|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
1-457 |
0e+00 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 600.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 1 MVSSVGYRVLQWTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAH 80
Cdd:cd16159 68 MASSHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 81 weLSEKRVDLEQKLNFLFQVLALVTLTLAAGKFMHLISISWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTI 158
Cdd:cd16159 148 --GSNGEYDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 159 TEQPMRFQRVTPLILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEG 238
Cdd:cd16159 224 VEQPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 239 LTNSTLIYFASDHGGSLENQFANSQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQL 318
Cdd:cd16159 304 LKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAAL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 319 AGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTLWKVHFVTPVFQPEGAGaCYGRKVCPCS 398
Cdd:cd16159 384 AGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCF 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1864524957 399 GEKVVHHDPPLLFDLSRDPSEAHVLTPASEPlFYHVMERVQQAVWEHQQTLSPVALQLD 457
Cdd:cd16159 463 GDSVTHHDPPLLFDLSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
7-424 |
3.63e-105 |
|
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: 319.12 E-value: 3.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 7 YRVLQWTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagDH-CHHPLHHGFDYFYGMPLSMTGDCAHWELSE 85
Cdd:cd16026 69 PGVVGPPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRND 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 86 KRVDLeqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadCFLMRNHTITEQPMRF 165
Cdd:cd16026 142 PPGPL-----------------------------------------------------------PPLMENEEVIEQPADQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 166 QRVTPLILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLI 245
Cdd:cd16026 163 SSLTQRYTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 246 YFASDHGGSLENQFAN-----------SQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFP 313
Cdd:cd16026 243 IFTSDNGPWLEYGGHGgsagplrggkgTTWeGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 314 TVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGacygrk 393
Cdd:cd16026 306 TLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG------ 373
|
410 420 430
....*....|....*....|....*....|.
gi 1864524957 394 vcpcsGEKVVHHDPPLLFDLSRDPSEAHVLT 424
Cdd:cd16026 374 -----GLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
10-442 |
1.51e-94 |
|
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: 293.57 E-value: 1.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 10 LQWTgaSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDyFYGMPLSMTGdcaHWELSekrvd 89
Cdd:cd16160 76 LPWD--IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGTNLPFTN---SWACD----- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 90 leqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllTTSYFagalIVHAD---CFLMRNHTITEQPMRFQ 166
Cdd:cd16160 145 ----------------------------------------------DTGRH----VDFPDrsaCFLYYNDTIVEQPIQHE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 167 RVTPLILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIY 246
Cdd:cd16160 175 HLTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 247 FASDHG------------GSLENQFANSQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPT 314
Cdd:cd16160 255 FLSDHGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 315 VVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtlWKVHFVT---PVFQPEGAGACYG 391
Cdd:cd16160 317 FVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1864524957 392 RKVCP------CSGEKVVHHDPPLLFDLSRDPSEAHVLTPAsepLFYHVMERVQQAV 442
Cdd:cd16160 390 GPLSDyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPS---VYEHMLEAVEKLI 443
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
14-479 |
3.08e-61 |
|
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: 207.68 E-value: 3.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 14 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAgdhcHHPLHHGFDYFYGMPLSMT-GDCAHwelsekrvdleq 92
Cdd:cd16158 76 GSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHDqGPCQN------------ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 93 klnflfqvlalvtltlaagkfmhlisiswmpviwsalLAVFLLTTSYFAGALIVHADCFLMRNHTITEQPMRFQRVTPLI 172
Cdd:cd16158 140 -------------------------------------LTCFPPNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 173 LQEVKSFL----KRNKlgPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFA 248
Cdd:cd16158 183 AKFAKDFIadnaKEGK--PFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 249 SDHGGSLENQfansQYGGwNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVQLAGGEVPqDRV 328
Cdd:cd16158 261 SDNGPSTMRK----SRGG-NAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 329 IDGRDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdrgtlWKVHFVT---PVFQPEGAGACYGRKvcpcsgeK 401
Cdd:cd16158 334 LDGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCHPSA-------E 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 402 VVHHDPPLLFDLSRDPSEAHVLTPASEplFYHVMERVQQAVWEHQQTLSPVALQLDSLGNlwrPWLQPC----CGPFPLC 477
Cdd:cd16158 401 LTSHDPPLLFDLSQDPSENYNLLGLPE--YNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPCckpgCTPKPSC 475
|
..
gi 1864524957 478 WC 479
Cdd:cd16158 476 CQ 477
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
15-424 |
1.72e-60 |
|
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: 203.08 E-value: 1.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 15 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGdcahwELSEKRVDleqkl 94
Cdd:cd16161 77 SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFSHDS-----SLADRYAQ----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 95 nflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyFAGAlivhadcFLMRNHTITEqpmrfqrvtplilq 174
Cdd:cd16161 141 ---------------------------------------------FATD-------FIQRASAKDR-------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 175 evksflkrnklgPFLLLVSFLHVHIPLITTKNFLGKSAH-GLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG- 252
Cdd:cd16161 155 ------------PFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGp 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 253 --------GSLENQFANSQyGGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVP 324
Cdd:cd16161 223 wevkcelaVGPGTGDWQGN-LGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 325 QDRVIDGRDLLPLLLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtlWKVHFVTpvfqpEGAGACYGRKvCPcsg 399
Cdd:cd16161 297 PGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALACCGST-GP--- 360
|
410 420
....*....|....*....|....*
gi 1864524957 400 ekVVHHDPPLLFDLSRDPSEAHVLT 424
Cdd:cd16161 361 --KLYHDPPLLFDLEVDPAESFPLT 383
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
345-479 |
1.15e-56 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 184.05 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 345 SDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGACYGRKVCpcsgekVVHHDPPLLFDLSRDPSEAHVLT 424
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1864524957 425 PASePLFYHVMERVQQAVWEHQQTLSPVALQLDSLGNLWRPWLQPCCGPFPLCWC 479
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
11-419 |
1.78e-56 |
|
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: 191.98 E-value: 1.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 11 QWTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncESAGdhcHHPLHHGFDYFYGMPLsmtgdcahwelsekrvdl 90
Cdd:cd16142 73 GLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDG---RLPTDHGFDEFYGNLY------------------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 91 eqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnHTITEQpmrfqrvtp 170
Cdd:cd16142 129 -----------------------------------------------------------------HTIDEE--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 171 lILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGKS-AHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYF 247
Cdd:cd16142 135 -IVDKAIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSsGKGKYADSMVELDDHVGQILDALDELGIADNTIVIF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 248 ASDHGGSLeNQFANSQY------------GGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTV 315
Cdd:cd16142 214 TTDNGPEQ-DVWPDGGYtpfrgekgttweGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 316 VQLAGGEVP------QDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVtpVFQPEGAGAC 389
Cdd:cd16142 276 AALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTG 347
|
410 420 430
....*....|....*....|....*....|
gi 1864524957 390 YGRKVCPCsgekvvhhdpPLLFDLSRDPSE 419
Cdd:cd16142 348 EPFYVLTF----------PLIFNLRRDPKE 367
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
17-457 |
1.03e-54 |
|
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: 189.99 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 17 GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsagdhcHHPLHHGFDYFYGMPlsmtgDCaHWelseKRVDLEQKLNf 96
Cdd:cd16157 86 GGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NC-HF----GPYDNKAYPN- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 97 lfqvLALVTLTLAAGKFMHLISIswmpviwsallavfllttsyfagalivhadcflmrNHTITEQpmrfqRVTPLILQEV 176
Cdd:cd16157 149 ----IPVYRDWEMIGRYYEEFKI-----------------------------------DKKTGES-----NLTQIYLQEA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 177 KSFLKR--NKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGS 254
Cdd:cd16157 185 LEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 255 LenqFANSQYGGWNGIYKGGKGMGGWEGgIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDL 334
Cdd:cd16157 265 L---ISAPEQGGSNGPFLCGKQTTFEGG-MREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 335 LPLLLgtAQHSDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVT----PVFQPEGAGACYGRKVCPCSGEKVVHH-DPPL 409
Cdd:cd16157 341 LPVLL--NGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQTDHtKLPL 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1864524957 410 LFDLSRDPSEAHVLTPASePLFYHVMERVQQAVWEHQQTLSPVALQLD 457
Cdd:cd16157 413 LFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
18-421 |
3.30e-51 |
|
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: 179.28 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 18 GLPTNETTFAKILKEKGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGmplsmtGDCAHwelsekrvdleqklnfl 97
Cdd:cd16144 91 RLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG------GTGNG----------------- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 98 fqvlalvtltlaAGKfmhlisiswmpviwsallavfllttSYFAGALIVHADCFLmrnhtITEQPMRFQRVTplilQEVK 177
Cdd:cd16144 142 ------------GPP-------------------------SYYFPPGKPNPDLED-----GPEGEYLTDRLT----DEAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 178 SFLKRNKLGPFLLLVSFLHVHIPLITTK----NFLGKSAHGLYGDN-------VEEMDWMVGQILDALDTEGLTNSTLIY 246
Cdd:cd16144 176 DFIEQNKDKPFFLYLSHYAVHTPIQARPelieKYEKKKKGLRKGQKnpvyaamIESLDESVGRILDALEELGLADNTLVI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 247 FASDHGG-SLENQFANSQY-----------GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPT 314
Cdd:cd16144 256 FTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRWPGVIKPGSVSDVPVIGTDLYPT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 315 VVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMhycerflhaarWHQrdrgtlwkvhfvtPVFQPEGAGacygrkv 394
Cdd:cd16144 319 FLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALF-----------WHF-------------PHYHGQGGR------- 367
|
410 420 430
....*....|....*....|....*....|....*
gi 1864524957 395 cPCS----GE-KVVHH---DPPLLFDLSRDPSEAH 421
Cdd:cd16144 368 -PASairkGDwKLIEFyedGRVELYNLKNDIGETN 401
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-421 |
1.60e-50 |
|
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: 177.01 E-value: 1.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 7 YRVLQWTGASGG-----LPTNETTFAKILKEKGYATGLIGKWHLGLN-CESAGDHCHH---------------PLHHGFD 65
Cdd:cd16143 64 WRSRLKGGVLGGfspplIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwKKKDGKKAATgtgkdvdyskpikggPLDHGFD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 66 YFYGMPLSmtgdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagali 145
Cdd:cd16143 144 YYFGIPAS------------------------------------------------------------------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 146 vhadcflmrnhtiteqpmrfqRVTPLILQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEM 223
Cdd:cd16143 152 ---------------------EVLPTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYEL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 224 DWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQF---------ANSQY---------GGwngiykggkgmggweggIR 285
Cdd:cd16143 211 DWVVGRILDALKELGLAENTLVIFTSDNGPSPYADYkelekfghdPSGPLrgmkadiyeGG-----------------HR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 286 VPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHycerflHAARWHQ 365
Cdd:cd16143 274 VPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSF 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1864524957 366 RDRGTLWKVhfvtpVFQPEGAGACYGRKvcpcsgeKVVHHDPP-LLFDLSRDPSEAH 421
Cdd:cd16143 348 AIRKGDWKL-----IDGTGSGGFSYPRG-------KEKLGLPPgQLYNLSTDPGESN 392
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
13-421 |
2.17e-47 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 168.52 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 13 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleq 92
Cdd:COG3119 95 EGYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL--------------------------------------------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 93 klnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvTPLI 172
Cdd:COG3119 130 ----------------------------------------------------------------------------TDLL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 173 LQEVKSFLKRNKLG--PFLLLVSFLHVHIPLITTKNFLGK-----------------------SAHGLYGDNVEEMDWMV 227
Cdd:COG3119 134 TDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 228 GQILDALDTEGLTNSTLIYFASDHGGSLENQ-FA---NSQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVI 302
Cdd:COG3119 214 GRLLDALEELGLADNTIVVFTSDNGPSLGEHgLRggkGTLYeGG-----------------IRVPLIVRWPGKIKAGSVS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 303 GEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRdrgtlWKVHFvtpvfq 382
Cdd:COG3119 277 DALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKLIR------ 343
|
410 420 430
....*....|....*....|....*....|....*....
gi 1864524957 383 pegagaCYGRKvcpcsgekvvhhDPPLLFDLSRDPSEAH 421
Cdd:COG3119 344 ------YYDDD------------GPWELYDLKNDPGETN 364
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
19-421 |
4.85e-40 |
|
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: 149.28 E-value: 4.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 19 LPTNETTFAKILKEKGYATGLIGKWHLGLNcESAGdhchHPLHHGFDYFYGmplsmtgdcahwelsekrvdleqklnFLF 98
Cdd:cd16145 79 LPPDDVTLAEVLKKAGYATAAFGKWGLGGP-GTPG----HPTKQGFDYFYG--------------------------YLD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 99 QVLAlvtltlaagkfmHlisiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-------EQPMRFQRVTPL 171
Cdd:cd16145 128 QVHA------------H----------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTYSHDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 172 ILQEVKSFLKRNKLGPFLLLVSFLHVHIPLITTK---NFLGKSAHGLYGDN------------VEEMDWMVGQILDALDT 236
Cdd:cd16145 174 FTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDdgpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILALLKE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 237 EGLTNSTLIYFASDHGGSLE------NQFANSQ----------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLPAG 299
Cdd:cd16145 254 LGIDENTLVVFTSDNGPHSEggsehdPDFFDSNgplrgykrslYeGG-----------------IRVPFIARWPGKIPAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 300 RVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdrgtlWKVh 375
Cdd:cd16145 317 SVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG------WKA- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1864524957 376 fvtpVFQPEGAGacygrkvcpcsgekvvhhdPPLLFDLSRDPSEAH 421
Cdd:cd16145 386 ----VRHGKKDG-------------------PFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-363 |
1.31e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 138.89 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 17 GGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESAGDHchhPLHHGFDYFygmplsmtgdCAhWELSEKRVDLEQKLNF 96
Cdd:cd16151 69 GYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGDY---PHEFGFDEY----------CL-WQLTETGEKYSRPATP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 97 LFQVLALVTLTLAAGKFMhlisiswmPVIWSAllavfllttsyfagalivhadcFLMRnhtiteqpmrfqrvtplilqev 176
Cdd:cd16151 134 TFNIRNGKLLETTEGDYG--------PDLFAD----------------------FLID---------------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 177 ksFLKRNKLGPFLLLVSFLHVHIPLITT----------KNFLGKSAHglYGDNVEEMDWMVGQILDALDTEGLTNSTLIY 246
Cdd:cd16151 162 --FIERNKDQPFFAYYPMVLVHDPFVPTpdspdwdpddKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTIII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 247 FASDHGGSLE-NQFANSQY--GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEV 323
Cdd:cd16151 238 FTGDNGTHRPiTSRTNGREvrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1864524957 324 PQDRVIDGRDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 363
Cdd:cd16151 309 PEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
22-421 |
6.15e-34 |
|
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: 132.29 E-value: 6.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 22 NETTFAKILKEKGYATGLIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEkrvdleqklnflfqvl 101
Cdd:cd16146 79 DETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND---------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 102 alvtltlaagkfmhlisiswmpviwsallavfllttsYFagalivhaDCFLMRNHTITeqpmRFQR-VTPLILQEVKSFL 180
Cdd:cd16146 137 -------------------------------------YF--------DDTYYHNGKFV----KTEGyCTDVFFDEAIDFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 181 KRNKLGPFLLLVSFLHVHIPLITTKNF--------LGKSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 252
Cdd:cd16146 168 EENKDKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 253 --GSLENQF-AN------SQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGE 322
Cdd:cd16146 247 paGGVPKRFnAGmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 323 VPQDRVIDGRDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTLWKVHFVtpVFQPEgagacYgRKVCPcsgekv 402
Cdd:cd16146 310 LPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W-RLVSP------ 366
|
410
....*....|....*....
gi 1864524957 403 vHHDPPLLFDLSRDPSEAH 421
Cdd:cd16146 367 -KGFQPELYDIENDPGEEN 384
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
174-333 |
7.33e-33 |
|
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: 124.86 E-value: 7.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 174 QEVKSFLKRN-KLGPFLLLVSFLHVHIPLIttknflgksahglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 252
Cdd:cd16022 103 DEAIDFIERRdKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 253 GSLENQfaNSQYGGWNGIYKGgkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGR 332
Cdd:cd16022 170 DMLGDH--GLRGKKGSLYEGG----------IRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGR 235
|
.
gi 1864524957 333 D 333
Cdd:cd16022 236 S 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
19-421 |
5.26e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 126.53 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 19 LPTNETTFAKILKEKGYATGLIGKWHLGLNCESAGDHCHH----PLHHGFDYFYGMplsmtgDCAH-------WELSEKR 87
Cdd:cd16034 75 LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------ECNHdhnnphyYDDDGKR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 88 VDLEQklnflfqvlalvtltlaagkfmhlisisWMPvIWSALLAVfllttSYfagalivhadcflMRNHTITEQP----- 162
Cdd:cd16034 149 IYIKG----------------------------YSP-DAETDLAI-----EY-------------LENQADKDKPfalvl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 163 ------MRFQRVtPlilQEVKSFLKRNKLgpflllvsFLHVHIPLIT-TKNFLGKSAHGLYGdNVEEMDWMVGQILDALD 235
Cdd:cd16034 182 swnpphDPYTTA-P---EEYLDMYDPKKL--------LLRPNVPEDKkEEAGLREDLRGYYA-MITALDDNIGRLLDALK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 236 TEGLTNSTLIYFASDHG---GSLENQFANSQYGGwngiykggkgmggwegGIRVPGIFRWPGVLPAGRVIGEPTSLMDVF 312
Cdd:cd16034 249 ELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYPGKIKAGRVVDLLINTVDIM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 313 PTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTL----WKvhFVtpvfqpegaga 388
Cdd:cd16034 313 PTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtdrYT--YV----------- 377
|
410 420 430
....*....|....*....|....*....|...
gi 1864524957 389 cygrkvcpcsgekVVHHDPPLLFDLSRDPSEAH 421
Cdd:cd16034 378 -------------RDKNGPWLLFDNEKDPYQLN 397
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
156-417 |
6.42e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 118.80 E-value: 6.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 156 HTITEQPMRFQRVTPLILQEVKSFLKRNKL--GPFLLLVSFLHVHIPLITTKNFLGKSAHGL---YGDNVEEMDWMVGQI 230
Cdd:cd16037 99 HFRGEDQRHGFRYDRDVTEAAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 231 LDALDTEGLTNSTLIYFASDHGgslENQFANSQYGgwngiykggkGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMD 310
Cdd:cd16037 179 LDALEELGLLDNTLIIYTSDHG---DMLGERGLWG----------KSTMYEESVRVPMIISGPGI-PAGKRVKTPVSLVD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 311 VFPTVVQLAGGEVPQDRviDGRDLLPLLLGTAQHSDHEFlmhyCErfLHAA---------RWHQrdrgtlWK-VHFVtpv 380
Cdd:cd16037 245 LAPTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVF----SE--YHAHgspsgafmlRKGR------WKyIYYV--- 307
|
250 260 270
....*....|....*....|....*....|....*..
gi 1864524957 381 fqpegagacygrkvcpcsgekvvhHDPPLLFDLSRDP 417
Cdd:cd16037 308 ------------------------GYPPQLFDLENDP 320
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
12-423 |
7.69e-28 |
|
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: 114.57 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 12 WTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesagdHCHH---PLHHGFDYFYGMPLSMTGdcaHWelsekrv 88
Cdd:cd16029 72 LAGEPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGYYGGAED---YY------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 89 dleqklnflfqvlalvtltlaagkfmhlisiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-EQPMRFqr 167
Cdd:cd16029 134 -------------------------------------------------THTSGGANDYGNDDLRDNEEPAwDYNGTY-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 168 VTPLILQEVKSFLKR-NKLGPFLLLVSFLHVHIPLITTKNFL----GKSAHGLYGD------NVEEMDWMVGQILDALDT 236
Cdd:cd16029 163 STDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYAdpyeDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 237 EGLTNSTLIYFASDHGGSLENQFANSQY-----------GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIG 303
Cdd:cd16029 243 KGMLDNTLIVFTSDNGGPTGGGDGGSNYplrggkntlweGG-----------------VRVPA-FVWSPLLPpkRGTVSD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 304 EPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRGTLWKVHfvtpvfqp 383
Cdd:cd16029 305 GLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDDITRTTGG-------- 363
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1864524957 384 egAGACYGRKvcpcsgeKVVHHDPplLFDLSRDPSEAHVL 423
Cdd:cd16029 364 --AAIRVGDW-------KLIVGKP--LFNIENDPCERNDL 392
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
17-320 |
1.20e-27 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 112.13 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 17 GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAgdhchhPLHHGFDYFYGmplsmtgdcahwelsekrvdleqklnf 96
Cdd:pfam00884 73 VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG--------------------------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 97 lfqvlalvtltlaagkfmhlisiswmpviwsallavFLLTTSYFAGALIVHADCFLMRNHTiteqpmrfQRVTPLILQev 176
Cdd:pfam00884 120 ------------------------------------RNTGSDLYADPPDVPYNCSGGGVSD--------EALLDEALE-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 177 ksFLKRNKlGPFLLLVSFLHVHIPLITTKNFLGKSA------------HGLYGDNVEEMDWMVGQILDALDTEGLTNSTL 244
Cdd:pfam00884 154 --FLDNND-KPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864524957 245 IYFASDHGGSLENQFANSQYGGWNGIYKGGkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 320
Cdd:pfam00884 231 VVYTSDHGESLGEGGGYLHGGKYDNAPEGG---------YRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
187-417 |
4.83e-27 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 111.13 E-value: 4.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 187 PFLLLVSFLHVHIPLITTKNFLG----KSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL------- 255
Cdd:cd16032 134 PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLgerglwy 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 256 -ENQFANSqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRV-IDGRD 333
Cdd:cd16032 213 kMSFFEGS---------------------ARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpLDGRS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 334 LLPLLLGTAQHSDHEFLMHYC-ERFLHAARWHQRDRgtlWKvhFVtpvfqpegagacygrkvcpcsgekVVHHDPPLLFD 412
Cdd:cd16032 271 LLPLLEGGDSGGEDEVISEYLaEGAVAPCVMIRRGR---WK--FI------------------------YCPGDPDQLFD 321
|
....*
gi 1864524957 413 LSRDP 417
Cdd:cd16032 322 LEADP 326
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
174-364 |
2.16e-25 |
|
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: 107.21 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 174 QEVKSFLKRNKLG-PFLLLVSFLHVHIPLITTKNFLGK-------------------SAHGLYGDNVEEMDWMVGQILDA 233
Cdd:cd16027 129 SNAADFLNRAKKGqPFFLWFGFHDPHRPYPPGDGEEPGydpekvkvppylpdtpevrEDLADYYDEIERLDQQVGEILDE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 234 LDTEGLTNSTLIYFASDHGGslenQFANS-----QYGgwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSL 308
Cdd:cd16027 209 LEEDGLLDNTIVIFTSDHGM----PFPRAkgtlyDSG------------------LRVPLIVRWPGKIKPGSVSDALVSF 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864524957 309 MDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLG-TAQHSDHEFLMH-------YCERFLHAARWH 364
Cdd:cd16027 267 IDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK 328
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-364 |
6.52e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 100.37 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 14 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesagdhcHHPLHHGFDYFygMPLSMTGDcaHWeLSEKRVDLEQK 93
Cdd:cd16033 76 AYSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPE--------ETPLDYGFDEY--LPVETTIE--YF-LADRAIEMLEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 94 LnflfqvlalvtltLAAGK-FMHLISIsWMPviwsallavfllttsyfagalivHADCF-------LMRNHTITEqPMRF 165
Cdd:cd16033 143 L-------------AADDKpFFLRVNF-WGP-----------------------HDPYIppepyldMYDPEDIPL-PESF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 166 QRvtPLILqevKSFLKRNKLGPFLLLVSFLHVHIPLIttknflgksAHglYGDNVEEMDWMVGQILDALDTEGLTNSTLI 245
Cdd:cd16033 185 AD--DFED---KPYIYRRERKRWGVDTEDEEDWKEII---------AH--YWGYITLIDDAIGRILDALEELGLADDTLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 246 YFASDHGGSLENQfansqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQ 325
Cdd:cd16033 249 IFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPP 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1864524957 326 DrvIDGRDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWH 364
Cdd:cd16033 317 K--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYK 361
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
19-421 |
1.29e-22 |
|
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: 99.91 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 19 LPTNETTFAKILKEKGYATGLIGKWHLGlncesaGDHCHHPlhHGFDYFYGMPlsmtgdcahwelsekrvdlEQklnflf 98
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGKWHLG------SGGDLPP--PGFDYWVSFP-------------------GQ------ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 99 qvlalvtltlaagkfmhlisiswmpviwsallavflltTSYFAGALIVhadcflMRNHTITEQPmrfqrVTPLILQEVKS 178
Cdd:cd16031 124 --------------------------------------GSYYDPEFIE------NGKRVGQKGY-----VTDIITDKALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 179 FLKRNKLG-PFLLLVSFLHVH-----------------IPLITT---KNFLGKS-------------------AHGLYGD 218
Cdd:cd16031 155 FLKERDKDkPFCLSLSFKAPHrpftpaprhrglyedvtIPEPETfddDDYAGRPewareqrnrirgvldgrfdTPEKYQR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 219 NVE-------EMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-ENQFA-------NSqyggwngiykggkgmggwegg 283
Cdd:cd16031 235 YMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLgEHGLFdkrlmyeES--------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 284 IRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHS-DHEFLMHYCE--RFLHA 360
Cdd:cd16031 294 IRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864524957 361 ARWH--QRDRgtlWK-VHFvtpvfqpegagacygrkvcpcsgekvvHHDPPL--LFDLSRDPSEAH 421
Cdd:cd16031 372 PTHEgvRTER---YKyIYY---------------------------YGVWDEeeLYDLKKDPLELN 407
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
220-421 |
3.61e-22 |
|
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: 98.28 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 220 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFAN------------SQYGGwngiykggkgmggweggIRVP 287
Cdd:cd16025 225 VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPGWANasntpfrlykqaSHEGG-----------------IRTP 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 288 GIFRWP-GVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRV------IDGRDLLPLLLGTAQHSDHEFLmhYCERFLHA 360
Cdd:cd16025 288 LIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ--YFELFGNR 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864524957 361 ARWHQRdrgtlWKVhfvtpvfqpegagacygrkvcpcsgekVVHHDPPL------LFDLSRDPSEAH 421
Cdd:cd16025 366 AIRKGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
220-445 |
1.61e-21 |
|
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: 96.94 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 220 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQyGGWNGIYKggkgmggweggiRVPGIFRWPGVL--- 296
Cdd:cd16028 244 IAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGK-DGFFDQAY------------RVPLIVRDPRREada 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 297 PAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQRDRG 369
Cdd:cd16028 311 TRGQVVDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALG 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864524957 370 TlwkvhfvtpvfQPEGAGACYGRkvcpcSGE-KVVHHD--PPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEH 445
Cdd:cd16028 382 L-----------SPDECSLAVIR-----DERwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSW 442
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
169-336 |
9.46e-20 |
|
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: 88.76 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 169 TPLILQEVKSFLKRNKLG-PFlllvsFLHVHIplittknFlgkSAHGLYG-DN-VEEMDWMVGQILDALDTEGLTNSTLI 245
Cdd:cd16148 130 AERVTDRALEWLDRNADDdPF-----FLFLHY-------F---DPHEPYLyDAeVRYVDEQIGRLLDKLKELGLLEDTLV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 246 YFASDHGgslENQFANSQYGGWNgiykggkgMGGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVQLAGGEVPQ 325
Cdd:cd16148 195 IVTSDHG---EEFGEHGLYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPD 262
|
170
....*....|.
gi 1864524957 326 DrvIDGRDLLP 336
Cdd:cd16148 263 Y--SDGRSLLP 271
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
157-319 |
2.48e-19 |
|
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: 87.09 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 157 TITEQpMRFQRVTPLILQEVKSFLKRNKLGPFLLLVSFLHVHIPLittknFLGKSAHGLYGDNVEEMDWMVGQILDALDT 236
Cdd:cd00016 91 TIPEL-LKQAGYRTGVIGLLKAIDETSKEKPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 237 EGLTNSTLIYFASDHGGSLEnqfansqygGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVV 316
Cdd:cd00016 165 AGDADDTVIIVTADHGGIDK---------GHGGDPKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLA 234
|
...
gi 1864524957 317 QLA 319
Cdd:cd00016 235 DLL 237
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
179-336 |
3.15e-19 |
|
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: 87.29 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 179 FLKRNKLG--PFLLLVSFLHVHIPlittknflgksaHGlYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGgsle 256
Cdd:cd16149 118 FLRRRAEAekPFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNG---- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 257 nqFANSQYGGW---------NGIYKGgkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDR 327
Cdd:cd16149 181 --FNMGHHGIWgkgngtfplNMYDNS----------VKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADP 248
|
....*....
gi 1864524957 328 VIDGRDLLP 336
Cdd:cd16149 249 RLPGRSFAD 257
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
223-347 |
9.31e-18 |
|
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: 85.32 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 223 MDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-ENQ----FANsqyggWNGIykggkgmggweggIRVPGIFRWPGVLP 297
Cdd:cd16030 270 VDAQVGRVLDALEELGLADNTIVVLWSDHGWHLgEHGhwgkHTL-----FEEA-------------TRVPLIIRAPGVTK 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1864524957 298 AGRVIGEPTSLMDVFPTVVQLAGgeVPQDRVIDGRDLLPLLLGTAQHSDH 347
Cdd:cd16030 332 PGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKD 379
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
170-353 |
3.35e-17 |
|
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: 82.26 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 170 PLILQEVKSFLKR-----NKLGPFLLLVSFL--H-VHIPLITTKNFlgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTN 241
Cdd:cd16035 117 PGIAAQAVEWLRErgaknADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLAD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 242 STLIYFASDHG---GS--LENQFANSqYGgwngiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVV 316
Cdd:cd16035 195 NTIVVFTSDHGemgGAhgLRGKGFNA-YE----------------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLL 257
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1864524957 317 QLAGGEVPQDRVID----GRDLLPLLLGTAQHSDHE-FLMHY 353
Cdd:cd16035 258 GLAGVDAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
220-429 |
4.64e-17 |
|
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: 82.61 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 220 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL--------ENQFANSqyggwngiykggkgmggweggIRVPGIFR 291
Cdd:cd16155 198 ITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVgshglmgkQNLYEHS---------------------MRVPLIIS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 292 WPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQhsdheflMHYCERFLHAARWHQRDRGTL 371
Cdd:cd16155 257 GPGI-PKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKK-------AVRDTLYGAYRDGQRAIRDDR 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524957 372 WKVHFVTPvfqpegagacygrkvcpcsGEKVVhhdppLLFDLSRDPSEAHVLtpASEP 429
Cdd:cd16155 327 WKLIIYVP-------------------GVKRT-----QLFDLKKDPDELNNL--ADEP 358
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
205-341 |
3.69e-16 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 80.87 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 205 KNFLGKSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL--ENQFANS-QYGGwngiykggkgmggwe 281
Cdd:PRK13759 260 EEYARRARAAYYG-LITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLgdHYLFRKGyPYEG--------------- 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864524957 282 gGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGT 341
Cdd:PRK13759 324 -SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ 383
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
186-334 |
5.01e-16 |
|
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: 78.19 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 186 GPFLLLVSFLHVHIPLITTKNFLGKSA-HGL--YGDNveemdwMVGQILDALDTEGLTN---STLIYFASDHGGSLENQF 259
Cdd:cd16153 143 KPFFVRLSFLQPHTPVLPPKEFRDRFDyYAFcaYGDA------QVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQG 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864524957 260 ANSQYGGWNGIykggkgmggweggIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDL 334
Cdd:cd16153 217 ILAKFTFWPQS-------------HRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
220-453 |
7.41e-15 |
|
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: 76.50 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 220 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHG------GSLE---NQFANSQyggwngiykggkgmggweggIRVPGIF 290
Cdd:cd16150 206 VSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGdytgdyGLVEkwpNTFEDCL--------------------TRVPLII 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 291 RWPGvLPAGRVIGEPTSLMDVFPTVVQLAGgeVPQDRVIDGRDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHQRDR 368
Cdd:cd16150 266 KPPG-GPAGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQAMEGG 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 369 GTlwKVHFVTPVFQPEGAGACYGRKVCPCSGE-KVV--HHDPPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEH 445
Cdd:cd16150 339 HG--PYDLKWPRLLQQEEPPEHTKAVMIRTRRyKYVyrLYEPDELYDLEADPLELHNL--IGDPAYAEIIAEMKQRLLRW 414
|
....*...
gi 1864524957 446 QQTLSPVA 453
Cdd:cd16150 415 MVETSDVV 422
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
187-418 |
2.57e-14 |
|
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: 74.11 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 187 PFLLlvsFLHVHIPLITTKNFLGKSAHGL------YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG-SLEN-Q 258
Cdd:cd16171 166 PFAL---YLGLNLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGElAMEHrQ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 259 FAN-SQYGGwngiykggkgmggwegGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPL 337
Cdd:cd16171 243 FYKmSMYEG----------------SSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 338 LLGTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTLWKvhFVTpvfqpegagacYGrkvcpcSGEKVvhhd 406
Cdd:cd16171 304 LSESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YA------DGNSV---- 354
|
250
....*....|..
gi 1864524957 407 PPLLFDLSRDPS 418
Cdd:cd16171 355 PPQLFDLSKDPD 366
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
18-343 |
1.15e-13 |
|
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: 72.26 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 18 GLPTNETTFAKILKEKGYATGLIGKWHLglncesAGdhchhplhhgfdyfYgmplsmtgdcahwelsekRVDleqklnfl 97
Cdd:cd16152 74 PLPADEKTLAHYFRDAGYETGYVGKWHL------AG--------------Y------------------RVD-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 98 fqvlalvTLTLAAGKFMHlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilqevk 177
Cdd:cd16152 108 -------ALTDFAIDYLD-------------------------------------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 178 sflKRNKLGPFLLLVSFLHVH----------------------IP--LittKNFLGKSAHGL---YGdNVEEMDWMVGQI 230
Cdd:cd16152 119 ---NRQKDKPFFLFLSYLEPHhqndrdryvapegsaerfanfwVPpdL---AALPGDWAEELpdyLG-CCERLDENVGRI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 231 LDALDTEGLTNSTLIYFASDHGgsleNQFA--NSQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEPTSL 308
Cdd:cd16152 192 RDALKELGLYDNTIIVFTSDHG----CHFRtrNAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEELVSL 255
|
330 340 350
....*....|....*....|....*....|....*
gi 1864524957 309 MDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQ 343
Cdd:cd16152 256 IDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVE 288
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
223-332 |
7.42e-13 |
|
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: 69.89 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 223 MDWMVGQILDALDTEGLTNSTLIYFASDHG---GSLENQFANSQ-YggwngiykggkgmggwEGGIRVPGIFRWPGVlPA 298
Cdd:cd16147 251 VDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHRLPPGKRTpY----------------EEDIRVPLLVRGPGI-PA 313
|
90 100 110
....*....|....*....|....*....|....
gi 1864524957 299 GRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGR 332
Cdd:cd16147 314 GVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
18-338 |
3.58e-10 |
|
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: 62.01 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 18 GLPTNETTFAKILKEKGYATGLIGKWHLglnceSAGDH-----ChhPLHHGFDYFYGMplsmtgDCAHWELSEKRVdleq 92
Cdd:cd16156 73 ALGDNVKTIGQRLSDNGIHTAYIGKWHL-----DGGDYfgngiC--PQGWDPDYWYDM------RNYLDELTEEER---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 93 klnflfqvlalvtltlaagkfmhlisiswmpVIWSALLAVfllttsyfagalivhadcflMRNHTITEQPMRFQRVTPLI 172
Cdd:cd16156 136 -------------------------------RKSRRGLTS--------------------LEAEGIKEEFTYGHRCTNRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 173 LQevksFLKRNKLGPFLLLVSFLHVHIPLITTKNF----------LGKSAHglygDNVEE-------------------- 222
Cdd:cd16156 165 LD----FIEKHKDEDFFLVVSYDEPHHPFLCPKPYasmykdfefpKGENAY----DDLENkplhqrlwagakphedgdkg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 223 -------------MDWMVGQILDALDtEGLTNSTLIYfASDHGgslENQFANSQYGgwngiykggKGMGGWEGGIRVPGI 289
Cdd:cd16156 237 tikhplyfgcnsfVDYEIGRVLDAAD-EIAEDAWVIY-TSDHG---DMLGAHKLWA---------KGPAVYDEITNIPLI 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1864524957 290 FRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGgeVPQDRVIDGRDLLPLL 338
Cdd:cd16156 303 IRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
173-320 |
1.53e-07 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 52.69 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 173 LQEVKSFLKRNKLGPFlllvsFLHV-----H----IPLITTKNFLGKSAHGLYGDN----VEEMDWMVGQILDALDTEGL 239
Cdd:cd16015 143 FDQALEELEELKKKPF-----FIFLvtmsnHgpydLPEEKKDEPLKVEEDKTELENylnaIHYTDKALGEFIEKLKKSGL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 240 TNSTLIYFASDHGGSLENQFANSQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTVVQLA 319
Cdd:cd16015 218 YENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLL 282
|
.
gi 1864524957 320 G 320
Cdd:cd16015 283 G 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
220-335 |
1.79e-07 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 53.50 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 220 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYggwngiykggkgmggwEGGIRVPGIFRWPGvLPAG 299
Cdd:COG1368 423 VRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENP----------------LERYRVPLLIYSPG-LKKP 485
|
90 100 110
....*....|....*....|....*....|....*.
gi 1864524957 300 RVIGEPTSLMDVFPTVVQLAGGEVPQDRVIdGRDLL 335
Cdd:COG1368 486 KVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
220-317 |
1.78e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 50.29 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 220 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-ENQ----FANSQYGGWNgiykggkgmggweggIRVPGIFRWPG 294
Cdd:COG3083 433 VHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnENGqnywGHNSNFSRYQ---------------LQVPLVIHWPG 497
|
90 100
....*....|....*....|...
gi 1864524957 295 VLPagRVIGEPTSLMDVFPTVVQ 317
Cdd:COG3083 498 TPP--QVISKLTSHLDIVPTLMQ 518
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
13-345 |
3.38e-06 |
|
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: 49.27 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 13 TGASGGLPTNETTFAKILKE----KGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEKRV 88
Cdd:cd16154 69 LAVPDELLLSEETLLQLLIKdattAGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 89 DLEQKlnflfqvlalvtlTLAAGKFMHLiSISWM-----PviWSALLAvfllttsYFAgalivhadcflmrNHTiteqpm 163
Cdd:cd16154 143 TTNST-------------EYATTKLTNL-AIDWIdqqtkP--WFLWLA-------YNA-------------PHT------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 164 rfqrvtplilqevksflkrnklgPFLLLVSFLHvhiplitTKNFLGKSAHglYGDN--------VEEMDWMVGQILDALD 235
Cdd:cd16154 181 -----------------------PFHLPPAELH-------SRSLLGDSAD--IEANprpyylaaIEAMDTEIGRLLASID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524957 236 TEGLTNsTLIYFASDHG--------GSLENQFANSQY-GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPT 306
Cdd:cd16154 229 EEEREN-TIIIFIGDNGtpgqvvdlPYTRNHAKGSLYeGG-----------------INVPLIVSGAGV---ERANERES 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1864524957 307 SLM---DVFPTVVQLAGGEVPQdrVIDGRDLLPLLLGTAQHS 345
Cdd:cd16154 288 ALVnatDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNAST 327
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
220-252 |
1.61e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 40.50 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|...
gi 1864524957 220 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 252
Cdd:COG1524 211 LREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
218-252 |
5.49e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 38.94 E-value: 5.49e-03
10 20 30
....*....|....*....|....*....|....*
gi 1864524957 218 DNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 252
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| |
