|
Name |
Accession |
Description |
Interval |
E-value |
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
1-385 |
2.21e-113 |
|
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: 336.40 E-value: 2.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 1 MYGLHQdvHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVGPEAVYPFDFAYTEENgsvlQVGRNITRIKLLVRKFLQTQD 80
Cdd:cd16027 66 AHGLRS--RGFPLPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPD----DGGRNAWDYASNAADFLNRAK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 81 -DRPFFLYVAFHDPHRCGHSQPQYGTFcekfgngesgmgripdwtpqaYDPLDVLVPYFVPDTPAARADLAAQYTTIGRM 159
Cdd:cd16027 140 kGQPFFLWFGFHDPHRPYPPGDGEEPG---------------------YDPEKVKVPPYLPDTPEVREDLADYYDEIERL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 160 DQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWF 239
Cdd:cd16027 199 DQQVGEILDELEEDGLLDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPGKIKP-GSVSDALVSFIDLAPTLLDLA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 240 SVPYPSYtifgsktihLTGRSLLPALEAE--PLWATVFGSQSHHEVTmSYPMRSVQHRNFRLVHNLNFkmpfpidqdfyv 317
Cdd:cd16027 278 GIEPPEY---------LQGRSFLPLLKGEkdPGRDYVFAERDRHDET-YDPIRSVRTGRYKYIRNYMP------------ 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685600221 318 sptfqdllnrttagqptgwykdlhhyyyrarWELYDQSRDPHETQNLAADPRFAQVLEMLRAQLTKWQ 385
Cdd:cd16027 336 -------------------------------EELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWM 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-391 |
2.85e-51 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 176.99 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 1 MYGLHQDVHHFNSF---------DKVRSLPLLLSQAGVRTGIIGKKHVgpeavYpFDFAYTEEngsvlqvgrnitrikll 71
Cdd:COG3119 80 LTGRYPHRTGVTDNgegyngglpPDEPTLAELLKEAGYRTALFGKWHL-----Y-LTDLLTDK----------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 72 VRKFLQTQ--DDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYDPLDVLVP-YFVPD---TPAA 145
Cdd:COG3119 137 AIDFLERQadKDKPFFLYLAFNAPHAPYQAPEEY---------------------LDKYDGKDIPLPpNLAPRdltEEEL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 146 RADLAAQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPS-----GRTNLYWPGTAEPLLVSSPEHPKRwGQ 220
Cdd:COG3119 196 RRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEhglrgGKGTLYEGGIRVPLIVRWPGKIKA-GS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 221 VSEAYVSLLDLTPTILDWFSVPYPSytifgsktiHLTGRSLLPALE-AEPLWATVFgsqsHHEVTMSYPMRSVQHRNFRL 299
Cdd:COG3119 275 VSDALVSLIDLLPTLLDLAGVPIPE---------DLDGRSLLPLLTgEKAEWRDYL----YWEYPRGGGNRAIRTGRWKL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 300 VHNlnfkmpfpidqdfyvsptfqdllnrttagqptgwykdlhhYYYRARWELYDQSRDPHETQNLAADprFAQVLEMLRA 379
Cdd:COG3119 342 IRY----------------------------------------YDDDGPWELYDLKNDPGETNNLAAD--YPEVVAELRA 379
|
410
....*....|..
gi 685600221 380 QLTKWQWETHDP 391
Cdd:COG3119 380 LLEAWLKELGDP 391
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
3-381 |
7.80e-40 |
|
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: 147.29 E-value: 7.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 3 GLHQDVHHFNSFDK------VRSLPLLLSQAGVRTGIIGKKHVGPEAVYP---FDF------------AYTEENGSVLQV 61
Cdd:cd16031 61 GQYSHRHGVTDNNGplfdasQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPppgFDYwvsfpgqgsyydPEFIENGKRVGQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 62 GRNITRIKL-LVRKFLQTQD-DRPFFLYVAFHDPHRCGHSQPQY------------GTFCEKFGNGEsgmgriPDWTpQA 127
Cdd:cd16031 141 KGYVTDIITdKALDFLKERDkDKPFCLSLSFKAPHRPFTPAPRHrglyedvtipepETFDDDDYAGR------PEWA-RE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 128 YDPLDVLVPYFVPDTPAARADLA-AQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipFPSG-------RTnLY 199
Cdd:cd16031 214 QRNRIRGVLDGRFDTPEKYQRYMkDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG--FFLGehglfdkRL-MY 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 200 WPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPSytifgsktiHLTGRSLLPALEAEPL--WAT---- 273
Cdd:cd16031 291 EESIRVPLIIRDPRLIKA-GTVVDALVLNIDFAPTILDLAGVPIPE---------DMQGRSLLPLLEGEKPvdWRKefyy 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 274 -VFGSQSHHEVTMSYPMRsvqhrnfrlvhnlnfkmpfpidqdfyvsptfqdllnrttagqpTGWYKDLHHYYYRARWELY 352
Cdd:cd16031 361 eYYEEPNFHNVPTHEGVR-------------------------------------------TERYKYIYYYGVWDEEELY 397
|
410 420
....*....|....*....|....*....
gi 685600221 353 DQSRDPHETQNLAADPRFAQVLEMLRAQL 381
Cdd:cd16031 398 DLKKDPLELNNLANDPEYAEVLKELRKRL 426
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
15-364 |
2.77e-35 |
|
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: 134.11 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 15 DKVRSLPLLLSQAGVRTGIIGKKHVGPEAVYpFDFAYTEengsvlqvgrnitriKLLvrKFLQTQ--DDRPFFLYVAF-- 90
Cdd:cd16025 86 DSAATIAEVLKDAGYHTYMSGKWHLGPDDYY-STDDLTD---------------KAI--EYIDEQkaPDKPFFLYLAFga 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 91 -HDPHrcgHSQPQY-----GTFcekfgngESG--------------MGRIPDWTPQAYDPLDVlvpyfvPD----TPAAR 146
Cdd:cd16025 148 pHAPL---QAPKEWidkykGKY-------DAGwdalreerlerqkeLGLIPADTKLTPRPPGV------PAwdslSPEEK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 147 ADL-------AAQyttIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IPFPSGRTNLYWPGTAEPL 207
Cdd:cd16025 212 KLEarrmevyAAM---VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaepgwanasnTPFRLYKQASHEGGIRTPL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 208 LVSSPEHPKRWGQVSEAYVSLLDLTPTILDWFSVPYPSyTIFGSKTIHLTGRSLLPALEAEPLWAT-------VFGSqsh 280
Cdd:cd16025 289 IVSWPKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPK-TVNGVPQLPLDGVSLLPTLDGAAAPSRrrtqyfeLFGN--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 281 hevtmsypmRSVQHRNFRLVHNlnfkmpfpidqdfyvsptfqdllnrttaGQPTGWYkdlhhyyyrARWELYDQSRDPHE 360
Cdd:cd16025 365 ---------RAIRKGGWKAVAL----------------------------HPPPGWG---------DQWELYDLAKDPSE 398
|
....
gi 685600221 361 TQNL 364
Cdd:cd16025 399 THDL 402
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-381 |
7.01e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 129.99 E-value: 7.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 17 VRSLPLLLSQAGVRTGIIGKKHVgpeavypfDFAYTEEngsvlqvgrnitrikllvrKFL--QTQDDRPFFLYVAFHDPH 94
Cdd:cd16155 83 DKTWPETFKKAGYRTFATGKWHN--------GFADAAI-------------------EFLeeYKDGDKPFFMYVAFTAPH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 95 rcghsQPQYGT--FCEKFGNGEsgmgrIPDwtPQAYDPL------------DVLVPYfvPDTPAA-RADLAAQYTTIGRM 159
Cdd:cd16155 136 -----DPRQAPpeYLDMYPPET-----IPL--PENFLPQhpfdngegtvrdEQLAPF--PRTPEAvRQHLAEYYAMITHL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 160 DQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLLDLTPTI 235
Cdd:cd16155 202 DAQIGRILDALEASGELDNTIIVFTSDHGLAVGShglmGKQNLYEHSMRVPLIISGPGIPK--GKRRDALVYLQDVFPTL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 236 LDWFSVPYPSytifgsktiHLTGRSLLPALEAEplwatvfgSQSHHEvTMSYPMRSVQhrnfRLVHNLNFKMpfpidqDF 315
Cdd:cd16155 280 CELAGIEIPE---------SVEGKSLLPVIRGE--------KKAVRD-TLYGAYRDGQ----RAIRDDRWKL------II 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685600221 316 YVSPTfqdllNRTtagqptgwykdlhhyyyrarwELYDQSRDPHETQNLAADPRFAQVLEMLRAQL 381
Cdd:cd16155 332 YVPGV-----KRT---------------------QLFDLKKDPDELNNLADEPEYQERLKKLLAEL 371
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-390 |
2.17e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 126.57 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 15 DKVRSLPLLLSQAGVRTGIIGKKHVGPEAVyPFDFAYtEENGSVLQ------VGRNITRIkllvRKFLQtqDDRPFFLYV 88
Cdd:cd16033 83 PGVETFSEDLREAGYRNGYVGKWHVGPEET-PLDYGF-DEYLPVETtieyflADRAIEML----EELAA--DDKPFFLRV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 89 AFHDPHrcghsQPqYgtfcekfgngesgmgRIPDWTPQAYDPLDVLVP--YFVP--DTPAA------------------R 146
Cdd:cd16033 155 NFWGPH-----DP-Y---------------IPPEPYLDMYDPEDIPLPesFADDfeDKPYIyrrerkrwgvdtedeedwK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 147 ADLAAQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRTNLYWPGTAE-----PLLVSSPEHpKRWGQV 221
Cdd:cd16033 214 EIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKGPFMYEetyriPLIIKWPGV-IAAGQV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 222 SEAYVSLLDLTPTILDWFSVPYPSYTifgsktihlTGRSLLPAL--EAEPLWATVFGSQSH-HEVTmsYPMRSVQHRNFR 298
Cdd:cd16033 293 VDEFVSLLDLAPTILDLAGVDVPPKV---------DGRSLLPLLrgEQPEDWRDEVVTEYNgHEFY--LPQRMVRTDRYK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 299 LVHNlnfkmPFPIDqdfyvsptfqdllnrttagqptgwykdlhhyyyrarwELYDQSRDPHETQNLAADPRFAQVLEMLR 378
Cdd:cd16033 362 YVFN-----GFDID-------------------------------------ELYDLESDPYELNNLIDDPEYEEILREMR 399
|
410
....*....|..
gi 685600221 379 AQLTKWQWETHD 390
Cdd:cd16033 400 TRLYEWMEETGD 411
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
15-260 |
4.95e-32 |
|
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: 121.39 E-value: 4.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 15 DKVRSLPLLLSQAGVRTGIIGKKHvgPEAVypfdfayteengsvlqvgrnitrikllvrKFLQTQD-DRPFFLYVAFHDP 93
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH--DEAI-----------------------------DFIERRDkDKPFFLYVSFNAP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 94 HrcghsqpqygtfcekfgngesgmgripdwTPQAYdpldvlvpyfvpdtpaaradlaaqYTTIGRMDQGVGLVLQELRDA 173
Cdd:cd16022 128 H-----------------------------PPFAY------------------------YAMVSAIDDQIGRILDALEEL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 174 GVLNDTLVIFTSDNGIPFPSGR-----TNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPSyti 248
Cdd:cd16022 155 GLLDNTLIVFTSDHGDMLGDHGlrgkkGSLYEGGIRVPFIVRWPGKIPA-GQVSDALVSLLDLLPTLLDLAGIEPPE--- 230
|
250
....*....|..
gi 685600221 249 fgsktiHLTGRS 260
Cdd:cd16022 231 ------GLDGRS 236
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
19-241 |
4.39e-31 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 120.61 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 19 SLPLLLSQAGVRTGIIGKKHVGP-----EAVYPFDFAYTEENGSVLQVGRNITRI---------KLLVRKFLQ--TQDDR 82
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWHLGWynnqsPCNLGFDKFFGRNTGSDLYADPPDVPYncsgggvsdEALLDEALEflDNNDK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 83 PFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYdpldvlvPYFVPDTPAARADLAAQYTTIGRMDQG 162
Cdd:pfam00884 161 PFFLVLHTLGSHGPPYYPDRY---------------------PEKY-------ATFKPSSCSEEQLLNSYDNTLLYTDDA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 163 VGLVLQELRDAGVLNDTLVIFTSDNGIPF--------PSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPT 234
Cdd:pfam00884 213 IGRVLDKLEENGLLDNTLVVYTSDHGESLgegggylhGGKYDNAPEGGYRVPLLIWSPGGKAK-GQKSEALVSHVDLFPT 291
|
....*..
gi 685600221 235 ILDWFSV 241
Cdd:pfam00884 292 ILDLAGI 298
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
19-384 |
2.34e-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: 293763 [Multi-domain] Cd Length: 421 Bit Score: 121.11 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 19 SLPLLLSQAGVRTGIIGKKHVGPEAVY-P----FD---------------FAYTEENGSVLQVGRNITRIKLLVR---KF 75
Cdd:cd16144 98 TIAEALKDAGYATAHFGKWHLGGEGGYgPedqgFDvniggtgnggppsyyFPPGKPNPDLEDGPEGEYLTDRLTDeaiDF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 76 LQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAydpldvlvpyfvpdtpaARADLAAQYTT 155
Cdd:cd16144 178 IEQNKDKPFFLYLSHYAVH-----------------------------TPIQ-----------------ARPELIEKYEK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 156 IGR-----------------MDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IPFPSGRTNLYWPGTAEP 206
Cdd:cd16144 212 KKKglrkgqknpvyaamiesLDESVGRILDALEELGLADNTLVIFTSDNGglstrggpptsnAPLRGGKGSLYEGGIRVP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 207 LLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPsytifgsKTIHLTGRSLLPALEAEplwatvfgsqshhevTMS 286
Cdd:cd16144 292 LIVRWPGVIKP-GSVSDVPVIGTDLYPTFLELAGGPLP-------PPQHLDGVSLVPLLKGG---------------EAD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 287 YPMRS-VQHrnfrlvhnlnfkmpFPIDQDFYVSPtfqdllnrTTA---GQptgwYKdLHHYYYRARWELYDQSRDPHETQ 362
Cdd:cd16144 349 LPRRAlFWH--------------FPHYHGQGGRP--------ASAirkGD----WK-LIEFYEDGRVELYNLKNDIGETN 401
|
410 420
....*....|....*....|..
gi 685600221 363 NLAADprFAQVLEMLRAQLTKW 384
Cdd:cd16144 402 NLAAE--MPEKAAELKKKLDAW 421
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
24-384 |
7.78e-29 |
|
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: 116.50 E-value: 7.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 24 LSQAGVRTGIIGKKHVGPEavYP-------FDFAYTEENGSVLQVG-------------RNITRIK-------LLVR--- 73
Cdd:cd16146 87 FKDAGYRTGIFGKWHLGDN--YPyrpqdrgFDEVLGHGGGGIGQYPdywgndyfddtyyHNGKFVKtegyctdVFFDeai 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 74 KFLQTQDDRPFFLYVAFHDPHRcghsqpqygtfcekfgngesgmgripdwtpqaydpldvlvPYFVPDTPAAR------- 146
Cdd:cd16146 165 DFIEENKDKPFFAYLATNAPHG----------------------------------------PLQVPDKYLDPykdmgld 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 147 ADLAAQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipfPSGRTNLYWP-------------GTAEPLLVSSPE 213
Cdd:cd16146 205 DKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG---PAGGVPKRFNagmrgkkgsvyegGHRVPFFIRWPG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 214 HpKRWGQVSEAYVSLLDLTPTILDWFSVPYPsytifgsKTIHLTGRSLLPALEAE--PLWATVFGSQSHHEVTMSYPMR- 290
Cdd:cd16146 282 K-ILAGKDVDTLTAHIDLLPTLLDLCGVKLP-------EGIKLDGRSLLPLLKGEsdPWPERTLFTHSGRWPPPPKKKRn 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 291 -SVQHRNFRLVHNLNFKmpfpidqdfyvsptfqdllnrttagqptgwykdlhhyyyrarWELYDQSRDPHETQNLAADpr 369
Cdd:cd16146 354 aAVRTGRWRLVSPKGFQ------------------------------------------PELYDIENDPGEENDVADE-- 389
|
410
....*....|....*
gi 685600221 370 FAQVLEMLRAQLTKW 384
Cdd:cd16146 390 HPEVVKRLKAAYEAW 404
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
8-305 |
5.53e-25 |
|
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: 104.16 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 8 VHHFNSFD-------KVRSLPLLLSQAGVRTGIIGKKHVGPEAVYPFdFAYTeengsvlqvgRNITRiklLVRKFLQTQ- 79
Cdd:cd16037 62 VHETGVWDnadpydgDVPSWGHALRAAGYETVLIGKLHFRGEDQRHG-FRYD----------RDVTE---AAVDWLREEa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 80 -DDRPFFLYVAFHDPHrcghsqpqygtfcekFgngesgmgriPDWTPQA-YDpldvlvpYFVpdtpaaRADLAAQYTTIG 157
Cdd:cd16037 128 aDDKPWFLFVGFVAPH---------------F----------PLIAPQEfYD-------LYV------RRARAAYYGLVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 158 RMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLLDLTP 233
Cdd:cd16037 170 FLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGErglwGKSTMYEESVRVPMIISGPGIPA--GKRVKTPVSLVDLAP 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685600221 234 TILDWFSVPYPSytifgsktiHLTGRSLLPALEAEPLWA-TVFgSQSH-HEVTMsyPMRSVQHRNFRLVHNLNF 305
Cdd:cd16037 248 TILEAAGAPPPP---------DLDGRSLLPLAEGPDDPDrVVF-SEYHaHGSPS--GAFMLRKGRWKYIYYVGY 309
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-387 |
5.61e-25 |
|
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: 105.00 E-value: 5.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 17 VRSLPLLLSQAGVRTGIIGKKHVgpeAVYPFDFayteengsvlqvgrnITRIKLlvrKFLQT-QDDRPFFLYVAFHDPHr 95
Cdd:cd16152 79 EKTLAHYFRDAGYETGYVGKWHL---AGYRVDA---------------LTDFAI---DYLDNrQKDKPFFLFLSYLEPH- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 96 cgHsQPQYGTF------CEKFGNgesgmgripdwtpqaydpldvlvpYFVPDTPAAR-----ADLAAQYTTIGRMDQGVG 164
Cdd:cd16152 137 --H-QNDRDRYvapegsAERFAN------------------------FWVPPDLAALpgdwaEELPDYLGCCERLDENVG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 165 LVLQELRDAGVLNDTLVIFTSDNGIPFPSgRTNLYWPGTAE-----PLLVSSPehPKRWGQVSEAYVSLLDLTPTILDWF 239
Cdd:cd16152 190 RIRDALKELGLYDNTIIVFTSDHGCHFRT-RNAEYKRSCHEssirvPLVIYGP--GFNGGGRVEELVSLIDLPPTLLDAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 240 SVPYPSYtifgsktihLTGRSLLPALEAEPL-WAT-VFGSQSHHEVTmsypmRSVQHRNFRL-VHNLNFKMPFPIDQDFY 316
Cdd:cd16152 267 GIDVPEE---------MQGRSLLPLVDGKVEdWRNeVFIQISESQVG-----RAIRTDRWKYsVAAPDKDGWKDSGSDVY 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685600221 317 VSptfqdllnrttagqptgwykdlhhyyyrarWELYDQSRDPHETQNLAADPRFAQVLEMLRAQLTKWQWE 387
Cdd:cd16152 333 VE------------------------------DYLYDLEADPYELVNLIGRPEYREVAAELRERLLARMAE 373
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
74-390 |
6.48e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 100.00 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 74 KFLQT-QDDRPFFLYVAFHDPHrcghsqPQYGtfCEKfgngesgmgriPDWTpqAYDPLDVLVPYFVPDTPAARADL--- 149
Cdd:cd16150 123 DWLRNrRPDKPFCLYLPLIFPH------PPYG--VEE-----------PWFS--MIDREKLPPRRPPGLRAKGKPSMleg 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 150 ------------------AAQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipfpsGRTNLY-----WPGTAE- 205
Cdd:cd16150 182 iekqgldrwseerwrelrATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHG-----DYTGDYglvekWPNTFEd 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 206 -----PLLVSSPEHPKrwGQVSEAYVSLLDLTPTILDWFSVPyPSYTIFgsktihltGRSLLPALEAEP--LWATVF--- 275
Cdd:cd16150 257 cltrvPLIIKPPGGPA--GGVSDALVELVDIPPTLLDLAGIP-LSHTHF--------GRSLLPVLAGETeeHRDAVFseg 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 276 ----GSQSHHEVTMS----YPMRSVQHRNFRLV------HNLNFKmpfpidqdfYVsptfqdllnRTTAGQPtgwykdlh 341
Cdd:cd16150 326 grlhGEEQAMEGGHGpydlKWPRLLQQEEPPEHtkavmiRTRRYK---------YV---------YRLYEPD-------- 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 685600221 342 hyyyrarwELYDQSRDPHETQNLAADPRFAQVLEMLRAQLTKWQWETHD 390
Cdd:cd16150 380 --------ELYDLEADPLELHNLIGDPAYAEIIAEMKQRLLRWMVETSD 420
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
20-365 |
7.49e-23 |
|
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: 99.17 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 20 LPLLLSQAGVRTGIIGKKHVG-PEAVYP----FDFAY---------------TEENGSVLQVGRNITRI----------K 69
Cdd:cd16026 88 IAEVLKKAGYRTALVGKWHLGhQPEFLPtrhgFDEYFgipysndmwpfplyrNDPPGPLPPLMENEEVIeqpadqssltQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 70 LLVRK---FLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwtpqaydpldvlVPYFVPDTPAAR 146
Cdd:cd16026 168 RYTDEavdFIERNKDQPFFLYLAHTMPH----------------------------------------VPLFASEKFKGR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 147 ADLAAQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IPFPSGRTNLYWPGTAEPLLVSSPEH 214
Cdd:cd16026 208 SGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwleygghggsaGPLRGGKGTTWEGGVRVPFIAWWPGV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 215 PKRwGQVSEAYVSLLDLTPTILDWFSVPYPSYTIfgsktihLTGRSLLPALEAEPlwatvfgSQSHHEVTMSYPmrsvqH 294
Cdd:cd16026 288 IPA-GTVSDELASTMDLLPTLAALAGAPLPEDRV-------IDGKDISPLLLGGS-------KSPPHPFFYYYD-----G 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685600221 295 RNFRLVHNLNFKMPFPidqDFYVSPTFQDLLNRTTAGQPtgwykdlhhyyyrarwELYDQSRDPHETQNLA 365
Cdd:cd16026 348 GDLQAVRSGRWKLHLP---TTYRTGTDPGGLDPTKLEPP----------------LLYDLEEDPGETYNVA 399
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
18-246 |
2.62e-22 |
|
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: 97.62 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 18 RSLPLLLSQAGVRTGIIGK------KHVGPEAVYP-FDFAYTEENGSV-----LQVGRNITRIK---------LLVRK-- 74
Cdd:cd16147 85 STLPVWLQEAGYRTAYAGKylngygVPGGVSYVPPgWDEWDGLVGNSTyynytLSNGGNGKHGVsypgdyltdVIANKal 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 75 -FLQT--QDDRPFFLYVAFHDPHRCGHSQPQYGtfcekfgNGESGMGRIPDWTPQAYDPLDVlvPYFVPDTPAARADLAA 151
Cdd:cd16147 165 dFLRRaaADDKPFFLVVAPPAPHGPFTPAPRYA-------NLFPNVTAPPRPPPNNPDVSDK--PHWLRRLPPLNPTQIA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 152 QYTTIGR--------MDQGVGLVLQELRDAGVLNDTLVIFTSDNGipF-------PSGRTNLYWPGTAEPLLVSSPEHPK 216
Cdd:cd16147 236 YIDELYRkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNG--YhlgqhrlPPGKRTPYEEDIRVPLLVRGPGIPA 313
|
250 260 270
....*....|....*....|....*....|
gi 685600221 217 rwGQVSEAYVSLLDLTPTILDWFSVPYPSY 246
Cdd:cd16147 314 --GVTVDQLVSNIDLAPTILDLAGAPPPSD 341
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
15-367 |
2.82e-22 |
|
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: 98.05 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 15 DKVRSLPLLLSQAGVRTGIIGKKHVGPE--AVYP----FDF---------------AYTEENG------SVLQVGRNITR 67
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPgtPGHPtkqgFDYfygyldqvhahnyypEYLWRNGekvplpNNVIPPLDEGN 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 68 IKLLVR-------------KFLQTQDDRPFFLYVAFHDPHrcGHSQpqygtfcekfgngesgmgrIPDWTPQAYDPLDvL 134
Cdd:cd16145 161 NAGGGGgtyshdlftdealDFIRENKDKPFFLYLAYTLPH--APLQ-------------------VPDDGPYKYKPKD-P 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 135 VPYFVPDTPAARADLAAQyttIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI-----------------PFPSGRTN 197
Cdd:cd16145 219 GIYAYLPWPQPEKAYAAM---VTRLDRDVGRILALLKELGIDENTLVVFTSDNGPhseggsehdpdffdsngPLRGYKRS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 198 LYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPSytifgsktiHLTGRSLLPALEAEPlwatvfgs 277
Cdd:cd16145 296 LYEGGIRVPFIARWPGKIPA-GSVSDHPSAFWDFMPTLADLAGAEPPE---------DIDGISLLPTLLGKP-------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 278 qshhevtmsypmRSVQHRNfrLVHNLNFKMpfpidqdfyvsptFQDLLNRttagqptGWYKDLHHYYYRARWELYDQSRD 357
Cdd:cd16145 358 ------------QQQQHDY--LYWEFYEGG-------------GAQAVRM-------GGWKAVRHGKKDGPFELYDLSTD 403
|
410
....*....|
gi 685600221 358 PHETQNLAAD 367
Cdd:cd16145 404 PGETNNLAAQ 413
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
24-301 |
7.31e-20 |
|
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: 89.56 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 24 LSQAGVRTGIIGKKH-VGPEAVYPFDfaYTEEngsvlqVGRNITRiKL--LVRKflqtQDDRPFFLYVAFHDPHrcghsq 100
Cdd:cd16032 85 LRAAGYRTALSGKMHfVGPDQLHGFD--YDEE------VAFKAVQ-KLydLARG----EDGRPFFLTVSFTHPH------ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 101 pqygtfcekfgngesgmgripdwtpqayDPLDVLVPYFVPDTPAARAdlaAQYTTIGRMDQGVGLVLQELRDAGVLNDTL 180
Cdd:cd16032 146 ----------------------------DPYVIPQEYWDLYVRRARR---AYYGMVSYVDDKVGQLLDTLERTGLADDTI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 181 VIFTSDN-------GIPFpsgRTNLYWPGTAEPLLVSSPE--HPKRwgqVSEAyVSLLDLTPTILDWFSVPYPSYtifgs 251
Cdd:cd16032 195 VIFTSDHgdmlgerGLWY---KMSFFEGSARVPLIISAPGrfAPRR---VAEP-VSLVDLLPTLVDLAGGGTAPH----- 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 685600221 252 kTIHLTGRSLLPALE-AEPLWATVFGSQSHHEVTMSyPMRSVQHRNFRLVH 301
Cdd:cd16032 263 -VPPLDGRSLLPLLEgGDSGGEDEVISEYLAEGAVA-PCVMIRRGRWKFIY 311
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
75-383 |
2.13e-19 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 90.11 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 75 FLQTQD-DRPFFLYVAFHDPHRcGHSQPQYgtFCEKFGNGESGMGRIPDWT------PQAYDPlDVLVPYFVPDtpAARA 147
Cdd:PRK13759 192 FLRRRDpTKPFFLKMSFARPHS-PYDPPKR--YFDMYKDADIPDPHIGDWEyaedqdPEGGSI-DALRGNLGEE--YARR 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 148 DLAAQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG--------------------IPFPsgrtnLYWPGTAepl 207
Cdd:PRK13759 266 ARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGdmlgdhylfrkgypyegsahIPFI-----IYDPGGL--- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 208 lvsspEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPSytifgsktiHLTGRSLLPALEA-EPLWATVFgsqsHHEvtms 286
Cdd:PRK13759 338 -----LAGNR-GTVIDQVVELRDIMPTLLDLAGGTIPD---------DVDGRSLKNLIFGqYEGWRPYL----HGE---- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 287 ypmrsvqHrnfrlvhnlnfkmpfpidqdfyvsptfqdllnrTTAGQPTGWYKDLHHYY----YRARWELYDQSRDPHETQ 362
Cdd:PRK13759 395 -------H---------------------------------ALGYSSDNYLTDGKWKYiwfsQTGEEQLFDLKKDPHELH 434
|
330 340
....*....|....*....|.
gi 685600221 363 NLAADPRFAQVLEMLRAQLTK 383
Cdd:PRK13759 435 NLSPSEKYQPRLREMRKKLVD 455
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
1-263 |
6.92e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 85.68 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 1 MYGLHQDVHHFNSFDKVRSLPLLLSQAGVRTGIIGKkHVGPEAVYPFDFAYTEENGSVLQVGRNI----TRIKLLVRKFL 76
Cdd:cd16148 60 LYPFYHGVWGGPLEPDDPTLAEILRKAGYYTAAVSS-NPHLFGGPGFDRGFDTFEDFRGQEGDPGeegdERAERVTDRAL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 77 ----QTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYDpldvlvpyfvpdtpaaradlaaq 152
Cdd:cd16148 139 ewldRNADDDPFFLFLHYFDPH-----------------------------EPYLYD----------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 153 yTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPF------PSGRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYV 226
Cdd:cd16148 167 -AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFgehglyWGHGSNLYDEQLHVPLIIRWPGKEP--GKRVDALV 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 685600221 227 SLLDLTPTILDWFSVPYPSYtifgsktihLTGRSLLP 263
Cdd:cd16148 244 SHIDIAPTLLDLLGVEPPDY---------SDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
79-370 |
9.76e-19 |
|
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: 87.63 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 79 QDDRPFFLYVAFHDPHRcghsqP---------QYGTFCEKFGNGESGMG----RIPDWT--PQAYDPLDVLVPYFVPDTP 143
Cdd:cd16030 178 DSDKPFFLAVGFYKPHL-----PfvapkkyfdLYPLESIPLPNPFDPIDlpevAWNDLDdlPKYGDIPALNPGDPKGPLP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 144 AARADLAAQ--YTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipFPSG-------RTNlyWPGTAE-PLLVSSPE 213
Cdd:cd16030 253 DEQARELRQayYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG--WHLGehghwgkHTL--FEEATRvPLIIRAPG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 214 HPKRwGQVSEAYVSLLDLTPTILDWFSVPYPSytifgsktiHLTGRSLLPALE-AEPLWATVFGSQSHHEVTMSYPMRSv 292
Cdd:cd16030 329 VTKP-GKVTDALVELVDIYPTLAELAGLPAPP---------CLEGKSLVPLLKnPSAKWKDAAFSQYPRPSIMGYSIRT- 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685600221 293 qhRNFRLVHnlnfkmpfpidqdfyvsptfqdllnrttagqptgwYKDLHHYYYRarwELYDQSRDPHETQNLAADPRF 370
Cdd:cd16030 398 --ERYRYTE-----------------------------------WVDFDKVGAE---ELYDHKNDPNEWKNLANDPEY 435
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
74-391 |
2.09e-18 |
|
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: 86.54 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 74 KFLQTQDDRPFFLYVAFHDPH----------------------RCGHSQ------PQYGTFCEKFGNGESGMGRIPDWTp 125
Cdd:cd16028 149 EYLDERQDEPWFLHLSYIRPHppfvapapyhalydpadvpppiRAESLAaeaaqhPLLAAFLERIESLSFSPGAANAAD- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 126 qaydpldvlvpyfvpDTPAARADLAAQYT-TIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFP---SGRTNLYWP 201
Cdd:cd16028 228 ---------------LDDEEVAQMRATYLgLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGdhwLWGKDGFFD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 202 GTAE-PLLVSSPEHPKR--WGQVSEAYVSLLDLTPTILDWFSVPYPSytifgsktiHLTGRSLLPALEAE--PLWATvfg 276
Cdd:cd16028 293 QAYRvPLIVRDPRREADatRGQVVDAFTESVDVMPTILDWLGGEIPH---------QCDGRSLLPLLAGAqpSDWRD--- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 277 sqshhEVTMSYPMRSVQHRNFRLVHNLNfkmpfPIDQDFYVsptFQDllNRttagqptgwYKDLHHYYYRARweLYDQSR 356
Cdd:cd16028 361 -----AVHYEYDFRDVSTRRPQEALGLS-----PDECSLAV---IRD--ER---------WKYVHFAALPPL--LFDLKN 414
|
330 340 350
....*....|....*....|....*....|....*
gi 685600221 357 DPHETQNLAADPRFAQVLEMLRAQLTKWQWETHDP 391
Cdd:cd16028 415 DPGELRDLAADPAYAAVVLRYAQKLLSWRMRHADR 449
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
15-396 |
1.99e-17 |
|
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: 83.97 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 15 DKVRSLPLLLSQAGVRTGIIGKKHV-------------GPEAVYPFDFA-YTEE----------NGSVLQVGRNIT---- 66
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKWHLdggdyfgngicpqGWDPDYWYDMRnYLDElteeerrksrRGLTSLEAEGIKeeft 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 67 ---RIKLLVRKFLQTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFgngesgmgRIPDwTPQAYDPLDVLVPYFVPDTP 143
Cdd:cd16156 156 yghRCTNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDF--------EFPK-GENAYDDLENKPLHQRLWAG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 144 AARADLAAQYTTIGRM--------DQGVGLVLQELRDagVLNDTLVIFTSDNGIPFpsGRTNLYWPGTAE-------PLL 208
Cdd:cd16156 227 AKPHEDGDKGTIKHPLyfgcnsfvDYEIGRVLDAADE--IAEDAWVIYTSDHGDML--GAHKLWAKGPAVydeitniPLI 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 209 VSSPEHPKRWGQVSeAYVSLLDLTPTILDWFSVPYPSYtifgsktihLTGRSLLPALEAE--PLWATVFGSQSHHEVTMS 286
Cdd:cd16156 303 IRGKGGEKAGTVTD-TPVSHIDLAPTILDYAGIPQPKV---------LEGESILATIEDPeiPENRGVFVEFGRYEVDHD 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 287 -----YPMRSVQHRNFRLVHNLnfkmpfpIDQDfyvsptfqdllnrttagqptgwykdlhhyyyrarwELYDQSRDPHET 361
Cdd:cd16156 373 gfggfQPVRCVVDGRYKLVINL-------LSTD-----------------------------------ELYDLEKDPYEM 410
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 685600221 362 QNLAADPRFAQVLEMLRAQLTKWQWETHDP-----WVCAP 396
Cdd:cd16156 411 HNLIDDPDYADVRDQLHDELLDYMNETRDPfrgyyWECRP 450
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
18-365 |
2.97e-16 |
|
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: 79.50 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 18 RSLPLLLSQAGVRTGIIGKKHVG--PEAvYP----FD----FAYT---EEngsvlQVGRNITRIKllvRkflQTQDDRPF 84
Cdd:cd16142 86 PTLAELLKDAGYATAQFGKWHLGdeDGR-LPtdhgFDefygNLYHtidEE-----IVDKAIDFIK---R---NAKADKPF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 85 FLYVAFHDPHRCGHSQPQYgtfcekfgngesgMGRIPDWTPQAydplDVLVpyfvpdtpaaradlaaqyttigRMDQGVG 164
Cdd:cd16142 154 FLYVNFTKMHFPTLPSPEF-------------EGKSSGKGKYA----DSMV----------------------ELDDHVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 165 LVLQELRDAGVLNDTLVIFTSDNG---IPFP-SGRTNL------------------YWPGTAEPllvsspehpkrwGQVS 222
Cdd:cd16142 195 QILDALDELGIADNTIVIFTTDNGpeqDVWPdGGYTPFrgekgttweggvrvpaivRWPGKIKP------------GRVS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 223 EAYVSLLDLTPTILDWFSVPYPSYTIFGSKtIHLTGRSLLPALEAEplwatvfGSQSHHEV----TMSYPMrSVQHRNFR 298
Cdd:cd16142 263 NEIVSHLDWFPTLAALAGAPDPKDKLLGKD-RHIDGVDQSPFLLGK-------SEKSRRSEffyfGEGELG-AVRWKNWK 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685600221 299 LVhnlnfkmpfpidqdfyvsptfqdllnrTTAGQPTGWykDLHHYYYRARW-ELYDQSRDPHETQNLA 365
Cdd:cd16142 334 VH---------------------------FKAQEDTGG--PTGEPFYVLTFpLIFNLRRDPKERYDVT 372
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
20-365 |
5.44e-16 |
|
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: 79.17 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 20 LPLLLSQAGVRTGIIGKKHVG-----------PEAVYP----------------FDFAYTEENGSVLqvgrnitriKLLV 72
Cdd:cd16143 88 LAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggpldhgFDYYFGIPASEVL---------PTLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 73 RK---FLQTQ--DDRPFFLYVAFHDPHrcGHSQPqygtfCEKFgNGESGMGripdwtpqaydpldvlvpyfvpdtpaARA 147
Cdd:cd16143 159 DKaveFIDQHakKDKPFFLYFALPAPH--TPIVP-----SPEF-QGKSGAG--------------------------PYG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 148 DLAAQyttigrMDQGVGLVLQELRDAGVLNDTLVIFTSDNG-IPFPSGRTNL---YWP--------------GTAEPLLV 209
Cdd:cd16143 205 DFVYE------LDWVVGRILDALKELGLAENTLVIFTSDNGpSPYADYKELEkfgHDPsgplrgmkadiyegGHRVPFIV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 210 SSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPsytifgsKTIHLTGRSLLPAL---EAEPLWATVFgsqsHHEVTMS 286
Cdd:cd16143 279 RWPGKIPA-GSVSDQLVSLTDLFATLAAIVGQKLP-------DNAAEDSFSFLPALlgpKKQEVRESLV----HHSGNGS 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685600221 287 YPMRSVQhrnfrlvhnlnFKMpfpIDQDFyvSPTFQDLLNRTTAGQPTGwykdlhhyyyrarwELYDQSRDPHETQNLA 365
Cdd:cd16143 347 FAIRKGD-----------WKL---IDGTG--SGGFSYPRGKEKLGLPPG--------------QLYNLSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
19-263 |
3.88e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 74.58 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 19 SLPLLLSQAGVRTGIIGKKHVGPEAVypfDFAYTEEngsvlqvgrnitrikllvrkflqtQDDRPFFLYVAFHDPHrcgh 98
Cdd:cd16149 91 TLPEVLQDAGYRCGLSGKWHLGDDAA---DFLRRRA------------------------EAEKPFFLSVNYTAPH---- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 99 sqpqygtfcekfgngesgmgripdwTPQAYdpldvlvpyfvpdtpaaradlaaqYTTIGRMDQGVGLVLQELRDAGVLND 178
Cdd:cd16149 140 -------------------------SPWGY------------------------FAAVTGVDRNVGRLLDELEELGLTEN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 179 TLVIFTSDNGipFPSG------------RTNLYWPGTAEPLLVSSPEHpKRWGQVSEAYVSLLDLTPTILDWFSVPYPSy 246
Cdd:cd16149 171 TLVIFTSDNG--FNMGhhgiwgkgngtfPLNMYDNSVKVPFIIRWPGV-VPAGRVVDSLVSAYDFFPTLLELAGVDPPA- 246
|
250
....*....|....*..
gi 685600221 247 tifgskTIHLTGRSLLP 263
Cdd:cd16149 247 ------DPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
8-306 |
1.33e-14 |
|
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: 74.56 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 8 VHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVG---PEAVYPFDFAYTE-----------------------ENGSVLQV 61
Cdd:cd16151 66 VVFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEFGFDEyclwqltetgekysrpatptfniRNGKLLET 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 62 GRNITRIKLLVRK---FLQTQDDRPFFLY---VAFHDPHrcghsqpqYGTfcekfgngesgmgriPD---WTPQAYDPLD 132
Cdd:cd16151 146 TEGDYGPDLFADFlidFIERNKDQPFFAYypmVLVHDPF--------VPT---------------PDspdWDPDDKRKKD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 133 VLvPYFvpdtpaarADLAAqYttigrMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFP-SGRTN----------LYWP 201
Cdd:cd16151 203 DP-EYF--------PDMVA-Y-----MDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPiTSRTNgrevrggkgkTTDA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 202 GTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPsytifgsKTIHLTGRSLLPALEAEPlwatvfgSQSHH 281
Cdd:cd16151 268 GTHVPLIVNWPGLIPA-GGVSDDLVDFSDFLPTLAELAGAPLP-------EDYPLDGRSFAPQLLGKT-------GSPRR 332
|
330 340
....*....|....*....|....*
gi 685600221 282 EVTMSYPMRSVQHRNFRLVHNLNFK 306
Cdd:cd16151 333 EWIYWYYRNPHKKFGSRFVRTKRYK 357
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
20-265 |
2.25e-14 |
|
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: 74.43 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 20 LPLLLSQAGVRTGIIGKKHVGPEAVY-P----FDFAYTEENGSV-----------------LQVGR-------------- 63
Cdd:cd16157 95 LPELLKKAGYRNKIVGKWHLGHRPQYhPlkhgFDEWFGAPNCHFgpydnkaypnipvyrdwEMIGRyyeefkidkktges 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 64 NITRIkLLVR--KFLQTQ--DDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGnGESGMGRIPDwtpqaydpldvlvpyfv 139
Cdd:cd16157 175 NLTQI-YLQEalEFIEKQhdAQKPFFLYWAPDATH-----APVYAS--KPFL-GTSQRGLYGD----------------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 140 pdtpaaradlaaqytTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI-------------PFPSGRTNLYWPGTAEP 206
Cdd:cd16157 229 ---------------AVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAalisapeqggsngPFLCGKQTTFEGGMREP 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 685600221 207 LLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPSYTIfgsktihLTGRSLLPAL 265
Cdd:cd16157 294 AIAWWPGHIKP-GQVSHQLGSLMDLFTTSLALAGLPIPSDRA-------IDGIDLLPVL 344
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
2-260 |
1.13e-12 |
|
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: 69.04 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 2 YGLHQDVHHFNSFDKVRSLPL-------LLSQAGVRTGIIGKKHVGPEAVY-P----FDFAY--TEENGSVLQvgrniTR 67
Cdd:cd16161 63 LGLRNGVGHNFLPTSVGGLPLnettlaeVLRQAGYATGMIGKWHLGQREAYlPnsrgFDYYFgiPFSHDSSLA-----DR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 68 IKLLVRKFLQ--TQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYDPLdvlvpyfVPDTPAA 145
Cdd:cd16161 138 YAQFATDFIQraSAKDRPFFLYAALAHVH-----------------------------VPLANLPR-------FQSPTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 146 RADLAAqytTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG--------IPFPSG---RTNLYWP---------GTAE 205
Cdd:cd16161 182 RGPYGD---ALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelAVGPGTgdwQGNLGGSvakastwegGHRE 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 685600221 206 PLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYPSYTIFGSKTIH--LTGRS 260
Cdd:cd16161 259 PAIVYWPGRIPA-NSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSpvLFGGS 314
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-245 |
2.00e-12 |
|
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: 68.36 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 15 DKVRSLPLLLSQAGVRTGIIGKKHV-GPEAVYP--------------FDF------------AYTEENGSVLQVGRNITR 67
Cdd:cd16034 77 PDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppperrhgFDYwkgyecnhdhnnPHYYDDDGKRIYIKGYSP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 68 IKL--LVRKFL--QTQDDRPFFLYVAFHDPHrcghsqPQYGTFCEKFGNGesgmgripdwtpqaYDPLDVLVPYFVPDTP 143
Cdd:cd16034 157 DAEtdLAIEYLenQADKDKPFALVLSWNPPH------DPYTTAPEEYLDM--------------YDPKKLLLRPNVPEDK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 144 AARADLAAQ----YTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPS-GRT--NLYWPGTAE-PLLVSSPEHP 215
Cdd:cd16034 217 KEEAGLREDlrgyYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGShGLMnkQVPYEESIRvPFIIRYPGKI 296
|
250 260 270
....*....|....*....|....*....|
gi 685600221 216 KRwGQVSEAYVSLLDLTPTILDWFSVPYPS 245
Cdd:cd16034 297 KA-GRVVDLLINTVDIMPTLLGLCGLPIPD 325
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-269 |
3.66e-12 |
|
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: 66.85 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 17 VRSLPLLLSQAGVRTGIIGKKHV--GPEAVYPFDFAYTEENgsvlqvgrnitrIKLLVRKFLQTQDDRPFFLYVAFHDPH 94
Cdd:cd16035 83 VPTLGHMLRAAGYYTAYKGKWHLsgAAGGGYKRDPGIAAQA------------VEWLRERGAKNADGKPWFLVVSLVNPH 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 95 rcghsqpqygtfcekfgngesgmgripdwtpqaydplDVLvpYFVPDTPAARADLAAQYTTIGRMDQGVGLVLQELRDAG 174
Cdd:cd16035 151 -------------------------------------DIM--FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 175 VLNDTLVIFTSDNG----------IPFpsgrtNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSVPYP 244
Cdd:cd16035 192 LADNTIVVFTSDHGemggahglrgKGF-----NAYEEALHVPLIISHPDLFGT-GQTTDALTSHIDLLPTLLGLAGVDAE 265
|
250 260
....*....|....*....|....*
gi 685600221 245 SYTifgSKTIHLTGRSLLPALEAEP 269
Cdd:cd16035 266 ARA---TEAPPLPGRDLSPLLTDAD 287
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
81-238 |
4.26e-12 |
|
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: 67.19 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 81 DRPFFLYVAFHDPHrcghsqpqygtfcekFGNGEsgmgripdwtPQAYDPLDVLVPYFVPDTpaARADLAAqytTIGRMD 160
Cdd:cd16029 181 SKPLFLYLAFQAVH---------------APLQV----------PPEYADPYEDKFAHIKDE--DRRTYAA---MVSALD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 161 QGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRT-----------NLYWPGTAEPLLVSSPEHPKRWGQVSEAYVSLL 229
Cdd:cd16029 231 ESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsnyplrggknTLWEGGVRVPAFVWSPLLPPKRGTVSDGLMHVT 310
|
....*....
gi 685600221 230 DLTPTILDW 238
Cdd:cd16029 311 DWLPTLLSL 319
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
75-237 |
6.30e-12 |
|
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: 67.07 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 75 FLQTQDDRPFFLYVAFhdphrcghSQPQYGTFCEKFGNGESGMGRIPDwtpqaydpldvlvpyfvpdtpaaradlaaqyt 154
Cdd:cd16160 187 FIEDNQENPFFLYFSF--------PQTHTPLFASKRFKGKSKRGRYGD-------------------------------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 155 TIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI------------PFPSGRTN-----------LYWPGTAEPllvss 211
Cdd:cd16160 227 NINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPhveycleggstgGLKGGKGNsweggirvpfiAYWPGTIKP----- 301
|
170 180
....*....|....*....|....*.
gi 685600221 212 pehpkrwgQVSEAYVSLLDLTPTILD 237
Cdd:cd16160 302 --------RVSHEVVSTMDIFPTFVD 319
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
79-410 |
3.51e-11 |
|
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: 64.77 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 79 QDDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGNgESGMGRIPDwtpqaydpldvlvpyfvpdtpaaradlaaqytTIGR 158
Cdd:cd16158 195 KEGKPFFLYYASHHTH-----YPQFAG--QKFAG-RSSRGPFGD--------------------------------ALAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 159 MDQGVGLVLQELRDAGVLNDTLVIFTSDNGipfPS---------------GRTNLYWPGTAEPLLVSSPEHPKRwgQVSE 223
Cdd:cd16158 235 LDGSVGELLQTLKENGIDNNTLVFFTSDNG---PStmrksrggnagllkcGKGTTYEGGVREPAIAYWPGRIKP--GVTH 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 224 AYVSLLDLTPTILDWFSVPYPSYTifgsktihLTGRSLLPALeaeplwatvFGS-QSHHEVTMSYPMRSVQHRNFRLVHN 302
Cdd:cd16158 310 ELASTLDILPTIAKLAGAPLPNVT--------LDGVDMSPIL---------FEQgKSPRQTFFYYPTSPDPDKGVFAVRW 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 303 LNFKMPFpIDQDFYVSPTFQDllnrttagqptgwyKDLHHYYYRARWE---LYDQSRDPHETQNLAADPRFAQVLEMLra 379
Cdd:cd16158 373 GKYKAHF-YTQGAAHSGTTPD--------------KDCHPSAELTSHDpplLFDLSQDPSENYNLLGLPEYNQVLKQI-- 435
|
330 340 350
....*....|....*....|....*....|....
gi 685600221 380 QLTKWQWETHDPWvcAPDGV---LEEKLSPQCQP 410
Cdd:cd16158 436 QQVKERFEASMKF--GESEInkgEDPALEPCCKP 467
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
136-250 |
8.92e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 63.52 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 136 PYFVPDTPAARAD-----LAAQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPsGRTNLYWPGTAE--PLL 208
Cdd:COG1368 398 PYTLPEEDKKIPDygkttLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSP-GKTDYENPLERYrvPLL 476
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 685600221 209 VSSPEHPKrwGQVSEAYVSLLDLTPTILDWFSVPYPSYTIFG 250
Cdd:COG1368 477 IYSPGLKK--PKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFG 516
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
15-237 |
6.36e-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: 58.97 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 15 DKVRSLPLLLSQAGVRTGIIGkkhvgpeavypfdfayteengsvlqvgrnitrikllVRKFL-QTQDDRPFFLYVAFHDP 93
Cdd:cd00016 87 EDGPTIPELLKQAGYRTGVIG------------------------------------LLKAIdETSKEKPFVLFLHFDGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 94 HRCGHSqpqygtfcekfgngesgmgriPDWTPQAYdpldvlvpyfvpdtpaaradlaaqYTTIGRMDQGVGLVLQELRDA 173
Cdd:cd00016 131 DGPGHA---------------------YGPNTPEY------------------------YDAVEEIDERIGKVLDALKKA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685600221 174 GVLNDTLVIFTSDNG-IPFPSGRTNLYWP-------GTAEPLLVSSPEHPKrwGQVSEAYVSLLDLTPTILD 237
Cdd:cd00016 166 GDADDTVIIVTADHGgIDKGHGGDPKADGkadkshtGMRVPFIAYGPGVKK--GGVKHELISQYDIAPTLAD 235
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
74-266 |
7.48e-10 |
|
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: 60.76 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 74 KFLQTQDDRPFFLYVAFHDPHRcghsqpqyGTFCEKFGNGESGMGRIPDwtpqaydpldvlvpyfvpdtpaaradlaaqy 153
Cdd:cd16159 243 SFLERNKERPFLLVMSFLHVHT--------ALFTSKKFKGRSKHGRYGD------------------------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 154 tTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG-----------------IPFPSGRTNLYWPGTAEPLLVSSPEHPK 216
Cdd:cd16159 284 -NVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGghleeisvggeygggngGIYGGKKMGGWEGGIRVPTIVRWPGVIP 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 685600221 217 RWGQVSEAyVSLLDLTPTILDWFSVPYPSytifgskTIHLTGRSLLPALE 266
Cdd:cd16159 363 PGSVIDEP-TSLMDIFPTVAALAGAPLPS-------DRIIDGRDLMPLLT 404
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
153-267 |
1.52e-08 |
|
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: 56.01 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 153 YTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGR----TNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSL 228
Cdd:cd16171 199 YAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRqfykMSMYEGSSHVPLLIMGPGIKA--GQQVSDVVSL 276
|
90 100 110
....*....|....*....|....*....|....*....
gi 685600221 229 LDLTPTILDWFSVPYPSytifgsktiHLTGRSLLPALEA 267
Cdd:cd16171 277 VDIYPTMLDIAGVPQPQ---------NLSGYSLLPLLSE 306
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
337-390 |
4.55e-08 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 50.71 E-value: 4.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 685600221 337 YKDLHHYYYRARWELYDQSRDPHETQNLAADPRFAQVLEMLRAQLTKWQWETHD 390
Cdd:pfam16347 50 YKLIHFYNDIDEWELYDLQKDPKEMNNVYGDPEYAEVQAELKEELEELRKQYKD 103
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-237 |
1.92e-06 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 49.66 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 27 AGVRTGIIGKKHVG------PEAVYPFDFA---------YTE----ENGSVLQVGR-NITRIKLLVRKFLQTQDdRPFFL 86
Cdd:cd16154 93 AGYSSAVIGKWHLGgndnspNNPGGIPYYAgilgggvqdYYNwnltNNGQTTNSTEyATTKLTNLAIDWIDQQT-KPWFL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 87 YVAFHDPHRCGHSQPqygtfcekfgNGESGMGRIPDWTPQAYDPLdvlvPYFvpdtpaaradLAAqyttIGRMDQGVGLV 166
Cdd:cd16154 172 WLAYNAPHTPFHLPP----------AELHSRSLLGDSADIEANPR----PYY----------LAA----IEAMDTEIGRL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 167 LQELrDAGVLNDTLVIFTSDNGIP-------FPSGRT--NLYWPGTAEPLLVSSPEHPkRWGQVSEAYVSLLDLTPTILD 237
Cdd:cd16154 224 LASI-DEEERENTIIIFIGDNGTPgqvvdlpYTRNHAkgSLYEGGINVPLIVSGAGVE-RANERESALVNATDLYATIAE 301
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
136-239 |
9.30e-05 |
|
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: 43.83 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 136 PYFVPDTPAARADLAAQYTTIGRMDQGVGLVLQELRDAGVLNDTLVIFTSD---NGIPFPSGRTNLYWPGTAEPLLVSSP 212
Cdd:cd16015 178 KDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDhlpSLGSDYDETDEDPLDLYRTPLLIYSP 257
|
90 100
....*....|....*....|....*..
gi 685600221 213 EHPKrwGQVSEAYVSLLDLTPTILDWF 239
Cdd:cd16015 258 GLKK--PKKIDRVGSQIDIAPTLLDLL 282
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
140-189 |
4.61e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 42.04 E-value: 4.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 685600221 140 PDTPAARADLAaqyttigRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI 189
Cdd:COG1524 202 PDSPEYRAALR-------EVDAALGRLLDALKARGLYEGTLVIVTADHGM 244
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
67-189 |
2.58e-03 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 39.49 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685600221 67 RIKLLVRKFlqtQDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPDTPAAR 146
Cdd:cd16018 144 RVDTILEWL---DLERPDLILLYFEEPDSAGH---KYG-----------------------------------PDSPEVN 182
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 685600221 147 ADLAaqyttigRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI 189
Cdd:cd16018 183 EALK-------RVDRRLGYLIEALKERGLLDDTNIIVVSDHGM 218
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