|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
38-561 |
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: 783.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGYRVLQWT 117
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 AASGGLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSDDHCHHPLHHGFDHFYGMPFTLMGDCAQWDVSEKRAGLERK 197
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 198 LNLCFHLVAFAALTLTAGKLtrLLSVSWTP----AIWSTIVAILLLTTSYSVGPLivhaDCFLMRNHSITEQPMHFQRTT 273
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLY--LGAVSKRFfvflLILSLLFISLFFLLLITNRYF----NCILMRNHEVVEQPMSLENLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 274 SRFLQEVSSFVRRNKQRPFLLFVSFLHVHTPLVTTEKFLGTSLHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTS 353
Cdd:cd16159 235 QRLTKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 354 DHGGSLESQLGNNQYGGWNGIYQGGKGMGGWEGGIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDRVI 433
Cdd:cd16159 315 DNGGHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRII 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 434 DGRDLLPLLLGKAQHSDHEFLLHYCESFLHAVRWHQRDRGAVWKVHYVTPRFHPDGAGaCYGSMVCPCSGDKVIHHEPPL 513
Cdd:cd16159 395 DGRDLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1124021505 514 LFDLSRDPSEAHALTPATEPsFYEVMERVAQAVKEHRRTLSPVPLQLD 561
Cdd:cd16159 474 LFDLSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-525 |
2.86e-160 |
|
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: 463.57 E-value: 2.86e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvssngYRVLQWT 117
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 AASGGLPTNETTFAKILQDKGYATGLIGKWHLGlncessdDH-CHHPLHHGFDHFYGMPFTLMGDCAQWDVSEKRagler 196
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 197 klnlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvgplivHADCFLMRNHSITEQPMHFQRTTSRF 276
Cdd:cd16026 144 ------------------------------------------------------GPLPPLMENEEVIEQPADQSSLTQRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 277 LQEVSSFVRRNKQRPFLLFVSFLHVHTPLVTTEKFLGTSLHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHG 356
Cdd:cd16026 170 TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 357 GSLESQL--GNNQ------YGGWNGiyqggkgmggwegGIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVP 428
Cdd:cd16026 250 PWLEYGGhgGSAGplrggkGTTWEG-------------GVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 429 QDRVIDGRDLLPLLLGKAQHSDHEFLLHYCESFLHAVRWHQrdrgavWKVHYVTPRFHPDGAGACYGsmvcpcsgdkvIH 508
Cdd:cd16026 317 EDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPGGLDP-----------TK 379
|
490
....*....|....*..
gi 1124021505 509 HEPPLLFDLSRDPSEAH 525
Cdd:cd16026 380 LEPPLLYDLEEDPGETY 396
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
38-542 |
3.26e-134 |
|
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: 399.11 E-value: 3.26e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGYrVLQWT 117
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRV-FLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 aaSGGLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSDDHCHHPLHHGFDhFYG--MPFTLMGDCAQWdvsekragle 195
Cdd:cd16160 80 --IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGtnLPFTNSWACDDT---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 196 rklnlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvGPLIVHAD---CFLMRNHSITEQPMHFQRT 272
Cdd:cd16160 147 --------------------------------------------------GRHVDFPDrsaCFLYYNDTIVEQPIQHEHL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 273 TSRFLQEVSSFVRRNKQRPFLLFVSFLHVHTPLVTTEKFLGTSLHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFT 352
Cdd:cd16160 177 TETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 353 SDHGGSLESQLGNNQYGG--------WNGiyqggkgmggwegGIRVPGIVRWPGVLPaGRVIQEPTSLMDVFPTVVQLAG 424
Cdd:cd16160 257 SDHGPHVEYCLEGGSTGGlkggkgnsWEG-------------GIRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 425 GQVPQDRVIDGRDLLPLLLGKAQhSDHEFLLHYCESFLHAVRWHQrdrgavWKVHYVTPRFHPD---GAGACYGSMVCP- 500
Cdd:cd16160 323 GTLPTDRIYDGLSITDLLLGEAD-SPHDDILYYCCSRLMAVRYGS------YKIHFKTQPLPSQeslDPNCDGGGPLSDy 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1124021505 501 -----CSGDKVIHHEPPLLFDLSRDPSEAHALTPATEPSFYEVMERV 542
Cdd:cd16160 396 ivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPSVYEHMLEAVEKL 442
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
39-583 |
2.27e-98 |
|
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: 307.83 E-value: 2.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvssngYRVLQWTA 118
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGV-----YPGVFYPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 ASGGLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSddhcHHPLHHGFDHFYGMPFTL-MGDCaqwdvsekraglerk 197
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHdQGPC--------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 198 LNL-CFhlvafaaltltagkltrllsvswtpaiWSTIVAILLLTTSYSVGPLIVhadcflmrNHSITEQPMHFQRTTSRF 276
Cdd:cd16158 138 QNLtCF---------------------------PPNIPCFGGCDQGEVPCPLFY--------NESIVQQPVDLLTLEERY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 277 LQEVSSFVRRNKQ--RPFLLFVSFLHVHTPLVTTEKFLGTSLHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSD 354
Cdd:cd16158 183 AKFAKDFIADNAKegKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 355 HGGSLESQlgnnQYGGWNGIYQgGKGMGGWEGGIRVPGIVRWPGVLPAGRVIqEPTSLMDVFPTVVQLAGGQVPqDRVID 434
Cdd:cd16158 263 NGPSTMRK----SRGGNAGLLK-CGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 435 GRDLLPLLLGKAQHSDHEFLLHYCESF----LHAVRWHQrdrgavWKVHYVTP-RFHPDGAG--ACYGSMvcpcsgdKVI 507
Cdd:cd16158 336 GVDMSPILFEQGKSPRQTFFYYPTSPDpdkgVFAVRWGK------YKAHFYTQgAAHSGTTPdkDCHPSA-------ELT 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124021505 508 HHEPPLLFDLSRDPSEAHALTpaTEPSFYEVMERVAQAVKEHRRTLSPVPLQLD-GLDNSWKPWLQPCCGLFPLCWC 583
Cdd:cd16158 403 SHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERFEASMKFGESEINkGEDPALEPCCKPGCTPKPSCCQ 477
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
22-558 |
8.95e-98 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 303.34 E-value: 8.95e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 22 FLLGARPSACSDLSGSRPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPI 101
Cdd:COG3119 7 LLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 102 RSGMVSsNGYrvlqwtAASGGLPTNETTFAKILQDKGYATGLIGKWHLglnceSSDDhchhplhhgfdhfygmpftlmgd 181
Cdd:COG3119 87 RTGVTD-NGE------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-----YLTD----------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 182 caqwdvsekraglerklnlcfhLVAFAALtltagkltrllsvswtpaiwstivailllttsysvgplivhadcflmrnhs 261
Cdd:COG3119 132 ----------------------LLTDKAI--------------------------------------------------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 262 iteqpmhfqrttsRFLQEvssfvRRNKQRPFLLFVSFLHVHTPLVTTEKFLG-----------------------TSLHG 318
Cdd:COG3119 139 -------------DFLER-----QADKDKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnlaprdlteeelRRARA 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 319 LYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHGGSLESQlgnnqygGWNG----IYQGGkgmggweggIRVPGIV 394
Cdd:COG3119 201 AYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEH-------GLRGgkgtLYEGG---------IRVPLIV 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 395 RWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDrvIDGRDLLPLLLGKAQHSDHEFLLHYCESF-LHAVRWHQrdrg 473
Cdd:COG3119 265 RWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGgNRAIRTGR---- 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 474 avWKvhYVtpRFHPDGagacygsmvcpcsgdkvihhEPPLLFDLSRDPSEAHALTpATEPsfyEVMERVAQAVKEHRRTL 553
Cdd:COG3119 339 --WK--LI--RYYDDD--------------------GPWELYDLKNDPGETNNLA-ADYP---EVVAELRALLEAWLKEL 388
|
....*
gi 1124021505 554 SPVPL 558
Cdd:COG3119 389 GDPPL 393
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
39-548 |
5.99e-97 |
|
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: 302.16 E-value: 5.99e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGM--VSSNGYRVLQW 116
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 117 TAA-----SGGLPTNETTFAKILQDKGYATGLIGKWHLGlncessDDHCHHPLHHGFDH------------FYGMPFTLM 179
Cdd:cd16144 81 TKLipppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVniggtgnggppsYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 180 GDCAQWDVSEKRAglerklnlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvgplivhadcflmrn 259
Cdd:cd16144 155 PDLEDGPEGEYLT------------------------------------------------------------------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 260 HSITeqpmhfqrttsrflQEVSSFVRRNKQRPFLLFVSFLHVHTPLVTT----EKFLGTSLHGLYGDN-------VEEMD 328
Cdd:cd16144 168 DRLT--------------DEAIDFIEQNKDKPFFLYLSHYAVHTPIQARpeliEKYEKKKKGLRKGQKnpvyaamIESLD 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 329 WMVGRVLDALDTEGLTNRTLVYFTSDHGG-SLESQLGNNQY-----------GGwngiyqggkgmggweggIRVPGIVRW 396
Cdd:cd16144 234 ESVGRILDALEELGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRW 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 397 PGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDRVIDGRDLLPLLLGKAQHSDHEFLlhycesflhavrwhqrdrgaVW 476
Cdd:cd16144 297 PGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRAL--------------------FW 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 477 kvHYvtPRFHPDGAGacygsmvcPCS----GD-KVIHH---EPPLLFDLSRDPSEAHALTpATEPsfyevmERVAQAVKE 548
Cdd:cd16144 357 --HF--PHYHGQGGR--------PASairkGDwKLIEFyedGRVELYNLKNDIGETNNLA-AEMP------EKAAELKKK 417
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
38-528 |
1.53e-96 |
|
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: 299.77 E-value: 1.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGN-TTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGYRvlqw 116
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 117 taASGGLPTNETTFAKILQDKGYATGLIGKWHLGLNcessddHCHHPLHHGFDHFYGMPFTLmgdcaqwDVSekragler 196
Cdd:cd16161 77 --SVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPFSH-------DSS-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 197 klnLCFHLVAFAALtltagkltrllsvswtpaiwstivailllttsysvgplivhadcFLMRNhsiteqpmhfqrttsrf 276
Cdd:cd16161 134 ---LADRYAQFATD--------------------------------------------FIQRA----------------- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 277 lqevssfvrRNKQRPFLLFVSFLHVHTPLVTTEKFLGTSLH-GLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDH 355
Cdd:cd16161 150 ---------SAKDRPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 356 G-----GSLESQLGNNQY---GGWNGIYQGGKGMGgweggIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQV 427
Cdd:cd16161 221 GpwevkCELAVGPGTGDWqgnLGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASL 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 428 PQDRVIDGRDLLPLLLGKAQhSDHEFLLHYCESF-----LHAVRWHQrdrgavWKVHYVTPrfhpdgagacyGSMVCPCS 502
Cdd:cd16161 296 PPGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSGAagagaLSAVRCGD------YKAHYATG-----------GALACCGS 357
|
490 500
....*....|....*....|....*.
gi 1124021505 503 GDKVIHHEPPLLFDLSRDPSEAHALT 528
Cdd:cd16161 358 TGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
39-527 |
4.19e-93 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 291.41 E-value: 4.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYG-NTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSgmvsSNGYRVLQWT 117
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRS----RLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 AASGgLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSDDHCHH----------------PLHHGFDHFYGMPftlmgd 181
Cdd:cd16143 77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 182 CAQwdvsekraglerklnlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysVGPlivhadcflmrnhs 261
Cdd:cd16143 150 ASE------------------------------------------------------------VLP-------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 262 iteqpmhfqrttsRFLQEVSSFVRRNKQ--RPFLLFVSFLHVHTPLVTTEKFLGTSLHGLYGDNVEEMDWMVGRVLDALD 339
Cdd:cd16143 156 -------------TLTDKAVEFIDQHAKkdKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 340 TEGLTNRTLVYFTSDHGGS------LESQLGNNQYGGWNG----IYQggkgmggweGGIRVPGIVRWPGVLPAGRVIQEP 409
Cdd:cd16143 223 ELGLAENTLVIFTSDNGPSpyadykELEKFGHDPSGPLRGmkadIYE---------GGHRVPFIVRWPGKIPAGSVSDQL 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 410 TSLMDVFPTVVQLAGGQVPQDRVIDGRDLLPLLLGKAQHSDHEFLLHycesflHAVRWHQRDRGAVWKVHyvtprFHPDG 489
Cdd:cd16143 294 VSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKLI-----DGTGS 362
|
490 500 510
....*....|....*....|....*....|....*....
gi 1124021505 490 AGACYgsmvcpcSGDKVIHHEPP-LLFDLSRDPSEAHAL 527
Cdd:cd16143 363 GGFSY-------PRGKEKLGLPPgQLYNLSTDPGESNNL 394
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
39-523 |
1.76e-91 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 286.35 E-value: 1.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIR---TPNINRLAAGGVRLTQHLAAASmCTPSRAAFLTGRYPIRSGMvssngYRVlQ 115
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-----TTV-G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 116 WTAASGGLPTNETTFAKILQDKGYATGLIGKWHLGlnceSSDDHchHPLHHGFDHFYGMPFTLMgDcaqwDVSEKRAgle 195
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG----DEDGR--LPTDHGFDEFYGNLYHTI-D----EEIVDKA--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 196 rklnlcfhlVAFaaltltagkltrllsvswtpaiwstivailllttsysvgplivhadcflMRNHSITEQPmhfqrttsr 275
Cdd:cd16142 140 ---------IDF-------------------------------------------------IKRNAKADKP--------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 276 flqevssfvrrnkqrpFLLFVSFLHVHTPLVTTEKFLGTSL-HGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSD 354
Cdd:cd16142 153 ----------------FFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTD 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 355 HGGSLES-----------QLGNNQYGGWngiyqggkgmggweggiRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLA 423
Cdd:cd16142 217 NGPEQDVwpdggytpfrgEKGTTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALA 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 424 GGQVP------QDRVIDGRDLLPLLLGKAQHSDHEFLLHYCESFLHAVRWHQrdrgavWKVHYVtpRFHPDGAGACYGSM 497
Cdd:cd16142 280 GAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFY 351
|
490 500
....*....|....*....|....*.
gi 1124021505 498 VCPCsgdkvihhepPLLFDLSRDPSE 523
Cdd:cd16142 352 VLTF----------PLIFNLRRDPKE 367
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
38-566 |
6.85e-90 |
|
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: 285.52 E-value: 6.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGYRVLQWT 117
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 AAS--GGLPTNETTFAKILQDKGYATGLIGKWHLGLNCEssddhcHHPLHHGFDHFYGMPftlmgDC---AQWDVSEKRA 192
Cdd:cd16157 81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NChfgPYDNKAYPNI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 193 GLERKLNLcfhlvafaaltltAGKLTRLLSVswtpaiwstivailllttsysvgplivhadcflmrNHSITEQPMhfqrt 272
Cdd:cd16157 150 PVYRDWEM-------------IGRYYEEFKI-----------------------------------DKKTGESNL----- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 273 TSRFLQEVSSFVRR--NKQRPFLLFVSFLHVHTPLVTTEKFLGTSLHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVY 350
Cdd:cd16157 177 TQIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVF 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 351 FTSDHGGSLesqLGNNQYGGWNGIYqGGKGMGGWEGGIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQD 430
Cdd:cd16157 257 FSSDNGAAL---ISAPEQGGSNGPF-LCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 431 RVIDGRDLLPLLLGKaqHSDHEFLLHYCESFLHAVRWHQrdrgavWKVHYVTprfhPDGAGACYGSMVCPCSGDKVI--- 507
Cdd:cd16157 333 RAIDGIDLLPVLLNG--KEKDRPIFYYRGDELMAVRLGQ------YKAHFWT----WSNSWEEFRKGINFCPGQNVPgvt 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124021505 508 ------HHEPPLLFDLSRDPSEAHALTPATePSFYEVMERVAQAVKEHRRTLSPVPLQLDGLDNS 566
Cdd:cd16157 401 thnqtdHTKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDLA 464
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
39-525 |
1.98e-80 |
|
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: 259.06 E-value: 1.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGYRvlqwta 118
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 ASGGLPTNETTFAKILQDKGYATGLIGKWHLGlncesSDDHCHHPLHHGFDHFYGMpftlmgdcaqwdvsekraglerkl 198
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLG-----GPGTPGHPTKQGFDYFYGY------------------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nLCfHLVA--FaaltltagkltrllsvsWTPAIW--STIVAIlllttsysVGPLIVHADcflmrnHSITEQPMHFQRTTS 274
Cdd:cd16145 126 -LD-QVHAhnY-----------------YPEYLWrnGEKVPL--------PNNVIPPLD------EGNNAGGGGGTYSHD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 275 RFLQEVSSFVRRNKQRPFLLFVSFLHVHTPLVTTE------KFLGTSLHGLYGDN---------VEEMDWMVGRVLDALD 339
Cdd:cd16145 173 LFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDdgpykyKPKDPGIYAYLPWPqpekayaamVTRLDRDVGRILALLK 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 340 TEGLTNRTLVYFTSDHGGSLESQLGN-----NQYGGWNGI----YQggkgmggweGGIRVPGIVRWPGVLPAGRVIQEPT 410
Cdd:cd16145 253 ELGIDENTLVVFTSDNGPHSEGGSEHdpdffDSNGPLRGYkrslYE---------GGIRVPFIARWPGKIPAGSVSDHPS 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 411 SLMDVFPTVVQLAGGQVPQDrvIDGRDLLPLLLGKAQHSDHEFLlhYCESFLH----AVRWHQrdrgavWKvhYVtpRFH 486
Cdd:cd16145 324 AFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG------WK--AV--RHG 389
|
490 500 510
....*....|....*....|....*....|....*....
gi 1124021505 487 PDGagacygsmvcpcsgdkvihhEPPLLFDLSRDPSEAH 525
Cdd:cd16145 390 KKD--------------------GPFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
39-437 |
3.23e-79 |
|
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: 249.66 E-value: 3.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvssngyrVLQWTA 118
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 ASGGLPTNETTFAKILQDKGYATGLIGKWHlglncessddhchhplhhgfdhfygmpftlmgdcaqwdvsekraglerkl 198
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvgplivhadcflmrNHSIteqpmhfqrttsRFLQ 278
Cdd:cd16022 103 ------------------------------------------------------------DEAI------------DFIE 110
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 279 evssfvRRNKQRPFLLFVSFLHVHTPLVttekflgtslhglYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHGGS 358
Cdd:cd16022 111 ------RRDKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDM 171
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124021505 359 LESqlgNNQYGGWNGIYQggkgmggweGGIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDrvIDGRD 437
Cdd:cd16022 172 LGD---HGLRGKKGSLYE---------GGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-486 |
1.76e-76 |
|
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: 247.51 E-value: 1.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTqHLAAASMCTPSRAAFLTGRYPIRSGmvssngyrvlqwtA 118
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY-------------V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 ASGGLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSDdhchHPLHHGFDHFygmpftlmgdCAqWDVSEKRAGLERkl 198
Cdd:cd16151 67 VFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEY----------CL-WQLTETGEKYSR-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nlcfhlvafaaltltagkltrllsvsWTPAIWSTIVAILLLTTSYSVGPLIVhadcflmrnhsiteqpmhfqrttSRFLQ 278
Cdd:cd16151 130 --------------------------PATPTFNIRNGKLLETTEGDYGPDLF-----------------------ADFLI 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 279 EvssFVRRNKQRPFLLFVSFLHVHTPLVTT------EKFLGTS--LHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVY 350
Cdd:cd16151 161 D---FIERNKDQPFFAYYPMVLVHDPFVPTpdspdwDPDDKRKkdDPEYFPDMVAYMDKLVGKLVDKLEELGLRENTIII 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 351 FTSDHG--GSLESQLGNNQYGGWNGiyqggkgmGGWEGGIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVP 428
Cdd:cd16151 238 FTGDNGthRPITSRTNGREVRGGKG--------KTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLP 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124021505 429 QDRVIDGRDLLPLLLGKAQHSDHEFLLHYcesfLHAVRWHQRDRGA---VWKvHYVTPRFH 486
Cdd:cd16151 310 EDYPLDGRSFAPQLLGKTGSPRREWIYWY----YRNPHKKFGSRFVrtkRYK-LYADGRFF 365
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
39-525 |
5.45e-76 |
|
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: 247.08 E-value: 5.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQ-HlaAASMCTPSRAAFLTGRYPIRSGMVSSNGYRVLqwt 117
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 aasggLPTNETTFAKILQDKGYATGLIGKWHLGlncessDDHCHHPLHHGFDHFY-------GMPFTLMGDcAQWDVSEK 190
Cdd:cd16146 76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLG------DNYPYRPQDRGFDEVLghggggiGQYPDYWGN-DYFDDTYY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 191 RAGLERKlnlcfhlvafaaltltagkltrllsvswtpaiwstivailllTTSYsvgplivhadCflmrnhsiteqpmhfq 270
Cdd:cd16146 144 HNGKFVK------------------------------------------TEGY----------C---------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 271 rtTSRFLQEVSSFVRRNKQRPFLLFVSFLHVHTPLVTTEKF--------LGTSLHGLYGdNVEEMDWMVGRVLDALDTEG 342
Cdd:cd16146 156 --TDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIENIDDNVGRLLAKLKELG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 343 LTNRTLVYFTSDHGGSLESQLGNNqyGGWNG----IYQGGkgmggweggIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPT 418
Cdd:cd16146 233 LEENTIVIFMSDNGPAGGVPKRFN--AGMRGkkgsVYEGG---------HRVPFFIRWPGKILAGKDVDTLTAHIDLLPT 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 419 VVQLAGGQVPQDRVIDGRDLLPLLLGKAQHSDHEFLlhycesFLHAVRW----HQRDRGAVWKVHY--VTPrfhpdgaga 492
Cdd:cd16146 302 LLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTHSGRWppppKKKRNAAVRTGRWrlVSP--------- 366
|
490 500 510
....*....|....*....|....*....|...
gi 1124021505 493 cygsmvcpcsgdkviHHEPPLLFDLSRDPSEAH 525
Cdd:cd16146 367 ---------------KGFQPELYDIENDPGEEN 384
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-527 |
1.76e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 222.06 E-value: 1.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVsSNGYRvlqwt 117
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 aasggLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSDDHCHH----PLHHGFDHFYGMpftlmgdcaqwdvsekrag 193
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 194 lerklnLCFHlvafaaltltagkltrllsVSWTPAIWSTiVAILLLTTSYSVGPLivhadcflmrnhsiTEQpmhfqrtT 273
Cdd:cd16034 131 ------ECNH-------------------DHNNPHYYDD-DGKRIYIKGYSPDAE--------------TDL-------A 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 274 SRFLQEvssfvRRNKQRPFLLFVSFLHVHTPLVT-------------------------TEKFLGTSLHGLYGdNVEEMD 328
Cdd:cd16034 164 IEYLEN-----QADKDKPFALVLSWNPPHDPYTTapeeyldmydpkklllrpnvpedkkEEAGLREDLRGYYA-MITALD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 329 WMVGRVLDALDTEGLTNRTLVYFTSDHGGSLESQlGNNQYGGWngiYQggkgmggweGGIRVPGIVRWPGVLPAGRVIQE 408
Cdd:cd16034 238 DNIGRLLDALKELGLLENTIVVFTSDHGDMLGSH-GLMNKQVP---YE---------ESIRVPFIIRYPGKIKAGRVVDL 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 409 PTSLMDVFPTVVQLAGGQVPQDrvIDGRDLLPLLLGKAQHSDHEFLLHYCESFLHAVRWHQRDRGAV----WKvhYVtpr 484
Cdd:cd16034 305 LINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtdrYT--YV--- 377
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1124021505 485 fhpdgagacygsmvcpcsgdkVIHHEPPLLFDLSRDPSEAHAL 527
Cdd:cd16034 378 ---------------------RDKNGPWLLFDNEKDPYQLNNL 399
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
39-525 |
5.65e-65 |
|
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: 217.80 E-value: 5.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAAsMCTPSRAAFLTGRYPIRSGMvssnGYRVLqWTA 118
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGM----QHGVI-LAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 ASGGLPTNETTFAKILQDKGYATGLIGKWHLGlncessddHCHH---PLHHGFDHFYGMpftLMGdcAQWDVSEKRAGLE 195
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY---YGG--AEDYYTHTSGGAN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 196 RKLNLCFHLVAFAALTlTAGKltrllsvswtpaiWSTivailllttsysvgplivhadcFLMRNHSIteqpmhfqrttsR 275
Cdd:cd16029 142 DYGNDDLRDNEEPAWD-YNGT-------------YST----------------------DLFTDRAV------------D 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 276 FLQEvssfvrRNKQRPFLLFVSFLHVHTPL----VTTEKFLGTSLHGLYGD------NVEEMDWMVGRVLDALDTEGLTN 345
Cdd:cd16029 174 IIEN------HDPSKPLFLYLAFQAVHAPLqvppEYADPYEDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKGMLD 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 346 RTLVYFTSDHGG-SLESQLGNN------QYGGWNGiyqggkgmggwegGIRVPGIVrWPGVLP--AGRVIQEPTSLMDVF 416
Cdd:cd16029 248 NTLIVFTSDNGGpTGGGDGGSNyplrggKNTLWEG-------------GVRVPAFV-WSPLLPpkRGTVSDGLMHVTDWL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 417 PTVVQLAGGQVPQDRVIDGRDLLPLLLGKAQHSDHEFLLHYcesflhavrwhqrdrgavwkvhyvtprfHPDGAGACYGS 496
Cdd:cd16029 314 PTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNI----------------------------DDITRTTGGAA 365
|
490 500 510
....*....|....*....|....*....|
gi 1124021505 497 MVcpcSGD-KVIHHEPplLFDLSRDPSEAH 525
Cdd:cd16029 366 IR---VGDwKLIVGKP--LFNIENDPCERN 390
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
39-551 |
1.96e-64 |
|
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: 215.84 E-value: 1.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGiADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvssNGYRVLQWTa 118
Cdd:cd16027 1 PNILWIIADDLS-PDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 asggLPTNETTFAKILQDKGYATGLIGKWhlglncessddhcHHPLHHGFDHFYGMPFTLMGDCAQWDVSEKRAglerkl 198
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKT-------------HYNPDAVFPFDDEMRGPDDGGRNAWDYASNAA------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvgplivhadcflmrnhsiteqpmhfqrttsRFLQ 278
Cdd:cd16027 133 ----------------------------------------------------------------------------DFLN 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 279 evssfvRRNKQRPFLLFVSFLHVHTP-LVTTEKFLGTSL------------------HGLYGDNVEEMDWMVGRVLDALD 339
Cdd:cd16027 137 ------RAKKGQPFFLWFGFHDPHRPyPPGDGEEPGYDPekvkvppylpdtpevredLADYYDEIERLDQQVGEILDELE 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 340 TEGLTNRTLVYFTSDHGGSLESQLGNNQYGGwngiyqggkgmggweggIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTV 419
Cdd:cd16027 211 EDGLLDNTIVIFTSDHGMPFPRAKGTLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTL 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 420 VQLAGGQVPQDrvIDGRDLLPLLLGKAQHSdHEFLlhYCESFLHAVR-WHQRdrgAVwkvhyVTPRFhpdgagacygsmv 498
Cdd:cd16027 274 LDLAGIEPPEY--LQGRSFLPLLKGEKDPG-RDYV--FAERDRHDETyDPIR---SV-----RTGRY------------- 327
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1124021505 499 cpcsgdKVIHH-EPPLLFDLSRDPSEAHALtpATEPSFYEVMERVAQAVKEHRR 551
Cdd:cd16027 328 ------KYIRNyMPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
37-541 |
1.31e-60 |
|
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: 207.38 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 37 SRPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGyrvlqw 116
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 117 taasGGLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSDDhchhplhhGFDHFYGMPftlmGDCAQWDVSEKRAGLER 196
Cdd:cd16031 75 ----PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFP----GQGSYYDPEFIENGKRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 197 KlnlcfhlvafaaltlTAGKLTRLLsvswtpaiwstivaillltTSYSVgplivhadcflmrnhsiteqpmhfqrttsRF 276
Cdd:cd16031 139 G---------------QKGYVTDII-------------------TDKAL-----------------------------DF 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 277 LQEvssfvrRNKQRPFLLFVSFLHVHTPLVTTEKFLGT-----------------------------SLHG--------- 318
Cdd:cd16031 156 LKE------RDKDKPFCLSLSFKAPHRPFTPAPRHRGLyedvtipepetfddddyagrpewareqrnRIRGvldgrfdtp 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 319 -LYGDNVE-------EMDWMVGRVLDALDTEGLTNRTLVYFTSDHGgsleSQLGNNQYGG-WNgIYQggkgmggweGGIR 389
Cdd:cd16031 230 eKYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNG----FFLGEHGLFDkRL-MYE---------ESIR 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 390 VPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDrvIDGRDLLPLLLGKAQHS-DHEFLLHYcesflhavrWH 468
Cdd:cd16031 296 VPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY---------YE 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 469 QRDRGAVWKVH-YVTPRFhpdgagacygsmvcpcsgdKVIH--HEPPL--LFDLSRDPSEAH--ALTPATEPSFYEVMER 541
Cdd:cd16031 365 EPNFHNVPTHEgVRTERY-------------------KYIYyyGVWDEeeLYDLKKDPLELNnlANDPEYAEVLKELRKR 425
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
39-424 |
1.61e-59 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 200.34 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGyrvlqwta 118
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 asGGLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSddhchhPLHHGFDHFYGMPFTLMGDCAQWDVsekraglerkl 198
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFGRNTGSDLYADPPDV----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvGPLIVHADCFlmrnhsiteqpmhfqrtTSRFLQ 278
Cdd:pfam00884 134 -----------------------------------------------PYNCSGGGVS-----------------DEALLD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 279 EVSSFVRRNkQRPFLLFVSFLHVHTPLVTTEKFLGT------------SLHGLYGDNVEEMDWMVGRVLDALDTEGLTNR 346
Cdd:pfam00884 150 EALEFLDNN-DKPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscseeQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124021505 347 TLVYFTSDHGGSLEsqlgnnqygGWNGIYQGGKGMGGWEGGIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAG 424
Cdd:pfam00884 229 TLVVYTSDHGESLG---------EGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
449-583 |
1.00e-57 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 189.06 E-value: 1.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 449 SDHEFLLHYCESFLHAVRWHQrdrgavWKVHYVTPRFHPDGAGACYGSmvcpcsGDKVIHHEPPLLFDLSRDPSEAHALT 528
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGS------KVPVTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1124021505 529 PATePSFYEVMERVAQAVKEHRRTLSPVPLQLDGLDNSWKPWLQPCCGLFPLCWC 583
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-521 |
2.83e-54 |
|
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: 186.98 E-value: 2.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPirsgmvSSNGYrvlqWTA 118
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYV------HETGV----WDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 ASGgLPTNETTFAKILQDKGYATGLIGKWHLglncESSDDHchhplhHGFDHfygmpftlmgdcaqwdvsekraglERkl 198
Cdd:cd16037 71 ADP-YDGDVPSWGHALRAAGYETVLIGKLHF----RGEDQR------HGFRY------------------------DR-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvgplivhadcflmrnhSITEqpmhfqrTTSRFLQ 278
Cdd:cd16037 114 --------------------------------------------------------------DVTE-------AAVDWLR 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 279 EvssfvRRNKQRPFLLFVSFLHVHTPLVTTEKFLGTSLHGL---YGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDH 355
Cdd:cd16037 125 E-----EAADDKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDH 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 356 GgsleSQLGnnQYGGW--NGIYQggkgmggweGGIRVPGIVRWPGVlPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDRvi 433
Cdd:cd16037 200 G----DMLG--ERGLWgkSTMYE---------ESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-- 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 434 DGRDLLPLLLGKAQHSD---HEFLLHYCESFLHAVRWHQrdrgavWK-VHYVtprfhpdgagacygsmvcpcsgdkvihH 509
Cdd:cd16037 262 DGRSLLPLAEGPDDPDRvvfSEYHAHGSPSGAFMLRKGR------WKyIYYV---------------------------G 308
|
490
....*....|..
gi 1124021505 510 EPPLLFDLSRDP 521
Cdd:cd16037 309 YPPQLFDLENDP 320
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
38-525 |
4.25e-53 |
|
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: 186.11 E-value: 4.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGNTtIRTPNINRLAAGGVRLTQ-HlaAASMCTPSRAAFLTGRYPIRSGMvSSNGYRVLQW 116
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 117 TAASGGLPTNETTFAKILQDKGYATGLIGKWHLglncessddhchhplhhGFDHFYgmpftlmgdcaqwdvsekragler 196
Cdd:cd16025 78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHL-----------------GPDDYY------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 197 klnlcfhlvafaaltltagkltrllsvswtpaiwstivaillLTTSYsvgplivhADcflmrnHSIteqpmhfqrttsRF 276
Cdd:cd16025 117 ------------------------------------------STDDL--------TD------KAI------------EY 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 277 LQEvssfvRRNKQRPFLLFVSFLHVHTPL----VTTEKFLGT-----------------SLhGLYGDN------------ 323
Cdd:cd16025 129 IDE-----QKAPDKPFFLYLAFGAPHAPLqapkEWIDKYKGKydagwdalreerlerqkEL-GLIPADtkltprppgvpa 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 324 ----------------------VEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHGGSLES---QLGN---NQY------G 369
Cdd:cd16025 203 wdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPgwaNASNtpfRLYkqasheG 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 370 GwngiyqggkgmggweggIRVPGIVRWP-GVLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDRV------IDGRDLLPLL 442
Cdd:cd16025 283 G-----------------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTL 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 443 LGKAQHSDHEFLlhYCESFLHAVRWHQRdrgavWKVhyVtpRFHPdgagacygsmvcpcSGDKVIHHEpplLFDLSRDPS 522
Cdd:cd16025 346 DGAAAPSRRRTQ--YFELFGNRAIRKGG-----WKA--V--ALHP--------------PPGWGDQWE---LYDLAKDPS 397
|
...
gi 1124021505 523 EAH 525
Cdd:cd16025 398 ETH 400
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-455 |
1.02e-52 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 185.50 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVsSNGYRVLqwtA 118
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVL-NNVENAG---A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 ASGGLPTNETTFAKILQDKGYATGLIGKWHLGLNCESSDDHC--HHPLHHGFDHFYgmpftlmGDCAQwDVSEKRAGLER 196
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEETPLDYGFdeYLPVETTIEYFL-------ADRAI-EMLEELAADDK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 197 KlnlcFHL-VAFaaltltagkltrllsvswtpaiwstivailllttsysVGPlivHADCF-------LMRNHSITE---- 264
Cdd:cd16033 149 P----FFLrVNF-------------------------------------WGP---HDPYIppepyldMYDPEDIPLpesf 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 265 ------QPMHFQRTTSRFLQEVSSFVRrnkQRPFLlfvsflhvhtplvttEKFLGtslhglygdNVEEMDWMVGRVLDAL 338
Cdd:cd16033 185 addfedKPYIYRRERKRWGVDTEDEED---WKEII---------------AHYWG---------YITLIDDAIGRILDAL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 339 DTEGLTNRTLVYFTSDHGGSLESQlgnnqyGGWN-GI--YQGGKgmggweggiRVPGIVRWPGVLPAGRVIQEPTSLMDV 415
Cdd:cd16033 238 EELGLADDTLVIFTSDHGDALGAH------RLWDkGPfmYEETY---------RIPLIIKWPGVIAAGQVVDEFVSLLDL 302
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1124021505 416 FPTVVQLAGGQVPQDrvIDGRDLLPLLLGK----------AQHSDHEFLL 455
Cdd:cd16033 303 APTILDLAGVDVPPK--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFYL 350
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-440 |
8.26e-48 |
|
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: 167.80 E-value: 8.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPirsgmvSSNGyrVLQW-- 116
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMP------SQHG--IHDWiv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 117 ------TAASGGLPTNETTFAKILQDKGYATGLIGKWHLGlncessDDHChhplhhgfdhfygmpftlmgdcaqwdvsek 190
Cdd:cd16149 73 egshgkTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------DDAA------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 191 raglerklnlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvgplivhadCFLMRNHSiteqpmhfq 270
Cdd:cd16149 117 ---------------------------------------------------------------DFLRRRAE--------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 271 rttsrflqevssfvrrnKQRPFLLFVSFLHVHTPlvttekflgtslHGlYGDNVEEMDWMVGRVLDALDTEGLTNRTLVY 350
Cdd:cd16149 125 -----------------AEKPFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVI 174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 351 FTSDHGGSLesqlgnNQYGGW---NGIYQGGKGMGGweggIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQV 427
Cdd:cd16149 175 FTSDNGFNM------GHHGIWgkgNGTFPLNMYDNS----VKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDP 244
|
410
....*....|...
gi 1124021505 428 PQDRVIDGRDLLP 440
Cdd:cd16149 245 PADPRLPGRSFAD 257
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
39-521 |
1.11e-47 |
|
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: 169.68 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMvssngyrvlqWTA 118
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 ASGgLPTNETTFAKILQDKGYATGLIGKWHLglncessddhCHHPLHHGFDHfygmpftlmgdcaqwdvSEKraglerkl 198
Cdd:cd16032 71 AAE-FPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFDY-----------------DEE-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nlcfhlVAFAALtltagkltrllsvswtpaiwstivailllttsysvgplivhadcflmrnhsiteqpmhfqrttsRFLQ 278
Cdd:cd16032 115 ------VAFKAV----------------------------------------------------------------QKLY 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 279 EVSsfvRRNKQRPFLLFVSFLHVHTPLVTTEKFLG----TSLHGLYGdNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSD 354
Cdd:cd16032 125 DLA---RGEDGRPFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 355 HGgsleSQLGnnQYGGWngiYQggkgMGGWEGGIRVPGIVRWPGvLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDRV-I 433
Cdd:cd16032 201 HG----DMLG--ERGLW---YK----MSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpL 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 434 DGRDLLPLLLGKAQHSDHEFLLHYC-ESFLHAVRWHQRDRgavWKVHYvtprfhpdgagacygsmvcpCSGDkvihhePP 512
Cdd:cd16032 267 DGRSLLPLLEGGDSGGEDEVISEYLaEGAVAPCVMIRRGR---WKFIY--------------------CPGD------PD 317
|
....*....
gi 1124021505 513 LLFDLSRDP 521
Cdd:cd16032 318 QLFDLEADP 326
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-440 |
1.08e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 159.64 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLgIAD-VGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRsgmvssngyrvlqWT 117
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY-------------HG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 AASGGLPTNETTFAKILQDKGYATGLIGkwhlglncessdDHCHHPLHHGFDHFYgmpftlmgdcaqwDVSEKRAGLErk 197
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAVS------------SNPHLFGGPGFDRGF-------------DTFEDFRGQE-- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 198 lnlcfhlvafaaltltagklTRLLSVSWTPAiwstivailllttsysvgplivhadcflmrnhsiteqpmhfQRTTSRFL 277
Cdd:cd16148 120 --------------------GDPGEEGDERA-----------------------------------------ERVTDRAL 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 278 QevssFVRRNKQ-RPFLLFVSFLHVHTPLvttekflgtslhgLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHG 356
Cdd:cd16148 139 E----WLDRNADdDPFFLFLHYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 357 gslESQLGNNQYGGWNGIYqggkgmggWEGGIRVPGIVRWPGVLPAGRvIQEPTSLMDVFPTVVQLAGGQVPQDrvIDGR 436
Cdd:cd16148 202 ---EEFGEHGLYWGHGSNL--------YDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SDGR 267
|
....
gi 1124021505 437 DLLP 440
Cdd:cd16148 268 SLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
39-551 |
2.20e-43 |
|
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: 160.89 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGiAD-VGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSsNGYRvlqwt 117
Cdd:cd16028 1 RNVLFITADQWR-ADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVW-NGTP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 aasggLPTNETTFAKILQDKGYATGLIGKWHLglnceSSDDHCHHPLHhgfdhfygmPFTLMGDCAQwdvsekrAGLERk 197
Cdd:cd16028 74 -----LDARHLTLALELRKAGYDPALFGYTDT-----SPDPRGLAPLD---------PRLLSYELAM-------PGFDP- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 198 lnLCFHLVAFAALTLTAgkltrllsvswtpaiWSTIVAILLLTtSYSVGPLIVHADcfLMRNHS--ITEQPMHFQRTTSr 275
Cdd:cd16028 127 --VDRLDEYPAEDSDTA---------------FLTDRAIEYLD-ERQDEPWFLHLS--YIRPHPpfVAPAPYHALYDPA- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 276 flqEVSSFVRRN------KQRPFLLF-------VSFLHVHTPLVTTEKFLGTSLHGLYGDNVEEMDWMVGRVLDALDTEG 342
Cdd:cd16028 186 ---DVPPPIRAEslaaeaAQHPLLAAfleriesLSFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 343 LTNRTLVYFTSDHGgsleSQLGNNQYGGWNGIYQGGKgmggweggiRVPGIVRWPGVL---PAGRVIQEPTSLMDVFPTV 419
Cdd:cd16028 263 QWDDTLIVFTSDHG----EQLGDHWLWGKDGFFDQAY---------RVPLIVRDPRREadaTRGQVVDAFTESVDVMPTI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 420 VQLAGGQVPQDrvIDGRDLLPLLLG-------KAQHSDHEFllhycesFLHAVRWHQRDRGavwkvhyvtprFHPDGAGA 492
Cdd:cd16028 330 LDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALG-----------LSPDECSL 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124021505 493 CygsMVcpCSGD-KVIHHE--PPLLFDLSRDPSEAHALtpATEPSFYEVMERVAQAVKEHRR 551
Cdd:cd16028 390 A---VI--RDERwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSWRM 444
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
37-451 |
9.33e-42 |
|
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: 156.19 E-value: 9.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 37 SRPNILLLMADDLGiADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGYrvlqW 116
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 117 TAASGglptNETTFAKILQDKGYATGLIGKWHlglncessddhchhplHHGFDHFYGMPftlmgdcAQWDVSEKRAGLER 196
Cdd:cd16030 76 RKVAP----DAVTLPQYFKENGYTTAGVGKIF----------------HPGIPDGDDDP-------ASWDEPPNPPGPEK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 197 KLNLCFHlvafaALTLTAGKLTRLLSVSWTPaiwstivailllttsysvGPLIVHADcflmrnHSITEQpmhfqrtTSRF 276
Cdd:cd16030 129 YPPGKLC-----PGKKGGKGGGGGPAWEAAD------------------VPDEAYPD------GKVADE-------AIEQ 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 277 LQEvssfvRRNKQRPFLLFVSFLHVHTPLVTTEKFL--------------------GTSLHGL-----YGD--------- 322
Cdd:cd16030 173 LRK-----LKDSDKPFFLAVGFYKPHLPFVAPKKYFdlyplesiplpnpfdpidlpEVAWNDLddlpkYGDipalnpgdp 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 323 ------------------NVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHGgsleSQLG-NNQYG---GWNgiyqggkg 380
Cdd:cd16030 248 kgplpdeqarelrqayyaSVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG----WHLGeHGHWGkhtLFE-------- 315
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124021505 381 mggweGGIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGgqVPQDRVIDGRDLLPLLLGKAQHSDH 451
Cdd:cd16030 316 -----EATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKD 379
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
36-549 |
1.08e-39 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 151.36 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 36 GSRPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVssnGYrvlq 115
Cdd:PRK13759 4 TKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 116 wtaASGGLPTNETTFAKILQDKGYATGLIGKWHLglncessddhchHP--LHHGFDHfygmpfTLMGDC----------A 183
Cdd:PRK13759 77 ---GDVVPWNYKNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHDGylhsgrnedkS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 184 QWD-VSEKRAGLERKlnlcfhlvafaaltlTAGKLTRLLSVSWtpaiwstivailllttsysvgplivhaDCflmrnHSI 262
Cdd:PRK13759 136 QFDfVSDYLAWLREK---------------APGKDPDLTDIGW---------------------------DC-----NSW 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 263 TEQPMHF---QRTTSRFLQEVSSFVRR-NKQRPFLLFVSFLHVHTPLVTTEKFL-------------------------G 313
Cdd:PRK13759 169 VARPWDLeerLHPTNWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 314 TSLHGLYGD---------------NVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHGgsleSQLGNNQ-------YGGw 371
Cdd:PRK13759 249 GSIDALRGNlgeeyarraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 372 ngiyqggkgmggwegGIRVPGIVRWPG---VLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDrvIDGRDLLPLLLGKA-- 446
Cdd:PRK13759 324 ---------------SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYeg 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 447 --QHSDHEfllhycesflHAVrWHQRDrgavwkvHYVTprfhpDGAgacygsmvcpcsgDKVI---HHEPPLLFDLSRDP 521
Cdd:PRK13759 387 wrPYLHGE----------HAL-GYSSD-------NYLT-----DGK-------------WKYIwfsQTGEEQLFDLKKDP 430
|
570 580
....*....|....*....|....*...
gi 1124021505 522 SEAHALTPAtePSFYEVMERVAQAVKEH 549
Cdd:PRK13759 431 HELHNLSPS--EKYQPRLREMRKKLVDH 456
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-549 |
2.58e-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: 142.37 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmVSSNGyrvlqwt 117
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG-CFRNG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 aasGGLPTNETTFAKILQDKGYATGLIGKWHLglncessddhchhplhhgfdhfygmpftlmgdcaqwdvsekrAGlerk 197
Cdd:cd16152 73 ---IPLPADEKTLAHYFRDAGYETGYVGKWHL------------------------------------------AG---- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 198 lnlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsYSVgplivhaDCFLMRnhsiteqpmhfqrtTSRFL 277
Cdd:cd16152 104 ---------------------------------------------YRV-------DALTDF--------------AIDYL 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 278 QEvssfvrRNKQRPFLLFVSFLHVH---------TPLVTTEKF------------LGTS---LHGLYGdNVEEMDWMVGR 333
Cdd:cd16152 118 DN------RQKDKPFFLFLSYLEPHhqndrdryvAPEGSAERFanfwvppdlaalPGDWaeeLPDYLG-CCERLDENVGR 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 334 VLDALDTEGLTNRTLVYFTSDHGGSLESQlgNNQYggwngiyqggkGMGGWEGGIRVPGIVRWPGVLpAGRVIQEPTSLM 413
Cdd:cd16152 191 IRDALKELGLYDNTIIVFTSDHGCHFRTR--NAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEELVSLI 256
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 414 DVFPTVVQLAGGQVPQDrvIDGRDLLPLLLGKAQHSDHEFLLHYCESFL-HAVRWHQrdrgavWKVHYVTPRFHPdgaGA 492
Cdd:cd16152 257 DLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISESQVgRAIRTDR------WKYSVAAPDKDG---WK 325
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124021505 493 CYGSMVcpcsgdkvihHEPPLLFDLSRDPSEAHALtpATEPSFYEVMERVAQAVKEH 549
Cdd:cd16152 326 DSGSDV----------YVEDYLYDLEADPYELVNL--IGRPEYREVAAELRERLLAR 370
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-541 |
4.84e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 141.55 E-value: 4.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 37 SRPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASM----CTPSRAAFLTGRYpirsgmvssngyr 112
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 113 VLQWTAASG-GLPTNETTFAKILQDKGYATGLIGKWHLGlncessddhchhplhhgfdhfygmpftlmgdcaqwdvsekr 191
Cdd:cd16155 68 LFHAPEGGKaAIPSDDKTWPETFKKAGYRTFATGKWHNG----------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 192 aglerklnlcfhlvafaaltltagkltrllsvswtpaiwstivailllttsysvgplivHADcflmrnhsiteqpmhfqr 271
Cdd:cd16155 107 -----------------------------------------------------------FAD------------------ 109
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 272 TTSRFLQEvssfvRRNKQRPFLLFVSFLHVHTPLVTTEKFLGtslhgLYG----------------DN------------ 323
Cdd:cd16155 110 AAIEFLEE-----YKDGDKPFFMYVAFTAPHDPRQAPPEYLD-----MYPpetiplpenflpqhpfDNgegtvrdeqlap 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 324 ------------------VEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHGGSLESQ--LG-NNQYGGwngiyqggkgmg 382
Cdd:cd16155 180 fprtpeavrqhlaeyyamITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHglMGkQNLYEH------------ 247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 383 gwegGIRVPGIVRWPGVlPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDrvIDGRDLLPLLLGKAQHsdhefllHYCESFL 462
Cdd:cd16155 248 ----SMRVPLIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKKA-------VRDTLYG 313
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 463 hAVRWHQRD-RGAVWKVHYVTPRfhpdgagacygsmvcpcsgdkvIHHEppLLFDLSRDPSEAHALtpATEPSFYEVMER 541
Cdd:cd16155 314 -AYRDGQRAiRDDRWKLIIYVPG----------------------VKRT--QLFDLKKDPDELNNL--ADEPEYQERLKK 366
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
39-442 |
1.27e-34 |
|
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: 136.74 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNgyrvlqwta 118
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNC--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 asGGLPTNETTFAKILQDKGYATGLIGKWHLglncessddhchhplhHGFDHFyGmpftlMGDCAQ-WDvSEKRAGLERK 197
Cdd:cd16156 72 --MALGDNVKTIGQRLSDNGIHTAYIGKWHL----------------DGGDYF-G-----NGICPQgWD-PDYWYDMRNY 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 198 LNlcfhlvafaalTLTAGKLTrllsvswtpaIWStivaiLLLTTSYsvgplivhadcflmrNHSITEQPMHFQRTTSRFL 277
Cdd:cd16156 127 LD-----------ELTEEERR----------KSR-----RGLTSLE---------------AEGIKEEFTYGHRCTNRAL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 278 QevssFVRRNKQRPFLLFVSFLHVHTPLVTTEKF----------LGTSLHglygDNVEE--------------------- 326
Cdd:cd16156 166 D----FIEKHKDEDFFLVVSYDEPHHPFLCPKPYasmykdfefpKGENAY----DDLENkplhqrlwagakphedgdkgt 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 327 ------------MDWMVGRVLDALDtEGLTNrTLVYFTSDHGGSLESqlgNNQYGGWNGIYQGGKgmggweggiRVPGIV 394
Cdd:cd16156 238 ikhplyfgcnsfVDYEIGRVLDAAD-EIAED-AWVIYTSDHGDMLGA---HKLWAKGPAVYDEIT---------NIPLII 303
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1124021505 395 RWPGVLPAGRVIQEPTSLMDVFPTVVQLAGgqVPQDRVIDGRDLLPLL 442
Cdd:cd16156 304 RGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
38-436 |
1.07e-33 |
|
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: 132.67 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLgiaDVGcYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYP----IRSGMVSSNGYRV 113
Cdd:cd16147 1 RPNIVLILTDDQ---DVE-LGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 114 LQWTaasgGLptNETTFAKILQDKGYATGLIGKWhlgLN-CESSDDHCHHPLhhGFDHFYGMPFTLMGDcaQWDVSEKRA 192
Cdd:cd16147 77 FWQN----GL--ERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVGNSTYY--NYTLSNGGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 193 GlerklnlcFHLVAFAALTLTagkltrllsvswtpaiwstivailllttsysvgplivhaDcfLMRNHSIteqpmhfqrt 272
Cdd:cd16147 144 G--------KHGVSYPGDYLT---------------------------------------D--VIANKAL---------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 273 tsRFLQEvssfvRRNKQRPFLLFVSFLHVHTPLVTTEKFLGTS----------------------LHGLYGDNVEEMDW- 329
Cdd:cd16147 165 --DFLRR-----AAADDKPFFLVVAPPAPHGPFTPAPRYANLFpnvtapprpppnnpdvsdkphwLRRLPPLNPTQIAYi 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 330 ----------------MVGRVLDALDTEGLTNRTLVYFTSDHGgsleSQLGN-NQYGGWNGIYQggkgmggweGGIRVPG 392
Cdd:cd16147 238 delyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNG----YHLGQhRLPPGKRTPYE---------EDIRVPL 304
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1124021505 393 IVRWPGVlPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDrvIDGR 436
Cdd:cd16147 305 LVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-546 |
2.62e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 129.28 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGiAD-VGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPirsgmvSSNGYRVLQWT 117
Cdd:cd16150 1 PNIVIFVADQLR-ADsLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYP------HVNGHRTLHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 aasggLPTNETTFAKILQDKGYATGLIGKWHLglncessddhchhplhhgfdhfygmpftLMGDCAqWDVSEKRAglerk 197
Cdd:cd16150 74 -----LRPDEPNLLKTLKDAGYHVAWAGKNDD----------------------------LPGEFA-AEAYCDSD----- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 198 lnlcfhlvafaaltltagkltrllsvswtpaiWSTIvailllttsysvgplivhadcflmrnhsiteqpmhfqRTTSRFL 277
Cdd:cd16150 115 --------------------------------EACV-------------------------------------RTAIDWL 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 278 QevssfvRRNKQRPFLLFVSFLHVHTPLVTTEKF--------------------------LGTSLHGLYGDN-------- 323
Cdd:cd16150 126 R------NRRPDKPFCLYLPLIFPHPPYGVEEPWfsmidreklpprrppglrakgkpsmlEGIEKQGLDRWSeerwrelr 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 324 ------VEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHGGslesqlgnnqYGG-------W-NGIYQGGKgmggweggiR 389
Cdd:cd16150 200 atylgmVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGD----------YTGdyglvekWpNTFEDCLT---------R 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 390 VPGIVRWPGvLPAGRVIQEPTSLMDVFPTVVQLAGgqVPQDRVIDGRDLLPLLLG-KAQHSDHEFllhyCE-SFLH---- 463
Cdd:cd16150 261 VPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHgeeq 333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 464 AVRWHQRDRGAVWKvhYVTPRFHPDGAGACygsMVCPCSGDKVI--HHEPPLLFDLSRDPSEAHALtpATEPSFYEVMER 541
Cdd:cd16150 334 AMEGGHGPYDLKWP--RLLQQEEPPEHTKA---VMIRTRRYKYVyrLYEPDELYDLEADPLELHNL--IGDPAYAEIIAE 406
|
....*
gi 1124021505 542 VAQAV 546
Cdd:cd16150 407 MKQRL 411
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
39-423 |
7.47e-32 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 123.30 E-value: 7.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRL-TQHLAAASMCTPSRAAFLTGRYPIRSGMvSSNGYRVLQWT 117
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGY-TGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 118 AASGGLPTNETTFAKILQDKGYATGLIGkwhlglncessddhchhplhhgfdhfygmpftlmgdcaqwdvsekraglerk 197
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 198 lnlcfhlvafaaltltagkltrllsvswtpaIWSTIVailllttsysvgplivhadcflmrnhsiteqpmhfqrttsrfl 277
Cdd:cd00016 108 -------------------------------LLKAID------------------------------------------- 113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 278 qevssfvRRNKQRPFLLFVSFLHVHTPLvttekFLGTSLHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHGG 357
Cdd:cd00016 114 -------ETSKEKPFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124021505 358 SLEsqlgnnqygGWNGIYQGGKGMGGWEGGIRVPGIVRWPGVlPAGRVIQEPTSLMDVFPTVVQLA 423
Cdd:cd00016 182 IDK---------GHGGDPKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-444 |
2.15e-31 |
|
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: 123.86 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVSSNGYRVlQWTa 118
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPM-QPL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 asggLPTNETTFAKILQDKGYATGLIGKWHLGlncessddhcHHPLHhGFDHfygmpftlmgdcaqwdvsekraglerkl 198
Cdd:cd16035 79 ----LSPDVPTLGHMLRAAGYYTAYKGKWHLS----------GAAGG-GYKR---------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nlcfhlvafaaltltagkltrllsvswTPAIWSTIVailllttsysvgplivhadcflmrnhsiteqpmhfqrttsRFLQ 278
Cdd:cd16035 116 ---------------------------DPGIAAQAV----------------------------------------EWLR 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 279 EVSsfVRRNKQRPFLLFVSFL--H-VHTPLVTTEKFlgTSLHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFTSDH 355
Cdd:cd16035 129 ERG--AKNADGKPWFLVVSLVnpHdIMFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDH 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 356 GGSLESQLGNNQyggWNGIYQggkgmggweGGIRVPGIVRWPGVLPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDRVID- 434
Cdd:cd16035 205 GEMGGAHGLRGK---GFNAYE---------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEAp 272
|
410
....*....|...
gi 1124021505 435 ---GRDLLPLLLG 444
Cdd:cd16035 273 plpGRDLSPLLTD 285
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-438 |
7.35e-31 |
|
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: 121.71 E-value: 7.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 38 RPNILLLMADDLGIADVGCYGN----------TTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGMVS 107
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 108 SNGYrvlqWTAASGGLPtnetTFAKILQDKGYATGLIGKWHLGlncessddhchhplhhgfdhfygmpftlmgdcaqwdv 187
Cdd:cd16153 81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSHLE------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 188 sekraglerklnlcfhlvAFAALTLTAGKltrllsvswtpaiwstivailllttsysvgplivhadcflmrnhsiteqpm 267
Cdd:cd16153 116 ------------------AFQRYLKNANQ--------------------------------------------------- 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 268 HFQRTTSRFLQEVSSfvrrnkQRPFLLFVSFLHVHTPLVTTEKFLGT-SLHGL--YGDNveemdwMVGRVLDALDTEGLT 344
Cdd:cd16153 127 SYKSFWGKIAKGADS------DKPFFVRLSFLQPHTPVLPPKEFRDRfDYYAFcaYGDA------QVGRAVEAFKAYSLK 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 345 N---RTLVYFTSDHGGSLESQLGNNQYGGWNgiyqggkgmggweGGIRVPGIVRWPGVL--PAGRVIQEPTSLMDVFPTV 419
Cdd:cd16153 195 QdrdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTL 261
|
410
....*....|....*....
gi 1124021505 420 VQLAGGQVPQDRVIDGRDL 438
Cdd:cd16153 262 LAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
39-449 |
3.50e-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: 110.52 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCY--GNTTIRTPNINRLAAGGVRLTqHLAAASMCTPSRAAFLTGRYPIRSGMvssngyrvlqw 116
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYslSSDLPVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 117 TAASGGLPTNETT--FAKILQDK--GYATGLIGKWHLGlNCESSDDHchhplHHGFDHFYGMPFTLMGDCAQWDvsekra 192
Cdd:cd16154 69 LAVPDELLLSEETllQLLIKDATtaGYSSAVIGKWHLG-GNDNSPNN-----PGGIPYYAGILGGGVQDYYNWN------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 193 glerklnlcfhlvafaaLTLTAGKLTrllsvswtpaiwSTIVAillltTSYSVGPLI-----VHADCFLMRNHSITEQPM 267
Cdd:cd16154 137 -----------------LTNNGQTTN------------STEYA-----TTKLTNLAIdwidqQTKPWFLWLAYNAPHTPF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 268 HF--QRTTSRFLQEVSSFVRRNKqRPFllfvsflhvhtplvttekflgtslhglYGDNVEEMDWMVGRVLDALDTEGLtN 345
Cdd:cd16154 183 HLppAELHSRSLLGDSADIEANP-RPY---------------------------YLAAIEAMDTEIGRLLASIDEEER-E 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 346 RTLVYFTSDHG--GSLESQLGNNQyGGWNGIYQggkgmggweGGIRVPGIVRWPGVlpaGRVIQEPTSLM---DVFPTVV 420
Cdd:cd16154 234 NTIIIFIGDNGtpGQVVDLPYTRN-HAKGSLYE---------GGINVPLIVSGAGV---ERANERESALVnatDLYATIA 300
|
410 420
....*....|....*....|....*....
gi 1124021505 421 QLAGGQVPQdrVIDGRDLLPLLLGKAQHS 449
Cdd:cd16154 301 ELAGVDAAE--IHDSVSFKPLLSDVNAST 327
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
39-522 |
1.31e-20 |
|
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: 93.76 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRAAFLTGRYPIRSGmvSSNGYRvlqwta 118
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE--SWNNYK------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 119 asgGLPTNETTFAKILQDKGYATGLIGKwhlgLNCESSddhchhplHHgfdhfygmpftlmgdcaqwdvsekraglerkl 198
Cdd:cd16171 73 ---GLDPNYPTWMDRLEKHGYHTQKYGK----LDYTSG--------HH-------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 199 nlcfhlvafaaltltagkltrllSVSWTPAIWSTIVAILLLTTSYSVGPLIVHA--DCFLMRNHSITEQPMHFQRTTSRf 276
Cdd:cd16171 106 -----------------------SVSNRVEAWTRDVPFLLRQEGRPTVNLVGDRstVRVMLKDWQNTDKAVHWIRKEAP- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 277 lqevssfvrrNKQRPFLLFVSfLHVHTPLVTT---EKFLGT-SLHGLYGDNVEEMDWMVGRVLDALDTEGLTNRTLVYFT 352
Cdd:cd16171 162 ----------NLTQPFALYLG-LNLPHPYPSPsmgENFGSIrNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 353 SDHGgslESQLGNNQYggwngiYQGGKGMGGWeggiRVPGIVRWPGVlPAGRVIQEPTSLMDVFPTVVQLAGGQVPQDrv 432
Cdd:cd16171 231 SDHG---ELAMEHRQF------YKMSMYEGSS----HVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN-- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 433 IDGRDLLPLLLGKAQHSDHEFLLH--YCESFLHAVRWHQRD---RGAVWKvhYVTprfhpdgagacYGsmvcpcSGDKVi 507
Cdd:cd16171 295 LSGYSLLPLLSESSIKESPSRVPHpdWVLSEFHGCNVNASTymlRTNSWK--YIA-----------YA------DGNSV- 354
|
490
....*....|....*
gi 1124021505 508 hhePPLLFDLSRDPS 522
Cdd:cd16171 355 ---PPQLFDLSKDPD 366
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
270-439 |
2.41e-12 |
|
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: 69.55 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 270 QRTTSRFLQEVSsfvRRNKQRPFLLFVSFLHVHT------------------PLVTTEKFLGTSLHGLYGDNVEEMDWMV 331
Cdd:COG3083 364 RQITAQWLQWLD---QRDSDRPWFSYLFLDAPHAysfpadypkpfqpsedcnYLALDNESDPTPFKNRYRNAVHYVDSQI 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 332 GRVLDALDTEGLTNRTLVYFTSDHGGSLeSQLGNNqYGGWNG---IYQggkgmggweggIRVPGIVRWPGVLPagRVIQE 408
Cdd:COG3083 441 GRVLDTLEQRGLLENTIVIITADHGEEF-NENGQN-YWGHNSnfsRYQ-----------LQVPLVIHWPGTPP--QVISK 505
|
170 180 190
....*....|....*....|....*....|....*
gi 1124021505 409 PTSLMDVFPTVVQ-LAGGQVPqdrVID---GRDLL 439
Cdd:COG3083 506 LTSHLDIVPTLMQrLLGVQNP---ASDysqGEDLF 537
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
27-439 |
6.62e-10 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 61.98 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 27 RPSACSDLSGSRPNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMcTpSRA--AFLTGRYPIRSG 104
Cdd:COG1368 223 RPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGR-T-SRGefAVLTGLPPLPGG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 105 -MVSSNGYRVLQwtaasgglptnetTFAKILQDKGYATgligkwhlglncessddHCHHP------------LHHGFDHF 171
Cdd:COG1368 301 sPYKRPGQNNFP-------------SLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFDEF 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 172 YGMPFTLMGDCAQWDVSEKraglerklnlcfHLVAFAALTLTAGKltrllsvswTPAIwstivaILLLTTSysvgplivh 251
Cdd:COG1368 351 YDREDFDDPFDGGWGVSDE------------DLFDKALEELEKLK---------KPFF------AFLITLS--------- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 252 adcflmrNHSiteqPMHFQRTTSRFLQEVSSFVrrnkqrpfllfvsflhvhtplvttEKFLGTslhglygdnVEEMDWMV 331
Cdd:COG1368 395 -------NHG----PYTLPEEDKKIPDYGKTTL------------------------NNYLNA---------VRYADQAL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 332 GRVLDALDTEGLTNRTLVYFTSDHGGSLEsqlGNNQYGGWNGIYqggkgmggweggiRVPGIVRWPGvLPAGRVIQEPTS 411
Cdd:COG1368 431 GEFIEKLKKSGWYDNTIFVIYGDHGPRSP---GKTDYENPLERY-------------RVPLLIYSPG-LKKPKVIDTVGS 493
|
410 420
....*....|....*....|....*...
gi 1124021505 412 LMDVFPTVVQLAGGQVPQDRVIdGRDLL 439
Cdd:COG1368 494 QIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
39-424 |
2.14e-09 |
|
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: 58.85 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 39 PNILLLMADDLGIADVGCYGNTTIRTPNINRLAAGGVRLTQHLAAASMCTPSRA--AFLTGRYPIRSGMVSSNGYRvlqw 116
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 117 taasgglPTNETTFAKILQDKGYATGLIgkwhlglncessddHCHHP---------LHHGFDHFYG---MPFTLMGDcAQ 184
Cdd:cd16015 77 -------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFYDledFPDDEKET-NG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 185 WDVSEKraglerklnlcfHLVAFAALTLTAGKLTRLLsvswtpaiwstivaILLLTTSysvgplivhadcflmrNHSite 264
Cdd:cd16015 135 WGVSDE------------SLFDQALEELEELKKKPFF--------------IFLVTMS----------------NHG--- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 265 qpmhfqrttsrflqevssfvrrnkqrPFLLFVSFLHVHTPLVTTEKFLGTSLHGLYgdnveEMDWMVGRVLDALDTEGLT 344
Cdd:cd16015 170 --------------------------PYDLPEEKKDEPLKVEEDKTELENYLNAIH-----YTDKALGEFIEKLKKSGLY 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 345 NRTLVYFTSDHGGSLESQLGNNQYGGWNgIYqggkgmggweggiRVPGIVRWPGVLPaGRVIQEPTSLMDVFPTVVQLAG 424
Cdd:cd16015 219 ENTIIVIYGDHLPSLGSDYDETDEDPLD-LY-------------RTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
22-356 |
8.10e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 45.12 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 22 FLLGARPSACSDLSGSRPNILLLMADDLGIADVgcygnTTIRTPNINRLAAGGVRLTQHLAAA-SMCTPSRAAFLTGRYP 100
Cdd:COG1524 7 LLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 101 IRSGMVssnGYRVlqwtaasgglptnettfakilqdkgyatgligkwhlglncessddhchhplhhgFDHFYGMPFTLMG 180
Cdd:COG1524 82 GEHGIV---GNGW------------------------------------------------------YDPELGRVVNSLS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 181 DCAQWDVSEKRAGLErKLnlcFHLVAFAALTLTAgkltrllsVSWtpaiwstivaillltTSYSVGPLIVHADCFLMRNH 260
Cdd:COG1524 105 WVEDGFGSNSLLPVP-TI---FERARAAGLTTAA--------VFW---------------PSFEGSGLIDAARPYPYDGR 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 261 SiteqPMHFQRTTSRFLQEVSSFVRRNKqRPFLLFVSFLHV----HtplvttekflgtsLHGLYGDN----VEEMDWMVG 332
Cdd:COG1524 158 K----PLLGNPAADRWIAAAALELLREG-RPDLLLVYLPDLdyagH-------------RYGPDSPEyraaLREVDAALG 219
|
330 340
....*....|....*....|....
gi 1124021505 333 RVLDALDTEGLTNRTLVYFTSDHG 356
Cdd:COG1524 220 RLLDALKARGLYEGTLVIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
268-356 |
2.69e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 40.10 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124021505 268 HFQRTTSRFLQE--VSSFVRRNKQRPFLLFVSFLHVhtplvttekflGTSLHgLYG-------DNVEEMDWMVGRVLDAL 338
Cdd:pfam01663 138 FEDRVDTAVLQTwlDLPFADVAAERPDLLLVYLEEP-----------DYAGH-RYGpdspeveDALRRVDRAIGDLLEAL 205
|
90
....*....|....*...
gi 1124021505 339 DTEGLTNRTLVYFTSDHG 356
Cdd:pfam01663 206 DERGLFEDTNVIVVSDHG 223
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
285-356 |
5.58e-03 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 39.11 E-value: 5.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124021505 285 RRNKQRPFLLFVSFLHVhtplvttekflGTSLHGlYGDN-------VEEMDWMVGRVLDALDTEGLTNRTLVYFTSDHG 356
Cdd:cd16018 151 WLDLERPDLILLYFEEP-----------DSAGHK-YGPDspevneaLKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| |
