|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
62-585 |
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: 755.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQK 221
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 222 LNFLFQVLALVALTLVAGKLthLIPVSWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 301
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLY--LGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 302 QEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 381
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 382 SLENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQD 461
Cdd:cd16159 319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 462 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDL 541
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1593597358 542 SRDPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 585
Cdd:cd16159 478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
62-549 |
3.90e-156 |
|
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: 453.94 E-value: 3.90e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRVLQWT 141
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 GASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasDH-CHHPLHHGFDHFYGMPFSLMGDCARWELSEKRvnleq 220
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 221 klnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivHADCFLMRNHTITEQPMcFQRT-TPL 299
Cdd:cd16026 144 ------------------------------------------------------GPLPPLMENEEVIEQPA-DQSSlTQR 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 300 ILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD- 378
Cdd:cd16026 169 YTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDn 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 379 --------HGGSleNQL-----GNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR 445
Cdd:cd16026 249 gpwleyggHGGS--AGPlrggkGTTWEGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 446 LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGacygrkvcpc 525
Cdd:cd16026 310 LAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG---------- 373
|
490 500
....*....|....*....|....
gi 1593597358 526 fGEKVVHHDPPLLFDLSRDPSETH 549
Cdd:cd16026 374 -GLDPTKLEPPLLYDLEEDPGETY 396
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
62-566 |
6.75e-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: 396.42 E-value: 6.75e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsiGYRV-LQW 140
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 141 TgaSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDhFYG--MPFSLMGDCARWELSekrvnl 218
Cdd:cd16160 79 D--IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGtnLPFTNSWACDDTGRH------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 219 eqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalIVHAD---CFLMRNHTITEQPMCFQR 295
Cdd:cd16160 150 ------------------------------------------------------VDFPDrsaCFLYYNDTIVEQPIQHEH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 296 TTPLILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYF 375
Cdd:cd16160 176 LTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 376 TSDHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTV 443
Cdd:cd16160 256 LSDHGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 444 VRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACYGR 520
Cdd:cd16160 318 VDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGGG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1593597358 521 KVCP------CFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMERV 566
Cdd:cd16160 391 PLSDyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPSVYEHMLEAVEKL 442
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
63-607 |
3.67e-99 |
|
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: 310.53 E-value: 3.67e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqwTG 142
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhcHHPLHHGFDHFYGMPFSL-MGDCArwelsekrvnleqk 221
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHdQGPCQ-------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 222 lnflfqvlalvaltlvagKLTHLIPvswmpviwsalsavlllASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLIL 301
Cdd:cd16158 139 ------------------NLTCFPP-----------------NIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 302 QEVASFL----KRNKhgPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTS 377
Cdd:cd16158 184 KFAKDFIadnaKEGK--PFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 378 DHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVR 445
Cdd:cd16158 262 DNGpstmrksrggnaGLLKCGKGTTYEGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 446 LAGGEVPqDRVIDGQDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACY 518
Cdd:cd16158 324 LAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCH 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 519 GRKvcpcfgeKVVHHDPPLLFDLSRDPSETHILTpaSEPVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNiwrPWLQPC 598
Cdd:cd16158 397 PSA-------ELTSHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPC 464
|
570
....*....|...
gi 1593597358 599 ----CGPFPLCWC 607
Cdd:cd16158 465 ckpgCTPKPSCCQ 477
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
44-549 |
9.58e-96 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 298.72 E-value: 9.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 123
Cdd:COG3119 5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 124 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLncesasdhchhplhhgfdhfygmpfslm 203
Cdd:COG3119 85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYL---------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 204 gdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 283
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 284 htiteqpmcfqrtTPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGK----------------------- 338
Cdd:COG3119 130 -------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelr 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 339 SLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlG-----NTQY-GGwngiykggkgmggweggI 412
Cdd:COG3119 197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEH-GlrggkGTLYeGG-----------------I 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 413 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWH 492
Cdd:COG3119 259 RVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRT 336
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1593597358 493 QRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhhDPPLLFDLSRDPSETH 549
Cdd:COG3119 337 GR-----WKLIR------------YYDDD------------GPWELYDLKNDPGETN 364
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-552 |
1.09e-95 |
|
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: 297.91 E-value: 1.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssigYRVlQ 139
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-----TTV-G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 140 WTGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPFSLMGDcarwELSEKRVNle 219
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG------RLPTDHGFDEFYGNLYHTIDE----EIVDKAID-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 220 qklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcFLMRNHtiteqpmcfqrttpl 299
Cdd:cd16142 142 -----------------------------------------------------------FIKRNA--------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 300 ilqevasflKRNKhgPFLLFVSFLHVHIPLITMENFLGKSL-HGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 378
Cdd:cd16142 148 ---------KADK--PFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTD 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 379 HG-----------GSLENQLGNTQYGGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLA 447
Cdd:cd16142 217 NGpeqdvwpdggyTPFRGEKGTTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALA 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 448 GGEVP------QDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVtpVFQPEGAGACYGRK 521
Cdd:cd16142 280 GAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFY 351
|
490 500 510
....*....|....*....|....*....|.
gi 1593597358 522 VCPCfgekvvhhdpPLLFDLSRDPSETHILT 552
Cdd:cd16142 352 VLTF----------PLIFNLRRDPKERYDVT 372
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
62-552 |
3.30e-90 |
|
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: 284.36 E-value: 3.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRvlqw 140
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 141 tgASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSlmGDCarwELSEKRVNLeq 220
Cdd:cd16161 77 --SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFS--HDS---SLADRYAQF-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 221 klnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhADCFLMRNhtiteqpmcfqrttpli 300
Cdd:cd16161 142 -------------------------------------------------------ATDFIQRA----------------- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 301 lqevasflkRNKHGPFLLFVSFLHVHIPLITMENFLGKSLH-GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 379
Cdd:cd16161 150 ---------SAKDRPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 380 G-----GSLENQLGNTQY---GGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEV 451
Cdd:cd16161 221 GpwevkCELAVGPGTGDWqgnLGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASL 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 452 PQDRVIDGQDLLPLLLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtmWKVHFVTpvfqpEGAGACygrkvCPCF 526
Cdd:cd16161 296 PPGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALAC-----CGST 358
|
490 500
....*....|....*....|....*.
gi 1593597358 527 GEKvVHHDPPLLFDLSRDPSETHILT 552
Cdd:cd16161 359 GPK-LYHDPPLLFDLEVDPAESFPLT 383
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-549 |
1.32e-89 |
|
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: 283.67 E-value: 1.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 142
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 A-------SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDH------------FYGMPFSLM 203
Cdd:cd16144 81 TklipppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVniggtgnggppsYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 204 GDCARWELSEKRVNleqklnflfqvlalvALTlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrn 283
Cdd:cd16144 155 PDLEDGPEGEYLTD---------------RLT------------------------------------------------ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 284 htiteqpmcfqrttplilQEVASFLKRNKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYGDN-------VEEMD 352
Cdd:cd16144 172 ------------------DEAIDFIEQNKDKPFFLYLSHYAVHTPIQarpeLIEKYEKKKKGLRKGQKnpvyaamIESLD 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 353 WMVGRILDTLDVEGLSNSTLIYFTSDHGG-SLENQLGNTQY-----------GGwngiykggkgmggweggIRVPGIFRW 420
Cdd:cd16144 234 ESVGRILDALEELGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRW 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 421 PGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYcerFLHAARWHQRDRGTM- 499
Cdd:cd16144 297 PGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWH---FPHYHGQGGRPASAIr 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1593597358 500 ---WK-VHFvtpvfqpegagacygrkvcpcfgekvvHHDPPL-LFDLSRDPSETH 549
Cdd:cd16144 374 kgdWKlIEF---------------------------YEDGRVeLYNLKNDIGETN 401
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-549 |
1.83e-88 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 279.86 E-value: 1.83e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssiGYRVLQWT 141
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRL----KGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 GASGgLPTNETTFAKILKEKGYATGLIGKWHLGLN------CESASDHCHH----------PLHHGFDHFYGMPFSlmgd 205
Cdd:cd16143 77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwkkkdgKKAATGTGKDvdyskpikggPLDHGFDYYFGIPAS---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 206 carwelsekrvnleqklnflfQVLalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnht 285
Cdd:cd16143 152 ---------------------EVL-------------------------------------------------------- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 286 iteqpmcfqrttPLILQEVASFLKRNKHG--PFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLD 363
Cdd:cd16143 155 ------------PTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 364 VEGLSNSTLIYFTSDHGGSLENQLGNTQ-----------------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLP 425
Cdd:cd16143 223 ELGLAENTLVIFTSDNGPSPYADYKELEkfghdpsgplrgmkadiYeGG-----------------HRVPFIVRWPGKIP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 426 AGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTMWKVhfv 505
Cdd:cd16143 286 AGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL--- 356
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1593597358 506 tpVFQPEGAGACYGRKvcpcfgeKVVHHDPP-LLFDLSRDPSETH 549
Cdd:cd16143 357 --IDGTGSGGFSYPRG-------KEKLGLPPgQLYNLSTDPGESN 392
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
62-585 |
2.33e-86 |
|
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: 277.04 E-value: 2.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 GAS--GGLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPfslmgDCARWELSEKRvnle 219
Cdd:cd16157 81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGPYDNKA---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 220 qklnflfqvlalvaltlvagklTHLIPV--SWmpviwsalsavlLLASSYFVGALIvhadcflmrNHTITEQPMcfqrtT 297
Cdd:cd16157 146 ----------------------YPNIPVyrDW------------EMIGRYYEEFKI---------DKKTGESNL-----T 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 298 PLILQEVASFLKR--NKHGPFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYF 375
Cdd:cd16157 178 QIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 376 TSDHGGSLenqLGNTQYGGWNgIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDR 455
Cdd:cd16157 258 SSDNGAAL---ISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDR 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 456 VIDGQDLLPLLLgtAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVT----PVFQPEGAGACYGRKVCPCFGEKVV 531
Cdd:cd16157 334 AIDGIDLLPVLL--NGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQT 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1593597358 532 HH-DPPLLFDLSRDPSETHILTPASePVFYQVMERVQQAVWEHQRTLSPVPLQLD 585
Cdd:cd16157 406 DHtKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-549 |
3.45e-75 |
|
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: 245.97 E-value: 3.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyRVLQWTG 142
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasDHCHHPLHHGFDHFYGmpfslmgdcarwelsekrvnleqkl 222
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGP-----GTPGHPTKQGFDYFYG------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 nFLFQVLAlvaltlvagkltHlipvswmpviwsalsavlllasSYFVGALIVHADCFLMRNHTIT-------EQPMCFQR 295
Cdd:cd16145 125 -YLDQVHA------------H----------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 296 TTPLILQEVASFLKRNKHGPFLLFVSFLHVHIPLIT-------MENFLGKSLHGLYGDNVEE--------MDWMVGRILD 360
Cdd:cd16145 170 SHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVpddgpykYKPKDPGIYAYLPWPQPEKayaamvtrLDRDVGRILA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 361 TLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQY--------------------GGwngiykggkgmggweggIRVPGIFRW 420
Cdd:cd16145 250 LLKELGIDENTLVVFTSDNGPHSE---GGSEHdpdffdsngplrgykrslyeGG-----------------IRVPFIARW 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 421 PGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdr 496
Cdd:cd16145 310 PGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG--- 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1593597358 497 gtmWKVhfvtpVFQPEGAGacygrkvcpcfgekvvhhdPPLLFDLSRDPSETH 549
Cdd:cd16145 383 ---WKA-----VRHGKKDG-------------------PFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
63-461 |
1.36e-74 |
|
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: 238.11 E-value: 1.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssigyrVLQWTG 142
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqkl 222
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplilQ 302
Cdd:cd16022 103 -------------------------------------------------------------------------------D 103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 303 EVASFLKRNKHG-PFLLFVSFLHVHIPLItmenflgkslhglYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 381
Cdd:cd16022 104 EAIDFIERRDKDkPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 382 SLENqlGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQD 461
Cdd:cd16022 171 MLGD--HGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
63-572 |
6.51e-72 |
|
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: 237.06 E-value: 6.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSIGYRVLqwt 141
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSLMGDCARWELSEkrvnleqk 221
Cdd:cd16146 76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 222 lnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassYFvgalivhaDCFLMRNHTiteqpmcFQRT----T 297
Cdd:cd16146 137 ---------------------------------------------YF--------DDTYYHNGK-------FVKTegycT 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 298 PLILQEVASFLKRNKHGPFLLFVSFLHVHIPLITMEN----FLGKSLH----GLYGdNVEEMDWMVGRILDTLDVEGLSN 369
Cdd:cd16146 157 DVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKyldpYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 370 STLIYFTSDHGGSLENQLGN---------TQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDV 439
Cdd:cd16146 236 NTIVIFMSDNGPAGGVPKRFnagmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDL 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 440 FPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTMWKVHFVtpVFQPEgagacYg 519
Cdd:cd16146 299 LPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W- 361
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1593597358 520 RKVCPcfgekvvHHDPPLLFDLSRDPSETHILTpASEPVFYQVMERVQQAVWE 572
Cdd:cd16146 362 RLVSP-------KGFQPELYDIENDPGEENDVA-DEHPEVVKRLKAAYEAWWD 406
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-491 |
3.99e-66 |
|
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: 220.93 E-value: 3.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqwtg 142
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 aSGGLPTNETTFAKILKEKGYATGLIGKWHLGLNcESASDhchHPLHHGFDHFygmpfslmgdCArWELSEKRVNLEQKL 222
Cdd:cd16151 68 -FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEY----------CL-WQLTETGEKYSRPA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 NFLFQVLalvaltlvAGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcFLMRnhtiteqpmcfqrttplilq 302
Cdd:cd16151 132 TPTFNIR--------NGKLLETTEGDYGPDLFAD----------------------FLID-------------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 303 evasFLKRNKHGPFLLFVSFLHVHIPL----------ITMENFLGKSLHglYGDNVEEMDWMVGRILDTLDVEGLSNSTL 372
Cdd:cd16151 162 ----FIERNKDQPFFAYYPMVLVHDPFvptpdspdwdPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 373 IYFTSDHG--GSLENQLGNTQY-GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGG 449
Cdd:cd16151 236 IIFTGDNGthRPITSRTNGREVrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGA 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1593597358 450 EVPQDRVIDGQDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 491
Cdd:cd16151 307 PLPEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
62-551 |
6.78e-63 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 212.81 E-value: 6.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVsSIGYRvlqwt 141
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHH----PLHHGFDHFYGMpfslmgdcarwelsekrvn 217
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 218 leqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhaDCFLMRNHTI----TEQPMCF 293
Cdd:cd16034 131 -----------------------------------------------------------ECNHDHNNPHyyddDGKRIYI 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 294 QRTTPLILQEVA-SFLKRNKHG--PFLLFVSF------------------------LHVHIPLITMENF-LGKSLHGLYG 345
Cdd:cd16034 152 KGYSPDAETDLAiEYLENQADKdkPFALVLSWnpphdpyttapeeyldmydpkkllLRPNVPEDKKEEAgLREDLRGYYA 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 346 dNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQYGGwngiykggkgmggwegGIRVPGIFRWPG 422
Cdd:cd16034 232 -MITALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYPG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 423 VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTM--- 499
Cdd:cd16034 295 KIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtd 372
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1593597358 500 -WKvhFVtpvfqpegagacygrkvcpcfgekVVHHDPPLLFDLSRDPSETHIL 551
Cdd:cd16034 373 rYT--YV------------------------RDKNGPWLLFDNEKDPYQLNNL 399
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
63-549 |
9.37e-63 |
|
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: 212.41 E-value: 9.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssiGYRVLqWTG 142
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVI-LAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasdHCHH---PLHHGFDHFYGMpFSLMGDcarwelsekrvnle 219
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY-YGGAED-------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 220 qklnflfqvlalvaltlvagkltHLIPVSWMPVIWSalsavlllassyfvgalivhaDCFLMRNHTIT-EQPMCFqrTTP 298
Cdd:cd16029 132 -----------------------YYTHTSGGANDYG---------------------NDDLRDNEEPAwDYNGTY--STD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 299 LILQEVASFLKR-NKHGPFLLFVSFLHVHIPL------ITMENFLGKSLHG----LYGDNVEEMDWMVGRILDTLDVEGL 367
Cdd:cd16029 166 LFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLqvppeyADPYEDKFAHIKDedrrTYAAMVSALDESVGNVVDALKAKGM 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 368 SNSTLIYFTSDHGGSLENQLG----------NTQY-GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIGEPT 434
Cdd:cd16029 246 LDNTLIVFTSDNGGPTGGGDGgsnyplrggkNTLWeGG-----------------VRVPA-FVWSPLLPpkRGTVSDGLM 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 435 SLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRgtmwkvhfvtPVFQPEGA 514
Cdd:cd16029 308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDD----------ITRTTGGA 364
|
490 500 510
....*....|....*....|....*....|....*
gi 1593597358 515 GACYGRKvcpcfgeKVVHHDPplLFDLSRDPSETH 549
Cdd:cd16029 365 AIRVGDW-------KLIVGKP--LFNIENDPCERN 390
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
63-575 |
1.22e-58 |
|
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: 200.81 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssIGYRVLQWTg 142
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 asggLPTNETTFAKILKEKGYATGLIGKWHlgLNCESASDHCHHPLHHGFDHFYGMPFslMGDCARWelsEKRVNLEQkl 222
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWDY--ASNAADF---LNRAKKGQ-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 NFLFQvlalvaltlVAGKLTHlipVSWMPVIWSAL----SAVLLlaSSYFVgalivhaDcflmrnhtiteqpmcfqrtTP 298
Cdd:cd16027 143 PFFLW---------FGFHDPH---RPYPPGDGEEPgydpEKVKV--PPYLP-------D-------------------TP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 299 LILQEVASFLkrnkhgpfllfvsflhvhiplitmenflgkslhglygDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 378
Cdd:cd16027 183 EVREDLADYY-------------------------------------DEIERLDQQVGEILDELEEDGLLDNTIVIFTSD 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 379 HGGSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvID 458
Cdd:cd16027 226 HGMPFPRAKGTLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQ 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 459 GQDLLPLLLG-TAQHSDHEFLMH-------YCERFLHAARWHqrdrgtmwkvhfvtpvfqpegagacYgrkvcpcfgekV 530
Cdd:cd16027 287 GRSFLPLLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK-------------------------Y-----------I 330
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1593597358 531 VHHDPPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 575
Cdd:cd16027 331 RNYMPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
63-448 |
3.91e-58 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 197.26 E-value: 3.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtg 142
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 asGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESAsdhchhPLHHGFDHFYGmpfslmgdcaRWELSEKRVNLEqkl 222
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFG----------RNTGSDLYADPP--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmRNHTITEQPMCF-QRTTPLIL 301
Cdd:pfam00884 132 -----------------------------------------------------------DVPYNCSGGGVSdEALLDEAL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 302 QevasfLKRNKHGPFLLFVSFLHVHIPL------------ITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSN 369
Cdd:pfam00884 153 E-----FLDNNDKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1593597358 370 STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 448
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
473-607 |
4.91e-58 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 190.60 E-value: 4.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 473 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 552
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1593597358 553 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 607
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
61-568 |
8.52e-56 |
|
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: 194.67 E-value: 8.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 61 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqw 140
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 141 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDhchhplhhGFDHFYGMP---------FSLMGDCARWEL 211
Cdd:cd16031 71 DNNGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFPgqgsyydpeFIENGKRVGQKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 212 SEKRVNLEQKLNFL--------FqvlalvALTlVAGKLTHLipvSWMPViwsalsavlllassyfvgalIVHADcfLMRN 283
Cdd:cd16031 143 YVTDIITDKALDFLkerdkdkpF------CLS-LSFKAPHR---PFTPA--------------------PRHRG--LYED 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 284 HTITE-----------QPMCFQRTTPLI-LQEVASFLKRNKHGpfllfvsflhvhiplITMENFLGkSLHGlygdnveeM 351
Cdd:cd16031 191 VTIPEpetfddddyagRPEWAREQRNRIrGVLDGRFDTPEKYQ---------------RYMKDYLR-TVTG--------V 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 352 DWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGG-WNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVI 430
Cdd:cd16031 247 DDNVGRILDYLEEQGLADNTIIIYTSDNG----FFLGEHGLFDkRL----------MYEESIRVPLIIRDPRLIKAGTVV 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 431 GEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHS-DHEFLMHYCE--RFLHAARWH--QRDRgtmWK-VHF 504
Cdd:cd16031 313 DALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNVPTHEgvRTER---YKyIYY 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1593597358 505 vtpvfqpegagacygrkvcpcfgekvvHHDPPL--LFDLSRDPSETH--ILTPASEPVFYQVMERVQQ 568
Cdd:cd16031 388 ---------------------------YGVWDEeeLYDLKKDPLELNnlANDPEYAEVLKELRKRLEE 428
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
62-549 |
7.19e-54 |
|
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: 188.81 E-value: 7.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEDGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSIGYRVLQW 140
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 141 TGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLN----CESASDH-----------------------CHHPLH---- 189
Cdd:cd16025 78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPDdyysTDDLTDKaieyideqkapdkpfflylafgaPHAPLQapke 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 190 -----HG-FDhfygmpfslMGdcarWE-LSEKRvnLE-QKlnflfqvlalvALTLVAG--KLTHLIPvsWMPViWSALSA 259
Cdd:cd16025 158 widkyKGkYD---------AG----WDaLREER--LErQK-----------ELGLIPAdtKLTPRPP--GVPA-WDSLSP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 260 vlllassyfvgalivhadcflmrnhtitEQPMCFQRttpliLQEV-ASFlkrnkhgpfllfvsflhvhiplitmenflgk 338
Cdd:cd16025 209 ----------------------------EEKKLEAR-----RMEVyAAM------------------------------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 339 slhglygdnVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN---QLGNTQY---------GGwngiykggkgmg 406
Cdd:cd16025 225 ---------VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPgwaNASNTPFrlykqasheGG------------ 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 407 gweggIRVPGIFRWP-GVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV------IDGQDLLPLLLGTAQHSDHEFLm 479
Cdd:cd16025 284 -----IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ- 357
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593597358 480 hYCERFLHAARWHQRdrgtmWKVhfvtpvfqpegagacygrkvcpcfgekVVHHDPPL------LFDLSRDPSETH 549
Cdd:cd16025 358 -YFELFGNRAIRKGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-545 |
3.47e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 173.88 E-value: 3.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRsgmvssIGYrvlqWTG 142
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASGgLPTNETTFAKILKEKGYATGLIGKWHLGLNCEsasdhchhplHHGFDHfygmpfslmgdcarwelsekrvnleqkl 222
Cdd:cd16037 71 ADP-YDGDVPSWGHALRAAGYETVLIGKLHFRGEDQ----------RHGFRY---------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhaDcflmRNhtiteqpmcfqrttplILQ 302
Cdd:cd16037 112 ------------------------------------------------------D----RD----------------VTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 303 EVASFLKRNKH--GPFLLFVSFLHVHIPLITMENFLGKSLHGL---YGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTS 377
Cdd:cd16037 118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 378 DHGgsleNQLG-------NTQYggwngiykggkgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGE 450
Cdd:cd16037 198 DHG----DMLGerglwgkSTMY----------------EESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAP 256
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 451 VPQDRviDGQDLLPLLLGTAQHSDHEFlmhyCErfLHAARwhQRDRGTM-----WK-VHFVtpvfqpegagacygrkvcp 524
Cdd:cd16037 257 PPPDL--DGRSLLPLAEGPDDPDRVVF----SE--YHAHG--SPSGAFMlrkgrWKyIYYV------------------- 307
|
490 500
....*....|....*....|.
gi 1593597358 525 cfgekvvhHDPPLLFDLSRDP 545
Cdd:cd16037 308 --------GYPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-572 |
2.72e-46 |
|
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: 168.55 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqWTG 142
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 A-SGGLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHC--HHPLHHGFDHFYgmpfslmGDCARWELSEkrvnLE 219
Cdd:cd16033 76 AySRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEETPLDYGFdeYLPVETTIEYFL-------ADRAIEMLEE----LA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 220 QKlnflfqvlalvaltlvaGKlthliPvsWMpvIWSAlsavlllassyFVGAlivHADCFLmrnhtitEQPMcFQRTTPL 299
Cdd:cd16033 145 AD-----------------DK-----P--FF--LRVN-----------FWGP---HDPYIP-------PEPY-LDMYDPE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 300 ILQEVASF---------LKRNKHGPFLLFVSFLHVHIPLITmeNFLGkslhglygdNVEEMDWMVGRILDTLDVEGLSNS 370
Cdd:cd16033 177 DIPLPESFaddfedkpyIYRRERKRWGVDTEDEEDWKEIIA--HYWG---------YITLIDDAIGRILDALEELGLADD 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 371 TLIYFTSDHGGSLENQlgntqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGE 450
Cdd:cd16033 246 TLVIFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 451 VPQDrvIDGQDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWHQrdrgtmwkvhfvtpVFQPEGagacygr 520
Cdd:cd16033 314 VPPK--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYKY--------------VFNGFD------- 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1593597358 521 kvcpcFGEkvvhhdpplLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWE 572
Cdd:cd16033 369 -----IDE---------LYDLESDPYELNNL--IDDPEYEEILREMRTRLYE 404
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
63-545 |
3.49e-43 |
|
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: 3.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 142
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASGgLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhCHHPLHHGFDHfygmpfslmgDcarwelsekrvnlEQkl 222
Cdd:cd16032 71 AAE-FPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFDY----------D-------------EE-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 nflfqvlalvaltlvagklthlipvswmpVIWSALSAVLLLAssyfvgalivhadcflmRNHTiteqpmcfqrttplilq 302
Cdd:cd16032 115 -----------------------------VAFKAVQKLYDLA-----------------RGED----------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 303 evasflKRnkhgPFLLFVSFLHVHIPLITMENFLG----KSLHGLYGdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 378
Cdd:cd16032 132 ------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 379 HGgsleNQLGntQYGGWngiykggKGMGGWEGGIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV-I 457
Cdd:cd16032 201 HG----DMLG--ERGLW-------YKMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpL 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 458 DGQDLLPLLLGTAQHSDHEFLMHYCErflhaarwhqrdrgtmwkvhfvtpvfqpEGAGAcygrkvcPCF-----GEKVVH 532
Cdd:cd16032 267 DGRSLLPLLEGGDSGGEDEVISEYLA----------------------------EGAVA-------PCVmirrgRWKFIY 311
|
490
....*....|....*
gi 1593597358 533 --HDPPLLFDLSRDP 545
Cdd:cd16032 312 cpGDPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-464 |
1.46e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 153.93 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 142
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASGGLPTNETTFAKILKEKGYATGLIGKWHLGlncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqkl 222
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 nflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgaliVHADCFLMRNHtiteqpmcfqrttplilq 302
Cdd:cd16149 113 ---------------------------------------------------DDAADFLRRRA------------------ 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 303 evasflKRNKhgPFLLFVSFLHVHIPlitmenflgkslHGlYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGS 382
Cdd:cd16149 124 ------EAEK--PFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFN 182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 383 LenqlgnTQYGGW---------NgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQ 453
Cdd:cd16149 183 M------GHHGIWgkgngtfplN----------MYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPA 246
|
410
....*....|.
gi 1593597358 454 DRVIDGQDLLP 464
Cdd:cd16149 247 DPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-464 |
1.95e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 153.86 E-value: 1.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyrvLQWT 141
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 GASGGLPTNETTFAKILKEKGYATGLIgkwhlglncesaSDHCHHPLHHGFDH--FYGMPFSLMGDCARWELSEkrvnle 219
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDRgfDTFEDFRGQEGDPGEEGDE------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 220 qklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrTTPL 299
Cdd:cd16148 129 ----------------------------------------------------------------------------RAER 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 300 ILQEVASFLKRNKHG-PFLLFVSFLHVHIPLitmenflgkslhgLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD 378
Cdd:cd16148 133 VTDRALEWLDRNADDdPFFLFLHYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 379 HGGSLeNQLGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVRLAGGEVPQDrvID 458
Cdd:cd16148 200 HGEEF-GEHGLYWGHGSN----------LYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SD 265
|
....*.
gi 1593597358 459 GQDLLP 464
Cdd:cd16148 266 GRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
63-575 |
5.40e-40 |
|
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: 152.03 E-value: 5.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqWTG 142
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASggLPTNETTFAKILKEKGYATGLIGKWHL-----GLNCESASDHCHHPLHHGFDHFYGMPFslmgdcARWELSEKRVN 217
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFDPVDRLDE------YPAEDSDTAFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 218 LEQKLNFL--------FQVLA-------LVAltlvagklthliPVSWMPVI-WSALSAVLllassyfvgalivhadcflm 281
Cdd:cd16028 144 TDRAIEYLderqdepwFLHLSyirphppFVA------------PAPYHALYdPADVPPPI-------------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 282 RNHTITEQpmcfQRTTPLIlqevASFLKRNKHGpfllfvSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDT 361
Cdd:cd16028 192 RAESLAAE----AAQHPLL----AAFLERIESL------SFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDY 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 362 LDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGGwngiykggkGMGGWEGGIRVPGIFRWPGVL---PAGRVIGEPTSLMD 438
Cdd:cd16028 258 LKETGQWDDTLIVFTSDHG----EQLGDHWLWG---------KDGFFDQAYRVPLIVRDPRREadaTRGQVVDAFTESVD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 439 VFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQRDRGTmwkvhfvtpvfQP 511
Cdd:cd16028 325 VMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALGL-----------SP 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1593597358 512 EGAGACYGRkvcpcfGE--KVVHHD--PPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 575
Cdd:cd16028 385 DECSLAVIR------DErwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSWRM 444
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
61-475 |
1.09e-39 |
|
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: 150.80 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 61 SRPNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqW 140
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 141 TGASGglptNETTFAKILKEKGYATGLIGKWHlglncesasdhchhplHHGFDHFYGMPFSlmgdcarWELSEKRVNLEQ 220
Cdd:cd16030 76 RKVAP----DAVTLPQYFKENGYTTAGVGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 221 KLNFLFQVLALVALTLVAGKLTHLIPV--SWMPVIWSALSAVLLLAS------SYFVGA--------LIVHADCFLMRNH 284
Cdd:cd16030 129 YPPGKLCPGKKGGKGGGGGPAWEAADVpdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 285 TITEQPMCFQRT-TPLI----LQEVasflkRNKHGPFLLFVSFLHVHIPlitmENFLGKSLHGLYGdNVEEMDWMVGRIL 359
Cdd:cd16030 209 ESIPLPNPFDPIdLPEVawndLDDL-----PKYGDIPALNPGDPKGPLP----DEQARELRQAYYA-SVSYVDAQVGRVL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 360 DTLDVEGLSNSTLIYFTSDHGGslenQLGntQYGGW---------NgiykggkgmggweggiRVPGIFRWPGVLPAGRVI 430
Cdd:cd16030 279 DALEELGLADNTIVVLWSDHGW----HLG--EHGHWgkhtlfeeaT----------------RVPLIIRAPGVTKPGKVT 336
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1593597358 431 GEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLLLGTAQHSDH 475
Cdd:cd16030 337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKD 379
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
61-556 |
1.72e-38 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 148.28 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 61 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssiGYrvlq 139
Cdd:PRK13759 5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 140 wtgASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchHP--LHHGFDHfygmpfSLMGDcarWELSEKRVN 217
Cdd:PRK13759 77 ---GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHD---GYLHSGRNE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 218 LEQKLNFLFQVLALVALTLVaGKLTHLIPVSWMPVIWSAlsavlllassyfvgalivhadcflmRNHTITEQpmcfQRTT 297
Cdd:PRK13759 133 DKSQFDFVSDYLAWLREKAP-GKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 298 PLILQEVASFLKR-NKHGPFLLFVSFLHVHIPLITMENFL-------------------------GKSLHGLYGD----- 346
Cdd:PRK13759 183 NWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeey 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 347 ----------NVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ-------YGGwngiykggkgmggwe 409
Cdd:PRK13759 263 arraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG--------------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 410 gGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-YCER 484
Cdd:PRK13759 324 -SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYS 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1593597358 485 FLHaarWHQRDRGT-MWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSRDPSETHILTPASE 556
Cdd:PRK13759 401 SDN---YLTDGKWKyIW--FSQTGEEQ---------------------------LFDLKKDPHELHNLSPSEK 441
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
62-568 |
1.92e-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: 142.75 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRvlqwt 141
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 gASGGLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqk 221
Cdd:cd16152 71 -NGIPLPADEKTLAHYFRDAGYETGYVGKWHL------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 222 lnflfqvlalvaltlvAGklthlipvswmpviwsalsavlllassYFVGALIVHADCFLMrnhtiteqpmcfqrttplil 301
Cdd:cd16152 102 ----------------AG---------------------------YRVDALTDFAIDYLD-------------------- 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 302 qevasflKRNKHGPFLLFVSFLHVHiplitMEN------------------FLGKSLHGLYGDN----------VEEMDW 353
Cdd:cd16152 119 -------NRQKDKPFFLFLSYLEPH-----HQNdrdryvapegsaerfanfWVPPDLAALPGDWaeelpdylgcCERLDE 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 354 MVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlgNTQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEP 433
Cdd:cd16152 187 NVGRIRDALKELGLYDNTIIVFTSDHGCHFRTR--NAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEEL 252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 434 TSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCE----RFLHAARW----HQRDRGtmWKVHFV 505
Cdd:cd16152 253 VSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISEsqvgRAIRTDRWkysvAAPDKD--GWKDSG 328
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1593597358 506 TPVFQPEgagacygrkvcpcfgekvvhhdppLLFDLSRDPSETHILtpASEPVFYQVMERVQQ 568
Cdd:cd16152 329 SDVYVED------------------------YLYDLEADPYELVNL--IGRPEYREVAAELRE 365
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
61-565 |
1.47e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 134.61 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 61 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssigy 135
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 136 rvlqwtGASGGLPTNETTFAKILKEKGYATGLIGKWHLGLnCESASDHCHHP--------LHHGFDH---FYGMPFSLMg 204
Cdd:cd16155 74 ------GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF-ADAAIEFLEEYkdgdkpffMYVAFTAphdPRQAPPEYL- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 205 dcarwelseKRVNLEqklnflfqvlalvaltlvagklTHLIPVSWMPViwsalsavlllassY-FVGALIVHADcflmrn 283
Cdd:cd16155 146 ---------DMYPPE----------------------TIPLPENFLPQ--------------HpFDNGEGTVRD------ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 284 htitEQPMCFQRTTplilQEVASFLKRNkhgpfllfvsflhvhiplitmenflgkslhglYGdNVEEMDWMVGRILDTLD 363
Cdd:cd16155 175 ----EQLAPFPRTP----EAVRQHLAEY--------------------------------YA-MITHLDAQIGRILDALE 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 364 VEGLSNSTLIYFTSDHG------GSLENQlgNTQYGGWngiykggkgmggweggiRVPGIFRWPGVlPAGRVIGEPTSLM 437
Cdd:cd16155 214 ASGELDNTIIVFTSDHGlavgshGLMGKQ--NLYEHSM-----------------RVPLIISGPGI-PKGKRRDALVYLQ 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 438 DVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMhycerFLHAARWHQRDRgtmWKVHFVTPvfqpegaga 516
Cdd:cd16155 274 DVFPTLCELAGIEIPES--VEGKSLLPVIRGeKKAVRDTLYGA-----YRDGQRAIRDDR---WKLIIYVP--------- 334
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1593597358 517 cygrkvcpcfGEKVVhhdppLLFDLSRDPSETHILtpASEPVFYQVMER 565
Cdd:cd16155 335 ----------GVKRT-----QLFDLKKDPDELNNL--ADEPEYQERLKK 366
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
63-447 |
8.19e-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: 120.60 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQwT 141
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPEL-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 GASGGLPTNETTFAKILKEKGYATGLIGkwhlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnLEQK 221
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------------------LLKA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 222 LNFLfqvlalvaltlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplil 301
Cdd:cd00016 112 IDET---------------------------------------------------------------------------- 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 302 qevasflkrNKHGPFLLFVSFLHVHIPLitmenFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGG 381
Cdd:cd00016 116 ---------SKEKPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593597358 382 SLENqLGNTqyggwngiYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLA 447
Cdd:cd00016 182 IDKG-HGGD--------PKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-549 |
1.30e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 124.65 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssiGYRVLQWT 141
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 142 gasggLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHChhplhhgfdhfygmpfslmgdcarwelSEKRVNLEQK 221
Cdd:cd16150 74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC---------------------------DSDEACVRTA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 222 LNFLFQvlalvaltlvagkltHLIPVSWmpviwsalsaVLLLASSY----FVgaliVHADCFLMrnhtITEQPMCFQRTT 297
Cdd:cd16150 122 IDWLRN---------------RRPDKPF----------CLYLPLIFphppYG----VEEPWFSM----IDREKLPPRRPP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 298 PLILQEVASFLK-RNKHGpfllFVSflhvhiplITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFT 376
Cdd:cd16150 169 GLRAKGKPSMLEgIEKQG----LDR--------WSEERW--RELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFF 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 377 SDHG-------------GSLENQLgntqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTV 443
Cdd:cd16150 235 SDHGdytgdyglvekwpNTFEDCL------------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPPTL 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 444 VRLAGgeVPQDRVIDGQDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHqrdrgtMWKVHFVTPVFQPEG----AGAC 517
Cdd:cd16150 290 LDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQA------MEGGHGPYDLKWPRLlqqeEPPE 357
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1593597358 518 YGRKVcpcfgeKVVHHD---------PPLLFDLSRDPSETH 549
Cdd:cd16150 358 HTKAV------MIRTRRykyvyrlyePDELYDLEADPLELH 392
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
63-466 |
7.33e-29 |
|
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: 120.18 E-value: 7.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 142
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 aSGGLPTNETTFAKILKEKGYATGLIGKWHL------GLN-CESASDHchhplhhgfDHFYGMPFSLMgdcarwELSEKR 215
Cdd:cd16156 71 -CMALGDNVKTIGQRLSDNGIHTAYIGKWHLdggdyfGNGiCPQGWDP---------DYWYDMRNYLD------ELTEEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 216 VnleqklnflfqvlalvaltlvagklthlipvswmpVIWSalsavLLLASSYfvgalivhadcflmrNHTITEQPMCFQR 295
Cdd:cd16156 135 R-----------------------------------RKSR-----RGLTSLE---------------AEGIKEEFTYGHR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 296 TTPLILQevasFLKRNKHGPFLLFVSFLHVHIPLI------TM-------------ENFLGKSLH------GLYGDNVEE 350
Cdd:cd16156 160 CTNRALD----FIEKHKDEDFFLVVSYDEPHHPFLcpkpyaSMykdfefpkgenayDDLENKPLHqrlwagAKPHEDGDK 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 351 M--------------DWMVGRILDTLDvEGLSNSTLIYfTSDHGGSLENQL----GNTQYggwngiykggkgmggwEGGI 412
Cdd:cd16156 236 GtikhplyfgcnsfvDYEIGRVLDAAD-EIAEDAWVIY-TSDHGDMLGAHKlwakGPAVY----------------DEIT 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1593597358 413 RVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLL 466
Cdd:cd16156 298 NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
62-460 |
9.34e-29 |
|
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: 118.42 E-value: 9.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSIGYRV 137
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 138 LQWTGAsgglptNETTFAKILKEKGYATGLIGKWhlgLN-CESASDHCHHPLhhGFDHFYGMPFslmgdcarwelsekrv 216
Cdd:cd16147 77 FWQNGL------ERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVG---------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 217 nleqklNFLFQVLALVALTLVAGklthliPVSWmpviwsalsavlllASSYFvgalivhadcflmrnhtiteqpmcfqrt 296
Cdd:cd16147 130 ------NSTYYNYTLSNGGNGKH------GVSY--------------PGDYL---------------------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 297 TPLILQEVASFLKR--NKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYG---------------------DNVE 349
Cdd:cd16147 156 TDVIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTpaprYANLFPNVTAPPRPPpnnpdvsdkphwlrrlpplnpTQIA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 350 EMDW--------------MVGRILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQ-YggwngiykggkgmggwEGG 411
Cdd:cd16147 236 YIDElyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHRLPPGKRTpY----------------EED 299
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1593597358 412 IRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQ 460
Cdd:cd16147 300 IRVPLLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
62-462 |
5.66e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 113.62 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 62 RPNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVS 131
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 132 SIGYrvlqWTGASGGLPtnetTFAKILKEKGYATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwel 211
Cdd:cd16153 81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH--------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 212 sekrvnLEQKLNFLFQvlALVALTLVAGKlthlipVSWMPviwsalsavlllassyfvgalivhadcflmrnhtiteqpm 291
Cdd:cd16153 114 ------LEAFQRYLKN--ANQSYKSFWGK------IAKGA---------------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 292 cfqrttplilqevasflKRNKhgPFLLFVSFLHVHIPLITMENFLGK-SLHGL--YGDNveemdwMVGRILDTLDVEGLS 368
Cdd:cd16153 140 -----------------DSDK--PFFVRLSFLQPHTPVLPPKEFRDRfDYYAFcaYGDA------QVGRAVEAFKAYSLK 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 369 N---STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmggweGGIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTV 443
Cdd:cd16153 195 QdrdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTL 261
|
410
....*....|....*....
gi 1593597358 444 VRLAGGEVPQDRVIDGQDL 462
Cdd:cd16153 262 LAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-481 |
5.73e-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: 108.45 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYR 136
Cdd:cd16035 1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 137 VlQWTgasggLPTNETTFAKILKEKGYATGLIGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrv 216
Cdd:cd16035 75 M-QPL-----LSPDVPTLGHMLRAAGYYTAYKGKWHL------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 217 nleqklnflfqvlalvaltlvagklthlipvswmpviwsalsavlllaSSYFVGALivhadcflMRNHTITEQPMCFqrt 296
Cdd:cd16035 106 ------------------------------------------------SGAAGGGY--------KRDPGIAAQAVEW--- 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 297 tpliLQEVASflKRNKHGPFLLFVSFL--H-VHIPLITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLI 373
Cdd:cd16035 127 ----LRERGA--KNADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIV 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 374 YFTSDHG------GSLENqlGNTQYGgwngiykggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLA 447
Cdd:cd16035 199 VFTSDHGemggahGLRGK--GFNAYE----------------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLA 260
|
410 420 430
....*....|....*....|....*....|....*....
gi 1593597358 448 GGEVPQDRVID----GQDLLPLLLGTAQHSDHE-FLMHY 481
Cdd:cd16035 261 GVDAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-473 |
6.62e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 109.75 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSIGYRVLQw 140
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 141 tgasgglpTNETTFAKILKE---KGYATGLIGKWHLGlNCESasdhcHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVN 217
Cdd:cd16154 78 --------SEETLLQLLIKDattAGYSSAVIGKWHLG-GNDN-----SPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 218 LEQKlnflfqvlalvalTLVAGKLTHLiPVSWmpviwsalsavlllassyfvgalivhadcflmrnhtITEQpmcfqrTT 297
Cdd:cd16154 144 TNST-------------EYATTKLTNL-AIDW------------------------------------IDQQ------TK 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 298 P--LILQEVASflkrnkHGPFllfvsflhvHIPLITMENflgKSLHGLY---GDN--------VEEMDWMVGRILDTLDV 364
Cdd:cd16154 168 PwfLWLAYNAP------HTPF---------HLPPAELHS---RSLLGDSadiEANprpyylaaIEAMDTEIGRLLASIDE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 365 EGLSNsTLIYFTSDHG--GSLENQLGNTQY-------GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPTS 435
Cdd:cd16154 230 EEREN-TIIIFIGDNGtpGQVVDLPYTRNHakgslyeGG-----------------INVPLIVSGAGV---ERANERESA 288
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1593597358 436 LM---DVFPTVVRLAGGEVPQdrVIDGQDLLPLLLGTAQHS 473
Cdd:cd16154 289 LVnatDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNAST 327
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
63-546 |
4.53e-15 |
|
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: 77.20 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyRVLQWTG 142
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESWN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 143 ASGGLPTNETTFAKILKEKGYATGLIGKwhlgLNCESAsdhchhplHHgfdhfygmpfSLMGDCARWElsekrvnleQKL 222
Cdd:cd16171 70 NYKGLDPNYPTWMDRLEKHGYHTQKYGK----LDYTSG--------HH----------SVSNRVEAWT---------RDV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 223 NFLFQVLALVALTLVAGKLTHLIpvswmpviwsalsavlllassyfvgalivhadcfLMRNHTITEqpmcfqRTTPLILQ 302
Cdd:cd16171 119 PFLLRQEGRPTVNLVGDRSTVRV----------------------------------MLKDWQNTD------KAVHWIRK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 303 EVASFLKrnkhgPFLLFVSFLHVH-IPLITM-ENFLG-KSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 379
Cdd:cd16171 159 EAPNLTQ-----PFALYLGLNLPHpYPSPSMgENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDH 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 380 GgslENQLGNTQYggwngiykggKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDG 459
Cdd:cd16171 234 G---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 460 QDLLPLLLGTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTMWKvhFVTpvfqpegagacYGRkvcpcfGE 528
Cdd:cd16171 298 YSLLPLLSESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YAD------GN 352
|
490
....*....|....*...
gi 1593597358 529 KVvhhdPPLLFDLSRDPS 546
Cdd:cd16171 353 SV----PPQLFDLSKDPD 366
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
51-463 |
6.28e-09 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 58.90 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 51 APSASSDISASRPNILLLM----ADDLgigdIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVR 126
Cdd:COG1368 223 RPTPNPFGPAKKPNVVVILlesfSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 127 SG-MVSSIGYRVLQwtgasgglptnetTFAKILKEKGYATgligkwhlglncesasdHCHHP------------LHHGFD 193
Cdd:COG1368 299 GGsPYKRPGQNNFP-------------SLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFD 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 194 HFYGMPfslmgdcarwELSEKRVNleqklnflfqvlalvaltlvagklthlipvSWmpviwsalsavlllassyfvGAli 273
Cdd:COG1368 349 EFYDRE----------DFDDPFDG------------------------------GW--------------------GV-- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 274 vhADcflmrnhtiteQPMcfqrttpliLQEVASFLKRNKhGPFLLFVsflhvhiplITMEN---F-----------LGKS 339
Cdd:COG1368 367 --SD-----------EDL---------FDKALEELEKLK-KPFFAFL---------ITLSNhgpYtlpeedkkipdYGKT 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 340 LHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQYggwngiykggkgmGGWEGGIRVPGIFR 419
Cdd:COG1368 415 TLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSP---GKTDY-------------ENPLERYRVPLLIY 478
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1593597358 420 WPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIdGQDLL 463
Cdd:COG1368 479 SPG-LKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
281-463 |
1.90e-08 |
|
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: 57.22 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 281 MRNHTITEQPMCFQRTTpLILQEVASFL-KRNKHGPFLLFVSFLHVHI------------------PLITMENFLGKSLH 341
Cdd:COG3083 348 VSLPRLHTPGGPAQRDR-QITAQWLQWLdQRDSDRPWFSYLFLDAPHAysfpadypkpfqpsedcnYLALDNESDPTPFK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 342 GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSL----ENQLG-NTQYGGWNgiykggkgmggweggIRVPG 416
Cdd:COG3083 427 NRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGhNSNFSRYQ---------------LQVPL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1593597358 417 IFRWPGVLPagRVIGEPTSLMDVFPTVV-RLAGGEVPqdrVID---GQDLL 463
Cdd:COG3083 492 VIHWPGTPP--QVISKLTSHLDIVPTLMqRLLGVQNP---ASDysqGEDLF 537
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
63-448 |
3.68e-08 |
|
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: 55.00 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 63 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSIGYRvl 138
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 139 qwtgasgglPTNETTFAKILKEKGYATGLIgkwhlglncesasdHCHHP---------LHHGFDHFYgmpfslmgDCARW 209
Cdd:cd16015 77 ---------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFY--------DLEDF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 210 ELSEKRVNleqklnflfqvlalvaltlvagklthlipvSWMpviwsalsavlllassyfvgalivhadcflmrnhtITEQ 289
Cdd:cd16015 126 PDDEKETN------------------------------GWG-----------------------------------VSDE 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 290 PMcfqrttpliLQEVASFLKRNKHGPFLLFVsflhvhiplITMENflgkslHGLYGDN---------------------- 347
Cdd:cd16015 141 SL---------FDQALEELEELKKKPFFIFL---------VTMSN------HGPYDLPeekkdeplkveedktelenyln 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 348 -VEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPa 426
Cdd:cd16015 197 aIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK- 261
|
410 420
....*....|....*....|..
gi 1593597358 427 GRVIGEPTSLMDVFPTVVRLAG 448
Cdd:cd16015 262 PKKIDRVGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
44-218 |
1.48e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 53.98 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGR 122
Cdd:COG1524 5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593597358 123 YPVRSGMVSSIGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIGKWHLGlncESASDHCHHPLHH-G 191
Cdd:COG1524 80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdG 156
|
170 180
....*....|....*....|....*....
gi 1593597358 192 FDHFYGMPFS--LMGDCARWELSEKRVNL 218
Cdd:COG1524 157 RKPLLGNPAAdrWIAAAALELLREGRPDL 185
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
87-131 |
3.49e-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: 40.10 E-value: 3.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1593597358 87 RTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVS 131
Cdd:pfam01663 19 LTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVG 64
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
346-380 |
8.82e-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: 38.56 E-value: 8.82e-03
10 20 30
....*....|....*....|....*....|....*
gi 1593597358 346 DNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG 380
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| |
