|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
50-477 |
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: 580.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 129
Cdd:cd16159 2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAHweLSEKRVDLEQKL 209
Cdd:cd16159 82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSFDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 NFLFQVLALVTLTLAAGKFMHLISISWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTITEQPMRFQRVTPLI 287
Cdd:cd16159 160 LFPLLTAFVLITALTIFLLLYLGAVSKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEVVEQPMSLENLTQRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 288 LQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 367
Cdd:cd16159 238 TKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 368 GSLENQFANSQYGGWNGIYKGG---------------------------------------------------------- 389
Cdd:cd16159 318 GHLEEISVGGEYGGGNGGIYGGkkmggweggirvptivrwpgvippgsvideptslmdifptvaalagaplpsdriidgr 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 390 -------------------------------------TLWKVHFVTPVFQPEGAGaCYGRKVCPCSGEKVVHHDPPLLFD 432
Cdd:cd16159 398 dlmplltgqekrspheflfhycgaelhavryrprdggAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1864524953 433 LSRDPSEAHVLTPASEPlFYHVMERVQQAVWEHQQTLSPVALQLD 477
Cdd:cd16159 477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
50-444 |
4.76e-102 |
|
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: 311.80 E-value: 4.76e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgYRVLQWTG 129
Cdd:cd16026 2 PNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesaGDH-CHHPLHHGFDYFYGMPLSMTGDCAHWELSEKRVDLeqk 208
Cdd:cd16026 77 SKGGLPPDEITIAEVLKKAGYRTALVGKWHL-------GHQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 209 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadCFLMRNHTITEQPMRFQRVTPLIL 288
Cdd:cd16026 147 --------------------------------------------------------PPLMENEEVIEQPADQSSLTQRYT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 289 QEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG 368
Cdd:cd16026 171 DEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 369 SLEnqfaNSQYGGWNGIYKGG--------------------------------------TL------------------- 391
Cdd:cd16026 251 WLE----YGGHGGSAGPLRGGkgttweggvrvpfiawwpgvipagtvsdelastmdllpTLaalagaplpedrvidgkdi 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 392 -------------------------------WKVHFVTPVFQPEGAGacygrkvcpcsGEKVVHHDPPLLFDLSRDPSEA 440
Cdd:cd16026 327 splllggskspphpffyyydggdlqavrsgrWKLHLPTTYRTGTDPG-----------GLDPTKLEPPLLYDLEEDPGET 395
|
....
gi 1864524953 441 HVLT 444
Cdd:cd16026 396 YNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
50-462 |
1.18e-96 |
|
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: 299.73 E-value: 1.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsvGYRV-LQWT 128
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 129 gaSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDyFYGMPLSMTGdcaHWELSekrvdleqk 208
Cdd:cd16160 80 --IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGTNLPFTN---SWACD--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 209 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllTTSYFagalIVHAD---CFLMRNHTITEQPMRFQRVTP 285
Cdd:cd16160 145 ------------------------------------------DTGRH----VDFPDrsaCFLYYNDTIVEQPIQHEHLTE 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 286 LILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 365
Cdd:cd16160 179 TLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 366 HGGSLE--------NQF----ANSQYGG--------WNGIYK---------------------GGTL------------- 391
Cdd:cd16160 259 HGPHVEycleggstGGLkggkGNSWEGGirvpfiayWPGTIKprvshevvstmdifptfvdlaGGTLptdriydglsitd 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 392 ----------------------------WKVHFVT---PVFQPEGAGACYGRKVCP------CSGEKVVHHDPPLLFDLS 434
Cdd:cd16160 339 lllgeadsphddilyyccsrlmavrygsYKIHFKTqplPSQESLDPNCDGGGPLSDyivcydCEDECVTKHNPPLIFDVE 418
|
490 500
....*....|....*....|....*...
gi 1864524953 435 RDPSEAHVLTPAsepLFYHVMERVQQAV 462
Cdd:cd16160 419 KDPGEQYPLQPS---VYEHMLEAVEKLI 443
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
50-499 |
9.77e-73 |
|
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: 238.50 E-value: 9.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqwTG 129
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAgdhcHHPLHHGFDYFYGMPLSMT-GDCAHwelsekrvdleqk 208
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHDqGPCQN------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 209 lnflfqvlalvtltlaagkfmhlisiswmpviwsalLAVFLLTTSYFAGALIVHADCFLMRNHTITEQPMRFQRVTPLIL 288
Cdd:cd16158 140 ------------------------------------LTCFPPNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 289 QEVKSFL----KRNKlgPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFAS 364
Cdd:cd16158 184 KFAKDFIadnaKEGK--PFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 365 DHGGSLENQfansQYGGWNGI--------YKGG-----------------------TL---------------------- 391
Cdd:cd16158 262 DNGPSTMRK----SRGGNAGLlkcgkgttYEGGvrepaiaywpgrikpgvthelasTLdilptiaklagaplpnvtldgv 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 392 -------------------------------------WKVHFVT---PVFQPEGAGACYGRKvcpcsgeKVVHHDPPLLF 431
Cdd:cd16158 338 dmspilfeqgksprqtffyyptspdpdkgvfavrwgkYKAHFYTqgaAHSGTTPDKDCHPSA-------ELTSHDPPLLF 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864524953 432 DLSRDPSEAHVLTPASEplFYHVMERVQQAVWEHQQTLSPVALQLDSLGNlwrPWLQPC----CGPFPLCWC 499
Cdd:cd16158 411 DLSQDPSENYNLLGLPE--YNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPCckpgCTPKPSCCQ 477
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
50-392 |
2.82e-68 |
|
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: 224.39 E-value: 2.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVgyrvlqWT 128
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV------LG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 129 GASGGL-PTNETTFAKILKEKGYATGLIGKWHLGLN-CESAGDHCHH---------------PLHHGFDYFYGMPLSmtg 191
Cdd:cd16143 75 GFSPPLiEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwKKKDGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPAS--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 192 dcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnh 271
Cdd:cd16143 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 272 titeqpmrfqRVTPLILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDAL 349
Cdd:cd16143 152 ----------EVLPTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDAL 221
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1864524953 350 DTEGLTNSTLIYFASDHGGSLENQF-ANSQYGGW-NGIYKG--GTLW 392
Cdd:cd16143 222 KELGLAENTLVIFTSDNGPSPYADYkELEKFGHDpSGPLRGmkADIY 268
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
50-390 |
7.12e-63 |
|
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: 210.86 E-value: 7.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGM--VSSVGYRVLQW 127
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 128 TGA-----SGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGmplsmtGDCAHwelsekr 202
Cdd:cd16144 81 TKLipppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG------GTGNG------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 203 vdleqklnflfqvlalvtltlaAGKfmhlisiswmpviwsallavfllttSYFAGALIVHADCFLmrnhtITEQPMRFQR 282
Cdd:cd16144 142 ----------------------GPP-------------------------SYYFPPGKPNPDLED-----GPEGEYLTDR 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 283 VTplilQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTK----NFLGKSAHGLYGDN-------VEEMDWMVGQILDALDT 351
Cdd:cd16144 170 LT----DEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPelieKYEKKKKGLRKGQKnpvyaamIESLDESVGRILDALEE 245
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1864524953 352 EGLTNSTLIYFASDHGG-SLENQFANSQY---GGWNGIYKGGT 390
Cdd:cd16144 246 LGLADNTLVIFTSDNGGlSTRGGPPTSNAplrGGKGSLYEGGI 288
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
50-392 |
1.32e-61 |
|
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: 206.23 E-value: 1.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEFGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvSSVGyrvlq 126
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-TTVG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 127 WTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncESAGdhcHHPLHHGFDYFYGMPLsmtgdcahwelsekrvdle 206
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDG---RLPTDHGFDEFYGNLY------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 207 qklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnHTITEQpmrfqrvtpl 286
Cdd:cd16142 129 ----------------------------------------------------------------HTIDEE---------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 287 ILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGKS-AHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFA 363
Cdd:cd16142 135 IVDKAIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSsGKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
|
330 340
....*....|....*....|....*....
gi 1864524953 364 SDHGGSLeNQFANSQYGGWNGIYkgGTLW 392
Cdd:cd16142 215 TDNGPEQ-DVWPDGGYTPFRGEK--GTTW 240
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
31-373 |
1.20e-60 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 204.34 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 31 LSVLLSLAPSASSDVSASWPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRY 110
Cdd:COG3119 5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 111 PVRSGMVSSVGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesagdhchhplhhgfdyfygmplsmt 190
Cdd:COG3119 85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 191 gdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrn 270
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 271 htiteqpmrfqrvTPLILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGK----------------------- 325
Cdd:COG3119 130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1864524953 326 SAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQ 373
Cdd:COG3119 197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEH 244
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
50-401 |
8.51e-59 |
|
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: 199.23 E-value: 8.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRvlqwt 128
Cdd:cd16161 2 PNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 129 gASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGdcahwELSEKRVDleqk 208
Cdd:cd16161 77 -SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFSHDS-----SLADRYAQ---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 209 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyFAGAlivhadcFLMRNHTITEqpmrfqrvtplil 288
Cdd:cd16161 141 ----------------------------------------------FATD-------FIQRASAKDR------------- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 289 qevksflkrnklgPFLLLVSFLHVHIPLITTKNFLGKSAH-GLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 367
Cdd:cd16161 155 -------------PFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNG 221
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1864524953 368 ---------GSLENQFANSQyGGWNGiYKGGTlWKVHFVTPVF 401
Cdd:cd16161 222 pwevkcelaVGPGTGDWQGN-LGGSV-AKAST-WEGGHREPAI 261
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
50-477 |
4.31e-57 |
|
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: 196.92 E-value: 4.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 129
Cdd:cd16157 2 PNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 AS--GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsagdhcHHPLHHGFDYFYGMPlsmtgDCaHWelseKRVDLEQ 207
Cdd:cd16157 82 QNivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NC-HF----GPYDNKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 208 KLNflfqvLALVTLTLAAGKFMHLISIswmpviwsallavfllttsyfagalivhadcflmrNHTITEqpmrfQRVTPLI 287
Cdd:cd16157 146 YPN-----IPVYRDWEMIGRYYEEFKI-----------------------------------DKKTGE-----SNLTQIY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 288 LQEVKSFLKR--NKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 365
Cdd:cd16157 181 LQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 366 HGGSLenqFANSQYGGWNG------------------------------------------------------------- 384
Cdd:cd16157 261 NGAAL---ISAPEQGGSNGpflcgkqttfeggmrepaiawwpghikpgqvshqlgslmdlfttslalaglpipsdraidg 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 385 ------------------IYKGGTL-------WKVHFVT----PVFQPEGAGACYGRKVCPCSGEKVVHH-DPPLLFDLS 434
Cdd:cd16157 338 idllpvllngkekdrpifYYRGDELmavrlgqYKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQTDHtKLPLLFHLG 417
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1864524953 435 RDPSEAHVLTPASePLFYHVMERVQQAVWEHQQTLSPVALQLD 477
Cdd:cd16157 418 RDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
50-389 |
1.14e-53 |
|
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: 186.26 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyRVLQWTG 129
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESAGdhchHPLHHGFDYFYGmplsmtgdcahwelsekrvdleqkl 209
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGP-GTPG----HPTKQGFDYFYG------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 nFLFQVLAlvtltlaagkfmHlisiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-------EQPMRFQR 282
Cdd:cd16145 125 -YLDQVHA------------H----------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 283 VTPLILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTK---NFLGKSAHGLYGDN------------VEEMDWMVGQILD 347
Cdd:cd16145 170 SHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDdgpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILA 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1864524953 348 ALDTEGLTNSTLIYFASDHGGSLE------NQFANSqYGGWNGI----YKGG 389
Cdd:cd16145 250 LLKELGIDENTLVVFTSDNGPHSEggsehdPDFFDS-NGPLRGYkrslYEGG 300
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
50-392 |
1.59e-53 |
|
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: 185.45 E-value: 1.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMVSSVGyrvlqWTG 129
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGMQHGVI-----LAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdHCHH---PLHHGFDYFYGMPLSMTGdcaHWelsekrvdle 206
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGYYGGAED---YY---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 207 qklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-EQPMRFqrVTP 285
Cdd:cd16029 134 ----------------------------------------------THTSGGANDYGNDDLRDNEEPAwDYNGTY--STD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 286 LILQEVKSFLKR-NKLGPFLLLVSFLHVHIPLITTKNFL----GKSAHGLYGD------NVEEMDWMVGQILDALDTEGL 354
Cdd:cd16029 166 LFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYAdpyeDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKGM 245
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1864524953 355 TNSTLIYFASDHGGslenqFANSQYGGWNGIYKGG--TLW 392
Cdd:cd16029 246 LDNTLIVFTSDNGG-----PTGGGDGGSNYPLRGGknTLW 280
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
50-392 |
4.45e-53 |
|
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: 179.17 E-value: 4.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssvgyrVLQWTG 129
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHlglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqkl 209
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilQ 289
Cdd:cd16022 103 -------------------------------------------------------------------------------D 103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 290 EVKSFLKRN-KLGPFLLLVSFLHVHIPLIttknflgksahglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG 368
Cdd:cd16022 104 EAIDFIERRdKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340
....*....|....*....|....
gi 1864524953 369 SLenqfansqyGGWNGIYKGGTLW 392
Cdd:cd16022 171 ML---------GDHGLRGKKGSLY 185
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-367 |
6.55e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 172.40 E-value: 6.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqwtg 129
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 aSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESAGDhchHPLHHGFDYFygmplsmtgdCAhWELSEKRVDLEQKL 209
Cdd:cd16151 68 -FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEY----------CL-WQLTETGEKYSRPA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 NFLFQVLALVTLTLAAGKFmhlisiswMPVIWSAllavfllttsyfagalivhadcFLMRnhtiteqpmrfqrvtplilq 289
Cdd:cd16151 132 TPTFNIRNGKLLETTEGDY--------GPDLFAD----------------------FLID-------------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 290 evksFLKRNKLGPFLLLVSFLHVHIPLITT----------KNFLGKSAHglYGDNVEEMDWMVGQILDALDTEGLTNSTL 359
Cdd:cd16151 162 ----FIERNKDQPFFAYYPMVLVHDPFVPTpdspdwdpddKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
|
....*...
gi 1864524953 360 IYFASDHG 367
Cdd:cd16151 236 IIFTGDNG 243
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
392-499 |
6.81e-45 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 153.62 E-value: 6.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 392 WKVHFVTPVFQPEGAGACYGRKVCpcsgekVVHHDPPLLFDLSRDPSEAHVLTPASePLFYHVMERVQQAVWEHQQTLSP 471
Cdd:pfam14707 22 YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLSPDS-PEYPEVLAEIKAAVEEHKATLVP 94
|
90 100
....*....|....*....|....*...
gi 1864524953 472 VALQLDSLGNLWRPWLQPCCGPFPLCWC 499
Cdd:pfam14707 95 VPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
50-401 |
1.26e-44 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 158.74 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqwtg 129
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAgdhchhPLHHGFDYFYGmplsmtgdcahwelsekrvdleqkl 209
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 nflfqvlalvtltlaagkfmhlisiswmpviwsallavFLLTTSYFAGALIVHADCFLMRNHTiteqpmrfQRVTPLILQ 289
Cdd:pfam00884 120 --------------------------------------RNTGSDLYADPPDVPYNCSGGGVSD--------EALLDEALE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 290 evksFLKRNKlGPFLLLVSFLHVHIPLITTKNFLGKSA------------HGLYGDNVEEMDWMVGQILDALDTEGLTNS 357
Cdd:pfam00884 154 ----FLDNND-KPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1864524953 358 TLIYFASDHGGSLEnqfansQYGGWNGIYKGGTLWKVHFVTPVF 401
Cdd:pfam00884 229 TLVVYTSDHGESLG------EGGGYLHGGKYDNAPEGGYRVPLL 266
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-367 |
1.98e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 155.80 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqwtg 129
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 asggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHH----PLHHGFDYFYGMplsmtgDCAH-------WEL 198
Cdd:cd16034 75 ----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------ECNHdhnnphyYDD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 199 SEKRVDLEQklnflfqvlalvtltlaagkfmhlisisWMPvIWSALLAVfllttSYfagalivhadcflMRNHTITEQP- 277
Cdd:cd16034 145 DGKRIYIKG----------------------------YSP-DAETDLAI-----EY-------------LENQADKDKPf 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 278 ----------MRFQRVtPlilQEVKSFLKRNKLgpflllvsFLHVHIPLIT-TKNFLGKSAHGLYGdNVEEMDWMVGQIL 346
Cdd:cd16034 178 alvlswnpphDPYTTA-P---EEYLDMYDPKKL--------LLRPNVPEDKkEEAGLREDLRGYYA-MITALDDNIGRLL 244
|
330 340
....*....|....*....|.
gi 1864524953 347 DALDTEGLTNSTLIYFASDHG 367
Cdd:cd16034 245 DALKELGLLENTIVVFTSDHG 265
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
50-389 |
5.84e-42 |
|
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: 154.63 E-value: 5.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSVGYRVLqwt 128
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 129 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEkrvdleqk 208
Cdd:cd16146 76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 209 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsYFagalivhaDCFLMRNHTI--TEQpmrFqrVTPL 286
Cdd:cd16146 137 ---------------------------------------------YF--------DDTYYHNGKFvkTEG---Y--CTDV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 287 ILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNF--------LGKSAHGLYGdNVEEMDWMVGQILDALDTEGLTNST 358
Cdd:cd16146 159 FFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIENIDDNVGRLLAKLKELGLEENT 237
|
330 340 350
....*....|....*....|....*....|.
gi 1864524953 359 LIYFASDHGGSlenqfansqyGGWNGIYKGG 389
Cdd:cd16146 238 IVIFMSDNGPA----------GGVPKRFNAG 258
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
50-370 |
8.40e-37 |
|
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: 139.57 E-value: 8.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssVGYRVLQWTg 129
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 asggLPTNETTFAKILKEKGYATGLIGKWHlgLNCESAGDHCHHPLHHGFDYFYGMPlsMTGDCAHWelsEKRVDLEQkl 209
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWD--YASNAADF---LNRAKKGQ-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 nflfqvlalvtltlaagkfmhlisiswmPviwsallavFllttsyfagalivhadcFLMRNHTITEQPMRFQRVTPLI-- 287
Cdd:cd16027 143 ----------------------------P---------F-----------------FLWFGFHDPHRPYPPGDGEEPGyd 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 288 LQEVksflkrnKLGPFLllvsflhVHIPLIttknflgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 367
Cdd:cd16027 169 PEKV-------KVPPYL-------PDTPEV-------REDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG 227
|
...
gi 1864524953 368 GSL 370
Cdd:cd16027 228 MPF 230
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
50-367 |
1.02e-35 |
|
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: 137.66 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqwTG 129
Cdd:cd16031 3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT----------DN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesaGDHCHHPlhHGFDYFYGMPlsmtgdcahwelsekrvdlEQkl 209
Cdd:cd16031 73 NGPLFDASQPTYPKLLRKAGYQTAFIGKWHLG------SGGDLPP--PGFDYWVSFP-------------------GQ-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 nflfqvlalvtltlaagkfmhlisiswmpviwsallavflltTSYFAGALIVhadcflMRNHTITEQPmrfqrVTPLILQ 289
Cdd:cd16031 124 ------------------------------------------GSYYDPEFIE------NGKRVGQKGY-----VTDIITD 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 290 EVKSFLKRNKLG-PFLLLVSFLHVH-----------------IPLITT---KNFLGKS-------------------AHG 329
Cdd:cd16031 151 KALDFLKERDKDkPFCLSLSFKAPHrpftpaprhrglyedvtIPEPETfddDDYAGRPewareqrnrirgvldgrfdTPE 230
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1864524953 330 LYGDNVE-------EMDWMVGQILDALDTEGLTNSTLIYFASDHG 367
Cdd:cd16031 231 KYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNG 275
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
50-161 |
2.12e-35 |
|
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: 136.42 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEFGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSVGYRVLQWT 128
Cdd:cd16025 3 PNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGKP 78
|
90 100 110
....*....|....*....|....*....|...
gi 1864524953 129 GASGGLPTNETTFAKILKEKGYATGLIGKWHLG 161
Cdd:cd16025 79 GYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG 111
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-370 |
3.76e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 124.64 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqWTG 129
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 A-SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdhcHHPLHHGFDYFygMPLSMTGDcaHWeLSEKRVDLEQK 208
Cdd:cd16033 76 AySRGLPPGVETFSEDLREAGYRNGYVGKWHVGPE--------ETPLDYGFDEY--LPVETTIE--YF-LADRAIEMLEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 209 LnflfqvlalvtltLAAGK-FMHLISIsWMPviwsallavfllttsyfagalivHADCF-------LMRNHTItEQPMRF 280
Cdd:cd16033 143 L-------------AADDKpFFLRVNF-WGP-----------------------HDPYIppepyldMYDPEDI-PLPESF 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 281 QRvtPLILqevKSFLKRNKLGPFLLLVSFLHVHIPLIttknflgksAHglYGDNVEEMDWMVGQILDALDTEGLTNSTLI 360
Cdd:cd16033 185 AD--DFED---KPYIYRRERKRWGVDTEDEEDWKEII---------AH--YWGYITLIDDAIGRILDALEELGLADDTLV 248
|
330
....*....|
gi 1864524953 361 YFASDHGGSL 370
Cdd:cd16033 249 IFTSDHGDAL 258
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-367 |
8.89e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 116.10 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 129
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGV----------WDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASgGLPTNETTFAKILKEKGYATGLIGKWHLglncESAGDhchhplHHGFDYfygmplsmtgdcahwelsekrvDLEqkl 209
Cdd:cd16037 71 AD-PYDGDVPSWGHALRAAGYETVLIGKLHF----RGEDQ------RHGFRY----------------------DRD--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplILQ 289
Cdd:cd16037 115 -----------------------------------------------------------------------------VTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 290 EVKSFLKRNKL--GPFLLLVSFLHVHIPLITTKNFLGKSAHGL---YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFAS 364
Cdd:cd16037 118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
...
gi 1864524953 365 DHG 367
Cdd:cd16037 198 DHG 200
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-161 |
1.46e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 113.87 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTG 129
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHLG 161
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG 112
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
50-367 |
8.38e-27 |
|
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: 110.75 E-value: 8.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 129
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASgGLPTNETTFAKILKEKGYATGLIGKWHLglncesagdhCHHPLHHGFDYfygmplsmtgdcahwelsekrvDLEqkl 209
Cdd:cd16032 71 AA-EFPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFDY----------------------DEE--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 nflfqvlalvtltlaagkfmhlisiswmpVIWSALLAVFllttsyfagalivhaDcfLMRNHTiteqpmrfqrvtplilq 289
Cdd:cd16032 115 -----------------------------VAFKAVQKLY---------------D--LARGED----------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 290 evksflKRnklgPFLLLVSFLHVHIPLITTKNFLG----KSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASD 365
Cdd:cd16032 132 ------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
|
..
gi 1864524953 366 HG 367
Cdd:cd16032 201 HG 202
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-160 |
8.66e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 111.55 E-value: 8.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgYRvlqwtg 129
Cdd:cd16152 2 PNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR------ 70
|
90 100 110
....*....|....*....|....*....|.
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKWHL 160
Cdd:cd16152 71 NGIPLPADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-384 |
2.54e-23 |
|
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: 99.16 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssvgyrvLQWT 128
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 129 GASGGLPTNETTFAKILKEKGYATGLIgkwhlglncesaGDHCHHPLHHGFDyfygmplsmtgdcahwelseKRVDleqk 208
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFD--------------------RGFD---- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 209 lnflfqvlalvtltlaagkfmhlisiSWMPVIWsallavfllttsyfagalivhadcflMRNHTITEQPMRFQRVTplil 288
Cdd:cd16148 111 --------------------------TFEDFRG--------------------------QEGDPGEEGDERAERVT---- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 289 QEVKSFLKRNKLG-PFlllvsFLHVHIplittknFlgkSAHGLYG-DN-VEEMDWMVGQILDALDTEGLTNSTLIYFASD 365
Cdd:cd16148 135 DRALEWLDRNADDdPF-----FLFLHY-------F---DPHEPYLyDAeVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
|
330
....*....|....*....
gi 1864524953 366 HGgslENQFANSQYGGWNG 384
Cdd:cd16148 200 HG---EEFGEHGLYWGHGS 215
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
50-367 |
7.67e-23 |
|
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: 100.73 E-value: 7.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqWTG 129
Cdd:cd16030 3 PNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----FRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGglptNETTFAKILKEKGYATGLIGKWHlglncesagdhchhplHHGFDYFYGMPLSmtgdcahWELSEKRVDLEQKL 209
Cdd:cd16030 78 VAP----DAVTLPQYFKENGYTTAGVGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEKYP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 NFLFQVLALVTLTLAAGKFMHLISI--SWMPVIWSALLAVFLLTT------SYFAGA--------LIVHADCFLMRNHTI 273
Cdd:cd16030 131 PGKLCPGKKGGKGGGGGPAWEAADVpdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPLES 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 274 TEQPMRFQRV-TPLI----LQEVksflkRNKLGPFLLLVSFLHVHIPLITTKNFLgksaHGLYGdNVEEMDWMVGQILDA 348
Cdd:cd16030 211 IPLPNPFDPIdLPEVawndLDDL-----PKYGDIPALNPGDPKGPLPDEQARELR----QAYYA-SVSYVDAQVGRVLDA 280
|
330
....*....|....*....
gi 1864524953 349 LDTEGLTNSTLIYFASDHG 367
Cdd:cd16030 281 LEELGLADNTIVVLWSDHG 299
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-200 |
4.30e-22 |
|
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: 97.81 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEFGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSVGYRVLQw 127
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864524953 128 tgasgglpTNETTFAKILKE---KGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGMPLSMTGDCAHWELSE 200
Cdd:cd16154 78 --------SEETLLQLLIKDattAGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAGILGGGVQDYYNWNLTN 139
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-367 |
9.24e-22 |
|
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: 97.31 E-value: 9.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssvGYRVLQWT 128
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 129 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHChhplhhgfdyfygmplsmTGDcahWELSEKRVD-LEQ 207
Cdd:cd16150 74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC------------------DSD---EACVRTAIDwLRN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 208 KLN----FLFqvlalVTLTL------AAGKFMHLISISWMPVIWSAllavfLLTTSYFAGALIvhadcfLMRNHtiteqp 277
Cdd:cd16150 128 RRPdkpfCLY-----LPLIFphppygVEEPWFSMIDREKLPPRRPP-----GLRAKGKPSMLE------GIEKQ------ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 278 mRFQRVTPLILQEVKsflkrnklgpflllvsflhvhiplittKNFLGKsahglygdnVEEMDWMVGQILDALDTEGLTNS 357
Cdd:cd16150 186 -GLDRWSEERWRELR---------------------------ATYLGM---------VSRLDHQFGRLLEALKETGLYDD 228
|
330
....*....|
gi 1864524953 358 TLIYFASDHG 367
Cdd:cd16150 229 TAVFFFSDHG 238
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
50-185 |
1.06e-21 |
|
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: 97.84 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTG 129
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864524953 130 aSGGLPTNETTFAKILKEKGYATGLIGKWHLglnceSAGDH-----ChhPLHHGFDYFYGM 185
Cdd:cd16156 71 -CMALGDNVKTIGQRLSDNGIHTAYIGKWHL-----DGGDYfgngiC--PQGWDPDYWYDM 123
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-161 |
2.48e-21 |
|
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: 95.71 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssvgyrv 124
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE-------- 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 1864524953 125 lqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLG 161
Cdd:cd16155 74 ----GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNG 106
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
50-372 |
4.45e-21 |
|
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: 92.10 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSvGYRVLQWT 128
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGN-GSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 129 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqk 208
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 209 lnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplil 288
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 289 qeVKSFLKRNKLG-PFLLLVSFLHVHIPLittknFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 367
Cdd:cd00016 108 --LLKAIDETSKEkPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
|
....*
gi 1864524953 368 GSLEN 372
Cdd:cd00016 181 GIDKG 185
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-161 |
8.09e-21 |
|
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: 92.44 E-value: 8.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSS 119
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1864524953 120 VGYrvlqWTGASGGLPtnetTFAKILKEKGYATGLIGKWHLG 161
Cdd:cd16153 82 EAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSHLE 115
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
50-367 |
1.07e-20 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 94.74 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssVGYrvlqwt 128
Cdd:PRK13759 7 PNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR---VGY------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 129 gASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesagdhchHP--LHHGFDYfygmplSMTGDcahWELSEKRVDLE 206
Cdd:PRK13759 77 -GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNEDK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 207 QKLNFLFQVLALVTLTlAAGKFMHLISISWMPVIWSAllavfllttsyfagalivhadcflmRNHTITEQpmrfQRVTPL 286
Cdd:PRK13759 135 SQFDFVSDYLAWLREK-APGKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPTNW 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 287 ILQEVKSFLKR-NKLGPFLLLVSFLHVHIPLITTKNFL-------------------------GKSAHGLYGD------- 333
Cdd:PRK13759 185 VGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeeyar 264
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1864524953 334 --------NVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 367
Cdd:PRK13759 265 raraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG 306
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
50-367 |
9.53e-20 |
|
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: 91.55 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqWTG 129
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASggLPTNETTFAKILKEKGYATGLIGKWHLglnceSAGDHCHHPLH----------HGFDY-----FYGMPLSmtgDCA 194
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDT-----SPDPRGLAPLDprllsyelamPGFDPvdrldEYPAEDS---DTA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 195 HweLSEKrvdleqklnflfqvlALVTLTLAAGK--FMHLISISWMPviwsallavfllttsyfagALIVHADCFLMRNHT 272
Cdd:cd16028 142 F--LTDR---------------AIEYLDERQDEpwFLHLSYIRPHP-------------------PFVAPAPYHALYDPA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 273 ITEQPMRfqRVTPLILQEVKSFLKRnklgpflllvsflhvHIPLITTKNFLGKSAHGLYGDN-------------VEEMD 339
Cdd:cd16028 186 DVPPPIR--AESLAAEAAQHPLLAA---------------FLERIESLSFSPGAANAADLDDeevaqmratylglIAEVD 248
|
330 340
....*....|....*....|....*...
gi 1864524953 340 WMVGQILDALDTEGLTNSTLIYFASDHG 367
Cdd:cd16028 249 DHLGRLFDYLKETGQWDDTLIVFTSDHG 276
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
50-185 |
8.43e-18 |
|
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: 85.29 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSVGYRVL 125
Cdd:cd16147 2 PNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPKF 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864524953 126 QWTGAsgglptNETTFAKILKEKGYATGLIGKWhlgLN-CESAGDHCHHPLhhGFDYFYGM 185
Cdd:cd16147 78 WQNGL------ERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGL 127
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-367 |
1.48e-14 |
|
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: 74.55 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYR 123
Cdd:cd16035 1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 124 VlQWTgasggLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdhchhplhhgfdyfygmplSMTGDCAHwelsekrv 203
Cdd:cd16035 75 M-QPL-----LSPDVPTLGHMLRAAGYYTAYKGKWHLS--------------------------GAAGGGYK-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 204 dleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmRNHTITEQPMRFqrv 283
Cdd:cd16035 115 -----------------------------------------------------------------RDPGIAAQAVEW--- 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 284 tpliLQEVKSflKRNKLGPFLLLVSFL--H-VHIPLITTKNFlgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLI 360
Cdd:cd16035 127 ----LRERGA--KNADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIV 198
|
....*..
gi 1864524953 361 YFASDHG 367
Cdd:cd16035 199 VFTSDHG 205
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
31-205 |
4.53e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 52.06 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 31 LSVLLSLAPSASSDVSASWPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEFGVKLTQHISAA-SLCTPSRAAFLTGR 109
Cdd:COG1524 5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 110 YPVRSGMVSSVGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIGKWHLGlncESAGDHCHHPLHH-G 178
Cdd:COG1524 80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdG 156
|
170 180
....*....|....*....|....*....
gi 1864524953 179 FDYFYGMPLS--MTGDCAHWELSEKRVDL 205
Cdd:COG1524 157 RKPLLGNPAAdrWIAAAALELLREGRPDL 185
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
50-367 |
3.54e-06 |
|
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: 49.08 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssvgyRVLQWTG 129
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESWN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 130 ASGGLPTNETTFAKILKEKGYATGLIGKwhlglncesagdhchhplhhgFDYFYGmplsmtgdcaHWELSEKRVDLEQKL 209
Cdd:cd16171 70 NYKGLDPNYPTWMDRLEKHGYHTQKYGK---------------------LDYTSG----------HHSVSNRVEAWTRDV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 210 NFLFQVLALVTLTLAAGKfmhlisiswmpviwsallavfllttsyfagalivHADCFLMRNHTITEQPMRFQRVTPLILQ 289
Cdd:cd16171 119 PFLLRQEGRPTVNLVGDR----------------------------------STVRVMLKDWQNTDKAVHWIRKEAPNLT 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 290 EvksflkrnklgPFLLlvsFLHVHIPLITTKNFLGKSAHGL------YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFA 363
Cdd:cd16171 165 Q-----------PFAL---YLGLNLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTYVFFT 230
|
....
gi 1864524953 364 SDHG 367
Cdd:cd16171 231 SDHG 234
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
50-379 |
4.88e-05 |
|
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: 44.98 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 50 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEFGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSVGYRvl 125
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 126 qwtgasgglPTNETTFAKILKEKGYATGLIgkwhlglncesagdHCHHP---------LHHGFDYFYG---MPLSMTGDc 193
Cdd:cd16015 77 ---------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFYDledFPDDEKET- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 194 AHWELSEKrvdleqklnFLFQVLALVTLTLAAGKFMhlisiswmpviwsallaVFLLTTSyfagalivhadcflmrNHti 273
Cdd:cd16015 133 NGWGVSDE---------SLFDQALEELEELKKKPFF-----------------IFLVTMS----------------NH-- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524953 274 teqpmrfqrvtplilqevksflkrnklGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYgdnveEMDWMVGQILDALDTEG 353
Cdd:cd16015 169 ---------------------------GPYDLPEEKKDEPLKVEEDKTELENYLNAIH-----YTDKALGEFIEKLKKSG 216
|
330 340
....*....|....*....|....*.
gi 1864524953 354 LTNSTLIYFASDHGGSLENQFANSQY 379
Cdd:cd16015 217 LYENTIIVIYGDHLPSLGSDYDETDE 242
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
333-367 |
3.74e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 39.71 E-value: 3.74e-03
10 20 30
....*....|....*....|....*....|....*
gi 1864524953 333 DNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 367
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
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