|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
37-560 |
0e+00 |
|
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: 752.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 116
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQK 196
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 LNFLFQVLALVALTLVAGKLthLIPVSWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 276
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLY--LGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 QEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 356
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 357 SLENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQD 436
Cdd:cd16159 319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 437 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDL 516
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 157266309 517 SRDPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 560
Cdd:cd16159 478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
37-524 |
3.76e-156 |
|
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: 453.17 E-value: 3.76e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRVLQWT 116
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasDH-CHHPLHHGFDHFYGMPFSLMGDCARWELSEKRvnleq 195
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 196 klnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivHADCFLMRNHTITEQPMcFQRT-TPL 274
Cdd:cd16026 144 ------------------------------------------------------GPLPPLMENEEVIEQPA-DQSSlTQR 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 275 ILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD- 353
Cdd:cd16026 169 YTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDn 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 --------HGGSleNQL-----GNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR 420
Cdd:cd16026 249 gpwleyggHGGS--AGPlrggkGTTWEGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 421 LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGacygrkvcpc 500
Cdd:cd16026 310 LAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG---------- 373
|
490 500
....*....|....*....|....
gi 157266309 501 fGEKVVHHDPPLLFDLSRDPSETH 524
Cdd:cd16026 374 -GLDPTKLEPPLLYDLEEDPGETY 396
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
37-541 |
1.70e-132 |
|
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: 394.49 E-value: 1.70e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsiGYRV-LQW 115
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 TgaSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDhFYG--MPFSLMGDCARWELSekrvnl 193
Cdd:cd16160 79 D--IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGtnLPFTNSWACDDTGRH------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 194 eqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalIVHAD---CFLMRNHTITEQPMCFQR 270
Cdd:cd16160 150 ------------------------------------------------------VDFPDrsaCFLYYNDTIVEQPIQHEH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 271 TTPLILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYF 350
Cdd:cd16160 176 LTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 351 TSDHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTV 418
Cdd:cd16160 256 LSDHGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 419 VRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACYGR 495
Cdd:cd16160 318 VDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGGG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 157266309 496 KVCP------CFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMERV 541
Cdd:cd16160 391 PLSDyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPSVYEHMLEAVEKL 442
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
38-582 |
2.69e-99 |
|
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: 310.15 E-value: 2.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqwTG 117
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhcHHPLHHGFDHFYGMPFSL-MGDCArwelsekrvnleqk 196
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHdQGPCQ-------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 lnflfqvlalvaltlvagKLTHLIPvswmpviwsalsavlllASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 276
Cdd:cd16158 139 ------------------NLTCFPP-----------------NIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 QEVASFL----KRNKhgPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTS 352
Cdd:cd16158 184 KFAKDFIadnaKEGK--PFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 353 DHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVR 420
Cdd:cd16158 262 DNGpstmrksrggnaGLLKCGKGTTYEGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 421 LAGGEVPqDRVIDGQDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACY 493
Cdd:cd16158 324 LAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCH 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 494 GRKvcpcfgeKVVHHDPPLLFDLSRDPSETHILTpaSEPVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNiwrPWLQPC 573
Cdd:cd16158 397 PSA-------ELTSHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPC 464
|
570
....*....|...
gi 157266309 574 ----CGPFPLCWC 582
Cdd:cd16158 465 ckpgCTPKPSCCQ 477
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-527 |
9.35e-96 |
|
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: 297.52 E-value: 9.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssigYRVlQ 114
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-----TTV-G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 115 WTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPFSLMGDcarwELSEKRVNle 194
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG------RLPTDHGFDEFYGNLYHTIDE----EIVDKAID-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 qklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcFLMRNHtiteqpmcfqrttpl 274
Cdd:cd16142 142 -----------------------------------------------------------FIKRNA--------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 275 ilqevasflKRNKhgPFLLFVSFLHVHIPLITMENFLGKSL-HGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 353
Cdd:cd16142 148 ---------KADK--PFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTD 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 HG-----------GSLENQLGNTQYGGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLA 422
Cdd:cd16142 217 NGpeqdvwpdggyTPFRGEKGTTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALA 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 423 GGEVP------QDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVtpVFQPEGAGACYGRK 496
Cdd:cd16142 280 GAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFY 351
|
490 500 510
....*....|....*....|....*....|.
gi 157266309 497 VCPCfgekvvhhdpPLLFDLSRDPSETHILT 527
Cdd:cd16142 352 VLTF----------PLIFNLRRDPKERYDVT 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
19-524 |
1.34e-95 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 297.56 E-value: 1.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 19 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 98
Cdd:COG3119 5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 99 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesasdhchhplhhgfdhfygmpfslm 178
Cdd:COG3119 85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 179 gdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 258
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 htiteqpmcfqrtTPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGK----------------------- 313
Cdd:COG3119 130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 314 SLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlG-----NTQY-GGwngiykggkgmggweggI 387
Cdd:COG3119 197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEH-GlrggkGTLYeGG-----------------I 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 388 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWH 467
Cdd:COG3119 259 RVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRT 336
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 157266309 468 QRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhhDPPLLFDLSRDPSETH 524
Cdd:COG3119 337 GR-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
37-527 |
2.67e-90 |
|
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: 283.59 E-value: 2.67e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRvlqw 115
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 tgASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSlmGDCarwELSEKRVNLeq 195
Cdd:cd16161 77 --SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFS--HDS---SLADRYAQF-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 196 klnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhADCFLMRNhtiteqpmcfqrttpli 275
Cdd:cd16161 142 -------------------------------------------------------ATDFIQRA----------------- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 276 lqevasflkRNKHGPFLLFVSFLHVHIPLITMENFLGKSLH-GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 354
Cdd:cd16161 150 ---------SAKDRPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 355 G-----GSLENQLGNTQY---GGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEV 426
Cdd:cd16161 221 GpwevkCELAVGPGTGDWqgnLGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASL 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 427 PQDRVIDGQDLLPLLLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtmWKVHFVTpvfqpEGAGACygrkvCPCF 501
Cdd:cd16161 296 PPGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALAC-----CGST 358
|
490 500
....*....|....*....|....*.
gi 157266309 502 GEKvVHHDPPLLFDLSRDPSETHILT 527
Cdd:cd16161 359 GPK-LYHDPPLLFDLEVDPAESFPLT 383
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-524 |
1.19e-89 |
|
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: 283.28 E-value: 1.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 117
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 A-------SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDH------------FYGMPFSLM 178
Cdd:cd16144 81 TklipppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVniggtgnggppsYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 179 GDCARWELSEKRVNleqklnflfqvlalvALTlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 258
Cdd:cd16144 155 PDLEDGPEGEYLTD---------------RLT------------------------------------------------ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 htiteqpmcfqrttplilQEVASFLKRNKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYGDN-------VEEMD 327
Cdd:cd16144 172 ------------------DEAIDFIEQNKDKPFFLYLSHYAVHTPIQarpeLIEKYEKKKKGLRKGQKnpvyaamIESLD 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 328 WMVGRILDTLDVEGLSNSTLIYFTSDHGG-SLENQLGNTQY-----------GGwngiykggkgmggweggIRVPGIFRW 395
Cdd:cd16144 234 ESVGRILDALEELGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRW 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 396 PGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYcerFLHAARWHQRDRGTM- 474
Cdd:cd16144 297 PGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWH---FPHYHGQGGRPASAIr 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 157266309 475 ---WK-VHFvtpvfqpegagacygrkvcpcfgekvvHHDPPL-LFDLSRDPSETH 524
Cdd:cd16144 374 kgdWKlIEF---------------------------YEDGRVeLYNLKNDIGETN 401
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-524 |
1.61e-88 |
|
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: 279.47 E-value: 1.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssiGYRVLQWT 116
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRL----KGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGgLPTNETTFAKILKEKGYATGLIGKWHLGLN------CESASDHCHH----------PLHHGFDHFYGMPFSlmgd 180
Cdd:cd16143 77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwkkkdgKKAATGTGKDvdyskpikggPLDHGFDYYFGIPAS---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 181 carwelsekrvnleqklnflfQVLalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnht 260
Cdd:cd16143 152 ---------------------EVL-------------------------------------------------------- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 261 iteqpmcfqrttPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLD 338
Cdd:cd16143 155 ------------PTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 339 VEGLSNSTLIYFTSDHGGSLENQLGNTQ-----------------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLP 400
Cdd:cd16143 223 ELGLAENTLVIFTSDNGPSPYADYKELEkfghdpsgplrgmkadiYeGG-----------------HRVPFIVRWPGKIP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 401 AGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTMWKVhfv 480
Cdd:cd16143 286 AGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL--- 356
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 157266309 481 tpVFQPEGAGACYGRKvcpcfgeKVVHHDPP-LLFDLSRDPSETH 524
Cdd:cd16143 357 --IDGTGSGGFSYPRG-------KEKLGLPPgQLYNLSTDPGESN 392
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
37-560 |
1.58e-86 |
|
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: 276.66 E-value: 1.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 116
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GAS--GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPfslmgDCARWELSEKRvnle 194
Cdd:cd16157 81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGPYDNKA---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 qklnflfqvlalvaltlvagklTHLIPV--SWmpviwsalsavlLLASSYFVGALIvhadcflmrNHTITEQPMcfqrtT 272
Cdd:cd16157 146 ----------------------YPNIPVyrDW------------EMIGRYYEEFKI---------DKKTGESNL-----T 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 PLILQEVASFLKR--NKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYF 350
Cdd:cd16157 178 QIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 351 TSDHGGSLenqLGNTQYGGWNgIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDR 430
Cdd:cd16157 258 SSDNGAAL---ISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDR 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 431 VIDGQDLLPLLLgtAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVT----PVFQPEGAGACYGRKVCPCFGEKVV 506
Cdd:cd16157 334 AIDGIDLLPVLL--NGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQT 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 157266309 507 HH-DPPLLFDLSRDPSETHILTPASePVFYQVMERVQQAVWEHQRTLSPVPLQLD 560
Cdd:cd16157 406 DHtKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-524 |
5.12e-75 |
|
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: 244.81 E-value: 5.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyRVLQWTG 117
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasDHCHHPLHHGFDHFYGmpfslmgdcarwelsekrvnleqkl 197
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGP-----GTPGHPTKQGFDYFYG------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nFLFQVLAlvaltlvagkltHlipvswmpviwsalsavlllasSYFVGALIVHADCFLMRNHTIT-------EQPMCFQR 270
Cdd:cd16145 125 -YLDQVHA------------H----------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 271 TTPLILQEVASFLKRNKHGPFLLFVSFLHVHIPLIT-------MENFLGKSLHGLYGDNVEE--------MDWMVGRILD 335
Cdd:cd16145 170 SHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVpddgpykYKPKDPGIYAYLPWPQPEKayaamvtrLDRDVGRILA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 336 TLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQY--------------------GGwngiykggkgmggweggIRVPGIFRW 395
Cdd:cd16145 250 LLKELGIDENTLVVFTSDNGPHSE---GGSEHdpdffdsngplrgykrslyeGG-----------------IRVPFIARW 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 396 PGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdr 471
Cdd:cd16145 310 PGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG--- 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 157266309 472 gtmWKVhfvtpVFQPEGAGacygrkvcpcfgekvvhhdPPLLFDLSRDPSETH 524
Cdd:cd16145 383 ---WKA-----VRHGKKDG-------------------PFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
38-436 |
1.35e-74 |
|
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: 237.72 E-value: 1.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssigyrVLQWTG 117
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqkl 197
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplilQ 277
Cdd:cd16022 103 -------------------------------------------------------------------------------D 103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 EVASFLKRNKHG-PFLLFVSFLHVHIPLItmenflgkslhglYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 356
Cdd:cd16022 104 EAIDFIERRDKDkPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 357 SLENqlGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQD 436
Cdd:cd16022 171 MLGD--HGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
38-547 |
1.05e-71 |
|
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: 235.91 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSIGYRVLqwt 116
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSLMGDCARWELSEkrvnleqk 196
Cdd:cd16146 76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 lnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassYFvgalivhaDCFLMRNHTITE-QPMCfqrtTPLI 275
Cdd:cd16146 137 ---------------------------------------------YF--------DDTYYHNGKFVKtEGYC----TDVF 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 276 LQEVASFLKRNKHGPFLLFVSFLHVHIPLITMEN----FLGKSLH----GLYGdNVEEMDWMVGRILDTLDVEGLSNSTL 347
Cdd:cd16146 160 FDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKyldpYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEENTI 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 348 IYFTSDHGGSLENQLGN---------TQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPT 417
Cdd:cd16146 239 VIFMSDNGPAGGVPKRFnagmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLPT 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 418 VVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTMWKVHFVtpVFQPEgagacYgRKV 497
Cdd:cd16146 302 LLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W-RLV 364
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 157266309 498 CPcfgekvvHHDPPLLFDLSRDPSETHILTpASEPVFYQVMERVQQAVWE 547
Cdd:cd16146 365 SP-------KGFQPELYDIENDPGEENDVA-DEHPEVVKRLKAAYEAWWD 406
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-466 |
2.35e-66 |
|
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: 220.93 E-value: 2.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqwtg 117
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 aSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESASDhchHPLHHGFDHFygmpfslmgdCArWELSEKRVNLEQKL 197
Cdd:cd16151 68 -FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEY----------CL-WQLTETGEKYSRPA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 NFLFQVLalvaltlvAGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcFLMRnhtiteqpmcfqrttplilq 277
Cdd:cd16151 132 TPTFNIR--------NGKLLETTEGDYGPDLFAD----------------------FLID-------------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 evasFLKRNKHGPFLLFVSFLHVHIPL----------ITMENFLGKSLHglYGDNVEEMDWMVGRILDTLDVEGLSNSTL 347
Cdd:cd16151 162 ----FIERNKDQPFFAYYPMVLVHDPFvptpdspdwdPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 348 IYFTSDHG--GSLENQLGNTQY-GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGG 424
Cdd:cd16151 236 IIFTGDNGthRPITSRTNGREVrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGA 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 157266309 425 EVPQDRVIDGQDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 466
Cdd:cd16151 307 PLPEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-526 |
1.14e-62 |
|
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: 211.66 E-value: 1.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVsSIGYRvlqwt 116
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHH----PLHHGFDHFYGMpfslmgdcarwelsekrvn 192
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 leqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhaDCFLMRNHTI----TEQPMCF 268
Cdd:cd16034 131 -----------------------------------------------------------ECNHDHNNPHyyddDGKRIYI 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 269 QRTTPLILQEVA-SFLKRNKHG--PFLLFVSF------------------------LHVHIPLITMENF-LGKSLHGLYG 320
Cdd:cd16034 152 KGYSPDAETDLAiEYLENQADKdkPFALVLSWnpphdpyttapeeyldmydpkkllLRPNVPEDKKEEAgLREDLRGYYA 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 321 dNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQYGGwngiykggkgmggwegGIRVPGIFRWPG 397
Cdd:cd16034 232 -MITALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYPG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 398 VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTM--- 474
Cdd:cd16034 295 KIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtd 372
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 157266309 475 -WKvhFVtpvfqpegagacygrkvcpcfgekVVHHDPPLLFDLSRDPSETHIL 526
Cdd:cd16034 373 rYT--YV------------------------RDKNGPWLLFDNEKDPYQLNNL 399
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
38-524 |
1.94e-62 |
|
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: 210.87 E-value: 1.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssiGYRVLqWTG 117
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVI-LAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasdHCHH---PLHHGFDHFYGMpFSLMGDcarwelsekrvnle 194
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY-YGGAED-------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 qklnflfqvlalvaltlvagkltHLIPVSWMPVIWSalsavlllassyfvgalivhaDCFLMRNHTIT-EQPMCFqrTTP 273
Cdd:cd16029 132 -----------------------YYTHTSGGANDYG---------------------NDDLRDNEEPAwDYNGTY--STD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 274 LILQEVASFLKR-NKHGPFLLFVSFLHVHIPL------ITMENFLGKSLHG----LYGDNVEEMDWMVGRILDTLDVEGL 342
Cdd:cd16029 166 LFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLqvppeyADPYEDKFAHIKDedrrTYAAMVSALDESVGNVVDALKAKGM 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 343 SNSTLIYFTSDHGGSLENQLG----------NTQY-GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIGEPT 409
Cdd:cd16029 246 LDNTLIVFTSDNGGPTGGGDGgsnyplrggkNTLWeGG-----------------VRVPA-FVWSPLLPpkRGTVSDGLM 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 410 SLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRgtmwkvhfvtPVFQPEGA 489
Cdd:cd16029 308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDD----------ITRTTGGA 364
|
490 500 510
....*....|....*....|....*....|....*
gi 157266309 490 GACYGRKvcpcfgeKVVHHDPplLFDLSRDPSETH 524
Cdd:cd16029 365 AIRVGDW-------KLIVGKP--LFNIENDPCERN 390
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
38-550 |
1.74e-58 |
|
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: 200.04 E-value: 1.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssIGYRVLQWTg 117
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 asggLPTNETTFAKILKEKGYATGLIGKWHlgLNCESASDHCHHPLHHGFDHFYGMPFslMGDCARWelsEKRVNLEQkl 197
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWDY--ASNAADF---LNRAKKGQ-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 NFLFQvlalvaltlVAGKLTHlipVSWMPVIWSAL----SAVLLlaSSYFVgalivhaDcflmrnhtiteqpmcfqrtTP 273
Cdd:cd16027 143 PFFLW---------FGFHDPH---RPYPPGDGEEPgydpEKVKV--PPYLP-------D-------------------TP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 274 LILQEVASFLkrnkhgpfllfvsflhvhiplitmenflgkslhglygDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 353
Cdd:cd16027 183 EVREDLADYY-------------------------------------DEIERLDQQVGEILDELEEDGLLDNTIVIFTSD 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 HGGSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvID 433
Cdd:cd16027 226 HGMPFPRAKGTLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQ 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 434 GQDLLPLLLG-TAQHSDHEFLMH-------YCERFLHAARWHqrdrgtmwkvhfvtpvfqpegagacYgrkvcpcfgekV 505
Cdd:cd16027 287 GRSFLPLLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK-------------------------Y-----------I 330
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 157266309 506 VHHDPPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 550
Cdd:cd16027 331 RNYMPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
38-423 |
5.08e-58 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 196.49 E-value: 5.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtg 117
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhchhPLHHGFDHFYGmpfslmgdcaRWELSEKRVNLEqkl 197
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG----------RNTGSDLYADPP--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmRNHTITEQPMCF-QRTTPLIL 276
Cdd:pfam00884 132 -----------------------------------------------------------DVPYNCSGGGVSdEALLDEAL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 QevasfLKRNKHGPFLLFVSFLHVHIPL------------ITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSN 344
Cdd:pfam00884 153 E-----FLDNNDKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157266309 345 STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 423
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
448-582 |
1.05e-57 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 189.06 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 448 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 527
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 157266309 528 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 582
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
36-543 |
5.30e-56 |
|
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: 194.67 E-value: 5.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 36 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqw 115
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDhchhplhhGFDHFYGMP---------FSLMGDCARWEL 186
Cdd:cd16031 71 DNNGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFPgqgsyydpeFIENGKRVGQKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 187 SEKRVNLEQKLNFL--------FqvlalvALTlVAGKLTHLipvSWMPViwsalsavlllassyfvgalIVHADcfLMRN 258
Cdd:cd16031 143 YVTDIITDKALDFLkerdkdkpF------CLS-LSFKAPHR---PFTPA--------------------PRHRG--LYED 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 HTITE-----------QPMCFQRTTPLI-LQEVASFLKRNKHGpfllfvsflhvhiplITMENFLGkSLHGlygdnveeM 326
Cdd:cd16031 191 VTIPEpetfddddyagRPEWAREQRNRIrGVLDGRFDTPEKYQ---------------RYMKDYLR-TVTG--------V 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 327 DWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGG-WNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVI 405
Cdd:cd16031 247 DDNVGRILDYLEEQGLADNTIIIYTSDNG----FFLGEHGLFDkRL----------MYEESIRVPLIIRDPRLIKAGTVV 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 406 GEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHS-DHEFLMHYCE--RFLHAARWH--QRDRgtmWK-VHF 479
Cdd:cd16031 313 DALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNVPTHEgvRTER---YKyIYY 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157266309 480 vtpvfqpegagacygrkvcpcfgekvvHHDPPL--LFDLSRDPSETH--ILTPASEPVFYQVMERVQQ 543
Cdd:cd16031 388 ---------------------------YGVWDEeeLYDLKKDPLELNnlANDPEYAEVLKELRKRLEE 428
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
37-524 |
8.55e-54 |
|
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: 188.04 E-value: 8.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEDGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSIGYRVLQW 115
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLN----CESASDH-----------------------CHHPLH---- 164
Cdd:cd16025 78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPDdyysTDDLTDKaieyideqkapdkpfflylafgaPHAPLQapke 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 165 -----HG-FDhfygmpfslMGdcarWE-LSEKRvnLE-QKlnflfqvlalvALTLVAG--KLTHLIPvsWMPViWSALSA 234
Cdd:cd16025 158 widkyKGkYD---------AG----WDaLREER--LErQK-----------ELGLIPAdtKLTPRPP--GVPA-WDSLSP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 235 vlllassyfvgalivhadcflmrnhtitEQPMCFQRttpliLQEV-ASFlkrnkhgpfllfvsflhvhiplitmenflgk 313
Cdd:cd16025 209 ----------------------------EEKKLEAR-----RMEVyAAM------------------------------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 314 slhglygdnVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN---QLGNTQY---------GGwngiykggkgmg 381
Cdd:cd16025 225 ---------VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPgwaNASNTPFrlykqasheGG------------ 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 382 gweggIRVPGIFRWP-GVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV------IDGQDLLPLLLGTAQHSDHEFLm 454
Cdd:cd16025 284 -----IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ- 357
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157266309 455 hYCERFLHAARWHQRdrgtmWKVhfvtpvfqpegagacygrkvcpcfgekVVHHDPPL------LFDLSRDPSETH 524
Cdd:cd16025 358 -YFELFGNRAIRKGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-520 |
6.11e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 172.73 E-value: 6.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRsgmvssIGYrvlqWTG 117
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGgLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhchhplHHGFDHfygmpfslmgdcarwelsekrvnleqkl 197
Cdd:cd16037 71 ADP-YDGDVPSWGHALRAAGYETVLIGKLHFRGEDQ----------RHGFRY---------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhaDcflmRNhtiteqpmcfqrttplILQ 277
Cdd:cd16037 112 ------------------------------------------------------D----RD----------------VTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 EVASFLKRNKH--GPFLLFVSFLHVHIPLITMENFLGKSLHGL---YGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTS 352
Cdd:cd16037 118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 353 DHGgsleNQLG-------NTQYggwngiykggkgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGE 425
Cdd:cd16037 198 DHG----DMLGerglwgkSTMY----------------EESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAP 256
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 426 VPQDRviDGQDLLPLLLGTAQHSDHEFlmhyCErfLHAARwhQRDRGTM-----WK-VHFVtpvfqpegagacygrkvcp 499
Cdd:cd16037 257 PPPDL--DGRSLLPLAEGPDDPDRVVF----SE--YHAHG--SPSGAFMlrkgrWKyIYYV------------------- 307
|
490 500
....*....|....*....|.
gi 157266309 500 cfgekvvhHDPPLLFDLSRDP 520
Cdd:cd16037 308 --------GYPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-547 |
6.20e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 167.01 E-value: 6.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqWTG 117
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 A-SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHC--HHPLHHGFDHFYgmpfslmGDCARWELSEkrvnLE 194
Cdd:cd16033 76 AySRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEETPLDYGFdeYLPVETTIEYFL-------ADRAIEMLEE----LA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 QKlnflfqvlalvaltlvaGKlthliPvsWMpvIWSAlsavlllassyFVGAlivHADCFLmrnhtitEQPMcFQRTTPL 274
Cdd:cd16033 145 AD-----------------DK-----P--FF--LRVN-----------FWGP---HDPYIP-------PEPY-LDMYDPE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 275 ILQEVASF---------LKRNKHGPFLLFVSFLHVHIPLITmeNFLGkslhglygdNVEEMDWMVGRILDTLDVEGLSNS 345
Cdd:cd16033 177 DIPLPESFaddfedkpyIYRRERKRWGVDTEDEEDWKEIIA--HYWG---------YITLIDDAIGRILDALEELGLADD 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 346 TLIYFTSDHGGSLENQlgntqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGE 425
Cdd:cd16033 246 TLVIFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 426 VPQDrvIDGQDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWHQrdrgtmwkvhfvtpVFQPEGagacygr 495
Cdd:cd16033 314 VPPK--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYKY--------------VFNGFD------- 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 157266309 496 kvcpcFGEkvvhhdpplLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWE 547
Cdd:cd16033 369 -----IDE---------LYDLESDPYELNNL--IDDPEYEEILREMRTRLYE 404
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
38-520 |
4.15e-43 |
|
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: 156.97 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 117
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGgLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhCHHPLHHGFDHfygmpfslmgDcarwelsekrvnlEQkl 197
Cdd:cd16032 71 AAE-FPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFDY----------D-------------EE-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpVIWSALSAVLLLAssyfvgalivhadcflmRNHTiteqpmcfqrttplilq 277
Cdd:cd16032 115 -----------------------------VAFKAVQKLYDLA-----------------RGED----------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 evasflKRnkhgPFLLFVSFLHVHIPLITMENFLG----KSLHGLYGdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 353
Cdd:cd16032 132 ------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 HGgsleNQLGntQYGGWngiykggKGMGGWEGGIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV-I 432
Cdd:cd16032 201 HG----DMLG--ERGLW-------YKMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpL 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 433 DGQDLLPLLLGTAQHSDHEFLMHYCErflhaarwhqrdrgtmwkvhfvtpvfqpEGAGAcygrkvcPCF-----GEKVVH 507
Cdd:cd16032 267 DGRSLLPLLEGGDSGGEDEVISEYLA----------------------------EGAVA-------PCVmirrgRWKFIY 311
|
490
....*....|....*
gi 157266309 508 --HDPPLLFDLSRDP 520
Cdd:cd16032 312 cpGDPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-439 |
2.21e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 152.78 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 117
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqkl 197
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgaliVHADCFLMRNHtiteqpmcfqrttplilq 277
Cdd:cd16149 113 ---------------------------------------------------DDAADFLRRRA------------------ 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 evasflKRNKhgPFLLFVSFLHVHIPlitmenflgkslHGlYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGS 357
Cdd:cd16149 124 ------EAEK--PFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFN 182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 358 LenqlgnTQYGGW---------NgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQ 428
Cdd:cd16149 183 M------GHHGIWgkgngtfplN----------MYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPA 246
|
410
....*....|.
gi 157266309 429 DRVIDGQDLLP 439
Cdd:cd16149 247 DPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-439 |
6.45e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 151.93 E-value: 6.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyrvLQWT 116
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIgkwhlglncesaSDHCHHPLHHGFDH--FYGMPFSLMGDCARWELSEkrvnle 194
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDRgfDTFEDFRGQEGDPGEEGDE------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 195 qklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrTTPL 274
Cdd:cd16148 129 ----------------------------------------------------------------------------RAER 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 275 ILQEVASFLKRNKHG-PFLLFVSFLHVHIPLitmenflgkslhgLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 353
Cdd:cd16148 133 VTDRALEWLDRNADDdPFFLFLHYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 354 HGGSLeNQLGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVRLAGGEVPQDrvID 433
Cdd:cd16148 200 HGEEF-GEHGLYWGHGSN----------LYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SD 265
|
....*.
gi 157266309 434 GQDLLP 439
Cdd:cd16148 266 GRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
38-550 |
1.08e-39 |
|
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: 150.87 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqWTG 117
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASggLPTNETTFAKILKEKGYATGLIGKWHL-----GLNCESASDHCHHPLHHGFDHFYGMPFslmgdcARWELSEKRVN 192
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFDPVDRLDE------YPAEDSDTAFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 LEQKLNFL--------FQVLA-------LVAltlvagklthliPVSWMPVI-WSALSAVLllassyfvgalivhadcflm 256
Cdd:cd16028 144 TDRAIEYLderqdepwFLHLSyirphppFVA------------PAPYHALYdPADVPPPI-------------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 257 RNHTITEQpmcfQRTTPLIlqevASFLKRNKHGpfllfvSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDT 336
Cdd:cd16028 192 RAESLAAE----AAQHPLL----AAFLERIESL------SFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDY 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 337 LDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGGwngiykggkGMGGWEGGIRVPGIFRWPGVL---PAGRVIGEPTSLMD 413
Cdd:cd16028 258 LKETGQWDDTLIVFTSDHG----EQLGDHWLWG---------KDGFFDQAYRVPLIVRDPRREadaTRGQVVDAFTESVD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 414 VFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQRDRGTmwkvhfvtpvfQP 486
Cdd:cd16028 325 VMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALGL-----------SP 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157266309 487 EGAGACYGRkvcpcfGE--KVVHHD--PPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 550
Cdd:cd16028 385 DECSLAVIR------DErwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSWRM 444
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
36-450 |
1.53e-39 |
|
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: 150.03 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 36 SRPNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqW 115
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 TGASGglptNETTFAKILKEKGYATGLIGKWHlglncesasdhchhplHHGFDHFYGMPFSlmgdcarWELSEKRVNLEQ 195
Cdd:cd16030 76 RKVAP----DAVTLPQYFKENGYTTAGVGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 196 KLNFLFQVLALVALTLVAGKLTHLIPV--SWMPVIWSALSAVLLLAS------SYFVGA--------LIVHADCFLMRNH 259
Cdd:cd16030 129 YPPGKLCPGKKGGKGGGGGPAWEAADVpdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 260 TITEQPMCFQRT-TPLI----LQEVasflkRNKHGPFLLFVSFLHVHIPlitmENFLGKSLHGLYGdNVEEMDWMVGRIL 334
Cdd:cd16030 209 ESIPLPNPFDPIdLPEVawndLDDL-----PKYGDIPALNPGDPKGPLP----DEQARELRQAYYA-SVSYVDAQVGRVL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 335 DTLDVEGLSNSTLIYFTSDHGGslenQLGntQYGGW---------NgiykggkgmggweggiRVPGIFRWPGVLPAGRVI 405
Cdd:cd16030 279 DALEELGLADNTIVVLWSDHGW----HLG--EHGHWgkhtlfeeaT----------------RVPLIIRAPGVTKPGKVT 336
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 157266309 406 GEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLLLGTAQHSDH 450
Cdd:cd16030 337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKD 379
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
36-531 |
3.18e-38 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 147.12 E-value: 3.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 36 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssiGYrvlq 114
Cdd:PRK13759 5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 115 wtgASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchHP--LHHGFDHfygmpfSLMGDcarWELSEKRVN 192
Cdd:PRK13759 77 ---GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 LEQKLNFLFQVLALVALTLVaGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcflmRNHTITEQpmcfQRTT 272
Cdd:PRK13759 133 DKSQFDFVSDYLAWLREKAP-GKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 PLILQEVASFLKR-NKHGPFLLFVSFLHVHIPLITMENFL-------------------------GKSLHGLYGD----- 321
Cdd:PRK13759 183 NWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeey 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 322 ----------NVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ-------YGGwngiykggkgmggwe 384
Cdd:PRK13759 263 arraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG--------------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 385 gGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-YCER 459
Cdd:PRK13759 324 -SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYS 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157266309 460 FLHaarWHQRDR-GTMWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSRDPSETHILTPASE 531
Cdd:PRK13759 401 SDN---YLTDGKwKYIW--FSQTGEEQ---------------------------LFDLKKDPHELHNLSPSEK 441
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-543 |
2.34e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 142.37 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRvlqwt 116
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 gASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqk 196
Cdd:cd16152 71 -NGIPLPADEKTLAHYFRDAGYETGYVGKWHL------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 lnflfqvlalvaltlvAGklthlipvswmpviwsalsavlllassYFVGALIVHADCFLMrnhtiteqpmcfqrttplil 276
Cdd:cd16152 102 ----------------AG---------------------------YRVDALTDFAIDYLD-------------------- 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 qevasflKRNKHGPFLLFVSFLHVHiplitMEN------------------FLGKSLHGLYGDN----------VEEMDW 328
Cdd:cd16152 119 -------NRQKDKPFFLFLSYLEPH-----HQNdrdryvapegsaerfanfWVPPDLAALPGDWaeelpdylgcCERLDE 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 329 MVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlgNTQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEP 408
Cdd:cd16152 187 NVGRIRDALKELGLYDNTIIVFTSDHGCHFRTR--NAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEEL 252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 409 TSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCE----RFLHAARW----HQRDRGtmWKVHFV 480
Cdd:cd16152 253 VSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISEsqvgRAIRTDRWkysvAAPDKD--GWKDSG 328
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157266309 481 TPVFQPEgagacygrkvcpcfgekvvhhdppLLFDLSRDPSETHILtpASEPVFYQVMERVQQ 543
Cdd:cd16152 329 SDVYVED------------------------YLYDLEADPYELVNL--IGRPEYREVAAELRE 365
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-540 |
1.79e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 134.23 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 36 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssigy 110
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 111 rvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLnCESASDHCHHP--------LHHGFDH---FYGMPFSLMg 179
Cdd:cd16155 74 ------GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF-ADAAIEFLEEYkdgdkpffMYVAFTAphdPRQAPPEYL- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 180 dcarwelseKRVNLEqklnflfqvlalvaltlvagklTHLIPVSWMPViwsalsavlllassY-FVGALIVHADcflmrn 258
Cdd:cd16155 146 ---------DMYPPE----------------------TIPLPENFLPQ--------------HpFDNGEGTVRD------ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 259 htitEQPMCFQRTTplilQEVASFLKRNkhgpfllfvsflhvhiplitmenflgkslhglYGdNVEEMDWMVGRILDTLD 338
Cdd:cd16155 175 ----EQLAPFPRTP----EAVRQHLAEY--------------------------------YA-MITHLDAQIGRILDALE 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 339 VEGLSNSTLIYFTSDHG------GSLENQlgNTQYGGWngiykggkgmggweggiRVPGIFRWPGVlPAGRVIGEPTSLM 412
Cdd:cd16155 214 ASGELDNTIIVFTSDHGlavgshGLMGKQ--NLYEHSM-----------------RVPLIISGPGI-PKGKRRDALVYLQ 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 413 DVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMhycerFLHAARWHQRDRgtmWKVHFVTPvfqpegaga 491
Cdd:cd16155 274 DVFPTLCELAGIEIPES--VEGKSLLPVIRGeKKAVRDTLYGA-----YRDGQRAIRDDR---WKLIIYVP--------- 334
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 157266309 492 cygrkvcpcfGEKVVhhdppLLFDLSRDPSETHILtpASEPVFYQVMER 540
Cdd:cd16155 335 ----------GVKRT-----QLFDLKKDPDELNNL--ADEPEYQERLKK 366
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
38-422 |
1.22e-30 |
|
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: 119.83 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQwT 116
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPEL-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnLEQK 196
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------------------LLKA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 LNFLfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplil 276
Cdd:cd00016 112 IDET---------------------------------------------------------------------------- 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 277 qevasflkrNKHGPFLLFVSFLHVHIPLitmenFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 356
Cdd:cd00016 116 ---------SKEKPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157266309 357 SLENqLGNTqyggwngiYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLA 422
Cdd:cd00016 182 IDKG-HGGD--------PKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-524 |
2.07e-30 |
|
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: 123.50 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssiGYRVLQWT 116
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 117 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHChhplhhgfdhfygmpfslmgdcarwelSEKRVNLEQK 196
Cdd:cd16150 74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC---------------------------DSDEACVRTA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 197 LNFLFQvlalvaltlvagkltHLIPVSWmpviwsalsaVLLLASSY----FVgaliVHADCFLMrnhtITEQPMCFQRTT 272
Cdd:cd16150 122 IDWLRN---------------RRPDKPF----------CLYLPLIFphppYG----VEEPWFSM----IDREKLPPRRPP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 PLILQEVASFLK-RNKHGpfllFVSflhvhiplITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFT 351
Cdd:cd16150 169 GLRAKGKPSMLEgIEKQG----LDR--------WSEERW--RELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFF 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 352 SDHG-------------GSLENQLgntqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTV 418
Cdd:cd16150 235 SDHGdytgdyglvekwpNTFEDCL------------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPPTL 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 419 VRLAGgeVPQDRVIDGQDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHqrdrgtMWKVHFVTPVFQPEG----AGAC 492
Cdd:cd16150 290 LDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQA------MEGGHGPYDLKWPRLlqqeEPPE 357
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 157266309 493 YGRKVcpcfgeKVVHHD---------PPLLFDLSRDPSETH 524
Cdd:cd16150 358 HTKAV------MIRTRRykyvyrlyePDELYDLEADPLELH 392
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
38-441 |
6.33e-29 |
|
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: 120.18 E-value: 6.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 117
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 aSGGLPTNETTFAKILKEKGYATGLIGKWHL------GLN-CESASDHchhplhhgfDHFYGMPFSLMgdcarwELSEKR 190
Cdd:cd16156 71 -CMALGDNVKTIGQRLSDNGIHTAYIGKWHLdggdyfGNGiCPQGWDP---------DYWYDMRNYLD------ELTEEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 191 VnleqklnflfqvlalvaltlvagklthlipvswmpVIWSalsavLLLASSYfvgalivhadcflmrNHTITEQPMCFQR 270
Cdd:cd16156 135 R-----------------------------------RKSR-----RGLTSLE---------------AEGIKEEFTYGHR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 271 TTPLILQevasFLKRNKHGPFLLFVSFLHVHIPLI------TM-------------ENFLGKSLH------GLYGDNVEE 325
Cdd:cd16156 160 CTNRALD----FIEKHKDEDFFLVVSYDEPHHPFLcpkpyaSMykdfefpkgenayDDLENKPLHqrlwagAKPHEDGDK 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 326 M--------------DWMVGRILDTLDvEGLSNSTLIYfTSDHGGSLENQL----GNTQYggwngiykggkgmggwEGGI 387
Cdd:cd16156 236 GtikhplyfgcnsfvDYEIGRVLDAAD-EIAEDAWVIY-TSDHGDMLGAHKlwakGPAVY----------------DEIT 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 157266309 388 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLL 441
Cdd:cd16156 298 NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
37-435 |
1.44e-28 |
|
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: 117.65 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSIGYRV 112
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 113 LQWTGAsgglptNETTFAKILKEKGYATGLIGKWhlgLN-CESASDHCHHPLhhGFDHFYGMPFslmgdcarwelsekrv 191
Cdd:cd16147 77 FWQNGL------ERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVG---------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 192 nleqklNFLFQVLALVALTLVAGklthliPVSWmpviwsalsavlllASSYFvgalivhadcflmrnhtiteqpmcfqrt 271
Cdd:cd16147 130 ------NSTYYNYTLSNGGNGKH------GVSY--------------PGDYL---------------------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 272 TPLILQEVASFLKR--NKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYG---------------------DNVE 324
Cdd:cd16147 156 TDVIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTpaprYANLFPNVTAPPRPPpnnpdvsdkphwlrrlpplnpTQIA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 325 EMDW--------------MVGRILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQ-YggwngiykggkgmggwEGG 386
Cdd:cd16147 236 YIDElyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHRLPPGKRTpY----------------EED 299
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 157266309 387 IRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQ 435
Cdd:cd16147 300 IRVPLLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-437 |
6.53e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 113.24 E-value: 6.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 37 RPNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVS 106
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 107 SIGYrvlqWTGASGGLPtnetTFAKILKEKGYATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwel 186
Cdd:cd16153 81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH--------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 187 sekrvnLEQKLNFLFQvlALVALTLVAGKlthlipVSWMPviwsalsavlllassyfvgalivhadcflmrnhtiteqpm 266
Cdd:cd16153 114 ------LEAFQRYLKN--ANQSYKSFWGK------IAKGA---------------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 267 cfqrttplilqevasflKRNKhgPFLLFVSFLHVHIPLITMENFLGK-SLHGL--YGDNveemdwMVGRILDTLDVEGLS 343
Cdd:cd16153 140 -----------------DSDK--PFFVRLSFLQPHTPVLPPKEFRDRfDYYAFcaYGDA------QVGRAVEAFKAYSLK 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 344 N---STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmggweGGIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTV 418
Cdd:cd16153 195 QdrdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTL 261
|
410
....*....|....*....
gi 157266309 419 VRLAGGEVPQDRVIDGQDL 437
Cdd:cd16153 262 LAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-448 |
5.92e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 109.75 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSIGYRVLQw 115
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 116 tgasgglpTNETTFAKILKE---KGYATGLIGKWHLGlNCESasdhcHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVN 192
Cdd:cd16154 78 --------SEETLLQLLIKDattAGYSSAVIGKWHLG-GNDN-----SPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 193 LEQKlnflfqvlalvalTLVAGKLTHLiPVSWmpviwsalsavlllassyfvgalivhadcflmrnhtITEQpmcfqrTT 272
Cdd:cd16154 144 TNST-------------EYATTKLTNL-AIDW------------------------------------IDQQ------TK 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 273 P--LILQEVASflkrnkHGPFllfvsflhvHIPLITMENflgKSLHGLY---GDN--------VEEMDWMVGRILDTLDV 339
Cdd:cd16154 168 PwfLWLAYNAP------HTPF---------HLPPAELHS---RSLLGDSadiEANprpyylaaIEAMDTEIGRLLASIDE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 340 EGLSNsTLIYFTSDHG--GSLENQLGNTQY-------GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPTS 410
Cdd:cd16154 230 EEREN-TIIIFIGDNGtpGQVVDLPYTRNHakgslyeGG-----------------INVPLIVSGAGV---ERANERESA 288
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 157266309 411 LM---DVFPTVVRLAGGEVPQdrVIDGQDLLPLLLGTAQHS 448
Cdd:cd16154 289 LVnatDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNAST 327
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-456 |
8.56e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 108.06 E-value: 8.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYR 111
Cdd:cd16035 1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 112 VlQWTgasggLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrv 191
Cdd:cd16035 75 M-QPL-----LSPDVPTLGHMLRAAGYYTAYKGKWHL------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 192 nleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllaSSYFVGALivhadcflMRNHTITEQPMCFqrt 271
Cdd:cd16035 106 ------------------------------------------------SGAAGGGY--------KRDPGIAAQAVEW--- 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 272 tpliLQEVASflKRNKHGPFLLFVSFL--H-VHIPLITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLI 348
Cdd:cd16035 127 ----LRERGA--KNADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIV 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 349 YFTSDHG------GSLENqlGNTQYGgwngiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLA 422
Cdd:cd16035 199 VFTSDHGemggahGLRGK--GFNAYE----------------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLA 260
|
410 420 430
....*....|....*....|....*....|....*....
gi 157266309 423 GGEVPQDRVID----GQDLLPLLLGTAQHSDHE-FLMHY 456
Cdd:cd16035 261 GVDAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
38-521 |
5.20e-15 |
|
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: 76.81 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyRVLQWTG 117
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESWN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 118 ASGGLPTNETTFAKILKEKGYATGLIGKwhlgLNCESAsdhchhplHHgfdhfygmpfSLMGDCARWElsekrvnleQKL 197
Cdd:cd16171 70 NYKGLDPNYPTWMDRLEKHGYHTQKYGK----LDYTSG--------HH----------SVSNRVEAWT---------RDV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 198 NFLFQVLALVALTLVAGKLTHLIpvswmpviwsalsavlllassyfvgalivhadcfLMRNHTITEqpmcfqRTTPLILQ 277
Cdd:cd16171 119 PFLLRQEGRPTVNLVGDRSTVRV----------------------------------MLKDWQNTD------KAVHWIRK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 278 EVASFLKrnkhgPFLLFVSFLHVH-IPLITM-ENFLG-KSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 354
Cdd:cd16171 159 EAPNLTQ-----PFALYLGLNLPHpYPSPSMgENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDH 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 355 GgslENQLGNTQYggwngiykggKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDG 434
Cdd:cd16171 234 G---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 435 QDLLPLLLGTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTMWKvhFVTpvfqpegagacYGRkvcpcfGE 503
Cdd:cd16171 298 YSLLPLLSESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YAD------GN 352
|
490
....*....|....*...
gi 157266309 504 KVvhhdPPLLFDLSRDPS 521
Cdd:cd16171 353 SV----PPQLFDLSKDPD 366
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
26-438 |
6.52e-09 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 58.51 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 26 APSASSDISASRPNILLLM----ADDLgigdIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVR 101
Cdd:COG1368 223 RPTPNPFGPAKKPNVVVILlesfSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 102 SG-MVSSIGYRVLQwtgasgglptnetTFAKILKEKGYATgligkwhlglncesasdHCHHP------------LHHGFD 168
Cdd:COG1368 299 GGsPYKRPGQNNFP-------------SLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFD 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 169 HFYGMPfslmgdcarwELSEKRVNleqklnflfqvlalvaltlvagklthlipvSWmpviwsalsavlllassyfvGAli 248
Cdd:COG1368 349 EFYDRE----------DFDDPFDG------------------------------GW--------------------GV-- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 249 vhADcflmrnhtiteQPMcfqrttpliLQEVASFLKRNKhGPFLLFVsflhvhiplITMEN---F-----------LGKS 314
Cdd:COG1368 367 --SD-----------EDL---------FDKALEELEKLK-KPFFAFL---------ITLSNhgpYtlpeedkkipdYGKT 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 315 LHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQYggwngiykggkgmGGWEGGIRVPGIFR 394
Cdd:COG1368 415 TLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSP---GKTDY-------------ENPLERYRVPLLIY 478
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 157266309 395 WPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIdGQDLL 438
Cdd:COG1368 479 SPG-LKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
256-438 |
1.84e-08 |
|
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: 57.22 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 256 MRNHTITEQPMCFQRTTpLILQEVASFL-KRNKHGPFLLFVSFLHVHI------------------PLITMENFLGKSLH 316
Cdd:COG3083 348 VSLPRLHTPGGPAQRDR-QITAQWLQWLdQRDSDRPWFSYLFLDAPHAysfpadypkpfqpsedcnYLALDNESDPTPFK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 317 GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSL----ENQLG-NTQYGGWNgiykggkgmggweggIRVPG 391
Cdd:COG3083 427 NRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGhNSNFSRYQ---------------LQVPL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157266309 392 IFRWPGVLPagRVIGEPTSLMDVFPTVV-RLAGGEVPqdrVID---GQDLL 438
Cdd:COG3083 492 VIHWPGTPP--QVISKLTSHLDIVPTLMqRLLGVQNP---ASDysqGEDLF 537
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
38-423 |
3.41e-08 |
|
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: 55.00 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 38 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSIGYRvl 113
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 114 qwtgasgglPTNETTFAKILKEKGYATGLIgkwhlglncesasdHCHHP---------LHHGFDHFYgmpfslmgDCARW 184
Cdd:cd16015 77 ---------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFY--------DLEDF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 185 ELSEKRVNleqklnflfqvlalvaltlvagklthlipvSWMpviwsalsavlllassyfvgalivhadcflmrnhtITEQ 264
Cdd:cd16015 126 PDDEKETN------------------------------GWG-----------------------------------VSDE 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 265 PMcfqrttpliLQEVASFLKRNKHGPFLLFVsflhvhiplITMENflgkslHGLYGDN---------------------- 322
Cdd:cd16015 141 SL---------FDQALEELEELKKKPFFIFL---------VTMSN------HGPYDLPeekkdeplkveedktelenyln 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 323 -VEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPa 401
Cdd:cd16015 197 aIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK- 261
|
410 420
....*....|....*....|..
gi 157266309 402 GRVIGEPTSLMDVFPTVVRLAG 423
Cdd:cd16015 262 PKKIDRVGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
19-193 |
1.67e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 53.60 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 19 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGR 97
Cdd:COG1524 5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157266309 98 YPVRSGMVSSIGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIGKWHLGlncESASDHCHHPLHH-G 166
Cdd:COG1524 80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdG 156
|
170 180
....*....|....*....|....*....
gi 157266309 167 FDHFYGMPFS--LMGDCARWELSEKRVNL 193
Cdd:COG1524 157 RKPLLGNPAAdrWIAAAALELLREGRPDL 185
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
62-106 |
3.94e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 39.71 E-value: 3.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 157266309 62 RTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVS 106
Cdd:pfam01663 19 LTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVG 64
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
321-355 |
9.53e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 38.56 E-value: 9.53e-03
10 20 30
....*....|....*....|....*....|....*
gi 157266309 321 DNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG 355
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| |
