|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
49-391 |
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: 540.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNE--NCSSASWQA 126
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 127 QHEIRTFAVYLNNTGYRTAFFGKYLNEY----NGSYVPPGWKQWVGLIKNSRFYNYTLCrNGMKEKHGFDYSKDYLTDLI 202
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 203 TNDSISFFRMSKKMypHRPVLMVISHAAPHGPEDSAPQYSHLFANAS-QHITPSYNYAPNPDKHWIMRYTGPMkPIHMEF 281
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLN-PTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 282 TNMLQRKRLQTLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPTVEAGSL 361
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 1835678661 362 NPHIVLNIDLAPTILDIAGLDIPADMDGKS 391
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
49-421 |
1.92e-90 |
|
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: 292.90 E-value: 1.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQ--DVeLGSMQ-VMNKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSA 122
Cdd:cd16031 2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 123 SwqaqheIRTFAVYLNNTGYRTAFFGKYLNEYNGSYVPPGWKQWVGLIKNSRFYNYTLCRNGmkekhGFDYSKDYLTDLI 202
Cdd:cd16031 80 S------QPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENG-----KRVGQKGYVTDII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 203 TNDSISFFRMSKKmypHRPVLMVISHAAPHGPEDSAPQYSHLFANAsqHITP-----SYNYAPNPD--KHWIMRYTGPMK 275
Cdd:cd16031 149 TDKALDFLKERDK---DKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEpetfdDDDYAGRPEwaREQRNRIRGVLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 276 -PIHMEFT---NMlqRKRLQTLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYV 351
Cdd:cd16031 224 gRFDTPEKyqrYM--KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLII 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835678661 352 RGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTErpanrfhfqkKAKVWRDSFLVE 421
Cdd:cd16031 301 RDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGE----------KPVDWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
49-429 |
2.47e-71 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 240.55 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQDV-ELGSM-QVMNKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcssAS 123
Cdd:COG3119 23 RPNILFILADDLGYgDLGCYgNPLIKTpniDRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG---YN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 WQAQHEIRTFAVYLNNTGYRTAFFGKYLNeyngsyvppgwkqwvgliknsrfynytlcrngmkekhgfdyskdYLTDLIT 203
Cdd:COG3119 99 GGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLLT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 204 NDSISFFRMSKKmyPHRPVLMVISHAAPHGPEDSAPQYSHLFANasQHITPSYNYAPNPDKHWIMRYtgpmkpihmeftn 283
Cdd:COG3119 135 DKAIDFLERQAD--KDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 284 mLQRKRLQTLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGP-TVEAGSLN 362
Cdd:COG3119 198 -ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGSVS 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835678661 363 PHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLdterpanrfhfQKKAKVWRDSFLVERGKLLHKR 429
Cdd:COG3119 277 DALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL-----------TGEKAEWRDYLYWEYPRGGGNR 332
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
538-673 |
1.75e-64 |
|
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.
Pssm-ID: 463628 Cd Length: 142 Bit Score: 212.59 E-value: 1.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 538 RNRSIRSVSIEIDGEMHNLEKEEAYQPLLSQNVTKRHmaeQDVTEEDKDM-EEYSGTGSI---TNELLVPTSIKVTHRCY 613
Cdd:pfam12548 6 RTRQKRSLSVEFEGEVYDIDLEEEYQPLEPRNLLKRH---ARDDGEEGEEgEESSGTGSKrdsSNSVGPPASVKVTHRCY 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 614 ILANDTVRCDKDLYKSLQAWKDHKLHIDHEIETLQSKIKNLREVRGHLKKKRPEECDCDK 673
Cdd:pfam12548 83 ILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
50-391 |
8.89e-49 |
|
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: 172.62 E-value: 8.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQ---DVE-LGSMQVmnKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcssa 122
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 123 SWQAQHEIRTFAVYLNNTGYRTAFFGKylneyngsyvppgwkqWvgliknsrfynytlcrngmkekHgfdyskdyltdli 202
Cdd:cd16022 74 GGGLPPDEPTLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 203 tNDSISFFRMSKKmypHRPVLMVISHAAPHGPedsapqyshlfanasqhitpsYNYApnpdkhwimrytgpmkpiHMeft 282
Cdd:cd16022 103 -DEAIDFIERRDK---DKPFFLYVSFNAPHPP---------------------FAYY------------------AM--- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 283 nmlqrkrlqtLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGP-TVEAGSL 361
Cdd:cd16022 137 ----------VSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIPAGQV 206
|
330 340 350
....*....|....*....|....*....|
gi 1835678661 362 NPHIVLNIDLAPTILDIAGLDIPADMDGKS 391
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-402 |
1.22e-48 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 177.76 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDD---QDveLGSMQVMN-KT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencss 121
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTpnlDRLAKEG-VVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 122 aSWQAQHEIRTFAVYLNNTGYRTAFFGK--------YLNEYNGSYVPP----GWKQWVGLIKNSRFYNYTLCRNGMKEKH 189
Cdd:cd16034 72 -DVPLPPDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 190 GFDYSKDYLTDLItndsISFfrMSKKMYPHRPVLMVISHAAPHGPEDSAPQ-YSHLFANASQHitpsynYAPNPDKhwim 268
Cdd:cd16034 151 IKGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLL------LRPNVPE---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 269 rytgpmkpihmeftNMLQRKRLQTLM--------SVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVkGKSMP 340
Cdd:cd16034 215 --------------DKKEEAGLREDLrgyyamitALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVP 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835678661 341 YEFDIRVPFYVRGPTV-EAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPA 402
Cdd:cd16034 280 YEESIRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDD 342
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
50-407 |
8.74e-47 |
|
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: 173.11 E-value: 8.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDqdveLGSMQV---MNK---TRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKY--------VHNHNTY 113
Cdd:cd16144 1 PNIVLILVDD----LGWADLgcyGSKfyeTPNIdrLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 114 TNNENCSSASWQAQH---EIRTFAVYLNNTGYRTAFFGKY-LNEyNGSYVPpgwKQW-----VGLIKNSRFYNYTLCRNG 184
Cdd:cd16144 77 PPDNTKLIPPPSTTRlplEEVTIAEALKDAGYATAHFGKWhLGG-EGGYGP---EDQgfdvnIGGTGNGGPPSYYFPPGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 185 MKEKHGFDYSKDYLTDLITNDSISFFRMSKKmyphRPVLMVISHAAPHGPEDSAPQYSHLFANAsqhitpsynYAPNPDK 264
Cdd:cd16144 153 PNPDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKYEKK---------KKGLRKG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 265 HWIMRYTGpmkpihmeftnMLQrkrlqtlmSVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLV-------KGK 337
Cdd:cd16144 220 QKNPVYAA-----------MIE--------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGGK 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835678661 338 SMPYEFDIRVPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLL--DTERPANR---FHF 407
Cdd:cd16144 281 GSLYEGGIRVPLIVRWPgVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLLkgGEADLPRRalfWHF 358
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
50-404 |
1.36e-46 |
|
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: 171.15 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQDVELGSmqVMN---KTRRIME--QGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencSSASW 124
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGL----RSRGF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 125 QAQHEIRTFAVYLNNTGYRTAFFGKYlnEYNGSYVPPGWkqwvgliknsrFYNYTLCRNGMKEKHGFDYSKDYLTDLITN 204
Cdd:cd16027 75 PLPDGVKTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKKG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 205 D----SISFFrmskkmYPHRPVLMVISHAAPHGPEDsapqyshlfanasqhITPSYNYAPNPdkhwIMRYtgpmkpihmE 280
Cdd:cd16027 142 QpfflWFGFH------DPHRPYPPGDGEEPGYDPEK---------------VKVPPYLPDTP----EVRE---------D 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 281 FTNMLQrkrlqTLMSVDESMEQIYNALVETAELDNTYIIYTADHGYhigqfGLVKGKSMPYEFDIRVPFYVRGP-TVEAG 359
Cdd:cd16027 188 LADYYD-----EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPgKIKPG 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1835678661 360 SLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPANR 404
Cdd:cd16027 258 SVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
50-396 |
4.43e-41 |
|
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: 156.22 E-value: 4.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQDV-ELGSM-QVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKyvHNHNTY--TNNENCSSAS 123
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTGHTRvrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 WQAqhEIRTFAVYLNNTGYRTAFFGKY-LNEYNGSYVPP--GWKQWVGLIKNSR---FYNYTLCRNGMKE---------- 187
Cdd:cd16145 79 LPP--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGYLDQVHahnYYPEYLWRNGEKVplpnnvippl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 188 -------KHGFDYSkdylTDLITNDSISFFRMSKKmyphRPVLMVISHAAPHGPedsapqyshlfanasqHITPSYNYAP 260
Cdd:cd16145 157 degnnagGGGGTYS----HDLFTDEALDFIRENKD----KPFFLYLAYTLPHAP----------------LQVPDDGPYK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 261 NPDKHWIMRYTGPMKPIHMEFTNMLQRkrlqtlmsVDESMEQIYNALVETAELDNTYIIYTADHGYHI-------GQF-- 331
Cdd:cd16145 213 YKPKDPGIYAYLPWPQPEKAYAAMVTR--------LDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfd 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 332 ---GLVKGK-SMpYEFDIRVPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLL 396
Cdd:cd16145 285 sngPLRGYKrSL-YEGGIRVPFIARWPgKIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
50-381 |
1.07e-39 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 149.11 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQ---DVELGSMqVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNEncssasW 124
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLYGY-PRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 125 QAQHEIRTFAVYLNNTGYRTAFFGKYLNEYNGSYVPP--GWKQWVGLIKNSRFYNYtlcrngMKEKHGFDYSKDYLTDLI 202
Cdd:pfam00884 74 GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYAD------PPDVPYNCSGGGVSDEAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 203 TNDSISFfrmskKMYPHRPVLMVISHAAPHGPEDSAPQYshlfanasqhITPSYNYAPNPDKHWIMRytgpmkpihmeft 282
Cdd:pfam00884 148 LDEALEF-----LDNNDKPFFLVLHTLGSHGPPYYPDRY----------PEKYATFKPSSCSEEQLL------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 283 nmlqRKRLQTLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFG--LVKGKSM-PYEFDIRVPFYVRGPTVEA- 358
Cdd:pfam00884 200 ----NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAk 275
|
330 340
....*....|....*....|...
gi 1835678661 359 GSLNPHIVLNIDLAPTILDIAGL 381
Cdd:pfam00884 276 GQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-404 |
2.86e-39 |
|
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: 150.07 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQ--DVeLGSM-QVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSas 123
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIPLPA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 wqaqhEIRTFAVYLNNTGYRTAFFGKylneyngsyvppgwkqWvgliknsrfynytlcrngmkekHGFDYSKDYLTDLit 203
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 204 ndSISFFRmskKMYPHRPVLMVISHAAPH---------GPEDSAPQYSHLFA---------NASQHItpsynyapnPDkh 265
Cdd:cd16152 113 --AIDYLD---NRQKDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWVppdlaalpgDWAEEL---------PD-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 266 wimrYTGpmkpihmeftnMLQRkrlqtlmsVDESMEQIYNALVETAELDNTYIIYTADHGYHigqFGLVKG--KSMPYEF 343
Cdd:cd16152 177 ----YLG-----------CCER--------LDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835678661 344 DIRVPFYVRGPTVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPANR 404
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWR 291
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-404 |
2.03e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 138.47 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQDVE----LGSMQVmnKTRRI--MEQGGAHFINAFVTTPM----CCPSRSSILTGKYVHNhntytnNEN 118
Cdd:cd16155 2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH------APE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 119 CSSASWQAQHeiRTFAVYLNNTGYRTAFFGKYLNEYngsyvppgwkqwvgliknsrfynytlcrngmkekhgfdyskdyl 198
Cdd:cd16155 74 GGKAAIPSDD--KTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 199 tdliTNDSISFFRmsKKMYPHRPVLMVISHAAPHGPEDSAPQYSHLFAnaSQHITPSYNYAP-NPdkhwimrytgpmkpi 277
Cdd:cd16155 108 ----ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLPqHP--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 278 hmeFTNMLQRKRLQTL-------------------MS--VDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVkG 336
Cdd:cd16155 165 ---FDNGEGTVRDEQLapfprtpeavrqhlaeyyaMIthLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-G 240
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835678661 337 KSMPYEFDIRVPFYVRGPTVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPANR 404
Cdd:cd16155 241 KQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVR 308
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-421 |
2.29e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 139.28 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQ--DVELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSASWQ 125
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 126 AQHEIRTFAVYLNNTGYRTAFFGKylneyngsyvppgwkqW-VGLIKNSRFYnytlcrnGMKEKHGFDYSKDYLtdlITN 204
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGK----------------WhVGPEETPLDY-------GFDEYLPVETTIEYF---LAD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 205 DSISFFRMSKKmyPHRPVLMVISHAAPHGPEDSAPQYSHLFANASQHITPSYN--YAPNPDKHWIMRytgpMKPIHMEFT 282
Cdd:cd16033 135 RAIEMLEELAA--DDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFAddFEDKPYIYRRER----KRWGVDTED 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 283 NMLQRKRLQ------TLMsvDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLV-KGKSMpYEFDIRVPFYVRGP- 354
Cdd:cd16033 209 EEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKWPg 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835678661 355 TVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPANrfhfqkkakvWRDSFLVE 421
Cdd:cd16033 286 VIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
50-396 |
3.64e-35 |
|
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: 138.84 E-value: 3.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQ---DVELGSMQVMnKT---RRIMEQGgAHFINaFVTTPMCCPSRSSILTGKYVHN---HNTYTNNENCS 120
Cdd:cd16146 1 PNVILILTDDQgygDLGFHGNPIL-KTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHTILGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 121 SaswqaqhEIRTFAVYLNNTGYRTAFFGKYLNEYNGSYVPP-------------GWKQWVGLIKNSRFYNyTLCRNGMKE 187
Cdd:cd16146 78 L-------DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrgfdevlghgggGIGQYPDYWGNDYFDD-TYYHNGKFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 188 KHgfdysKDYLTDLITNDSISFFRMSKKmyphRPVLMVISHAAPHGPEDSAPQYSHLFANASQHITPSYNYApnpdkhwi 267
Cdd:cd16146 150 KT-----EGYCTDVFFDEAIDFIEENKD----KPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG-------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 268 mrytgpmkpihmeftnMLQRkrlqtlmsVDESMEQIYNALVETAELDNTYIIYTADHGYHIG-----QFGLVKGKSMPYE 342
Cdd:cd16146 213 ----------------MIEN--------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYE 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1835678661 343 FDIRVPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLL 396
Cdd:cd16146 269 GGHRVPFFIRWPgKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEgiKLDGRSLLPLL 325
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
75-407 |
9.84e-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: 135.36 E-value: 9.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 75 RIMEQGGAhFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSaswqaqhEIRTFAVYLNNTGYRTAFFGKylney 154
Cdd:cd16037 31 RLAARGTR-FENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGK----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 155 ngsyvppgwkqwvgliknsrfynytLCRNGMKEKHGFDYSKDyltdlITNDSISFFRmsKKMYPHRPVLMVISHAAPHGP 234
Cdd:cd16037 98 -------------------------LHFRGEDQRHGFRYDRD-----VTEAAVDWLR--EEAADDKPWFLFVGFVAPHFP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 235 edsapqyshlfanasqhitpsynyapnpdkhwimrYTGPMkpihmEFTNMLQRKRLQT---LMS-VDESMEQIYNALVET 310
Cdd:cd16037 146 -----------------------------------LIAPQ-----EFYDLYVRRARAAyygLVEfLDENIGRVLDALEEL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 311 AELDNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPTVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGK 390
Cdd:cd16037 186 GLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGR 264
|
330
....*....|....*..
gi 1835678661 391 SILKLLDTERPANRFHF 407
Cdd:cd16037 265 SLLPLAEGPDDPDRVVF 281
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
49-407 |
2.75e-33 |
|
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: 133.07 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQ---DVE-LGSMQVmnKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTNNE 117
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGSPLI--KTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 118 NCSSASwqaqhEIrTFAVYLNNTGYRTAFFGKYLNEYNGSYVPP--GWKQWVGLI------------KNSRFYNYTLCRN 183
Cdd:cd16026 79 GGLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIPysndmwpfplyrNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 184 gmKEKHGFDYSKDYLTDLITNDSISFFRMSKKmyphRPVLMVISHAAPHGPEDSapqySHLFANASQHitpsynyapnpd 263
Cdd:cd16026 153 --EEVIEQPADQSSLTQRYTDEAVDFIERNKD----QPFFLYLAHTMPHVPLFA----SEKFKGRSGA------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 264 khwimrytGPMKpihmeftnmlqrkrlQTLMSVDESMEQIYNALVETAELDNTYIIYTADHG--YHIGQFG-----LVKG 336
Cdd:cd16026 211 --------GLYG---------------DVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGG 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835678661 337 KSMPYEFDIRVPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLLDTERPANRFHF 407
Cdd:cd16026 268 KGTTWEGGVRVPFIAWWPgVIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLLLGGSKSPPHPF 341
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-407 |
3.48e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 127.71 E-value: 3.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQ----DVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnENCSSAS-W 124
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 125 QAQHEIRTFAVYLNNTGYRTAFFGKY-LNEYNGSYvppgwkqwvgliknsrfynytlcrngmkekhgfdYSKDyltDLIT 203
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 204 NDSISFFR-MSKKMYPHRPVLMVISHAAPH----GPEDsAPQYsHLFANAsqhitpsynYApnpdkhwimrytgpmkpih 278
Cdd:cd16035 121 AQAVEWLReRGAKNADGKPWFLVVSLVNPHdimfPPDD-EERW-RRFRNF---------YY------------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 279 meftNMLQRkrlqtlmsVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPTVEA 358
Cdd:cd16035 171 ----NLIRD--------VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFG 238
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835678661 359 G-----SLNPHivlnIDLAPTILDIAGLDIPA------DMDGKSILKLL-----DTERPANRFHF 407
Cdd:cd16035 239 TgqttdALTSH----IDLLPTLLGLAGVDAEArateapPLPGRDLSPLLtdadaDAVRDGILFTY 299
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
79-404 |
7.20e-31 |
|
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: 124.23 E-value: 7.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 79 QGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencsSASWQAqhEIRTFAVYLNNTGYRTAFFGKYlneyngSY 158
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDN-----AAEFPA--DIPTFAHYLRAAGYRTALSGKM------HF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 159 VPPgwkqwvgliknsrfynytlcrngmKEKHGFDY-------SKDYLTDLITNDsisffrmskkmyPHRPVLMVISHAAP 231
Cdd:cd16032 101 VGP------------------------DQLHGFDYdeevafkAVQKLYDLARGE------------DGRPFFLTVSFTHP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 232 HGPEDSAPQYSHLFANASQHitpSYnYApnpdkhwIMRYtgpmkpihmeftnmlqrkrlqtlmsVDESMEQIYNALVETA 311
Cdd:cd16032 145 HDPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 312 ELDNTYIIYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPTVEAGSLNPHIVLNIDLAPTILDIAG---LDIPADMD 388
Cdd:cd16032 189 LADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGggtAPHVPPLD 267
|
330
....*....|....*.
gi 1835678661 389 GKSILKLLDTERPANR 404
Cdd:cd16032 268 GRSLLPLLEGGDSGGE 283
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
50-404 |
2.58e-30 |
|
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: 125.57 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQDVELGS------MQVMNKTRriMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSas 123
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcygnkaMKTPNLDR--LAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 wqaqhEIRTFAVYLNNTGYRTAFFGKY-LN--EYNGSYV-PPGWKQ--WVGL-----------IKNSRFYNYTLCRNGMK 186
Cdd:cd16156 77 -----NVKTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMrnyldelteeeRRKSRRGLTSLEAEGIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 187 EKHGFDYSkdyltdlITNDSISFFRMSKKmyphRPVLMVISHAAPHGPEDSAPQYSHLFANASQHITPSY--NYAPNPDK 264
Cdd:cd16156 152 EEFTYGHR-------CTNRALDFIEKHKD----EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPLH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 265 H--WIMRYTGP----MKPIHMEFtnmlqrkrLQTLMSVDESMEQIYNALVETAEldNTYIIYTADHGYHIGQFGL-VKGK 337
Cdd:cd16156 221 QrlWAGAKPHEdgdkGTIKHPLY--------FGCNSFVDYEIGRVLDAADEIAE--DAWVIYTSDHGDMLGAHKLwAKGP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835678661 338 SMpYEFDIRVPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLL-DTERPANR 404
Cdd:cd16156 291 AV-YDEITNIPLIIRGKgGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIeDPEIPENR 358
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
81-438 |
7.15e-30 |
|
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: 123.91 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 81 GAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencssASWQAQHEiRTFAVYLNNTGYRTAFFGKylneynGSYVP 160
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN------GTPLDARH-LTLALELRKAGYDPALFGY------TDTSP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 161 PGwkqwVGLIKNS-RFYNYTLCRNGMKEKHGFDYSKDYLTD--LITNDSISFFRMskkmYPHRPVLMVISHAAPHGP-ED 236
Cdd:cd16028 103 DP----RGLAPLDpRLLSYELAMPGFDPVDRLDEYPAEDSDtaFLTDRAIEYLDE----RQDEPWFLHLSYIRPHPPfVA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 237 SAPqYSHLFANASqhiTPSYNYAPNPD---------KHWIMRYtgPMKPIHMEFTNM-----LQRKRLQT----LMS-VD 297
Cdd:cd16028 175 PAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMRAtylgLIAeVD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 298 ESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPTVEA----GSLNPHIVLNIDLAP 373
Cdd:cd16028 249 DHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREAdatrGQVVDAFTESVDVMP 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835678661 374 TILDIAGLDIPADMDGKSILKLLDTERPANRfhfqKKAKVWRDSFlvERGKLLHKRENEKISPQD 438
Cdd:cd16028 328 TILDWLGGEIPHQCDGRSLLPLLAGAQPSDW----RDAVHYEYDF--RDVSTRRPQEALGLSPDE 386
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
49-418 |
1.01e-29 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 124.01 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQDVE-LGSM---QVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcssASW 124
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDV---VPW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 125 QAQHEI-RTFAvylnNTGYRTAFFGKYlneyngsYVPPGwKQWVGliknsrFYNYTL----CRNGMKEKHG-FDYSKDYL 198
Cdd:PRK13759 83 NYKNTLpQEFR----DAGYYTQCIGKM-------HVFPQ-RNLLG------FHNVLLhdgyLHSGRNEDKSqFDFVSDYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 199 -------------------------------------TDLITNDSISFFRmskKMYPHRPVLMVISHAAPHGPEDSAPQY 241
Cdd:PRK13759 145 awlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 242 SHLFANASQHITPSYNYA----PNPDKHWIMRYTGPMKPihmeftNMLQRKRLQTLMS---VDESMEQIYNALVETAELD 314
Cdd:PRK13759 222 FDMYKDADIPDPHIGDWEyaedQDPEGGSIDALRGNLGE------EYARRARAAYYGLithIDHQIGRFLQALKEFGLLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 315 NTYIIYTADHGYHIGQFGLVKgKSMPYEFDIRVPFYVRGP----TVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGK 390
Cdd:PRK13759 296 NTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGR 374
|
410 420
....*....|....*....|....*...
gi 1835678661 391 SILKLLDTERPANRFHFQKKAKVWRDSF 418
Cdd:PRK13759 375 SLKNLIFGQYEGWRPYLHGEHALGYSSD 402
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
50-396 |
1.58e-29 |
|
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: 121.92 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDqdVELGSMQVMNKTRRI-------MEQGGAHFINAFVTTPMCCPSRSSILTGKYvhNHNTYTNNENCSSA 122
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY--PWRSRLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 123 SWQAQHEIR-TFAVYLNNTGYRTAFFGKY---LNEY--NGSYVPPGWKQWVGLikNSRFynytlcRNGMKEkHGFDYSkd 196
Cdd:cd16143 77 SPPLIEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKDVDY--SKPI------KGGPLD-HGFDYY-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 197 YLT------DLITNDSISFFRMSKKmyPHRPVLMVISHAAPHGPedsapqyshlfanasqhITPSYNYAPNPDkhwimry 270
Cdd:cd16143 146 FGIpasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSPEFQGKSG------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 271 TGPmkpiHMEFTnmlqrkrlqtlMSVDESMEQIYNALVETAELDNTYIIYTADHG---YHIGQFGLVKG----------K 337
Cdd:cd16143 200 AGP----YGDFV-----------YELDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgplrgmK 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835678661 338 SMPYEFDIRVPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 396
Cdd:cd16143 265 ADIYEGGHRVPFIVRWPgKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL 326
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-419 |
5.69e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 116.93 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQDVE-LGSM-QVMNKTRRI--MEQGGAHFINAFvTTPMCCPSRSSILTGKYvhNHNTYTNNENcssaSWQ 125
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKY--NFRNYVVFGY----LDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 126 AQHeirTFAVYLNNTGYRTAFFGK---YLNEYNGSYVPP-GWKQWV-------GLIKNSRFYNYTLCRNGMKEKhgfDYS 194
Cdd:cd16151 74 KQK---TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 195 KDYLTDLITNDSISFFRMSKK-----MYPhrpvlMVIshaaPHGPedsapqyshlfanasqhitpsynYAPNPD-KHWiM 268
Cdd:cd16151 148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDP-----------------------FVPTPDsPDW-D 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 269 RYTGPMKPIHMEFTNMLQrkrlqtlmSVDESMEQIYNALVETAELDNTYIIYTADHGYHIG-----QFGLVKG-KSMPYE 342
Cdd:cd16151 195 PDDKRKKDDPEYFPDMVA--------YMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 343 FDIRVPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL-----DTERPANRFHFQKKAKVW 414
Cdd:cd16151 267 AGTHVPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQLlgktgSPRREWIYWYYRNPHKKF 346
|
....*
gi 1835678661 415 RDSFL 419
Cdd:cd16151 347 GSRFV 351
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-393 |
1.57e-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: 112.33 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQ---------DVELgSMQVMNKtrriMEQGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTN 115
Cdd:cd16149 1 PNILFILTDDQgpwalgcygNSEA-VTPNLDR----LAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgIHDWIVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 116 NENCSSASWQAQHEIrTFAVYLNNTGYRTAFFGKylneyngsyvppgwkqWvgliknsrfynytlcrngmkekHGFDYSK 195
Cdd:cd16149 76 HGKTKKPEGYLEGQT-TLPEVLQDAGYRCGLSGK----------------W----------------------HLGDDAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 196 DYLTDLITNDsisffrmskkmyphRPVLMVISHAAPHGPEdsapQYshlFANASqhitpsynyapnpdkhwimrytgpmk 275
Cdd:cd16149 117 DFLRRRAEAE--------------KPFFLSVNYTAPHSPW----GY---FAAVT-------------------------- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 276 pihmeftnmlqrkrlqtlmSVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGlVKGK-------SMpYEFDIRVP 348
Cdd:cd16149 150 -------------------GVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1835678661 349 FYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMD--GKSIL 393
Cdd:cd16149 209 FIIRWPgVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
49-397 |
2.04e-27 |
|
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: 116.13 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQDVELGSMqvmnktrrimeqgGAHFI----------------NAFVTTPMCCPSRSSILTGKYVHNHNT 112
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCY-------------GGHPAktpnidrlaargvlftNAYCQQPVCGPSRASLLTGRRPDTTGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 113 YTNNencsSASWQAQHEIRTFAVYLNNTGYRTAFFGK-------YLNEYNGSYVPPGWKQwvGLIKNSRFYNYTLCRNGM 185
Cdd:cd16030 69 YDNN----SYFRKVAPDAVTLPQYFKENGYTTAGVGKifhpgipDGDDDPASWDEPPNPP--GPEKYPPGKLCPGKKGGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 186 KEKHGFDYS------KDYLTDLITNDSIS-----------FFrMS-------------KK---MYPHRPVLMVISHAAPH 232
Cdd:cd16030 143 GGGGGPAWEaadvpdEAYPDGKVADEAIEqlrklkdsdkpFF-LAvgfykphlpfvapKKyfdLYPLESIPLPNPFDPID 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 233 GPEDSAPQYSHLfanasqhitpsynyaPNPDKHWIMRYTGPMKPIHMEFtnmlQRKRLQT-LMSV---DESMEQIYNALV 308
Cdd:cd16030 222 LPEVAWNDLDDL---------------PKYGDIPALNPGDPKGPLPDEQ----ARELRQAyYASVsyvDAQVGRVLDALE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 309 ETAELDNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPTV-EAGSLNPHIVLNIDLAPTILDIAGLDIPADM 387
Cdd:cd16030 283 ELGLADNTIVVLWSDHGWHLGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCL 361
|
410
....*....|
gi 1835678661 388 DGKSILKLLD 397
Cdd:cd16030 362 EGKSLVPLLK 371
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-394 |
5.26e-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: 111.49 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTD----DQdvelgsMQVMNKTRRIM------EQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnenc 119
Cdd:cd16148 1 MNVILIVIDslraDH------LGCYGYDRVTTpnldrlAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 120 ssaSWQAQHEIRTFAVYLNNTGYRTAFFGkylneyNGSYVPPGWkqwvGLikNSRFYNYTLCRNGMKEKHGFDYSKDylt 199
Cdd:cd16148 69 ---GGPLEPDDPTLAEILRKAGYYTAAVS------SNPHLFGGP----GF--DRGFDTFEDFRGQEGDPGEEGDERA--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 200 DLITNDSISFFrmsKKMYPHRPVLMVISHAAPHGPedsapqysHLFANAsqhitpsynyapnpdkhwimrytgpmkpIHM 279
Cdd:cd16148 131 ERVTDRALEWL---DRNADDDPFFLFLHYFDPHEP--------YLYDAE----------------------------VRY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 280 eftnmlqrkrlqtlmsVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVKGKSMP-YEFDIRVPFYVRGPTVEA 358
Cdd:cd16148 172 ----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEP 235
|
330 340 350
....*....|....*....|....*....|....*.
gi 1835678661 359 GSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILK 394
Cdd:cd16148 236 GKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
50-407 |
1.69e-26 |
|
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: 112.64 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQ---DVEL-GSMQVmnKTRRIME--QGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSAS 123
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 WQAQHEiRTFAVYLNNTGYRTAFFGKY-LNEYNGSYVPPG----------------WKQWVGLIKNsrFYNYTLCRNgmk 186
Cdd:cd16029 78 GLPLNE-TLLPQYLKELGYATHLVGKWhLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSGGAND--YGNDDLRDN--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 187 EKHGFDYSKDYLTDLITNDSISFFRMSKkmyPHRPVLMVISHAAPHGPedsapqyshlfanasqhitpsyNYAPnpdKHW 266
Cdd:cd16029 152 EEPAWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAP----------------------LQVP---PEY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 267 IMRYTGPMKPIHMEftnmlQRKRLQTLMS-VDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFG------LVKGKSM 339
Cdd:cd16029 204 ADPYEDKFAHIKDE-----DRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNT 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835678661 340 PYEFDIRVPFYVRGPTVE--AGSLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLLDTERPANRFHF 407
Cdd:cd16029 279 LWEGGVRVPAFVWSPLLPpkRGTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQWDALSGGAPSPRTEI 350
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
49-408 |
4.73e-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: 111.38 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDqdveLG-----------SMQVMNKtrriMEQGGAHFiNAFVTTPMCCPSRSSILTGkyVHNHNTYTNNE 117
Cdd:cd16025 2 RPNILLILADD----LGfsdlgcfggeiPTPNLDA----LAAEGLRF-TNFHTTALCSPTRAALLTG--RNHHQVGMGTM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 118 NCSSASWQA-----QHEIRTFAVYLNNTGYRTAFFGKYLNeyngsyVPPGWkqwvgliknsrfynytlcrngmkekhgfd 192
Cdd:cd16025 71 AELATGKPGyegylPDSAATIAEVLKDAGYHTYMSGKWHL------GPDDY----------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 193 yskdYLTDLITNDSISFFRMSKKmyPHRPVLMVISHAAPHGPedsapqysHlfanasqHitpsynyAPnpdKHWIMRYTG 272
Cdd:cd16025 116 ----YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP--------L-------Q-------AP---KEWIDKYKG 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 273 P---------------MK-----PIHMEFTNML------------QRKRLQTLMSV--------DESMEQIYNALVETAE 312
Cdd:cd16025 165 KydagwdalreerlerQKelgliPADTKLTPRPpgvpawdslspeEKKLEARRMEVyaamvehmDQQIGRLIDYLKELGE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 313 LDNTYIIYTADHG--YHIG--QFG---LVKGKSMPYEFDIRVPFYVRGPTV--EAGSLNPHIVLNIDLAPTILDIAGLDI 383
Cdd:cd16025 245 LDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELAGVEY 324
|
410 420 430
....*....|....*....|....*....|...
gi 1835678661 384 PAD--------MDGKSILKLLDTERPANRFHFQ 408
Cdd:cd16025 325 PKTvngvpqlpLDGVSLLPTLDGAAAPSRRRTQ 357
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
50-406 |
6.26e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 107.82 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQDVE------LGSMQVMNKTRRIMEQGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSAS 123
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 wqaqHEI-RTFAVYLNNTGYRTAFFGKYL--NEYNGSYVPPGWKQWVGLIKN--SRFYNYTLCRNGMKEKHgfdysKDYL 198
Cdd:cd16154 80 ----ETLlQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-----TEYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 199 TDLITNDSISFFRMSkkmypHRPVLMVISHAAPHGPedsapqyshlFanasqHITPSYNYAPNPdkhwimryTGPMKPIH 278
Cdd:cd16154 151 TTKLTNLAIDWIDQQ-----TKPWFLWLAYNAPHTP----------F-----HLPPAELHSRSL--------LGDSADIE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 279 MEftnmlqrkRLQTLMSVDESMEQIYNALVET---AELDNTYIIYTADHGYHiGQ-----FGLVKGKSMPYEFDIRVPFY 350
Cdd:cd16154 203 AN--------PRPYYLAAIEAMDTEIGRLLASideEERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVPLI 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1835678661 351 VRGPTVEAGSLNPHIVLNI-DLAPTILDIAGLDIPADMDGKSILKLLDTERPANRFH 406
Cdd:cd16154 274 VSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQY 330
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
49-404 |
1.56e-23 |
|
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: 104.82 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQDV-----------ELGSM-QVMNKtrrimeqgGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNN 116
Cdd:cd16160 1 KPNIVLFFADDMGYgdlasyghptqERGPIdDMAAE--------GIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 117 ENC--SSASWQAQHEIrTFAVYLNNTGYRTAFFGKY---LNEYN---GSYVPP--GWkQWVGliKNSRFYNYTLCR---- 182
Cdd:cd16160 73 RVFlpWDIGGLPKTEV-TMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLPShhGF-DFVG--TNLPFTNSWACDdtgr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 183 --NGMKEKHGFDYSKD----------YLTDLITNDSISFFRMSKkmypHRPVLMVISHAAPHGPedsapqyshLFANAsq 250
Cdd:cd16160 149 hvDFPDRSACFLYYNDtiveqpiqheHLTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTHTP---------LFASK-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 251 hitpsynyapnpdkhwimrytgpmkpihmEFTNMLQRKRL-QTLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHI- 328
Cdd:cd16160 214 -----------------------------RFKGKSKRGRYgDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVe 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 329 -----GQFGLVKG-KSMPYEFDIRVPFYVRGPTVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLLDTER 400
Cdd:cd16160 265 yclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDLLLGEA 344
|
....
gi 1835678661 401 PANR 404
Cdd:cd16160 345 DSPH 348
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-394 |
6.86e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 96.68 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQDV------------ELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYt 114
Cdd:cd16153 1 KPNILWIITDDQRVdslscynnahtgKSESRLGYVESPNIdaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 115 NNEncssASWQAQHEIR-TFAVYLNNTGYRTAFFGKylneyngsyvpPGWKQWVGLIKNSrfyNYTLCRNGMKEKHGFDY 193
Cdd:cd16153 80 GFE----AAHPALDHGLpTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGADS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 194 SKDYLTdlitndSISFfrmskkMYPHRPVLmvishaaphgpedsapqyshlfanasqhitpsynyapnPDKHWIMRYTgp 273
Cdd:cd16153 142 DKPFFV------RLSF------LQPHTPVL--------------------------------------PPKEFRDRFD-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 274 mkpiHMEFTNMlqrkrlqtlmsVDESMEQIYNALVETAEL---DNTYIIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFY 350
Cdd:cd16153 170 ----YYAFCAY-----------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVPLI 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1835678661 351 VRGPTVE---AGSLNPHIVLNIDLAPTILDIAGLDI--PADMDGKSILK 394
Cdd:cd16153 234 VVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDLFE 282
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
50-396 |
4.76e-20 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 92.99 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQDVELgSMQVMNKTRRI-----MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSasw 124
Cdd:cd16171 1 PNVVMVMSDSFDGRL-TFRPGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 125 qaqhEIRTFAVYLNNTGYRTAFFGKyLNEYNGSY-VPPGWKQWvgliknSRFYNYTLCRNGMKekhgfdyskdyLTDLIT 203
Cdd:cd16171 77 ----NYPTWMDRLEKHGYHTQKYGK-LDYTSGHHsVSNRVEAW------TRDVPFLLRQEGRP-----------TVNLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 204 NDSISffRMSKKMYPhrpvlmvISHAAPHGPEDSAPQYSHLFA-----NASqHITPSYNYAPNpdkhwimryTGPMKPIH 278
Cdd:cd16171 135 DRSTV--RVMLKDWQ-------NTDKAVHWIRKEAPNLTQPFAlylglNLP-HPYPSPSMGEN---------FGSIRNIR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 279 MEFTNMLQRkrlqtlmsVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPTVEA 358
Cdd:cd16171 196 AFYYAMCAE--------TDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGPGIKA 266
|
330 340 350
....*....|....*....|....*....|....*...
gi 1835678661 359 GSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLL 396
Cdd:cd16171 267 GQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
49-408 |
1.48e-19 |
|
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: 93.12 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDqdveLGSMQVM---NKTRR-----IMEQGGAHFINAFVTTPMCCPSRSSILTGKY------VHNHNTYT 114
Cdd:cd16159 1 KPNIVLFMADD----LGIGDVGcfgNDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHGMRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 115 NNENCSSASWQaQHEIrTFAVYLNNTGYRTAFFGKY----------------LN-----------------------EYN 155
Cdd:cd16159 77 ILFTASSGGLP-PNET-TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 156 GSYVPPGWKQ--------------------------------------WVGLIKNSRFYNYTLCRNG-MKEKhgfDYSKD 196
Cdd:cd16159 155 LSFDPLFPLLtafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHeVVEQ---PMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 197 YLTDLITNDSISFFRMSKkmypHRPVLMVISHAAPHGPEDSAPqyshLFANASQHitpsYNYAPNpdkhwimrytgpmkp 276
Cdd:cd16159 232 NLTQRLTKEAISFLERNK----ERPFLLVMSFLHVHTALFTSK----KFKGRSKH----GRYGDN--------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 277 ihmeftnmlqrkrlqtLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHI-----------GQFGLVKGKSMP-YEFD 344
Cdd:cd16159 285 ----------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEGG 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835678661 345 IRVPFYVRGPTV-EAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLLD--TERPANRFHFQ 408
Cdd:cd16159 349 IRVPTIVRWPGViPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTgqEKRSPHEFLFH 417
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
757-806 |
3.73e-18 |
|
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: 87.61 E-value: 3.73e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1835678661 757 CTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDLNTDPYQLINAVNTL 806
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
81-404 |
1.37e-17 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 86.13 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 81 GAHFINAFVTTPMCCPSRSSILTGKY--VHNHNTYTnnencssaswqaqHEIR----TFAVYLNNTGYRTAFFGKylney 154
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLH-------------HLLRpdepNLLKTLKDAGYHVAWAGK----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 155 NGSYVPPGWKQwvgliknsrfyNYTLCrngmkekhgfdyskDYLTdliTNDSISFFRMSKkmyPHRPVLMVISHAAPHGP 234
Cdd:cd16150 98 NDDLPGEFAAE-----------AYCDS--------------DEAC---VRTAIDWLRNRR---PDKPFCLYLPLIFPHPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 235 -EDSAPQYSHLFANAS-QHITPSYNYAPNPDKHWIMRYTGpMKPIHMEFTNMLQRKRLQTLMSVDESMEQIYNALVETAE 312
Cdd:cd16150 147 yGVEEPWFSMIDREKLpPRRPPGLRAKGKPSMLEGIEKQG-LDRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 313 LDNTYIIYTADHGYHIGQFGLV-KGKSMPYEFDIRVPFYVRGPTVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKS 391
Cdd:cd16150 226 YDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRS 305
|
330
....*....|...
gi 1835678661 392 ILKLLDTERPANR 404
Cdd:cd16150 306 LLPVLAGETEEHR 318
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
49-414 |
4.43e-17 |
|
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: 85.21 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDDQDV-ELGSMQVMNK-TRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSA-- 122
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 123 -----SWQAQHEIrTFAVYLNNTGYRTAFFGKYLNEYNGSYVP--PGWKQW-------VGLIKNSRFYNYTLCRNG-MKE 187
Cdd:cd16157 81 pqnivGGIPDSEI-LLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWfgapnchFGPYDNKAYPNIPVYRDWeMIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 188 KHGFDYSKDY------LTDLITNDSISFfrMSKKMYPHRPVLMVISHAAPHgpedsAPQYshlfanASQHitpsynyapn 261
Cdd:cd16157 160 RYYEEFKIDKktgesnLTQIYLQEALEF--IEKQHDAQKPFFLYWAPDATH-----APVY------ASKP---------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 262 pdkhwimrytgpmkpihmeFTNMLQRKRL-QTLMSVDESMEQIYNALVETAELDNTYIIYTADHG---YHIGQFG----- 332
Cdd:cd16157 217 -------------------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngp 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 333 LVKGKSMPYEFDIRVPFYVRGP-TVEAGSLNpHIVLNI-DLAPTILDIAGLDIPAD--MDGKSILKLLDTERPANRFHF- 407
Cdd:cd16157 278 FLCGKQTTFEGGMREPAIAWWPgHIKPGQVS-HQLGSLmDLFTTSLALAGLPIPSDraIDGIDLLPVLLNGKEKDRPIFy 356
|
410
....*....|....*....
gi 1835678661 408 ------------QKKAKVW 414
Cdd:cd16157 357 yrgdelmavrlgQYKAHFW 375
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
50-424 |
1.41e-15 |
|
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: 80.57 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDQDV-ELG-----SMQVMNKTRriMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSAS 123
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 WQAQHEIrTFAVYLNNTGYRTAFFGKY---LNEyNGSYVPPgwkqwvgliknsrfynytlcRNGMKEKHGFDYSKDY--- 197
Cdd:cd16158 80 GLPLNET-TIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT--------------------HQGFDHYLGIPYSHDQgpc 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 198 --LTDLITNDSIsfFRMSKKMYPHRPVLM--VISHAAPHGPeDSAPQY----SHLFANASQHITPSYNYAPNPDKHWiMR 269
Cdd:cd16158 138 qnLTCFPPNIPC--FGGCDQGEVPCPLFYneSIVQQPVDLL-TLEERYakfaKDFIADNAKEGKPFFLYYASHHTHY-PQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 270 YTGpmkpihMEFTNMLQRKRL-QTLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHI------GQFGLVK-GKSMPY 341
Cdd:cd16158 214 FAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 342 EFDIRVPFYVRGPTVEAGSLNPHIVLNIDLAPTILDIAGLDIP-ADMDGKSILKLLDTERPANR---FHFQKKAKVWRDS 417
Cdd:cd16158 288 EGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPnVTLDGVDMSPILFEQGKSPRqtfFYYPTSPDPDKGV 367
|
....*..
gi 1835678661 418 FLVERGK 424
Cdd:cd16158 368 FAVRWGK 374
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
50-379 |
1.15e-14 |
|
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: 74.38 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDD---QDVELGSMQVMNKTR-RIMEQGGAHFiNAFVTTPMC--CPSRSSILTGKYVHNHNTYTNNENCSSAS 123
Cdd:cd00016 1 KHVVLIVLDGlgaDDLGKAGNPAPTTPNlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 WQAQHEI---RTFAVYLNNTGYRTAFFG--KYLNEyngsyvppgwkqwvgliknsrfynytlcrngmkekhgfdyskdyl 198
Cdd:cd00016 80 SRAAGKDedgPTIPELLKQAGYRTGVIGllKAIDE--------------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 199 tdlitndsisffrmskkMYPHRPVLMVISHAAPHGPedsapqyshlfanasqhitpSYNYAPNPDkhwimrytgpmkpih 278
Cdd:cd00016 115 -----------------TSKEKPFVLFLHFDGPDGP--------------------GHAYGPNTP--------------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 279 mEFTNMLQRkrlqtlmsVDESMEQIYNALVETAELDNTYIIYTADHG---YHIGQFGLVKGKSMPYEFDIRVPFYVRGPT 355
Cdd:cd00016 143 -EYYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPG 213
|
330 340
....*....|....*....|....
gi 1835678661 356 VEAGSLNPHIVLNIDLAPTILDIA 379
Cdd:cd00016 214 VKKGGVKHELISQYDIAPTLADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
49-407 |
4.73e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 75.85 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLtddqdVElgSMQ--VMNKT----------RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKY-VHNHNTYTN 115
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 116 NencssaswqAQHEIRTFAVYLNNTGYRTAFFgkylneYNGsyvppgwkqwvglikNSRFYNytlcRNGMKEKHGFD--Y 193
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 194 SKDYLTDLITN-----DSiSFFRMSKKMYPhrpvlmvishaaphgpEDSAPQYSHLFaNASQHiTPsYNYaPNPDKHWIm 268
Cdd:COG1368 352 DREDFDDPFDGgwgvsDE-DLFDKALEELE----------------KLKKPFFAFLI-TLSNH-GP-YTL-PEEDKKIP- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 269 rytgpmkpihmEFTNMLQRKRLQTLMSVDESMEQIYNALVETAELDNTYIIYTADHGyhigqfGLVKGKSmPYEFDI--- 345
Cdd:COG1368 410 -----------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLery 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835678661 346 RVPFYVRGPTVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD-MDGKSILKLLDTERPANRFHF 407
Cdd:COG1368 472 RVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDLLSPDTDPFAFRNGGF 534
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
50-386 |
5.11e-14 |
|
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: 74.49 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVLTDDqdveLGSMQV--------M-NKTRRI--MEQGGAHFINAFVTtPMCCPSRSSILTGKYVhnhntytNNEN 118
Cdd:cd16142 1 PNILVILGDD----IGWGDLgcygggigRgAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 119 CSSASWQAQ-----HEIRTFAVYLNNTGYRTAFFGK-YLNEYNGSYvpPgwkqwvgliknsrfynytlcrngmkEKHGFD 192
Cdd:cd16142 69 LTTVGLPGSpgglpPWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--P-------------------------TDHGFD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 193 YSKDYLT----DLITNDSISFFRMSKKmyPHRPVLMVISHAAPHGPEDSAPQYSHlfanasqHITPSYNYApnpdkhwim 268
Cdd:cd16142 122 EFYGNLYhtidEEIVDKAIDFIKRNAK--ADKPFFLYVNFTKMHFPTLPSPEFEG-------KSSGKGKYA--------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 269 rytgpmkpihmeftnmlqrkrlQTLMSVDESMEQIYNALVETAELDNTYIIYTADHG-----YHIGQFGLVKG-KSMPYE 342
Cdd:cd16142 184 ----------------------DSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWE 241
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1835678661 343 FDIRVPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD 386
Cdd:cd16142 242 GGVRVPAIVRWPgKIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
50-380 |
2.80e-12 |
|
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: 68.09 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 50 PNIILVL-----TDDQDVELGSMQVMNKTRRIMEQGgAHFINAFVTTPMCCPSRS--SILTGkyvhnhnTYTNNENCSSA 122
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 123 SWQAQHEIRTFAVYLNNTGYRTAFFgkylneYNGsyvppgwkqwvglikNSRFYNytlcRNGMKEKHGFD--YSKDYLTD 200
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 201 LITNDSI------SFFRMSKKMY---PHRPVLMVISHAAPHGPedsapqyshlfanasqhitpsYNYAPNPDKhwimryt 271
Cdd:cd16015 128 DEKETNGwgvsdeSLFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 272 gpmKPIHMEFTNMLQRKRLQTLMSVDESMEQIYNALVETAELDNTYIIYTADHGYHIGQFGLVKGKSMPYEFdiRVPFYV 351
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 1835678661 352 RGPTVEAGSLNPHIVLNIDLAPTILDIAG 380
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
49-396 |
3.02e-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: 69.42 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 49 RPNIILVLTDD---QDVELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYvHNHNTYTNNENCSSAS 123
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRL-GLRNGVGHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 124 WQAQHEIrTFAVYLNNTGYRTAFFGKYLNEYNGSYVPpgwkqwvglikNSRFYNYTLcrngmkekhGFDYSKD-YLTDLI 202
Cdd:cd16161 80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---------GIPFSHDsSLADRY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 203 TNDSISFF-RMSKKmypHRPVLMVISHAAPHGPEDSAPqyshLFANASQHITPsynyapnpdkhwimryTGpmkpihmef 281
Cdd:cd16161 139 AQFATDFIqRASAK---DRPFFLYAALAHVHVPLANLP----RFQSPTSGRGP----------------YG--------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 282 tnmlqrkrlQTLMSVDESMEQIYNALVETAELDNTYIIYTAD---------------HGYHIGQFGLVKGKSMPYEFDIR 346
Cdd:cd16161 187 ---------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHR 257
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1835678661 347 VPFYVRGP-TVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 396
Cdd:cd16161 258 EPAIVYWPgRIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
296-393 |
2.27e-08 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 57.43 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 296 VDESMEQIYNALVEtaeLDNTYIIyTADHG-----YHIGQFGLVKGKSMPyefdiRVPFYVRGP-----TVEAGSLnphi 365
Cdd:cd16010 412 VDECLGRIVEAVLE---NGGTLLI-TADHGnaeemIDPETGGPHTAHTTN-----PVPFIIVDPglkrkLLKDGGL---- 478
|
90 100
....*....|....*....|....*...
gi 1835678661 366 vlnIDLAPTILDIAGLDIPADMDGKSIL 393
Cdd:cd16010 479 ---ADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
296-394 |
4.86e-08 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 56.65 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 296 VDESMEQIYNALVEtaeLDNTYIIyTADHG-------YHIGQfglvkgksmPY-----EfdiRVPF-YVRGPTV--EAGS 360
Cdd:PRK05434 417 VDECLGRVVDAVLK---VGGTLLI-TADHGnaeqmidPETGQ---------PHtahttN---PVPFiLVGGKALrlEGGK 480
|
90 100 110
....*....|....*....|....*....|....
gi 1835678661 361 LNphivlniDLAPTILDIAGLDIPADMDGKSILK 394
Cdd:PRK05434 481 LA-------DIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
296-394 |
8.28e-07 |
|
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440460 Cd Length: 511 Bit Score: 52.75 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 296 VDESMEQIYNALVETaelDNTYIIyTADHG---YHIGqfgLVKGKSM------PyefdirVPFYVRGPTvEAGSLNPHIV 366
Cdd:COG0696 418 VDECLGRVVDAVLAA---GGTLLI-TADHGnaeQMID---PDTGGPHtahttnP------VPFILVGGD-KGVKLREDGR 483
|
90 100
....*....|....*....|....*...
gi 1835678661 367 LnIDLAPTILDIAGLDIPADMDGKSILK 394
Cdd:COG0696 484 L-ADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
236-376 |
7.53e-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: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 236 DSAPQYSHLFANASQhitPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDESMEQIYNALVETAELDN 315
Cdd:COG3083 379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835678661 316 TYIIYTADHGY-----------HIGQFGlvkgksmPYEfdIRVPFYVRGPTVEAGSLNpHIVLNIDLAPTIL 376
Cdd:COG3083 456 TIVIITADHGEefnengqnywgHNSNFS-------RYQ--LQVPLVIHWPGTPPQVIS-KLTSHLDIVPTLM 517
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
349-398 |
2.19e-05 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 47.98 E-value: 2.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1835678661 349 FYVRGPTVEAGSLNPHIVLnIDLAPTILDIAGLDIPADMDGKSILKLLDT 398
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFAR 470
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
258-380 |
9.51e-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: 45.27 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 258 YAPNPD--KHwimRYtGPMKPihmEFTNMLQRkrlqtlmsVDESMEQIYNALVETAELDNTYIIYTADHGY-----HiGQ 330
Cdd:cd16018 163 YFEEPDsaGH---KY-GPDSP---EVNEALKR--------VDRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GY 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1835678661 331 FglvkgksmPYEFDIRVPFYVRGPTVEAGSLNPHIvLNIDLAPTILDIAG 380
Cdd:cd16018 227 D--------NELPDMRAIFIARGPAFKKGKKLGPF-RNVDIYPLMCNLLG 267
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
297-392 |
5.63e-04 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 42.94 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 297 DESMEQIYNALVETAELDNTYIIYTADHGY-----HigqfglvkGKSMPYEfdIRVPFYVRGPTVEAGSLNPH------- 364
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHGMtdagnH--------GGSSPGE--TSVPLLFISPKFSSKPSNADgelsyye 246
|
90 100
....*....|....*....|....*...
gi 1835678661 365 IVLNIDLAPTILDIAGLDIPADMDGKSI 392
Cdd:cd16024 247 TVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
296-404 |
2.68e-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: 41.18 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 296 VDESMEQIYNALVETAELDNTYIIYTADHGYHIGQF-GLVKGK---SMPYEFdIRVP--FYVRGPT-VEAGSLNPH-IVL 367
Cdd:pfam02995 313 LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLrRTSQGMleeRLPLMS-IRYPpwFRETYPQaVENLELNANrLTT 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1835678661 368 NIDLAPTILDIAGLDIPADMDGKSILKLLDTER--------PANR 404
Cdd:pfam02995 392 PFDLHATLKDILHLGELSDKELQDRMKALDCPRgislflpiPDNR 436
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|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
291-384 |
4.65e-03 |
|
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293743 [Multi-domain] Cd Length: 292 Bit Score: 40.04 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 291 QTLMSVDESMEQIYNALVetaelDNTYIIYTADHG-----YHIGQ---------FGLVKGKSMP--YEFDIRVPFYVRGP 354
Cdd:cd16019 180 KKLDQMDNLIRDIYDRMD-----NDTLLVVVSDHGmnndgNHGGSsteetssffFFISKKGFFKkrPIDQIEKIKQNNEQ 254
|
90 100 110
....*....|....*....|....*....|
gi 1835678661 355 TVEAGSLNPHIVLNIDLAPTILDIAGLDIP 384
Cdd:cd16019 255 QKIDPSEYIRIIYQIDILPTICYLLGIPIP 284
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
290-385 |
6.34e-03 |
|
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293744 Cd Length: 294 Bit Score: 39.49 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835678661 290 LQTLMSVDESMEQIYNaLVETAELDN-TYIIYTADHG-----YHigqfglvkGKSMPYEfdIRVPFY-----VRGPTVEA 358
Cdd:cd16020 182 LENIRYVDKGIEKTYP-LIEEYFNDGrTAYIFTSDHGmtdwgSH--------GDGSPDE--TETPFIawgagIKHPTPGR 250
|
90 100 110
....*....|....*....|....*....|....*..
gi 1835678661 359 GSLNP----------HIVLNIDLAPTILDIAGLDIPA 385
Cdd:cd16020 251 GPSFSanwgglrlprHDLDQADLAPLMSALLGLPPPV 287
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