|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
6-530 |
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: 764.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSpYNLNRALTW 85
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMAS-SHGMRVILF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 LGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNDHCYHPLNHGFHYFYGVPFGLLSDCQASKTPEL---HRW 162
Cdd:cd16159 80 TASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYdlsFDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 163 LRIKLWISTVAIALVPFLLLIPKFarwfsVPWKVIFVFALLAFLFFTSWYSSYGFTRRWNCILMRNHEIIQQPMKEEKVA 242
Cdd:cd16159 160 LFPLLTAFVLITALTIFLLLYLGA-----VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 243 SLMLKEALAFIERVKREPFLLFFSFLHVHTPLISKEKFVGHSKYGRYGDNVEEMDWMVGKILDALDRECLANNTLVYFTS 322
Cdd:cd16159 235 QRLTKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 323 DNGGHLEPLDGAVQLGGWNGIYKGGKGMGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILPQDRVI 402
Cdd:cd16159 315 DNGGHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRII 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 403 DGRNLMPLLEGRASYSDHEFLFHYCGVYLHTVRWHQKDCATVWKAHYVTPKFYPdGTGACYGSGICSCSGD-VTYHDPPL 481
Cdd:cd16159 395 DGRDLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYP-GTEGCCGTLLCRCFGDsVTHHDPPL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1622970644 482 LFDISRDPSEALPLNPDNEPlFDSVIKKMEAAIKEHRRTLTPVPQQFSV 530
Cdd:cd16159 474 LFDLSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLSF 521
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
6-495 |
4.41e-152 |
|
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: 441.62 E-value: 4.41e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvsPYNLNRAltw 85
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL--PGVVGPP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 lGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrnDH-CYHPLNHGFHYFYGVPFGLLSDCqasktpelHRWLR 164
Cdd:cd16026 76 -GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWP--------FPLYR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 165 IKLWIStvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwNCILMRNHEIIQQPMKEEKVASL 244
Cdd:cd16026 140 NDPPGP---------------------------------------------------LPPLMENEEVIEQPADQSSLTQR 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 245 MLKEALAFIERVKREPFLLFFSFLHVHTPLISKEKFVGHSKYGRYGDNVEEMDWMVGKILDALDRECLANNTLVYFTSDN 324
Cdd:cd16026 169 YTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 325 GGHLE---------PLDGAVQL---GGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIG 392
Cdd:cd16026 249 GPWLEygghggsagPLRGGKGTtweGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALA 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 393 GGILPQDRVIDGRNLMPLLEGRASYSDHEFLFHYCGVYLHTVRWHQkdcatvWKAHYVTPKFYPDGTGAcygsgicscsG 472
Cdd:cd16026 312 GAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPGG----------L 375
|
490 500
....*....|....*....|...
gi 1622970644 473 DVTYHDPPLLFDISRDPSEALPL 495
Cdd:cd16026 376 DPTKLEPPLLYDLEEDPGETYNV 398
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
6-508 |
8.22e-123 |
|
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: 368.68 E-value: 8.22e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSPynlNRA-LT 84
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGG---TRVfLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 85 WlgGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNDHCYHPLNHGFHyFYGV--PFGLlsdcqasktpelhrw 162
Cdd:cd16160 78 W--DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGTnlPFTN--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 163 lriklwistvaialvpflllipkfaRWFSVPWKVifvfallaflfftswysSYGFTRRWNCILMRNHEIIQQPMKEEKVA 242
Cdd:cd16160 140 -------------------------SWACDDTGR-----------------HVDFPDRSACFLYYNDTIVEQPIQHEHLT 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 243 SLMLKEALAFIERVKREPFLLFFSFLHVHTPLISKEKFVGHSKYGRYGDNVEEMDWMVGKILDALDRECLANNTLVYFTS 322
Cdd:cd16160 178 ETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 323 DNGGHLEPL----DGAVQLGG----WNgiykggkgmggweGGIRVPGIFRWPSVLeAGRVINEPTSLMDIYPTLSYIGGG 394
Cdd:cd16160 258 DHGPHVEYCleggSTGGLKGGkgnsWE-------------GGIRVPFIAYWPGTI-KPRVSHEVVSTMDIFPTFVDLAGG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 395 ILPQDRVIDGRNLMPLLEGRASYSDHEFLFHYCGVyLHTVRWHQkdcatvWKAHYVTPKF--------YPDGTGACYGSG 466
Cdd:cd16160 324 TLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTQPLpsqesldpNCDGGGPLSDYI 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622970644 467 ICS-CSGD-VTYHDPPLLFDISRDPSEALPLNP-DNEPLFDSVIK 508
Cdd:cd16160 397 VCYdCEDEcVTKHNPPLIFDVEKDPGEQYPLQPsVYEHMLEAVEK 441
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
7-551 |
8.61e-101 |
|
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: 313.23 E-value: 8.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSpynlnrALTWL 86
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYP------GVFYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLScasrNDHCYHPLNHGFHYFYGVPFgllSDCQASKTPELHRWLRIK 166
Cdd:cd16158 76 GSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPY---SHDQGPCQNLTCFPPNIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 LWiSTVAIALVPflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwnCILMRNHEIIQQPMKEEKVASLML 246
Cdd:cd16158 149 CF-GGCDQGEVP--------------------------------------------CPLFYNESIVQQPVDLLTLEERYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 247 KEALAFIERVKRE--PFLLFFSFLHVHTPLISKEKFVGHSKYGRYGDNVEEMDWMVGKILDALDRECLANNTLVYFTSDN 324
Cdd:cd16158 184 KFAKDFIADNAKEgkPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDN 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 325 G------------GHLEPLDGAVQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVInEPTSLMDIYPTLSYIG 392
Cdd:cd16158 264 GpstmrksrggnaGLLKCGKGTTYEGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 393 GGILPqDRVIDGRNLMPLLEGRASYSDHEFLFHYC------GVYlhTVRWHQkdcatvWKAHYVTPKFYPDGTGAcygSG 466
Cdd:cd16158 326 GAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTspdpdkGVF--AVRWGK------YKAHFYTQGAAHSGTTP---DK 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 467 ICSCSGDVTYHDPPLLFDISRDPSEALPLNpdNEPLFDSVIKKMEAAIKEHRRTLTPVPQQFSVFNtiwKPWLQPCC--G 544
Cdd:cd16158 394 DCHPSAELTSHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERFEASMKFGESEINKGE---DPALEPCCkpG 468
|
....*..
gi 1622970644 545 TFPFCGC 551
Cdd:cd16158 469 CTPKPSC 475
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
6-533 |
8.39e-94 |
|
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: 294.76 E-value: 8.39e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSPYNLNR-ALT 84
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARnAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 85 WLGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrNDHCYHPLNHGFHYFYGVPfgllsDCQasktpelhrwlr 164
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLG------HRPQYHPLKHGFDEWFGAP-----NCH------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 165 iklwistvaialvpflllipkFARWFSVPWKVIFVFallaflfftswyssygftRRWNCILMRNHEI-IQQPMKEEKVAS 243
Cdd:cd16157 138 ---------------------FGPYDNKAYPNIPVY------------------RDWEMIGRYYEEFkIDKKTGESNLTQ 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 244 LMLKEALAFIER--VKREPFLLFFSFLHVHTPLISKEKFVGHSKYGRYGDNVEEMDWMVGKILDALDRECLANNTLVYFT 321
Cdd:cd16157 179 IYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFS 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 322 SDNGGhlePLDGAVQLGGWNgIYKGGKGMGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILPQDRV 401
Cdd:cd16157 259 SDNGA---ALISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 402 IDGRNLMPLLegRASYSDHEFLFHYCGVYLHTVRWHQkdcatvWKAHYVTpkfyPDGTGACYGSGICSCSGD----VTYH 477
Cdd:cd16157 335 IDGIDLLPVL--LNGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWT----WSNSWEEFRKGINFCPGQnvpgVTTH 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622970644 478 ------DPPLLFDISRDPSEALPLNPdNEPLFDSVIKKMEAAIKEHRRTLTPVPQQFSVFNT 533
Cdd:cd16157 403 nqtdhtKLPLLFHLGRDPGEKYPISF-KSAEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDL 463
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-492 |
5.45e-93 |
|
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: 290.98 E-value: 5.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGM------VSPYNLN 80
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdvipgRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 81 RALTWLGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrNDHCYHPLNHGFHYFYGVpfgllsdcqasktpelH 160
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIGG----------------T 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 161 RWlriklwistvaialvpfllliPKFARWFSVPWKVIFVFallaflfftswyssygftrrwncilmrnheiiQQPMKEEK 240
Cdd:cd16144 139 GN---------------------GGPPSYYFPPGKPNPDL--------------------------------EDGPEGEY 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 241 VASLMLKEALAFIERVKREPFLLFFSFLHVHTPLISK----EKFVGHSKYGRYGDN-------VEEMDWMVGKILDALDR 309
Cdd:cd16144 166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARpeliEKYEKKKKGLRKGQKnpvyaamIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 310 ECLANNTLVYFTSDNGGHLEPLDGAVQL------------GGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVINE 377
Cdd:cd16144 246 LGLADNTLVIFTSDNGGLSTRGGPPTSNaplrggkgslyeGG-----------------IRVPLIVRWPGVIKPGSVSDV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 378 PTSLMDIYPTLSYIGGGILPQDRVIDGRNLMPLLEGRASYSDHEFLFHYCGVYLHTVrwhQKDCATV----WKAHYvtpk 453
Cdd:cd16144 309 PVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWHFPHYHGQG---GRPASAIrkgdWKLIE---- 381
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622970644 454 FYPDGTgacygsgicscsgdvtyhdpPLLFDISRDPSEA 492
Cdd:cd16144 382 FYEDGR--------------------VELYNLKNDIGET 400
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
6-526 |
1.49e-91 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 286.39 E-value: 1.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSPYNlnraltw 85
Cdd:COG3119 23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 lGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLglscasrndhcyhplnhgfhyfygvpfgllsdcqasktpelhrwlri 165
Cdd:COG3119 96 -GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL----------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 166 klwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswYSSYGFTRRwncilmrnheiiqqpmkeekvaslm 245
Cdd:COG3119 128 ----------------------------------------------YLTDLLTDK------------------------- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 246 lkeALAFIERVKR--EPFLLFFSFLHVHTPLISKEKFVG-----------------------HSKYGRYGDNVEEMDWMV 300
Cdd:COG3119 137 ---AIDFLERQADkdKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnlaprdlteeelRRARAAYAAMIEEVDDQV 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 301 GKILDALDRECLANNTLVYFTSDNGGHLE----------PLDGAvqlggwngiykggkgmggweggIRVPGIFRWPSVLE 370
Cdd:COG3119 214 GRLLDALEELGLADNTIVVFTSDNGPSLGehglrggkgtLYEGG----------------------IRVPLIVRWPGKIK 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 371 AGRVINEPTSLMDIYPTLSYIGGgiLPQDRVIDGRNLMPLLEGRASYSDHEFLFHYCGVY-LHTVRWHQkdcatvWKAHY 449
Cdd:COG3119 272 AGSVSDALVSLIDLLPTLLDLAG--VPIPEDLDGRSLLPLLTGEKAEWRDYLYWEYPRGGgNRAIRTGR------WKLIR 343
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622970644 450 vtpkFYPDGtgacygsgicscsgdvtyhDPPLLFDISRDPSEALPLNpDNEPlfdSVIKKMEAAIKEHRRTLTPVPQ 526
Cdd:COG3119 344 ----YYDDD-------------------GPWELYDLKNDPGETNNLA-ADYP---EVVAELRALLEAWLKELGDPPL 393
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
6-495 |
8.47e-91 |
|
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: 283.98 E-value: 8.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGN-NSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSPYNLNralt 84
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 85 wlgGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCAsrndhcYHPLNHGFHYFYGVPFgllsDCQASktpelhrwlr 164
Cdd:cd16161 77 ---SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA------YLPNSRGFDYYFGIPF----SHDSS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 165 iklwistvaialvpfllLIPKFArwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkeekvasl 244
Cdd:cd16161 134 -----------------LADRYA--------------------------------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 245 mlKEALAFIER--VKREPFLLFFSFLHVHTPL-ISKEKFVGHSKYGRYGDNVEEMDWMVGKILDALDRECLANNTLVYFT 321
Cdd:cd16161 140 --QFATDFIQRasAKDRPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFT 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 322 SDNGGHLEPLDGAVQLGGWNGIYKGGKGMGGWEG---GIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILPQ 398
Cdd:cd16161 218 SDNGPWEVKCELAVGPGTGDWQGNLGGSVAKASTwegGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPP 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 399 DRVIDGRNLMPLLEGRASySDHEFLFHYCGVY-----LHTVRWHQkdcatvWKAHYVTpkfypDGTGACYGSGicscsGD 473
Cdd:cd16161 298 GRIYDGKDLSPVLFGGSK-TGHRCLFHPNSGAagagaLSAVRCGD------YKAHYAT-----GGALACCGST-----GP 360
|
490 500
....*....|....*....|..
gi 1622970644 474 VTYHDPPLLFDISRDPSEALPL 495
Cdd:cd16161 361 KLYHDPPLLFDLEVDPAESFPL 382
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-491 |
3.38e-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: 293761 [Multi-domain] Cd Length: 372 Bit Score: 277.11 E-value: 3.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYG---NNSVSTPNIDRLANEGVRLTQHLAAASmCTPSRAAFLTGRYPIRSGMVSPynlnral 83
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 84 TWLGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrnDHCYH-PLNHGFHYFYGVPFGLLSDcqasktpelhrw 162
Cdd:cd16142 73 GLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG-------DEDGRlPTDHGFDEFYGNLYHTIDE------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 163 lriklwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnhEIIQQpmkeekva 242
Cdd:cd16142 134 -------------------------------------------------------------------EIVDK-------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 243 slmlkeALAFIERVKR--EPFLLFFSFLHVHTPLISKEKFVGHSK-YGRYGDNVEEMDWMVGKILDALDRECLANNTLVY 319
Cdd:cd16142 139 ------AIDFIKRNAKadKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 320 FTSDNGGHLE--------PLDGA---VQLGGWngiykggkgmggweggiRVPGIFRWPSVLEAGRVINEPTSLMDIYPTL 388
Cdd:cd16142 213 FTTDNGPEQDvwpdggytPFRGEkgtTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 389 SYIGGGILP------QDRVIDGRNLMPLLEGRASYSDHEFLFHYCGVYLHTVRWHQkdcatvWKAHYVTpkFYPDGTGAC 462
Cdd:cd16142 276 AALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFKA--QEDTGGPTG 347
|
490 500
....*....|....*....|....*....
gi 1622970644 463 YGSGICSCsgdvtyhdpPLLFDISRDPSE 491
Cdd:cd16142 348 EPFYVLTF---------PLIFNLRRDPKE 367
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-491 |
6.61e-87 |
|
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: 274.46 E-value: 6.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNS-VSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvspynlNRALTW 85
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSR-------LKGGVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 LGGSGGL-PTNETTFAKLLQHRGYRTGLIGKWHLGL----------SCASRNDHCYH------PLNHGFHYFYGVPfgll 148
Cdd:cd16143 74 GGFSPPLiEPDRVTLAKMLKQAGYRTAMVGKWHLGLdwkkkdgkkaATGTGKDVDYSkpikggPLDHGFDYYFGIP---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 149 sdcqASKtpelhrwlriklwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrn 228
Cdd:cd16143 150 ----ASE------------------------------------------------------------------------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 229 heiiqqpmkeekVASLMLKEALAFIERVKR--EPFLLFFSFLHVHTPLISKEKFVGHSKYGRYGDNVEEMDWMVGKILDA 306
Cdd:cd16143 153 ------------VLPTLTDKAVEFIDQHAKkdKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDA 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 307 LDRECLANNTLVYFTSDNGGHLEPLDGAVQL------------------GGwngiykggkgmggweggIRVPGIFRWPSV 368
Cdd:cd16143 221 LKELGLAENTLVIFTSDNGPSPYADYKELEKfghdpsgplrgmkadiyeGG-----------------HRVPFIVRWPGK 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 369 LEAGRVINEPTSLMDIYPTLSYIGGGILPQDRVIDGRNLMPLLEGRASYSDHEFLFHYCGVYLHTVRwhQKDcatvWKah 448
Cdd:cd16143 284 IPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIR--KGD----WK-- 355
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622970644 449 YVTpkfypdgtgaCYGSGICSCSGDVTYHDPP--LLFDISRDPSE 491
Cdd:cd16143 356 LID----------GTGSGGFSYPRGKEKLGLPpgQLYNLSTDPGE 390
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-491 |
3.68e-73 |
|
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: 239.42 E-value: 3.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvspynlnRALTWL 86
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV-------RGNSEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLscasrNDHCYHPLNHGFHYFYGvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16145 74 GGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGG-----PGTPGHPTKQGFDYFYG------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 lWISTVaialvpflllipkFARWFSVPwkvifvfallaFLfftsWYSSYGFTRRWNCILMRNHEIIQQPMKEEKVASLML 246
Cdd:cd16145 125 -YLDQV-------------HAHNYYPE-----------YL----WRNGEKVPLPNNVIPPLDEGNNAGGGGGTYSHDLFT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 247 KEALAFIERVKREPFLLFFSFLHVHTPLISKE---KFVGHSKYGRYGDN------------VEEMDWMVGKILDALDREC 311
Cdd:cd16145 176 DEALDFIRENKDKPFFLYLAYTLPHAPLQVPDdgpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILALLKELG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 312 LANNTLVYFTSDNGGHLE--------------PLDG---AVQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRV 374
Cdd:cd16145 256 IDENTLVVFTSDNGPHSEggsehdpdffdsngPLRGykrSLYEGG-----------------IRVPFIARWPGKIPAGSV 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 375 INEPTSLMDIYPTLSYIGGGILPQDrvIDGRNLMPLLEGRASYSDHEFL---FHYCGvYLHTVRWHQkdcatvWKAHYVT 451
Cdd:cd16145 319 SDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLyweFYEGG-GAQAVRMGG------WKAVRHG 389
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1622970644 452 PKfypdgtgacygsgicscsgdvtyHDPPLLFDISRDPSE 491
Cdd:cd16145 390 KK-----------------------DGPFELYDLSTDPGE 406
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
7-491 |
6.33e-73 |
|
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: 238.60 E-value: 6.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQ-HlaAASMCTPSRAAFLTGRYPIRSGMVSpynlnralTW 85
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTGVWH--------TI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 LGGSgGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrNDHCYHPLNHGFHYFYGVPFGLLSDcqasktpelhrwlri 165
Cdd:cd16146 71 LGRE-RMRLDETTLAEVFKDAGYRTGIFGKWHLG------DNYPYRPQDRGFDEVLGHGGGGIGQ--------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 166 klwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswYSSYGFTRRWNCILMRNHEIIQQpmkEEKVASLM 245
Cdd:cd16146 129 ----------------------------------------------YPDYWGNDYFDDTYYHNGKFVKT---EGYCTDVF 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 246 LKEALAFIERVKREPFLLFFSFLHVHTPLISKEKFVGhsKYGRYGDN---------VEEMDWMVGKILDALDRECLANNT 316
Cdd:cd16146 160 FDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYLD--PYKDMGLDdklaafygmIENIDDNVGRLLAKLKELGLEENT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 317 LVYFTSDNGGHLEPLD----------GAVQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVINEPTSLMDIYP 386
Cdd:cd16146 238 IVIFMSDNGPAGGVPKrfnagmrgkkGSVYEGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 387 TLSYIGGGILPQDRVIDGRNLMPLLEGRASYSDHEFLFhycgvyLHTVRW----HQKDCATVWKAHY--VTPKfypdgtg 460
Cdd:cd16146 301 TLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLF------THSGRWppppKKKRNAAVRTGRWrlVSPK------- 367
|
490 500 510
....*....|....*....|....*....|.
gi 1622970644 461 acygsgicscsgdvtyHDPPLLFDISRDPSE 491
Cdd:cd16146 368 ----------------GFQPELYDIENDPGE 382
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
7-406 |
1.41e-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: 1.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVspynlnralTWL 86
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVR---------GNV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHlglscasrndhcyhplnhgfhyfygvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16022 72 GNGGGLPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 lwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkeekvaslml 246
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 247 KEALAFIERVKRE-PFLLFFSFLHVHTPLIskekfvghskygrYGDNVEEMDWMVGKILDALDRECLANNTLVYFTSDNG 325
Cdd:cd16022 103 DEAIDFIERRDKDkPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHG 169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 326 GHLEplDGAVQLGGWNgiykggkgmgGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILPQDrvIDGR 405
Cdd:cd16022 170 DMLG--DHGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGR 235
|
.
gi 1622970644 406 N 406
Cdd:cd16022 236 S 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-455 |
2.52e-64 |
|
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: 214.77 E-value: 2.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTqHLAAASMCTPSRAAFLTGRYPIRSGMVspynlnraltwl 86
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 ggSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNdhcyHPLNHGFHYFYgvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16151 68 --FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYC------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 LWISTVAIALvpflllipkfarwfsvpwkvifvfallaflfftswYSSYgFTRRWNCILMRNHEIIQQ---PmkeekvaS 243
Cdd:cd16151 117 LWQLTETGEK-----------------------------------YSRP-ATPTFNIRNGKLLETTEGdygP-------D 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 244 LMLKEALAFIERVKREPFLLFFSFLHVHTPL-----------ISKEKFvghSKYGRYGDNVEEMDWMVGKILDALDRECL 312
Cdd:cd16151 154 LFADFLIDFIERNKDQPFFAYYPMVLVHDPFvptpdspdwdpDDKRKK---DDPEYFPDMVAYMDKLVGKLVDKLEELGL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 313 ANNTLVYFTSDNGGHLEP---LDGAVQLGGwngiykggkGMGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLS 389
Cdd:cd16151 231 RENTIIIFTGDNGTHRPItsrTNGREVRGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLA 301
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622970644 390 YIGGGILPQDRVIDGRNLMPLLEGRASYSDHEFLFHycgvYLHTVRWHQKDCA---TVWKaHYVTPKFY 455
Cdd:cd16151 302 ELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYW----YYRNPHKKFGSRFvrtKRYK-LYADGRFF 365
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
418-551 |
1.37e-61 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 198.69 E-value: 1.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 418 SDHEFLFHYCGVYLHTVRWHQkdcatvWKAHYVTPKFYPDGTGACYGSGICscsgdVTYHDPPLLFDISRDPSEALPLNP 497
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP-----VTHHDPPLLFDLERDPSEKYPLSP 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622970644 498 DNePLFDSVIKKMEAAIKEHRRTLTPVPQQFSVFNTIWKPWLQPCCGTFPFCGC 551
Cdd:pfam14707 70 DS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
7-426 |
8.43e-58 |
|
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: 198.16 E-value: 8.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAAsMCTPSRAAFLTGRYPIRSGMVSPYNLNraltwl 86
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscASRNDHCyhPLNHGFHYFYGvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16029 74 GEPYGLPLNETLLPQYLKELGYATHLVGKWHLG---FYTWEYT--PTNRGFDSFYG------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 lwistvaialvpflllipkfarwfsvpwkvifvfallaflFFTS----WYSSYGFTRRWNCILMRNHEIIQQPMKEEKVA 242
Cdd:cd16029 125 ----------------------------------------YYGGaedyYTHTSGGANDYGNDDLRDNEEPAWDYNGTYST 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 243 SLMLKEALAFIER-VKREPFLLFFSFLHVHTPLISKEKFVGHSKYGRYGDN----------VEEMDWMVGKILDALDREC 311
Cdd:cd16029 165 DLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKdedrrtyaamVSALDESVGNVVDALKAKG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 312 LANNTLVYFTSDNGGHLE--------PLDGA---VQLGGwngiykggkgmggweggIRVPGiFRWPSVLE--AGRVINEP 378
Cdd:cd16029 245 MLDNTLIVFTSDNGGPTGggdggsnyPLRGGkntLWEGG-----------------VRVPA-FVWSPLLPpkRGTVSDGL 306
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622970644 379 TSLMDIYPTLSYIGGGILPQDRVIDGRNLMPLLEGRASYSDHEFLFHY 426
Cdd:cd16029 307 MHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNI 354
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
7-424 |
7.45e-56 |
|
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: 192.34 E-value: 7.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNsVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvspYNLNRALTWl 86
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNV-VKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 ggsggLPTNETTFAKLLQHRGYRTGLIGKWHlglscasrndhcyhplnHGFHYFYGVPFGLLSDCQASKTPELHrwlrik 166
Cdd:cd16027 76 -----LPDGVKTLPELLREAGYYTGLIGKTH-----------------YNPDAVFPFDDEMRGPDDGGRNAWDY------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 lwistvaialvpflllIPKFARWFSV-----PWkvifvfallaFLFFTSWYSsygftrrwncilmrnHEIIQQPMKEEKV 241
Cdd:cd16027 128 ----------------ASNAADFLNRakkgqPF----------FLWFGFHDP---------------HRPYPPGDGEEPG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 242 ASLmlkealafiERVKREPFLlffsflhVHTPLISKEkfvghskYGRYGDNVEEMDWMVGKILDALDRECLANNTLVYFT 321
Cdd:cd16027 167 YDP---------EKVKVPPYL-------PDTPEVRED-------LADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFT 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 322 SDNGGhlePLDGA---VQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVINEPTSLMDIYPT-LSYIGggiLP 397
Cdd:cd16027 224 SDHGM---PFPRAkgtLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTlLDLAG---IE 280
|
410 420
....*....|....*....|....*..
gi 1622970644 398 QDRVIDGRNLMPLLEGrASYSDHEFLF 424
Cdd:cd16027 281 PPEYLQGRSFLPLLKG-EKDPGRDYVF 306
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
7-388 |
1.38e-53 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 183.78 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSPYNlnraltwl 86
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 ggsGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLScaSRNDhcyhPLNHGFHYFYGvpFGLLSDcqasktpelhrwlrik 166
Cdd:pfam00884 73 ---VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWY--NNQS----PCNLGFDKFFG--RNTGSD---------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 lwistvaialvpflllipkfarwfsvpwkvifvfallaflffTSWYSSYgftRRWNCILMRNHEIIqqpmkeekvaslML 246
Cdd:pfam00884 126 ------------------------------------------LYADPPD---VPYNCSGGGVSDEA------------LL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 247 KEALAFIERVKRePFLLFFSFLHVHTPLISKEKFVGHSK------------YGRYGDNVEEMDWMVGKILDALDRECLAN 314
Cdd:pfam00884 149 DEALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622970644 315 NTLVYFTSDNGGHLEPLDGAVQLGGWNgiykggkgmGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTL 388
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTI 292
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-489 |
5.85e-52 |
|
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: 182.77 E-value: 5.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvsPYNLNRaltw 85
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV--FGNDVP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 lggsggLPTNETTFAKLLQHRGYRTGLIGKWHLG----LSCASRNDHCYHPLNHGFHYFYGvpfgllSDCQasktpelHR 161
Cdd:cd16034 75 ------LPPDAPTIADVLKDAGYRTGYIGKWHLDgperNDGRADDYTPPPERRHGFDYWKG------YECN-------HD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 162 wlriklwistvaialvpflllipkfarwfsvpwkvifvfallaflFFTSWYssygFTRRWNCILMRNHEIIQQpmkeekv 241
Cdd:cd16034 136 ---------------------------------------------HNNPHY----YDDDGKRIYIKGYSPDAE------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 242 aslmLKEALAFIERVKRE--PFLLFFSFLHVHTP------------------------LISKEKFVGHSKYGRYGDNVEE 295
Cdd:cd16034 160 ----TDLAIEYLENQADKdkPFALVLSWNPPHDPyttapeeyldmydpkklllrpnvpEDKKEEAGLREDLRGYYAMITA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 296 MDWMVGKILDALDRECLANNTLVYFTSDNG------GHLE---PLDGAvqlggwngiykggkgmggweggIRVPGIFRWP 366
Cdd:cd16034 236 LDDNIGRLLDALKELGLLENTIVVFTSDHGdmlgshGLMNkqvPYEES----------------------IRVPFIIRYP 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 367 SVLEAGRVINEPTSLMDIYPTLSYIGGgiLPQDRVIDGRNLMPLLEGRASYSDHEFLFHYcgvylhTVRWHQKDCATVWK 446
Cdd:cd16034 294 GKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLLQC------FVPFGGGSARDGGE 365
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1622970644 447 AHYVTPKFYpdgTGACYGSGicscsgdvtyhdPPLLFDISRDP 489
Cdd:cd16034 366 WRGVRTDRY---TYVRDKNG------------PWLLFDNEKDP 393
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
6-512 |
2.19e-49 |
|
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: 176.57 E-value: 2.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVspyNLNRALtw 85
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT---DNNGPL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 lggsggLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNDhcyhplnhGFHYFYGVPfGllsdcQAS-KTPELH---R 161
Cdd:cd16031 77 ------FDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFP-G-----QGSyYDPEFIengK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 162 WLRIKLWISTV----AIALV-------PFLLLIPKFA--RWFSVPWKVIFVFALLAF----LFFTSWYSsygftrrwnci 224
Cdd:cd16031 137 RVGQKGYVTDIitdkALDFLkerdkdkPFCLSLSFKAphRPFTPAPRHRGLYEDVTIpepeTFDDDDYA----------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 225 lmrnheiiQQPMkeekvaslMLKEALAFIERVKREPFllffsflhvHTPLiskekfvghsKYGRYGDN----VEEMDWMV 300
Cdd:cd16031 206 --------GRPE--------WAREQRNRIRGVLDGRF---------DTPE----------KYQRYMKDylrtVTGVDDNV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 301 GKILDALDRECLANNTLVYFTSDNGGHLepldGAVQLGG-WNgiykggkgmgGWEGGIRVPGIFRWPSVLEAGRVINEPT 379
Cdd:cd16031 251 GRILDYLEEQGLADNTIIIYTSDNGFFL----GEHGLFDkRL----------MYEESIRVPLIIRDPRLIKAGTVVDALV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 380 SLMDIYPT-LSYIGggiLPQDRVIDGRNLMPLLEGRASYS-DHEFLFHYcgvylhtvrWHQKDCATVWKAH-YVTPKF-Y 455
Cdd:cd16031 317 LNIDFAPTiLDLAG---VPIPEDMQGRSLLPLLEGEKPVDwRKEFYYEY---------YEEPNFHNVPTHEgVRTERYkY 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622970644 456 pdgtgACYgsgicscsgdvtYHDPPL--LFDISRDPSEA--LPLNPDNEPLFDSVIKKMEA 512
Cdd:cd16031 385 -----IYY------------YGVWDEeeLYDLKKDPLELnnLANDPEYAEVLKELRKRLEE 428
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
6-492 |
1.60e-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: 173.40 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNnSVSTPNIDRLANEGVRLTQ-HlaAASMCTPSRAAFLTGRYPIRSGMVSPYNLnrALT 84
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGG-EIPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGMGTMAEL--ATG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 85 WLGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrndhcyhplnhgfhyfygvpfgllsdcqasktPElhrwlr 164
Cdd:cd16025 77 KPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG-------------------------------------PD------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 165 iklwistvaialvpflllipkfarwfsvpwkvifvfallaflfftSWYSSYGFTRRwncilmrnheiiqqpmkeekvasl 244
Cdd:cd16025 114 ---------------------------------------------DYYSTDDLTDK------------------------ 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 245 mlkeALAFIERVKRE--PFLLFFSFLHVHTPLISKEKFVghSKY-GRYGDN----------------------------- 292
Cdd:cd16025 125 ----AIEYIDEQKAPdkPFFLYLAFGAPHAPLQAPKEWI--DKYkGKYDAGwdalreerlerqkelglipadtkltprpp 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 293 --------------------------VEEMDWMVGKILDALDRECLANNTLVYFTSDNGGHLE---------PLD---GA 334
Cdd:cd16025 199 gvpawdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEpgwanasntPFRlykQA 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 335 VQLGGwngiykggkgmggweggIRVPGIFRWPS-VLEAGRVINEPTSLMDIYPTL----------SYIGGGILPqdrvID 403
Cdd:cd16025 279 SHEGG-----------------IRTPLIVSWPKgIKAKGGIRHQFAHVIDIAPTIlelagveypkTVNGVPQLP----LD 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 404 GRNLMPLLEGRASYSDHEF----LFHYCGVYlhtvrwhQKDcatvWKAhyvtpkfypdgtgacygsgicscsgdVTYHDP 479
Cdd:cd16025 338 GVSLLPTLDGAAAPSRRRTqyfeLFGNRAIR-------KGG----WKA--------------------------VALHPP 380
|
570
....*....|....*....
gi 1622970644 480 PL------LFDISRDPSEA 492
Cdd:cd16025 381 PGwgdqweLYDLAKDPSET 399
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-450 |
3.31e-45 |
|
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: 164.70 E-value: 3.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSPYNLNRALtwl 86
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 ggSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCAsrndhcyhPLNHGFHYFYGVpfgllsdcQASKTpelhRWL--R 164
Cdd:cd16033 78 --SRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEET--------PLDYGFDEYLPV--------ETTIE----YFLadR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 165 IKLWISTVAIALVPFLLLIPkfarwfsvpwkviFVFALLAFLFFTSWYSSYgftrrwncilmrnheiiqQPMKEEKVASl 244
Cdd:cd16033 136 AIEMLEELAADDKPFFLRVN-------------FWGPHDPYIPPEPYLDMY------------------DPEDIPLPES- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 245 mLKEALA---FIERVKREPFLLFFSFLHVHTPLISkekfvghskygRYGDNVEEMDWMVGKILDALDRECLANNTLVYFT 321
Cdd:cd16033 184 -FADDFEdkpYIYRRERKRWGVDTEDEEDWKEIIA-----------HYWGYITLIDDAIGRILDALEELGLADDTLVIFT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 322 SDNGGHLepldGAvqLGGWNGIYKGGKGMGgweggiRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIgGGILPQDRV 401
Cdd:cd16033 252 SDHGDAL----GA--HRLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDL-AGVDVPPKV 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622970644 402 iDGRNLMPLLEGRASYSDHEFLF---HYCGVYLHTVRWHQKDcatvWKahYV 450
Cdd:cd16033 319 -DGRSLLPLLRGEQPEDWRDEVVteyNGHEFYLPQRMVRTDR----YK--YV 363
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-489 |
1.54e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 152.31 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvspynlnralTWl 86
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETG-----------VW- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscaSRNDhcyhplNHGFHYfygvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16037 69 DNADPYDGDVPSWGHALRAAGYETVLIGKLHFR----GEDQ------RHGFRY--------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 lwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkEEKVAslml 246
Cdd:cd16037 112 -----------------------------------------------------------------------DRDVT---- 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 247 KEALAFIERVKR--EPFLLFFSFLHVHTPLISKEKFVghSKYGR-----YGDNVEEMDWMVGKILDALDRECLANNTLVY 319
Cdd:cd16037 117 EAAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFY--DLYVRraraaYYGLVEFLDENIGRVLDALEELGLLDNTLII 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 320 FTSDNGGHLepldGAVQLGGWNgiykggkgmGGWEGGIRVPGIFRWPSVlEAGRVINEPTSLMDIYPTLSYIGGgiLPQD 399
Cdd:cd16037 195 YTSDHGDML----GERGLWGKS---------TMYEESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAG--APPP 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 400 RVIDGRNLMPLLEG-----RASYSdhEFLFHYCGVYLHTVRWHQkdcatvWKAHYvtpkfYPDgtgacygsgicscsgdv 474
Cdd:cd16037 259 PDLDGRSLLPLAEGpddpdRVVFS--EYHAHGSPSGAFMLRKGR------WKYIY-----YVG----------------- 308
|
490
....*....|....*
gi 1622970644 475 tyhDPPLLFDISRDP 489
Cdd:cd16037 309 ---YPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-409 |
8.33e-40 |
|
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: 145.46 E-value: 8.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYP--------IRSGMVSPYn 78
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPsqhgihdwIVEGSHGKT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 79 lNRALTWLGGsgglptnETTFAKLLQHRGYRTGLIGKWHLGlscasrndhcyhplnhgfhyfygvpfgllsdcqasktpe 158
Cdd:cd16149 80 -KKPEGYLEG-------QTTLPEVLQDAGYRCGLSGKWHLG--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 159 lhrwlriklwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmke 238
Cdd:cd16149 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 239 ekvaslmlKEALAFIERV--KREPFLLFFSFLHVHTPliskekfvghskYGrYGDNVEEMDWMVGKILDALDRECLANNT 316
Cdd:cd16149 113 --------DDAADFLRRRaeAEKPFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENT 171
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 317 LVYFTSDNG---GH---LEPLDGAVQLGGWNgiykggkgmggweGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSY 390
Cdd:cd16149 172 LVIFTSDNGfnmGHhgiWGKGNGTFPLNMYD-------------NSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLE 238
|
410
....*....|....*....
gi 1622970644 391 IGGGILPQDRVIDGRNLMP 409
Cdd:cd16149 239 LAGVDPPADPRLPGRSFAD 257
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
7-489 |
4.47e-36 |
|
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: 137.32 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvspYNlNRAltwl 86
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA---YD-NAA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 ggsgGLPTNETTFAKLLQHRGYRTGLIGKWH------LglscasrndhcyhplnHGFHYfygvpfgllsDCQAsktpelh 160
Cdd:cd16032 73 ----EFPADIPTFAHYLRAAGYRTALSGKMHfvgpdqL----------------HGFDY----------DEEV------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 161 rwlriklwistvaialvpflllipkfarwfsvpwkvifVFALLAFLFftswyssygftrrwncILMRNHEiiqqpmkeek 240
Cdd:cd16032 116 --------------------------------------AFKAVQKLY----------------DLARGED---------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 241 vaslmlkealafiervkREPFLLFFSFLHVHTPLISKEKF----VGHSKYGRYGdNVEEMDWMVGKILDALDRECLANNT 316
Cdd:cd16032 132 -----------------GRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDT 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 317 LVYFTSDNGGHL---------EPLDGAVqlggwngiykggkgmggweggiRVPGIFRWPSVLEAGRViNEPTSLMDIYPT 387
Cdd:cd16032 194 IVIFTSDHGDMLgerglwykmSFFEGSA----------------------RVPLIISAPGRFAPRRV-AEPVSLVDLLPT 250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 388 L-SYIGGGILPQDRVIDGRNLMPLLEGRASYSDHEFLFHYCGVYLHTvrwhqkDCATVWKAHYvtpKFYpdgtgacygsg 466
Cdd:cd16032 251 LvDLAGGGTAPHVPPLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVA------PCVMIRRGRW---KFI----------- 310
|
490 500
....*....|....*....|...
gi 1622970644 467 icscsgdVTYHDPPLLFDISRDP 489
Cdd:cd16032 311 -------YCPGDPDQLFDLEADP 326
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
6-435 |
1.38e-35 |
|
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: 138.47 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVgDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvspYNLNRALTW 85
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV---YDNNSYFRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 LGGsgglptNETTFAKLLQHRGYRTGLIGKwhlglscasrndhCYHPlnhgfhyfyGVPFGLLSDCQASKTPelhrwlri 165
Cdd:cd16030 78 VAP------DAVTLPQYFKENGYTTAGVGK-------------IFHP---------GIPDGDDDPASWDEPP-------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 166 klwistvaialvpfllliPKFARWFSVPWKVIFVfallaflffTSWYSSYGFTRRWNCILMRNHEiiqqpMKEEKVASlm 245
Cdd:cd16030 122 ------------------NPPGPEKYPPGKLCPG---------KKGGKGGGGGPAWEAADVPDEA-----YPDGKVAD-- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 246 lkEALAFIERVKR--EPFLLFFSFLHVHTPLISKEKF----------VGHS---------KYGRYGDNVEE--------- 295
Cdd:cd16030 168 --EAIEQLRKLKDsdKPFFLAVGFYKPHLPFVAPKKYfdlyplesipLPNPfdpidlpevAWNDLDDLPKYgdipalnpg 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 296 ------------------------MDWMVGKILDALDRECLANNTLVYFTSDNGGHLE---------PLDGAVqlggwng 342
Cdd:cd16030 246 dpkgplpdeqarelrqayyasvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGehghwgkhtLFEEAT------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 343 iykggkgmggweggiRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGgiLPQDRVIDGRNLMPLLEGRASYSDHEF 422
Cdd:cd16030 319 ---------------RVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKDAA 381
|
490
....*....|....*
gi 1622970644 423 L--FHYCGVYLHTVR 435
Cdd:cd16030 382 FsqYPRPSIMGYSIR 396
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-409 |
1.71e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 131.52 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLM-----ADDLGvgdlcCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIrsgmvspynlnr 81
Cdd:cd16148 1 MNVILIVidslrADHLG-----CYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPF------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 82 alTWLGGSGGLPTNETTFAKLLQHRGYRTGLIGkwhlglscasrnDHCYHPLNHGFHyfygvpfgllsdcqasktpelhr 161
Cdd:cd16148 64 --YHGVWGGPLEPDDPTLAEILRKAGYYTAAVS------------SNPHLFGGPGFD----------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 162 wlriklwistvaialvpflllipkfarwfsvpwkvifvfallaFLFFTSWYSSYGFTRRWNCILMRNHEIIQqpmkeekv 241
Cdd:cd16148 107 -------------------------------------------RGFDTFEDFRGQEGDPGEEGDERAERVTD-------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 242 aslmlkEALAFIERVKR-EPFLLFFSFLHVHTPliskekfvghskYgRYGDNVEEMDWMVGKILDALDRECLANNTLVYF 320
Cdd:cd16148 136 ------RALEWLDRNADdDPFFLFLHYFDPHEP------------Y-LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIV 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 321 TSD----------NGGHLEPLDGAVqlggwngiykggkgmggweggIRVPGIFRWPSVlEAGRVINEPTSLMDIYPT-LS 389
Cdd:cd16148 197 TSDhgeefgehglYWGHGSNLYDEQ---------------------LHVPLIIRWPGK-EPGKRVDALVSHIDIAPTlLD 254
|
410 420
....*....|....*....|
gi 1622970644 390 YIGGgilPQDRVIDGRNLMP 409
Cdd:cd16148 255 LLGV---EPPDYSDGRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
7-519 |
9.54e-34 |
|
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: 133.54 E-value: 9.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMV---SPynlnral 83
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVwngTP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 84 twlggsggLPTNETTFAKLLQHRGYRTGLIGKWHL-----GLSCASRNDHCYHPLNHGFHyfYGVPFGLLSDcQASKTPe 158
Cdd:cd16028 74 --------LDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFD--PVDRLDEYPA-EDSDTA- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 159 lhrwlriklWISTVAIAlvpflllipkfarWFSV----PWkvifvFALLAFL-----FFTS--WYSSYgftrrwncilmr 227
Cdd:cd16028 142 ---------FLTDRAIE-------------YLDErqdePW-----FLHLSYIrphppFVAPapYHALY------------ 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 228 NHEIIQQPMKEEKVASLMLKEAL--AFIERVKREPFllffsFLHVHTPLISKEKFVGHSKYGRYGdNVEEMDWMVGKILD 305
Cdd:cd16028 183 DPADVPPPIRAESLAAEAAQHPLlaAFLERIESLSF-----SPGAANAADLDDEEVAQMRATYLG-LIAEVDDHLGRLFD 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 306 ALDRECLANNTLVYFTSDNGGHLepldGAVQLGGwngiykggkGMGGWEGGIRVPGIFRWPSVLE---AGRVINEPTSLM 382
Cdd:cd16028 257 YLKETGQWDDTLIVFTSDHGEQL----GDHWLWG---------KDGFFDQAYRVPLIVRDPRREAdatRGQVVDAFTESV 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 383 DIYPT-LSYIGGGILPQdrvIDGRNLMPLLEG-------RASYSDHEFlfhYCGVYLHTVR---WHQKDC-ATV-----W 445
Cdd:cd16028 324 DVMPTiLDWLGGEIPHQ---CDGRSLLPLLAGaqpsdwrDAVHYEYDF---RDVSTRRPQEalgLSPDECsLAVirderW 397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622970644 446 KahYVT-PKFypdgtgacygsgicscsgdvtyhdPPLLFDISRDPSEALPLNPDnePLFDSVIKKMEAAIKEHRR 519
Cdd:cd16028 398 K--YVHfAAL------------------------PPLLFDLKNDPGELRDLAAD--PAYAAVVLRYAQKLLSWRM 444
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
1-426 |
2.33e-32 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 130.17 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 1 MTRNARPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVspynln 80
Cdd:PRK13759 1 MVQTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 81 raltwlGGSGGLPTN-ETTFAKLLQHRGYRTGLIGKWHLGlscASRNDHCYH-------PLNHGFHYfYGVPFGLLSDCQ 152
Cdd:PRK13759 75 ------GYGDVVPWNyKNTLPQEFRDAGYYTQCIGKMHVF---PQRNLLGFHnvllhdgYLHSGRNE-DKSQFDFVSDYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 153 AsktpelhrWLRIKlwistvAIALVPFLllipkfarwfsvpwkvifvfallaflfftswyssygFTRRWNCilmrnHEII 232
Cdd:PRK13759 145 A--------WLREK------APGKDPDL------------------------------------TDIGWDC-----NSWV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 233 QQPM-KEEKV--ASLMLKEALAFIERV-KREPFLLFFSFLHVHTPL---------------------------------- 274
Cdd:PRK13759 170 ARPWdLEERLhpTNWVGSESIEFLRRRdPTKPFFLKMSFARPHSPYdppkryfdmykdadipdphigdweyaedqdpegg 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 275 -------ISKEKFVGHSKYGRYGdNVEEMDWMVGKILDALDRECLANNTLVYFTSDNGGHLE---------PLDGAvqlg 338
Cdd:PRK13759 250 sidalrgNLGEEYARRARAAYYG-LITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGdhylfrkgyPYEGS---- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 339 gwngiykggkgmggweggIRVPGIFRWPS---VLEAGRVINEPTSLMDIYPTLSYIGGGILPQDrvIDGRNLMPLLEGRA 415
Cdd:PRK13759 325 ------------------AHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQY 384
|
490
....*....|....*
gi 1622970644 416 S----YSDHEFLFHY 426
Cdd:PRK13759 385 EgwrpYLHGEHALGY 399
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-515 |
4.46e-32 |
|
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: 127.30 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASM----CTPSRAAFLTGRypirsgmvspyNLNR 81
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR-----------TLFH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 82 ALtwLGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHlglscasrNDHCYHPLNHgfhyfygvpfglLSDCQASKTpelhr 161
Cdd:cd16155 71 AP--EGGKAAIPSDDKTWPETFKKAGYRTFATGKWH--------NGFADAAIEF------------LEEYKDGDK----- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 162 wlriklwistvaialvPFLLLIPkfarwFSVPwkvifvfallaflfftswyssygftrrwncilmrnHEIIQQPMKeekv 241
Cdd:cd16155 124 ----------------PFFMYVA-----FTAP-----------------------------------HDPRQAPPE---- 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 242 aslmlkealaFIERVKREPFLLFFSFLHVHT-----PLISKEKFVGH--------SKYGRYGDNVEEMDWMVGKILDALD 308
Cdd:cd16155 144 ----------YLDMYPPETIPLPENFLPQHPfdngeGTVRDEQLAPFprtpeavrQHLAEYYAMITHLDAQIGRILDALE 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 309 RECLANNTLVYFTSDNG---GH--LepldgavqLGGWNgiykggkgmgGWEGGIRVPGIFRWPSVlEAGRVINEPTSLMD 383
Cdd:cd16155 214 ASGELDNTIIVFTSDHGlavGShgL--------MGKQN----------LYEHSMRVPLIISGPGI-PKGKRRDALVYLQD 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 384 IYPTLSYIGGgiLPQDRVIDGRNLMPLLEGRASySDHEFLFhycGVYLHTVRWHQKDcatVWKAHYVTPKfypdgtgacy 463
Cdd:cd16155 275 VFPTLCELAG--IEIPESVEGKSLLPVIRGEKK-AVRDTLY---GAYRDGQRAIRDD---RWKLIIYVPG---------- 335
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622970644 464 gsgicscsGDVTyhdppLLFDISRDPSEALPLNPdnEPLFDSVIKKMEAAIK 515
Cdd:cd16155 336 --------VKRT-----QLFDLKKDPDELNNLAD--EPEYQERLKKLLAELK 372
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
7-391 |
6.80e-32 |
|
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: 123.30 E-value: 6.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRL-TQHLAAASMCTPSRAAFLTGRYPIRSGMVSpyNLNRALTW 85
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTG--NGSADPEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 LGGSGGLPTNETTFAKLLQHRGYRTGLIGkwhlglscasrndhcyhplnhgfhyfygvpfgllsdcqasktpelhrwlri 165
Cdd:cd00016 79 PSRAAGKDEDGPTIPELLKQAGYRTGVIG--------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 166 klwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkeekvaslm 245
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 246 lkeALAFIERVKRE-PFLLFFSFLHVHTPliskekfvGHS---KYGRYGDNVEEMDWMVGKILDALDRECLANNTLVYFT 321
Cdd:cd00016 108 ---LLKAIDETSKEkPFVLFLHFDGPDGP--------GHAygpNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVT 176
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 322 SDNGGHLEPLDGAVQLGGwngiykggkGMGGWEGGIRVPGIFRWPSVLeAGRVINEPTSLMDIYPTLSYI 391
Cdd:cd00016 177 ADHGGIDKGHGGDPKADG---------KADKSHTGMRVPFIAYGPGVK-KGGVKHELISQYDIAPTLADL 236
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-415 |
1.62e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 122.72 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADD-----LGvgdlcCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvspynln 80
Cdd:cd16152 1 KPNVIVFFTDQqrwdtLG-----CYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 81 raltWLGGsGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrndhcyhplnhgfhyfygvpfGLLSDCqasktpelh 160
Cdd:cd16152 69 ----FRNG-IPLPADEKTLAHYFRDAGYETGYVGKWHLA--------------------------GYRVDA--------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 161 rwlriklwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygFTRRwncilmrnheiiqqpmkeek 240
Cdd:cd16152 109 --------------------------------------------------------LTDF-------------------- 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 241 vaslmlkeALAFI-ERVKREPFLLFFSFLHVH---------TPLISKEKFVG--------------HSKYGRYGDNVEEM 296
Cdd:cd16152 113 --------AIDYLdNRQKDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANfwvppdlaalpgdwAEELPDYLGCCERL 184
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 297 DWMVGKILDALDRECLANNTLVYFTSDNGGHLE---------PLDGAvqlggwngiykggkgmggweggIRVPGIFRWPS 367
Cdd:cd16152 185 DENVGRIRDALKELGLYDNTIIVFTSDHGCHFRtrnaeykrsCHESS----------------------IRVPLVIYGPG 242
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622970644 368 vLEAGRVINEPTSLMDIYPTLSYIGGgiLPQDRVIDGRNLMPLLEGRA 415
Cdd:cd16152 243 -FNGGGRVEELVSLIDLPPTLLDAAG--IDVPEEMQGRSLLPLVDGKV 287
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-407 |
3.83e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 114.01 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDLCCYGN----------NSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVS 75
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 76 pynlNRAlTWLGGSGGLPtnetTFAKLLQHRGYRTGLIGKWHLGlscasrndhcyhplnhgfhyfygvpfgllsdcqask 155
Cdd:cd16153 81 ----FEA-AHPALDHGLP----TFPEVLKKAGYQTASFGKSHLE------------------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 156 tpelhrwlriklwistvaialvpflllipKFARWFSVPWKvifvfallaflfftswyssyGFTRRWncilmrnHEIIQQP 235
Cdd:cd16153 116 -----------------------------AFQRYLKNANQ--------------------SYKSFW-------GKIAKGA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 236 mkeekvaslmlkealafierVKREPFLLFFSFLHVHTPLISKEKFVGHSKYgrYGdNVEEMDWMVGKILDALDRECLAN- 314
Cdd:cd16153 140 --------------------DSDKPFFVRLSFLQPHTPVLPPKEFRDRFDY--YA-FCAYGDAQVGRAVEAFKAYSLKQd 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 315 --NTLVYFTSDNGGHLEPlDGAV-QLGGWNgiykggkgmggweGGIRVPGIFRWPSVLE--AGRVINEPTSLMDIYPTLS 389
Cdd:cd16153 197 rdYTIVYVTGDHGWHLGE-QGILaKFTFWP-------------QSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTLL 262
|
410
....*....|....*...
gi 1622970644 390 YIGGGILPQDRVIDGRNL 407
Cdd:cd16153 263 AAAGVDVDAPDYLDGRDL 280
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
6-405 |
6.69e-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: 112.64 E-value: 6.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLGVGDlccyGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVS---PYNLNRA 82
Cdd:cd16147 1 RPNIVLILTDDQDVEL----GSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNnspPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 83 LTWLGgsgglpTNETTFAKLLQHRGYRTGLIGKwhlglscasrndhcYhpLNHgfhyfYGVPFGLlsdcqasktpelhrw 162
Cdd:cd16147 77 FWQNG------LERSTLPVWLQEAGYRTAYAGK--------------Y--LNG-----YGVPGGV--------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 163 lriklwistvaiALVPfllliPKFARWFsvpwkvifvfallaFLFFTSWYSSYGFTrrwncilmrNHEIIQQPMKEEKVA 242
Cdd:cd16147 115 ------------SYVP-----PGWDEWD--------------GLVGNSTYYNYTLS---------NGGNGKHGVSYPGDY 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 243 S--LMLKEALAFIERVKR--EPFLLFFSFLHVHTPLIS----KEKFVGHSKYGRYG---------------------DNV 293
Cdd:cd16147 155 LtdVIANKALDFLRRAAAddKPFFLVVAPPAPHGPFTPapryANLFPNVTAPPRPPpnnpdvsdkphwlrrlpplnpTQI 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 294 EEMDW--------------MVGKILDALDRECLANNTLVYFTSDNGGHL-------------EPlDgavqlggwngiykg 346
Cdd:cd16147 235 AYIDElyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGYHLgqhrlppgkrtpyEE-D-------------- 299
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622970644 347 gkgmggweggIRVPGIFRWPSVlEAGRVINEPTSLMDIYPTLSYIGGGILPQDrvIDGR 405
Cdd:cd16147 300 ----------IRVPLLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-514 |
5.55e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 110.40 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvspynlNRALTWL 86
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG-------HRTLHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 ggsggLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNDHCyhplnhgfhyfygvpfglLSDcqasktpelhrWLRIK 166
Cdd:cd16150 74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC------------------DSD-----------EACVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 167 lwistVAIALV-------PFLLLIPKFARW--FSVPWKvifvfallaflfftsWYSSYGftrrwncilmrnheiiQQPMK 237
Cdd:cd16150 120 -----TAIDWLrnrrpdkPFCLYLPLIFPHppYGVEEP---------------WFSMID----------------REKLP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 238 EEKVASLMLKEALAFIERVKREpfllffsflhvHTPLISKEKFVG-HSKYgrYGdNVEEMDWMVGKILDALDRECLANNT 316
Cdd:cd16150 164 PRRPPGLRAKGKPSMLEGIEKQ-----------GLDRWSEERWRElRATY--LG-MVSRLDHQFGRLLEALKETGLYDDT 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 317 LVYFTSDNG------GHLEPLDGAVQlggwngiykggkgmggwEGGIRVPGIFRwPSVLEAGRVINEPTSLMDIYPTLSY 390
Cdd:cd16150 230 AVFFFSDHGdytgdyGLVEKWPNTFE-----------------DCLTRVPLIIK-PPGGPAGGVSDALVELVDIPPTLLD 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 391 IGGgiLPQDRVIDGRNLMPLLEG------RASYSDheflfhycGVYLHtvrwHQKDCatVWKAHYVTPKFYPDGT----G 460
Cdd:cd16150 292 LAG--IPLSHTHFGRSLLPVLAGeteehrDAVFSE--------GGRLH----GEEQA--MEGGHGPYDLKWPRLLqqeeP 355
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622970644 461 ACYGSGICSCSGDVTY----HDPPLLFDISRDPSEAlpLNPDNEPLFDSVIKKMEAAI 514
Cdd:cd16150 356 PEHTKAVMIRTRRYKYvyrlYEPDELYDLEADPLEL--HNLIGDPAYAEIIAEMKQRL 411
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
7-412 |
7.72e-26 |
|
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: 110.55 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVspynlnraltwl 86
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSW------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLglscasrndhcyhplnHGFHYF-YGV-PFGLLSD------CQASKTPE 158
Cdd:cd16156 69 TNCMALGDNVKTIGQRLSDNGIHTAYIGKWHL----------------DGGDYFgNGIcPQGWDPDywydmrNYLDELTE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 159 LHRWLRiklwistvaialvpflllipkfarwfsvpwkvifvfallaflfftswyssygftRRWNCILMRNHeiiqqpMKE 238
Cdd:cd16156 133 EERRKS------------------------------------------------------RRGLTSLEAEG------IKE 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 239 EKV-ASLMLKEALAFIERVKREPFLLFFSFLHVHTPLISKEKFVghSKYGRYG--------DNVEE-------------- 295
Cdd:cd16156 153 EFTyGHRCTNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYA--SMYKDFEfpkgenayDDLENkplhqrlwagakph 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 296 -------------------MDWMVGKILDALDREclANNTLVYFTSDNGGHLepldGAVQLGGWNGIYKGGKGmggwegg 356
Cdd:cd16156 231 edgdkgtikhplyfgcnsfVDYEIGRVLDAADEI--AEDAWVIYTSDHGDML----GAHKLWAKGPAVYDEIT------- 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622970644 357 iRVPGIFRWPSVLEAGRVINEPTSLMDIYPT-LSYIGggiLPQDRVIDGRNLMPLLE 412
Cdd:cd16156 298 -NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTiLDYAG---IPQPKVLEGESILATIE 350
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-426 |
2.64e-25 |
|
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: 106.52 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 33 PNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvsPYNLNRALTWLggsggLPTNETTFAKLLQHRGYRTGL 112
Cdd:cd16035 27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGV--TDTLGSPMQPL-----LSPDVPTLGHMLRAAGYYTAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 113 IGKWHLglscasrNDHCYHPLNHGfhyfygvpfgllsdcqasktpelhrwlriklwistvaialvpfllliPKFARwfsv 192
Cdd:cd16035 100 KGKWHL-------SGAAGGGYKRD-----------------------------------------------PGIAA---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 193 pwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkeekvaslmlkEALAFIERVKR-----EPFLLFFSF 267
Cdd:cd16035 122 -------------------------------------------------------QAVEWLRERGAknadgKPWFLVVSL 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 268 L--H-VHTPLISKEKFVGHSKYgrYGDNVEEMDWMVGKILDALDRECLANNTLVYFTSDNGghlEpLDGAVQL-GGWNgi 343
Cdd:cd16035 147 VnpHdIMFPPDDEERWRRFRNF--YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG---E-MGGAHGLrGKGF-- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 344 ykggkgmGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILPQDRVID----GRNLMPLLEGRASYSD 419
Cdd:cd16035 219 -------NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAV 291
|
....*...
gi 1622970644 420 HE-FLFHY 426
Cdd:cd16035 292 RDgILFTY 299
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-150 |
5.13e-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: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGVGDLCCYGNNSV--STPNIDRLANEGVRLTqHLAAASMCTPSRAAFLTGRYPIRSGmvspynlnraLT 84
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG----------VL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622970644 85 WLGGSGGLPTNETTFAKLLQHR--GYRTGLIGKWHLGlscasrNDHcYHPLNHG-FHYFYGVPFGLLSD 150
Cdd:cd16154 70 AVPDELLLSEETLLQLLIKDATtaGYSSAVIGKWHLG------GND-NSPNNPGgIPYYAGILGGGVQD 131
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
7-490 |
2.66e-12 |
|
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: 68.34 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 7 PNIVLLMADDLGvGDLCCYGNNS-VSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPirsGMVSPYNLNRaltw 85
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRPGNQvVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT---HLTESWNNYK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 86 lggsgGLPTNETTFAKLLQHRGYRTGLIGKwhlgLSCASrndhcyhplnhGFHyfygvpfgllsdcqaSKTPELHRWLRI 165
Cdd:cd16171 73 -----GLDPNYPTWMDRLEKHGYHTQKYGK----LDYTS-----------GHH---------------SVSNRVEAWTRD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 166 klwistvaialVPFLLlipkfaRWFSVPWKVIFVFALLAFLFFTSWYSSygftrrwncilmrnheiiqqpmkeEKVASLM 245
Cdd:cd16171 118 -----------VPFLL------RQEGRPTVNLVGDRSTVRVMLKDWQNT------------------------DKAVHWI 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 246 LKEALAFiervkREPFLLFFSFLHVHT-PLISKEKFVGHSKYGR--YGDNVEEMDWMVGKILDALDRECLANNTLVYFTS 322
Cdd:cd16171 157 RKEAPNL-----TQPFALYLGLNLPHPyPSPSMGENFGSIRNIRafYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTS 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 323 DNGghleplDGAVQlggwngiYKGGKGMGGWEGGIRVPGIFRWPSVlEAGRVINEPTSLMDIYPTLSYIGGGILPQDrvI 402
Cdd:cd16171 232 DHG------ELAME-------HRQFYKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--L 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 403 DGRNLMPLLEGRASYSDHEFL---------FHYCGVYLHT--VRWHQkdcatvWKahYVTpkfYPDGTGAcygsgicscs 471
Cdd:cd16171 296 SGYSLLPLLSESSIKESPSRVphpdwvlseFHGCNVNASTymLRTNS------WK--YIA---YADGNSV---------- 354
|
490
....*....|....*....
gi 1622970644 472 gdvtyhdPPLLFDISRDPS 490
Cdd:cd16171 355 -------PPQLFDLSKDPD 366
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
245-388 |
1.08e-06 |
|
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: 50.37 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 245 MLKEALAFIERVKREPFLLFFSFLHVHTP----LISKEKFVGHSKYGRYGDN----VEEMDWMVGKILDALDRECLANNT 316
Cdd:cd16015 142 LFDQALEELEELKKKPFFIFLVTMSNHGPydlpEEKKDEPLKVEEDKTELENylnaIHYTDKALGEFIEKLKKSGLYENT 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622970644 317 LVYFTSDnggHLEPLDGAVQLGGWNGIYKGgkgmggweggiRVPGIFRWPSvLEAGRVINEPTSLMDIYPTL 388
Cdd:cd16015 222 IIVIYGD---HLPSLGSDYDETDEDPLDLY-----------RTPLLIYSPG-LKKPKKIDRVGSQIDIAPTL 278
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
6-408 |
6.49e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 48.88 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 6 RPNIVLLMADDLG---VGDlccYGNNSVSTPNIDRLANEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvSPYNLNra 82
Cdd:COG1368 234 KPNVVVILLESFSdffIGA---LGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGG--SPYKRP-- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 83 ltwlggsgglPTNET-TFAKLLQHRGYRTgligkwhlglscasrndHCYHPlnhGFHYFYGvpfgllsdcqasktpelhr 161
Cdd:COG1368 307 ----------GQNNFpSLPSILKKQGYET-----------------SFFHG---GDGSFWN------------------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 162 wlriklwistvaialvpflllipkfarwfsvpwkvifvfallaflfFTSWYSSYGFTRrwncILMRNHeiiqqpMKEEKV 241
Cdd:COG1368 338 ----------------------------------------------RDSFYKNLGFDE----FYDRED------FDDPFD 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 242 ASL------MLKEALAFIERVKrEPFLLFFSFLHVHTPLISKEKFV-----GHSKYGRYGDNVEEMDWMVGKILDALDRE 310
Cdd:COG1368 362 GGWgvsdedLFDKALEELEKLK-KPFFAFLITLSNHGPYTLPEEDKkipdyGKTTLNNYLNAVRYADQALGEFIEKLKKS 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 311 CLANNTLVYFTSDnggHLEPLDGavqlggwngiykgGKGMGGWEGGIRVPGIFrWPSVLEAGRVINEPTSLMDIYPT-LS 389
Cdd:COG1368 441 GWYDNTIFVIYGD---HGPRSPG-------------KTDYENPLERYRVPLLI-YSPGLKKPKVIDTVGSQIDIAPTlLD 503
|
410 420
....*....|....*....|
gi 1622970644 390 YIGggiLPQDRVID-GRNLM 408
Cdd:COG1368 504 LLG---IDYPSYYAfGRDLL 520
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
288-388 |
1.42e-05 |
|
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: 47.98 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 288 RYGDNVEEMDWMVGKILDALDRECLANNTLVYFTSDNGghlEPLDGavqlggwNGIYKGGKGMGGWEGGIRVPGIFRWPS 367
Cdd:COG3083 428 RYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHG---EEFNE-------NGQNYWGHNSNFSRYQLQVPLVIHWPG 497
|
90 100
....*....|....*....|.
gi 1622970644 368 vlEAGRVINEPTSLMDIYPTL 388
Cdd:COG3083 498 --TPPQVISKLTSHLDIVPTL 516
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
5-146 |
7.77e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 45.12 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 5 ARPNIVLLMADDLGVGDLccygnNSVSTPNIDRLANEGVRLTQHLAAA-SMCTPSRAAFLTGRYPIRSGMVS-------- 75
Cdd:COG1524 22 PAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIVGngwydpel 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622970644 76 ---PYNLNRALTWLGGSGGLPTneTTFAKLLQHRGYRTGLIGKWHLGLSCASRNDHCYHPlnHGFHYFYGVPFG 146
Cdd:COG1524 97 grvVNSLSWVEDGFGSNSLLPV--PTIFERARAAGLTTAAVFWPSFEGSGLIDAARPYPY--DGRKPLLGNPAA 166
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
238-340 |
1.22e-04 |
|
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: 44.33 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970644 238 EEKVASLMLKE--ALAFIERVKREPFLLFFSFLHVHTpliskekfVGHsKYG----RYGDNVEEMDWMVGKILDALDREC 311
Cdd:pfam01663 139 EDRVDTAVLQTwlDLPFADVAAERPDLLLVYLEEPDY--------AGH-RYGpdspEVEDALRRVDRAIGDLLEALDERG 209
|
90 100
....*....|....*....|....*....
gi 1622970644 312 LANNTLVYFTSDNGGHLEPLDGAVQLGGW 340
Cdd:pfam01663 210 LFEDTNVIVVSDHGMTPVSDDKVIFLNDY 238
|
|
| |
