|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
21-543 |
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: 751.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 100
Cdd:cd16159 2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAHweLSEKRVDLEQKL 180
Cdd:cd16159 82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSFDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 NFLFQVLALVTLTLAAGKFMHLISISWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTITEQPMRFQRVTPLI 258
Cdd:cd16159 160 LFPLLTAFVLITALTIFLLLYLGAVSKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEVVEQPMSLENLTQRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 259 LQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 338
Cdd:cd16159 238 TKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 339 GSLENQFANSQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGR 418
Cdd:cd16159 318 GHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 419 DLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTLWKVHFVTPVFQPEGAGaCYGRKVCPCSGEKVVHHDPPLLFD 498
Cdd:cd16159 398 DLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1864524947 499 LSRDPSEAHVLTPASEPlFYHVMERVQQAVWEHQQTLSPVALQLD 543
Cdd:cd16159 477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
21-510 |
2.30e-151 |
|
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: 440.46 E-value: 2.30e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgYRVLQWTG 100
Cdd:cd16026 2 PNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagDH-CHHPLHHGFDYFYGMPLSMTGDCAHWELSEKRVDLeqk 179
Cdd:cd16026 77 SKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 180 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadCFLMRNHTITEQPMRFQRVTPLIL 259
Cdd:cd16026 147 --------------------------------------------------------PPLMENEEVIEQPADQSSLTQRYT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 260 QEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG 339
Cdd:cd16026 171 DEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 340 SLENQFAN-----------SQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGG 407
Cdd:cd16026 251 WLEYGGHGgsagplrggkgTTWeGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 408 EVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGacygrkvcpcsGEK 487
Cdd:cd16026 314 PLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG-----------GLD 376
|
490 500
....*....|....*....|...
gi 1864524947 488 VVHHDPPLLFDLSRDPSEAHVLT 510
Cdd:cd16026 377 PTKLEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
21-528 |
2.57e-131 |
|
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: 391.02 E-value: 2.57e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsvGYRV-LQWT 99
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 gaSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDyFYGMPLSMTGdcaHWELSekrvdleqk 179
Cdd:cd16160 80 --IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGTNLPFTN---SWACD--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 180 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllTTSYFagalIVHAD---CFLMRNHTITEQPMRFQRVTP 256
Cdd:cd16160 145 ------------------------------------------DTGRH----VDFPDrsaCFLYYNDTIVEQPIQHEHLTE 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 257 LILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 336
Cdd:cd16160 179 TLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 337 HG------------GSLENQFANSQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTVVQL 404
Cdd:cd16160 259 HGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 405 AGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtlWKVHFVT---PVFQPEGAGACYGRKVC 481
Cdd:cd16160 321 AGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGGGPLS 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1864524947 482 P------CSGEKVVHHDPPLLFDLSRDPSEAHVLTPAsepLFYHVMERVQQAV 528
Cdd:cd16160 394 DyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPS---VYEHMLEAVEKLI 443
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
21-565 |
3.04e-97 |
|
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: 304.37 E-value: 3.04e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqwTG 100
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAgdhcHHPLHHGFDYFYGMPLSMT-GDCAHwelsekrvdleqk 179
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHDqGPCQN------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 180 lnflfqvlalvtltlaagkfmhlisiswmpviwsalLAVFLLTTSYFAGALIVHADCFLMRNHTITEQPMRFQRVTPLIL 259
Cdd:cd16158 140 ------------------------------------LTCFPPNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 260 QEVKSFL----KRNKlgPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFAS 335
Cdd:cd16158 184 KFAKDFIadnaKEGK--PFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 336 DHGGSLENQfansQYGGwNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVQLAGGEVPqDRVI 415
Cdd:cd16158 262 DNGPSTMRK----SRGG-NAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 416 DGRDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdrgtlWKVHFVT---PVFQPEGAGACYGRKvcpcsgeKV 488
Cdd:cd16158 335 DGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCHPSA-------EL 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 489 VHHDPPLLFDLSRDPSEAHVLTPASEplFYHVMERVQQAVWEHQQTLSPVALQLDSLGNlwrPWLQPC----CGPFPLCW 564
Cdd:cd16158 402 TSHDPPLLFDLSQDPSENYNLLGLPE--YNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPCckpgCTPKPSCC 476
|
.
gi 1864524947 565 C 565
Cdd:cd16158 477 Q 477
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-505 |
1.54e-94 |
|
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: 293.67 E-value: 1.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEFGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvSSVGyrvlq 97
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-TTVG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 98 WTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncESAGdhcHHPLHHGFDYFYGMPLsmtgdcahwelsekrvdle 177
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDG---RLPTDHGFDEFYGNLY------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 178 qklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnHTITEQpmrfqrvtpl 257
Cdd:cd16142 129 ----------------------------------------------------------------HTIDEE---------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 258 ILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGKS-AHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFA 334
Cdd:cd16142 135 IVDKAIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSsGKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 335 SDHGGSLeNQFANSQY------------GGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVV 402
Cdd:cd16142 215 TDNGPEQ-DVWPDGGYtpfrgekgttweGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLA 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 403 QLAGGEVP------QDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVtpVFQPEGAGACY 476
Cdd:cd16142 277 ALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGE 348
|
490 500
....*....|....*....|....*....
gi 1864524947 477 GRKVCPCsgekvvhhdpPLLFDLSRDPSE 505
Cdd:cd16142 349 PFYVLTF----------PLIFNLRRDPKE 367
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
2-507 |
6.18e-91 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 285.23 E-value: 6.18e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 2 LSVLLSLAPSASSDVSASWPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRY 81
Cdd:COG3119 5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 82 PVRSGMVSSVGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesagdhchhplhhgfdyfygmplsmt 161
Cdd:COG3119 85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 162 gdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrn 241
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 242 htiteqpmrfqrvTPLILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGK----------------------- 296
Cdd:COG3119 130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 297 SAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQ-FA---NSQY-GGwngiykggkgmggweggIR 371
Cdd:COG3119 197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHgLRggkGTLYeGG-----------------IR 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 372 VPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQ 451
Cdd:COG3119 260 VPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTG 337
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1864524947 452 RdrgtlWKVHFvtpvfqpegagaCYGRKvcpcsgekvvhhDPPLLFDLSRDPSEAH 507
Cdd:COG3119 338 R-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
21-510 |
2.36e-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: 283.21 E-value: 2.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRvlqwt 99
Cdd:cd16161 2 PNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 gASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGdcahwELSEKRVDleqk 179
Cdd:cd16161 77 -SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFSHDS-----SLADRYAQ---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 180 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyFAGAlivhadcFLMRNHTITEqpmrfqrvtplil 259
Cdd:cd16161 141 ----------------------------------------------FATD-------FIQRASAKDR------------- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 260 qevksflkrnklgPFLLLVSFLHVHIPLITTKNFLGKSAH-GLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 338
Cdd:cd16161 155 -------------PFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNG 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 339 ---------GSLENQFANSQyGGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEV 409
Cdd:cd16161 222 pwevkcelaVGPGTGDWQGN-LGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASL 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 410 PQDRVIDGRDLLPLLLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtlWKVHFVTpvfqpEGAGACYGRKvCPcs 484
Cdd:cd16161 296 PPGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALACCGST-GP-- 360
|
490 500
....*....|....*....|....*.
gi 1864524947 485 gekVVHHDPPLLFDLSRDPSEAHVLT 510
Cdd:cd16161 361 ---KLYHDPPLLFDLEVDPAESFPLT 383
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-507 |
3.55e-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: 293763 [Multi-domain] Cd Length: 421 Bit Score: 279.04 E-value: 3.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGM--VSSVGYRVLQW 98
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 99 TGA-----SGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGmplsmtGDCAHwelsekr 173
Cdd:cd16144 81 TKLipppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG------GTGNG------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 174 vdleqklnflfqvlalvtltlaAGKfmhlisiswmpviwsallavfllttSYFAGALIVHADCFLmrnhtITEQPMRFQR 253
Cdd:cd16144 142 ----------------------GPP-------------------------SYYFPPGKPNPDLED-----GPEGEYLTDR 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 254 VTplilQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTK----NFLGKSAHGLYGDN-------VEEMDWMVGQILDALDT 322
Cdd:cd16144 170 LT----DEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPelieKYEKKKKGLRKGQKnpvyaamIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 323 EGLTNSTLIYFASDHGG-SLENQFANSQY-----------GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGE 390
Cdd:cd16144 246 LGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRWPGVIKPGSVSDV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 391 PTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMhycerflhaarWHQrdrgtlwkvhfvtPVFQPE 470
Cdd:cd16144 309 PVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALF-----------WHF-------------PHYHGQ 364
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1864524947 471 GAGacygrkvcPCS----GE-KVVHH---DPPLLFDLSRDPSEAH 507
Cdd:cd16144 365 GGR--------PASairkGDwKLIEFyedGRVELYNLKNDIGETN 401
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-507 |
6.51e-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: 277.16 E-value: 6.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVgyrvlqWT 99
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV------LG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 GASGGL-PTNETTFAKILKEKGYATGLIGKWHLGLN-CESAGDHCHH---------------PLHHGFDYFYGMPLSmtg 162
Cdd:cd16143 75 GFSPPLiEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwKKKDGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPAS--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 163 dcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnh 242
Cdd:cd16143 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 243 titeqpmrfqRVTPLILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDAL 320
Cdd:cd16143 152 ----------EVLPTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDAL 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 321 DTEGLTNSTLIYFASDHGGSLENQF---------ANSQY---------GGwngiykggkgmggweggIRVPGIFRWPGVL 382
Cdd:cd16143 222 KELGLAENTLVIFTSDNGPSPYADYkelekfghdPSGPLrgmkadiyeGG-----------------HRVPFIVRWPGKI 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 383 PAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTLWKVhf 462
Cdd:cd16143 285 PAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL-- 356
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1864524947 463 vtpVFQPEGAGACYGRKvcpcsgeKVVHHDPP-LLFDLSRDPSEAH 507
Cdd:cd16143 357 ---IDGTGSGGFSYPRG-------KEKLGLPPgQLYNLSTDPGESN 392
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
21-543 |
2.79e-84 |
|
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: 270.11 E-value: 2.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 100
Cdd:cd16157 2 PNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 AS--GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsagdhcHHPLHHGFDYFYGMPlsmtgDCaHWelseKRVDLEQ 178
Cdd:cd16157 82 QNivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NC-HF----GPYDNKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 179 KLNflfqvLALVTLTLAAGKFMHLISIswmpviwsallavfllttsyfagalivhadcflmrNHTITEQpmrfqRVTPLI 258
Cdd:cd16157 146 YPN-----IPVYRDWEMIGRYYEEFKI-----------------------------------DKKTGES-----NLTQIY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 259 LQEVKSFLKR--NKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 336
Cdd:cd16157 181 LQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 337 HGGSLenqFANSQYGGWNGIYKGGKGMGGWEGgIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVID 416
Cdd:cd16157 261 NGAAL---ISAPEQGGSNGPFLCGKQTTFEGG-MREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAID 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 417 GRDLLPLLLgtAQHSDHEFLMHYCERFLHAARwhqrdRGtLWKVHFVT----PVFQPEGAGACYGRKVCPCSGEKVVHH- 491
Cdd:cd16157 337 GIDLLPVLL--NGKEKDRPIFYYRGDELMAVR-----LG-QYKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQTDHt 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1864524947 492 DPPLLFDLSRDPSEAHVLTPASePLFYHVMERVQQAVWEHQQTLSPVALQLD 543
Cdd:cd16157 409 KLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-507 |
1.04e-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: 246.35 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyRVLQWTG 100
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESAGdhchHPLHHGFDYFYGmplsmtgdcahwelsekrvdleqkl 180
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGP-GTPG----HPTKQGFDYFYG------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nFLFQVLAlvtltlaagkfmHlisiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-------EQPMRFQR 253
Cdd:cd16145 125 -YLDQVHA------------H----------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 254 VTPLILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTK---NFLGKSAHGLYGDN------------VEEMDWMVGQILD 318
Cdd:cd16145 170 SHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDdgpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 319 ALDTEGLTNSTLIYFASDHGGSLE------NQFANSQ----------Y-GGwngiykggkgmggweggIRVPGIFRWPGV 381
Cdd:cd16145 250 LLKELGIDENTLVVFTSDNGPHSEggsehdPDFFDSNgplrgykrslYeGG-----------------IRVPFIARWPGK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 382 LPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdrgtl 457
Cdd:cd16145 313 IPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG------ 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1864524947 458 WKVhfvtpVFQPEGAGacygrkvcpcsgekvvhhdPPLLFDLSRDPSEAH 507
Cdd:cd16145 383 WKA-----VRHGKKDG-------------------PFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
21-419 |
2.18e-71 |
|
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: 228.86 E-value: 2.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssvgyrVLQWTG 100
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHlglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqkl 180
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilQ 260
Cdd:cd16022 103 -------------------------------------------------------------------------------D 103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 EVKSFLKRN-KLGPFLLLVSFLHVHIPLIttknflgksahglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG 339
Cdd:cd16022 104 EAIDFIERRdKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 340 SLENQfaNSQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRD 419
Cdd:cd16022 171 MLGDH--GLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-449 |
7.74e-67 |
|
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: 221.70 E-value: 7.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqwtg 100
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 aSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESAGDhchHPLHHGFDYFygmplsmtgdCAhWELSEKRVDLEQKL 180
Cdd:cd16151 68 -FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEY----------CL-WQLTETGEKYSRPA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 NFLFQVLALVTLTLAAGKFmhlisiswMPVIWSAllavfllttsyfagalivhadcFLMRnhtiteqpmrfqrvtplilq 260
Cdd:cd16151 132 TPTFNIRNGKLLETTEGDY--------GPDLFAD----------------------FLID-------------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 evksFLKRNKLGPFLLLVSFLHVHIPLITT----------KNFLGKSAHglYGDNVEEMDWMVGQILDALDTEGLTNSTL 330
Cdd:cd16151 162 ----FIERNKDQPFFAYYPMVLVHDPFVPTpdspdwdpddKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 331 IYFASDHGGSLE-NQFANSQY--GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGG 407
Cdd:cd16151 236 IIFTGDNGTHRPiTSRTNGREvrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGA 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1864524947 408 EVPQDRVIDGRDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 449
Cdd:cd16151 307 PLPEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
21-507 |
6.74e-66 |
|
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: 220.11 E-value: 6.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSVGYRVLqwt 99
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEkrvdleqk 179
Cdd:cd16146 76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 180 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsYFagalivhaDCFLMRNHTI--TEQpmrFqrVTPL 257
Cdd:cd16146 137 ---------------------------------------------YF--------DDTYYHNGKFvkTEG---Y--CTDV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 258 ILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNF--------LGKSAHGLYGdNVEEMDWMVGQILDALDTEGLTNST 329
Cdd:cd16146 159 FFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIENIDDNVGRLLAKLKELGLEENT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 330 LIYFASDHG--GSLENQF-AN------SQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFP 399
Cdd:cd16146 238 IVIFMSDNGpaGGVPKRFnAGmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 400 TVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTLWKVHFVtpVFQPEgagacYgRK 479
Cdd:cd16146 301 TLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W-RL 363
|
490 500
....*....|....*....|....*...
gi 1864524947 480 VCPcsgekvvHHDPPLLFDLSRDPSEAH 507
Cdd:cd16146 364 VSP-------KGFQPELYDIENDPGEEN 384
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
21-509 |
1.17e-61 |
|
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: 208.56 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMVSSVGyrvlqWTG 100
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGMQHGVI-----LAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdHCHH---PLHHGFDYFYGMPLSMTGdcaHWelsekrvdle 177
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGYYGGAED---YY---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 178 qklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-EQPMRFqrVTP 256
Cdd:cd16029 134 ----------------------------------------------THTSGGANDYGNDDLRDNEEPAwDYNGTY--STD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 257 LILQEVKSFLKR-NKLGPFLLLVSFLHVHIPLITTKNFL----GKSAHGLYGD------NVEEMDWMVGQILDALDTEGL 325
Cdd:cd16029 166 LFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYAdpyeDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKGM 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 326 TNSTLIYFASDHGGSLENQFANSQY-----------GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIGEPT 392
Cdd:cd16029 246 LDNTLIVFTSDNGGPTGGGDGGSNYplrggkntlweGG-----------------VRVPA-FVWSPLLPpkRGTVSDGLM 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 393 SLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRGTLWKVHfvtpvfqpegA 472
Cdd:cd16029 308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDDITRTTGG----------A 364
|
490 500 510
....*....|....*....|....*....|....*..
gi 1864524947 473 GACYGRKvcpcsgeKVVHHDPplLFDLSRDPSEAHVL 509
Cdd:cd16029 365 AIRVGDW-------KLIVGKP--LFNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-507 |
1.01e-58 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 200.87 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqwtg 100
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 asggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHH----PLHHGFDYFYGMplsmtgDCAH-------WEL 169
Cdd:cd16034 75 ----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------ECNHdhnnphyYDD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 170 SEKRVDLEQklnflfqvlalvtltlaagkfmhlisisWMPvIWSALLAVfllttSYfagalivhadcflMRNHTITEQP- 248
Cdd:cd16034 145 DGKRIYIKG----------------------------YSP-DAETDLAI-----EY-------------LENQADKDKPf 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 249 ----------MRFQRVtPlilQEVKSFLKRNKLgpflllvsFLHVHIPLIT-TKNFLGKSAHGLYGdNVEEMDWMVGQIL 317
Cdd:cd16034 178 alvlswnpphDPYTTA-P---EEYLDMYDPKKL--------LLRPNVPEDKkEEAGLREDLRGYYA-MITALDDNIGRLL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 318 DALDTEGLTNSTLIYFASDHG---GSLENQFANSQYGGwngiykggkgmggwegGIRVPGIFRWPGVLPAGRVIGEPTSL 394
Cdd:cd16034 245 DALKELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYPGKIKAGRVVDLLINT 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 395 MDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTL----WKvhFVtpvfqpe 470
Cdd:cd16034 309 VDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtdrYT--YV------- 377
|
490 500 510
....*....|....*....|....*....|....*..
gi 1864524947 471 gagacygrkvcpcsgekVVHHDPPLLFDLSRDPSEAH 507
Cdd:cd16034 378 -----------------RDKNGPWLLFDNEKDPYQLN 397
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
431-565 |
9.72e-57 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 186.36 E-value: 9.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 431 SDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGACYGRKVCpcsgekVVHHDPPLLFDLSRDPSEAHVLT 510
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1864524947 511 PASePLFYHVMERVQQAVWEHQQTLSPVALQLDSLGNLWRPWLQPCCGPFPLCWC 565
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
21-533 |
3.87e-55 |
|
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: 190.41 E-value: 3.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssVGYRVLQWTg 100
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 asggLPTNETTFAKILKEKGYATGLIGKWHlgLNCESAGDHCHHPLHHGFDYFYGMPlsMTGDCAHWelsEKRVDLEQkl 180
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWD--YASNAADF---LNRAKKGQ-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nflfqvlalvtltlaagkfmhlisiswmPviwsallavFllttsyfagalivhadcFLMRNHTITEQPMRFQRVTPLI-- 258
Cdd:cd16027 143 ----------------------------P---------F-----------------FLWFGFHDPHRPYPPGDGEEPGyd 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 259 LQEVksflkrnKLGPFLllvsflhVHIPLIttknflgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 338
Cdd:cd16027 169 PEKV-------KVPPYL-------PDTPEV-------REDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 339 GslenQFANS-----QYGgwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDr 413
Cdd:cd16027 228 M----PFPRAkgtlyDSG------------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY- 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 414 vIDGRDLLPLLLG-TAQHSDHEFLMH-------YCERFLHAARWHqrdrgtlwkvhfvtpvfqpegagacYgrkvcpcsg 485
Cdd:cd16027 285 -LQGRSFLPLLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK-------------------------Y--------- 329
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1864524947 486 ekVVHHDPPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEHQQ 533
Cdd:cd16027 330 --IRNYMPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
21-406 |
1.84e-54 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 186.47 E-value: 1.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqwtg 100
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAgdhchhPLHHGFDYFYGmplsmtgdcahwelsekrvdleqkl 180
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nflfqvlalvtltlaagkfmhlisiswmpviwsallavFLLTTSYFAGALIVHADCFLMRNHTiteqpmrfQRVTPLILQ 260
Cdd:pfam00884 120 --------------------------------------RNTGSDLYADPPDVPYNCSGGGVSD--------EALLDEALE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 evksFLKRNKlGPFLLLVSFLHVHIPLITTKNFLGKSA------------HGLYGDNVEEMDWMVGQILDALDTEGLTNS 328
Cdd:pfam00884 154 ----FLDNND-KPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524947 329 TLIYFASDHGGSLENQFANSQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 406
Cdd:pfam00884 229 TLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
21-507 |
9.66e-52 |
|
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: 183.11 E-value: 9.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqwTG 100
Cdd:cd16031 3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT----------DN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesaGDHCHHPlhHGFDYFYGMPlsmtgdcahwelsekrvdlEQkl 180
Cdd:cd16031 73 NGPLFDASQPTYPKLLRKAGYQTAFIGKWHLG------SGGDLPP--PGFDYWVSFP-------------------GQ-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nflfqvlalvtltlaagkfmhlisiswmpviwsallavflltTSYFAGALIVhadcflMRNHTITEQPmrfqrVTPLILQ 260
Cdd:cd16031 124 ------------------------------------------GSYYDPEFIE------NGKRVGQKGY-----VTDIITD 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 EVKSFLKRNKLG-PFLLLVSFLHVH-----------------IPLITT---KNFLGKS-------------------AHG 300
Cdd:cd16031 151 KALDFLKERDKDkPFCLSLSFKAPHrpftpaprhrglyedvtIPEPETfddDDYAGRPewareqrnrirgvldgrfdTPE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 301 LYGDNVE-------EMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-ENQFA-------NSqyggwngiykggkgmgg 365
Cdd:cd16031 231 KYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLgEHGLFdkrlmyeES----------------- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 366 weggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHS-DHEFLMHYCE--R 442
Cdd:cd16031 294 ----IRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepN 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 443 FLHAARWH--QRDRgtlWK-VHFvtpvfqpegagacygrkvcpcsgekvvHHDPPL--LFDLSRDPSEAH 507
Cdd:cd16031 368 FHNVPTHEgvRTER---YKyIYY---------------------------YGVWDEeeLYDLKKDPLELN 407
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-450 |
1.40e-48 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 173.95 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqWTG 100
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 A-SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdhcHHPLHHGFDYFygMPLSMTGDcaHWeLSEKRVDLEQK 179
Cdd:cd16033 76 AySRGLPPGVETFSEDLREAGYRNGYVGKWHVGPE--------ETPLDYGFDEY--LPVETTIE--YF-LADRAIEMLEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 180 LnflfqvlalvtltLAAGK-FMHLISIsWMPviwsallavfllttsyfagalivHADCF-------LMRNHTItEQPMRF 251
Cdd:cd16033 143 L-------------AADDKpFFLRVNF-WGP-----------------------HDPYIppepyldMYDPEDI-PLPESF 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 252 QRvtPLILqevKSFLKRNKLGPFLLLVSFLHVHIPLIttknflgksAHglYGDNVEEMDWMVGQILDALDTEGLTNSTLI 331
Cdd:cd16033 185 AD--DFED---KPYIYRRERKRWGVDTEDEEDWKEII---------AH--YWGYITLIDDAIGRILDALEELGLADDTLV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 332 YFASDHGGSLENQfansqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQ 411
Cdd:cd16033 249 IFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPP 316
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1864524947 412 DrvIDGRDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWH 450
Cdd:cd16033 317 K--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYK 361
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
21-507 |
2.62e-48 |
|
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: 173.01 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEFGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSVGYRVLQWT 99
Cdd:cd16025 3 PNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLN----CESAGDH-----------------------CHHPLH----- 147
Cdd:cd16025 79 GYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPDdyysTDDLTDKaieyideqkapdkpfflylafgaPHAPLQapkew 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 148 ---------HGFDyfygmplsmtgdcahwELSEKRvdLE-QKlnflfqvlalvtltlAAGkfmhlisiswmpviwsalla 217
Cdd:cd16025 159 idkykgkydAGWD----------------ALREER--LErQK---------------ELG-------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 218 vfllttsyfagalIVHADCFLM-RNHTI-------TEQPMRFQRvtpliLQEVksflkrnklgpflllvsflhvhiplit 289
Cdd:cd16025 186 -------------LIPADTKLTpRPPGVpawdslsPEEKKLEAR-----RMEV--------------------------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 290 tknflgksahglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFAN------------SQYGGwngiy 357
Cdd:cd16025 221 ------------YAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPGWANasntpfrlykqaSHEGG----- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 358 kggkgmggweggIRVPGIFRWP-GVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRV------IDGRDLLPLLLGTAQH 430
Cdd:cd16025 284 ------------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAP 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 431 SDHEFLmhYCERFLHAARWHQRdrgtlWKVhfvtpvfqpegagacygrkvcpcsgekVVHHDPPL------LFDLSRDPS 504
Cdd:cd16025 352 SRRRTQ--YFELFGNRAIRKGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPS 397
|
...
gi 1864524947 505 EAH 507
Cdd:cd16025 398 ETH 400
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-503 |
3.10e-47 |
|
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: 167.72 E-value: 3.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 100
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGV----------WDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGgLPTNETTFAKILKEKGYATGLIGKWHLglncESAGDHchhplhHGFDYfygmplsmtgdcahwelsekrvDLEqkl 180
Cdd:cd16037 71 ADP-YDGDVPSWGHALRAAGYETVLIGKLHF----RGEDQR------HGFRY----------------------DRD--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplILQ 260
Cdd:cd16037 115 -----------------------------------------------------------------------------VTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 EVKSFLKRNKL--GPFLLLVSFLHVHIPLITTKNFLGKSAHGL---YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFAS 335
Cdd:cd16037 118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 336 DHGgslENQFANSQYGgwngiykggkGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRvi 415
Cdd:cd16037 198 DHG---DMLGERGLWG----------KSTMYEESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-- 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 416 DGRDLLPLLLGTAQHSDHEFlmhyCErfLHAA---------RWHQrdrgtlWK-VHFVtpvfqpegagacygrkvcpcsg 485
Cdd:cd16037 262 DGRSLLPLAEGPDDPDRVVF----SE--YHAHgspsgafmlRKGR------WKyIYYV---------------------- 307
|
490
....*....|....*...
gi 1864524947 486 ekvvhHDPPLLFDLSRDP 503
Cdd:cd16037 308 -----GYPPQLFDLENDP 320
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
21-503 |
2.74e-45 |
|
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: 162.75 E-value: 2.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 100
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGgLPTNETTFAKILKEKGYATGLIGKWHLglncesagdhCHHPLHHGFDYfygmplsmtgdcahwelsekrvDLEqkl 180
Cdd:cd16032 71 AAE-FPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFDY----------------------DEE--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nflfqvlalvtltlaagkfmhlisiswmpVIWSALLAVFllttsyfagalivhaDcfLMRNHTiteqpmrfqrvtplilq 260
Cdd:cd16032 115 -----------------------------VAFKAVQKLY---------------D--LARGED----------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 evksflKRnklgPFLLLVSFLHVHIPLITTKNFLG----KSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 336
Cdd:cd16032 132 ------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 337 HGGSL--------ENQFANSqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVQLAGGE 408
Cdd:cd16032 201 HGDMLgerglwykMSFFEGS---------------------ARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGG 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 409 VPQDRV-IDGRDLLPLLLGTAQHSDHEFLMHYC-ERFLHAARWHQRDRgtlWKvhFVtpvfqpegagacygrkvcpcsge 486
Cdd:cd16032 259 TAPHVPpLDGRSLLPLLEGGDSGGEDEVISEYLaEGAVAPCVMIRRGR---WK--FI----------------------- 310
|
490
....*....|....*..
gi 1864524947 487 kVVHHDPPLLFDLSRDP 503
Cdd:cd16032 311 -YCPGDPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-422 |
5.14e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 148.93 E-value: 5.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 100
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqkl 180
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagaliVHADCFLMRNHtiteqpmrfqrvtplilq 260
Cdd:cd16149 113 ---------------------------------------------------DDAADFLRRRA------------------ 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 evksflKRNKlgPFLLLVSFLHVHIPlittknflgksaHGlYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGgs 340
Cdd:cd16149 124 ------EAEK--PFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNG-- 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 341 lenqFANSQYGGW---------NgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQ 411
Cdd:cd16149 181 ----FNMGHHGIWgkgngtfplN----------MYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPA 246
|
410
....*....|.
gi 1864524947 412 DRVIDGRDLLP 422
Cdd:cd16149 247 DPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-422 |
1.56e-38 |
|
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: 142.69 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssvgyrvLQWT 99
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesagDHCHHPLHHGFDyfygmplsmtgdcahwelseKRVDleqk 179
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAVS------------SNPHLFGGPGFD--------------------RGFD---- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 180 lnflfqvlalvtltlaagkfmhlisiSWMPVIWsallavfllttsyfagalivhadcflMRNHTITEQPMRFQRVTplil 259
Cdd:cd16148 111 --------------------------TFEDFRG--------------------------QEGDPGEEGDERAERVT---- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 260 QEVKSFLKRNKLG-PFlllvsFLHVHIplittknFlgkSAHGLYG-DN-VEEMDWMVGQILDALDTEGLTNSTLIYFASD 336
Cdd:cd16148 135 DRALEWLDRNADDdPF-----FLFLHY-------F---DPHEPYLyDAeVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 337 HGgslENQFANSQYGGWNgiykggkgMGGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVQLAGGEVPQDrvID 416
Cdd:cd16148 200 HG---EEFGEHGLYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SD 265
|
....*.
gi 1864524947 417 GRDLLP 422
Cdd:cd16148 266 GRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
21-531 |
1.48e-37 |
|
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: 144.32 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqWTG 100
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASggLPTNETTFAKILKEKGYATGLIGKWHLglnceSAGDHCHHPLH----------HGFDY-----FYGMPLSmtgDCA 165
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDT-----SPDPRGLAPLDprllsyelamPGFDPvdrldEYPAEDS---DTA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 166 HweLSEKrvdleqklnflfqvlALVTLTLAAGK--FMHLISISWMPviwsallavfllttsyfagALIVHADCFLMRNHT 243
Cdd:cd16028 142 F--LTDR---------------AIEYLDERQDEpwFLHLSYIRPHP-------------------PFVAPAPYHALYDPA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 244 ITEQPMRfqRVTPLILQEVKSFLKRnklgpflllvsflhvHIPLITTKNFLGKSAHGLYGDN-------------VEEMD 310
Cdd:cd16028 186 DVPPPIR--AESLAAEAAQHPLLAA---------------FLERIESLSFSPGAANAADLDDeevaqmratylglIAEVD 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 311 WMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQyGGWNGIYKggkgmggweggiRVPGIFRWPGVL---PAGRV 387
Cdd:cd16028 249 DHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGK-DGFFDQAY------------RVPLIVRDPRREadaTRGQV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 388 IGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQRDRGTlwkv 460
Cdd:cd16028 316 VDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALGL---- 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864524947 461 hfvtpvfQPEGAGACYGRkvcpcSGE-KVVHHD--PPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEH 531
Cdd:cd16028 383 -------SPDECSLAVIR-----DERwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSW 442
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
21-433 |
3.97e-37 |
|
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: 143.10 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqWTG 100
Cdd:cd16030 3 PNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----FRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGglptNETTFAKILKEKGYATGLIGKWHlglncesagdhchhplHHGFDYFYGMPLSmtgdcahWELSEKRVDLEQKL 180
Cdd:cd16030 78 VAP----DAVTLPQYFKENGYTTAGVGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEKYP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 NFLFQVLALVTLTLAAGKFMHLISI--SWMPVIWSALLAVFLLTT------SYFAGA--------LIVHADCFLMRNHTI 244
Cdd:cd16030 131 PGKLCPGKKGGKGGGGGPAWEAADVpdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPLES 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 245 TEQPMRFQRV-TPLI----LQEVksflkRNKLGPFLLLVSFLHVHIPLITTKNFLgksaHGLYGdNVEEMDWMVGQILDA 319
Cdd:cd16030 211 IPLPNPFDPIdLPEVawndLDDL-----PKYGDIPALNPGDPKGPLPDEQARELR----QAYYA-SVSYVDAQVGRVLDA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 320 LDTEGLTNSTLIYFASDHGGSL-ENQ----FANsqyggWNgiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSL 394
Cdd:cd16030 281 LEELGLADNTIVVLWSDHGWHLgEHGhwgkHTL-----FE-------------EATRVPLIIRAPGVTKPGKVTDALVEL 342
|
410 420 430
....*....|....*....|....*....|....*....
gi 1864524947 395 MDVFPTVVQLAGgeVPQDRVIDGRDLLPLLLGTAQHSDH 433
Cdd:cd16030 343 VDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKD 379
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
21-514 |
1.52e-34 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 136.34 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvGYrvlqwt 99
Cdd:PRK13759 7 PNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 gASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesagdhchHP--LHHGFDYfygmplSMTGDcahWELSEKRVDLE 177
Cdd:PRK13759 77 -GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNEDK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 178 QKLNFLFQVLALVTLTlAAGKFMHLISISWMPVIWSAllavfllttsyfagalivhadcflmRNHTITEQpmrfQRVTPL 257
Cdd:PRK13759 135 SQFDFVSDYLAWLREK-APGKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPTNW 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 258 ILQEVKSFLKR-NKLGPFLLLVSFLHVHIPLITTKNFL-------------------------GKSAHGLYGD------- 304
Cdd:PRK13759 185 VGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeeyar 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 305 --------NVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL--ENQFANS-QYGGwngiykggkgmggwegGIRVP 373
Cdd:PRK13759 265 raraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLgdHYLFRKGyPYEG----------------SAHIP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 374 GIFRWPG---VLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLG-TAQHSDHEFLMH-YCERFLHaar 448
Cdd:PRK13759 329 FIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYSSDN--- 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524947 449 WHQRDRgtlWKV--HFVTPVFQpegagacygrkvcpcsgekvvhhdpplLFDLSRDPSEAHVLTPASE 514
Cdd:PRK13759 404 YLTDGK---WKYiwFSQTGEEQ---------------------------LFDLKKDPHELHNLSPSEK 441
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-429 |
2.39e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 133.89 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgYRvlqwtg 100
Cdd:cd16152 2 PNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesAGdhchhplhhgfdYfygmplsmtgdcahwelsekRVDleqkl 180
Cdd:cd16152 71 NGIPLPADEKTLAHYFRDAGYETGYVGKWHL------AG------------Y--------------------RVD----- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 nflfqvlalvTLTLAAGKFMHlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilq 260
Cdd:cd16152 108 ----------ALTDFAIDYLD----------------------------------------------------------- 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 evksflKRNKLGPFLLLVSFLHVH----------------------IP--LittKNFLGKSAHGL---YGdNVEEMDWMV 313
Cdd:cd16152 119 ------NRQKDKPFFLFLSYLEPHhqndrdryvapegsaerfanfwVPpdL---AALPGDWAEELpdyLG-CCERLDENV 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 314 GQILDALDTEGLTNSTLIYFASDHGgsleNQFA--NSQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEP 391
Cdd:cd16152 189 GRIRDALKELGLYDNTIIVFTSDHG----CHFRtrNAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEEL 252
|
410 420 430
....*....|....*....|....*....|....*...
gi 1864524947 392 TSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQ 429
Cdd:cd16152 253 VSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVE 288
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-515 |
1.39e-31 |
|
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: 125.75 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssvgyrv 95
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 96 lqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLnCESAGDHCHHP--------LHHGF----DyfygmPLSMTGd 163
Cdd:cd16155 74 ----GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF-ADAAIEFLEEYkdgdkpffMYVAFtaphD-----PRQAPP- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 164 cahwELSEK--RVDLEQKLNFLFQvlalvtltlaagkfmHlisiswmPviwsallavfllttsyFAGALIVHADcflmrn 241
Cdd:cd16155 143 ----EYLDMypPETIPLPENFLPQ---------------H-------P----------------FDNGEGTVRD------ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 242 htitEQPMRFQRvTPlilQEVKSFLKRNklgpflllvsflhvhiplittknflgksahglYGdNVEEMDWMVGQILDALD 321
Cdd:cd16155 175 ----EQLAPFPR-TP---EAVRQHLAEY--------------------------------YA-MITHLDAQIGRILDALE 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 322 TEGLTNSTLIYFASDHGGSL--------ENQFANSqyggwngiykggkgmggweggIRVPGIFRWPGVlPAGRVIGEPTS 393
Cdd:cd16155 214 ASGELDNTIIVFTSDHGLAVgshglmgkQNLYEHS---------------------MRVPLIISGPGI-PKGKRRDALVY 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 394 LMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQhsdheflMHYCERFLHAARWHQRDRGTLWKVHFVTPvfqpegag 473
Cdd:cd16155 272 LQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKK-------AVRDTLYGAYRDGQRAIRDDRWKLIIYVP-------- 334
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1864524947 474 acygrkvcpcsGEKVVhhdppLLFDLSRDPSEAHVLtpASEP 515
Cdd:cd16155 335 -----------GVKRT-----QLFDLKKDPDELNNL--ADEP 358
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-539 |
1.49e-31 |
|
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: 126.97 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssvGYRVLQWT 99
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHChhplhhgfdyfygmplsmTGDcahWELSEKRVD-LEQ 178
Cdd:cd16150 74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC------------------DSD---EACVRTAIDwLRN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 179 KLN----FLFqvlalVTLTL------AAGKFMHLISISWMPVIWSAllavfLLTTSYFAGALIvhadcfLMRNHtiteqp 248
Cdd:cd16150 128 RRPdkpfCLY-----LPLIFphppygVEEPWFSMIDREKLPPRRPP-----GLRAKGKPSMLE------GIEKQ------ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 249 mRFQRVTPLILQEVKsflkrnklgpflllvsflhvhiplittKNFLGKsahglygdnVEEMDWMVGQILDALDTEGLTNS 328
Cdd:cd16150 186 -GLDRWSEERWRELR---------------------------ATYLGM---------VSRLDHQFGRLLEALKETGLYDD 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 329 TLIYFASDHG------GSLE---NQFANSQyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFP 399
Cdd:cd16150 229 TAVFFFSDHGdytgdyGLVEkwpNTFEDCL--------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 400 TVVQLAGgeVPQDRVIDGRDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHQRDRGTlwKVHFVTPVFQPEGAGACYG 477
Cdd:cd16150 288 TLLDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQAMEGGHG--PYDLKWPRLLQQEEPPEHT 359
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864524947 478 RKVCPCSGE-KVV--HHDPPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEHQQTLSPVA 539
Cdd:cd16150 360 KAVMIRTRRyKYVyrLYEPDELYDLEADPLELHNL--IGDPAYAEIIAEMKQRLLRWMVETSDVV 422
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
21-424 |
1.24e-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: 122.11 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 100
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 aSGGLPTNETTFAKILKEKGYATGLIGKWHLglnceSAGDH-----ChhPLHHGFDYFYGMplsmtgDCAHWELSEKRVd 175
Cdd:cd16156 71 -CMALGDNVKTIGQRLSDNGIHTAYIGKWHL-----DGGDYfgngiC--PQGWDPDYWYDM------RNYLDELTEEER- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 176 leqklnflfqvlalvtltlaagkfmhlisiswmpVIWSALLAVfllttsyfagalivhadcflMRNHTITEQPMRFQRVT 255
Cdd:cd16156 136 ----------------------------------RKSRRGLTS--------------------LEAEGIKEEFTYGHRCT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 256 PLILQevksFLKRNKLGPFLLLVSFLHVHIPLITTKNF----------LGKSAHglygDNVEE----------------- 308
Cdd:cd16156 162 NRALD----FIEKHKDEDFFLVVSYDEPHHPFLCPKPYasmykdfefpKGENAY----DDLENkplhqrlwagakphedg 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 309 ----------------MDWMVGQILDALDtEGLTNSTLIYfASDHGgslENQFANSQYGgwngiykggKGMGGWEGGIRV 372
Cdd:cd16156 234 dkgtikhplyfgcnsfVDYEIGRVLDAAD-EIAEDAWVIY-TSDHG---DMLGAHKLWA---------KGPAVYDEITNI 299
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1864524947 373 PGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGgeVPQDRVIDGRDLLPLL 424
Cdd:cd16156 300 PLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-420 |
2.17e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 117.48 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSS 90
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 91 VGYrvlqWTGASGGLPtnetTFAKILKEKGYATGLIGKWHlglncesagdhchhplhhgfdyfygmplsmtgdcahwels 170
Cdd:cd16153 82 EAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH---------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 171 ekrvdLEQKLNFLFQvlALVTLTLAAGKfmhlisISWMPviwsallavfllttsyfagalivhadcflmrnhtiteqpmr 250
Cdd:cd16153 114 -----LEAFQRYLKN--ANQSYKSFWGK------IAKGA----------------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 251 fqrvtplilqevksflKRNKlgPFLLLVSFLHVHIPLITTKNFLGKSA-HGL--YGDNveemdwMVGQILDALDTEGLTN 327
Cdd:cd16153 140 ----------------DSDK--PFFVRLSFLQPHTPVLPPKEFRDRFDyYAFcaYGDA------QVGRAVEAFKAYSLKQ 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 328 ---STLIYFASDHGGSLENQFANSQYGGWNgiykggkgmggweGGIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTVV 402
Cdd:cd16153 196 drdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLL 262
|
410
....*....|....*...
gi 1864524947 403 QLAGGEVPQDRVIDGRDL 420
Cdd:cd16153 263 AAAGVDVDAPDYLDGRDL 280
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
21-405 |
3.86e-29 |
|
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: 115.60 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSvGYRVLQWT 99
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGN-GSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 100 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqk 179
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 180 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplil 259
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 260 qeVKSFLKRNKLG-PFLLLVSFLHVHIPLittknFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 338
Cdd:cd00016 108 --LLKAIDETSKEkPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864524947 339 GSLEnqfansqygGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLA 405
Cdd:cd00016 181 GIDK---------GHGGDPKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
21-418 |
9.20e-27 |
|
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: 112.26 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSVGYRVL 96
Cdd:cd16147 2 PNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 97 QWTGAsgglptNETTFAKILKEKGYATGLIGKWhlgLN-CESAGDHCHHPLhhGFDYFYGMP---------LSMTGDCAH 166
Cdd:cd16147 78 WQNGL------ERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVgnstyynytLSNGGNGKH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 167 WELSEKR--VDL--EQKLNFLfqvlalvTLTLAAGKfmhlisiswmPviwsallavFLLTTSYFAgaliVHAdcflmrNH 242
Cdd:cd16147 147 GVSYPGDylTDViaNKALDFL-------RRAAADDK----------P---------FFLVVAPPA----PHG------PF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 243 TITEQPMR-FQRVTPL--------ILQEVKSFLKRNKlgpflllvsflhvhiplittknflgksahGLYGDNVEEMDW-- 311
Cdd:cd16147 191 TPAPRYANlFPNVTAPprpppnnpDVSDKPHWLRRLP-----------------------------PLNPTQIAYIDEly 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 312 ------------MVGQILDALDTEGLTNSTLIYFASDHG---GSLENQFANSQ-YggwngiykggkgmggwEGGIRVPGI 375
Cdd:cd16147 242 rkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHRLPPGKRTpY----------------EEDIRVPLL 305
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1864524947 376 FRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGR 418
Cdd:cd16147 306 VRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-439 |
4.54e-24 |
|
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: 102.67 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYR 94
Cdd:cd16035 1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 95 VlQWTgasggLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdhchhplhhgfdyfygmplSMTGDCAHwelsekrv 174
Cdd:cd16035 75 M-QPL-----LSPDVPTLGHMLRAAGYYTAYKGKWHLS--------------------------GAAGGGYK-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 175 dleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmRNHTITEQPMRFqrv 254
Cdd:cd16035 115 -----------------------------------------------------------------RDPGIAAQAVEW--- 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 255 tpliLQEVKSflKRNKLGPFLLLVSFL--H-VHIPLITTKNFlgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLI 331
Cdd:cd16035 127 ----LRERGA--KNADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIV 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 332 YFASDHG---GS--LENQFANSqYGgwngiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 406
Cdd:cd16035 199 VFTSDHGemgGAhgLRGKGFNA-YE----------------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAG 261
|
410 420 430
....*....|....*....|....*....|....*...
gi 1864524947 407 GEVPQDRVID----GRDLLPLLLGTAQHSDHE-FLMHY 439
Cdd:cd16035 262 VDAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-431 |
9.29e-24 |
|
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: 103.20 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEFGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSVGYRVLQw 98
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 99 tgasgglpTNETTFAKILKE---KGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEKRVD 175
Cdd:cd16154 78 --------SEETLLQLLIKDattAGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 176 LEQKlnflfqvlalvtlTLAAGKFMHLiSISWM-----PviWSALLAvfllttsYFAgalivhadcflmrNHTiteqpmr 250
Cdd:cd16154 144 TNST-------------EYATTKLTNL-AIDWIdqqtkP--WFLWLA-------YNA-------------PHT------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 251 fqrvtplilqevksflkrnklgPFLLLVSFLHvhiplitTKNFLGKSAHglYGDN--------VEEMDWMVGQILDALDT 322
Cdd:cd16154 181 ----------------------PFHLPPAELH-------SRSLLGDSAD--IEANprpyylaaIEAMDTEIGRLLASIDE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 323 EGLTNsTLIYFASDHG--------GSLENQFANSQY-GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPTS 393
Cdd:cd16154 230 EEREN-TIIIFIGDNGtpgqvvdlPYTRNHAKGSLYeGG-----------------INVPLIVSGAGV---ERANERESA 288
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1864524947 394 LM---DVFPTVVQLAGGEVPQdrVIDGRDLLPLLLGTAQHS 431
Cdd:cd16154 289 LVnatDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNAST 327
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
21-504 |
3.06e-16 |
|
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: 80.66 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssvgyRVLQWTG 100
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESWN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 101 ASGGLPTNETTFAKILKEKGYATGLIGKwhlglncesagdhchhplhhgFDYFYGmplsmtgdcaHWELSEKRVDLEQKL 180
Cdd:cd16171 70 NYKGLDPNYPTWMDRLEKHGYHTQKYGK---------------------LDYTSG----------HHSVSNRVEAWTRDV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 181 NFLFQVLALVTLTLAAGKfmhlisiswmpviwsallavfllttsyfagalivHADCFLMRNHTITEQPMRFQRVTPLILQ 260
Cdd:cd16171 119 PFLLRQEGRPTVNLVGDR----------------------------------STVRVMLKDWQNTDKAVHWIRKEAPNLT 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 261 EvksflkrnklgPFLLlvsFLHVHIPLITTKNFLGKSAHGL------YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFA 334
Cdd:cd16171 165 Q-----------PFAL---YLGLNLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTYVFFT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 335 SDHGG-SLEN-QFAN-SQYGGwngiykggkgmggwegGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQ 411
Cdd:cd16171 231 SDHGElAMEHrQFYKmSMYEG----------------SSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 412 DrvIDGRDLLPLLLGTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTLWKvhFVTpvfqpegagacYGrkv 480
Cdd:cd16171 294 N--LSGYSLLPLLSESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YA--- 349
|
490 500
....*....|....*....|....
gi 1864524947 481 cpcSGEKVvhhdPPLLFDLSRDPS 504
Cdd:cd16171 350 ---DGNSV----PPQLFDLSKDPD 366
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
21-406 |
4.10e-10 |
|
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: 60.77 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 21 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSVGYRvl 96
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 97 qwtgasgglPTNETTFAKILKEKGYATGLIgkwhlglncesagdHCHHP---------LHHGFDYFYG---MPLSMTGDc 164
Cdd:cd16015 77 ---------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFYDledFPDDEKET- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 165 AHWELSEKrvdleqklnFLFQVLALVTLTLAAGKFMhlisiswmpviwsallaVFLLTTSyfagalivhadcflmrNHti 244
Cdd:cd16015 133 NGWGVSDE---------SLFDQALEELEELKKKPFF-----------------IFLVTMS----------------NH-- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 245 teqpmrfqrvtplilqevksflkrnklGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYgdnveEMDWMVGQILDALDTEG 324
Cdd:cd16015 169 ---------------------------GPYDLPEEKKDEPLKVEEDKTELENYLNAIH-----YTDKALGEFIEKLKKSG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 325 LTNSTLIYFASDHGGSLENQFANSQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTVVQL 404
Cdd:cd16015 217 LYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDL 281
|
..
gi 1864524947 405 AG 406
Cdd:cd16015 282 LG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
9-421 |
1.06e-07 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 54.66 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 9 APSASSDVSASWPNILLLM----ADDLgigdIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVR 84
Cdd:COG1368 223 RPTPNPFGPAKKPNVVVILlesfSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 85 SG-MVSSVGYRVLQwtgasgglptnetTFAKILKEKGYATgligkwhlglncesagdHCHHP------------LHHGFD 151
Cdd:COG1368 299 GGsPYKRPGQNNFP-------------SLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFD 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 152 YFYG---MPLSMTGdcaHWELSEKrvdleqklnFLFQvLALVTLTLAAGKFMhlisiswmpviwsallaVFLLTTSyfag 228
Cdd:COG1368 349 EFYDredFDDPFDG---GWGVSDE---------DLFD-KALEELEKLKKPFF-----------------AFLITLS---- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 229 alivhadcflmrNHTITEQPMRFQRVTPLILQEVKSFLKrnklgpflllvsflHVHiplittknflgksahglygdnveE 308
Cdd:COG1368 395 ------------NHGPYTLPEEDKKIPDYGKTTLNNYLN--------------AVR-----------------------Y 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 309 MDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYggwngiykggkgmggwEGGIRVPGIFRWPGvLPAGRVI 388
Cdd:COG1368 426 ADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENP----------------LERYRVPLLIYSPG-LKKPKVI 488
|
410 420 430
....*....|....*....|....*....|...
gi 1864524947 389 GEPTSLMDVFPTVVQLAGGEVPQDRVIdGRDLL 421
Cdd:COG1368 489 DTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
2-176 |
9.68e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 51.29 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 2 LSVLLSLAPSASSDVSASWPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEFGVKLTQHISAA-SLCTPSRAAFLTGR 80
Cdd:COG1524 5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 81 YPVRSGMVSSVGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIGKWHLGlncESAGDHCHHPLHH-G 149
Cdd:COG1524 80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdG 156
|
170 180
....*....|....*....|....*....
gi 1864524947 150 FDYFYGMPLS--MTGDCAHWELSEKRVDL 176
Cdd:COG1524 157 RKPLLGNPAAdrWIAAAALELLREGRPDL 185
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
306-403 |
2.11e-06 |
|
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: 50.67 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524947 306 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-ENQ----FANSQYGGWNgiykggkgmggweggIRVPGIFRWPG 380
Cdd:COG3083 433 VHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnENGqnywGHNSNFSRYQ---------------LQVPLVIHWPG 497
|
90 100
....*....|....*....|...
gi 1864524947 381 VLPagRVIGEPTSLMDVFPTVVQ 403
Cdd:COG3083 498 TPP--QVISKLTSHLDIVPTLMQ 518
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
304-338 |
5.72e-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: 39.33 E-value: 5.72e-03
10 20 30
....*....|....*....|....*....|....*
gi 1864524947 304 DNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 338
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| |
