSLFPTLAGLAGLQVPPRCPVPsfhv 429
Cdd:cd16032 216 FFEGSARVPLIISAPGRFA------------------------PRRVA-EPVSLVDLLPTLVDLAGGGTAPHVPPL---- 266
|
410 420 430
....*....|....*....|....*....|....*..
gi 2335187 430 elcrEGKNLLKHFRFRDleedpylPGNPREliAYSQY 466
Cdd:cd16032 267 ----DGRSLLPLLEGGD-------SGGEDE--VISEY 290
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-420 |
8.05e-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: 171.57 E-value: 8.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16144 2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 S---------------TIPQYFKENGYVTMSVGKvFHPGISSNHT--------DDSPYSWSFPPYHPSSEKYENTKTCRG 173
Cdd:cd16144 82 KlipppsttrlpleevTIAEALKDAGYATAHFGK-WHLGGEGGYGpedqgfdvNIGGTGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 174 PDGElHanllcPVDVLdvpegtlpdkqsTEQAIQLLEkmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdP 253
Cdd:cd16144 161 PEGE-Y-----LTDRL------------TDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKY----------E 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 254 EVPDGLPPVAYNPwmdirqredvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTS 333
Cdd:cd16144 211 KKKKGLRKGQKNP--------------------------------VYAAMIESLDESVGRILDALEELGLADNTLVIFTS 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 334 DHGwALGEHGEWA---------KYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELV 404
Cdd:cd16144 259 DNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIK------------------------PGSVSDVPVIGT 313
|
410
....*....|....*.
gi 2335187 405 SLFPTLAGLAGLQVPP 420
Cdd:cd16144 314 DLYPTFLELAGGPLPP 329
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-540 |
8.65e-48 |
|
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: 171.65 E-value: 8.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16150 2 NIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 StipQYFKENGYVTMSVGKvfhpgissNHTDDSPYSWsfppyhpssEKYEntktcrgpdgelhanllcpvdvldvpegtL 196
Cdd:cd16150 82 L---KTLKDAGYHVAWAGK--------NDDLPGEFAA---------EAYC-----------------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 197 PDKQSTEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPdPEVPDGLPpvAYNPWMDIRQREDv 276
Cdd:cd16150 113 SDEACVRTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLR--AKGKPSMLEGIEK- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 277 QALNisvpygPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSN-F-DVA 354
Cdd:cd16150 185 QGLD------RWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 355 THVPLIFYVPGRTaslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvPSFhvelcre 434
Cdd:cd16150 259 TRVPLIIKPPGGP-------------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THF------- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 435 GKNLLKHFRFRDLEEDPY-------LPGNPReliAYSQYPRPSDIPQWNS---DKPSLKDIKIMgysIRTIDYRYtVWVG 504
Cdd:cd16150 303 GRSLLPVLAGETEEHRDAvfseggrLHGEEQ---AMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VYRL 375
|
490 500 510
....*....|....*....|....*....|....*.
gi 2335187 505 FNPDeflanfsdihagELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16150 376 YEPD------------ELYDLEADPLELHNLIGDPA 399
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
38-469 |
4.04e-47 |
|
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: 170.52 E-value: 4.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFN--SYWR---V 111
Cdd:cd16028 2 NVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR-------YLMNhrSVWNgtpL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 112 HAGnFSTIPQYFKENGYVTMSVGKvfhpgissnhTDDSPYSWSFPPYHPSSEKYENtktcrgpdgelhanLLCPVDVLDV 191
Cdd:cd16028 75 DAR-HLTLALELRKAGYDPALFGY----------TDTSPDPRGLAPLDPRLLSYEL--------------AMPGFDPVDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 192 PEGtLPDKQS-----TEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDPEVPDGLPPVa 263
Cdd:cd16028 130 LDE-YPAEDSdtaflTDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQHPL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 264 YNPWMDIRQREDVQALNISVPYGPIPVdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHG 343
Cdd:cd16028 206 LAAFLERIESLSFSPGAANAADLDDEE--VAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHW 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 344 EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfDSASqlmepGRQSMDLVELVSLFPTLAGLAGLQVPPRCp 423
Cdd:cd16028 284 LWGKDGFFDQAYRVPLIVRDPRREA----------------DATR-----GQVVDAFTESVDVMPTILDWLGGEIPHQC- 341
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2335187 424 vpsfhvelcrEGKNLLKHfrfrdLEEDPylPGNPRELIAYSQYPRP 469
Cdd:cd16028 342 ----------DGRSLLPL-----LAGAQ--PSDWRDAVHYEYDFRD 370
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-419 |
2.69e-42 |
|
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: 156.18 E-value: 2.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16026 3 NIVVILADDLGYGdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 115 -NFSTIPQYFKENGYVTMSVGKvFHPGISSNH--TD---DS----PYS---WSFPPYHPSSEKYEntktcrgpdgelhAN 181
Cdd:cd16026 83 pDEITIAEVLKKAGYRTALVGK-WHLGHQPEFlpTRhgfDEyfgiPYSndmWPFPLYRNDPPGPL-------------PP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 182 LLCPVDVLDVPegtlPD-----KQSTEQAIQLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFqklyplENITLApdpevp 256
Cdd:cd16026 149 LMENEEVIEQP----ADqssltQRYTDEAVDFIERNKD--QPFFLYLAHTMPHVPLFASEKF------KGRSGA------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 257 dGLppvaynpwmdirqredvqalnisvpYGpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16026 211 -GL-------------------------YG---------------DVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 337 WALGEHGEW--------AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFP 408
Cdd:cd16026 250 PWLEYGGHGgsagplrgGKGTTWEGGVRVPFIAWWPGV------------------------IPAGTVSDELASTMDLLP 305
|
410
....*....|.
gi 2335187 409 TLAGLAGLQVP 419
Cdd:cd16026 306 TLAALAGAPLP 316
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-427 |
2.49e-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: 149.31 E-value: 2.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRV----- 111
Cdd:cd16149 2 NILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHgktkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 112 ---HAGNFSTIPQYFKENGYVTMSVGKvFHPGissnhtddspyswsfppyhpssekyentktcrgpdgelhanllcpvdv 188
Cdd:cd16149 82 pegYLEGQTTLPEVLQDAGYRCGLSGK-WHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 189 ldvpegtlpdkqstEQAIQLLEKMKTSASPFFLAVGYHKPHipfrypkefqklyplenitlapdpevpdglppvayNPWm 268
Cdd:cd16149 113 --------------DDAADFLRRRAEAEKPFFLSVNYTAPH-----------------------------------SPW- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 269 dirqredvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAK- 347
Cdd:cd16149 143 ------------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKg 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 348 -----YSNFDVATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVP--P 420
Cdd:cd16149 193 ngtfpLNMYDNSVKVPFIIRWPGVV------------------------PAGRVVDSLVSAYDFFPTLLELAGVDPPadP 248
|
....*..
gi 2335187 421 RCPVPSF 427
Cdd:cd16149 249 RLPGRSF 255
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
38-534 |
7.95e-40 |
|
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: 149.62 E-value: 7.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNaFAQQAVCAPSRVSFLTGRRPDTTRLydfnsyWRVHAG-- 114
Cdd:cd16146 2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGV------WHTILGre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 115 ----NFSTIPQYFKENGYVTMSVGKvFHPGissnhtDDSPY----------------SWSFPPYHPSSEKYENTKTCRGP 174
Cdd:cd16146 75 rmrlDETTLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 175 ----DGelhanlLCPvDVLdvpegtlpdkqsTEQAIQLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFQKLYplenitla 250
Cdd:cd16146 148 fvktEG------YCT-DVF------------FDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPY-------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 251 PDPEVPDGlppvaynpwmdirqredvqalnisvpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIA 330
Cdd:cd16146 199 KDMGLDDK--------------------------------------LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 331 FTSDHGWALGEHGEW------AKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELV 404
Cdd:cd16146 241 FMSDNGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKIL------------------------AGKDVDTLTAHI 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 405 SLFPTLAGLAGLQVPPrcpvpsfHVELcrEGKNLLKhfrfrdLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSdkpslkd 484
Cdd:cd16146 297 DLLPTLLDLCGVKLPE-------GIKL--DGRSLLP------LLKGESDPWPERTLFTHSGRWPPPPKKKRNA------- 354
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2335187 485 ikimgySIRTIDYRYTVWVGFNPdeflanfsdihagELYFVDSDPLQDHN 534
Cdd:cd16146 355 ------AVRTGRWRLVSPKGFQP-------------ELYDIENDPGEEND 385
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-421 |
2.99e-39 |
|
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: 148.13 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY---WRVHA 113
Cdd:cd16145 2 NIIFILADDLGYGdLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPggqDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 114 GNfSTIPQYFKENGYVTMSVGKVfhpGISSNHTDDSPYS----------------WSFPPYhpsseKYENTKTcrgpdgE 177
Cdd:cd16145 82 DD-VTLAEVLKKAGYATAAFGKW---GLGGPGTPGHPTKqgfdyfygyldqvhahNYYPEY-----LWRNGEK------V 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 178 LHANLLCPVDVLDVPEGTLPDKQS----TEQAIQLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDP 253
Cdd:cd16145 147 PLPNNVIPPLDEGNNAGGGGGTYShdlfTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 254 EVPDGLPPVAYNPWMDIRQRedvqalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTS 333
Cdd:cd16145 213 YKPKDPGIYAYLPWPQPEKA--------------------------YAAMVTRLDRDVGRILALLKELGIDENTLVVFTS 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 334 DHGwALGEHGEWAKYSNFDVA--------------THVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMD 399
Cdd:cd16145 267 DNG-PHSEGGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPGKI------------------------PAGSVSDH 321
|
410 420
....*....|....*....|..
gi 2335187 400 LVELVSLFPTLAGLAGLQVPPR 421
Cdd:cd16145 322 PSAFWDFMPTLADLAGAEPPED 343
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
38-416 |
5.04e-37 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 139.09 E-value: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVhAGNF 116
Cdd:pfam00884 2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYV-STPVGL-PRTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 STIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelhanllcpvdvldvPEGTL 196
Cdd:pfam00884 80 PSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------SGGGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 197 PDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:pfam00884 143 SDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA--------------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 277 qalnISVPYGpipvDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVA-- 354
Cdd:pfam00884 187 ----TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApe 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2335187 355 --THVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGL 416
Cdd:pfam00884 259 ggYRVPLLIWSPGGKA------------------------KGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-534 |
7.77e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 137.73 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAqQAVCAPSRVSFLTGRRPDTTrlYDFNSYWrvHAGNf 116
Cdd:cd16151 2 NIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRN--YVVFGYL--DPKQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 STIPQYFKENGYVTMSVGKvfhPGISSNhTDDSPYS-------WSFPPYHPSSEKYENTKTcrgPDGELHANllcpVDVL 189
Cdd:cd16151 76 KTFGHLLKDAGYATAIAGK---WQLGGG-RGDGDYPhefgfdeYCLWQLTETGEKYSRPAT---PTFNIRNG----KLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 190 DVPEGTLPDkQSTEQAIQLLEKMKtsASPFFLavgY------HKPHIPFrypkefqklyplenitlaPDPEvpdglppva 263
Cdd:cd16151 145 TTEGDYGPD-LFADFLIDFIERNK--DQPFFA---YypmvlvHDPFVPT------------------PDSP--------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 264 ynPWMDIRQRedvqalnisvpygpipvdfqRKIRQSYF-ASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEH 342
Cdd:cd16151 192 --DWDPDDKR--------------------KKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPIT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 343 GEW-------AKYSNFDVATHVPLIFYVPGrtaslpeageklfpyldpfdsasqLMEPGRQSMDLVELVSLFPTLAGLAG 415
Cdd:cd16151 250 SRTngrevrgGKGKTTDAGTHVPLIVNWPG------------------------LIPAGGVSDDLVDFSDFLPTLAELAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 416 LQVPPRCPVpsfhvelcrEGKNLLkhfrfrdleedPYL---PGNPRELIAYsqyprpsdipqWNSDKPSLKDIKimgYSI 492
Cdd:cd16151 306 APLPEDYPL---------DGRSFA-----------PQLlgkTGSPRREWIY-----------WYYRNPHKKFGS---RFV 351
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2335187 493 RTIDYRYtvwvgfnpdeflanFSDihaGELYFVDSDPLQDHN 534
Cdd:cd16151 352 RTKRYKL--------------YAD---GRFFDLREDPLEKNP 376
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-536 |
1.16e-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: 131.94 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRP-SLGCYGDK-LVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFNSY--WRVhA 113
Cdd:cd16143 2 NIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGR-------YPWRSRlkGGV-L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 114 GNFS---------TIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelHANLLC 184
Cdd:cd16143 74 GGFSppliepdrvTLAKMLKQAGYRTAMVGK-WHLGLDWKKKDGKKAATGTGKDVDYSKPIKGGPLDHGFD---YYFGIP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 185 PVDVLDvpegTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapdpevpdglppvay 264
Cdd:cd16143 150 ASEVLP----TL-----TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQG------------------------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 265 npwmdirqredVQALNisvPYGpipvDFqrkIRQsyfasvsyLDTQVGRLLSALDDLQLANSTIIAFTSDHG-------W 337
Cdd:cd16143 197 -----------KSGAG---PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyK 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 338 ALGEHGEWA-------KYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTL 410
Cdd:cd16143 248 ELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKIP------------------------AGSVSDQLVSLTDLFATL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 411 AGLAGLQVPPRCPVPSFhvelcregkNLLkhfrfrdleedPYLPGNPreliaySQYPRPSDIPQWNSDkpslkdikimGY 490
Cdd:cd16143 304 AAIVGQKLPDNAAEDSF---------SFL-----------PALLGPK------KQEVRESLVHHSGNG----------SF 347
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2335187 491 SIRTIDYRYTVWVGF--NPDEFLANFSDIHAGELYFVDSDPLQDHNMY 536
Cdd:cd16143 348 AIRKGDWKLIDGTGSggFSYPRGKEKLGLPPGQLYNLSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
38-452 |
2.94e-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: 132.12 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTtrlydfNSYWR---VHA 113
Cdd:cd16156 2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT------NGSWTncmALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 114 GNFSTIPQYFKENGYVTMSVGK-------VFHPGISSNHTDdSPYSWSFPPYHPSSEKYENTKTCRGPDgELHANllcpv 186
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKwhldggdYFGNGICPQGWD-PDYWYDMRNYLDELTEEERRKSRRGLT-SLEAE----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 187 dvlDVPEGTLPDKQSTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplENITLAPDPEVPDGLP--PVAY 264
Cdd:cd16156 149 ---GIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLHQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 265 NPWMDIRQREDVQALNISVPYgpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLqLANSTIIaFTSDHGWALGEHGE 344
Cdd:cd16156 222 RLWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI-AEDAWVI-YTSDHGDMLGAHKL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 345 WAK-YSNFDVATHVPLIFYVPGrtaslpeaGEKLFPYLD-PfdsasqlmepgrqsmdlVELVSLFPTLAGLAGLQVPPRC 422
Cdd:cd16156 286 WAKgPAVYDEITNIPLIIRGKG--------GEKAGTVTDtP-----------------VSHIDLAPTILDYAGIPQPKVL 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2335187 423 P----VPSFHVELCREGK----------------------------------NLLKHFRFRDLEEDPY 452
Cdd:cd16156 341 EgesiLATIEDPEIPENRgvfvefgryevdhdgfggfqpvrcvvdgryklviNLLSTDELYDLEKDPY 408
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-539 |
9.59e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 128.89 E-value: 9.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHAGNF 116
Cdd:cd16152 3 NVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFR-NG--IPLPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 STIPQYFKENGYVTMSVGKvfhpgissnhtddspysWSFPPYHpssekyentktcrgpdgelhanllcpVDVLdvpegtl 196
Cdd:cd16152 80 KTLAHYFRDAGYETGYVGK-----------------WHLAGYR--------------------------VDAL------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 197 pdkqsTEQAIQLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYplenitlaPDPEVPdglppvaynpwmdir 271
Cdd:cd16152 110 -----TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERF--------ANFWVP--------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 272 qrEDVQALnisvpygpiPVDFQRKIrQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHgwalGEH-----GEWa 346
Cdd:cd16152 161 --PDLAAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 347 KYSNFDVATHVPLIFYVPGrtaslpeageklfpyldpFDSasqlmepGRQSMDLVELVSLFPTLAGLAGLQVPprcpvPS 426
Cdd:cd16152 224 KRSCHESSIRVPLVIYGPG------------------FNG-------GGRVEELVSLIDLPPTLLDAAGIDVP-----EE 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 427 FHvelcreGKNLLkhfrfrdleedpylpgnprELIAYSQYPRPSDIPqwnsdkpslkdIKI----MGYSIRTIDYRYTVw 502
Cdd:cd16152 274 MQ------GRSLL-------------------PLVDGKVEDWRNEVF-----------IQIsesqVGRAIRTDRWKYSV- 316
|
490 500 510
....*....|....*....|....*....|....*...
gi 2335187 503 VGFNPDEFLANFSDIHAGE-LYFVDSDPLQDHNMYNDS 539
Cdd:cd16152 317 AAPDKDGWKDSGSDVYVEDyLYDLEADPYELVNLIGRP 354
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
38-424 |
1.00e-32 |
|
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: 129.21 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQaVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16029 2 HIVFILADDLGWNdVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILAGEPYGlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 115 -NFSTIPQYFKENGYVTMSVGKvFHPGISS-NHTD-----DSPYSwsfppYHPSSEKYENTKTCRGPDgelhanllCPVD 187
Cdd:cd16029 81 lNETLLPQYLKELGYATHLVGK-WHLGFYTwEYTPtnrgfDSFYG-----YYGGAEDYYTHTSGGAND--------YGND 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 188 VLDVPEGTLPDKQS-------TEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglp 260
Cdd:cd16029 147 DLRDNEEPAWDYNGtystdlfTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE----------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 261 pvaynpwmdirqredVQALNISvpygpipvDFQRKIrqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGwALG 340
Cdd:cd16029 209 ---------------DKFAHIK--------DEDRRT---YAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG-GPT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 341 EHGEWAkySNFdvathvPLifyvPGRTASLPEAGEKlfpyLDPFDSASQL-MEPGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16029 262 GGGDGG--SNY------PL----RGGKNTLWEGGVR----VPAFVWSPLLpPKRGTVSDGLMHVTDWLPTLLSLAGGDPD 325
|
....*
gi 2335187 420 PRCPV 424
Cdd:cd16029 326 DLPPL 330
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
38-452 |
3.21e-31 |
|
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: 124.97 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPSLGCYGD--KLVRspnidQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPD----TTRLYDFNSYWRV 111
Cdd:cd16147 3 NIVLILTDDQDVELGSMDPmpKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHnhgvTNNSPPGGGYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 112 HAGNF--STIPQYFKENGYVTMSVGKVFHpGISSNHTDDSP---YSWSFPPYHPSseKYENTKTCRGPDGELHANllCPV 186
Cdd:cd16147 78 WQNGLerSTLPVWLQEAGYRTAYAGKYLN-GYGVPGGVSYVppgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVS--YPG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 187 ----DVLdvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAP-----DPEVPD 257
Cdd:cd16147 153 dyltDVI------------ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPrpppnNPDVSD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 258 G--------LPPVAYNPWMDIRQREDVQALnisvpygpipvdfqrkirqsyfASVsylDTQVGRLLSALDDLQLANSTII 329
Cdd:cd16147 219 KphwlrrlpPLNPTQIAYIDELYRKRLRTL----------------------QSV---DDLVERLVNTLEATGQLDNTYI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 330 AFTSDHGWALGEHG-EWAKYSNFDVATHVPLIFYVPGrtasLPeageklfpyldpfdsasqlmePGRQSMDLVELVSLFP 408
Cdd:cd16147 274 IYTSDNGYHLGQHRlPPGKRTPYEEDIRVPLLVRGPG----IP---------------------AGVTVDQLVSNIDLAP 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2335187 409 TLAGLAGLQVPP--------RCPVPSFH-VELCREGKNLLKHF---RFR---DLEEDPY 452
Cdd:cd16147 329 TILDLAGAPPPSdmdgrscgDSNNNTYKcVRTVDDTYNLLYFEwctGFRelyDLTTDPY 387
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-420 |
5.86e-31 |
|
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: 123.80 E-value: 5.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVR---SPNIDQLASHSLLFQNAFAQQAvCAPSRVSFLTGRRPDTTRLYdfnsywRV-- 111
Cdd:cd16142 2 NILVILGDDIGWGdLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLT------TVgl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 112 -HAGNF-----STIPQYFKENGYVTMSVGKvfhpgissNHTDDSPYSWsfPpyhpssekyentkTCRGPDgELHANLLcp 185
Cdd:cd16142 75 pGSPGGlppwePTLAELLKDAGYATAQFGK--------WHLGDEDGRL--P-------------TDHGFD-EFYGNLY-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 186 vdvldvpegTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvAYN 265
Cdd:cd16142 129 ---------HTIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS-------------------GKG 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 266 PWMDirqredvqalnisvpygpipvdfqrkirqsyfaSVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG-----WALG 340
Cdd:cd16142 181 KYAD---------------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 341 EHGEW--AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:cd16142 228 GYTPFrgEKGTTWEGGVRVPAIVRWPGK------------------------IKPGRVSNEIVSHLDWFPTLAALAGAPD 283
|
..
gi 2335187 419 PP 420
Cdd:cd16142 284 PK 285
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
38-419 |
7.41e-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: 7.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDkLVRSPNIDQLASHSLLFQNaFAQQAVCAPSRVSFLTGRRP-------DTTRLYDFNSYW 109
Cdd:cd16025 4 NILLILADDLGFSdLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHhqvgmgtMAELATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 110 RVHAGNFSTIPQYFKENGYVTMSVGKvfhpgissnhtddspysW--SFPPYHpSSEKYentktcrgpdgelhanllcpvd 187
Cdd:cd16025 82 GYLPDSAATIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL---------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 188 vldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LY 242
Cdd:cd16025 122 --------------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 243 PlENITLAP-DPEVPdglppvaynPWMDIRQRE-DVQALNISVpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDD 320
Cdd:cd16025 188 P-ADTKLTPrPPGVP---------AWDSLSPEEkKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 321 LQLANSTIIAFTSDHGwALGEHGeWAKYSN-----FDVATH-----VPLIfyvpgrtASLPEAGEKlfpyldpfdsasql 390
Cdd:cd16025 242 LGELDNTLIIFLSDNG-ASAEPG-WANASNtpfrlYKQASHeggirTPLI-------VSWPKGIKA-------------- 298
|
410 420
....*....|....*....|....*....
gi 2335187 391 mePGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16025 299 --KGGIRHQFAHVIDIAPTILELAGVEYP 325
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-416 |
1.30e-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: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYD-FNSYWRVHAGN 115
Cdd:cd16035 2 NILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLLSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 116 -FSTIPQYFKENGYVTMSVGKvfhpgissnhtddspysWsfppyHPSSekyentktcrgpdgelHANllcpvdvldvpEG 194
Cdd:cd16035 82 dVPTLGHMLRAAGYYTAYKGK-----------------W-----HLSG----------------AAG-----------GG 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 195 TLPDKQSTEQAIQLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdpevpdglppvaynpwmdir 271
Cdd:cd16035 113 YKRDPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH------------------------------------------ 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 272 qreDVQalnisvpYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSN- 350
Cdd:cd16035 151 ---DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNa 220
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2335187 351 FDVATHVPLIFYVPGrtaslpeagekLFPyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGL 416
Cdd:cd16035 221 YEEALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGV 262
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
38-420 |
2.99e-24 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 104.55 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPSLGCY-GDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRlyDFNSYWRVHAgNF 116
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE--SWNNYKGLDP-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 STIPQYFKENGYVTMSVGKVFHpgiSSNHtddspyswsfppyHPSSEKYE----NTKTCRGPDGELHANLLCPVDVLDVp 192
Cdd:cd16171 79 PTWMDRLEKHGYHTQKYGKLDY---TSGH-------------HSVSNRVEawtrDVPFLLRQEGRPTVNLVGDRSTVRV- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 193 egTLPDKQSTEQAIQLLEKMKTSAS-PFFLAVGYHKPHiPFRYPkefqklypleniTLAPDpevpdglppvaynpwmdir 271
Cdd:cd16171 142 --MLKDWQNTDKAVHWIRKEAPNLTqPFALYLGLNLPH-PYPSP------------SMGEN------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 272 qredvqalnisvpYGPIpvdfqRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNF 351
Cdd:cd16171 188 -------------FGSI-----RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMY 249
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2335187 352 DVATHVPLIFYVPGrtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 420
Cdd:cd16171 250 EGSSHVPLLIMGPG-------------------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
38-419 |
6.55e-22 |
|
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: 99.28 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYwRV----- 111
Cdd:cd16159 3 NIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGM-RVilfta 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 112 -HAG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHTDDSpyswsfpPYHPSSEKYE--------NTKTCRGPDGElh 179
Cdd:cd16159 82 sSGGlppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDF-------CHHPLNHGFDyfyglpltNLKDCGDGSNG-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 180 ANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKL--------------YPLE 245
Cdd:cd16159 152 EYDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRYFncilmrnhevveqpMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 246 NITLAPDPEVPDGL------PPVAYNPWmdirqredvqaLNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALD 319
Cdd:cd16159 232 NLTQRLTKEAISFLernkerPFLLVMSF-----------LHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 320 DLQLANSTIIAFTSDHGWAL------GEHGEW-------AKYSNFDVATHVPLIFYVPGRtasLPeageklfpyldpfdS 386
Cdd:cd16159 301 ELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGV---IP--------------P 363
|
410 420 430
....*....|....*....|....*....|...
gi 2335187 387 ASQLMEPGRQsMDlvelvsLFPTLAGLAGLQVP 419
Cdd:cd16159 364 GSVIDEPTSL-MD------IFPTVAALAGAPLP 389
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
38-420 |
1.23e-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: 90.99 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVR-SPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVHAG- 114
Cdd:cd16161 3 NFLLLFADDLGwGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH-NFLPTSVGGl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 115 --NFSTIPQYFKENGYVTMSVGKvFHPGissnHTDdspyswsfpPYHPSSekyentktcRGPDgelhanllcpvDVLDVP 192
Cdd:cd16161 82 plNETTLAEVLRQAGYATGMIGK-WHLG----QRE---------AYLPNS---------RGFD-----------YYFGIP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 193 ---EGTLPDKQStEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdpevpdglppvaynpwmd 269
Cdd:cd16161 128 fshDSSLADRYA-QFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQ------------------------------ 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 270 irqredvQALNISVPYGpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG-WALG-------E 341
Cdd:cd16161 177 -------SPTSGRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 342 HGEW--------AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGL 413
Cdd:cd16161 235 TGDWqgnlggsvAKASTWEGGHREPAIVYWPGR------------------------IPANSTSAALVSTLDIFPTVVAL 290
|
....*..
gi 2335187 414 AGLQVPP 420
Cdd:cd16161 291 AGASLPP 297
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
38-419 |
2.77e-19 |
|
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: 90.97 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16158 3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 115 -NFSTIPQYFKENGYVTMSVGKvFHPGISSN-----------HTDDSPYSWSFPPYHPSSEKYENTK---TCRgpDGELH 179
Cdd:cd16158 83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNgtylpthqgfdHYLGIPYSHDQGPCQNLTCFPPNIPcfgGCD--QGEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 180 ANLLCPVDVLDVPeGTLPD--KQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdpevpd 257
Cdd:cd16158 160 CPLFYNESIVQQP-VDLLTleERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFA------------------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 258 glppvaynpwmdirqredvqalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGW 337
Cdd:cd16158 221 -----------------------------------GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 338 AL------GEHG--EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRqSMDLVELVSLFPT 409
Cdd:cd16158 266 STmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPGRIK------------------------PGV-THELASTLDILPT 320
|
410
....*....|
gi 2335187 410 LAGLAGLQVP 419
Cdd:cd16158 321 IAKLAGAPLP 330
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-419 |
8.11e-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: 89.06 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSywrvHAGNF 116
Cdd:cd16157 3 NIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA----HARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 117 ST--------------IPQYFKENGYVTMSVGK-------VFHPgisSNHTDD----SPySWSFPPY----HPSSEKYEN 167
Cdd:cd16157 79 YTpqnivggipdseilLPELLKKAGYRNKIVGKwhlghrpQYHP---LKHGFDewfgAP-NCHFGPYdnkaYPNIPVYRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 168 TKTCrgpdGELHANLlcPVDvLDVPEGTLpDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPfrypkefqkLYpleni 247
Cdd:cd16157 155 WEMI----GRYYEEF--KID-KKTGESNL-TQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAP---------VY----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 248 tlapdpevpdglppvAYNPWMDIRQREdvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANST 327
Cdd:cd16157 213 ---------------ASKPFLGTSQRG------------------------LYGDAVMELDSSVGKILESLKSLGIENNT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 328 IIAFTSDHGWAL-------GEHGEW--AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSM 398
Cdd:cd16157 254 FVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGH------------------------IKPGQVSH 309
|
410 420
....*....|....*....|.
gi 2335187 399 DLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16157 310 QLGSLMDLFTTSLALAGLPIP 330
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-419 |
1.28e-17 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 84.71 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDL-RPSLGCY--GDKLVRSPNIDQLASHSLLFQNAFAqQAVCAPSRVSFLTGRrpdttrlYDFN----SYWR 110
Cdd:cd16154 2 NILLIIADDQgLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGK-------YGFRtgvlAVPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 111 VHAGNFSTIPQYFKEN----GYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPS--SEKYENTKTCRGPDGELHanllc 184
Cdd:cd16154 74 ELLLSEETLLQLLIKDattaGYSSAVIGK-WHLGGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 185 pvdvldvpegTLPDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDpevpdgLPPV 262
Cdd:cd16154 148 ----------EYATTKLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGD------SADI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 263 AYNPwmdirqredvqalnisvpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIaFTSDHG------ 336
Cdd:cd16154 202 EANP------------------------------RPYYLAAIEAMDTEIGRLLASIDEEERENTIII-FIGDNGtpgqvv 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 337 --WALGEHgewAKYSNFDVATHVPLIFyvpgrtaslpeageklfpyldpfdSASQLMEPGRQSMDLVELVSLFPTLAGLA 414
Cdd:cd16154 251 dlPYTRNH---AKGSLYEGGINVPLIV------------------------SGAGVERANERESALVNATDLYATIAELA 303
|
....*
gi 2335187 415 GLQVP 419
Cdd:cd16154 304 GVDAA 308
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
38-419 |
4.98e-17 |
|
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: 83.63 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRpslgcYGDKLV-------RSPnIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY--DFNSY 108
Cdd:cd16160 3 NIVLFFADDMG-----YGDLASyghptqeRGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 109 WRVHAG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYswsFPPYH---------PssekYENTKTCrgPDG 176
Cdd:cd16160 77 PWDIGGlpkTEVTMAEALKEAGYTTGMVGK-WHLGINENNHSDGAH---LPSHHgfdfvgtnlP----FTNSWAC--DDT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 177 ELHanllcpVDVLDVPEGTLPDK-QSTEQAIQ---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyp 243
Cdd:cd16160 147 GRH------VDFPDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 244 lenitlapdpevpdglppvaynpwmdirqredvqalNISVpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQL 323
Cdd:cd16160 217 ------------------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 324 ANSTIIAFTSDHGWAL---GEHGEWA-----KYSNFDVATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmePGR 395
Cdd:cd16160 248 DQNTLVFFLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTI-------------------------KPR 302
|
410 420
....*....|....*....|....
gi 2335187 396 QSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16160 303 VSHEVVSTMDIFPTFVDLAGGTLP 326
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
26-439 |
4.99e-17 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 84.32 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 26 SETQANSTTDALNVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGrrpdttrLYD 104
Cdd:COG1368 224 PTPNPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-------LPP 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 105 FNS---YWRVHAGNFSTIPQYFKENGYVTMsvgkVFHPGissnhtddSPYSWSFPPYHP--------SSEKYENTKTcrG 173
Cdd:COG1368 297 LPGgspYKRPGQNNFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYKnlgfdefyDREDFDDPFD--G 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 174 PDGelhanllcpvdvldvpegtLPDKQSTEQAIQLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITL 249
Cdd:COG1368 363 GWG-------------------VSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 250 apdpevpdglppvaynpwmdirqredvqalnisvpygpipvdfqrkirQSYFASVSYLDTQVGRLLSALDDLQLANSTII 329
Cdd:COG1368 417 ------------------------------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIF 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 330 AFTSDHGwalGEHGEWAKYSNFDVATHVPLIFYVPGRTAslPEAGEKLfpyldpfdsASQlmepgrqsMDlvelvsLFPT 409
Cdd:COG1368 449 VIYGDHG---PRSPGKTDYENPLERYRVPLLIYSPGLKK--PKVIDTV---------GSQ--------ID------IAPT 500
|
410 420 430
....*....|....*....|....*....|
gi 2335187 410 LAGLAGLQVPPRcpvPSFhvelcreGKNLL 439
Cdd:COG1368 501 LLDLLGIDYPSY---YAF-------GRDLL 520
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
38-415 |
4.67e-15 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 75.80 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVC--APSRVSFLTGRRPDTTRLYDFNSYwrvHAG 114
Cdd:cd16015 2 NVIVILLESFsDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPPLPLGSGSYTLY---KLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 115 NFSTIPQYFKENGYVTMSvgkvFHPGissnhtddSPYSWSFPPYHP--------SSEKYENTKTCRGPDGelhanllcpv 186
Cdd:cd16015 79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPnlgfdefyDLEDFPDDEKETNGWG---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 187 dvldvpegtLPDKQSTEQAIQLLEKMKtsASPFFLAV----GyhkpHIPFRYPKEFQKLyplenitlapdpevpdglppv 262
Cdd:cd16015 137 ---------VSDESLFDQALEELEELK--KKPFFIFLvtmsN----HGPYDLPEEKKDE--------------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 263 aynpwmdirqredvqalnisvpygPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEH 342
Cdd:cd16015 181 ------------------------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2335187 343 GEWAKYSNFDvATHVPLIFYVPGrtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAG 415
Cdd:cd16015 237 YDETDEDPLD-LYRTPLLIYSPG-------------------------LKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
38-414 |
7.16e-14 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 71.30 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQnAFAQQAVC--APSRVSFLTGRRPDttrlydfnsywrvhag 114
Cdd:cd00016 2 HVVLIVLDGLGADdLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTssAPNHAALLTGAYPT---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 115 nfstipqyfkENGYVTMSVGKVFHPGISSNHTDDSPyswSFPpyhpssekyentktcrgpdgelhanllcpvdvldvpeG 194
Cdd:cd00016 65 ----------LHGYTGNGSADPELPSRAAGKDEDGP---TIP-------------------------------------E 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 195 TLPDKQSTEQAIQLLE--KMKTSASPFFLAVGYHKPHIPFRypkefqklyplenitlAPDPEVPdglppvaynpwmdirq 272
Cdd:cd00016 95 LLKQAGYRTGVIGLLKaiDETSKEKPFVLFLHFDGPDGPGH----------------AYGPNTP---------------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 273 redvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYS--- 349
Cdd:cd00016 143 --------------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgka 196
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2335187 350 -NFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmepGRQSMDLVELVSLFPTLAGLA 414
Cdd:cd00016 197 dKSHTGMRVPFIAYGPGVKK-------------------------GGVKHELISQYDIAPTLADLL 237
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
302-365 |
2.26e-06 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 49.12 E-value: 2.26e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2335187 302 ASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWA-LGEHGewakYSNFDVATHVPLIFYVPG 365
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
38-417 |
4.76e-05 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 45.31 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAqqavCAPS-RVS---FLTGR-RPDTTRLYDFNSywrv 111
Cdd:cd16017 4 NVVLVIGESARRDhMSLYGYPRDTTPFLSKLKKNLIVFDNVIS----CGTStAVSlpcMLSFAnRENYDRAYYQEN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 112 hagnfstIPQYFKENGYvtmsvgKVF----HPGISSNHTDDSPYSWSFppYHPSSEKYENTKTCrgPDGELhanllcpvd 187
Cdd:cd16017 76 -------LIDLAKKAGY------KTYwisnQGGCGGYDTRISAIAKIE--TVFTNKGSCNSSNC--YDEAL--------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 188 vldvpegtLPdkqsteqaiQLLEKMKTSASPFFLAV---GyhkPHIPF--RYPKEFQKLYPlenitlapdpevpdglppv 262
Cdd:cd16017 130 --------LP---------LLDEALADSSKKKLIVLhlmG---SHGPYydRYPEEFAKFTP------------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 263 aynpwmdirqredvqalnisVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQlaNSTIIAFTSDHGWALGEH 342
Cdd:cd16017 171 --------------------DCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGEN 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2335187 343 GEW--AKYSNFDVATHVPLIFYVPGRTASLPEAGEKLFPYLDPFdsasqlmepgrqSMDLvelvsLFPTLAGLAGLQ 417
Cdd:cd16017 229 GLYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPF------------SHDN-----LFHTLLGLLGIK 288
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-336 |
2.03e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 43.58 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 13 LGLVLSSVCVALGSETQANSttdalNVLLIIVDDLRPslgcygDKLVR--SPNIDQLASHSLLFQNAfaqQAVC----AP 86
Cdd:COG1524 5 LSLLLASLLAAAAAAAPPAK-----KVVLILVDGLRA------DLLERahAPNLAALAARGVYARPL---TSVFpsttAP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 87 SRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS------------------TIPQYFKENGyvtMSVGKVFHPGissnhTDD 148
Cdd:COG1524 71 AHTTLLTGLYPGEHGIVGNGWYDPELGRVVNslswvedgfgsnsllpvpTIFERARAAG---LTTAAVFWPS-----FEG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 149 SPYSWSFPPYHPSSEKYentktcrgpdgelhanllcpvdVLDVPEGtlpDKQSTEQAIQLLEKmktsaspfflavgyHKP 228
Cdd:COG1524 143 SGLIDAARPYPYDGRKP----------------------LLGNPAA---DRWIAAAALELLRE--------------GRP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 229 HIpfrypkefqkLYplenitlapdpevpdglppvAYNPWMD-IRQRedvqalnisvpYGPipvdfqrkirQS--YFASVS 305
Cdd:COG1524 184 DL----------LL--------------------VYLPDLDyAGHR-----------YGP----------DSpeYRAALR 212
|
330 340 350
....*....|....*....|....*....|.
gi 2335187 306 YLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:COG1524 213 EVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
306-419 |
2.66e-03 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 39.86 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335187 306 YLDTQVGRLLSALDDLQLANSTIIAFTSDHGW-ALGEHGEwAKYSNfdvaTHVPLIFYVPGrtaslpeageklfpyldpF 384
Cdd:cd16024 175 EMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMtDAGNHGG-SSPGE----TSVPLLFISPK------------------F 231
|
90 100 110
....*....|....*....|....*....|....*
gi 2335187 385 DSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16024 232 SSKPSNADGELSYYETVQQVDLAPTLALLLGLPIP 266
|
|
| |
