|
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: 599.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16030 4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 118 TIPQYFKENGYVTMSVGKVFHPGITsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVVDVPEGTLP 197
Cdd:cd16030 84 TLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 198 DKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDSEVPDGLPPVAYNPWMDIRQREDVQ 277
Cdd:cd16030 162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 278 ALNISVPYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNFDVATHV 357
Cdd:cd16030 241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 358 PLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvpsfhvelCREGKN 437
Cdd:cd16030 321 PLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 438 LLkhfrfrdleedPYL--PGNPRELIAYSQYPRPAdfpqwnsdkpslkdikIMGYSIRTIDYRYTVWVgfnpdeflaNFS 515
Cdd:cd16030 366 LV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFD 409
|
490 500
....*....|....*....|....*
gi 1622970024 516 DIHAGELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16030 410 KVGAEELYDHKNDPNEWKNLANDPE 434
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
22-538 |
5.00e-91 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 284.46 E-value: 5.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 22 VALGCETQANSTTDALNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT 100
Cdd:COG3119 9 LALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 101 RLYDFNSYWRVH-AGNFSTIPQYFKENGYVTMSVGKVFHpgitsnHTDDspyswsfppyhpssekyentktcrgpdgELh 179
Cdd:COG3119 89 GVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTD----------------------------LL- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 180 anllcpvdvvdvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlapdsEVPDGL 259
Cdd:COG3119 134 ----------------------TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI------PLPPNL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 260 PPVAYNPwmdirqredvqalnisvpygpipvEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWAL 339
Cdd:COG3119 186 APRDLTE------------------------EELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 340 GEHG-EWAKYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:COG3119 242 GEHGlRGGKGTLYEGGIRVPLIVRWPGKIK------------------------AGSVSDALVSLIDLLPTLLDLAGVPI 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 419 PPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPAdfpqwnsdkpslkdikiMGYSIRTIDYR 498
Cdd:COG3119 298 PEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRGG-----------------GNRAIRTGRWK 340
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1622970024 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 |
1.72e-61 |
|
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: 208.23 E-value: 1.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY----DFNSYWRVH 112
Cdd:cd16033 2 NILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 113 AGNFSTIPQYFKENGYVTMSVGKvFHPGitsnhTDDSPYSWSFPPYHPssekYENTKtcrgpdgelhanllcpvdvvdvp 192
Cdd:cd16033 82 PPGVETFSEDLREAGYRNGYVGK-WHVG-----PEETPLDYGFDEYLP----VETTI----------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 193 EGTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDSEVP-DGLPPVAYNpwmdIR 271
Cdd:cd16033 129 EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDfEDKPYIYRR----ER 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 272 QREDVQALNIsvpygpipvEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAK-YSN 350
Cdd:cd16033 200 KRWGVDTEDE---------EDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKgPFM 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 351 FDVATHVPLMFYVPGrtaslpeageklfpyldpfdsaseLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhve 430
Cdd:cd16033 271 YEETYRIPLIIKWPG------------------------VIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKV-------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 431 lcrEGKNLLKHFRfrdlEEDPylPGNPRELIAysqyprpadfpQWNSDKPSLkdikiMGYSIRTIDYRYTvwvgFNPdef 510
Cdd:cd16033 319 ---DGRSLLPLLR----GEQP--EDWRDEVVT-----------EYNGHEFYL-----PQRMVRTDRYKYV----FNG--- 366
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622970024 511 lanfSDIhaGELYFVDSDPLQDHNMYNDSQGGDLFQLLM 549
Cdd:cd16033 367 ----FDI--DELYDLESDPYELNNLIDDPEYEEILREMR 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
38-540 |
3.22e-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: 200.81 E-value: 3.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 118 TIPQYFKENGYVTMSVGKVFHPGitsnhtdDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANllcpvdvvdvpegtlP 197
Cdd:cd16027 82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRA---------------K 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 198 DKQsteqaiqllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDseVPDgLPPVaynpwmdirqREDVQ 277
Cdd:cd16027 140 KGQ-----------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPY--LPD-TPEV----------REDLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 278 AlnisvpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGehgeWAKYSNFDVATHV 357
Cdd:cd16027 190 D---------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGLRV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 358 PLMFYVPGRTaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvpsfhvELcrEGKN 437
Cdd:cd16027 245 PLIVRWPGKI------------------------KPGSVSDALVSFIDLAPTLLDLAGIEPPE---------YL--QGRS 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 438 LLkhfrfrDLEEDPYLPGNP-----RELIAYSQYP-RpadfpqwnsdkpslkdikimgySIRTIDYRYTvwvgFNPDEFl 511
Cdd:cd16027 290 FL------PLLKGEKDPGRDyvfaeRDRHDETYDPiR----------------------SVRTGRYKYI----RNYMPE- 336
|
490 500
....*....|....*....|....*....
gi 1622970024 512 anfsdihagELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16027 337 ---------ELYDLKNDPDELNNLADDPE 356
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-534 |
9.13e-58 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 197.79 E-value: 9.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLydFNSYWRVHAgNF 116
Cdd:cd16034 3 NILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV--FGNDVPLPP-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 STIPQYFKENGYVTMSVGKvFHpgITSNHTDDSPYSWSFPP-----------------YHPSSEKYENtktcrgpDGELH 179
Cdd:cd16034 80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDD-------DGKRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 180 anllcpvdvvdVPEGTLPDKQsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDseVPDG 258
Cdd:cd16034 150 -----------YIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN--VPED 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 259 LPPVAynpwmdirqredvqalnisvpygpipvEFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWA 338
Cdd:cd16034 216 KKEEA---------------------------GLREDLRG-YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 339 LGEHGEWAKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:cd16034 268 LGSHGLMNKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPI 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 419 PPrcpvpsfhvelCREGKNLLKHFrfrdLEEDPYLPGNpreliAYSQYPRPadFPQWNSDKPSLKDIkimgysIRTIDYR 498
Cdd:cd16034 324 PD-----------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVP--FGGGSARDGGEWRG------VRTDRYT 375
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622970024 499 YTVWVGfnpDEFLanfsdihageLYFVDSDPLQDHN 534
Cdd:cd16034 376 YVRDKN---GPWL----------LFDNEKDPYQLNN 398
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
38-419 |
1.81e-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: 191.88 E-value: 1.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16022 2 NILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 STIPQYFKENGYVTMSVGKvfhpgitsNHtddspyswsfppyhpssekyentktcrgpdgelhanllcpvdvvdvpegtl 196
Cdd:cd16022 82 PTLAELLKEAGYRTALIGK--------WH--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 197 pdkqstEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRypkefqklyplenitlapdsevpdglppvaynpwmdirqredv 276
Cdd:cd16022 103 ------DEAIDFIERRDKDK-PFFLYVSFNAPHPPFA------------------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 277 qalnisvpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGE-WAKYSNFDVAT 355
Cdd:cd16022 133 -----------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGI 189
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622970024 356 HVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16022 190 RVPFIVRWPGK------------------------IPAGQVSDALVSLLDLLPTLLDLAGIEPP 229
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-529 |
3.43e-55 |
|
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: 188.52 E-value: 3.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhAGNF 116
Cdd:cd16037 2 NILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPY---DGDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 STIPQYFKENGYVTMSVGKvfhpgitsnhtddspyswsfppyhpssekyentktcrgpdgeLHANLLcpvdvvDVPEGTL 196
Cdd:cd16037 79 PSWGHALRAAGYETVLIGK------------------------------------------LHFRGE------DQRHGFR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 197 PDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdsevpdglppvaynpwmdirqredv 276
Cdd:cd16037 111 YDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY---------------------------------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 277 qalnisvpygpipvefQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNFDVATH 356
Cdd:cd16037 157 ----------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVR 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 357 VPLMFYVPGRtaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPvpsfhvelcreGK 436
Cdd:cd16037 221 VPMIISGPGI-------------------------PAGKRVKTPVSLVDLAPTILEAAGAPPPPDLD-----------GR 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 437 NLLkhfrfrDLEEDPYlpgnPRELIAYSQYprpadfpqwnsdkpSLKDIKIMGYSIRTIDYRYTVWVGFNPdeflanfsd 516
Cdd:cd16037 265 SLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP--------- 311
|
490
....*....|...
gi 1622970024 517 ihagELYFVDSDP 529
Cdd:cd16037 312 ----QLFDLENDP 320
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
38-548 |
5.05e-53 |
|
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: 185.81 E-value: 5.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRvhAGNF 116
Cdd:cd16031 4 NIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLF--DASQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 STIPQYFKENGYVTMSVGKvFHPGITSNHTDDS--------PYSWSFPPYHPSSEKYentktcRGPDGelHANLLCpvdv 188
Cdd:cd16031 82 PTYPKLLRKAGYQTAFIGK-WHLGSGGDLPPPGfdywvsfpGQGSYYDPEFIENGKR------VGQKG--YVTDII---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 189 vdvpegtlpdkqsTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDSEVPD---GLPPVAYN 265
Cdd:cd16031 149 -------------TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPE-PETFDDDdyaGRPEWARE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 266 PWMDIRQREDVQALNisvpygpiPVEFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGeW 345
Cdd:cd16031 214 QRNRIRGVLDGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-L 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 346 A-KYSNFDVATHVPLMFYVPGRTaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCpv 424
Cdd:cd16031 284 FdKRLMYEESIRVPLIIRDPRLI------------------------KAGTVVDALVLNIDFAPTILDLAGVPIPEDM-- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 425 psfhvelcrEGKNLLKHFRFRDleedpylPGNPRE--LIAYSQYPRPADFPQWnsdkpslkdikimgYSIRTIDYRYTVW 502
Cdd:cd16031 338 ---------QGRSLLPLLEGEK-------PVDWRKefYYEYYEEPNFHNVPTH--------------EGVRTERYKYIYY 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1622970024 503 VGFNPDEflanfsdihagELYFVDSDPLQDHNMYNDSQGGDLFQLL 548
Cdd:cd16031 388 YGVWDEE-----------ELYDLKKDPLELNNLANDPEYAEVLKEL 422
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-440 |
5.71e-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: 184.31 E-value: 5.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQ----QAVCAPSRVSFLTGRrpdttrlydfnSYWRVH 112
Cdd:cd16155 4 NILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR-----------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 113 AGNFS-------TIPQYFKENGYVTMSVGKvfhpgitsNHTDdspyswsfppyhpssekyentktcrgpdgelHANllcp 185
Cdd:cd16155 73 EGGKAaipsddkTWPETFKKAGYRTFATGK--------WHNG-------------------------------FAD---- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 186 vdvvdvpegtlpdkqsteQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDSEVPdgLPPVAyN 265
Cdd:cd16155 110 ------------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL-PENFLP--QHPFD-N 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 266 PWMDIRqreDVQalnisvpYGPIPVEFQ--RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHG 343
Cdd:cd16155 168 GEGTVR---DEQ-------LAPFPRTPEavRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 344 EWAKYSNFDVATHVPLMFYVPGrtasLPeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQVPPRCp 423
Cdd:cd16155 238 LMGKQNLYEHSMRVPLIISGPG----IP---------------------KGKRRDALVYLQDVFPTLCELAGIEIPESV- 291
|
410
....*....|....*..
gi 1622970024 424 vpsfhvelcrEGKNLLK 440
Cdd:cd16155 292 ----------EGKSLLP 298
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
38-420 |
2.58e-51 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 182.95 E-value: 2.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHAGN 115
Cdd:PRK13759 8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 116 FS-TIPQYFKENGYVTMSVGKV----------FHpgitsNHTDDSPYSWSFPPYHPSseKYENTKTCR--------GPDG 176
Cdd:PRK13759 84 YKnTLPQEFRDAGYYTQCIGKMhvfpqrnllgFH-----NVLLHDGYLHSGRNEDKS--QFDFVSDYLawlrekapGKDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 177 EL-------HANLLCPVDVvdvPEGTLPDKQSTEQAIQLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitl 249
Cdd:PRK13759 157 DLtdigwdcNSWVARPWDL---EERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYK------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 250 apDSEVPDglPPVAynPWmDIRQREDVQALNISVPYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIV 329
Cdd:PRK13759 227 --DADIPD--PHIG--DW-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTII 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 330 AFTSDHGWALGEHGEWAKYSNFDVATHVPLMFYVPGRTASLPEageklfpyldpfdsaselmepGRQSMDLVELVSLFPT 409
Cdd:PRK13759 300 LFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNR---------------------GTVIDQVVELRDIMPT 358
|
410
....*....|.
gi 1622970024 410 LAGLAGLQVPP 420
Cdd:PRK13759 359 LLDLAGGTIPD 369
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-421 |
3.67e-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: 173.50 E-value: 3.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 37 LNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPdttrlydfnSYWRVHAG- 114
Cdd:cd16148 1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP---------FYHGVWGGp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 115 ---NFSTIPQYFKENGYVTMSVGkvfhpgitsnhtdDSPYSWSFPPYHPSSEKYENTktcRGPDGElhanllcpvdvvDV 191
Cdd:cd16148 72 lepDDPTLAEILRKAGYYTAAVS-------------SNPHLFGGPGFDRGFDTFEDF---RGQEGD------------PG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 192 PEGTLPDKQSTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapDsevpdglppvaynpwmdir 271
Cdd:cd16148 124 EEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-----------------D------------------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 272 qredvqalnisvpygpipvefqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAK-YSN 350
Cdd:cd16148 167 ------------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSN 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622970024 351 F-DVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVPPR 421
Cdd:cd16148 217 LyDEQLHVPLIIRWPGK-------------------------EPGKRVDALVSHIDIAPTLLDLLGVEPPDY 263
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
37-466 |
5.94e-49 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 171.99 E-value: 5.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 37 LNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfnsywrvHAGN 115
Cdd:cd16032 1 PNILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYD-------NAAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 116 FS----TIPQYFKENGYVTMSVGKVfhpgitsnHtddspyswsFPpyhpssekyentktcrGPDgELHanllcpvdvvdv 191
Cdd:cd16032 74 FPadipTFAHYLRAAGYRTALSGKM--------H---------FV----------------GPD-QLH------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 192 peGTLPDKQSTEQAIQLLEKMKTSAS--PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdsevpdglppvaynpwmd 269
Cdd:cd16032 108 --GFDYDEEVAFKAVQKLYDLARGEDgrPFFLTVSFTHPHDPYVIPQEYWDLY--------------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 270 irqredvqalnisvpygpipvefQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYS 349
Cdd:cd16032 159 -----------------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMS 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 350 NFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSmDLVELVSLFPTLAGLAGLQVPPRCPVPsfhv 429
Cdd:cd16032 216 FFEGSARVPLIISAPGRFA------------------------PRRVA-EPVSLVDLLPTLVDLAGGGTAPHVPPL---- 266
|
410 420 430
....*....|....*....|....*....|....*..
gi 1622970024 430 elcrEGKNLLKHFRFRDleedpylPGNPREliAYSQY 466
Cdd:cd16032 267 ----DGRSLLPLLEGGD-------SGGEDE--VISEY 290
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-418 |
7.33e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 167.94 E-value: 7.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRP-SLGCYGDKL----------VRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFN 106
Cdd:cd16153 3 NILWIITDDQRVdSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 107 SYWRVHAGNFSTIPQYFKENGYVTMSVGKvfhpgitsnhtddspyswsfppyhpssEKYENtktcrgpdgelhanllcPV 186
Cdd:cd16153 83 AAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA-----------------FQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 187 DVVDVPEgtlpdkQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdsevpdglppvaynp 266
Cdd:cd16153 119 RYLKNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 267 wmdiRQREDvqalnisvpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLAN---STIVAFTSDHGWALGEHG 343
Cdd:cd16153 165 ----RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQG 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622970024 344 EWAKYSNFDVATHVPLMFYVPGRtaslpeageKLFPyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:cd16153 217 ILAKFTFWPQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-420 |
1.59e-47 |
|
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: 170.80 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16144 2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 S---------------TIPQYFKENGYVTMSVGKvFHPGITSNHT--------DDSPYSWSFPPYHPSSEKYENTKTCRG 173
Cdd:cd16144 82 KlipppsttrlpleevTIAEALKDAGYATAHFGK-WHLGGEGGYGpedqgfdvNIGGTGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 174 PDGElhanllcpvdvvdvpegTLPDKqSTEQAIQLLEkmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapds 253
Cdd:cd16144 161 PEGE-----------------YLTDR-LTDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKYE---------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 254 EVPDGLPPVAYNPwmdirqredvqalnisvpygpipvefqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTS 333
Cdd:cd16144 211 KKKKGLRKGQKNP--------------------------------VYAAMIESLDESVGRILDALEELGLADNTLVIFTS 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 334 DHGwALGEHGEWA---------KYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELV 404
Cdd:cd16144 259 DNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIK------------------------PGSVSDVPVIGT 313
|
410
....*....|....*.
gi 1622970024 405 SLFPTLAGLAGLQVPP 420
Cdd:cd16144 314 DLYPTFLELAGGPLPP 329
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-540 |
1.75e-46 |
|
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: 168.18 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16150 2 NIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 StipQYFKENGYVTMSVGKvfhpgitsNHTDDSPYSWsfppyhpssEKYEntktcrgpdgelhanllcpvdvvdvpegtL 196
Cdd:cd16150 82 L---KTLKDAGYHVAWAGK--------NDDLPGEFAA---------EAYC-----------------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 197 PDKQSTEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPDsEVPDGLPpvAYNPWMDIRQREDv 276
Cdd:cd16150 113 SDEACVRTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLPP-RRPPGLR--AKGKPSMLEGIEK- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 277 QALNisvpygPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSN-F-DVA 354
Cdd:cd16150 185 QGLD------RWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 355 THVPLMFYVPGRTaslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvPSFhvelcre 434
Cdd:cd16150 259 TRVPLIIKPPGGP-------------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THF------- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 435 GKNLLKHFRFRDLEEDPY-------LPGNPReliAYSQYPRPADFPQWNS---DKPSLKDIKIMgysIRTIDYRYtVWVG 504
Cdd:cd16150 303 GRSLLPVLAGETEEHRDAvfseggrLHGEEQ---AMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VYRL 375
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622970024 505 FNPDeflanfsdihagELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16150 376 YEPD------------ELYDLEADPLELHNLIGDPA 399
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
38-475 |
2.25e-46 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 168.59 E-value: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFN--SYWR---V 111
Cdd:cd16028 2 NVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR-------YLMNhrSVWNgtpL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 112 HAGnFSTIPQYFKENGYVTMSVGKvfhpgitsnhTDDSPYSWSFPPYHPSSEKYENtktcrgpdgelhanLLCPVDVVDV 191
Cdd:cd16028 75 DAR-HLTLALELRKAGYDPALFGY----------TDTSPDPRGLAPLDPRLLSYEL--------------AMPGFDPVDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 192 PEGtLPDKQS-----TEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDSEVPDGLPPVa 263
Cdd:cd16028 130 LDE-YPAEDSdtaflTDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQHPL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 264 YNPWMDIRQREDVQALNIsvPYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHG 343
Cdd:cd16028 206 LAAFLERIESLSFSPGAA--NAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHW 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 344 EWAKYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfDSASelmepGRQSMDLVELVSLFPTLAGLAGLQVPPRCp 423
Cdd:cd16028 284 LWGKDGFFDQAYRVPLIVRDPRREA----------------DATR-----GQVVDAFTESVDVMPTILDWLGGEIPHQC- 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622970024 424 vpsfhvelcrEGKNLLKHfrfrdLEEDPylPGNPRELIAYSQYPRPADFPQW 475
Cdd:cd16028 342 ----------DGRSLLPL-----LAGAQ--PSDWRDAVHYEYDFRDVSTRRP 376
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-419 |
2.30e-43 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 158.88 E-value: 2.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16026 3 NIVVILADDLGYGdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 115 -NFSTIPQYFKENGYVTMSVGKvFHPGITSNH--TD---DS----PYS---WSFPPYHPSSEKYEntktcrgpdgelhAN 181
Cdd:cd16026 83 pDEITIAEVLKKAGYRTALVGK-WHLGHQPEFlpTRhgfDEyfgiPYSndmWPFPLYRNDPPGPL-------------PP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 182 LLCPVDVVDVPegtlPD-----KQSTEQAIQLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapDSEvp 256
Cdd:cd16026 149 LMENEEVIEQP----ADqssltQRYTDEAVDFIERNKD--QPFFLYLAHTMPHVPLFASEKFKG-----------RSG-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 257 DGLppvaynpwmdirqredvqalnisvpYGpipvefqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHG 336
Cdd:cd16026 210 AGL-------------------------YG---------------DVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 337 WALGEHGEW--------AKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFP 408
Cdd:cd16026 250 PWLEYGGHGgsagplrgGKGTTWEGGVRVPFIAWWPGV------------------------IPAGTVSDELASTMDLLP 305
|
410
....*....|.
gi 1622970024 409 TLAGLAGLQVP 419
Cdd:cd16026 306 TLAALAGAPLP 316
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
38-534 |
3.55e-41 |
|
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: 153.09 E-value: 3.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNaFAQQAVCAPSRVSFLTGRRPDTTRLydfnsyWRVHAG-- 114
Cdd:cd16146 2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGV------WHTILGre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 115 ----NFSTIPQYFKENGYVTMSVGKvFHPGitsnhtDDSPY----------------SWSFPPYHPSSEKYENTKTCRGp 174
Cdd:cd16146 75 rmrlDETTLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 175 dgelhanllcpvdVVDVPEGTLPDKQsTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapDSE 254
Cdd:cd16146 147 -------------KFVKTEGYCTDVF-FDEAIDFIEENKDK--PFFAYLATNAPHGPLQVPDKYLDPYK--------DMG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 255 VPDGlppvaynpwmdirqredvqalnisvpygpipvefqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSD 334
Cdd:cd16146 203 LDDK--------------------------------------LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSD 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 335 HGWALGEHGEW------AKYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFP 408
Cdd:cd16146 245 NGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKIL------------------------AGKDVDTLTAHIDLLP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 409 TLAGLAGLQVPPrcpvpsfHVELcrEGKNLLKhfrfrdLEEDPYLPGNPRELIAYSQYPRPADFPQWNSdkpslkdikim 488
Cdd:cd16146 301 TLLDLCGVKLPE-------GIKL--DGRSLLP------LLKGESDPWPERTLFTHSGRWPPPPKKKRNA----------- 354
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1622970024 489 gySIRTIDYRYTVWVGFNPdeflanfsdihagELYFVDSDPLQDHN 534
Cdd:cd16146 355 --AVRTGRWRLVSPKGFQP-------------ELYDIENDPGEEND 385
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-427 |
7.82e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 148.16 E-value: 7.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRV----- 111
Cdd:cd16149 2 NILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHgktkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 112 ---HAGNFSTIPQYFKENGYVTMSVGKvFHPGitsnhtddspyswsfppyhpssekyentktcrgpdgelhanllcpvdv 188
Cdd:cd16149 82 pegYLEGQTTLPEVLQDAGYRCGLSGK-WHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 189 vdvpegtlpdkqstEQAIQLLEKMKTSASPFFLAVGYHKPHipfrypkefqklyplenitlapdsevpdglppvayNPWm 268
Cdd:cd16149 113 --------------DDAADFLRRRAEAEKPFFLSVNYTAPH-----------------------------------SPW- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 269 dirqredvqalnisvpygpipvefqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAK- 347
Cdd:cd16149 143 ------------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKg 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 348 -----YSNFDVATHVPLMFYVPGRTaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVP--P 420
Cdd:cd16149 193 ngtfpLNMYDNSVKVPFIIRWPGVV------------------------PAGRVVDSLVSAYDFFPTLLELAGVDPPadP 248
|
....*..
gi 1622970024 421 RCPVPSF 427
Cdd:cd16149 249 RLPGRSF 255
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-421 |
1.98e-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: 148.51 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY---WRVHA 113
Cdd:cd16145 2 NIIFILADDLGYGdLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPggqDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 114 GNfSTIPQYFKENGYVTMSVGKVfhpGITSNHTDDSPYS----------------WSFPPYhpsseKYENTKtcRGPDGE 177
Cdd:cd16145 82 DD-VTLAEVLKKAGYATAAFGKW---GLGGPGTPGHPTKqgfdyfygyldqvhahNYYPEY-----LWRNGE--KVPLPN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 178 LHANLLCPVDVVDVPEGTLPDKQSTEQAIQLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDSEVPD 257
Cdd:cd16145 151 NVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYKYKPK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 258 GLPPVAYNPWMDIRQRedvqalnisvpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGw 337
Cdd:cd16145 217 DPGIYAYLPWPQPEKA--------------------------YAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 338 ALGEHGEWAKYSNFDVA--------------THVPLMFYVPGRTaslpeageklfpyldpfdsaselmEPGRQSMDLVEL 403
Cdd:cd16145 270 PHSEGGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPGKI------------------------PAGSVSDHPSAF 325
|
410
....*....|....*...
gi 1622970024 404 VSLFPTLAGLAGLQVPPR 421
Cdd:cd16145 326 WDFMPTLADLAGAEPPED 343
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
38-416 |
3.84e-37 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 139.48 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVhAGNF 116
Cdd:pfam00884 2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYV-STPVGL-PRTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 STIPQYFKENGYVTMSVGKvFHPGITSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGpdgelhanlLCPVDVVDvpegtl 196
Cdd:pfam00884 80 PSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPY---------NCSGGGVS------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 197 pDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdsevpdglppvaynpwmdirqredv 276
Cdd:pfam00884 144 -DEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA--------------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 277 qalnISVPYGPipveFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNFDVA-- 354
Cdd:pfam00884 187 ----TFKPSSC----SEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApe 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622970024 355 --THVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGL 416
Cdd:pfam00884 259 ggYRVPLLIWSPGGKA------------------------KGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-534 |
2.43e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 136.19 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAqQAVCAPSRVSFLTGRRPDTTrlYDFNSYWrvHAGNf 116
Cdd:cd16151 2 NIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRN--YVVFGYL--DPKQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 STIPQYFKENGYVTMSVGKvfhPGITSNhTDDSPYS-------WSFPPYHPSSEKYENTK--TCRGPDGELHAnllcpvd 187
Cdd:cd16151 76 KTFGHLLKDAGYATAIAGK---WQLGGG-RGDGDYPhefgfdeYCLWQLTETGEKYSRPAtpTFNIRNGKLLE------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 188 vvDVPEGTLPDkQSTEQAIQLLEKMKtsASPFFLavgY------HKPHIPFrypkefqklyplenitlaPDSEvpdglpp 261
Cdd:cd16151 145 --TTEGDYGPD-LFADFLIDFIERNK--DQPFFA---YypmvlvHDPFVPT------------------PDSP------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 262 vaynPWMDIRQRedvqalnisvpygpipvefqRKIRQSYF-ASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALG 340
Cdd:cd16151 192 ----DWDPDDKR--------------------KKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 341 EHGEW-------AKYSNFDVATHVPLMFYVPGrtaslpeageklfpyldpfdsaseLMEPGRQSMDLVELVSLFPTLAGL 413
Cdd:cd16151 248 ITSRTngrevrgGKGKTTDAGTHVPLIVNWPG------------------------LIPAGGVSDDLVDFSDFLPTLAEL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 414 AGLQVPPRCPVpsfhvelcrEGKNLLkhfrfrdleedPYL---PGNPRELIAYsqyprpadfpqWNSDKPSLKDIKimgY 490
Cdd:cd16151 304 AGAPLPEDYPL---------DGRSFA-----------PQLlgkTGSPRREWIY-----------WYYRNPHKKFGS---R 349
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1622970024 491 SIRTIDYRYtvwvgfnpdeflanFSDihaGELYFVDSDPLQDHN 534
Cdd:cd16151 350 FVRTKRYKL--------------YAD---GRFFDLREDPLEKNP 376
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
38-424 |
2.25e-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: 128.44 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQaVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16029 2 HIVFILADDLGWNdVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILAGEPYGlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 115 -NFSTIPQYFKENGYVTMSVGKvFHPGItsnhtddspYSWSFPP----------YHPSSEKYENTKTCRGPDgelhanll 183
Cdd:cd16029 81 lNETLLPQYLKELGYATHLVGK-WHLGF---------YTWEYTPtnrgfdsfygYYGGAEDYYTHTSGGAND-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 184 CPVDVVDVPEGTLPDKQS-------TEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdsevp 256
Cdd:cd16029 143 YGNDDLRDNEEPAWDYNGtystdlfTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 257 dglppvaynpwmdirqredVQALNIsvpygpipvefQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHG 336
Cdd:cd16029 209 -------------------DKFAHI-----------KDEDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 337 wALGEHGEWA--------KYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFP 408
Cdd:cd16029 259 -GPTGGGDGGsnyplrggKNTLWEGGVRVPAFVWSPLLPP-----------------------KRGTVSDGLMHVTDWLP 314
|
410
....*....|....*.
gi 1622970024 409 TLAGLAGLQVPPRCPV 424
Cdd:cd16029 315 TLLSLAGGDPDDLPPL 330
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-536 |
4.81e-32 |
|
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: 127.32 E-value: 4.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRP-SLGCYGDK-LVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFNSY--WRVhA 113
Cdd:cd16143 2 NIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGR-------YPWRSRlkGGV-L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 114 GNFS---------TIPQYFKENGYVTMSVGKvFHPGITSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelHANLLC 184
Cdd:cd16143 74 GGFSppliepdrvTLAKMLKQAGYRTAMVGK-WHLGLDWKKKDGKKAATGTGKDVDYSKPIKGGPLDHGFD---YYFGIP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 185 PVDVVDvpegTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLyplenitlapdSEVpdGlppvay 264
Cdd:cd16143 150 ASEVLP----TL-----TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGK-----------SGA--G------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 265 npwmdirqredvqalnisvPYGpipvEFqrkIRQsyfasvsyLDTQVGRLLSALDDLQLANSTIVAFTSDHG-------W 337
Cdd:cd16143 202 -------------------PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyK 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 338 ALGEHGEWA-------KYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTL 410
Cdd:cd16143 248 ELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKIP------------------------AGSVSDQLVSLTDLFATL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 411 AGLAGLQVPPRCPVPSFhvelcregkNLLkhfrfrdleedPYLPGNPreliaySQYPRPADFPQWNSDkpslkdikimGY 490
Cdd:cd16143 304 AAIVGQKLPDNAAEDSF---------SFL-----------PALLGPK------KQEVRESLVHHSGNG----------SF 347
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622970024 491 SIRTIDYRYTVWVGF--NPDEFLANFSDIHAGELYFVDSDPLQDHNMY 536
Cdd:cd16143 348 AIRKGDWKLIDGTGSggFSYPRGKEKLGLPPGQLYNLSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
38-452 |
5.18e-32 |
|
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: 128.65 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTtrlydfNSYWR---VHA 113
Cdd:cd16156 2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT------NGSWTncmALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 114 GNFSTIPQYFKENGYVTMSVGK-------VFHPGITSNHTDdSPYSWSFPPYHPSSEKYENTKTCRGPDgELHANllcpv 186
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKwhldggdYFGNGICPQGWD-PDYWYDMRNYLDELTEEERRKSRRGLT-SLEAE----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 187 dvvDVPEGTLPDKQSTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplenitlaPDSEVPDGlpPVAYN- 265
Cdd:cd16156 149 ---GIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--------KDFEFPKG--ENAYDd 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 266 ----P-----WMDIRQREDVQALNISVPYgpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLqLANSTIVaFTSDHG 336
Cdd:cd16156 214 lenkPlhqrlWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI-AEDAWVI-YTSDHG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 337 WALGEHGEWAK-YSNFDVATHVPLMFYVPGrtaslpeaGEKLFPYLD-PfdsaselmepgrqsmdlVELVSLFPTLAGLA 414
Cdd:cd16156 278 DMLGAHKLWAKgPAVYDEITNIPLIIRGKG--------GEKAGTVTDtP-----------------VSHIDLAPTILDYA 332
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622970024 415 GLQVPPRCP----VPSFHVELCREGK----------------------------------NLLKHFRFRDLEEDPY 452
Cdd:cd16156 333 GIPQPKVLEgesiLATIEDPEIPENRgvfvefgryevdhdgfggfqpvrcvvdgryklviNLLSTDELYDLEKDPY 408
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-420 |
7.27e-32 |
|
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: 126.49 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVR---SPNIDQLASHSLLFQNAFAQQAvCAPSRVSFLTGRRPdttrlydfnsywrVHA 113
Cdd:cd16142 2 NILVILGDDIGWGdLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP-------------IRT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 114 GNFS---------------TIPQYFKENGYVTMSVGKvfhpgitsNHTDDSPYSWsfPpyhpssekyentkTCRGPDgEL 178
Cdd:cd16142 68 GLTTvglpgspgglppwepTLAELLKDAGYATAQFGK--------WHLGDEDGRL--P-------------TDHGFD-EF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 179 HANLLcpvdvvdvpegTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdsevpdg 258
Cdd:cd16142 124 YGNLY-----------HTIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS--------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 259 lppvAYNPWMDirqredvqalnisvpygpipvefqrkirqsyfaSVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHG-- 336
Cdd:cd16142 178 ----GKGKYAD---------------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpe 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 337 ---WALGEHGEW--AKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLA 411
Cdd:cd16142 221 qdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGK------------------------IKPGRVSNEIVSHLDWFPTLA 276
|
....*....
gi 1622970024 412 GLAGLQVPP 420
Cdd:cd16142 277 ALAGAPDPK 285
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
38-452 |
3.43e-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: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPSLGCYGD--KLVRspnidQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSY----WRV 111
Cdd:cd16147 3 NIVLILTDDQDVELGSMDPmpKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTN-NSPpgggYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 112 HAGNF---STIPQYFKENGYVTMSVGKVFHpGITSNHTDDSP---YSWSFPPYHPSseKYENTKTCRGPDGELHANllCP 185
Cdd:cd16147 77 FWQNGlerSTLPVWLQEAGYRTAYAGKYLN-GYGVPGGVSYVppgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVS--YP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 186 V----DVVdvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAP-----DSEVP 256
Cdd:cd16147 152 GdyltDVI------------ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPrpppnNPDVS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 257 DG------LPPvaynPWMDIRQREDvqalnisvpygpipvEFQRKIRQSyFASVsylDTQVGRLLSALDDLQLANSTIVA 330
Cdd:cd16147 218 DKphwlrrLPP----LNPTQIAYID---------------ELYRKRLRT-LQSV---DDLVERLVNTLEATGQLDNTYII 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 331 FTSDHGWALGEHG-EWAKYSNFDVATHVPLMFYVPGrtasLPeageklfpyldpfdsaselmePGRQSMDLVELVSLFPT 409
Cdd:cd16147 275 YTSDNGYHLGQHRlPPGKRTPYEEDIRVPLLVRGPG----IP---------------------AGVTVDQLVSNIDLAPT 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622970024 410 LAGLAGLQVPP--------RCPVPSFH-VELCREGKNLLKHF---RFR---DLEEDPY 452
Cdd:cd16147 330 ILDLAGAPPPSdmdgrscgDSNNNTYKcVRTVDDTYNLLYFEwctGFRelyDLTTDPY 387
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-539 |
1.67e-29 |
|
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: 119.64 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHAGNF 116
Cdd:cd16152 3 NVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFR-NG--IPLPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 STIPQYFKENGYVTMSVGKvfhpgitsnhtddspysWSFPPYHpssekyentktcrgpdgelhanllcpVDVVdvpegtl 196
Cdd:cd16152 80 KTLAHYFRDAGYETGYVGK-----------------WHLAGYR--------------------------VDAL------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 197 pdkqsTEQAIQLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYplenitlaPDSEVPDGLPPVAYNPWmdiR 271
Cdd:cd16152 110 -----TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERF--------ANFWVPPDLAALPGDWA---E 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 272 QREDvqalnisvpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHgwalGEH-----GEWa 346
Cdd:cd16152 173 ELPD------------------------YLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 347 KYSNFDVATHVPLMFYVPGrtaslpeageklfpyldpFDSaselmepGRQSMDLVELVSLFPTLAGLAGLQVPprcpvPS 426
Cdd:cd16152 224 KRSCHESSIRVPLVIYGPG------------------FNG-------GGRVEELVSLIDLPPTLLDAAGIDVP-----EE 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 427 FHvelcreGKNLLKhfrfrDLEEDPylpgNPRELIAYSQyprpadfpqwnsdkpslkdIK--IMGYSIRTIDYRYTVwVG 504
Cdd:cd16152 274 MQ------GRSLLP-----LVDGKV----EDWRNEVFIQ-------------------ISesQVGRAIRTDRWKYSV-AA 318
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622970024 505 FNPDEFLANFSDIHAGE-LYFVDSDPLQDHNMYNDS 539
Cdd:cd16152 319 PDKDGWKDSGSDVYVEDyLYDLEADPYELVNLIGRP 354
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-416 |
5.73e-28 |
|
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: 113.84 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYD-FNSYWRVHAGN 115
Cdd:cd16035 2 NILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLLSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 116 -FSTIPQYFKENGYVTMSVGKvfhpgitsnhtddspysWsfppyHPSSekyentktcrgpdgelHANllcpvdvvdvpEG 194
Cdd:cd16035 82 dVPTLGHMLRAAGYYTAYKGK-----------------W-----HLSG----------------AAG-----------GG 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 195 TLPDKQSTEQAIQLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdsevpdglppvaynpwmdir 271
Cdd:cd16035 113 YKRDPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH------------------------------------------ 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 272 qreDVQalnisvpYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSN- 350
Cdd:cd16035 151 ---DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNa 220
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622970024 351 FDVATHVPLMFYVPGrtaslpeagekLFPyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGL 416
Cdd:cd16035 221 YEEALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGV 262
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
38-419 |
9.89e-28 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 115.23 E-value: 9.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDkLVRSPNIDQLASHSLLFQNaFAQQAVCAPSRVSFLTGRRP-------DTTRLYDFNSYW 109
Cdd:cd16025 4 NILLILADDLGFSdLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHhqvgmgtMAELATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 110 RVHAGNFSTIPQYFKENGYVTMSVGKvfhpgitsnhtddspysW--SFPPYHpSSEKYentktcrgpdgelhanllcpvd 187
Cdd:cd16025 82 GYLPDSAATIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL---------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 188 vvdvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LY 242
Cdd:cd16025 122 --------------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 243 PlENITLAPDsevPDGLPpvaynPWMDIRQRE-DVQALNISVpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDL 321
Cdd:cd16025 188 P-ADTKLTPR---PPGVP-----AWDSLSPEEkKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKEL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 322 QLANSTIVAFTSDHGwALGEHGeWAKYSN-----FDVATH-----VPLMfyvpgrtASLPEAGEKlfpyldpfdsaselm 391
Cdd:cd16025 243 GELDNTLIIFLSDNG-ASAEPG-WANASNtpfrlYKQASHeggirTPLI-------VSWPKGIKA--------------- 298
|
410 420
....*....|....*....|....*...
gi 1622970024 392 ePGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16025 299 -KGGIRHQFAHVIDIAPTILELAGVEYP 325
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
38-420 |
8.98e-26 |
|
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: 108.78 E-value: 8.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPSLGCY-GDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRlyDFNSYWRVHAgNF 116
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE--SWNNYKGLDP-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 STIPQYFKENGYVTMSVGKVFHpgiTSNHtddspyswsfppyHPSSEKYE----NTKTCRGPDGELHANLLCPVDVVDVp 192
Cdd:cd16171 79 PTWMDRLEKHGYHTQKYGKLDY---TSGH-------------HSVSNRVEawtrDVPFLLRQEGRPTVNLVGDRSTVRV- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 193 egTLPDKQSTEQAIQLLEKMKTSAS-PFFLAVGYHKPHiPFRYPkefqklypleniTLAPDsevpdglppvaynpwmdir 271
Cdd:cd16171 142 --MLKDWQNTDKAVHWIRKEAPNLTqPFALYLGLNLPH-PYPSP------------SMGEN------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 272 qredvqalnisvpYGPIpvefqRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNF 351
Cdd:cd16171 188 -------------FGSI-----RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMY 249
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622970024 352 DVATHVPLMFYVPGrtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 420
Cdd:cd16171 250 EGSSHVPLLIMGPG-------------------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
38-419 |
1.88e-21 |
|
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: 97.74 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYwRV----- 111
Cdd:cd16159 3 NIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGM-RVilfta 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 112 -HAG---NFSTIPQYFKENGYVTMSVGKvFHPGITSNHTDDSpyswsfpPYHPSSEKYE--------NTKTCRGPDGElh 179
Cdd:cd16159 82 sSGGlppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDF-------CHHPLNHGFDyfyglpltNLKDCGDGSNG-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 180 ANLLCPVDVVDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKL--------------YPLE 245
Cdd:cd16159 152 EYDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRYFncilmrnhevveqpMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 246 NIT--LAPDS----EVPDGLPPVAYNPWmdirqredvqaLNISVPYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALD 319
Cdd:cd16159 232 NLTqrLTKEAisflERNKERPFLLVMSF-----------LHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 320 DLQLANSTIVAFTSDHGWAL------GEHGEW-------AKYSNFDVATHVPLMFYVPGRtasLPeageklfpyldpfdS 386
Cdd:cd16159 301 ELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGV---IP--------------P 363
|
410 420 430
....*....|....*....|....*....|...
gi 1622970024 387 ASELMEPGRQsMDlvelvsLFPTLAGLAGLQVP 419
Cdd:cd16159 364 GSVIDEPTSL-MD------IFPTVAALAGAPLP 389
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
38-419 |
5.52e-20 |
|
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 92.89 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16158 3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 115 -NFSTIPQYFKENGYVTMSVGKvFHPGITSN-----------HTDDSPYSWSFPPYHPSSEKYENTK---TCRgpDGELH 179
Cdd:cd16158 83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNgtylpthqgfdHYLGIPYSHDQGPCQNLTCFPPNIPcfgGCD--QGEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 180 ANLLCPVDVVDVPeGTLPD--KQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdsevpd 257
Cdd:cd16158 160 CPLFYNESIVQQP-VDLLTleERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFA------------------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 258 glppvaynpwmdirqredvqalnisvpygpipvefQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGW 337
Cdd:cd16158 221 -----------------------------------GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 338 AL------GEHG--EWAKYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRqSMDLVELVSLFPT 409
Cdd:cd16158 266 STmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPGRIK------------------------PGV-THELASTLDILPT 320
|
410
....*....|
gi 1622970024 410 LAGLAGLQVP 419
Cdd:cd16158 321 IAKLAGAPLP 330
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
38-420 |
1.81e-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: 90.22 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVR-SPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVHAG- 114
Cdd:cd16161 3 NFLLLFADDLGwGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH-NFLPTSVGGl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 115 --NFSTIPQYFKENGYVTMSVGKvFHPGITSNhtddspyswsfppYHPSSekyentktcRGPDGELHANLLCPVdvvdvp 192
Cdd:cd16161 82 plNETTLAEVLRQAGYATGMIGK-WHLGQREA-------------YLPNS---------RGFDYYFGIPFSHDS------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 193 egTLPDKQStEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlAPDSevpdglppvaynpwmdirq 272
Cdd:cd16161 133 --SLADRYA-QFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQ----------SPTS------------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 273 redvqalnISVPYGpipvefqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHG-WALG-------EHGE 344
Cdd:cd16161 181 --------GRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpGTGD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 345 W--------AKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGL 416
Cdd:cd16161 238 WqgnlggsvAKASTWEGGHREPAIVYWPGR------------------------IPANSTSAALVSTLDIFPTVVALAGA 293
|
....
gi 1622970024 417 QVPP 420
Cdd:cd16161 294 SLPP 297
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-419 |
8.26e-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: 8.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSywrvHAGNF 116
Cdd:cd16157 3 NIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA----HARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 117 ST--------------IPQYFKENGYVTMSVGKvFHPGitsnHTddspyswsfPPYHPSSE--------------KYENT 168
Cdd:cd16157 79 YTpqnivggipdseilLPELLKKAGYRNKIVGK-WHLG----HR---------PQYHPLKHgfdewfgapnchfgPYDNK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 169 KTCRGP---DGELHANLLCPVDvVDVPEGTLPDKQS-TEQAIQLLEKMKTSASPFFLavgyhkphipfrypkefqklypl 244
Cdd:cd16157 145 AYPNIPvyrDWEMIGRYYEEFK-IDKKTGESNLTQIyLQEALEFIEKQHDAQKPFFL----------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 245 eniTLAPDSEvpdGLPPVAYNPWMDIRQREdvqalnisvpygpipvefqrkirqSYFASVSYLDTQVGRLLSALDDLQLA 324
Cdd:cd16157 201 ---YWAPDAT---HAPVYASKPFLGTSQRG------------------------LYGDAVMELDSSVGKILESLKSLGIE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 325 NSTIVAFTSDHGWAL-------GEHGEW--AKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGR 395
Cdd:cd16157 251 NNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGH------------------------IKPGQ 306
|
410 420
....*....|....*....|....
gi 1622970024 396 QSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16157 307 VSHQLGSLMDLFTTSLALAGLPIP 330
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-419 |
2.54e-18 |
|
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: 86.63 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDL-RPSLGCY--GDKLVRSPNIDQLASHSLLFQNAFAqQAVCAPSRVSFLTGRrpdttrlYDFN----SYWR 110
Cdd:cd16154 2 NILLIIADDQgLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGK-------YGFRtgvlAVPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 111 VHAGNFSTIPQYFKEN----GYVTMSVGKvFHPGITSNHTDDSPYSWSFPPYHPS--SEKYENTKTCRGpdgelhanllc 184
Cdd:cd16154 74 ELLLSEETLLQLLIKDattaGYSSAVIGK-WHLGGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNG----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 185 pvdvVDVPEGTLPDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDSevpdglPPV 262
Cdd:cd16154 142 ----QTTNSTEYATTKLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGDS------ADI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 263 AYNPwmdirqredvqalnisvpygpipvefqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANsTIVAFTSDHG------ 336
Cdd:cd16154 202 EANP------------------------------RPYYLAAIEAMDTEIGRLLASIDEEEREN-TIIIFIGDNGtpgqvv 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 337 --WALGEHgewAKYSNFDVATHVPLMFyvpgrtaslpeageklfpyldpfdSASELMEPGRQSMDLVELVSLFPTLAGLA 414
Cdd:cd16154 251 dlPYTRNH---AKGSLYEGGINVPLIV------------------------SGAGVERANERESALVNATDLYATIAELA 303
|
....*
gi 1622970024 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 |
6.70e-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: 83.25 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRpslgcYGDKLV-------RSPnIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY--DFNSY 108
Cdd:cd16160 3 NIVLFFADDMG-----YGDLASyghptqeRGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 109 WRVHAG---NFSTIPQYFKENGYVTMSVGKvFHPGITSNHTDDSPYswsFPPYH---------PssekYENTKTCrgPDG 176
Cdd:cd16160 77 PWDIGGlpkTEVTMAEALKEAGYTTGMVGK-WHLGINENNHSDGAH---LPSHHgfdfvgtnlP----FTNSWAC--DDT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 177 ELHanllcpVDVVDVPEGTLPDK-QSTEQAIQ---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyp 243
Cdd:cd16160 147 GRH------VDFPDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 244 lenitlapdsevpdglppvaynpwmdirqredvqalNISVpygpipvefqrkiRQSYFASVSYLDTQVGRLLSALDDLQL 323
Cdd:cd16160 217 ------------------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 324 ANSTIVAFTSDHGWAL---GEHGEWA-----KYSNFDVATHVPLMFYVPGRTaslpeageklfpyldpfdsaselmePGR 395
Cdd:cd16160 248 DQNTLVFFLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTI-------------------------KPR 302
|
410 420
....*....|....*....|....
gi 1622970024 396 QSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16160 303 VSHEVVSTMDIFPTFVDLAGGTLP 326
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
29-439 |
7.16e-17 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 83.55 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 29 QANSTTDALNILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGrrpdttrLYDFNS 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-------LPPLPG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 108 ---YWRVHAGNFSTIPQYFKENGYVTMsvgkVFHPGitsnhtddSPYSWSFPPYHPsSEKYENTKtcrgpDGElhanllc 184
Cdd:COG1368 300 gspYKRPGQNNFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYK-NLGFDEFY-----DRE------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 185 pvDVVDVPEGT--LPDKQSTEQAIQLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITLapdsevpdg 258
Cdd:COG1368 355 --DFDDPFDGGwgVSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL--------- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 259 lppvaynpwmdirqredvqalnisvpygpipvefqrkirQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGwa 338
Cdd:COG1368 417 ---------------------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG-- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 339 lGEHGEWAKYSNFDVATHVPLMFYVPGrtaslpeageklfpyldpfdsaseLMEPGRQSmDLVELVSLFPTLAGLAGLQV 418
Cdd:COG1368 456 -PRSPGKTDYENPLERYRVPLLIYSPG------------------------LKKPKVID-TVGSQIDIAPTLLDLLGIDY 509
|
410 420
....*....|....*....|.
gi 1622970024 419 PPRcpvPSFhvelcreGKNLL 439
Cdd:COG1368 510 PSY---YAF-------GRDLL 520
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
38-415 |
1.00e-14 |
|
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: 74.64 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVC--APSRVSFLTGRRPDTTRLYDFNSYwrvHAG 114
Cdd:cd16015 2 NVIVILLESFsDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPPLPLGSGSYTLY---KLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 115 NFSTIPQYFKENGYVTMSvgkvFHPGitsnhtddSPYSWSFPPYHP--------SSEKYENTKTCRGPDGelhanllcpv 186
Cdd:cd16015 79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPnlgfdefyDLEDFPDDEKETNGWG---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 187 dvvdvpegtLPDKQSTEQAIQLLEKMKtsASPFFLAV----GyhkpHIPFRYPKEFQKLyplenitlapdsevpdglppv 262
Cdd:cd16015 137 ---------VSDESLFDQALEELEELK--KKPFFIFLvtmsN----HGPYDLPEEKKDE--------------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 263 aynpwmdirqredvqalnisvpygPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEH 342
Cdd:cd16015 181 ------------------------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622970024 343 GEWAKYSNFDvATHVPLMFYVPGrtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAG 415
Cdd:cd16015 237 YDETDEDPLD-LYRTPLLIYSPG-------------------------LKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
198-368 |
7.27e-14 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 74.17 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 198 DKQSTEQAIQLLEKmKTSASPFFLAVGYHKPH---IPFRYPKEFQKLYPLENITLAPDSEVPdglppvaynpwmdirqre 274
Cdd:COG3083 363 DRQITAQWLQWLDQ-RDSDRPWFSYLFLDAPHaysFPADYPKPFQPSEDCNYLALDNESDPT------------------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 275 dvqalnisvpygpipvefqrKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGE--WAKYSNF- 351
Cdd:COG3083 424 --------------------PFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFs 483
|
170
....*....|....*..
gi 1622970024 352 DVATHVPLMFYVPGRTA 368
Cdd:COG3083 484 RYQLQVPLVIHWPGTPP 500
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
38-414 |
1.41e-12 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 67.45 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQnAFAQQAVC--APSRVSFLTGRRPDttrlydfnsywrvhag 114
Cdd:cd00016 2 HVVLIVLDGLGADdLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTssAPNHAALLTGAYPT---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 115 nfstipqyfkENGYVTMSVGKVFHPGITSNHTDDSPyswSFPpyhpssekyentktcrgpdgelhanllcpvdvvdvpeG 194
Cdd:cd00016 65 ----------LHGYTGNGSADPELPSRAAGKDEDGP---TIP-------------------------------------E 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 195 TLPDKQSTEQAIQLLE--KMKTSASPFFLAVGYHKPHIPFRYPKefqklyplenitlapdsevpdglppvaynpwmdirq 272
Cdd:cd00016 95 LLKQAGYRTGVIGLLKaiDETSKEKPFVLFLHFDGPDGPGHAYG------------------------------------ 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 273 redvqalnisvPYGPipvefqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYS--- 349
Cdd:cd00016 139 -----------PNTP-----------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgka 196
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622970024 350 -NFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmepGRQSMDLVELVSLFPTLAGLA 414
Cdd:cd00016 197 dKSHTGMRVPFIAYGPGVKK-------------------------GGVKHELISQYDIAPTLADLL 237
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
302-365 |
4.00e-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: 48.35 E-value: 4.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622970024 302 ASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWA-LGEHGewakYSNFDVATHVPLMFYVPG 365
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
38-417 |
2.52e-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: 46.08 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 38 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAqqavCAPS-RVS---FLTGR-RPDTTRLYDFNSywrv 111
Cdd:cd16017 4 NVVLVIGESARRDhMSLYGYPRDTTPFLSKLKKNLIVFDNVIS----CGTStAVSlpcMLSFAnRENYDRAYYQEN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 112 hagnfstIPQYFKENGYvtmsvgKVFHpgiTSNHTDDSPYSWSFPPYHPSSEKYENTKTCRG---PDGELhanllcpvdv 188
Cdd:cd16017 76 -------LIDLAKKAGY------KTYW---ISNQGGCGGYDTRISAIAKIETVFTNKGSCNSsncYDEAL---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 189 vdvpegtLPdkqsteqaiQLLEKMKTSASPFFLAV---GyhkPHIPF--RYPKEFQKLYPlenitlapdsevpdglppva 263
Cdd:cd16017 130 -------LP---------LLDEALADSSKKKLIVLhlmG---SHGPYydRYPEEFAKFTP-------------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970024 264 ynpwmdirqredvqalnisVPYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQlaNSTIVAFTSDHGWALGEHG 343
Cdd:cd16017 171 -------------------DCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENG 229
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622970024 344 EW--AKYSNFDVATHVPLMFYVPGRTASLPEAGEKLFPYLDPFdsaselmepgrqSMDLvelvsLFPTLAGLAGLQ 417
Cdd:cd16017 230 LYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPF------------SHDN-----LFHTLLGLLGIK 288
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
300-336 |
4.87e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 42.43 E-value: 4.87e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1622970024 300 YFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHG 336
Cdd:COG1524 207 YRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| |
