|
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: 766.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSaYNLNRAFTW 85
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMAS-SHGMRVILF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 LGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNDHCYHPLNHGFHYFYGVPFGLLSDCQAskTPELHRWLRI 165
Cdd:cd16159 80 TASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 166 KLWISTVALALVPFLLLIPKFARWFSVPWKVIFVFALLAFLFFTSWYSSYGFTRRWNCILMRNHEIIQQPMKEEKVASLM 245
Cdd:cd16159 158 DPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 246 LKEALAFIERYKREPFLLFFSFLHVHTPLISKKKFVGRSKYGRYGDNVEEMDWMVGKILDALDQERLANHTLVYFTSDNG 325
Cdd:cd16159 238 TKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 326 GHLEPLDGAVQLGGWNGIYKGGKGMGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILSQDRVIDGQ 405
Cdd:cd16159 318 GHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 406 NLMPLLEGRASHSDHEFLFHYCGVYLHTVRWHQKDCATVWKAHYVTPKFYPEGTGaCYGSGICSCSGD-VTYHDPPLLFD 484
Cdd:cd16159 398 DLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDsVTHHDPPLLFD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 58743319 485 ISRDPSEALPLNPDNEPlFDSVIKKMEAAIREHRRTLTPVPQQFSV 530
Cdd:cd16159 477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLSF 521
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
6-495 |
1.41e-148 |
|
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: 432.76 E-value: 1.41e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvsAYNLNRAftw 85
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL--PGVVGPP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 lGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrnDH-CYHPLNHGFHYFYGVPFGLLSDCqasktpelHRWLR 164
Cdd:cd16026 76 -GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWP--------FPLYR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 165 IKLWIStvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwNCILMRNHEIIQQPMKEEKVASL 244
Cdd:cd16026 140 NDPPGP---------------------------------------------------LPPLMENEEVIEQPADQSSLTQR 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 245 MLKEALAFIERYKREPFLLFFSFLHVHTPLISKKKFVGRSKYGRYGDNVEEMDWMVGKILDALDQERLANHTLVYFTSDN 324
Cdd:cd16026 169 YTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 325 GGHLE---------PLDGAVQL---GGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIG 392
Cdd:cd16026 249 GPWLEygghggsagPLRGGKGTtweGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALA 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 393 GGILSQDRVIDGQNLMPLLEGRASHSDHEFLFHYCGVYLHTVRWHQkdcatvWKAHYVTPKFYPEGTGAcygsgicscsG 472
Cdd:cd16026 312 GAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPGG----------L 375
|
490 500
....*....|....*....|...
gi 58743319 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 |
5.73e-120 |
|
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: 361.36 E-value: 5.73e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSAynlNRAF-T 84
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGG---TRVFlP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 85 WlgGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNDHCYHPLNHGFHyFYGV--PFGLlsdcqasktpelhrw 162
Cdd:cd16160 78 W--DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGTnlPFTN--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 163 lriklwistvalalvpflllipkfaRWFSVPWKVifvfallaflfftswysSYGFTRRWNCILMRNHEIIQQPMKEEKVA 242
Cdd:cd16160 140 -------------------------SWACDDTGR-----------------HVDFPDRSACFLYYNDTIVEQPIQHEHLT 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 243 SLMLKEALAFIERYKREPFLLFFSFLHVHTPLISKKKFVGRSKYGRYGDNVEEMDWMVGKILDALDQERLANHTLVYFTS 322
Cdd:cd16160 178 ETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 323 DNGGHLEPL----DGAVQLGG----WNgiykggkgmggweGGIRVPGIFRWPSVLeAGRVINEPTSLMDIYPTLSYIGGG 394
Cdd:cd16160 258 DHGPHVEYCleggSTGGLKGGkgnsWE-------------GGIRVPFIAYWPGTI-KPRVSHEVVSTMDIFPTFVDLAGG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 395 ILSQDRVIDGQNLMPLLEGRASHSDHEFLFHYCGVyLHTVRWHQkdcatvWKAHYVTPKFYPEGTGACYGSGICS----- 469
Cdd:cd16160 324 TLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTQPLPSQESLDPNCDGGGPlsdyi 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 58743319 470 ----CSGD-VTYHDPPLLFDISRDPSEALPLNP-DNEPLFDSVIK 508
Cdd:cd16160 397 vcydCEDEcVTKHNPPLIFDVEKDPGEQYPLQPsVYEHMLEAVEK 441
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
7-551 |
1.32e-100 |
|
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: 312.84 E-value: 1.32e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSAynlnraFTWL 86
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPG------VFYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLScasrNDHCYHPLNHGFHYFYGVPFgllSDCQASKTPELHRWLRIK 166
Cdd:cd16158 76 GSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPY---SHDQGPCQNLTCFPPNIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 LWiSTVALALVPflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwnCILMRNHEIIQQPMKEEKVASLML 246
Cdd:cd16158 149 CF-GGCDQGEVP--------------------------------------------CPLFYNESIVQQPVDLLTLEERYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 247 KEALAFIERYKRE--PFLLFFSFLHVHTPLISKKKFVGRSKYGRYGDNVEEMDWMVGKILDALDQERLANHTLVYFTSDN 324
Cdd:cd16158 184 KFAKDFIADNAKEgkPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDN 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 325 G------------GHLEPLDGAVQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVInEPTSLMDIYPTLSYIG 392
Cdd:cd16158 264 GpstmrksrggnaGLLKCGKGTTYEGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 393 GGILSqDRVIDGQNLMPLLEGRASHSDHEFLFHYC------GVYlhTVRWHQkdcatvWKAHYVTPKFYPEGTGAcygSG 466
Cdd:cd16158 326 GAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTspdpdkGVF--AVRWGK------YKAHFYTQGAAHSGTTP---DK 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 467 ICSCSGDVTYHDPPLLFDISRDPSEAlpLNPDNEPLFDSVIKKMEAAIREHRRTLTPVPQQFSVFNtiwKPWLQPCC--G 544
Cdd:cd16158 394 DCHPSAELTSHDPPLLFDLSQDPSEN--YNLLGLPEYNQVLKQIQQVKERFEASMKFGESEINKGE---DPALEPCCkpG 468
|
....*..
gi 58743319 545 TFPFCGC 551
Cdd:cd16158 469 CTPKPSC 475
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
6-533 |
1.27e-93 |
|
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: 294.37 E-value: 1.27e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSAYNLNR-AFT 84
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARnAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 85 WLGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrNDHCYHPLNHGFHYFYGVPfgllsDCQasktpelhrwlr 164
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLG------HRPQYHPLKHGFDEWFGAP-----NCH------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 165 iklwistvalalvpflllipkFARWFSVPWKVIFVFallaflfftswyssygftRRWNCILMRNHEI-IQQPMKEEKVAS 243
Cdd:cd16157 138 ---------------------FGPYDNKAYPNIPVY------------------RDWEMIGRYYEEFkIDKKTGESNLTQ 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 244 LMLKEALAFIER--YKREPFLLFFSFLHVHTPLISKKKFVGRSKYGRYGDNVEEMDWMVGKILDALDQERLANHTLVYFT 321
Cdd:cd16157 179 IYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFS 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 322 SDNGGhlePLDGAVQLGGWNgIYKGGKGMGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILSQDRV 401
Cdd:cd16157 259 SDNGA---ALISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 402 IDGQNLMPLLegRASHSDHEFLFHYCGVYLHTVRWHQkdcatvWKAHYVTpkfyPEGTGACYGSGICSCSGD----VTYH 477
Cdd:cd16157 335 IDGIDLLPVL--LNGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWT----WSNSWEEFRKGINFCPGQnvpgVTTH 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58743319 478 ------DPPLLFDISRDPSEALPLNPdNEPLFDSVIKKMEAAIREHRRTLTPVPQQFSVFNT 533
Cdd:cd16157 403 nqtdhtKLPLLFHLGRDPGEKYPISF-KSAEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDL 463
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-492 |
6.80e-91 |
|
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: 285.59 E-value: 6.80e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvsaynlnraFTWL 86
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGI---------TDVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 GGSGG---------------LPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrNDHCYHPLNHGFHYFYGVpfgllsdc 151
Cdd:cd16144 72 PGRRGppdntklipppsttrLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIGG-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 152 qasktpelHRWlriklwistvalalvpfllliPKFARWFSVPWKVIFVFallaflfftswyssygftrrwncilmrnhei 231
Cdd:cd16144 138 --------TGN---------------------GGPPSYYFPPGKPNPDL------------------------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 232 iQQPMKEEKVASLMLKEALAFIERYKREPFLLFFSFLHVHTPLISKK----KFVGRSKYGRYGDN-------VEEMDWMV 300
Cdd:cd16144 158 -EDGPEGEYLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPelieKYEKKKKGLRKGQKnpvyaamIESLDESV 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 301 GKILDALDQERLANHTLVYFTSDNGGHLEPLDGAVQL------------GGwngiykggkgmggweggIRVPGIFRWPSV 368
Cdd:cd16144 237 GRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNaplrggkgslyeGG-----------------IRVPLIVRWPGV 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 369 LEAGRVINEPTSLMDIYPTLSYIGGGILSQDRVIDGQNLMPLLEGRASHSDHEFLFHYCGVYLHTVrwhQKDCATV---- 444
Cdd:cd16144 300 IKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWHFPHYHGQG---GRPASAIrkgd 376
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 58743319 445 WKAHYvtpkfypegtgacygsgicscsgdvTYHDPPL-LFDISRDPSEA 492
Cdd:cd16144 377 WKLIE-------------------------FYEDGRVeLYNLKNDIGET 400
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
6-526 |
1.22e-90 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 284.08 E-value: 1.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSAYNlnraftw 85
Cdd:COG3119 23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 lGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLglscasrndhcyhplnhgfhyfygvpfgllsdcqasktpelhrwlri 165
Cdd:COG3119 96 -GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL----------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 166 klwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswYSSYGFTRRwncilmrnheiiqqpmkeekvaslm 245
Cdd:COG3119 128 ----------------------------------------------YLTDLLTDK------------------------- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 246 lkeALAFIERYKR--EPFLLFFSFLHVHTPLISKKKFVG-----------------------RSKYGRYGDNVEEMDWMV 300
Cdd:COG3119 137 ---AIDFLERQADkdKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnlaprdlteeelRRARAAYAAMIEEVDDQV 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 301 GKILDALDQERLANHTLVYFTSDNGGHLE----------PLDGAvqlggwngiykggkgmggweggIRVPGIFRWPSVLE 370
Cdd:COG3119 214 GRLLDALEELGLADNTIVVFTSDNGPSLGehglrggkgtLYEGG----------------------IRVPLIVRWPGKIK 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 371 AGRVINEPTSLMDIYPTLSYIGGgiLSQDRVIDGQNLMPLLEGRASHSDHEFLFHYCGVY-LHTVRWHQkdcatvWKAHY 449
Cdd:COG3119 272 AGSVSDALVSLIDLLPTLLDLAG--VPIPEDLDGRSLLPLLTGEKAEWRDYLYWEYPRGGgNRAIRTGR------WKLIR 343
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58743319 450 vtpkfYPEGTgacygsgicscsgdvtyhDPPLLFDISRDPSEALPLNpDNEPlfdSVIKKMEAAIREHRRTLTPVPQ 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 |
9.13e-89 |
|
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: 278.97 E-value: 9.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGN-NSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSAYNLNraft 84
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 85 wlgGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCAsrndhcYHPLNHGFHYFYGVPFgllsDCQASktpelhrwlr 164
Cdd:cd16161 77 ---SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA------YLPNSRGFDYYFGIPF----SHDSS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 165 iklwistvalalvpfllLIPKFArwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkeekvasl 244
Cdd:cd16161 134 -----------------LADRYA--------------------------------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 245 mlKEALAFIERY--KREPFLLFFSFLHVHTPL-ISKKKFVGRSKYGRYGDNVEEMDWMVGKILDALDQERLANHTLVYFT 321
Cdd:cd16161 140 --QFATDFIQRAsaKDRPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFT 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 322 SDNGGHLEPLDGAVQLGGWNGIYKGGKGMGGWEG---GIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILSQ 398
Cdd:cd16161 218 SDNGPWEVKCELAVGPGTGDWQGNLGGSVAKASTwegGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPP 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 399 DRVIDGQNLMPLLEGRAShSDHEFLFHYCGVY-----LHTVRWHQkdcatvWKAHYVTpkfypEGTGACYGSGicscsGD 473
Cdd:cd16161 298 GRIYDGKDLSPVLFGGSK-TGHRCLFHPNSGAagagaLSAVRCGD------YKAHYAT-----GGALACCGST-----GP 360
|
490 500
....*....|....*....|..
gi 58743319 474 VTYHDPPLLFDISRDPSEALPL 495
Cdd:cd16161 361 KLYHDPPLLFDLEVDPAESFPL 382
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-491 |
8.67e-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: 275.95 E-value: 8.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYG---NNSVSTPNIDRLASEGVRLTQHLAAASmCTPSRAAFLTGRYPIRSGMVSAynlnraf 83
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 84 TWLGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrnDHCYH-PLNHGFHYFYGVPFGLLSDcqasktpelhrw 162
Cdd:cd16142 73 GLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG-------DEDGRlPTDHGFDEFYGNLYHTIDE------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 163 lriklwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnhEIIQQpmkeekva 242
Cdd:cd16142 134 -------------------------------------------------------------------EIVDK-------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 243 slmlkeALAFIERYKR--EPFLLFFSFLHVHTPLISKKKFVGRSK-YGRYGDNVEEMDWMVGKILDALDQERLANHTLVY 319
Cdd:cd16142 139 ------AIDFIKRNAKadKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 320 FTSDNGGHLE--------PLDGA---VQLGGWngiykggkgmggweggiRVPGIFRWPSVLEAGRVINEPTSLMDIYPTL 388
Cdd:cd16142 213 FTTDNGPEQDvwpdggytPFRGEkgtTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 389 SYIGGG------ILSQDRVIDGQNLMPLLEGRASHSDHEFLFHYCGVYLHTVRWHQkdcatvWKAHYVTPKFYPEGTGAC 462
Cdd:cd16142 276 AALAGApdpkdkLLGKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFKAQEDTGGPTGEP 349
|
490 500
....*....|....*....|....*....
gi 58743319 463 YGSGICscsgdvtyhdpPLLFDISRDPSE 491
Cdd:cd16142 350 FYVLTF-----------PLIFNLRRDPKE 367
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-491 |
1.10e-85 |
|
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: 271.38 E-value: 1.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNS-VSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvsaynlNRAFTW 85
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSR-------LKGGVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 LGGSGGL-PTNETTFAKLLQHRGYRTGLIGKWHLGL----------SCASRNDHCYH------PLNHGFHYFYGVPfgll 148
Cdd:cd16143 74 GGFSPPLiEPDRVTLAKMLKQAGYRTAMVGKWHLGLdwkkkdgkkaATGTGKDVDYSkpikggPLDHGFDYYFGIP---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 149 sdcqASKtpelhrwlriklwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrn 228
Cdd:cd16143 150 ----ASE------------------------------------------------------------------------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 229 heiiqqpmkeekVASLMLKEALAFIERYKR--EPFLLFFSFLHVHTPLISKKKFVGRSKYGRYGDNVEEMDWMVGKILDA 306
Cdd:cd16143 153 ------------VLPTLTDKAVEFIDQHAKkdKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDA 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 307 LDQERLANHTLVYFTSDNGGHLEPLDGAVQL------------------GGwngiykggkgmggweggIRVPGIFRWPSV 368
Cdd:cd16143 221 LKELGLAENTLVIFTSDNGPSPYADYKELEKfghdpsgplrgmkadiyeGG-----------------HRVPFIVRWPGK 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 369 LEAGRVINEPTSLMDIYPTLSYIGGGILSQDRVIDGQNLMPLLEGRASHSDHEFLFHYCGVYLHTVRwhQKDcatvWKah 448
Cdd:cd16143 284 IPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIR--KGD----WK-- 355
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 58743319 449 YVTpkfypegtgaCYGSGICSCSGDVTYHDPP--LLFDISRDPSE 491
Cdd:cd16143 356 LID----------GTGSGGFSYPRGKEKLGLPpgQLYNLSTDPGE 390
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-491 |
7.40e-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: 238.26 E-value: 7.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvsaynlnRAFTWL 86
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV-------RGNSEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLscasrNDHCYHPLNHGFHYFYGvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16145 74 GGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGG-----PGTPGHPTKQGFDYFYG------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 lWISTValalvpflllipkFARWFSVPwkvifvfallaFLfftsWYSSYGFTRRWNCILMRNHEIIQQPMKEEKVASLML 246
Cdd:cd16145 125 -YLDQV-------------HAHNYYPE-----------YL----WRNGEKVPLPNNVIPPLDEGNNAGGGGGTYSHDLFT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 247 KEALAFIERYKREPFLLFFSFLHVHTPLI------SKKKFVGRSKYG---------RYGDNVEEMDWMVGKILDALDQER 311
Cdd:cd16145 176 DEALDFIRENKDKPFFLYLAYTLPHAPLQvpddgpYKYKPKDPGIYAylpwpqpekAYAAMVTRLDRDVGRILALLKELG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 312 LANHTLVYFTSDNGGHLE--------------PLDG---AVQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRV 374
Cdd:cd16145 256 IDENTLVVFTSDNGPHSEggsehdpdffdsngPLRGykrSLYEGG-----------------IRVPFIARWPGKIPAGSV 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 375 INEPTSLMDIYPTLSYIGGGILSQDrvIDGQNLMPLLEGRASHSDHEFL---FHYCGvYLHTVRWHQkdcatvWKAHYVT 451
Cdd:cd16145 319 SDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLyweFYEGG-GAQAVRMGG------WKAVRHG 389
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 58743319 452 PKfypegtgacygsgicscsgdvtyHDPPLLFDISRDPSE 491
Cdd:cd16145 390 KK-----------------------DGPFELYDLSTDPGE 406
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
7-491 |
3.44e-70 |
|
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: 231.28 E-value: 3.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQ-HlaAASMCTPSRAAFLTGRYPIRSGMVSaynlnrafTW 85
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTGVWH--------TI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 LGGSgGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrNDHCYHPLNHGFHYFYGVPFGLLSDcqasktpelhrwlri 165
Cdd:cd16146 71 LGRE-RMRLDETTLAEVFKDAGYRTGIFGKWHLG------DNYPYRPQDRGFDEVLGHGGGGIGQ--------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 166 klwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswYSSYGFTRRWNCILMRNHEIIQQpmkEEKVASLM 245
Cdd:cd16146 129 ----------------------------------------------YPDYWGNDYFDDTYYHNGKFVKT---EGYCTDVF 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 246 LKEALAFIERYKREPFLLFFSFLHVHTPLISKKKFVGrsKYGRYGDN---------VEEMDWMVGKILDALDQERLANHT 316
Cdd:cd16146 160 FDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYLD--PYKDMGLDdklaafygmIENIDDNVGRLLAKLKELGLEENT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 317 LVYFTSDNGGHLEPLD----------GAVQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVINEPTSLMDIYP 386
Cdd:cd16146 238 IVIFMSDNGPAGGVPKrfnagmrgkkGSVYEGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 387 TLSYIGGGILSQDRVIDGQNLMPLLEGRASHSDHEFLFhycgvyLHTVRW----HQKDCATVWKAHY--VTPKfypegtg 460
Cdd:cd16146 301 TLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLF------THSGRWppppKKKRNAAVRTGRWrlVSPK------- 367
|
490 500 510
....*....|....*....|....*....|.
gi 58743319 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 |
5.84e-70 |
|
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: 224.62 E-value: 5.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVsaynlnrafTWL 86
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVR---------GNV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHlglscasrndhcyhplnhgfhyfygvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16022 72 GNGGGLPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 lwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkeekvaslml 246
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 247 KEALAFIERYKRE-PFLLFFSFLHVHTPLIskkkfvgrskygrYGDNVEEMDWMVGKILDALDQERLANHTLVYFTSDNG 325
Cdd:cd16022 103 DEAIDFIERRDKDkPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHG 169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 326 GHLEplDGAVQLGGWNgiykggkgmgGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPT-LSYIGGGIlsqDRVIDG 404
Cdd:cd16022 170 DMLG--DHGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTlLDLAGIEP---PEGLDG 234
|
..
gi 58743319 405 QN 406
Cdd:cd16022 235 RS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-455 |
4.25e-63 |
|
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: 211.69 E-value: 4.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTqHLAAASMCTPSRAAFLTGRYPIRSGMVSAYnlnraftwl 86
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVVFGY--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 ggsggLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNdhcyHPLNHGFHYFYgvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16151 71 -----LDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYC------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 LWISTValalvpflllipkfarwfsvpwkvifvfallaflffTSWYSSYGFTRRWNCILMRNHEIIQQ---PmkeekvaS 243
Cdd:cd16151 117 LWQLTE------------------------------------TGEKYSRPATPTFNIRNGKLLETTEGdygP-------D 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 244 LMLKEALAFIERYKREPFLLFFSFLHVHTPL------ISKKKFVGRSK--YGRYGDNVEEMDWMVGKILDALDQERLANH 315
Cdd:cd16151 154 LFADFLIDFIERNKDQPFFAYYPMVLVHDPFvptpdsPDWDPDDKRKKddPEYFPDMVAYMDKLVGKLVDKLEELGLREN 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 316 TLVYFTSDNGGHLEP---LDGAVQLGGwngiykggkGMGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIG 392
Cdd:cd16151 234 TIIIFTGDNGTHRPItsrTNGREVRGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELA 304
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58743319 393 GGILSQDRVIDGQNLMPLLEGRASHSDHEFLFHycgvYLHTVRWHQKDCA---TVWKaHYVTPKFY 455
Cdd:cd16151 305 GAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYW----YYRNPHKKFGSRFvrtKRYK-LYADGRFF 365
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
418-551 |
1.02e-61 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 199.08 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 418 SDHEFLFHYCGVYLHTVRWHQkdcatvWKAHYVTPKFYPEGTGACYGSGICscsgdVTYHDPPLLFDISRDPSEALPLNP 497
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP-----VTHHDPPLLFDLERDPSEKYPLSP 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 58743319 498 DNePLFDSVIKKMEAAIREHRRTLTPVPQQFSVFNTIWKPWLQPCCGTFPFCGC 551
Cdd:pfam14707 70 DS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
7-426 |
1.66e-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: 200.08 E-value: 1.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAAsMCTPSRAAFLTGRYPIRSGMVSAYNLNraftwl 86
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscASRNDHCyhPLNHGFHYFYGvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16029 74 GEPYGLPLNETLLPQYLKELGYATHLVGKWHLG---FYTWEYT--PTNRGFDSFYG------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 lwistvalalvpflllipkfarwfsvpwkvifvfallaflFFTS----WYSSYGFTRRWNCILMRNHEIIQQPMKEEKVA 242
Cdd:cd16029 125 ----------------------------------------YYGGaedyYTHTSGGANDYGNDDLRDNEEPAWDYNGTYST 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 243 SLMLKEALAFIERY-KREPFLLFFSFLHVHTPLISKKKFVGRSKYGRYGDN----------VEEMDWMVGKILDALDQER 311
Cdd:cd16029 165 DLFTDRAVDIIENHdPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKdedrrtyaamVSALDESVGNVVDALKAKG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 312 LANHTLVYFTSDNGGHLE--------PLDGA---VQLGGwngiykggkgmggweggIRVPGiFRWPSVLE--AGRVINEP 378
Cdd:cd16029 245 MLDNTLIVFTSDNGGPTGggdggsnyPLRGGkntLWEGG-----------------VRVPA-FVWSPLLPpkRGTVSDGL 306
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 58743319 379 TSLMDIYPTLSYIGGGILSQDRVIDGQNLMPLLEGRASHSDHEFLFHY 426
Cdd:cd16029 307 MHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNI 354
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
7-425 |
1.35e-54 |
|
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: 188.87 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNsVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvsAYNLNRAFTwl 86
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNV-VKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA--HGLRSRGFP-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 ggsggLPTNETTFAKLLQHRGYRTGLIGKWHlglscasrndhcyhplnHGFHYFYGVPFGLLSDCQASKTPELHrwlrik 166
Cdd:cd16027 76 -----LPDGVKTLPELLREAGYYTGLIGKTH-----------------YNPDAVFPFDDEMRGPDDGGRNAWDY------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 lwistvalalvpflllIPKFARWFSV-----PWkvifvfallaFLFFTSWYSSYGFTRrwncilmrnHEIIQQPMKEEKV 241
Cdd:cd16027 128 ----------------ASNAADFLNRakkgqPF----------FLWFGFHDPHRPYPP---------GDGEEPGYDPEKV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 242 aslmlkealafieryKREPFLlffsflhVHTPLIskkkfvgRSKYGRYGDNVEEMDWMVGKILDALDQERLANHTLVYFT 321
Cdd:cd16027 173 ---------------KVPPYL-------PDTPEV-------REDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFT 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 322 SDNGGhlePLDGA---VQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVINEPTSLMDIYPT-LSYIGGGILS 397
Cdd:cd16027 224 SDHGM---PFPRAkgtLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTlLDLAGIEPPE 283
|
410 420
....*....|....*....|....*....
gi 58743319 398 QdrvIDGQNLMPLLEGR-ASHSDHEFLFH 425
Cdd:cd16027 284 Y---LQGRSFLPLLKGEkDPGRDYVFAER 309
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
7-388 |
5.33e-52 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 179.54 E-value: 5.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSAYNlnraftwl 86
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 ggsGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLScaSRNDhcyhPLNHGFHYFYGvpFGLLSDcqasktpelhrwlrik 166
Cdd:pfam00884 73 ---VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWY--NNQS----PCNLGFDKFFG--RNTGSD---------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 lwistvalalvpflllipkfarwfsvpwkvifvfallaflffTSWYSSYgftRRWNCILMRNHEIIqqpmkeekvaslML 246
Cdd:pfam00884 126 ------------------------------------------LYADPPD---VPYNCSGGGVSDEA------------LL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 247 KEALAFIERYKRePFLLFFSFLHVHTPLISKKKFVG------------RSKYGRYGDNVEEMDWMVGKILDALDQERLAN 314
Cdd:pfam00884 149 DEALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEkyatfkpsscseEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58743319 315 HTLVYFTSDNGGHLEPLDGAVQLGGWNgiykggkgmGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTL 388
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTI 292
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-489 |
1.32e-51 |
|
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: 181.61 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVsaYNLNRaftw 85
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF--GNDVP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 lggsggLPTNETTFAKLLQHRGYRTGLIGKWHLG----LSCASRNDHCYHPLNHGFHYFYGvpfgllSDCQasktpelHR 161
Cdd:cd16034 75 ------LPPDAPTIADVLKDAGYRTGYIGKWHLDgperNDGRADDYTPPPERRHGFDYWKG------YECN-------HD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 162 wlriklwistvalalvpflllipkfarwfsvpwkvifvfallaflFFTSWYssygFTRRWNCILMRNHEIIQQpmkeekv 241
Cdd:cd16034 136 ---------------------------------------------HNNPHY----YDDDGKRIYIKGYSPDAE------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 242 aslmLKEALAFIERYKRE--PFLLFFSFLHVHTP------------------------LISKKKFVGRSKYGRYGDNVEE 295
Cdd:cd16034 160 ----TDLAIEYLENQADKdkPFALVLSWNPPHDPyttapeeyldmydpkklllrpnvpEDKKEEAGLREDLRGYYAMITA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 296 MDWMVGKILDALDQERLANHTLVYFTSDNG------GHLE---PLDGAvqlggwngiykggkgmggweggIRVPGIFRWP 366
Cdd:cd16034 236 LDDNIGRLLDALKELGLLENTIVVFTSDHGdmlgshGLMNkqvPYEES----------------------IRVPFIIRYP 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 367 SVLEAGRVINEPTSLMDIYPTLSYIGGgiLSQDRVIDGQNLMPLLEGRASHSDHEFLFHYcgvylhTVRWHQKDCATVWK 446
Cdd:cd16034 294 GKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLLQC------FVPFGGGSARDGGE 365
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 58743319 447 AHYVTPKFYpegTGACYGSGicscsgdvtyhdPPLLFDISRDP 489
Cdd:cd16034 366 WRGVRTDRY---TYVRDKNG------------PWLLFDNEKDP 393
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
6-512 |
7.86e-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: 175.02 E-value: 7.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSaynlnraftw 85
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTD---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 lGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNDhcyhplnhGFHYFYGVPfGllsdcQAS-KTPELH---R 161
Cdd:cd16031 72 -NNGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFP-G-----QGSyYDPEFIengK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 162 WLRIKLWIS--TVALAL---------VPFLLLIPKFA--RWFSVPWKVIFVFALLAF----LFFTSWYSsygftrrwnci 224
Cdd:cd16031 137 RVGQKGYVTdiITDKALdflkerdkdKPFCLSLSFKAphRPFTPAPRHRGLYEDVTIpepeTFDDDDYA----------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 225 lmrnheiiQQPMkeekvaslMLKEALAFIERYKREPFllffsflhvHTPLiskkkfvgrsKYGRYGDN----VEEMDWMV 300
Cdd:cd16031 206 --------GRPE--------WAREQRNRIRGVLDGRF---------DTPE----------KYQRYMKDylrtVTGVDDNV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 301 GKILDALDQERLANHTLVYFTSDNGGHLepldGAVQLGG-WNgiykggkgmgGWEGGIRVPGIFRWPSVLEAGRVINEPT 379
Cdd:cd16031 251 GRILDYLEEQGLADNTIIIYTSDNGFFL----GEHGLFDkRL----------MYEESIRVPLIIRDPRLIKAGTVVDALV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 380 SLMDIYPT-LSYIGGGILSQdrvIDGQNLMPLLEGRASHS-DHEFLFHYcgvylhtvrWHQKDCATVWKAH-YVTPKF-Y 455
Cdd:cd16031 317 LNIDFAPTiLDLAGVPIPED---MQGRSLLPLLEGEKPVDwRKEFYYEY---------YEEPNFHNVPTHEgVRTERYkY 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58743319 456 pegtgACYgsgicscsgdvtYHDPPL--LFDISRDPSEA--LPLNPDNEPLFDSVIKKMEA 512
Cdd:cd16031 385 -----IYY------------YGVWDEeeLYDLKKDPLELnnLANDPEYAEVLKELRKRLEE 428
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
6-492 |
1.12e-46 |
|
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: 168.39 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNnSVSTPNIDRLASEGVRLTQ-HlaAASMCTPSRAAFLTGRYPIRSGMVSAYNLNRAFT 84
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGG-EIPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGMGTMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 85 wlGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrndhcyhplnhgfhyfygvpfgllsdcqasktPElhrwlr 164
Cdd:cd16025 79 --GYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG-------------------------------------PD------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 165 iklwistvalalvpflllipkfarwfsvpwkvifvfallaflfftSWYSSYGFTRRwncilmrnheiiqqpmkeekvasl 244
Cdd:cd16025 114 ---------------------------------------------DYYSTDDLTDK------------------------ 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 245 mlkeALAFIERYKRE--PFLLFFSFLHVHTPLISKKKFVgrSKY-GRYGDN----------------------------- 292
Cdd:cd16025 125 ----AIEYIDEQKAPdkPFFLYLAFGAPHAPLQAPKEWI--DKYkGKYDAGwdalreerlerqkelglipadtkltprpp 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 293 --------------------------VEEMDWMVGKILDALDQERLANHTLVYFTSDNGGHLE---------PLD---GA 334
Cdd:cd16025 199 gvpawdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEpgwanasntPFRlykQA 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 335 VQLGGwngiykggkgmggweggIRVPGIFRWPS-VLEAGRVINEPTSLMDIYPTL----------SYIGGGILSqdrvID 403
Cdd:cd16025 279 SHEGG-----------------IRTPLIVSWPKgIKAKGGIRHQFAHVIDIAPTIlelagveypkTVNGVPQLP----LD 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 404 GQNLMPLLEGRASHSDHEF----LFHYCGVYlhtvrwhQKDcatvWKAhyvtpkfypegtgacygsgicscsgdVTYHDP 479
Cdd:cd16025 338 GVSLLPTLDGAAAPSRRRTqyfeLFGNRAIR-------KGG----WKA--------------------------VALHPP 380
|
570
....*....|....*....
gi 58743319 480 PL------LFDISRDPSEA 492
Cdd:cd16025 381 PGwgdqweLYDLAKDPSET 399
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-516 |
1.13e-44 |
|
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: 163.16 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSAYNLNRAFtwl 86
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 ggSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCAsrndhcyhPLNHGFHYFYGVpfgllsdcQASKTpelhRWL--R 164
Cdd:cd16033 78 --SRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEET--------PLDYGFDEYLPV--------ETTIE----YFLadR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 165 IKLWISTVALALVPFLLLIPkfarwfsvpwkviFVFALLAFLFFTSWYSSYgftrrwncilmrnheiiqQPMKEEKVASl 244
Cdd:cd16033 136 AIEMLEELAADDKPFFLRVN-------------FWGPHDPYIPPEPYLDMY------------------DPEDIPLPES- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 245 mLKEALA---FIERYKREPFLLFFSFLHVHTPLISkkkfvgrskygRYGDNVEEMDWMVGKILDALDQERLANHTLVYFT 321
Cdd:cd16033 184 -FADDFEdkpYIYRRERKRWGVDTEDEEDWKEIIA-----------HYWGYITLIDDAIGRILDALEELGLADDTLVIFT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 322 SDNGGHLepldGAvqLGGWNGIYKGGKGMGgweggiRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGgiLSQDRV 401
Cdd:cd16033 252 SDHGDAL----GA--HRLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAG--VDVPPK 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 402 IDGQNLMPLLEGRASHSDHEFLF---HYCGVYLHTVRWHQKDcatvWKahYVtpkfypegtgaCYGSGICScsgdvtyhd 478
Cdd:cd16033 318 VDGRSLLPLLRGEQPEDWRDEVVteyNGHEFYLPQRMVRTDR----YK--YV-----------FNGFDIDE--------- 371
|
490 500 510
....*....|....*....|....*....|....*...
gi 58743319 479 pplLFDISRDPSEAlpLNPDNEPLFDSVIKKMEAAIRE 516
Cdd:cd16033 372 ---LYDLESDPYEL--NNLIDDPEYEEILREMRTRLYE 404
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-489 |
9.47e-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: 150.00 E-value: 9.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvsAYNlNraftwl 86
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETG---VWD-N------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 ggSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscaSRNDhcyhplNHGFHYfygvpfgllsdcqasktpelhrwlrik 166
Cdd:cd16037 71 --ADPYDGDVPSWGHALRAAGYETVLIGKLHFR----GEDQ------RHGFRY--------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 lwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkEEKVAslml 246
Cdd:cd16037 112 -----------------------------------------------------------------------DRDVT---- 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 247 KEALAFIERYKR--EPFLLFFSFLHVHTPLISKKKFVgrSKYGR-----YGDNVEEMDWMVGKILDALDQERLANHTLVY 319
Cdd:cd16037 117 EAAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFY--DLYVRraraaYYGLVEFLDENIGRVLDALEELGLLDNTLII 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 320 FTSDNGGHLepldGAVQLGGWNgiykggkgmGGWEGGIRVPGIFRWPSVlEAGRVINEPTSLMDIYPTLSYIGGgiLSQD 399
Cdd:cd16037 195 YTSDHGDML----GERGLWGKS---------TMYEESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAG--APPP 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 400 RVIDGQNLMPLLEGRASHSD---HEFLFHYCGVYLHTVRWHQkdcatvWKAHYvtpkfypegtgacygsgicscsgdvtY 476
Cdd:cd16037 259 PDLDGRSLLPLAEGPDDPDRvvfSEYHAHGSPSGAFMLRKGR------WKYIY--------------------------Y 306
|
490
....*....|....
gi 58743319 477 H-DPPLLFDISRDP 489
Cdd:cd16037 307 VgYPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-409 |
7.98e-36 |
|
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: 134.67 E-value: 7.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYP--------IRSGMVSAYn 78
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPsqhgihdwIVEGSHGKT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 79 lNRAFTWLGGsgglptnETTFAKLLQHRGYRTGLIGKWHLGlscasrndhcyhplnhgfhyfygvpfgllsdcqasktpe 158
Cdd:cd16149 80 -KKPEGYLEG-------QTTLPEVLQDAGYRCGLSGKWHLG--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 159 lhrwlriklwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmke 238
Cdd:cd16149 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 239 ekvaslmlKEALAFIER--YKREPFLLFFSFLHVHTPliskkkfvgrskYGrYGDNVEEMDWMVGKILDALDQERLANHT 316
Cdd:cd16149 113 --------DDAADFLRRraEAEKPFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENT 171
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 317 LVYFTSDNG---GH---LEPLDGAVQLGGWNgiykggkgmggweGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSY 390
Cdd:cd16149 172 LVIFTSDNGfnmGHhgiWGKGNGTFPLNMYD-------------NSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLE 238
|
410
....*....|....*....
gi 58743319 391 IGGGILSQDRVIDGQNLMP 409
Cdd:cd16149 239 LAGVDPPADPRLPGRSFAD 257
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
7-489 |
8.04e-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: 136.55 E-value: 8.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvsAYNlNRAftwl 86
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIG---AYD-NAA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 ggsgGLPTNETTFAKLLQHRGYRTGLIGKWH------LglscasrndhcyhplnHGFHY-----FYGVpfgllsdcqask 155
Cdd:cd16032 73 ----EFPADIPTFAHYLRAAGYRTALSGKMHfvgpdqL----------------HGFDYdeevaFKAV------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 156 tpelhRWLRiklwistvALAlvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmRNHEiiqqp 235
Cdd:cd16032 121 -----QKLY--------DLA---------------------------------------------------RGED----- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 236 mkeekvaslmlkealafierykREPFLLFFSFLHVHTPLISKKKF----VGRSKYGRYGdNVEEMDWMVGKILDALDQER 311
Cdd:cd16032 132 ----------------------GRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTG 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 312 LANHTLVYFTSDNGGHL---------EPLDGAVqlggwngiykggkgmggweggiRVPGIFRWPSVLEAGRViNEPTSLM 382
Cdd:cd16032 189 LADDTIVIFTSDHGDMLgerglwykmSFFEGSA----------------------RVPLIISAPGRFAPRRV-AEPVSLV 245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 383 DIYPTL-SYIGGGILSQDRVIDGQNLMPLLEGRASHSDHEFLFHYCGVYLHTvrwhqkDCATVWKAHYvtpKFYpegtga 461
Cdd:cd16032 246 DLLPTLvDLAGGGTAPHVPPLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVA------PCVMIRRGRW---KFI------ 310
|
490 500
....*....|....*....|....*...
gi 58743319 462 cygsgicscsgdVTYHDPPLLFDISRDP 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 |
4.08e-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: 136.93 E-value: 4.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVgDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvsaYNLNRAFTW 85
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV---YDNNSYFRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 LGGsgglptNETTFAKLLQHRGYRTGLIGK-WHLGLSC-----ASRNDHCYHPLNHGFHYFYGVPF-------GLLSDCQ 152
Cdd:cd16030 78 VAP------DAVTLPQYFKENGYTTAGVGKiFHPGIPDgdddpASWDEPPNPPGPEKYPPGKLCPGkkggkggGGGPAWE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 153 ASKTPEL----HRWLR--IKlWISTVALALVPFlllipkfarwfsvpwkvifvfallaFLfftswysSYGFTR---RWNC 223
Cdd:cd16030 152 AADVPDEaypdGKVADeaIE-QLRKLKDSDKPF-------------------------FL-------AVGFYKphlPFVA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 224 ilmrnheiiqqPMKeekvaslmlkealaFIERYKREPFLLFFSFLHVHTPLISKKKFVGRSKYGRYGD------------ 291
Cdd:cd16030 199 -----------PKK--------------YFDLYPLESIPLPNPFDPIDLPEVAWNDLDDLPKYGDIPAlnpgdpkgplpd 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 292 ------------NVEEMDWMVGKILDALDQERLANHTLVYFTSDNGGHLE---------PLDGAVqlggwngiykggkgm 350
Cdd:cd16030 254 eqarelrqayyaSVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGehghwgkhtLFEEAT--------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 351 ggweggiRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGgiLSQDRVIDGQNLMPLLEGRASHSDHEFL--FHYCG 428
Cdd:cd16030 319 -------RVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKDAAFsqYPRPS 389
|
....*..
gi 58743319 429 VYLHTVR 435
Cdd:cd16030 390 IMGYSIR 396
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-409 |
6.39e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 129.59 E-value: 6.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLM-----ADDLGvgdlcCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPirsgmvsaynlnr 81
Cdd:cd16148 1 MNVILIVidslrADHLG-----CYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 82 aFTWLGGSGGLPTNETTFAKLLQHRGYRTGLIGkwhlglscasrnDHCYHPLNHGFHyfygvpfgllsdcqasktpelhr 161
Cdd:cd16148 63 -FYHGVWGGPLEPDDPTLAEILRKAGYYTAAVS------------SNPHLFGGPGFD----------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 162 wlriklwistvalalvpflllipkfarwfsvpwkvifvfallaFLFFTSWYSSYGFTRRWNCILMRNHEIIQqpmkeekv 241
Cdd:cd16148 107 -------------------------------------------RGFDTFEDFRGQEGDPGEEGDERAERVTD-------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 242 aslmlkEALAFIERYKR-EPFLLFFSFLHVHTPliskkkfvgrskYgRYGDNVEEMDWMVGKILDALDQERLANHTLVYF 320
Cdd:cd16148 136 ------RALEWLDRNADdDPFFLFLHYFDPHEP------------Y-LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIV 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 321 TSD----------NGGHLEPLDGAVqlggwngiykggkgmggweggIRVPGIFRWPSVlEAGRVINEPTSLMDIYPT-LS 389
Cdd:cd16148 197 TSDhgeefgehglYWGHGSNLYDEQ---------------------LHVPLIIRWPGK-EPGKRVDALVSHIDIAPTlLD 254
|
410 420
....*....|....*....|
gi 58743319 390 YIGGGILSQdrvIDGQNLMP 409
Cdd:cd16148 255 LLGVEPPDY---SDGRSLLP 271
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
1-414 |
5.29e-33 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 132.10 E-value: 5.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 1 MTRNARPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVsAYNLN 80
Cdd:PRK13759 1 MVQTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV-GYGDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 81 RAFTWlggsgglptnETTFAKLLQHRGYRTGLIGKWHLGlscASRNDHCYH-------PLNHGFHYfYGVPFGLLSDCQA 153
Cdd:PRK13759 80 VPWNY----------KNTLPQEFRDAGYYTQCIGKMHVF---PQRNLLGFHnvllhdgYLHSGRNE-DKSQFDFVSDYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 154 sktpelhrWLRIKlwistvALALVPFLllipkfarwfsvpwkvifvfallaflfftswyssygFTRRWNCilmrnHEIIQ 233
Cdd:PRK13759 146 --------WLREK------APGKDPDL------------------------------------TDIGWDC-----NSWVA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 234 QPM-KEEKV--ASLMLKEALAFIERY-KREPFLLFFSFLHVHTPL----------------------------------- 274
Cdd:PRK13759 171 RPWdLEERLhpTNWVGSESIEFLRRRdPTKPFFLKMSFARPHSPYdppkryfdmykdadipdphigdweyaedqdpeggs 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 275 ------ISKKKFVGRSKYGRYGdNVEEMDWMVGKILDALDQERLANHTLVYFTSDNGGHLE---------PLDGAvqlgg 339
Cdd:PRK13759 251 idalrgNLGEEYARRARAAYYG-LITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGdhylfrkgyPYEGS----- 324
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58743319 340 wngiykggkgmggweggIRVPGIFRWPS---VLEAGRVINEPTSLMDIYPTLSYIGGGilSQDRVIDGQNLMPLLEGR 414
Cdd:PRK13759 325 -----------------AHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGG--TIPDDVDGRSLKNLIFGQ 383
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
7-519 |
7.48e-33 |
|
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: 130.84 E-value: 7.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSaynlNRAftwl 86
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVW----NGT---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 ggsgGLPTNETTFAKLLQHRGYRTGLIGKWHL-----GLSCASRNDHCYHPLNHGFHyfYGVPFGLLSDcQASKTPelhr 161
Cdd:cd16028 73 ----PLDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFD--PVDRLDEYPA-EDSDTA---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 162 wlriklWISTVALAlvpflllipkfarWFSV----PWkvifvFALLAFL-----FFTS--WYSSYgftrrwncilmrNHE 230
Cdd:cd16028 142 ------FLTDRAIE-------------YLDErqdePW-----FLHLSYIrphppFVAPapYHALY------------DPA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 231 IIQQPMKEEKVASLMLKEAL--AFIERYKREPFllffsFLHVHTPLISKKKFVGRSKYGRYGdNVEEMDWMVGKILDALD 308
Cdd:cd16028 186 DVPPPIRAESLAAEAAQHPLlaAFLERIESLSF-----SPGAANAADLDDEEVAQMRATYLG-LIAEVDDHLGRLFDYLK 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 309 QERLANHTLVYFTSDNGGHLepldGAVQLGGwngiykggkGMGGWEGGIRVPGIFRWPSVLE---AGRVINEPTSLMDIY 385
Cdd:cd16028 260 ETGQWDDTLIVFTSDHGEQL----GDHWLWG---------KDGFFDQAYRVPLIVRDPRREAdatRGQVVDAFTESVDVM 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 386 PT-LSYIGGGILSQdrvIDGQNLMPLLEG-------RASHSDHEFlfhYCGVYLHTVR---WHQKDC-ATV-----WKah 448
Cdd:cd16028 327 PTiLDWLGGEIPHQ---CDGRSLLPLLAGaqpsdwrDAVHYEYDF---RDVSTRRPQEalgLSPDECsLAVirderWK-- 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58743319 449 YVT-PKFypegtgacygsgicscsgdvtyhdPPLLFDISRDPSEALPLNPDnePLFDSVIKKMEAAIREHRR 519
Cdd:cd16028 399 YVHfAAL------------------------PPLLFDLKNDPGELRDLAAD--PAYAAVVLRYAQKLLSWRM 444
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-512 |
7.49e-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: 126.53 E-value: 7.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASM----CTPSRAAFLTGRypirsgmvsayNLNR 81
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR-----------TLFH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 82 AFtwLGGSGGLPTNETTFAKLLQHRGYRTGLIGKWHlglscasrNDHCYHPLNHgfhyfygvpfglLSDCQASKTpelhr 161
Cdd:cd16155 71 AP--EGGKAAIPSDDKTWPETFKKAGYRTFATGKWH--------NGFADAAIEF------------LEEYKDGDK----- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 162 wlriklwistvalalvPFLLLIPkfarwFSVPwkvifvfallaflfftswyssygftrrwncilmrnHEIIQQPMKeekv 241
Cdd:cd16155 124 ----------------PFFMYVA-----FTAP-----------------------------------HDPRQAPPE---- 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 242 aslmlkealaFIERYKREPFLLFFSFLHVHT-----PLISKKKFVG--------RSKYGRYGDNVEEMDWMVGKILDALD 308
Cdd:cd16155 144 ----------YLDMYPPETIPLPENFLPQHPfdngeGTVRDEQLAPfprtpeavRQHLAEYYAMITHLDAQIGRILDALE 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 309 QERLANHTLVYFTSDNG---GH--LepldgavqLGGWNgiykggkgmgGWEGGIRVPGIFRWPSVlEAGRVINEPTSLMD 383
Cdd:cd16155 214 ASGELDNTIIVFTSDHGlavGShgL--------MGKQN----------LYEHSMRVPLIISGPGI-PKGKRRDALVYLQD 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 384 IYPTLSYIGGgiLSQDRVIDGQNLMPLLEGrASHSDHEFLFhycGVYLHTVRWHQKDcatVWKAHYVTPKfypegtgacy 463
Cdd:cd16155 275 VFPTLCELAG--IEIPESVEGKSLLPVIRG-EKKAVRDTLY---GAYRDGQRAIRDD---RWKLIIYVPG---------- 335
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 58743319 464 gsgicscsGDVTyhdppLLFDISRDPSEALPLNPdnEPLFDSVIKKMEA 512
Cdd:cd16155 336 --------VKRT-----QLFDLKKDPDELNNLAD--EPEYQERLKKLLA 369
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
7-391 |
1.69e-31 |
|
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: 122.14 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRL-TQHLAAASMCTPSRAAFLTGRYPIRSGMVSayNLNRAFTW 85
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTG--NGSADPEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 LGGSGGLPTNETTFAKLLQHRGYRTGLIGkwhlglscasrndhcyhplnhgfhyfygvpfgllsdcqasktpelhrwlri 165
Cdd:cd00016 79 PSRAAGKDEDGPTIPELLKQAGYRTGVIG--------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 166 klwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygftrrwncilmrnheiiqqpmkeekvaslm 245
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 246 lkeALAFIERYKRE-PFLLFFSFLHVHTPLISKkkfvgRSKYGRYGDNVEEMDWMVGKILDALDQERLANHTLVYFTSDN 324
Cdd:cd00016 108 ---LLKAIDETSKEkPFVLFLHFDGPDGPGHAY-----GPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADH 179
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58743319 325 GGHLEPLDGAVQLGGwngiykggkGMGGWEGGIRVPGIFRWPSVLeAGRVINEPTSLMDIYPTLSYI 391
Cdd:cd00016 180 GGIDKGHGGDPKADG---------KADKSHTGMRVPFIAYGPGVK-KGGVKHELISQYDIAPTLADL 236
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-415 |
3.64e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 115.79 E-value: 3.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADD-----LGvgdlcCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvsaynln 80
Cdd:cd16152 1 KPNVIVFFTDQqrwdtLG-----CYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 81 rAFTwlgGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLGlscasrndhcyhplnhgfhyfygvpfGLLSDCqasktpelh 160
Cdd:cd16152 68 -CFR---NGIPLPADEKTLAHYFRDAGYETGYVGKWHLA--------------------------GYRVDA--------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 161 rwlriklwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygFTRRwncilmrnheiiqqpmkeek 240
Cdd:cd16152 109 --------------------------------------------------------LTDF-------------------- 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 241 vaslmlkeALAFI-ERYKREPFLLFFSFLHVH---------TPLISKKKFVG--------------RSKYGRYGDNVEEM 296
Cdd:cd16152 113 --------AIDYLdNRQKDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANfwvppdlaalpgdwAEELPDYLGCCERL 184
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 297 DWMVGKILDALDQERLANHTLVYFTSDNGGHLE---------PLDGAvqlggwngiykggkgmggweggIRVPGIFRWPS 367
Cdd:cd16152 185 DENVGRIRDALKELGLYDNTIIVFTSDHGCHFRtrnaeykrsCHESS----------------------IRVPLVIYGPG 242
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 58743319 368 vLEAGRVINEPTSLMDIYPTLSYIGGgiLSQDRVIDGQNLMPLLEGRA 415
Cdd:cd16152 243 -FNGGGRVEELVSLIDLPPTLLDAAG--IDVPEEMQGRSLLPLVDGKV 287
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-407 |
1.29e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 112.47 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDLCCYGN----------NSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVS 75
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 76 aynlNRAfTWLGGSGGLPtnetTFAKLLQHRGYRTGLIGKWHLGlscasrndhcyhplnhgfhyfygvpfgllsdcqask 155
Cdd:cd16153 81 ----FEA-AHPALDHGLP----TFPEVLKKAGYQTASFGKSHLE------------------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 156 tpelhrwlriklwistvalalvpflllipKFARWFSVPWKvifvfallaflfftswyssyGFTRRWNcilmrnheiiqqp 235
Cdd:cd16153 116 -----------------------------AFQRYLKNANQ--------------------SYKSFWG------------- 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 236 mKEEKVASlmlkealafieryKREPFLLFFSFLHVHTPLISKKKFvgRSKYGRYGdNVEEMDWMVGKILDALDQERLANH 315
Cdd:cd16153 134 -KIAKGAD-------------SDKPFFVRLSFLQPHTPVLPPKEF--RDRFDYYA-FCAYGDAQVGRAVEAFKAYSLKQD 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 316 ---TLVYFTSDNGGHLEPlDGAV-QLGGWNgiykggkgmggweGGIRVPGIFRWPSVLE--AGRVINEPTSLMDIYPTLS 389
Cdd:cd16153 197 rdyTIVYVTGDHGWHLGE-QGILaKFTFWP-------------QSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTLL 262
|
410
....*....|....*...
gi 58743319 390 YIGGGILSQDRVIDGQNL 407
Cdd:cd16153 263 AAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
7-412 |
6.18e-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: 110.93 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVsaynlnraftwl 86
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSW------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 GGSGGLPTNETTFAKLLQHRGYRTGLIGKWHLglscasrndhcyhplnHGFHYF-YGV-PFGLLSD------CQASKTPE 158
Cdd:cd16156 69 TNCMALGDNVKTIGQRLSDNGIHTAYIGKWHL----------------DGGDYFgNGIcPQGWDPDywydmrNYLDELTE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 159 LHRWLRiklwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswyssygftRRWNCILMRNHeiiqqpMKE 238
Cdd:cd16156 133 EERRKS------------------------------------------------------RRGLTSLEAEG------IKE 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 239 EKV-ASLMLKEALAFIERYKREPFLLFFSFLHVHTPLISKKKFVgrSKYGRYG--------DNVEE-------------- 295
Cdd:cd16156 153 EFTyGHRCTNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYA--SMYKDFEfpkgenayDDLENkplhqrlwagakph 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 296 -------------------MDWMVGKILDALDqERLANhTLVYFTSDNGGHLepldGAVQLGGWNGIYKGGKGmggwegg 356
Cdd:cd16156 231 edgdkgtikhplyfgcnsfVDYEIGRVLDAAD-EIAED-AWVIYTSDHGDML----GAHKLWAKGPAVYDEIT------- 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 58743319 357 iRVPGIFRWPSVLEAGRVINEPTSLMDIYPT-LSYIGggiLSQDRVIDGQNLMPLLE 412
Cdd:cd16156 298 -NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTiLDYAG---IPQPKVLEGESILATIE 350
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
6-405 |
6.24e-26 |
|
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: 109.95 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 6 RPNIVLLMADDLGVGDlccyGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVS---AYNLNRA 82
Cdd:cd16147 1 RPNIVLILTDDQDVEL----GSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNnspPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 83 FTWLGgsgglpTNETTFAKLLQHRGYRTGLIGKwhlglscasrndhcYhpLNHgfhyfYGVPFGllsdcqasktpelhrw 162
Cdd:cd16147 77 FWQNG------LERSTLPVWLQEAGYRTAYAGK--------------Y--LNG-----YGVPGG---------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 163 lriklwistvaLALVPfllliPKFARWFsvpwkvifvfallaFLFFTSWYSSYGFTrrwncilmrNHEIIQQPMKEEKVA 242
Cdd:cd16147 114 -----------VSYVP-----PGWDEWD--------------GLVGNSTYYNYTLS---------NGGNGKHGVSYPGDY 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 243 S--LMLKEALAFIERYKR--EPFLLFFSFLHVHTPLIS----KKKFVGRSKYGRYG---------------------DNV 293
Cdd:cd16147 155 LtdVIANKALDFLRRAAAddKPFFLVVAPPAPHGPFTPapryANLFPNVTAPPRPPpnnpdvsdkphwlrrlpplnpTQI 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 294 EEMDW--------------MVGKILDALDQERLANHTLVYFTSDNGGHL-------------EPlDgavqlggwngiykg 346
Cdd:cd16147 235 AYIDElyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGYHLgqhrlppgkrtpyEE-D-------------- 299
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 58743319 347 gkgmggweggIRVPGIFRWPSVlEAGRVINEPTSLMDIYPTLSYIGGgiLSQDRVIDGQ 405
Cdd:cd16147 300 ----------IRVPLLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAG--APPPSDMDGR 345
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-426 |
3.16e-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: 106.14 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 33 PNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSayNLNRAFTWLggsggLPTNETTFAKLLQHRGYRTGL 112
Cdd:cd16035 27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTD--TLGSPMQPL-----LSPDVPTLGHMLRAAGYYTAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 113 IGKWHLglscasrNDHCYHPLNHGfhyfygvpfGLLSDcQAsktpelHRWLRiklwistvalalvpflllipKFARwfsv 192
Cdd:cd16035 100 KGKWHL-------SGAAGGGYKRD---------PGIAA-QA------VEWLR--------------------ERGA---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 193 pwkvifvfallaflfftswyssygftrrwncilmRNHEiiqqpmkeekvaslmlkealafierykREPFLLFFSFL--H- 269
Cdd:cd16035 133 ----------------------------------KNAD---------------------------GKPWFLVVSLVnpHd 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 270 VHTPLISKKKFVGRSKYgrYGDNVEEMDWMVGKILDALDQERLANHTLVYFTSDNGghlEpLDGAVQL-GGWNgiykggk 348
Cdd:cd16035 152 IMFPPDDEERWRRFRNF--YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG---E-MGGAHGLrGKGF------- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 349 gmGGWEGGIRVPGIFRWPSVLEAGRVINEPTSLMDIYPTLSYIGGGILSQDRVID----GQNLMPLLEGRASHSDHE-FL 423
Cdd:cd16035 219 --NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAVRDgIL 296
|
...
gi 58743319 424 FHY 426
Cdd:cd16035 297 FTY 299
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-514 |
9.22e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 103.85 E-value: 9.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSVSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvsaynlNRAFTWL 86
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG-------HRTLHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 87 ggsggLPTNETTFAKLLQHRGYRTGLIGKWHLGLSCASRNDHCyhplnhgfhyfygvpfglLSDCQASKTPElhRWLRIK 166
Cdd:cd16150 74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC------------------DSDEACVRTAI--DWLRNR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 167 lwiSTVAlalvPFLLLIPKFARW--FSVPWKvifvfallaflfftsWYSSYgfTRRwncilmrnheiiqqpmkeekvasl 244
Cdd:cd16150 129 ---RPDK----PFCLYLPLIFPHppYGVEEP---------------WFSMI--DRE------------------------ 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 245 MLKEALAFIERYKREPFLLffsflhvhtpliskkkfVGRSKYGRYGDN--------------VEEMDWMVGKILDALDQE 310
Cdd:cd16150 161 KLPPRRPPGLRAKGKPSML-----------------EGIEKQGLDRWSeerwrelratylgmVSRLDHQFGRLLEALKET 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 311 RLANHTLVYFTSDNG------GHLEPLDGAVQlggwngiykggkgmggwEGGIRVPGIFRwPSVLEAGRVINEPTSLMDI 384
Cdd:cd16150 224 GLYDDTAVFFFSDHGdytgdyGLVEKWPNTFE-----------------DCLTRVPLIIK-PPGGPAGGVSDALVELVDI 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 385 YPTLSYIGGgiLSQDRVIDGQNLMPLLEG-RASHSDHEFlfhyC-GVYLHtvrwHQKDCatVWKAHYVTPKFYPEGT--- 459
Cdd:cd16150 286 PPTLLDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SeGGRLH----GEEQA--MEGGHGPYDLKWPRLLqqe 353
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 460 -GACYGSGICSCSGDVTY----HDPPLLFDISRDPSEAlpLNPDNEPLFDSVIKKMEAAI 514
Cdd:cd16150 354 ePPEHTKAVMIRTRRYKYvyrlYEPDELYDLEADPLEL--HNLIGDPAYAEIIAEMKQRL 411
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
7-413 |
2.95e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 95.49 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGVGDLCCYGNNSV--STPNIDRLASEGVRLTqHLAAASMCTPSRAAFLTGRYPIRSGMvsaynlnrafT 84
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV----------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 85 WLGGSGGLPTNETTFAKLLQHR--GYRTGLIGKWHLGlscasrNDHcYHPLNHG-FHYFYGVPFGLLSDcqasktpelhr 161
Cdd:cd16154 70 AVPDELLLSEETLLQLLIKDATtaGYSSAVIGKWHLG------GND-NSPNNPGgIPYYAGILGGGVQD----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 162 wlriklwistvalalvpflllipkfarwfsvpwkvifvfallaflfftswYSSYGFTRrwNCILMRNHEIIQqpmkeEKV 241
Cdd:cd16154 132 --------------------------------------------------YYNWNLTN--NGQTTNSTEYAT-----TKL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 242 ASLmlkeALAFIERyKREPFLLFFSFLHVHTPL-ISKKKFVGRSKYGRY---GDN--------VEEMDWMVGKILDALDQ 309
Cdd:cd16154 155 TNL----AIDWIDQ-QTKPWFLWLAYNAPHTPFhLPPAELHSRSLLGDSadiEANprpyylaaIEAMDTEIGRLLASIDE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 310 ERLANhTLVYFTSDNG--GHLEPLD-------GAVQLGGwngiykggkgmggweggIRVPGIFRWPSVLEAGRVINEPTS 380
Cdd:cd16154 230 EEREN-TIIIFIGDNGtpGQVVDLPytrnhakGSLYEGG-----------------INVPLIVSGAGVERANERESALVN 291
|
410 420 430
....*....|....*....|....*....|...
gi 58743319 381 LMDIYPTLSYIGGGILSQdrVIDGQNLMPLLEG 413
Cdd:cd16154 292 ATDLYATIAELAGVDAAE--IHDSVSFKPLLSD 322
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
7-490 |
7.08e-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: 67.18 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 7 PNIVLLMADDLGvGDLCCYGNNS-VSTPNIDRLASEGVRLTQHLAAASMCTPSRAAFLTGRYPirsGMVSAYNLNRaftw 85
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRPGNQvVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT---HLTESWNNYK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 86 lggsgGLPTNETTFAKLLQHRGYRTGLIGKwhlgLSCASrndhcyhplnhGFHyfygvpfgllsdcqaSKTPELHRWLRI 165
Cdd:cd16171 73 -----GLDPNYPTWMDRLEKHGYHTQKYGK----LDYTS-----------GHH---------------SVSNRVEAWTRD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 166 klwistvalalVPFLLlipkfaRWFSVPWKVIFVFALLAFLFFTSWYSSygftrrwncilmrnheiiqqpmkeEKVASLM 245
Cdd:cd16171 118 -----------VPFLL------RQEGRPTVNLVGDRSTVRVMLKDWQNT------------------------DKAVHWI 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 246 LKEALAFierykREPFLLFFSFLHVHT-PLISKKKFVGRSKYGR--YGDNVEEMDWMVGKILDALDQERLANHTLVYFTS 322
Cdd:cd16171 157 RKEAPNL-----TQPFALYLGLNLPHPyPSPSMGENFGSIRNIRafYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTS 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 323 DNGghleplDGAVQlggwngiYKGGKGMGGWEGGIRVPGIFRWPSVlEAGRVINEPTSLMDIYPTLSYIGGgiLSQDRVI 402
Cdd:cd16171 232 DHG------ELAME-------HRQFYKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAG--VPQPQNL 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 403 DGQNLMPLLEGRASHSDHEFL---------FHYCGVYLHT--VRWHQkdcatvWKahYVTpkfypegtgacYGSGICScs 471
Cdd:cd16171 296 SGYSLLPLLSESSIKESPSRVphpdwvlseFHGCNVNASTymLRTNS------WK--YIA-----------YADGNSV-- 354
|
490
....*....|....*....
gi 58743319 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 |
3.82e-07 |
|
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: 51.91 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 245 MLKEALAFIERYKREPFLLF---------FSFLHVHTPLISKKKFvGRSKYGRYGDNVEEMDWMVGKILDALDQERLANH 315
Cdd:cd16015 142 LFDQALEELEELKKKPFFIFlvtmsnhgpYDLPEEKKDEPLKVEE-DKTELENYLNAIHYTDKALGEFIEKLKKSGLYEN 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58743319 316 TLVYFTSDnggHLEPLDGAVQLGGWNGIYKGgkgmggweggiRVPGIFRWPSvLEAGRVINEPTSLMDIYPTL 388
Cdd:cd16015 221 TIIVIYGD---HLPSLGSDYDETDEDPLDLY-----------RTPLLIYSPG-LKKPKKIDRVGSQIDIAPTL 278
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
245-388 |
9.01e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 48.50 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 245 MLKEALAFIERYKrEPFLLFFSFLHVHTPLISKKKFVGRSKYGRYGDN-----VEEMDWMVGKILDALDQERLANHTLVY 319
Cdd:COG1368 371 LFDKALEELEKLK-KPFFAFLITLSNHGPYTLPEEDKKIPDYGKTTLNnylnaVRYADQALGEFIEKLKKSGWYDNTIFV 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58743319 320 FTSDnggHLEPLDGavqlggwngiykgGKGMGGWEGGIRVPGIFrWPSVLEAGRVINEPTSLMDIYPTL 388
Cdd:COG1368 450 IYGD---HGPRSPG-------------KTDYENPLERYRVPLLI-YSPGLKKPKVIDTVGSQIDIAPTL 501
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
288-388 |
1.77e-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: 47.59 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 288 RYGDNVEEMDWMVGKILDALDQERLANHTLVYFTSDNGghlEPLDGavqlggwNGIYKGGKGMGGWEGGIRVPGIFRWPS 367
Cdd:COG3083 428 RYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHG---EEFNE-------NGQNYWGHNSNFSRYQLQVPLVIHWPG 497
|
90 100
....*....|....*....|.
gi 58743319 368 vlEAGRVINEPTSLMDIYPTL 388
Cdd:COG3083 498 --TPPQVISKLTSHLDIVPTL 516
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
5-146 |
8.41e-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: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 5 ARPNIVLLMADDLGVGDLccygnNSVSTPNIDRLASEGVRLTQHLAAA-SMCTPSRAAFLTGRYPIRSGMVS-------- 75
Cdd:COG1524 22 PAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIVGngwydpel 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58743319 76 ---AYNLNRAFTWLGGSGGLPTneTTFAKLLQHRGYRTGLIGKWHLGLSCASRNDHCYHPlnHGFHYFYGVPFG 146
Cdd:COG1524 97 grvVNSLSWVEDGFGSNSLLPV--PTIFERARAAGLTTAAVFWPSFEGSGLIDAARPYPY--DGRKPLLGNPAA 166
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
238-340 |
4.69e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 39.33 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58743319 238 EEKVASLMLKE--ALAFIERYKREPFLLFFSFLHVHTpliskkkfVGRsKYG----RYGDNVEEMDWMVGKILDALDQER 311
Cdd:pfam01663 139 EDRVDTAVLQTwlDLPFADVAAERPDLLLVYLEEPDY--------AGH-RYGpdspEVEDALRRVDRAIGDLLEALDERG 209
|
90 100
....*....|....*....|....*....
gi 58743319 312 LANHTLVYFTSDNGGHLEPLDGAVQLGGW 340
Cdd:pfam01663 210 LFEDTNVIVVSDHGMTPVSDDKVIFLNDY 238
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
32-82 |
7.47e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 38.94 E-value: 7.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 58743319 32 TPNIDRLASEGVRLTQHLAAA-SMCTPSRAAFLTGRYPIRSGMVSAYNLNRA 82
Cdd:pfam01663 20 TPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGNTFYDPK 71
|
|
| |
