|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
1-428 |
0e+00 |
|
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: 551.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 1 MKKTRELIGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSAAWQKTAEPFAFPVYLNKMRYQTFYC 80
Cdd:cd16147 22 MPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGGYPKFWQNGLERSTLPVWLQEAGYRTAYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 81 GKYLNQYGSKdaGGVAHVPPGWDQWHALVGNSKYYNYTLSvNGKEEKHGDSYEKDYLTDLVLNRSLHFLEERSPSH-PFF 159
Cdd:cd16147 102 GKYLNGYGVP--GGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVIANKALDFLRRAAADDkPFF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 160 MMLCPPAPHSPWTAAPQYSGSFSGVKAPR--NGSFNKPGTDKHWLLRQPanPMPNSSIDYLDNAFRRRWQTLLSVDDLVE 237
Cdd:cd16147 179 LVVAPPAPHGPFTPAPRYANLFPNVTAPPrpPPNNPDVSDKPHWLRRLP--PLNPTQIAYIDELYRKRLRTLQSVDDLVE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 238 RLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGV 317
Cdd:cd16147 257 RLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 318 NLSTVnMDGQSflpqmapslrngterpfflveytgegyssqdpscpklgpglaecfpdcvCEDAFNNTYACVRTLKGA-N 396
Cdd:cd16147 337 PPPSD-MDGRS-------------------------------------------------CGDSNNNTYKCVRTVDDTyN 366
|
410 420 430
....*....|....*....|....*....|..
gi 1207108066 397 LQYCEFADNeaFVEMYNLTADPHQLENIVKKV 428
Cdd:cd16147 367 LLYFEWCTG--FRELYDLTTDPYQLTNLAGDL 396
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
8-443 |
2.82e-80 |
|
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: 254.76 E-value: 2.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 8 IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNsvEGNcSSAAWQKTaepfaFPVYLNKMRYQTFYCGKYLNQy 87
Cdd:cd16031 34 LAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDN--NGP-LFDASQPT-----YPKLLRKAGYQTAFIGKWHLG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 88 gskdaGGVAHVPPGWDQWHALVGNSKYYNYTLSVNGKEEKhgdsyEKDYLTDLVLNRSLHFLEERSPSHPFFMMLCPPAP 167
Cdd:cd16031 105 -----SGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVG-----QKGYVTDIITDKALDFLKERDKDKPFCLSLSFKAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 168 HSPWTAAPQYSGSFSGVKAPRNGSFNkpgtDKHWLLR-QPANPMPNSSIDYLDNAFRRRW----------QTLLSVDDLV 236
Cdd:cd16031 175 HRPFTPAPRHRGLYEDVTIPEPETFD----DDDYAGRpEWAREQRNRIRGVLDGRFDTPEkyqrymkdylRTVTGVDDNV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 237 ERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIA 315
Cdd:cd16031 251 GRILDYLEEQGLADNTIIIYTSDNGFFLGEHGL-FDKRLMYEESIRVPLIIRDPRlIKAGTVVDALVLNIDFAPTILDLA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 316 GVNLSTvNMDGQSFLPQmapsLRNGTERPF---FLVEYTGEGyssqdpscpklgpglaecfpdcvcedAFNNTYAC--VR 390
Cdd:cd16031 330 GVPIPE-DMQGRSLLPL----LEGEKPVDWrkeFYYEYYEEP--------------------------NFHNVPTHegVR 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207108066 391 TLKGANLQYCEFADNEafvEMYNLTADPHQLENIVKkvDP---SLLQIMNQRLIKL 443
Cdd:cd16031 379 TERYKYIYYYGVWDEE---ELYDLKKDPLELNNLAN--DPeyaEVLKELRKRLEEL 429
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
12-450 |
1.24e-74 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 239.01 E-value: 1.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSAAWQKTaepfaFPVYLNKMRYQTFYCGKylnqygskd 91
Cdd:COG3119 59 GVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGLPPDEPT-----LAELLKEAGYRTALFGK--------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 92 aggvahvppgwdqWHAlvgnskyynytlsvngkeekhgdsyekdYLTDLVLNRSLHFLEERS-PSHPFFMMLCPPAPHSP 170
Cdd:COG3119 125 -------------WHL----------------------------YLTDLLTDKAIDFLERQAdKDKPFFLYLAFNAPHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 171 WTAAPQYSGSFSGVKAPRngsfnkpgtdkhwllrqPANPMP-NSSIDYLDNAFRRRWQTLLSVDDLVERLLKKLDSVKEL 249
Cdd:COG3119 164 YQAPEEYLDKYDGKDIPL-----------------PPNLAPrDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 250 DNTYIFYTSDHGYHTGQFSLPIDKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDGQS 328
Cdd:COG3119 227 DNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 329 FLPQmapsLRNGTE--RPFFLVEYTGEGyssqdpscpklgpglaecfpdcvcedafnnTYACVRTlkgANLQYCEFADNE 406
Cdd:COG3119 306 LLPL----LTGEKAewRDYLYWEYPRGG------------------------------GNRAIRT---GRWKLIRYYDDD 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1207108066 407 AFVEMYNLTADPHQLENIVKKvDPSLLQIMNQRLIKLQSCAGDT 450
Cdd:COG3119 349 GPWELYDLKNDPGETNNLAAD-YPEVVAELRALLEAWLKELGDP 391
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
12-438 |
5.69e-49 |
|
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: 171.54 E-value: 5.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGnCSSAAWQKTaepfaFPVYLNKMRYQTFYCGKYlnqygskd 91
Cdd:cd16027 35 GVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRG-FPLPDGVKT-----LPELLREAGYYTGLIGKT-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 92 aggvaHVPPGWDqwhalvgnskyYNYTLSVNGKEEKHGDSYEKDYLTDlvlnrslHFLEERSPSHPFFMMLCPPAPHSPW 171
Cdd:cd16027 101 -----HYNPDAV-----------FPFDDEMRGPDDGGRNAWDYASNAA-------DFLNRAKKGQPFFLWFGFHDPHRPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 172 TAAPQYSGSF--SGVKAPRNGsFNKPGTDKHWLlrqpanpmpnssiDYLDNAFRrrwqtllsVDDLVERLLKKLDSVKEL 249
Cdd:cd16027 158 PPGDGEEPGYdpEKVKVPPYL-PDTPEVREDLA-------------DYYDEIER--------LDQQVGEILDELEEDGLL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 250 DNTYIFYTSDHGYhtgqfSLPIDKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDGQS 328
Cdd:cd16027 216 DNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKPGSVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 329 FLPQMAPSlrNGTERPFFlveytgegYSSQdpscpklgpglaecfpdcvceDAFNNTYACVRTLKGANLQYCEfadNEAF 408
Cdd:cd16027 290 FLPLLKGE--KDPGRDYV--------FAER---------------------DRHDETYDPIRSVRTGRYKYIR---NYMP 335
|
410 420 430
....*....|....*....|....*....|
gi 1207108066 409 VEMYNLTADPHQLENIVKkvDPSLLQIMNQ 438
Cdd:cd16027 336 EELYDLKNDPDELNNLAD--DPEYAEVLEE 363
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
12-328 |
1.17e-48 |
|
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: 166.46 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNsVEGNCSSAAWQKTaepfaFPVYLNKMRYQTFYCGKylnqygskd 91
Cdd:cd16022 36 GVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN-VGNGGGLPPDEPT-----LAELLKEAGYRTALIGK--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 92 aggvahvppgwdqWHalvgnskyynytlsvngkeekhgdsyekdyltdlvlNRSLHFLEERSPSHPFFMMLCPPAPHSPW 171
Cdd:cd16022 101 -------------WH------------------------------------DEAIDFIERRDKDKPFFLYVSFNAPHPPF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 172 TaapqYSGsfsgvkaprngsfnkpgtdkhwllrqpanpmpnssidyldnafrrrwqTLLSVDDLVERLLKKLDSVKELDN 251
Cdd:cd16022 132 A----YYA------------------------------------------------MVSAIDDQIGRILDALEELGLLDN 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207108066 252 TYIFYTSDHGYHTGQFSLPIDKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDGQS 328
Cdd:cd16022 160 TLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGkIPAGQVSDALVSLLDLLPTLLDLAGIEPPE-GLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-424 |
2.25e-47 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 167.75 E-value: 2.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHlvhnnSVEGNCSSaaWQKTAEPFAfpVYLNKMRYQTFYCGKY-LNQYGSK 90
Cdd:cd16034 37 GVVFTNAVSNYPVCSPYRASLLTGQYPLTN-----GVFGNDVP--LPPDAPTIA--DVLKDAGYRTGYIGKWhLDGPERN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 91 DAGGVAHVPP-----GWDQWHALVGNSKYYNYTLSVNGKEEKHGDSYEKDYLTDLVLNrslhFLEERS-PSHPFFMMLCP 164
Cdd:cd16034 108 DGRADDYTPPperrhGFDYWKGYECNHDHNNPHYYDDDGKRIYIKGYSPDAETDLAIE----YLENQAdKDKPFALVLSW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 165 PAPHSPWTAAPQ-YSGSFSgvkaprngsfnkpgtDKHWLLRqpanpmPNSSIDYLDNAFRRRWQT-----LLSVDDLVER 238
Cdd:cd16034 184 NPPHDPYTTAPEeYLDMYD---------------PKKLLLR------PNVPEDKKEEAGLREDLRgyyamITALDDNIGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 239 LLKKLDSVKELDNTYIFYTSDHG---YHTGQFSlpidKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDI 314
Cdd:cd16034 243 LLDALKELGLLENTIVVFTSDHGdmlGSHGLMN----KQVPYEESIRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 315 AGVNLSTvNMDGQSFlpqmAPSLRNGTERPFFLVEY-----TGEGYSSQDPscpklgpglaecfpdcvcedafnnTYACV 389
Cdd:cd16034 319 CGLPIPD-TVEGRDL----SPLLLGGKDDEPDSVLLqcfvpFGGGSARDGG------------------------EWRGV 369
|
410 420 430
....*....|....*....|....*....|....*
gi 1207108066 390 RTLKGanlQYCEFADNEAFveMYNLTADPHQLENI 424
Cdd:cd16034 370 RTDRY---TYVRDKNGPWL--LFDNEKDPYQLNNL 399
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
12-317 |
6.60e-47 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 163.75 E-value: 6.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHlvhnnsveGNCSSAAWQKTAEPFAFPVYLNKMRYQTFYCGKYLNQYGSKD 91
Cdd:pfam00884 36 GLLFSNFYSGGTLTAPSRFALLTGLPPHNF--------GSYVSTPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 92 AGGV--AHVPPGWDQWHALVGNSKYYNYTLSVNGkeekhgdsyekdYLTDLVLNRSLHFLeeRSPSHPFFMMLCPPAPHS 169
Cdd:pfam00884 108 SPCNlgFDKFFGRNTGSDLYADPPDVPYNCSGGG------------VSDEALLDEALEFL--DNNDKPFFLVLHTLGSHG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 170 PWTAAPQYSGSFSGVKAprngsfnkpgtdkhwllrqpanpmpnsSIDYLDNAFRRRWQTLLSVDDLVERLLKKLDSVKEL 249
Cdd:pfam00884 174 PPYYPDRYPEKYATFKP---------------------------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207108066 250 DNTYIFYTSDHGYHTGQFSLPID---KRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLN-IDLPMTILDIAGV 317
Cdd:pfam00884 227 DNTLVVYTSDHGESLGEGGGYLHggkYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVShVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-440 |
1.06e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 163.55 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSAAWQKTAEpfAFPVYLNKMRYQTFYCGKY--LNQYGS 89
Cdd:cd16033 36 GVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRGLPPGVE--TFSEDLREAGYRNGYVGKWhvGPEETP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 90 KDAGGVAHVPpgwdqwhalvgnskyynytlsvngkEEKHGDSYekdyLTDLVLNRSLHFLEErspSHPFFMMLCPPAPHS 169
Cdd:cd16033 114 LDYGFDEYLP-------------------------VETTIEYF----LADRAIEMLEELAAD---DKPFFLRVNFWGPHD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 170 PWTAAPQYSGSFSGVKAPRNGSFNKPGTDKHWLLRQPANpMPNssidyLDNAFRRRWQTLLS--------VDDLVERLLK 241
Cdd:cd16033 162 PYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYRRERK-RWG-----VDTEDEEDWKEIIAhywgyitlIDDAIGRILD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 242 KLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQ-LYEFDIRIPLLVRGPGIKAK-QTLQSPVLNIDLPMTILDIAGVnL 319
Cdd:cd16033 236 ALEELGLADDTLVIFTSDHGDALGAHRL-WDKGPfMYEETYRIPLIIKWPGVIAAgQVVDEFVSLLDLAPTILDLAGV-D 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 320 STVNMDGQSFLPQmapsLRNGTERPF---FLVEYTGEGYssqdpscpklgpglaecfpdcvcedafnntYACVRTLKGAN 396
Cdd:cd16033 314 VPPKVDGRSLLPL----LRGEQPEDWrdeVVTEYNGHEF------------------------------YLPQRMVRTDR 359
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1207108066 397 LQYCEfaDNEAFVEMYNLTADPHQLENIVK-KVDPSLLQIMNQRL 440
Cdd:cd16033 360 YKYVF--NGFDIDELYDLESDPYELNNLIDdPEYEEILREMRTRL 402
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-346 |
2.48e-43 |
|
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: 157.32 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYP------HNHLVHNNSVEGNCSSAAWQKT---AEPFAFPVYLNKMRYQTFYCGK 82
Cdd:cd16144 36 GMRFTQAYAAAPVCSPSRASILTGQYParlgitDVIPGRRGPPDNTKLIPPPSTTrlpLEEVTIAEALKDAGYATAHFGK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 83 Y----LNQYGSKDAG---GVAHvppgwDQWHAlvGNSKYYNYTLSVNGKEEKhgdsYEKDYLTDLVLNRSLHFLEERSpS 155
Cdd:cd16144 116 WhlggEGGYGPEDQGfdvNIGG-----TGNGG--PPSYYFPPGKPNPDLEDG----PEGEYLTDRLTDEAIDFIEQNK-D 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 156 HPFFMMLCPPAPHSPWTAapqysgsfsgvkaprngsfnKPGTDKHWLLRQPANPMPNSSIDYLdnafrrrwqTLL-SVDD 234
Cdd:cd16144 184 KPFFLYLSHYAVHTPIQA--------------------RPELIEKYEKKKKGLRKGQKNPVYA---------AMIeSLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 235 LVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPID-------KRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNID 306
Cdd:cd16144 235 SVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSnaplrggKGSLYEGGIRVPLIVRWPGvIKPGSVSDVPVIGTD 314
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1207108066 307 LPMTILDIAGVNLSTV-NMDGQSFLPQMAPSLRNGTERPFF 346
Cdd:cd16144 315 LYPTFLELAGGPLPPPqHLDGVSLVPLLKGGEADLPRRALF 355
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
12-427 |
5.80e-37 |
|
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: 140.40 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSvegncssAAWQKTAEPFA-FPVYLNKMRYQTFYCGKYLNQYGSK 90
Cdd:cd16030 37 GVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN-------SYFRKVAPDAVtLPQYFKENGYTTAGVGKIFHPGIPD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 91 DAggvaHVPPGWDQWHALVGNSKYYNYTLSVNGKEEKHG---------DSYEKDYLTDLVLNRSLHFLEERSPSH-PFFM 160
Cdd:cd16030 110 GD----DDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpaweaaDVPDEAYPDGKVADEAIEQLRKLKDSDkPFFL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 161 mlcppA-----PHSPWTAaPQ-----YSGSfSGVKAPRNGSFNKPGTDKHwllrqPANPMPNSSIDYLDNAFRR------ 224
Cdd:cd16030 186 -----AvgfykPHLPFVA-PKkyfdlYPLE-SIPLPNPFDPIDLPEVAWN-----DLDDLPKYGDIPALNPGDPkgplpd 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 225 -RWQTLLS--------VDDLVERLLKKLDSVKELDNTYIFYTSDHGYH---TGQFSlpidKRQLYEFDIRIPLLVRGPGI 292
Cdd:cd16030 254 eQARELRQayyasvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGWHlgeHGHWG----KHTLFEEATRVPLIIRAPGV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 293 KAK-QTLQSPVLNIDL-PmTILDIAGVNlSTVNMDGQSFLPQMAPSLRNGTERPFflveytgegysSQDPSCPKLGpgla 370
Cdd:cd16030 330 TKPgKVTDALVELVDIyP-TLAELAGLP-APPCLEGKSLVPLLKNPSAKWKDAAF-----------SQYPRPSIMG---- 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207108066 371 ecfpdcvcedafnntYAcVRTlkgANLQYCEFADNEA--FVEMYNLTADPHQLENIVKK 427
Cdd:cd16030 393 ---------------YS-IRT---ERYRYTEWVDFDKvgAEELYDHKNDPNEWKNLAND 432
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-442 |
1.94e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 138.91 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHnhlvhnnsVEGNCSSAAWQKTAEPfafpVYLNKMR---YQTFYCGKylnqyg 88
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYPH--------VNGHRTLHHLLRPDEP----NLLKTLKdagYHVAWAGK------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 89 skdaggvAHVPPGWDQWhalvgnskyynytlsvngkeekhgDSYEKDylTDLVLNRSLHFLEERSPSHPFFMMLCPPAPH 168
Cdd:cd16150 98 -------NDDLPGEFAA------------------------EAYCDS--DEACVRTAIDWLRNRRPDKPFCLYLPLIFPH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 169 SPWTAAPQYSGSFSGVKAPRNgsfnKPGTDKHwllRQPANPMPNSSIDYLDNAFRRRWQTLLSV--------DDLVERLL 240
Cdd:cd16150 145 PPYGVEEPWFSMIDREKLPPR----RPPGLRA---KGKPSMLEGIEKQGLDRWSEERWRELRATylgmvsrlDHQFGRLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 241 KKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQ--LYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVN 318
Cdd:cd16150 218 EALKETGLYDDTAVFFFSDHGDYTGDYGL-VEKWPntFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 319 LSTVNMdGQSFLPQMAPSLRNGTERPF----FLVEYTG--EGYSsqDPSCPKLGPGLAECFPDCVCEdAF---NNTYACV 389
Cdd:cd16150 297 LSHTHF-GRSLLPVLAGETEEHRDAVFseggRLHGEEQamEGGH--GPYDLKWPRLLQQEEPPEHTK-AVmirTRRYKYV 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207108066 390 RTLKGANlqycefadneafvEMYNLTADPHQLENIVKkvDP---SLLQIMNQRLIK 442
Cdd:cd16150 373 YRLYEPD-------------ELYDLEADPLELHNLIG--DPayaEIIAEMKQRLLR 413
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-443 |
2.98e-35 |
|
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: 134.28 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVegncSSAAWQKT-AEpfafpvYLNKMRYQTFYCGKylnqygsk 90
Cdd:cd16152 37 GVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGI----PLPADEKTlAH------YFRDAGYETGYVGK-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 91 daggvahvppgwdqWHaLVGnskyynytlsvngkeekhgdsYEKDYLTDLVLNrslhFLEERSPSHPFFMML-------- 162
Cdd:cd16152 99 --------------WH-LAG---------------------YRVDALTDFAID----YLDNRQKDKPFFLFLsylephhq 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 163 ----CPPAPHspwtaapqysGSfsgvkAPRNGSFNKPGtDkhwLLRQPANP---MPnssiDYLdNAFRRrwqtllsVDDL 235
Cdd:cd16152 139 ndrdRYVAPE----------GS-----AERFANFWVPP-D---LAALPGDWaeeLP----DYL-GCCER-------LDEN 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 236 VERLLKKLDSVKELDNTYIFYTSDHGYH----TGQFslpidKRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTI 311
Cdd:cd16152 188 VGRIRDALKELGLYDNTIIVFTSDHGCHfrtrNAEY-----KRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 312 LDIAGVNLStVNMDGQSFLPQMAPSLRNGTERPFFLVEYTGEG---------YSSQDpscPKLGPGlaecfpdcvcEDAF 382
Cdd:cd16152 263 LDAAGIDVP-EEMQGRSLLPLVDGKVEDWRNEVFIQISESQVGrairtdrwkYSVAA---PDKDGW----------KDSG 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207108066 383 NNTYAcvrtlkganlqycefadnEAFveMYNLTADPHQLENIVKkvDPSLLQI---MNQRLIKL 443
Cdd:cd16152 329 SDVYV------------------EDY--LYDLEADPYELVNLIG--RPEYREVaaeLRERLLAR 370
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
8-334 |
6.02e-35 |
|
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: 132.28 E-value: 6.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 8 IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSvegncssAAWQKTAEpfAFPVYLNKMRYQTFYCGKylnqy 87
Cdd:cd16037 32 LAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNA-------DPYDGDVP--SWGHALRAAGYETVLIGK----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 88 gskdaggvahvppgwdqwhalvgnskyynytLSVNGKEEKHGDSYEKDyltdlVLNRSLHFLEERSPS-HPFFMMLCPPA 166
Cdd:cd16037 98 -------------------------------LHFRGEDQRHGFRYDRD-----VTEAAVDWLREEAADdKPWFLFVGFVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 167 PHSPWTAAPQysgsfsgvkaprngsfnkpgtdkHWLLrqpanpmpnssidYLDNAFRRRWQTLLSVDDLVERLLKKLDSV 246
Cdd:cd16037 142 PHFPLIAPQE-----------------------FYDL-------------YVRRARAAYYGLVEFLDENIGRVLDALEEL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 247 KELDNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDG 326
Cdd:cd16037 186 GLLDNTLIIYTSDHGDMLGERGL-WGKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPP-DLDG 263
|
....*...
gi 1207108066 327 QSFLPQMA 334
Cdd:cd16037 264 RSLLPLAE 271
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
12-357 |
2.06e-32 |
|
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: 125.38 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHnhlvhnnsvegncSSAAWQKTAEpFA-----FPVYLNKMRYQTFYCGKylnq 86
Cdd:cd16032 36 GVVFDNAYCNSPLCAPSRASMMTGRLPS-------------RIGAYDNAAE-FPadiptFAHYLRAAGYRTALSGK---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 87 ygskdaggvAH-VPPgwDQwhalvgnskyynytlsvngkeeKHGDSYEkdyltDLVLNRSLHFLEERSPSH---PFFMML 162
Cdd:cd16032 98 ---------MHfVGP--DQ----------------------LHGFDYD-----EEVAFKAVQKLYDLARGEdgrPFFLTV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 163 CPPAPHSPWTAAPQYsgsfsgvkaprngsfnkpgtdkhWLLrqpanpmpnssidYLDNAfRRRWQTLLS-VDDLVERLLK 241
Cdd:cd16032 140 SFTHPHDPYVIPQEY-----------------------WDL-------------YVRRA-RRAYYGMVSyVDDKVGQLLD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 242 KLDSVKELDNTYIFYTSDHGYHTGQFSLPIdKRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLST 321
Cdd:cd16032 183 TLERTGLADDTIVIFTSDHGDMLGERGLWY-KMSFFEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAP 261
|
330 340 350
....*....|....*....|....*....|....*...
gi 1207108066 322 VN--MDGQSFLPQMApSLRNGTERPFFlVEYTGEGYSS 357
Cdd:cd16032 262 HVppLDGRSLLPLLE-GGDSGGEDEVI-SEYLAEGAVA 297
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
12-346 |
1.11e-31 |
|
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: 125.35 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNaFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNcssaawqktaepfafpvylnKMR--------------YQT 77
Cdd:cd16146 36 SVRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWHTILGRE--------------------RMRldettlaevfkdagYRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 78 FYCGKYLN----QYGSKD----------AGGVAHVPPGWdqwhalvgNSKYYNYTLSVNGKEEKHgdsyeKDYLTDLVLN 143
Cdd:cd16146 95 GIFGKWHLgdnyPYRPQDrgfdevlghgGGGIGQYPDYW--------GNDYFDDTYYHNGKFVKT-----EGYCTDVFFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 144 RSLHFLEERSpSHPFFMMLCPPAPHSPWTAAPQYSGsfsgvkaprngsfnkpgtdkhwllrqpanpmpnssiDYLDNAFR 223
Cdd:cd16146 162 EAIDFIEENK-DKPFFAYLATNAPHGPLQVPDKYLD------------------------------------PYKDMGLD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 224 RRWQTLL----SVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGqfslpIDKR----------QLYEFDIRIPLLVRG 289
Cdd:cd16146 205 DKLAAFYgmieNIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGG-----VPKRfnagmrgkkgSVYEGGHRVPFFIRW 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207108066 290 PG-IKAKQTLQSPVLNIDLPMTILDIAGVNLS-TVNMDGQSFLPQMAPSLRNGTERPFF 346
Cdd:cd16146 280 PGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPeGIKLDGRSLLPLLKGESDPWPERTLF 338
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
10-425 |
1.15e-31 |
|
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: 125.01 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 10 DAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSA--AWQKTaepfaFPVYLNKMRYQTFYCGKYlnqy 87
Cdd:cd16143 35 AEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPLiePDRVT-----LAKMLKQAGYRTAMVGKW---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 88 gskdaggvaHVppGWDqWHALVGNSKYYNYTLSVN-GKEEKHG------DSYekdYLT------DLVLNRSLHFLEERS- 153
Cdd:cd16143 106 ---------HL--GLD-WKKKDGKKAATGTGKDVDySKPIKGGpldhgfDYY---FGIpasevlPTLTDKAVEFIDQHAk 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 154 PSHPFFMMLCPPAPHSPWTAAPQYSGSfSGvkaprngsfnkpgtdkhwllrqpANPmpnssidYLDnaFrrrwqtLLSVD 233
Cdd:cd16143 171 KDKPFFLYFALPAPHTPIVPSPEFQGK-SG-----------------------AGP-------YGD--F------VYELD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 234 DLVERLLKKLDSVKELDNTYIFYTSDHG---YHTGQFSLPID----------KRQLYEFDIRIPLLVRGPG-IKAKQTLQ 299
Cdd:cd16143 212 WVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgplrgmKADIYEGGHRVPFIVRWPGkIPAGSVSD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 300 SPVLNIDLPMTILDIAGVNL-STVNMDGQSFLPQMAPslRNGTERPFFLVEYTGEGYSS--QDPScpKLgpglaecfpdC 376
Cdd:cd16143 292 QLVSLTDLFATLAAIVGQKLpDNAAEDSFSFLPALLG--PKKQEVRESLVHHSGNGSFAirKGDW--KL----------I 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1207108066 377 VCEDAFNNTYACVRTLKGANlqycefadneaFVEMYNLTADPHQLENIV 425
Cdd:cd16143 358 DGTGSGGFSYPRGKEKLGLP-----------PGQLYNLSTDPGESNNLY 395
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-354 |
3.51e-30 |
|
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: 121.16 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYP-HNHLVHNNSVEGncssaAWQKTAEPFAFPVYLNKMRYQTFYCGKylnqYGSK 90
Cdd:cd16145 36 GMRFTQHYAGAPVCAPSRASLLTGLHTgHTRVRGNSEPGG-----QDPLPPDDVTLAEVLKKAGYATAAFGK----WGLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 91 DAGGVAHVPP-GWDQW-------HA-------LVGNSKY--YNYTLSVNGKEEKHGDSYEKDYLTDLVLNRSLHFLEERS 153
Cdd:cd16145 107 GPGTPGHPTKqGFDYFygyldqvHAhnyypeyLWRNGEKvpLPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 154 pSHPFFMMLCPPAPHSPWtAAPQYSGSFsgvkaprnGSFNKPGTDKHWLLRQPanpmpnssidyldnafRRRWQTLLS-V 232
Cdd:cd16145 187 -DKPFFLYLAYTLPHAPL-QVPDDGPYK--------YKPKDPGIYAYLPWPQP----------------EKAYAAMVTrL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 233 DDLVERLLKKLDSVKELDNTYIFYTSDHGYHT-GQFSLPID-----------KRQLYEFDIRIPLLVRGPG-IKAKQTLQ 299
Cdd:cd16145 241 DRDVGRILALLKELGIDENTLVVFTSDNGPHSeGGSEHDPDffdsngplrgyKRSLYEGGIRVPFIARWPGkIPAGSVSD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1207108066 300 SPVLNIDLPMTILDIAGVNLSTvNMDGQSFLPQMAPSLRNGTERPFFLVEYTGEG 354
Cdd:cd16145 321 HPSAFWDFMPTLADLAGAEPPE-DIDGISLLPTLLGKPQQQQHDYLYWEFYEGGG 374
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-331 |
9.34e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 119.21 E-value: 9.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAF----TSTPLCCPSRSSFLSGRYphnhlVHNNSVEGNCSSAAWQKTaepfaFPVYLNKMRYQTFYCGKylnqy 87
Cdd:cd16155 38 GTSFTNAYnmggWSGAVCVPSRAMLMTGRT-----LFHAPEGGKAAIPSDDKT-----WPETFKKAGYRTFATGK----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 88 gskdaggvahvppgwdqWHalvgnskyynytlsvNGkeekHGDSYEKdyltdlvlnrslhFLEERSPS-HPFFMMLCPPA 166
Cdd:cd16155 103 -----------------WH---------------NG----FADAAIE-------------FLEEYKDGdKPFFMYVAFTA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 167 PHSPWTAAPQYSGSFSGVKAPRNGSFnkpgtdkhwllrQPANPMPNSSI---DYLDNAFRRRWQTLLS-----------V 232
Cdd:cd16155 134 PHDPRQAPPEYLDMYPPETIPLPENF------------LPQHPFDNGEGtvrDEQLAPFPRTPEAVRQhlaeyyamithL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 233 DDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTIL 312
Cdd:cd16155 202 DAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGL-MGKQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLC 280
|
330 340
....*....|....*....|
gi 1207108066 313 DIAGVNL-STVnmDGQSFLP 331
Cdd:cd16155 281 ELAGIEIpESV--EGKSLLP 298
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
10-351 |
1.09e-29 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 120.56 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 10 DAGATFSNAFTSTPLCCPSRSSFLSGRYPHNhlvhnNSVEGNCSSAAWQ-KTaepfaFPVYLNKMRYQTFYCGKYLNQYG 88
Cdd:cd16156 34 AEGVRFDSAYTTQPVCGPARSGLFTGLYPHT-----NGSWTNCMALGDNvKT-----IGQRLSDNGIHTAYIGKWHLDGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 89 skDAGGVAHVPPGWDQ--WHALVgnskyyNY---------TLSVNGKEEKHGDSYEKDY-LTDLVLNRSLHFLEERSpSH 156
Cdd:cd16156 104 --DYFGNGICPQGWDPdyWYDMR------NYldelteeerRKSRRGLTSLEAEGIKEEFtYGHRCTNRALDFIEKHK-DE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 157 PFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPRNGSF-----NKPGTDKHWllrqpANPMPNSSIDYLD---------NAF 222
Cdd:cd16156 175 DFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAyddleNKPLHQRLW-----AGAKPHEDGDKGTikhplyfgcNSF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 223 rrrwqtllsVDDLVERLLKKLDsvKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYEFDIRIPLLVRGPG-IKAKQTLQSP 301
Cdd:cd16156 250 ---------VDYEIGRVLDAAD--EIAEDAWVIYTSDHGDMLGAHKLWAKGPAVYDEITNIPLIIRGKGgEKAGTVTDTP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1207108066 302 VLNIDLPMTILDIAGVNLSTVnMDGQSFLPQMAPslRNGTERPFFLVEYT 351
Cdd:cd16156 319 VSHIDLAPTILDYAGIPQPKV-LEGESILATIED--PEIPENRGVFVEFG 365
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
12-331 |
2.08e-29 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 119.67 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVegncssaawqktaePFA-----FPVYLNKMRYQTfycgkYLNQ 86
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT--------------PLDarhltLALELRKAGYDP-----ALFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 87 YG--SKDAGGVAHV-PPGWDQWHALVGnskyYNYTLSVNGKEEKHGDSyekDYLTDlvlnRSLHFLEERsPSHPFFMMLC 163
Cdd:cd16028 97 YTdtSPDPRGLAPLdPRLLSYELAMPG----FDPVDRLDEYPAEDSDT---AFLTD----RAIEYLDER-QDEPWFLHLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 164 PPAPHSPWTAAPQYSGSF--SGVKAP-RNGSFNKPGTD----KHWLLRQPANP--MPNSSIDYLDNAFRRRWQT----LL 230
Cdd:cd16028 165 YIRPHPPFVAPAPYHALYdpADVPPPiRAESLAAEAAQhpllAAFLERIESLSfsPGAANAADLDDEEVAQMRAtylgLI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 231 S-VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLLVRGPGIKAKQTLQS----PVLNI 305
Cdd:cd16028 245 AeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWL-WGKDGFFDQAYRVPLIVRDPRREADATRGQvvdaFTESV 323
|
330 340
....*....|....*....|....*.
gi 1207108066 306 DLPMTILDIAGVNLSTVnMDGQSFLP 331
Cdd:cd16028 324 DVMPTILDWLGGEIPHQ-CDGRSLLP 348
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-331 |
2.85e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 109.64 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSAawqKTAEPF-----AFPVYLNKMRYQTFYCGKylnq 86
Cdd:cd16149 36 GVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKT---KKPEGYlegqtTLPEVLQDAGYRCGLSGK---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 87 ygskdaggvahvppgwdqWHalVGnskyynytlsvngkeekhgdsyekDYLTDlvlnrslHFLEERSPSHPFFMMLCPPA 166
Cdd:cd16149 109 ------------------WH--LG------------------------DDAAD-------FLRRRAEAEKPFFLSVNYTA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 167 PHSPWtaapQYSGSFSGVkaprngsfnkpgtdkhwllrqpanpmpnssidyldnafrrrwqtllsvDDLVERLLKKLDSV 246
Cdd:cd16149 138 PHSPW----GYFAAVTGV------------------------------------------------DRNVGRLLDELEEL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 247 KELDNTYIFYTSDHGYHTGQFSL--------PIDkrqLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGV 317
Cdd:cd16149 166 GLTENTLVIFTSDNGFNMGHHGIwgkgngtfPLN---MYDNSVKVPFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGV 242
|
330
....*....|....*
gi 1207108066 318 NLST-VNMDGQSFLP 331
Cdd:cd16149 243 DPPAdPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-331 |
9.65e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 108.40 E-value: 9.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNnsvegncssaaWQKTAEPFAFPVYLNKMRYQTFYCGkylnqygskD 91
Cdd:cd16148 36 GVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG-----------GPLEPDDPTLAEILRKAGYYTAAVS---------S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 92 AGGVaHVPPGWDQwhalvgnskYYNYTLSVNGKEEKHGDsyEKDYLTDLVLNRSLHFLEERSPSHPFFMMLCPPAPHSPW 171
Cdd:cd16148 96 NPHL-FGGPGFDR---------GFDTFEDFRGQEGDPGE--EGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEPY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 172 taapQYSGSfsgvkaprngsfnkpgtdkhwlLRQpanpmpnssidyldnafrrrwqtllsVDDLVERLLKKLDSVKELDN 251
Cdd:cd16148 164 ----LYDAE----------------------VRY--------------------------VDEQIGRLLDKLKELGLLED 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 252 TYIFYTSDHG--------YHTGQFSLpidkrqlYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLSTVn 323
Cdd:cd16148 192 TLVIVTSDHGeefgehglYWGHGSNL-------YDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDY- 263
|
....*...
gi 1207108066 324 MDGQSFLP 331
Cdd:cd16148 264 SDGRSLLP 271
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-333 |
1.03e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 110.77 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFtSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNcssaawQKTaepfaFPVYLNKMRYQTFYCGKY--LNQYGS 89
Cdd:cd16151 36 GVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPK------QKT-----FGHLLKDAGYATAIAGKWqlGGGRGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 90 KDAggVAHVppGWDQ---WHALVGNSKYYNYTLSVNGKEEKHGDSYEK-DYLTDLVLNRSLHFLeERSPSHPFF----MM 161
Cdd:cd16151 104 GDY--PHEF--GFDEyclWQLTETGEKYSRPATPTFNIRNGKLLETTEgDYGPDLFADFLIDFI-ERNKDQPFFayypMV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 162 LcppaPHSPWTAAPQysgsfSGVKAP-RNGSFNKPGTDKHwllrqpanpMpnssIDYLdnafrrrwqtllsvDDLVERLL 240
Cdd:cd16151 179 L----VHDPFVPTPD-----SPDWDPdDKRKKDDPEYFPD---------M----VAYM--------------DKLVGKLV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 241 KKLDSVKELDNTYIFYTSDHGYHTGQFSLPID------KRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILD 313
Cdd:cd16151 223 DKLEELGLRENTIIIFTGDNGTHRPITSRTNGrevrggKGKTTDAGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAE 302
|
330 340
....*....|....*....|.
gi 1207108066 314 IAGVNL-STVNMDGQSFLPQM 333
Cdd:cd16151 303 LAGAPLpEDYPLDGRSFAPQL 323
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
10-344 |
1.59e-26 |
|
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: 110.61 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 10 DAGATFSNaFTSTPLCCPSRSSFLSGRYphNHLVHNNSVegncssaawqkTAEPFAFPVY---LNK--------MR---Y 75
Cdd:cd16025 35 AEGLRFTN-FHTTALCSPTRAALLTGRN--HHQVGMGTM-----------AELATGKPGYegyLPDsaatiaevLKdagY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 76 QTFYCGKylnqygskdaggvahvppgwdqWHalVGNSKYYnytLSvngkeekhgdsyekDYLTDlvlnRSLHFLEE-RSP 154
Cdd:cd16025 101 HTYMSGK----------------------WH--LGPDDYY---ST--------------DDLTD----KAIEYIDEqKAP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 155 SHPFFMMLCPPAPHSPWTAAPQYSGSFSGVkaprngsFNKpGTDKhwlLRQ------------PAN----PMPNSSIDY- 217
Cdd:cd16025 136 DKPFFLYLAFGAPHAPLQAPKEWIDKYKGK-------YDA-GWDA---LREerlerqkelgliPADtkltPRPPGVPAWd 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 218 -LDNAfRRRWQTLL---------SVDDLVERLLKKLDSVKELDNTYIFYTSDHG--YHTG--QFS---LPIDKRQLYEFD 280
Cdd:cd16025 205 sLSPE-EKKLEARRmevyaamveHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGG 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207108066 281 IRIPLLVRGP-GIKAKQTLQS-PVLNIDLPMTILDIAGVNL-STVN------MDGQSflpqMAPSLRNGTERP 344
Cdd:cd16025 284 IRTPLIVSWPkGIKAKGGIRHqFAHVIDIAPTILELAGVEYpKTVNgvpqlpLDGVS----LLPTLDGAAAPS 352
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-331 |
8.74e-22 |
|
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: 96.26 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFtSTPLCCPSRSSFLSGRYPHNHLVhnNSVEGNCSSaawQKTAEPFAFPVYLNKMRYQTFYCGKYlnQYGSKD 91
Cdd:cd16154 38 GIVFDNLW-ATPACSPTRATILTGKYGFRTGV--LAVPDELLL---SEETLLQLLIKDATTAGYSSAVIGKW--HLGGND 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 92 AGGVAhvPPGWDQWHALVGN--SKYYNYTLSVNGKEEKHgDSYEKDYLTDLvlnrSLHFLEERspSHPFFMMLCPPAPHS 169
Cdd:cd16154 110 NSPNN--PGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-TEYATTKLTNL----AIDWIDQQ--TKPWFLWLAYNAPHT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 170 PWTAAPQ--YSGSFSGVKAPRNgsfnkpgtdkhwllrqpANPMPNssidYLdnafrrrwQTLLSVDDLVERLLKKLDSvK 247
Cdd:cd16154 181 PFHLPPAelHSRSLLGDSADIE-----------------ANPRPY----YL--------AAIEAMDTEIGRLLASIDE-E 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 248 ELDNTYIFYTSDHGyhT-GQ-----FSLPIDKRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNI-DLPMTILDIAGVNLS 320
Cdd:cd16154 231 ERENTIIIFIGDNG--TpGQvvdlpYTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNAtDLYATIAELAGVDAA 308
|
330
....*....|.
gi 1207108066 321 TVNmDGQSFLP 331
Cdd:cd16154 309 EIH-DSVSFKP 318
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
12-357 |
1.65e-21 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 96.66 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNH-LVHNNSVegncssAAWQKTAEpfaFPVYLNKMRYQTFYCGKylnqygsk 90
Cdd:PRK13759 42 GYNFENAYSAVPSCTPARAALLTGLSQWHHgRVGYGDV------VPWNYKNT---LPQEFRDAGYYTQCIGK-------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 91 daggvAHVPPGWDQ--WHALVGNSKYynytLSVNGKEEKHGDSYEKDYL--------------TDLVLN----------- 143
Cdd:PRK13759 105 -----MHVFPQRNLlgFHNVLLHDGY----LHSGRNEDKSQFDFVSDYLawlrekapgkdpdlTDIGWDcnswvarpwdl 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 144 -RSLH-----------FLEERSPSHPFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPRNGSFNKPGTDKHWLLR-QPANPM 210
Cdd:PRK13759 176 eERLHptnwvgsesieFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADIPDPHIGDWEYAEDQDPEGgSIDALR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 211 PNSSIDYLDNAFRRRWQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLLVRGP 290
Cdd:PRK13759 256 GNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYL-FRKGYPYEGSAHIPFIIYDP 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207108066 291 G----IKAKQTLQSPVLNIDLPMTILDIAGVNLSTVnMDGQSFLPqmAPSLRNGTERPFFLVEYTgEGYSS 357
Cdd:PRK13759 335 GgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD-VDGRSLKN--LIFGQYEGWRPYLHGEHA-LGYSS 401
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
23-344 |
5.88e-20 |
|
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: 91.46 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 23 PLCCPSRSSFLSGRYPHnHLVHNNSVEGNCSSAAWQKTaEPFaFPVYLNKMRYQTFYCGKY-LNQYGSKdaggvaHVPP- 100
Cdd:cd16029 46 PICTPSRAALMTGRYPI-HTGMQHGVILAGEPYGLPLN-ETL-LPQYLKELGYATHLVGKWhLGFYTWE------YTPTn 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 101 -GWD---------QWHALVGNSKYYNYTLSVNGKEEKHGDSYEKDYLTDLVLNRSLHFLEERSPSHPFFMMLCPPAPHSP 170
Cdd:cd16029 117 rGFDsfygyyggaEDYYTHTSGGANDYGNDDLRDNEEPAWDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 171 WTAAPQYsgsfsgvkaprngsfnkpgtdkhwllrQPANPMPNSSIDYLDnafRRRWQTLLS-VDDLVERLLKKLDSVKEL 249
Cdd:cd16029 197 LQVPPEY---------------------------ADPYEDKFAHIKDED---RRTYAAMVSaLDESVGNVVDALKAKGML 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 250 DNTYIFYTSDHGYHTGQFSL----PI--DKRQLYEFDIRIPLLVRGPGIKAKqtlqSPVLN------ID-LPmTILDIAG 316
Cdd:cd16029 247 DNTLIVFTSDNGGPTGGGDGgsnyPLrgGKNTLWEGGVRVPAFVWSPLLPPK----RGTVSdglmhvTDwLP-TLLSLAG 321
|
330 340
....*....|....*....|....*....
gi 1207108066 317 VN-LSTVNMDGQSflpqMAPSLRNGTERP 344
Cdd:cd16029 322 GDpDDLPPLDGVD----QWDALSGGAPSP 346
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-334 |
3.77e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 87.65 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 3 KTRELIGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSvegncsSAAWQKTAEPfAFPVYLNKMR---YQTFY 79
Cdd:cd16035 27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTL------GSPMQPLLSP-DVPTLGHMLRaagYYTAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 80 CGKylnqygskdaggvahvppgwdqWHalvgnskyynytLSvngkeEKHGDSYEKDyltDLVLNRSLHFLEERSPSH--- 156
Cdd:cd16035 100 KGK----------------------WH------------LS-----GAAGGGYKRD---PGIAAQAVEWLRERGAKNadg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 157 -PFFMMLcppaphspwtaapqysgsfsgvkaprngSFnkpgtdkhwllrqpANP---MpnssidyLDNAFRRRWQTLLS- 231
Cdd:cd16035 138 kPWFLVV----------------------------SL--------------VNPhdiM-------FPPDDEERWRRFRNf 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 232 -------VDDLVERLLKKLDSVKELDNTYIFYTSDHG----YHTGqfslpidKRQ---LYEFDIRIPLLVRGPGIKAK-Q 296
Cdd:cd16035 169 yynlirdVDRQIGRVLDALDASGLADNTIVVFTSDHGemggAHGL-------RGKgfnAYEEALHVPLIISHPDLFGTgQ 241
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1207108066 297 TLQSPVLNIDLPMTILDIAGVNLSTVNMD-----GQSFLPQMA 334
Cdd:cd16035 242 TTDALTSHIDLLPTLLGLAGVDAEARATEapplpGRDLSPLLT 284
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
12-418 |
1.32e-18 |
|
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: 86.83 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSvegncssaawqKTAEPfAFPVYLNKMRYQtfycGKYLNQYGSKD 91
Cdd:cd16171 36 GSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNY-----------KGLDP-NYPTWMDRLEKH----GYHTQKYGKLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 92 AGGVAH-VPPGWDQWhalvgnSKYYNYTLSVNGK-------EEKHGDSYEKDY-LTDLvlnrSLHFLEERSPSH--PFFM 160
Cdd:cd16171 100 YTSGHHsVSNRVEAW------TRDVPFLLRQEGRptvnlvgDRSTVRVMLKDWqNTDK----AVHWIRKEAPNLtqPFAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 161 MLCPPAPHsPWtAAPQYSGSFSGVKAPRngsfnkpgtdkhwllrqpanpmpnssidyldnAFRrrWQTLLSVDDLVERLL 240
Cdd:cd16171 170 YLGLNLPH-PY-PSPSMGENFGSIRNIR--------------------------------AFY--YAMCAETDAMLGEII 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 241 KKLDSVKELDNTYIFYTSDHGyhtgqfSLPIDKRQ-----LYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIA 315
Cdd:cd16171 214 SALKDTGLLDKTYVFFTSDHG------ELAMEHRQfykmsMYEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 316 GVNLsTVNMDGQSFLPQMAPSLRNGTER-----PFFLVEYTGegyssqdpsCpklgpglaecfpdcvceDAFNNTYacvr 390
Cdd:cd16171 288 GVPQ-PQNLSGYSLLPLLSESSIKESPSrvphpDWVLSEFHG---------C-----------------NVNASTY---- 336
|
410 420
....*....|....*....|....*....
gi 1207108066 391 TLKGANLQYCEFAD-NEAFVEMYNLTADP 418
Cdd:cd16171 337 MLRTNSWKYIAYADgNSVPPQLFDLSKDP 365
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
12-333 |
2.83e-18 |
|
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: 86.46 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYP-----HNHLVHNNSVEGncssaawQKTAEPFaFPVYLNKMRYQTFYCGKY--- 83
Cdd:cd16026 37 GVRFTDFYAAAPVCSPSRAALLTGRYPvrvglPGVVGPPGSKGG-------LPPDEIT-IAEVLKKAGYRTALVGKWhlg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 84 -------LNQ-----YGskdaggvahVPPGWDQWHALVGNSKYYNYTLSVNGKEEKHGDSYEKDYLTDLVLNRSLHFLEe 151
Cdd:cd16026 109 hqpeflpTRHgfdeyFG---------IPYSNDMWPFPLYRNDPPGPLPPLMENEEVIEQPADQSSLTQRYTDEAVDFIE- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 152 RSPSHPFFMMLCPPAPHSPWTAAPqysgSFSGVKapRNGsfnkpgtdkhwllrqpanpmpnssiDYLDnafrrrwqTLLS 231
Cdd:cd16026 179 RNKDQPFFLYLAHTMPHVPLFASE----KFKGRS--GAG-------------------------LYGD--------VVEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 232 VDDLVERLLKKLDSVKELDNTYIFYTSDHG-----YHTGQFSLPID--KRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVL 303
Cdd:cd16026 220 LDWSVGRILDALKELGLEENTLVIFTSDNGpwleyGGHGGSAGPLRggKGTTWEGGVRVPFIAWWPGvIPAGTVSDELAS 299
|
330 340 350
....*....|....*....|....*....|.
gi 1207108066 304 NIDLPMTILDIAGVNL-STVNMDGQSFLPQM 333
Cdd:cd16026 300 TMDLLPTLAALAGAPLpEDRVIDGKDISPLL 330
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
8-327 |
4.46e-15 |
|
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: 76.42 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 8 IGDAGATFSNaFTSTPLCCPSRSSFLSGRYPhnhlvhnnsVEGNCSSAAWQK-----TAEPFAFPVYLNKMRYQTFYCGK 82
Cdd:cd16142 35 LAKEGLRFTS-FYVEPSCTPGRAAFITGRHP---------IRTGLTTVGLPGspgglPPWEPTLAELLKDAGYATAQFGK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 83 ylNQYGSKDaggvAHVPP--GWDQWHAlvgnskYYNYTLsvngkeekhgDsyekDYLTDlvlnRSLHFLEERSPS-HPFF 159
Cdd:cd16142 105 --WHLGDED----GRLPTdhGFDEFYG------NLYHTI----------D----EEIVD----KAIDFIKRNAKAdKPFF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 160 MMLCPPAPHSPWTAAPQYSGsfsgvKAPRNGsfnkpgtdkhwllrqpanpmpnssiDYLDnafrrrwqTLLSVDDLVERL 239
Cdd:cd16142 155 LYVNFTKMHFPTLPSPEFEG-----KSSGKG-------------------------KYAD--------SMVELDDHVGQI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 240 LKKLDSVKELDNTYIFYTSDHGYHtgQFSLPI--------DKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMT 310
Cdd:cd16142 197 LDALDELGIADNTIVIFTTDNGPE--QDVWPDggytpfrgEKGTTWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPT 274
|
330
....*....|....*..
gi 1207108066 311 ILDIAGVNLSTVNMDGQ 327
Cdd:cd16142 275 LAALAGAPDPKDKLLGK 291
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
12-423 |
4.71e-15 |
|
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: 76.70 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHnhlvHNNSVEGNCSSAAWQKTAEP---FAFPVYLNKMRYQTFYCGKY---LN 85
Cdd:cd16160 37 GIRFTQAYSADSVCTPSRAALLTGRLPI----RSGMYGGTRVFLPWDIGGLPkteVTMAEALKEAGYTTGMVGKWhlgIN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 86 QYGSKDAggvAHVPP--GWD----------QW----------HALVGNSKYYNYTLSVNgkeekhgDSYEKDYLTDLVLN 143
Cdd:cd16160 113 ENNHSDG---AHLPShhGFDfvgtnlpftnSWacddtgrhvdFPDRSACFLYYNDTIVE-------QPIQHEHLTETLVG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 144 RSLHFLEERSpSHPFFMMLCPPAPHSPWTAAPQYSGSfsgvkaPRNGSfnkpgtdkhwllrqpanpmpnssidYLDNAFR 223
Cdd:cd16160 183 DAKSFIEDNQ-ENPFFLYFSFPQTHTPLFASKRFKGK------SKRGR-------------------------YGDNINE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 224 RRWQTLLSVDDLVErllKKLDsvkelDNTYIFYTSDHGYH-----TGQFSLPID--KRQLYEFDIRIPLLVRGPGIKAKQ 296
Cdd:cd16160 231 MSWAVGEVLDTLVD---TGLD-----QNTLVFFLSDHGPHveyclEGGSTGGLKggKGNSWEGGIRVPFIAYWPGTIKPR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 297 TLQSPVLNIDLPMTILDIAGVNLST-VNMDGQSflpqMAPSLRNGTERP----FFLVE----------YTGEGYSSQDPS 361
Cdd:cd16160 303 VSHEVVSTMDIFPTFVDLAGGTLPTdRIYDGLS----ITDLLLGEADSPhddiLYYCCsrlmavrygsYKIHFKTQPLPS 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 362 CPKLGPglaECFPDCVCEDAFnntyacvrtlkganlqYCEFADNEAFVE-----MYNLTADP---HQLEN 423
Cdd:cd16160 379 QESLDP---NCDGGGPLSDYI----------------VCYDCEDECVTKhnpplIFDVEKDPgeqYPLQP 429
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-326 |
3.10e-13 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 69.71 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNsvegncsSAAWQKTAEPF-AFPVYLNKMRYQTFYCGK-YLNQYGS 89
Cdd:cd16153 47 GVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF-------EAAHPALDHGLpTFPEVLKKAGYQTASFGKsHLEAFQR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 90 KdaggvahvppgwdqwhaLVGNSKYYNytlSVNGKEEKHGDSyekdyltdlvlnrslhfleerspSHPFFMMLCPPAPHS 169
Cdd:cd16153 120 Y-----------------LKNANQSYK---SFWGKIAKGADS-----------------------DKPFFVRLSFLQPHT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 170 PwtaapqysgsfsgVKAPrngsfnkpgtdKHWLLRqpanpmpnssIDYldNAFrrrwqtLLSVDDLVERLLKKLDSVKEL 249
Cdd:cd16153 157 P-------------VLPP-----------KEFRDR----------FDY--YAF------CAYGDAQVGRAVEAFKAYSLK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 250 ---DNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLLVRGPGIK---AKQTLQSPVLNIDLPMTILDIAGVNLSTVN 323
Cdd:cd16153 195 qdrDYTIVYVTGDHGWHLGEQGI-LAKFTFWPQSHRVPLIVVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVDAPD 273
|
....
gi 1207108066 324 -MDG 326
Cdd:cd16153 274 yLDG 277
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
12-346 |
1.81e-12 |
|
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: 69.03 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYP-HNHLVHNNSVEGNCSSAAWQKTAEP---FAFPVYLNKMRYQTFYCGKYlnqy 87
Cdd:cd16157 37 GMLFTDFYSANPLCSPSRAALLTGRLPiRNGFYTTNAHARNAYTPQNIVGGIPdseILLPELLKKAGYRNKIVGKW---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 88 gskdagGVAHVPP------GWDQW-------HALVGNSKYYNytLSVNGKEEKHGDSYE---------KDYLTDLVLNRS 145
Cdd:cd16157 113 ------HLGHRPQyhplkhGFDEWfgapnchFGPYDNKAYPN--IPVYRDWEMIGRYYEefkidkktgESNLTQIYLQEA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 146 LHFLE-ERSPSHPFFMMLCPPAPHSPWTAAPQYSGSfsgvkaPRNGSFNkpgtdkhwllrqpanpmpnssidyldnafrr 224
Cdd:cd16157 185 LEFIEkQHDAQKPFFLYWAPDATHAPVYASKPFLGT------SQRGLYG------------------------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 225 rwQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTgqFSLPID----------KRQLYEFDIRIPLLVRGPGIKA 294
Cdd:cd16157 228 --DAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAAL--ISAPEQggsngpflcgKQTTFEGGMREPAIAWWPGHIK 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207108066 295 KQTLQSPVLNI-DLPMTILDIAGVNLST-VNMDGQSFLpqmaPSLRNGTE--RPFF 346
Cdd:cd16157 304 PGQVSHQLGSLmDLFTTSLALAGLPIPSdRAIDGIDLL----PVLLNGKEkdRPIF 355
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
106-315 |
2.60e-10 |
|
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: 60.51 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 106 HALVGNSKYYNYTLSVNGKEEKHGDSY-----EKDYLTDLVLNrsLHFLEERSPSHPFFMMLCPPAPHspwtaapqysgs 180
Cdd:cd00016 66 HGYTGNGSADPELPSRAAGKDEDGPTIpellkQAGYRTGVIGL--LKAIDETSKEKPFVLFLHFDGPD------------ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 181 fsgvkaprnGSFNKPGTDkhwllrqpanpmPNSSIDyldnafrrrwqTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDH 260
Cdd:cd00016 132 ---------GPGHAYGPN------------TPEYYD-----------AVEEIDERIGKVLDALKKAGDADDTVIIVTADH 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207108066 261 G---YHTGQFSLPIDKRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIA 315
Cdd:cd00016 180 GgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
216-330 |
1.23e-09 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 60.44 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 216 DYLDNAFRRRWQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYefdiRIPLLVRGPGIKAK 295
Cdd:COG1368 410 DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLERY----RVPLLIYSPGLKKP 485
|
90 100 110
....*....|....*....|....*....|....*
gi 1207108066 296 QTLQSPVLNIDLPMTILDIAGVNLSTVNMDGQSFL 330
Cdd:COG1368 486 KVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLL 520
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
236-352 |
3.00e-07 |
|
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: 52.68 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 236 VERLLKKLDSVKELDNTYIFYTSDHGYHTGQfslpIDKRQLYE--------------FD--IRIPLLVRGPG-IKAKQTL 298
Cdd:cd16159 292 VGQILDALDELGLKDNTFVYFTSDNGGHLEE----ISVGGEYGggnggiyggkkmggWEggIRVPTIVRWPGvIPPGSVI 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207108066 299 QSPVLNIDLPMTILDIAGVNLST-VNMDGQSFLPQmapsLRNGTERPF--FLVEYTG 352
Cdd:cd16159 368 DEPTSLMDIFPTVAALAGAPLPSdRIIDGRDLMPL----LTGQEKRSPheFLFHYCG 420
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
233-316 |
1.24e-06 |
|
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: 49.99 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 233 DDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYEFdiRIPLLVRGPGIKAKQTLQSPVLNIDLPMTIL 312
Cdd:cd16015 202 DKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLIYSPGLKKPKKIDRVGSQIDIAPTLL 279
|
....
gi 1207108066 313 DIAG 316
Cdd:cd16015 280 DLLG 283
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
148-312 |
3.01e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 49.52 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 148 FLEERSPSHPFFmmlcppaphspwtaapqysgSFSGVKAPRNGSFNKPgtdkHWLLRQPANPMPNSSIDYLDNA--FRRR 225
Cdd:COG3083 373 WLDQRDSDRPWF--------------------SYLFLDAPHAYSFPAD----YPKPFQPSEDCNYLALDNESDPtpFKNR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 226 WQT-LLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGY-----------HTGQFSlpidkrqlyEFDIRIPLLVRGPGiK 293
Cdd:COG3083 429 YRNaVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS---------RYQLQVPLVIHWPG-T 498
|
170
....*....|....*....
gi 1207108066 294 AKQTLQSPVLNIDLPMTIL 312
Cdd:COG3083 499 PPQVISKLTSHLDIVPTLM 517
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
12-321 |
2.85e-05 |
|
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: 46.31 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 12 GATFSNAFTSTPLCCPSRSSFLSGRYP-HNHLVHN---NSVEG---NCSSAAWQktaepfafpvyLNKMRYQTFYCGKY- 83
Cdd:cd16161 38 GTRFVDWYSAASVCSPSRASLMTGRLGlRNGVGHNflpTSVGGlplNETTLAEV-----------LRQAGYATGMIGKWh 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 84 LNQYGskdaggvAHVPpgwdqwhalvgNSKYYNYTLSVNGKEEKH-GDSYeKDYLTDLVLNRSlhfleerSPSHPFFMML 162
Cdd:cd16161 107 LGQRE-------AYLP-----------NSRGFDYYFGIPFSHDSSlADRY-AQFATDFIQRAS-------AKDRPFFLYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 163 CPPAPHSPWTAAPQysgsfsgvkaprngsfnkpgtdkhwllrqPANPMPNSSIdYLDnafrrrwqTLLSVDDLVERLLKK 242
Cdd:cd16161 161 ALAHVHVPLANLPR-----------------------------FQSPTSGRGP-YGD--------ALQEMDDLVGQIMDA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 243 LDSVKELDNTYIFYTSD---------------HGYHTGQFSLPIDKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNID 306
Cdd:cd16161 203 VKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGrIPANSTSAALVSTLD 282
|
330
....*....|....*
gi 1207108066 307 LPMTILDIAGVNLST 321
Cdd:cd16161 283 IFPTVVALAGASLPP 297
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
227-316 |
6.27e-05 |
|
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: 44.50 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 227 QTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHT----GQFSlpidkrqlYEFDIRIPLLVRGPGIKAKQTLQsPV 302
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDvgthGYDN--------ELPDMRAIFIARGPAFKKGKKLG-PF 253
|
90
....*....|....
gi 1207108066 303 LNIDLPMTILDIAG 316
Cdd:cd16018 254 RNVDIYPLMCNLLG 267
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
228-318 |
8.68e-05 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 44.15 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 228 TLLSVDDLVERLLKKLDSVKEldNTYIFYTSDHG---YHTGQF--SLPIDKRQLYEfdirIPLLV--------RGPGIKA 294
Cdd:cd16017 191 SILYTDYVLSQIIERLKKKDK--DAALIYFSDHGeslGENGLYlhGAPYAPKEQYH----VPFIIwssdsykqRYPVERL 264
|
90 100
....*....|....*....|....
gi 1207108066 295 KQTLQSPVLNIDLPMTILDIAGVN 318
Cdd:cd16017 265 RANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
229-339 |
1.74e-04 |
|
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: 43.97 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 229 LLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFS-------LPIDKRQLYEFDIRIPLLVRGPG-IKAKQT--L 298
Cdd:cd16158 232 LAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSrggnaglLKCGKGTTYEGGVREPAIAYWPGrIKPGVTheL 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207108066 299 QSpvlNIDLPMTILDIAGVNLSTVNMDGQSFLP---QMAPSLRN 339
Cdd:cd16158 312 AS---TLDILPTIAKLAGAPLPNVTLDGVDMSPilfEQGKSPRQ 352
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
214-315 |
2.07e-04 |
|
uncharacterized Alkaline phosphatase subfamily; 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.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 42.89 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 214 SIDYLDNAFRrrwqtllsVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQF----------SLPIdkrqLYefdIRI 283
Cdd:cd16021 175 THDYLNGLSL--------ADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIretlqgkleeRLPF----LS---ISL 239
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207108066 284 P--LLVRGPGIKA-----KQTLQSPvlnIDLPMTILDIA 315
Cdd:cd16021 240 PkwFREKYPEAVAnlkknSNRLTTP---FDLHATLLDIL 275
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
222-339 |
3.37e-03 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 39.63 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108066 222 FRRRWQTLLS---------VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFslpidkRQLYE--FDIRIPLLVRG- 289
Cdd:pfam02995 294 FGFFWSNSLShddfnyasaLDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKL------RRTSQgmLEERLPLMSIRy 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207108066 290 -PGIKAK-----QTLQSP----VLNIDLPMTILDIAGVNLSTVNMD-----------GQS-FLPQmaPSLRN 339
Cdd:pfam02995 368 pPWFRETypqavENLELNanrlTTPFDLHATLKDILHLGELSDKELqdrmkaldcprGISlFLPI--PDNRT 437
|
|
| |
