|
Name |
Accession |
Description |
Interval |
E-value |
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
20-503 |
0e+00 |
|
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: 862.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPGVLEPSSRGG 99
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 LPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGSCDQGLVPI 179
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNLTCFPPNIPCFGGCDQGEVPC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 180 PLLANLSVVVQPPWLPGLEARYVAFARDLMADAQRQGRPFFLYYASHHTHYPQFSGQSFAGRSGRGPFGDSLMELDAAVG 259
Cdd:cd16158 161 PLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 260 ALMTAVGDLGLLGETLVIFAADNGPETMRMSRGGCSGLLRCGKGTTFEGGVREPALAFWPGHIAPGVTHELASSLDLLPT 339
Cdd:cd16158 241 ELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 340 LAALTGAPLPNITLDGVDLSPLLLGTGKSPRQTVFFYPANPDEVRGVFAVRSGKYKAHFFTQGSAHSDTTADPACHASSP 419
Cdd:cd16158 321 IAKLAGAPLPNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVFAVRWGKYKAHFYTQGAAHSGTTPDKDCHPSAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 420 LTAHEPPLLFDLSEDPSENYNLLEgvakvTSETLQALKHLQLLKAQFDATMTFSPSQMARGEDPALQICCQPSCTPWPSC 499
Cdd:cd16158 401 LTSHDPPLLFDLSQDPSENYNLLG-----LPEYNQVLKQIQQVKERFEASMKFGESEINKGEDPALEPCCKPGCTPKPSC 475
|
....
gi 545206886 500 CHCP 503
Cdd:cd16158 476 CQCH 479
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
20-441 |
0e+00 |
|
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: 552.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPGVLEPSSRGG 99
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 LPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPatpcdgscdqgLVPI 179
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPE--FLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP-----------GPLP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 180 PLLANLSVVVQPPWLPGLEARYVAFARDLMADAqrQGRPFFLYYASHHTHYPQFSGQSFAGRSGRGPFGDSLMELDAAVG 259
Cdd:cd16026 148 PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 260 ALMTAVGDLGLLGETLVIFAADNGPETMRMSRGGCSGLLRCGKGTTFEGGVREPALAFWPGHIAPG-VTHELASSLDLLP 338
Cdd:cd16026 226 RILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGtVSDELASTMDLLP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 339 TLAALTGAPLPNI-TLDGVDLSPLLLGTGKSPRQTVFFYPANPDevrgVFAVRSGKYKAHFFTQGSAHSDTtadpachAS 417
Cdd:cd16026 306 TLAALAGAPLPEDrVIDGKDISPLLLGGSKSPPHPFFYYYDGGD----LQAVRSGRWKLHLPTTYRTGTDP-------GG 374
|
410 420
....*....|....*....|....
gi 545206886 418 SPLTAHEPPLLFDLSEDPSENYNL 441
Cdd:cd16026 375 LDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
21-451 |
1.25e-133 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 394.49 E-value: 1.25e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPG--VLEPSSRG 98
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGtrVFLPWDIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 99 GLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPE----GAFLPPHQGFHrFLG--IPYSHdqgpcqNLTCFPPATPCDGSc 172
Cdd:cd16160 82 GLPKTEVTMAEALKEAGYTTGMVGKWHLGINENnhsdGAHLPSHHGFD-FVGtnLPFTN------SWACDDTGRHVDFP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 173 DQGLVPipLLANLSVVVQPPWLPGLEARYVAFARDLMADaqRQGRPFFLYYASHHTHYPQFSGQSFAGRSGRGPFGDSLM 252
Cdd:cd16160 154 DRSACF--LYYNDTIVEQPIQHEHLTETLVGDAKSFIED--NQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNIN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 253 ELDAAVGALMTAVGDLGLLGETLVIFAADNGPETMRMSRGGCSGLLRCGKGTTFEGGVREPALAFWPGHIAPGVTHELAS 332
Cdd:cd16160 230 EMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 333 SLDLLPTLAALTGAPLPNIT-LDGVDLSPLLLGTGKSPRQTVFFYPANPdevrgVFAVRSGKYKAHFFTQgSAHSDTTAD 411
Cdd:cd16160 310 TMDIFPTFVDLAGGTLPTDRiYDGLSITDLLLGEADSPHDDILYYCCSR-----LMAVRYGSYKIHFKTQ-PLPSQESLD 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545206886 412 PACHASSPL--------------TAHEPPLLFDLSEDPSENYNL--------LEGVAKVTSE 451
Cdd:cd16160 384 PNCDGGGPLsdyivcydcedecvTKHNPPLIFDVEKDPGEQYPLqpsvyehmLEAVEKLIAH 445
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
20-441 |
6.06e-122 |
|
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: 362.17 E-value: 6.06e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYGHPSS-TTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLyPGVLEPSSRG 98
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAiLTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 99 GLPLEEVTLAEVLAARGYLTGMAGKWHLGVgpEGAFLPPHQGFHRFLGIPYSHDQGpcqnltcfppatpcdgscdqglvp 178
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLGQ--REAYLPNSRGFDYYFGIPFSHDSS------------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 179 ipllanlsvvvqppwlpgLEARYVAFARDLMADAQRQGRPFFLYYASHHTHYPQFSGQSF-AGRSGRGPFGDSLMELDAA 257
Cdd:cd16161 134 ------------------LADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFqSPTSGRGPYGDALQEMDDL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 258 VGALMTAVGDLGLLGETLVIFAADNGPETMRMSRGGCSGL--------LRCGKGTTFEGGVREPALAFWPGHIAPGVTHE 329
Cdd:cd16161 196 VGQIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGPGTgdwqgnlgGSVAKASTWEGGHREPAIVYWPGRIPANSTSA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 330 -LASSLDLLPTLAALTGAPLP-NITLDGVDLSPLLLGTGKSPRQTVFFYPANPDEVRGVFAVRSGKYKAHFFTQGsahsd 407
Cdd:cd16161 276 aLVSTLDIFPTVVALAGASLPpGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAGAGALSAVRCGDYKAHYATGG----- 350
|
410 420 430
....*....|....*....|....*....|....
gi 545206886 408 ttADPACHASSPLTAHEPPLLFDLSEDPSENYNL 441
Cdd:cd16161 351 --ALACCGSTGPKLYHDPPLLFDLEVDPAESFPL 382
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-441 |
3.86e-121 |
|
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: 359.92 E-value: 3.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSST---TPNLDQLAAGGLRFTDFYVPVSlCTPSRAALLTGRLPVRMGLYPgVLEPSSR 97
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTT-VGLPGSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 98 GGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHdqgpcqnltcfppatpcdgscdqglv 177
Cdd:cd16142 79 GGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG--RLPTDHGFDEFYGNLYHT-------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 178 pipllanlsvvvqppwlpgLEARYVAFARDLMADAQRQGRPFFLYYASHHTHYPQFSGQSFAGRS-GRGPFGDSLMELDA 256
Cdd:cd16142 131 -------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSsGKGKYADSMVELDD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 257 AVGALMTAVGDLGLLGETLVIFAADNGPETMRMSRGGcSGLLRCGKGTTFEGGVREPALAFWPGHIAPG-VTHELASSLD 335
Cdd:cd16142 192 HVGQILDALDELGIADNTIVIFTTDNGPEQDVWPDGG-YTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGrVSNEIVSHLD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 336 LLPTLAALTGAPLPN-------ITLDGVDLSPLLLGTGKSPRQTVFFYPANPDevrgVFAVRSGKYKAHFFTQgsahsDT 408
Cdd:cd16142 271 WFPTLAALAGAPDPKdkllgkdRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGE----LGAVRWKNWKVHFKAQ-----ED 341
|
410 420 430
....*....|....*....|....*....|...
gi 545206886 409 TADPACHASSPLTAhepPLLFDLSEDPSENYNL 441
Cdd:cd16142 342 TGGPTGEPFYVLTF---PLIFNLRRDPKERYDV 371
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
20-470 |
7.43e-107 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 324.14 E-value: 7.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPgvLEPSSRGG 99
Cdd:COG3119 23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD--NGEGYNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 LPLEEVTLAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipYSHDqgpcqnltcfppatpcdgscdqglvpi 179
Cdd:COG3119 101 LPPDEPTLAELLKEAGYRTALFGKWHL----------------------YLTD--------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 180 pllanlsvvvqppwlpgleaRYVAFARDLMADAQRQGRPFFLYYASHHTHYP---------QFSGQSFA----------- 239
Cdd:COG3119 132 --------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldKYDGKDIPlppnlaprdlt 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 240 ---GRSGRGPFGDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNGPEtmrmsrGGCSGlLRCGKGTTFEGGVREPALA 316
Cdd:COG3119 192 eeeLRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS------LGEHG-LRGGKGTLYEGGIRVPLIV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 317 FWPGHIAPG-VTHELASSLDLLPTLAALTGAPLPNiTLDGVDLSPLLLGTGKSPRQTVFF-YPanpdEVRGVFAVRSGKY 394
Cdd:COG3119 265 RWPGKIKAGsVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPLLTGEKAEWRDYLYWeYP----RGGGNRAIRTGRW 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545206886 395 KAHFFTQGSahsdttadpachasspltahEPPLLFDLSEDPSENYNLlegvAKVTSETLQALKhlQLLKAQFDATM 470
Cdd:COG3119 340 KLIRYYDDD--------------------GPWELYDLKNDPGETNNL----AADYPEVVAELR--ALLEAWLKELG 389
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-441 |
7.75e-107 |
|
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: 324.15 E-value: 7.75e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGhPSST--TPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPGVLEPSSRG 98
Cdd:cd16143 1 PNIVIILADDLGYGDISCYN-PDSKipTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 99 GLPLEEVTLAEVLAARGYLTGMAGKWHLG-----VGPEGAFL---------------PPHQGFHRFLGIPYShdqgpcQN 158
Cdd:cd16143 80 LIEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkKDGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPAS------EV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 159 LtcfppatpcdgscdqglvpiPLLANLSVvvqppwlpglearyvafarDLMADAQRQGRPFFLYYASHHTHYPQFSGQSF 238
Cdd:cd16143 154 L--------------------PTLTDKAV-------------------EFIDQHAKKDKPFFLYFALPAPHTPIVPSPEF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 239 AGRSGRGPFGDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNGPETMR----MSRGG--CSGLLRCGKGTTFEGGVRE 312
Cdd:cd16143 195 QGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYAdykeLEKFGhdPSGPLRGMKADIYEGGHRV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 313 PALAFWPGHIAPG-VTHELASSLDLLPTLAALTGAPLP-NITLDGVDLSPLLLGTGKSPRQTVFFYPANpdevRGVFAVR 390
Cdd:cd16143 275 PFIVRWPGKIPAGsVSDQLVSLTDLFATLAAIVGQKLPdNAAEDSFSFLPALLGPKKQEVRESLVHHSG----NGSFAIR 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 545206886 391 SGKYKAhFFTQGSAHSDTtadPACHASSPLTAHEpplLFDLSEDPSENYNL 441
Cdd:cd16143 351 KGDWKL-IDGTGSGGFSY---PRGKEKLGLPPGQ---LYNLSTDPGESNNL 394
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
20-488 |
2.55e-106 |
|
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: 325.19 E-value: 2.55e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYP-------GVL 92
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharnAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 93 EPSSRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHdqgpcqnltcFPPATpcdgsc 172
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ--YHPLKHGFDEWFGAPNCH----------FGPYD------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 173 DQGLVPIPLLANLSVVVQ---------PPWLPGLEARYVAFARDLMADAQRQGRPFFLYYASHHTHYPQFSGQSFAGRSG 243
Cdd:cd16157 143 NKAYPNIPVYRDWEMIGRyyeefkidkKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 244 RGPFGDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNGPETM-RMSRGGCSGLLRCGKGTTFEGGVREPALAFWPGHI 322
Cdd:cd16157 223 RGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALIsAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 323 APG-VTHELASSLDLLPTLAALTGAPLP-NITLDGVDLSPLLLgTGKSPRQTVFFYPANPdevrgVFAVRSGKYKAHFFT 400
Cdd:cd16157 303 KPGqVSHQLGSLMDLFTTSLALAGLPIPsDRAIDGIDLLPVLL-NGKEKDRPIFYYRGDE-----LMAVRLGQYKAHFWT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 401 -QGSAHSDTTADPACHAS--SPLTAH------EPPLLFDLSEDPSENYNLlegvAKVTSETLQALKHLQLLKAQFDATMT 471
Cdd:cd16157 377 wSNSWEEFRKGINFCPGQnvPGVTTHnqtdhtKLPLLFHLGRDPGEKYPI----SFKSAEYKQAMPRISKVVQQHQKTLV 452
|
490
....*....|....*..
gi 545206886 472 fspsqmaRGEdPALQIC 488
Cdd:cd16157 453 -------PGE-PQLNVC 461
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-457 |
1.26e-101 |
|
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: 311.40 E-value: 1.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLY------------ 88
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITdvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 89 PGVLEPSSRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGvgPEGAFLPPHQGFHRflGIPYSHDQGPcqnLTCFPPATPc 168
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG--GEGGYGPEDQGFDV--NIGGTGNGGP---PSYYFPPGK- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 169 dgscdqglvpipllanlsvvVQPPWLPGLEARYVAFArdlMADA------QRQGRPFFLYYASHHTHYPQFSGQSF---- 238
Cdd:cd16144 153 --------------------PNPDLEDGPEGEYLTDR---LTDEaidfieQNKDKPFFLYLSHYAVHTPIQARPELieky 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 239 ------AGRSGRGPFGDSLME-LDAAVGALMTAVGDLGLLGETLVIFAADNGPETMRMSRGGCSGLLRCGKGTTFEGGVR 311
Cdd:cd16144 210 ekkkkgLRKGQKNPVYAAMIEsLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNAPLRGGKGSLYEGGIR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 312 EPALAFWPGHIAPG-VTHELASSLDLLPTLAALTGAPLP-NITLDGVDLSPLLLGTG-KSPRQTVFF-YP-ANPDEVRGV 386
Cdd:cd16144 290 VPLIVRWPGVIKPGsVSDVPVIGTDLYPTFLELAGGPLPpPQHLDGVSLVPLLKGGEaDLPRRALFWhFPhYHGQGGRPA 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545206886 387 FAVRSGKYK-AHFFTQGSAHsdttadpachasspltahepplLFDLSEDPSENYNLLEGVAKVTSETLQALK 457
Cdd:cd16144 370 SAIRKGDWKlIEFYEDGRVE----------------------LYNLKNDIGETNNLAAEMPEKAAELKKKLD 419
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
20-467 |
2.51e-100 |
|
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: 311.53 E-value: 2.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGL-----YPGVLEP 94
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMasshgMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 95 SSRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPE----GAFLPPHQGFHRFLGIPYSH--DQGPCQNL---TCFPPA 165
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCEsrndFCHHPLNHGFDYFYGLPLTNlkDCGDGSNGeydLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 166 TP-----------------CDGSCDQ----------GLVPIP--------------LLANLSVVVQPPWLPGLEARYVAF 204
Cdd:cd16159 161 FPlltafvlitaltiflllYLGAVSKrffvfllilsLLFISLfflllitnryfnciLMRNHEVVEQPMSLENLTQRLTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 205 ARDLMADaqRQGRPFFLYYASHHTHYPQFSGQSFAGRSGRGPFGDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNGP 284
Cdd:cd16159 241 AISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 285 ETMRMSR-----GGCSGLLRCGKGTTFEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALTGAPLPN-ITLDGVD 357
Cdd:cd16159 319 HLEEISVggeygGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGsVIDEPTSLMDIFPTVAALAGAPLPSdRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 358 LSPLLLGTGK-SPRQTVFFYPANpdEVRGV-FAVRSGK--YKAHFFTQGSaHSDTTADPA---CHASSP-LTAHEPPLLF 429
Cdd:cd16159 399 LMPLLTGQEKrSPHEFLFHYCGA--ELHAVrYRPRDGGavWKAHYFTPNF-YPGTEGCCGtllCRCFGDsVTHHDPPLLF 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 545206886 430 DLSEDPSENYNL---LEGVAKVTSETLQALK-HLQLLKA---QFD 467
Cdd:cd16159 476 DLSADPSESNPLdptDEPYQEIIKKILEAVAeHQSSIEPvesQLS 520
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
21-468 |
9.14e-86 |
|
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: 270.19 E-value: 9.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYV-PVslCTPSRAALLTGRLPVRMGLYpGVLEPSSRgg 99
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVsPV--CAPTRAALLTGRYPFRTGVW-HTILGRER-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 LPLEEVTLAEVLAARGYLTGMAGKWHLGVGPegAFLPPHQGFHRFLGIPYSH-DQGPcqnltcfppatpcDGSCDQGLVP 178
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNY--PYRPQDRGFDEVLGHGGGGiGQYP-------------DYWGNDYFDD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 179 IpLLANlsvvvqppwlpGLEARYVAFARDLMADA------QRQGRPFFLYYASHHTHYPQFSGQSFAGRSGRGPFGDSL- 251
Cdd:cd16146 141 T-YYHN-----------GKFVKTEGYCTDVFFDEaidfieENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLa 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 252 ----M--ELDAAVGALMTAVGDLGLLGETLVIFAADNGPETMRMSR--GGcsglLRCGKGTTFEGGVREPALAFWPGHIA 323
Cdd:cd16146 209 afygMieNIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRfnAG----MRGKKGSVYEGGHRVPFFIRWPGKIL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 324 PG-VTHELASSLDLLPTLAALTGAPLP-NITLDGVDLSPLLLGTGKSPRQTVFFY----PANPDEVRGVFAVRSGKYKah 397
Cdd:cd16146 285 AGkDVDTLTAHIDLLPTLLDLCGVKLPeGIKLDGRSLLPLLKGESDPWPERTLFThsgrWPPPPKKKRNAAVRTGRWR-- 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545206886 398 fFTQGSAhsdttadpachasspltahEPPLLFDLSEDPSENYNLLEGVAKVTSEtlqalkhlqlLKAQFDA 468
Cdd:cd16146 363 -LVSPKG-------------------FQPELYDIENDPGEENDVADEHPEVVKR----------LKAAYEA 403
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-441 |
3.93e-83 |
|
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: 263.69 E-value: 3.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTG----RLPVRMGlypgvlePSS 96
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGlhtgHTRVRGN-------SEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 97 RGGLPL--EEVTLAEVLAARGYLTGMAGKWHLG-VGPEGAflPPHQGFHRFLGIpysHDQGPCQNLtcFPPATPCDGscd 173
Cdd:cd16145 74 GGQDPLppDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGH--PTKQGFDYFYGY---LDQVHAHNY--YPEYLWRNG--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 174 qGLVPIPllanlsvvvQPPWLPGLEARYVAFAR-----DLMADA------QRQGRPFFLYYAS---H-HTHYPQFSG--Q 236
Cdd:cd16145 144 -EKVPLP---------NNVIPPLDEGNNAGGGGgtyshDLFTDEaldfirENKDKPFFLYLAYtlpHaPLQVPDDGPykY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 237 SFAGRSGRGPFGDSLME---------LDAAVGALMTAVGDLGLLGETLVIFAADNGPEtmrmSRGGC---------SGLL 298
Cdd:cd16145 214 KPKDPGIYAYLPWPQPEkayaamvtrLDRDVGRILALLKELGIDENTLVVFTSDNGPH----SEGGSehdpdffdsNGPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 299 RCGKGTTFEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALTGAPLPNiTLDGVDLSPLLLGTGKSPRQTVFFYp 377
Cdd:cd16145 290 RGYKRSLYEGGIRVPFIARWPGKIPAGsVSDHPSAFWDFMPTLADLAGAEPPE-DIDGISLLPTLLGKPQQQQHDYLYW- 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545206886 378 aNPDEVRGVFAVRSGKYKAHFFTQGSahsdttadpachasspltahEPPLLFDLSEDPSENYNL 441
Cdd:cd16145 368 -EFYEGGGAQAVRMGGWKAVRHGKKD--------------------GPFELYDLSTDPGETNNL 410
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
21-441 |
1.39e-79 |
|
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: 253.63 E-value: 1.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPvSLCTPSRAALLTGRLPVRMGLYPGVLEPSSRGGL 100
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 PLEEVTLAEVLAARGYLTGMAGKWHLGVGPEgAFLPPHQGFHRFLGiPYSHDQGPCQNLTCFPPATPCDGSCDQGLVPip 180
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTW-EYTPTNRGFDSFYG-YYGGAEDYYTHTSGGANDYGNDDLRDNEEPA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 181 llanlsvvvqppwlPGLEARYVA--FARDLMA--DAQRQGRPFFLYYASHHTHYP-QFSGQSFAGRSGRGPFGDS----- 250
Cdd:cd16029 156 --------------WDYNGTYSTdlFTDRAVDiiENHDPSKPLFLYLAFQAVHAPlQVPPEYADPYEDKFAHIKDedrrt 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 251 ----LMELDAAVGALMTAVGDLGLLGETLVIFAADNGPETMRMSrGGCSGLLRCGKGTTFEGGVREPALaFWPGHI---A 323
Cdd:cd16029 222 yaamVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRGGKNTLWEGGVRVPAF-VWSPLLppkR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 324 PGVTHELASSLDLLPTLAALTGA-PLPNITLDGVDLSPLLLGTGKSPRQTVFFYPANPDEVRGVFAVRSGKYKAHFFTQg 402
Cdd:cd16029 300 GTVSDGLMHVTDWLPTLLSLAGGdPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDITRTTGGAAIRVGDWKLIVGKP- 378
|
410 420 430
....*....|....*....|....*....|....*....
gi 545206886 403 sahsdttadpachasspltahepplLFDLSEDPSENYNL 441
Cdd:cd16029 379 -------------------------LFNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
21-357 |
2.78e-73 |
|
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: 231.94 E-value: 2.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYpgvLEPSSRGGL 100
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVR---GNVGNGGGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 PLEEVTLAEVLAARGYLTGMAGKWHlgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcDGSCDqglvpip 180
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------DEAID------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 181 llanlsvvvqppWLpglearyvafardlmaDAQRQGRPFFLYYASHHTHYPqfsgqsFAgrsgrgpFGDSLMELDAAVGA 260
Cdd:cd16022 108 ------------FI----------------ERRDKDKPFFLYVSFNAPHPP------FA-------YYAMVSAIDDQIGR 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 261 LMTAVGDLGLLGETLVIFAADNGPetMRMSRGgcsglLRCGKGTTFEGGVREPALAFWPGHIAPG-VTHELASSLDLLPT 339
Cdd:cd16022 147 ILDALEELGLLDNTLIVFTSDHGD--MLGDHG-----LRGKKGSLYEGGIRVPFIVRWPGKIPAGqVSDALVSLLDLLPT 219
|
330
....*....|....*...
gi 545206886 340 LAALTGAPLPNiTLDGVD 357
Cdd:cd16022 220 LLDLAGIEPPE-GLDGRS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-413 |
8.80e-73 |
|
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: 235.57 E-value: 8.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPvSLCTPSRAALLTGRLPVRMGLYPGVLEPSsrggl 100
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNYVVFGYLDPK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 pleEVTLAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCqnltcFPPATPcdgscdqglvpIP 180
Cdd:cd16151 75 ---QKTFGHLLKDAGYATAIAGKWQLGGGRGDGDYPHEFGFDEYCLWQLTETGEKY-----SRPATP-----------TF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 181 LLANLSVvvqppwlpgLEARYVAFARDLMAD------AQRQGRPFFLYYASHHTHYP----------QFSGQSFAGRSGR 244
Cdd:cd16151 136 NIRNGKL---------LETTEGDYGPDLFADflidfiERNKDQPFFAYYPMVLVHDPfvptpdspdwDPDDKRKKDDPEY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 245 gpFGDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNG--PETMRMSRGgcsGLLRCGKGTTFEGGVREPALAFWPGHI 322
Cdd:cd16151 207 --FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNG---REVRGGKGKTTDAGTHVPLIVNWPGLI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 323 APG-VTHELASSLDLLPTLAALTGAPLP-NITLDGVDLSPLLLG-TGKSPRQTVFFYPANPDEVRGVFAVRSGKYK---- 395
Cdd:cd16151 282 PAGgVSDDLVDFSDFLPTLAELAGAPLPeDYPLDGRSFAPQLLGkTGSPRREWIYWYYRNPHKKFGSRFVRTKRYKlyad 361
|
410
....*....|....*...
gi 545206886 396 AHFFtqgsahsDTTADPA 413
Cdd:cd16151 362 GRFF-------DLREDPL 372
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
21-441 |
1.81e-71 |
|
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: 232.01 E-value: 1.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYgDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPgvLEpSSRGGL 100
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHG--LR-SRGFPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 PLEEVTLAEVLAARGYLTGMAGKWHlgVGPEGAFLPPHQGFHRFLGIPYSHDqgpcqnltcfppatpcdgscdqglvpip 180
Cdd:cd16027 77 PDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWD---------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 181 llanlsvvvqppwlpglearYVAFARDLMaDAQRQGRPFFLYYASHHTHYPQFSGQSFAG-------------------R 241
Cdd:cd16027 127 --------------------YASNAADFL-NRAKKGQPFFLWFGFHDPHRPYPPGDGEEPgydpekvkvppylpdtpevR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 242 SGRGPFGDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNGpetMRMSRggcsgllrcGKGTTFEGGVREPALAFWPGH 321
Cdd:cd16027 186 EDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG---MPFPR---------AKGTLYDSGLRVPLIVRWPGK 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 322 IAPG-VTHELASSLDLLPTLAALTGAPLPNiTLDGVDLSPLLLGTGKSPRQTVFFY----PANPDEVRgvfAVRSGKYK- 395
Cdd:cd16027 254 IKPGsVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLLKGEKDPGRDYVFAErdrhDETYDPIR---SVRTGRYKy 329
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 545206886 396 AHFFtqgsahsdttadpachasspltahEPPLLFDLSEDPSENYNL 441
Cdd:cd16027 330 IRNY------------------------MPEELYDLKNDPDELNNL 351
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
19-441 |
1.85e-69 |
|
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: 227.71 E-value: 1.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 19 NPPNILLIFADDLGYGDLGSYGHPSSTtPNLDQLAAGGLRFTDFYVpVSLCTPSRAALLTGRLP--VRMGLYPGVLE--P 94
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIPT-PNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHhqVGMGTMAELATgkP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 95 SSRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGvgpegaflppHQGFHrflgipYSHDqgpcqnltcfppatpcdgscdq 174
Cdd:cd16025 79 GYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG----------PDDYY------STDD---------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 175 glvpipllanlsvvvqppwlpglearYVAFARDLMADAQRQGRPFFLYYASHHTHYP---------QFSGQSFAG----R 241
Cdd:cd16025 121 --------------------------LTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPlqapkewidKYKGKYDAGwdalR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 242 SGR------------------GPFG----DSL-----------ME--------LDAAVGALMTAVGDLGLLGETLVIFAA 280
Cdd:cd16025 175 EERlerqkelglipadtkltpRPPGvpawDSLspeekklearrMEvyaamvehMDQQIGRLIDYLKELGELDNTLIIFLS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 281 DNGPETMRMSRGGCSGLLRCGKGTTFEGGVREPALAFWPGHIAP--GVTHELASSLDLLPTLAALTGAPLPN-------I 351
Cdd:cd16025 255 DNGASAEPGWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkgGIRHQFAHVIDIAPTILELAGVEYPKtvngvpqL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 352 TLDGVDLSPLLLGTGKSPRQTVFFYpanpdEVRGVFAVRSGKYKahfftqgsahsdttadpACHASSPLTAHEPPLLFDL 431
Cdd:cd16025 335 PLDGVSLLPTLDGAAAPSRRRTQYF-----ELFGNRAIRKGGWK-----------------AVALHPPPGWGDQWELYDL 392
|
490
....*....|
gi 545206886 432 SEDPSENYNL 441
Cdd:cd16025 393 AKDPSETHDL 402
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
21-346 |
4.19e-65 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 213.05 E-value: 4.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYpgvlePSSRGGL 100
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY-----VSTPVGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 PLEEVTLAEVLAARGYLTGMAGKWHLGVGPEGAflPPHQGFHRFLGipyshdqgpcqnltcfppatpcdgscdqglvpip 180
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS--PCNLGFDKFFG---------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 181 LLANLSVVVQPPWLPGLEARYVAFARDLMADA----QRQGRPFFLYYASHHTHYP------------QFSGQSFAGRSGR 244
Cdd:pfam00884 120 RNTGSDLYADPPDVPYNCSGGGVSDEALLDEAleflDNNDKPFFLVLHTLGSHGPpyypdrypekyaTFKPSSCSEEQLL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 245 GPFGDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNGPetmrmSRGGCSGLLRCGKG-TTFEGGVREPALAFWPGHIA 323
Cdd:pfam00884 200 NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGE-----SLGEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKA 274
|
330 340
....*....|....*....|....
gi 545206886 324 PG-VTHELASSLDLLPTLAALTGA 346
Cdd:pfam00884 275 KGqKSEALVSHVDLFPTILDLAGI 298
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
20-441 |
1.85e-58 |
|
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: 199.29 E-value: 1.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMG---LYPGVLEPSs 96
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGvtdNNGPLFDAS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 97 rgglpleEVTLAEVLAARGYLTGMAGKWHLGVGPEgaflPPHQGFHRFLGIPyshDQGpcqnlTCFPPatpcdgscdqgl 176
Cdd:cd16031 81 -------QPTYPKLLRKAGYQTAFIGKWHLGSGGD----LPPPGFDYWVSFP---GQG-----SYYDP------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 177 vpiPLLANLSVVVQPPWLPGLearYVAFARDLMaDAQRQGRPFFLYY---ASH--------HTH--------YPQ-FSGQ 236
Cdd:cd16031 130 ---EFIENGKRVGQKGYVTDI---ITDKALDFL-KERDKDKPFCLSLsfkAPHrpftpaprHRGlyedvtipEPEtFDDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 237 SFAGR---------SGRGPFGDS-----------------LMELDAAVGALMTAVGDLGLLGETLVIFAADNGpetmrms 290
Cdd:cd16031 203 DYAGRpewareqrnRIRGVLDGRfdtpekyqrymkdylrtVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 291 rggcsglLRCG------KGTTFEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALTGAPLPNiTLDGVDLSPLLL 363
Cdd:cd16031 276 -------FFLGehglfdKRLMYEESIRVPLIIRDPRLIKAGtVVDALVLNIDFAPTILDLAGVPIPE-DMQGRSLLPLLE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 364 GTGKSPRQTVFFY----PANPDEVRGVFAVRSGKYK-AHFFTQGsahsdttadpachassplTAHEpplLFDLSEDPSEN 438
Cdd:cd16031 348 GEKPVDWRKEFYYeyyeEPNFHNVPTHEGVRTERYKyIYYYGVW------------------DEEE---LYDLKKDPLEL 406
|
...
gi 545206886 439 YNL 441
Cdd:cd16031 407 NNL 409
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-441 |
3.11e-50 |
|
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: 176.60 E-value: 3.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRlpvrmglYP---GVLEPSSR 97
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQ-------YPltnGVFGNDVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 98 ggLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEG-----AFLPPH---QGF---------HRFLGIPYSHDQGPcqnlt 160
Cdd:cd16034 75 --LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNdgradDYTPPPerrHGFdywkgyecnHDHNNPHYYDDDGK----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 161 cfppatpcdgscdqglvpipllanlsVVVQPPWLPGLEARyvaFARDLMADAQRQGRPFFLY---------YAS----HH 227
Cdd:cd16034 148 --------------------------RIYIKGYSPDAETD---LAIEYLENQADKDKPFALVlswnpphdpYTTapeeYL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 228 THYPQ------------FSGQSFAGRSGRGPFGdslM--ELDAAVGALMTAVGDLGLLGETLVIFAADNGpETMrmsrgG 293
Cdd:cd16034 199 DMYDPkklllrpnvpedKKEEAGLREDLRGYYA---MitALDDNIGRLLDALKELGLLENTIVVFTSDHG-DML-----G 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 294 CSGLLRcgKGTTFEGGVREPALAFWPGHI-APGVTHELASSLDLLPTLAALTGAPLPNiTLDGVDLSPLLLG-TGKSPRQ 371
Cdd:cd16034 270 SHGLMN--KQVPYEESIRVPFIIRYPGKIkAGRVVDLLINTVDIMPTLLGLCGLPIPD-TVEGRDLSPLLLGgKDDEPDS 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545206886 372 TVFFYPANPDE-----VRGVFAVRSGKYKahfFTqgsahsdttadpachasspLTAHEPPLLFDLSEDPSENYNL 441
Cdd:cd16034 347 VLLQCFVPFGGgsardGGEWRGVRTDRYT---YV-------------------RDKNGPWLLFDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-435 |
3.28e-47 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 166.56 E-value: 3.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYpgvlepSSRGGL 100
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVW------DNADPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 PLEEVTLAEVLAARGYLTGMAGKWHLgVGPEgaflPPHqGFHrflgipysHDqgpcqnltcfppatpcdgscdqglvpip 180
Cdd:cd16037 75 DGDVPSWGHALRAAGYETVLIGKLHF-RGED----QRH-GFR--------YD---------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 181 llanlsvvvqppwlpgleaRYVA-FARDLMADAQRQGRPFFLYYASHHTHYPQFSGQSF----AGRSGRGPFGdsLME-L 254
Cdd:cd16037 113 -------------------RDVTeAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFydlyVRRARAAYYG--LVEfL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 255 DAAVGALMTAVGDLGLLGETLVIFAADNGpETMrmsrgGCSGLLrcGKGTTFEGGVREPALAFWPGHIAPGVTHELASSL 334
Cdd:cd16037 172 DENIGRVLDALEELGLLDNTLIIYTSDHG-DML-----GERGLW--GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 335 DLLPTLAALTGAPLPNiTLDGVDLSPLLLGTGKSPRqTVFF-YPANPDEVrGVFAVRSGKYKAHFFtqgsahsdttadpa 413
Cdd:cd16037 244 DLAPTILEAAGAPPPP-DLDGRSLLPLAEGPDDPDR-VVFSeYHAHGSPS-GAFMLRKGRWKYIYY-------------- 306
|
410 420
....*....|....*....|..
gi 545206886 414 chasspltAHEPPLLFDLSEDP 435
Cdd:cd16037 307 --------VGYPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-441 |
2.82e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 162.73 E-value: 2.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVS----LCTPSRAALLTGRlpvrmGLYPgvLEPSS 96
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTGR-----TLFH--APEGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 97 RGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEGA-FLPPHQG----FhrFLGIPYS--HD--QGPCQNLTCFPPATp 167
Cdd:cd16155 76 KAAIPSDDKTWPETFKKAGYRTFATGKWHNGFADAAIeFLEEYKDgdkpF--FMYVAFTapHDprQAPPEYLDMYPPET- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 168 cdgscdqglVPIPllanLSVVVQPPWLPGLEA----RYVAFARDLMADAQRQGRpfflYYA--SHhthypqfsgqsfagr 241
Cdd:cd16155 153 ---------IPLP----ENFLPQHPFDNGEGTvrdeQLAPFPRTPEAVRQHLAE----YYAmiTH--------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 242 sgrgpfgdslmeLDAAVGALMTAVGDLGLLGETLVIFAADNGpetmrMSRGGcSGLLrcGKGTTFEGGVREPALAFWPGh 321
Cdd:cd16155 201 ------------LDAQIGRILDALEASGELDNTIIVFTSDHG-----LAVGS-HGLM--GKQNLYEHSMRVPLIISGPG- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 322 IAPG-VTHELASSLDLLPTLAALTGAPLPNiTLDGVDLSPLLLGTGKSPRQTVFFYPANpdevrGVFAVRSGKYKAHFFT 400
Cdd:cd16155 260 IPKGkRRDALVYLQDVFPTLCELAGIEIPE-SVEGKSLLPVIRGEKKAVRDTLYGAYRD-----GQRAIRDDRWKLIIYV 333
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 545206886 401 QGSAHSdttadpachasspltaheppLLFDLSEDPSENYNL 441
Cdd:cd16155 334 PGVKRT--------------------QLFDLKKDPDELNNL 354
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-360 |
1.15e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 157.79 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPGVLEPS-SRGG 99
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGShGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 LPL----EEVTLAEVLAARGYLTGMAGKWHLGvgpegaflpphqgfhrflgipyshDQGpcqnltcfppatpcdgscdqg 175
Cdd:cd16149 81 KPEgyleGQTTLPEVLQDAGYRCGLSGKWHLG------------------------DDA--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 176 lvpipllanlsvvvqppwlpglearyvafARDLMADAQRQgRPFFL---YYASHHTHypqfsgQSFAGRSGrgpfgdslm 252
Cdd:cd16149 116 -----------------------------ADFLRRRAEAE-KPFFLsvnYTAPHSPW------GYFAAVTG--------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 253 eLDAAVGALMTAVGDLGLLGETLVIFAADNGpetMRMsrgGCSGLLRCGKGTT----FEGGVREPALAFWPGHIAPG-VT 327
Cdd:cd16149 151 -VDRNVGRLLDELEELGLTENTLVIFTSDNG---FNM---GHHGIWGKGNGTFplnmYDNSVKVPFIIRWPGVVPAGrVV 223
|
330 340 350
....*....|....*....|....*....|....
gi 545206886 328 HELASSLDLLPTLAALTGAPLP-NITLDGVDLSP 360
Cdd:cd16149 224 DSLVSAYDFFPTLLELAGVDPPaDPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-443 |
4.49e-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: 160.46 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPGVLEPSS-RGG 99
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAySRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 LPLEEVTLAEVLAARGYLTGMAGKWHLGvgpegaflpPHQGfhrflgiPYSHDqgpcqnltcfppatpCDGSCDQGlvpi 179
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVG---------PEET-------PLDYG---------------FDEYLPVE---- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 180 pllanlsvvvqppwlPGLEARYVAFARDLMADAQRQGRPFFLYYASHHTHYPQFSGQSFAG------------------- 240
Cdd:cd16033 126 ---------------TTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDmydpediplpesfaddfed 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 241 -----RSGRGPFGDSLME-----------------LDAAVGALMTAVGDLGLLGETLVIFAADNGpETMrmsrgGCSGLL 298
Cdd:cd16033 191 kpyiyRRERKRWGVDTEDeedwkeiiahywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHG-DAL-----GAHRLW 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 299 RcgKGT-TFEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALTGAPLPNiTLDGVDLSPLLLG-TGKSPRQTVFF 375
Cdd:cd16033 265 D--KGPfMYEETYRIPLIIKWPGVIAAGqVVDEFVSLLDLAPTILDLAGVDVPP-KVDGRSLLPLLRGeQPEDWRDEVVT 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545206886 376 ypanpdEVRGVF------AVRSGKYKAHFftqgsahSDTTADpachasspltahEpplLFDLSEDPSENYNLLE 443
Cdd:cd16033 342 ------EYNGHEfylpqrMVRTDRYKYVF-------NGFDID------------E---LYDLESDPYELNNLID 387
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
21-435 |
6.85e-44 |
|
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: 157.74 E-value: 6.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPGVLEpssrggL 100
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAE------F 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 PLEEVTLAEVLAARGYLTGMAGKWHLgVGPEgaflpPHQGFH-----RFLGIPYSHDqgpcqnltcfppatpcdgscdqg 175
Cdd:cd16032 75 PADIPTFAHYLRAAGYRTALSGKMHF-VGPD-----QLHGFDydeevAFKAVQKLYD----------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 176 lvpipllanlsvvvqppwlpglearyvaFARdlmadaQRQGRPFFLYYASHHTHYPQFSGQSF----AGRSGRGPFGdSL 251
Cdd:cd16032 126 ----------------------------LAR------GEDGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 252 MELDAAVGALMTAVGDLGLLGETLVIFAADNGpeTMRMSRGgcsgllRCGKGTTFEGGVREPALAFWPGHIAPGVTHELA 331
Cdd:cd16032 171 SYVDDKVGQLLDTLERTGLADDTIVIFTSDHG--DMLGERG------LWYKMSFFEGSARVPLIISAPGRFAPRRVAEPV 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 332 SSLDLLPTLAALTGAPLPNIT--LDGVDLSPLLLGTGKSPRQTVFFYPANPDEVRGVFAVRSGKYKahfFTqgsahsdtt 409
Cdd:cd16032 243 SLVDLLPTLVDLAGGGTAPHVppLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVAPCVMIRRGRWK---FI--------- 310
|
410 420
....*....|....*....|....*.
gi 545206886 410 adpACHAsspltahEPPLLFDLSEDP 435
Cdd:cd16032 311 ---YCPG-------DPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
20-456 |
6.23e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 140.06 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYpgvlepssRGG 99
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF--------RNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 LPL--EEVTLAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdgscdqglv 177
Cdd:cd16152 73 IPLpaDEKTLAHYFRDAGYETGYVGKWHL--------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 178 pipllanlsvvvqppwlpgleARYVAfarDLMADA------QRQG-RPFFL---YYASHHT----HY--PQFSGQSFAGR 241
Cdd:cd16152 102 ---------------------AGYRV---DALTDFaidyldNRQKdKPFFLflsYLEPHHQndrdRYvaPEGSAERFANF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 242 S------GRGpfGDSLMEL----------DAAVGALMTAVGDLGLLGETLVIFAADNgpetmrmsrgGCSGLLRCG--KG 303
Cdd:cd16152 158 WvppdlaALP--GDWAEELpdylgccerlDENVGRIRDALKELGLYDNTIIVFTSDH----------GCHFRTRNAeyKR 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 304 TTFEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALTGAPLPNiTLDGVDLSPLLLGTGKSPRQTVFfypANPDEV 383
Cdd:cd16152 226 SCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPE-EMQGRSLLPLVDGKVEDWRNEVF---IQISES 301
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545206886 384 RGVFAVRSGKYKAhfftqgsAHSDTTADPACHASSPltAHEPPLLFDLSEDPSENYNLL-----EGVAKVTSETLQAL 456
Cdd:cd16152 302 QVGRAIRTDRWKY-------SVAAPDKDGWKDSGSD--VYVEDYLYDLEADPYELVNLIgrpeyREVAAELRERLLAR 370
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-360 |
2.59e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 135.75 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPGVLEPssrggl 100
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLEP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 plEEVTLAEVLAARGYLTGMAGkWHLGVGPEGAFlppHQGFHRFLGIPYSHDQGPcqnltcFPPATPCDGSCDQGLvpip 180
Cdd:cd16148 75 --DDPTLAEILRKAGYYTAAVS-SNPHLFGGPGF---DRGFDTFEDFRGQEGDPG------EEGDERAERVTDRAL---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 181 llanlsvvvqpPWLpglearyvafardlmaDAQRQGRPFFL---YYASHHthypqfsgqsfagrsgrgPFG--DSLMELD 255
Cdd:cd16148 139 -----------EWL----------------DRNADDDPFFLflhYFDPHE------------------PYLydAEVRYVD 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 256 AAVGALMTAVGDLGLLGETLVIFAADNGpETMrmsrgGCSGLLRcGKGTTF-EGGVREPALAFWPGHIAPGVTHELASSL 334
Cdd:cd16148 174 EQIGRLLDKLKELGLLEDTLVIVTSDHG-EEF-----GEHGLYW-GHGSNLyDEQLHVPLIIRWPGKEPGKRVDALVSHI 246
|
330 340
....*....|....*....|....*.
gi 545206886 335 DLLPTLAALTGAPlPNITLDGVDLSP 360
Cdd:cd16148 247 DIAPTLLDLLGVE-PPDYSDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
20-441 |
1.61e-34 |
|
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: 134.62 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYgDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPgvLEPSSRGG 99
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYD--NNSYFRKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 LPlEEVTLAEVLAARGYLTGMAGKWHlgvgpegaflppHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGSCDQGLVPi 179
Cdd:cd16030 79 AP-DAVTLPQYFKENGYTTAGVGKIF------------HPGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGG- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 180 pllanlsvVVQPPW--LPGLEARY-----VAFARDLMADAQRQGRPFFL----------YYA------------------ 224
Cdd:cd16030 145 --------GGGPAWeaADVPDEAYpdgkvADEAIEQLRKLKDSDKPFFLavgfykphlpFVApkkyfdlyplesiplpnp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 225 ------------SHHTHYPQFSGQSFAGRSGRGPFGDSL-MEL-----------DAAVGALMTAVGDLGLLGETLVIFAA 280
Cdd:cd16030 217 fdpidlpevawnDLDDLPKYGDIPALNPGDPKGPLPDEQaRELrqayyasvsyvDAQVGRVLDALEELGLADNTIVVLWS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 281 DNGpetmrMSRG--GcsgllRCGKGTTFEGGVREPaLAFW-PGHIAPG-VTHELASSLDLLPTLAALTGAPLPNiTLDGV 356
Cdd:cd16030 297 DHG-----WHLGehG-----HWGKHTLFEEATRVP-LIIRaPGVTKPGkVTDALVELVDIYPTLAELAGLPAPP-CLEGK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 357 DLSPLLLGTGKSPRQTVF-FYPANPdeVRGvFAVRSGKYKahfFTQgsaHSDTTAdpachasspLTAHEpplLFDLSEDP 435
Cdd:cd16030 365 SLVPLLKNPSAKWKDAAFsQYPRPS--IMG-YSIRTERYR---YTE---WVDFDK---------VGAEE---LYDHKNDP 423
|
....*.
gi 545206886 436 SENYNL 441
Cdd:cd16030 424 NEWKNL 429
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
368-501 |
8.31e-33 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 121.27 E-value: 8.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 368 SPRQTVFFYPANPdevrgVFAVRSGKYKAHFFTqGSAHSDTtaDPACHASSP-LTAHEPPLLFDLSEDPSENYNLlegvA 446
Cdd:pfam14707 1 SPHEFLFHYCGAA-----LHAVRWGPYKAHFFT-PSFDPPG--AEGCYGSKVpVTHHDPPLLFDLERDPSEKYPL----S 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 545206886 447 KVTSETLQALKHLQLLKAQFDATMTFSPSQMARGeDPALQICCQPSCTPWPSCCH 501
Cdd:pfam14707 69 PDSPEYPEVLAEIKAAVEEHKATLVPVPNQLSKG-NYLWDPWLQPCCPTFPACTC 122
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
21-343 |
6.52e-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: 119.83 E-value: 6.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDF-YVPVSLCTPSRAALLTGRLPVRMGLY----PGVLEPS 95
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRsVSPPTSSAPNHAALLTGAYPTLHGYTgngsADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 96 SRGGLPLEEVTLAEVLAARGYLTGMAGkwhlgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdgscdqg 175
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 176 lvpipllanlsvvvqppwlpglearyvafARDlMADAQRQGRPFFLYYashhtHYPQFSGQSFAGRSGRGPFGDSLMELD 255
Cdd:cd00016 108 -----------------------------LLK-AIDETSKEKPFVLFL-----HFDGPDGPGHAYGPNTPEYYDAVEEID 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 256 AAVGALMTAVGDLGLLGETLVIFAADNGpetmrMSRGGCSGLLR-CGKGTTFEGGVREPALAFWPGHIAPGVTHELASSL 334
Cdd:cd00016 153 ERIGKVLDALKKAGDADDTVIIVTADHG-----GIDKGHGGDPKaDGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQY 227
|
....*....
gi 545206886 335 DLLPTLAAL 343
Cdd:cd00016 228 DIAPTLADL 236
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-438 |
1.04e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 122.46 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSS--TTPNLDQLAAGGLRFTDFYV-PVslCTPSRAALLTGRLPVRMglypGVLEPSSR 97
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFDNLWAtPA--CSPTRATILTGKYGFRT----GVLAVPDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 98 GGLPLEEVTLAEVLAAR--GYLTGMAGKWHLGVGPEGaflPPHQGfhrflGIPYShdqgpcqnltcfppatpcdgscdQG 175
Cdd:cd16154 75 LLLSEETLLQLLIKDATtaGYSSAVIGKWHLGGNDNS---PNNPG-----GIPYY-----------------------AG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 176 LVP--IPLLANLSVVVQPPWLPGLEARYVAFArDLMAD-AQRQGRPFFLYYA-----------SHHTHYPQFSGQSFAGR 241
Cdd:cd16154 124 ILGggVQDYYNWNLTNNGQTTNSTEYATTKLT-NLAIDwIDQQTKPWFLWLAynaphtpfhlpPAELHSRSLLGDSADIE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 242 SGRGPFGDSLME-LDAAVGALMTAVgDLGLLGETLVIFAADNG-PETMR---MSRGGcsgllrcGKGTTFEGGVREPALA 316
Cdd:cd16154 203 ANPRPYYLAAIEaMDTEIGRLLASI-DEEERENTIIIFIGDNGtPGQVVdlpYTRNH-------AKGSLYEGGINVPLIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 317 FWPGhIAPGVTHE--LASSLDLLPTLAALTGAPLPNITlDGVDLSPLLLGTGKSPRQTVffYPANPDEVRGVFAVRSGKY 394
Cdd:cd16154 275 SGAG-VERANEREsaLVNATDLYATIAELAGVDAAEIH-DSVSFKPLLSDVNASTRQYN--YTEYESPTTTGWATRNQYY 350
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 545206886 395 KAHFFTQGSAHsdttadpachasspltahepplLFDLSEDPSEN 438
Cdd:cd16154 351 KLIESENGQEE----------------------LYDLINDPSEQ 372
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
20-355 |
1.40e-30 |
|
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: 122.66 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYgDLGSYGHPSSTTpnlDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLP----VRMGLYPGvleps 95
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPKTK---KLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPG----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 96 srGGLP------LEEVTLAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGI--PYSHDQ-GPCQNLTCFPPAT 166
Cdd:cd16147 72 --GGYPkfwqngLERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPPGWDEWDGLvgNSTYYNyTLSNGGNGKHGVS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 167 -PCDGSCDqglvpipLLANLSVvvqppwlpglearyvafarDLMADAQRQGRPFFLYYASH--HTHY---PQFSGqSFAG 240
Cdd:cd16147 150 yPGDYLTD-------VIANKAL-------------------DFLRRAAADDKPFFLVVAPPapHGPFtpaPRYAN-LFPN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 241 --RSGRGPFGD---------------------------------SLMELDAAVGALMTAVGDLGLLGETLVIFAADNGPE 285
Cdd:cd16147 203 vtAPPRPPPNNpdvsdkphwlrrlpplnptqiayidelyrkrlrTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYH 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 286 TmrmsrgGCSGLLRcGKGTTFEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALTGAPLPNiTLDG 355
Cdd:cd16147 283 L------GQHRLPP-GKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPS-DMDG 344
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
21-441 |
1.62e-29 |
|
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: 120.44 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGlypgvlepSSRGGL 100
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHR--------SVWNGT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 101 PL--EEVTLAEVLAARGYLTGMAGKWHLGVGPEG---------AFLPPHQGFH---RFLGIPYSHdqGPCQNLTcfppat 166
Cdd:cd16028 73 PLdaRHLTLALELRKAGYDPALFGYTDTSPDPRGlapldprllSYELAMPGFDpvdRLDEYPAED--SDTAFLT------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 167 pcDGSCD--QGLVPIPLLANLSVV-VQPPWLpgLEARYVAFAR-DLMADAQRQGRPFFL-----YYASHHTHYPQ--FSG 235
Cdd:cd16028 145 --DRAIEylDERQDEPWFLHLSYIrPHPPFV--APAPYHALYDpADVPPPIRAESLAAEaaqhpLLAAFLERIESlsFSP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 236 QSFAGRSGRGPFGDSLM--------ELDAAVGALMTAVGDLGLLGETLVIFAADNGpETMrmsrgGCSGLLrcGKGTTFE 307
Cdd:cd16028 221 GAANAADLDDEEVAQMRatylgliaEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG-EQL-----GDHWLW--GKDGFFD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 308 GGVREPALAFWPG----HIAPGVTHELASSLDLLPTLAALTGAPLPNItLDGVDLSPLLLGTGKSPRQTVFFY------- 376
Cdd:cd16028 293 QAYRVPLIVRDPRreadATRGQVVDAFTESVDVMPTILDWLGGEIPHQ-CDGRSLLPLLAGAQPSDWRDAVHYeydfrdv 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545206886 377 -PANPDEVRG-------VFAVRSGKYK-AHFftqgsahsdttadpachassplTAHePPLLFDLSEDPSENYNL 441
Cdd:cd16028 372 sTRRPQEALGlspdecsLAVIRDERWKyVHF----------------------AAL-PPLLFDLKNDPGELRDL 422
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
21-460 |
4.37e-29 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 119.77 E-value: 4.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLgYGD-LGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGL--YpgvlepsSR 97
Cdd:PRK13759 7 PNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRvgY-------GD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 98 GGLPLEEVTLAEVLAARGYLTGMAGKWHlgVGPEGAFLpphqGFHRFL---GIPYS-------------------HDQGP 155
Cdd:PRK13759 79 VVPWNYKNTLPQEFRDAGYYTQCIGKMH--VFPQRNLL----GFHNVLlhdGYLHSgrnedksqfdfvsdylawlREKAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 156 CQNLTCFppatpcdgscDQGLvpipllaNLSVVVQPPWlpGLEARY------VAFARDLMADAQRqGRPFFLY--YASHH 227
Cdd:PRK13759 153 GKDPDLT----------DIGW-------DCNSWVARPW--DLEERLhptnwvGSESIEFLRRRDP-TKPFFLKmsFARPH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 228 THY--PQFS-------------------------------------GQSFAGRSGRGPFGdSLMELDAAVGALMTAVGDL 268
Cdd:PRK13759 213 SPYdpPKRYfdmykdadipdphigdweyaedqdpeggsidalrgnlGEEYARRARAAYYG-LITHIDHQIGRFLQALKEF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 269 GLLGETLVIFAADNGpETMrmsrgGCSGLLRcgKGTTFEGGVREPALAFWPGHIAPG----VTHELASSLDLLPTLAALT 344
Cdd:PRK13759 292 GLLDNTIILFVSDHG-DML-----GDHYLFR--KGYPYEGSAHIPFIIYDPGGLLAGnrgtVIDQVVELRDIMPTLLDLA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 345 GAPLPNiTLDGVDLSPLLLGTGKSPR-----QTVFFYPANPdevrgvfAVRSGKYKAHFFTQgsahsdttadpachassp 419
Cdd:PRK13759 364 GGTIPD-DVDGRSLKNLIFGQYEGWRpylhgEHALGYSSDN-------YLTDGKWKYIWFSQ------------------ 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 545206886 420 lTAHEPplLFDLSEDPSENYNLL--EGVAKVTSETLQAL-KHLQ 460
Cdd:PRK13759 418 -TGEEQ--LFDLKKDPHELHNLSpsEKYQPRLREMRKKLvDHLR 458
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-376 |
1.12e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 109.99 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTgrlpvrmGLYP---GVLE---P 94
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYT-------GLHPqqtGVTDtlgS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 95 SSRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEGAflpphqgfhrflgipYSHDqgpcqnltcfppatpcdgscdq 174
Cdd:cd16035 74 PMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHLSGAAGGG---------------YKRD---------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 175 glvpipllanlsvvvqppwlPGLEARYVAFARDLMADAQrQGRPFFLyYAS----HHTHY-PQFSGQSfagRSGRGPFGD 249
Cdd:cd16035 117 --------------------PGIAAQAVEWLRERGAKNA-DGKPWFL-VVSlvnpHDIMFpPDDEERW---RRFRNFYYN 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 250 SLMELDAAVGALMTAVGDLGLLGETLVIFAADNGpetmrmSRGGCSGLLRCGkGTTFEGGVREPAL----AFWPGhiaPG 325
Cdd:cd16035 172 LIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG------EMGGAHGLRGKG-FNAYEEALHVPLIishpDLFGT---GQ 241
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 545206886 326 VTHELASSLDLLPTLAALTGAPLPNI-----TLDGVDLSPLLLGTGKSPRQ--TVFFY 376
Cdd:cd16035 242 TTDALTSHIDLLPTLLGLAGVDAEARateapPLPGRDLSPLLTDADADAVRdgILFTY 299
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-358 |
1.30e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 103.22 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSST----------TPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYP- 89
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAHTGksesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 90 GVLEPSSRGGLPleevTLAEVLAARGYLTGMAGKWHlgvgpegaflppHQGFHRFLGIPYSHDQGPcqnltcfppatpcD 169
Cdd:cd16153 82 EAAHPALDHGLP----TFPEVLKKAGYQTASFGKSH------------LEAFQRYLKNANQSYKSF-------------W 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 170 GSCDQGLVPI-PLLANLSvVVQP--PWLPGLEARyvafardlmadaQRqgrpfFLYYAshhthypqfsgqsFAGrsgrgp 246
Cdd:cd16153 133 GKIAKGADSDkPFFVRLS-FLQPhtPVLPPKEFR------------DR-----FDYYA-------------FCA------ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 247 FGDSLmeldaaVGALMTAVGDLGLLGE---TLVIFAADNGpetmrmSRGGCSGLLrcGKGTTFEGGVREPALAFWPGHI- 322
Cdd:cd16153 176 YGDAQ------VGRAVEAFKAYSLKQDrdyTIVYVTGDHG------WHLGEQGIL--AKFTFWPQSHRVPLIVVSSDKLk 241
|
330 340 350
....*....|....*....|....*....|....*....
gi 545206886 323 --APGVTHELASSLDLLPTLAALTGAPLPNIT-LDGVDL 358
Cdd:cd16153 242 apAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDyLDGRDL 280
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-441 |
2.44e-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: 105.01 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRlpvrmglYPGVlepssRGG- 99
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGW-------YPHV-----NGHr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 100 -----LPLEEVTLAEVLAARGYLTGMAGKWHLGVGP--------------EGA--FL---PPHQGFHRFLGIPYSHdqgp 155
Cdd:cd16150 69 tlhhlLRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEfaaeaycdsdeacvRTAidWLrnrRPDKPFCLYLPLIFPH---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 156 cqnltcfPPAT---PCDGSCDQGLVPipllanlsvvvqPPWLPGLEARYvafARDLMADAQRQGrpffLYYAS------- 225
Cdd:cd16150 145 -------PPYGveePWFSMIDREKLP------------PRRPPGLRAKG---KPSMLEGIEKQG----LDRWSeerwrel 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 226 HHTHYPQFSgqsfagrsgrgpfgdslmELDAAVGALMTAVGDLGLLGETLVIFAADNGPETmrmsrgGCSGLLRCGKGTT 305
Cdd:cd16150 199 RATYLGMVS------------------RLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT------GDYGLVEKWPNTF 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 306 FEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALTGAPlPNITLDGVDLSPLLLGTGKSPRQTVF----FYPANPD 381
Cdd:cd16150 255 EDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIP-LSHTHFGRSLLPVLAGETEEHRDAVFseggRLHGEEQ 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545206886 382 evrgvfAVRSGKYKAHFFT-QGSAHSDTTADPACHASSPLTA------HEPPLLFDLSEDPSENYNL 441
Cdd:cd16150 334 ------AMEGGHGPYDLKWpRLLQQEEPPEHTKAVMIRTRRYkyvyrlYEPDELYDLEADPLELHNL 394
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
21-436 |
2.13e-16 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 80.66 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGyGDLgsYGHPSSTT---PNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGrlpvrmgLYPGVLEP-SS 96
Cdd:cd16171 1 PNVVMVMSDSFD-GRL--TFRPGNQVvdlPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG-------LFTHLTESwNN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 97 RGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPegaflppHQGFHRFLG----IPYSHDQG--PCQNLTcfppatpcdG 170
Cdd:cd16171 71 YKGLDPNYPTWMDRLEKHGYHTQKYGKLDYTSGH-------HSVSNRVEAwtrdVPFLLRQEgrPTVNLV---------G 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 171 SCDQGLVPIPLLANLSVVVQppWLpglearyvafardlMADAQRQGRPFFLYYASHHTH-YP-QFSGQSFAG-RSGRGPF 247
Cdd:cd16171 135 DRSTVRVMLKDWQNTDKAVH--WI--------------RKEAPNLTQPFALYLGLNLPHpYPsPSMGENFGSiRNIRAFY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 248 GDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNGPETMRMSrggcsgllRCGKGTTFEGGVREPALAFWPGhIAPGVT 327
Cdd:cd16171 199 YAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHR--------QFYKMSMYEGSSHVPLLIMGPG-IKAGQQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 328 HELASSL-DLLPTLAALTGAPLPNiTLDGVDLSPLLLGTGKSPRQTVFFYPA-NPDEVRG------VFAVRSGKYKAHFF 399
Cdd:cd16171 270 VSDVVSLvDIYPTMLDIAGVPQPQ-NLSGYSLLPLLSESSIKESPSRVPHPDwVLSEFHGcnvnasTYMLRTNSWKYIAY 348
|
410 420 430
....*....|....*....|....*....|....*..
gi 545206886 400 TQGsahsdttadpachasspltAHEPPLLFDLSEDPS 436
Cdd:cd16171 349 ADG-------------------NSVPPQLFDLSKDPD 366
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
21-132 |
5.44e-16 |
|
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: 80.12 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTgrlpvrmGLYpgvlePSSRGG- 99
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFT-------GLY-----PHTNGSw 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 545206886 100 ---LPLEE--VTLAEVLAARGYLTGMAGKWHL--------GVGPEG 132
Cdd:cd16156 69 tncMALGDnvKTIGQRLSDNGIHTAYIGKWHLdggdyfgnGICPQG 114
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
19-358 |
9.05e-16 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 80.08 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 19 NPPNILLI----FADDLgygdLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPV--SlctpSRA--ALLTGRLPVRMGlypG 90
Cdd:COG1368 233 KKPNVVVIllesFSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGgrT----SRGefAVLTGLPPLPGG---S 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 91 VLEPSSRGGLPleevTLAEVLAARGYLT-----GMAGKWHLgvgpeGAFLpPHQGFHRFLGIPYshdqgpcqnltcFPPa 165
Cdd:COG1368 302 PYKRPGQNNFP----SLPSILKKQGYETsffhgGDGSFWNR-----DSFY-KNLGFDEFYDRED------------FDD- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 166 tPCDGS---CDQglvpipllanlsvvvqppwlpglearyvAFARDLMADAQRQGRPFFLYY--ASHHTHYPQFSGQSFAG 240
Cdd:COG1368 359 -PFDGGwgvSDE----------------------------DLFDKALEELEKLKKPFFAFLitLSNHGPYTLPEEDKKIP 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 241 RSGRGPFGD---SLMELDAAVGALMTAVGDLGLLGETLVIFAADNGPetmrMSRGGCSGLLRCGKGTTfeggvrePALaF 317
Cdd:COG1368 410 DYGKTTLNNylnAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP----RSPGKTDYENPLERYRV-------PLL-I 477
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 545206886 318 W-PGHIAPGVTHELASSLDLLPTLAALTGAPLPNITLDGVDL 358
Cdd:COG1368 478 YsPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDL 519
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
21-345 |
2.51e-12 |
|
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: 67.32 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 21 PNILLI----FADDLGYGDLGSYGHpsstTPNLDQLAAGGLRFTDFYVPVSLCTPSRA--ALLTGRLPVRMGlyPGVLEP 94
Cdd:cd16015 1 PNVIVIllesFSDPYIDKDVGGEDL----TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLG--SGSYTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 95 SSRGGLPleevTLAEVLAARGYLT-----GMAGKWHLgvgpeGAFLpPHQGFHRFLGIPYshdqgpcqnltcFPPATPCD 169
Cdd:cd16015 75 YKLNPLP----SLPSILKEQGYETifihgGDASFYNR-----DSVY-PNLGFDEFYDLED------------FPDDEKET 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 170 GS---CDQGLvpipllanlsvvvqppwlpglearyVAFARDLMADAQRQgrPFFLY---YASHH-----THYPQFSGQSF 238
Cdd:cd16015 133 NGwgvSDESL-------------------------FDQALEELEELKKK--PFFIFlvtMSNHGpydlpEEKKDEPLKVE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 239 AGRSGRGPFGDSLMELDAAVGALMTAVGDLGLLGETLVIFAADNGPetMRMSRGGCSGLLRCGKGTTfeggvrePALAFW 318
Cdd:cd16015 186 EDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLP--SLGSDYDETDEDPLDLYRT-------PLLIYS 256
|
330 340
....*....|....*....|....*..
gi 545206886 319 PGHIAPGVTHELASSLDLLPTLAALTG 345
Cdd:cd16015 257 PGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
20-283 |
1.28e-06 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 50.52 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 20 PPNILLIFADDLGYGDLGSYghpssTTPNLDQLAAGGLRFTDFYVPV-SLCTPSRAALLTGRLPVRMGL---------YP 89
Cdd:COG1524 23 AKKVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIvgngwydpeLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 90 GVLEPSSRGGLP------LEEVTLAEVLAARGYLTGMAGKWHLGVGP--EGAFLPPHQGFHRFLGIPYShdqgpcqnltc 161
Cdd:COG1524 98 RVVNSLSWVEDGfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGliDAARPYPYDGRKPLLGNPAA----------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 162 fppatpcdgscdqglvpipllanlsvvvqppwlpglEARYVAFARDLMadaqRQGRPFFLY-------YASHHThypqfs 234
Cdd:COG1524 167 ------------------------------------DRWIAAAALELL----REGRPDLLLvylpdldYAGHRY------ 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 545206886 235 gqsfagrsgrGPFG----DSLMELDAAVGALMTAVGDLGLLGETLVIFAADNG 283
Cdd:COG1524 201 ----------GPDSpeyrAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
187-283 |
4.35e-03 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 39.11 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545206886 187 VVVQPPWLPGLEARYVAFARDLMADAQRQGRPFFLYYashHTHYPQFSGQSFagrsgrGPFG----DSLMELDAAVGALM 262
Cdd:cd16018 126 IPLGGYWQPYNDSFPFEERVDTILEWLDLERPDLILL---YFEEPDSAGHKY------GPDSpevnEALKRVDRRLGYLI 196
|
90 100
....*....|....*....|.
gi 545206886 263 TAVGDLGLLGETLVIFAADNG 283
Cdd:cd16018 197 EALKERGLLDDTNIIVVSDHG 217
|
|
| |
