|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
76-418 |
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: 545.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNE--NCSSPSWQA 153
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 154 QHESRTFAVYLNSTGYRTAFFGKYLNEY----NGSYVPPGWKEWVGLLKNSRFYNYTLCrNGVKEKHGSDYSTDYLTDLI 229
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 230 TNDSVSFFRTSKKMypHRPVLMVISHAAPHGPEDSAPQYSRLFPNAS-QHITPSYNYAPNPDKHWIMRYTGPMkPIHMEF 308
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLN-PTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 309 TNMLQRKRLQTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGSL 388
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 357588455 389 NPHIVLNIDLAPTILDIAGLDIPADMDGKS 418
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
76-448 |
6.99e-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: 292.13 E-value: 6.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQ--DVeLGSMQ-VMNKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcSSP 149
Cdd:cd16031 2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 150 SWQaqhesRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGvkekhGSDYSTDYLTDLI 229
Cdd:cd16031 79 ASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENG-----KRVGQKGYVTDII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 230 TNDSVSFFRTSKKmypHRPVLMVISHAAPHGPEDSAPQYSRLFPNAsqHITP-----SYNYAPNPD--KHWIMRYTGPMK 302
Cdd:cd16031 149 TDKALDFLKERDK---DKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEpetfdDDDYAGRPEwaREQRNRIRGVLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 303 -PIHMEFT---NMlqRKRLQTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYV 378
Cdd:cd16031 224 gRFDTPEKyqrYM--KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLII 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357588455 379 RGP-NVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDserpvnrfhlKKKLRVWRDSFLVE 448
Cdd:cd16031 301 RDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
76-456 |
1.04e-70 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 239.39 E-value: 1.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQDV-ELGSM-QVMNKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPs 150
Cdd:COG3119 23 RPNILFILADDLGYgDLGCYgNPLIKTpniDRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 wqAQHESRTFAVYLNSTGYRTAFFGKYLNeyngsyvppgwkewvgllknsrfynytlcrngvkekhgsdystdYLTDLIT 230
Cdd:COG3119 101 --LPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLLT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 231 NDSVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPNasQHITPSYNYAPNPDKHWIMRYtgpmkpihmeftn 310
Cdd:COG3119 135 DKAIDFLERQAD--KDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 311 mLQRKRLQTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPN-VEAGSLN 389
Cdd:COG3119 198 -ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVS 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357588455 390 PHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERPvnrfhlkkklrVWRDSFLVERGKLLHKR 456
Cdd:COG3119 277 DALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKA-----------EWRDYLYWEYPRGGGNR 332
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
566-702 |
8.37e-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: 211.05 E-value: 8.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 566 KTSYARNRSIRSVAIEVDGEIYHVGLD---TVPQPRNLSKPHwpgAPEDQDDKDGGS-FSGTGGLPD----YSAPNPIKV 637
Cdd:pfam12548 1 KPRFVRTRQKRSLSVEFEGEVYDIDLEeeyQPLEPRNLLKRH---ARDDGEEGEEGEeSSGTGSKRDssnsVGPPASVKV 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357588455 638 THRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHR 702
Cdd:pfam12548 78 THRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
76-428 |
1.23e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 180.84 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDD---QDveLGSMQVMN-KT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencss 148
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTpnlDRLAKEG-VVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 149 pSWQAQHESRTFAVYLNSTGYRTAFFGK--------YLNEYNGSYVPP----GWKEWVGLLKNSRFYNYTLCRNGVKEKH 216
Cdd:cd16034 72 -DVPLPPDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 217 GSDYSTDYLTDLItndsVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQ-YSRLFPNASQHitpsynYAPNPDKhwim 295
Cdd:cd16034 151 IKGYSPDAETDLA----IEYLENQAD--KDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLL------LRPNVPE---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 296 rytgpmkpihmeftNMLQRKRLQTLM--------SVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVkGKSMP 367
Cdd:cd16034 215 --------------DKKEEAGLREDLrgyyamitALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVP 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357588455 368 YEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERP 428
Cdd:cd16034 280 YEESIRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKD 341
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
77-418 |
3.10e-47 |
|
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: 168.38 E-value: 3.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQ---DVE-LGSMQVmnKT---RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENcssP 149
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 150 SWQAQHEsRTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHgsdystdyltdli 229
Cdd:cd16022 75 GGLPPDE-PTLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 230 tNDSVSFFRTSKKmypHRPVLMVISHAAPHGPedsapqysrlfpnasqhitpsYNYApnpdkhwimrytgpmkpiHMeft 309
Cdd:cd16022 103 -DEAIDFIERRDK---DKPFFLYVSFNAPHPP---------------------FAYY------------------AM--- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 310 nmlqrkrlqtLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNV-EAGSL 388
Cdd:cd16022 137 ----------VSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKiPAGQV 206
|
330 340 350
....*....|....*....|....*....|
gi 357588455 389 NPHIVLNIDLAPTILDIAGLDIPADMDGKS 418
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
77-431 |
1.35e-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: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQDVELGSmqVMN---KTRRIME--QGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencSSPSW 151
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGL----RSRGF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 152 QAQHESRTFAVYLNSTGYRTAFFGKYlnEYNGSYVPPGWKEWVGllknsrfynytlcrngvkEKHGSDYSTDYLtdlitn 231
Cdd:cd16027 75 PLPDGVKTLPELLREAGYYTGLIGKT--HYNPDAVFPFDDEMRG------------------PDDGGRNAWDYA------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 232 DSVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASqhITPSYNYAPNPdkhwIMRYtgpmkpihmEFTNM 311
Cdd:cd16027 129 SNAADFLNRAK--KGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEK--VKVPPYLPDTP----EVRE---------DLADY 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 312 LQrkrlqTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYhigqfGLVKGKSMPYEFDIRVPFYVRGPN-VEAGSLNP 390
Cdd:cd16027 192 YD-----EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKPGSVSD 261
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 357588455 391 HIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERPVNR 431
Cdd:cd16027 262 ALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
77-423 |
1.90e-45 |
|
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: 169.26 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDqdveLGSMQV---MNK---TRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKY--------VHNHNTY 140
Cdd:cd16144 1 PNIVLILVDD----LGWADLgcyGSKfyeTPNIdrLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 141 TNNENCSSPSWQAQH---ESRTFAVYLNSTGYRTAFFGKY-LNEYNGSYvpP---GWKEWVGLLKNSRFYNYTLCRNGVK 213
Cdd:cd16144 77 PPDNTKLIPPPSTTRlplEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 214 EKHGSDYSTDYLTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSRLFPNAsqhitpsynYAPNPDKHW 293
Cdd:cd16144 155 PDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKYEKK---------KKGLRKGQK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 294 IMRYTGpmkpihmeftnMLQrkrlqtlmSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLV-------KGKSM 366
Cdd:cd16144 222 NPVYAA-----------MIE--------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGGKGS 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 367 PYEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLL 423
Cdd:cd16144 283 LYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLL 342
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
77-427 |
6.36e-43 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 161.61 E-value: 6.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQDV-ELGSM-QVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKyvHNHNTY--TNNENCSSPS 150
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTGHTRvrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 WQAqhESRTFAVYLNSTGYRTAFFGKY-LNEYNGSYVPP--GWKEWVGLLKNSR---FYNYTLCRNGVKEK--------- 215
Cdd:cd16145 79 LPP--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGYLDQVHahnYYPEYLWRNGEKVPlpnnvippl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 216 ----HGSDYSTDYLTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPedsapqysrlfpnasqHITPSYNYAPNPDK 291
Cdd:cd16145 157 degnNAGGGGGTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAP----------------LQVPDDGPYKYKPK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 292 HWIMRYTGPMKPIHMEFTNMLQRkrlqtlmsVDDSMETIYDMLVETGELDNTYILYTADHGYHI-------GQF-----G 359
Cdd:cd16145 217 DPGIYAYLPWPQPEKAYAAMVTR--------LDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngP 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 360 LVKGK-SMpYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSER 427
Cdd:cd16145 289 LRGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGKP 357
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
76-428 |
3.26e-41 |
|
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: 155.46 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQ--DVeLGSM-QVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNenCSSPS 150
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 wqaqhESRTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHGSDYSTDYLTDLit 230
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 231 ndSVSFFRTSKKmypHRPVLMVISHAAPH---------GPEDSAPQYS--------RLFP-NASQHItpsynyapnPDkh 292
Cdd:cd16152 113 --AIDYLDNRQK---DKPFFLFLSYLEPHhqndrdryvAPEGSAERFAnfwvppdlAALPgDWAEEL---------PD-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 293 wimrYTGpmkpihmeftnMLQRkrlqtlmsVDDSMETIYDMLVETGELDNTYILYTADHGYHigqFGLVKG--KSMPYEF 370
Cdd:cd16152 177 ----YLG-----------CCER--------LDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 357588455 371 DIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERP 428
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVE 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
77-408 |
5.07e-39 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 5.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQ---DVELGSMqVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNEncsspsW 151
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLYGY-PRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 152 QAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGLLKNSRFYNYTLCRNGVKEKHGsdystdYLTDLI 229
Cdd:pfam00884 74 GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 230 TNDSVSFFRTskkmyPHRPVLMVISHAAPHGPedsaPQYSRLFPNASQHITPSYNYAPNPDkhwimrytgpmkpihmeft 309
Cdd:pfam00884 148 LDEALEFLDN-----NDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 310 nmlqRKRLQTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFG--LVKGKSM-PYEFDIRVPFYVRGPNVEA- 385
Cdd:pfam00884 200 ----NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAk 275
|
330 340
....*....|....*....|...
gi 357588455 386 GSLNPHIVLNIDLAPTILDIAGL 408
Cdd:pfam00884 276 GQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-448 |
3.15e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 145.06 E-value: 3.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQ--DVELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQ 152
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 153 AQHESRTFAVYLNSTGYRTAFFGKY--LNEYN-GSYvppGWKEWVGllknsrfynytlcrngvKEKHGsDYstdYLTDLi 229
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWhvGPEETpLDY---GFDEYLP-----------------VETTI-EY---FLADR- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 230 tndSVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYN--YAPNPDKHWIMRytgpMKPIHME 307
Cdd:cd16033 136 ---AIEMLEELAA--DDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFAddFEDKPYIYRRER----KRWGVDT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 308 FTNMLQRKRLQ------TLMsvDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLV-KGKSMpYEFDIRVPFYVRG 380
Cdd:cd16033 207 EDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKW 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357588455 381 PNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERPVNrfhlkkklrvWRDSFLVE 448
Cdd:cd16033 284 PGViAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
76-461 |
4.96e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 143.47 E-value: 4.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQDVE----LGSMQVmnKTRRI--MEQGGAHFINAFVTTPM----CCPSRSSILTGKYVHNhntYTNNEN 145
Cdd:cd16155 2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 146 CSSPSwqaqhESRTFAVYLNSTGYRTAFFGKYLNEYngsyvppgwkewvgllknsrfynytlcrngvkekhgsdystdyl 225
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 226 tdliTNDSVSFFRTSKKmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPnaSQHITPSYNYAP-NPdkhwimrytgpmkpi 304
Cdd:cd16155 108 ----ADAAIEFLEEYKD--GDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLPqHP--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 305 hmeFTNMLQRKRLQTL-------------------MS--VDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVkG 363
Cdd:cd16155 165 ---FDNGEGTVRDEQLapfprtpeavrqhlaeyyaMIthLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-G 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 364 KSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERPVNRFHLKKKLRVWRD 443
Cdd:cd16155 241 KQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDTLYGAYRDGQR 320
|
410
....*....|....*...
gi 357588455 444 SFLVERGKLLHKREGDKV 461
Cdd:cd16155 321 AIRDDRWKLIIYVPGVKR 338
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
77-426 |
1.30e-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: 140.38 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQ---DVELGSMQVMnKT---RRIMEQGgAHFINaFVTTPMCCPSRSSILTGKYVHN---HNTYTNNENCS 147
Cdd:cd16146 1 PNVILILTDDQgygDLGFHGNPIL-KTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHTILGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 148 SpswqaqhESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGL----------LKNSRFYNYTLCRNGVKEK 215
Cdd:cd16146 78 L-------DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdYWGNDYFDDTYYHNGKFVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 216 HGSdystdYLTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYApnpdkhwim 295
Cdd:cd16146 151 TEG-----YCTDVFFDEAIDFIEENKD----KPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG--------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 296 rytgpmkpihmeftnMLQRkrlqtlmsVDDSMETIYDMLVETGELDNTYILYTADHGYHIG-----QFGLVKGKSMPYEF 370
Cdd:cd16146 213 ---------------MIEN--------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEG 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 357588455 371 DIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLLDSE 426
Cdd:cd16146 270 GHRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPEgiKLDGRSLLPLLKGE 328
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
76-431 |
1.39e-34 |
|
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: 136.92 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQ---DVE-LGSMQVmnKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTNNE 144
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGSPLI--KTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 145 NCSSPSwqaqheSRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPP--GWKEWVGLL------------KNSRFYNYTLCRN 210
Cdd:cd16026 79 GGLPPD------EITIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIPysndmwpfplyrNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 211 GVKEKHGSDYSTdyLTDLITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPedsapqysrLFPNasqhitpsynyapnpd 290
Cdd:cd16026 153 EEVIEQPADQSS--LTQRYTDEAVDFIERNKD----QPFFLYLAHTMPHVP---------LFAS---------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 291 khwimrytgpmkpihMEFTNMLQRKRL-QTLMSVDDSMETIYDMLVETGELDNTYILYTADHG--YHIGQFG-----LVK 362
Cdd:cd16026 202 ---------------EKFKGRSGAGLYgDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRG 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357588455 363 GKSMPYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLLDSERPVNR 431
Cdd:cd16026 267 GKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLLLGGSKSPP 338
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
108-428 |
4.90e-31 |
|
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: 127.38 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 108 GAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNnencSSPswQAQHEsRTFAVYLNSTGYRTAFFGK----------- 176
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARH-LTLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 177 YLNEYNGSY--VPPGWkEWVGLLknsrfynytlcrNGVKEKHgSDysTDYLTDlitnDSVSFFRTskkmYPHRPVLMVIS 254
Cdd:cd16028 109 PLDPRLLSYelAMPGF-DPVDRL------------DEYPAED-SD--TAFLTD----RAIEYLDE----RQDEPWFLHLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 255 HAAPHGP-EDSAPqYSRLFPNASqhiTPSYNYAPNPD---------KHWIMRYtgPMKPIHMEFTNM-----LQRKRLQT 319
Cdd:cd16028 165 YIRPHPPfVAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 320 ----LMS-VDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNVEA----GSLNP 390
Cdd:cd16028 239 tylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREAdatrGQVVD 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 357588455 391 HIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERP 428
Cdd:cd16028 318 AFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQP 355
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
102-432 |
1.62e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 123.04 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 102 RIMEQGGAhFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpswqaqhESRTFAVYLNSTGYRTAFFGK--YLN 179
Cdd:cd16037 31 RLAARGTR-FENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 180 EyngsyvppgwkewvgllknsrfynytlcrngvKEKHGSDYstdylTDLITNDSVSFFRTSKkmyPH-RPVLMVISHAAP 258
Cdd:cd16037 103 E--------------------------------DQRHGFRY-----DRDVTEAAVDWLREEA---ADdKPWFLFVGFVAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 259 HgpedsapqysrlFPnasqhitpsynyapnpdkhwimrYTGPMkpihmEFTNMLQRKRLQT---LMS-VDDSMETIYDML 334
Cdd:cd16037 143 H------------FP-----------------------LIAPQ-----EFYDLYVRRARAAyygLVEfLDENIGRVLDAL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 335 VETGELDNTYILYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPADM 414
Cdd:cd16037 183 EELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL 261
|
330
....*....|....*...
gi 357588455 415 DGKSILKLLDSERPVNRF 432
Cdd:cd16037 262 DGRSLLPLAEGPDDPDRV 279
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
77-423 |
1.89e-30 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 124.62 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDqdVELGSMQVMNKTRRI-------MEQGGAHFINAFVTTPMCCPSRSSILTGKYvhNHNTYTNNENCSSP 149
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY--PWRSRLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 150 SWQAQHESR-TFAVYLNSTGYRTAFFGKY---LNEY--NGSYVPPGWKEWVGLLKNsrfynytlCRNGVKEkHGSDYS-- 221
Cdd:cd16143 77 SPPLIEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKDVDYSKP--------IKGGPLD-HGFDYYfg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 222 --TDYLTDLITNDSVSFFRTSKKmyPHRPVLMVISHAAPHGPedsapqysrlfpnasqhITPSYNYAPNPDkhwimryTG 299
Cdd:cd16143 148 ipASEVLPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSPEFQGKSG-------AG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 300 PmkpiHMEFTnmlqrkrlqtlMSVDDSMETIYDMLVETGELDNTYILYTADHG---YHIGQFGLVKG----------KSM 366
Cdd:cd16143 202 P----YGDFV-----------YELDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgplrgmKAD 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 367 PYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 423
Cdd:cd16143 267 IYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL 326
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-412 |
1.50e-29 |
|
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: 120.00 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQ----DVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnENCSSPS-W 151
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 152 QAQHESRTFAVYLNSTGYRTAFFGKY-LNEYNGSYvppgwkewvgllknsrfYNYtlcrngvkekhgsdystdylTDLIT 230
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG-----------------YKR--------------------DPGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 231 NDSVSFFRTSKKMYPHR-PVLMVISHAAPH----GPEDsAPQYsRLFPNAsqhitpsynYApnpdkhwimrytgpmkpih 305
Cdd:cd16035 121 AQAVEWLRERGAKNADGkPWFLVVSLVNPHdimfPPDD-EERW-RRFRNF---------YY------------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 306 meftNMLQRkrlqtlmsVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEA 385
Cdd:cd16035 171 ----NLIRD--------VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFG 238
|
330 340 350
....*....|....*....|....*....|..
gi 357588455 386 G-----SLNPHivlnIDLAPTILDIAGLDIPA 412
Cdd:cd16035 239 TgqttdALTSH----IDLLPTLLGLAGVDAEA 266
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-423 |
9.48e-29 |
|
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: 119.24 E-value: 9.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQDVE-LGSM-QVMNKTRRI--MEQGGAHFINAFvTTPMCCPSRSSILTGKYvhNHNTYTNNencsSPSWQ 152
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKY--NFRNYVVF----GYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 153 AQHesrTFAVYLNSTGYRTAFFGK---YLNEYNGSYVPP-GWKEWV-------GLLKNSRFYNYTLCRNGVKEKH----- 216
Cdd:cd16151 74 KQK---TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLETtegdy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 217 GSDYSTDYLTDLI-TNDSVSFFrtskKMYPhrpvlMVIshaaPHGPedsapqysrlfpnasqhitpsynYAPNPD-KHWi 294
Cdd:cd16151 151 GPDLFADFLIDFIeRNKDQPFF----AYYP-----MVL----VHDP-----------------------FVPTPDsPDW- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 295 MRYTGPMKPIHMEFTNMLQrkrlqtlmSVDDSMETIYDMLVETGELDNTYILYTADHGYHIG-----QFGLVKG-KSMPY 368
Cdd:cd16151 194 DPDDKRKKDDPEYFPDMVA--------YMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTT 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 357588455 369 EFDIRVPFYVRGP-NVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 423
Cdd:cd16151 266 DAGTHVPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL 323
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
76-426 |
1.64e-27 |
|
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: 116.00 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDqdveLG-----------SMQVMNKtrriMEQGGAHFiNAFVTTPMCCPSRSSILTGKYVH-NHNTYTNN 143
Cdd:cd16025 2 RPNILLILADD----LGfsdlgcfggeiPTPNLDA----LAAEGLRF-TNFHTTALCSPTRAALLTGRNHHqVGMGTMAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 144 ENCSSPSWQAQ--HESRTFAVYLNSTGYRTAFFGKYLNeyngsyVPPGWkewvgllknsrfynytlcrngvkekhgsdYS 221
Cdd:cd16025 73 LATGKPGYEGYlpDSAATIAEVLKDAGYHTYMSGKWHL------GPDDY-----------------------------YS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 222 TDYLTDlitnDSVSFFRTSKKmyPHRPVLMVISHAAPHGPedsapqysrlfpnasQHitpsynyAPnpdKHWIMRYTGP- 300
Cdd:cd16025 118 TDDLTD----KAIEYIDEQKA--PDKPFFLYLAFGAPHAP---------------LQ-------AP---KEWIDKYKGKy 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 301 --------------MK-----PIHMEFTNML------------QRKRLQTLMSV--------DDSMETIYDMLVETGELD 341
Cdd:cd16025 167 dagwdalreerlerQKelgliPADTKLTPRPpgvpawdslspeEKKLEARRMEVyaamvehmDQQIGRLIDYLKELGELD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 342 NTYILYTADHG--YHIG--QFG---LVKGKSMPYEFDIRVPFYVRGPNV--EAGSLNPHIVLNIDLAPTILDIAGLDIPA 412
Cdd:cd16025 247 NTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELAGVEYPK 326
|
410 420
....*....|....*....|..
gi 357588455 413 D--------MDGKSILKLLDSE 426
Cdd:cd16025 327 TvngvpqlpLDGVSLLPTLDGA 348
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
77-431 |
2.21e-27 |
|
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: 116.71 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQDVELGS------MQVMNKTRriMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSps 150
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcygnkaMKTPNLDR--LAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 wqaqhESRTFAVYLNSTGYRTAFFGKY-LN--EYNGSYV-PPGWKE--WVGLlKN------------SRFYNYTLCRNGV 212
Cdd:cd16156 77 -----NVKTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDM-RNyldelteeerrkSRRGLTSLEAEGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 213 KEKHGSDYStdyltdlITNDSVSFFRTSKKmyphRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSY--NYAPNPD 290
Cdd:cd16156 151 KEEFTYGHR-------CTNRALDFIEKHKD----EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 291 KH--WIMRYTGP----MKPIHMEFtnmlqrkrLQTLMSVDDSMETIYDMLVETGEldNTYILYTADHGYHIGQFGL-VKG 363
Cdd:cd16156 220 HQrlWAGAKPHEdgdkGTIKHPLY--------FGCNSFVDYEIGRVLDAADEIAE--DAWVIYTSDHGDMLGAHKLwAKG 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 364 KSMpYEFDIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLL-DSERPVNR 431
Cdd:cd16156 290 PAV-YDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIeDPEIPENR 358
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
76-434 |
1.64e-26 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 114.38 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQDVE-LGSM---QVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSspsW 151
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 152 QAQHesrTFAVYLNSTGYRTAFFGKYlneyngsYVPPGwkewvgllKNSRFYNYTLCRNG------VKEKHGSDYSTDYL 225
Cdd:PRK13759 83 NYKN---TLPQEFRDAGYYTQCIGKM-------HVFPQ--------RNLLGFHNVLLHDGylhsgrNEDKSQFDFVSDYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 226 -------------------------------------TDLITNDSVSFFRTSKkmyPHRPVLMVISHAAPHGPEDSaPQY 268
Cdd:PRK13759 145 awlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLRRRD---PTKPFFLKMSFARPHSPYDP-PKR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 269 ------SRLFPNAsqhITPSYNYAPNPDKHWIMRYTGpmkpiHMEFTNMLQRKRLQ----TLMSVDDSMETIYDMLVETG 338
Cdd:PRK13759 221 yfdmykDADIPDP---HIGDWEYAEDQDPEGGSIDAL-----RGNLGEEYARRARAayygLITHIDHQIGRFLQALKEFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 339 ELDNTYILYTADHGYHIGQFGLVKgKSMPYEFDIRVPFYVRGP----NVEAGSLNPHIVLNIDLAPTILDIAGLDIPADM 414
Cdd:PRK13759 293 LLDNTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDV 371
|
410 420
....*....|....*....|
gi 357588455 415 DGKSILKLLDSERPVNRFHL 434
Cdd:PRK13759 372 DGRSLKNLIFGQYEGWRPYL 391
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
106-428 |
5.29e-26 |
|
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: 109.98 E-value: 5.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 106 QGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNenCSSPSwqaqhESRTFAVYLNSTGYRTAFFGKYlneyngSY 185
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPA-----DIPTFAHYLRAAGYRTALSGKM------HF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 186 VPPgwkewvgllknsrfynytlcrngvKEKHGSDYstdyltdlitNDSVSFfRTSKKMYPH------RPVLMVISHAAPH 259
Cdd:cd16032 101 VGP------------------------DQLHGFDY----------DEEVAF-KAVQKLYDLargedgRPFFLTVSFTHPH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 260 GPEDSAPQYSRLFPNASQHitpSYnYApnpdkhwIMRYtgpmkpihmeftnmlqrkrlqtlmsVDDSMETIYDMLVETGE 339
Cdd:cd16032 146 DPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTGL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 340 LDNTYILYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAG---LDIPADMDG 416
Cdd:cd16032 190 ADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGggtAPHVPPLDG 268
|
330
....*....|..
gi 357588455 417 KSILKLLDSERP 428
Cdd:cd16032 269 RSLLPLLEGGDS 280
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-420 |
6.44e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 107.71 E-value: 6.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQ---------DVELgSMQVMNKtrriMEQGGAHFINAFVTTPMCCPSRSSILTGKY-----VHNHNTYTN 142
Cdd:cd16149 1 PNILFILTDDQgpwalgcygNSEA-VTPNLDR----LAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgIHDWIVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 143 NENCSSPSWQAQHESrTFAVYLNSTGYRTAFFGKylneyngsyvppgwkeWvgllknsrfynytlcrngvkekHGSDYST 222
Cdd:cd16149 76 HGKTKKPEGYLEGQT-TLPEVLQDAGYRCGLSGK----------------W----------------------HLGDDAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 223 DYLTDLITNDsvsffrtskkmyphRPVLMVISHAAPHGPEdsapQYsrlfpnasqhitpsynYApnpdkhwimrytgpmk 302
Cdd:cd16149 117 DFLRRRAEAE--------------KPFFLSVNYTAPHSPW----GY----------------FA---------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 303 pihmeftnmlqrkrlqTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGlVKGK-------SMpYEFDIRVP 375
Cdd:cd16149 147 ----------------AVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 357588455 376 FYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPADMD--GKSIL 420
Cdd:cd16149 209 FIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-421 |
9.37e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 107.63 E-value: 9.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTD----DQdvelgsMQVMNKTRRIM------EQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnnenc 146
Cdd:cd16148 1 MNVILIVIDslraDH------LGCYGYDRVTTpnldrlAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 147 sspSWQAQHESRTFAVYLNSTGYRTAFFGkylneyNGSYVPPGWkewvGLlkNSRFYNYTLCRNGVKEKHGSDYSTDylt 226
Cdd:cd16148 69 ---GGPLEPDDPTLAEILRKAGYYTAAVS------SNPHLFGGP----GF--DRGFDTFEDFRGQEGDPGEEGDERA--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 227 DLITNDSVSFFRTSKKmypHRPVLMVISHAAPHGPedsapqysrlfpnasqhitpsYNYApnpdkhwimryTGpmkpIHM 306
Cdd:cd16148 131 ERVTDRALEWLDRNAD---DDPFFLFLHYFDPHEP---------------------YLYD-----------AE----VRY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 307 eftnmlqrkrlqtlmsVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVKGKSMP-YEFDIRVPFYVRGPNVEA 385
Cdd:cd16148 172 ----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEP 235
|
330 340 350
....*....|....*....|....*....|....*.
gi 357588455 386 GSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILK 421
Cdd:cd16148 236 GKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
76-424 |
2.21e-25 |
|
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: 110.36 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQDVELGSMqvmnktrrimeqgGAHFI----------------NAFVTTPMCCPSRSSILTGKYVHNHNT 139
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCY-------------GGHPAktpnidrlaargvlftNAYCQQPVCGPSRASLLTGRRPDTTGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 140 YTNNencsSPSWQAQHESRTFAVYLNSTGYRTAFFGKYL--NEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHG 217
Cdd:cd16030 69 YDNN----SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFhpGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 218 S---------------------DYSTDYLTDLITND-----SVSFFRtskkmyPHRPVlmvishAAPHG-----PEDSAP 266
Cdd:cd16030 145 GggpaweaadvpdeaypdgkvaDEAIEQLRKLKDSDkpfflAVGFYK------PHLPF------VAPKKyfdlyPLESIP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 267 QYSRLFP-NASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFtnmlQRKRLQT-LMSV---DDSMETIYDMLVETGELD 341
Cdd:cd16030 213 LPNPFDPiDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQ----ARELRQAyYASVsyvDAQVGRVLDALEELGLAD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 342 NTYILYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSIL 420
Cdd:cd16030 289 NTIVVLWSDHGWHLGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLV 367
|
....
gi 357588455 421 KLLD 424
Cdd:cd16030 368 PLLK 371
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
77-434 |
3.29e-25 |
|
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: 108.79 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQ---DVEL-GSMQVmnKTRRIME--QGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 150
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 WQAQHEsRTFAVYLNSTGYRTAFFGKY-LNEYNGSYVPPG----------------WKEWVGLLKNsrFYNYTLCRNgvk 213
Cdd:cd16029 78 GLPLNE-TLLPQYLKELGYATHLVGKWhLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSGGAND--YGNDDLRDN--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 214 EKHGSDYSTDYLTDLITNDSVSFFRTSKkmyPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPsynyapnpdkhw 293
Cdd:cd16029 152 EEPAWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 294 imrytgpmkpihmeftnmLQRKRLQTLMS-VDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFG------LVKGKSM 366
Cdd:cd16029 217 ------------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNT 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357588455 367 PYEFDIRVPFYVRGP--NVEAGSLNPHIVLNIDLAPTILDIAGLDIPA--DMDGKSILKLLDSERPVNRFHL 434
Cdd:cd16029 279 LWEGGVRVPAFVWSPllPPKRGTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQWDALSGGAPSPRTEI 350
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
76-438 |
6.63e-24 |
|
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: 105.97 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQDV-----------ELGSM-QVMNKtrrimeqgGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtnN 143
Cdd:cd16160 1 KPNIVLFFADDMGYgdlasyghptqERGPIdDMAAE--------GIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 144 ENCSSPSWQA---QHESRTFAVYLNSTGYRTAFFGKY---LNEYN---GSYVPP--GWkEWVGllKNSRFYNYTLCRNGV 212
Cdd:cd16160 71 GTRVFLPWDIgglPKTEVTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLPShhGF-DFVG--TNLPFTNSWACDDTG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 213 KEKHGSDYST----------------DYLTDLITNDSVSFFRTSKkmypHRPVLMVISHAAPHGPedsapqysrLFPNAs 276
Cdd:cd16160 148 RHVDFPDRSAcflyyndtiveqpiqhEHLTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTHTP---------LFASK- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 277 qhitpsynyapnpdkhwimrytgpmkpihmEFTNMLQRKRL-QTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHI 355
Cdd:cd16160 214 ------------------------------RFKGKSKRGRYgDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 356 ------GQFGLVKG-KSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL--- 423
Cdd:cd16160 264 eyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDLLlge 343
|
410
....*....|....*.
gi 357588455 424 -DSERPVNRFHLKKKL 438
Cdd:cd16160 344 aDSPHDDILYYCCSRL 359
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-433 |
1.31e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 103.97 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQDVE------LGSMQVMNKTRRIMEQGGAHFINAFVTtPMCCPSRSSILTGKYVHNHNTYTNNENCSSPS 150
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 wqaqHES-RTFAVYLNSTGYRTAFFGKYL--NEYNGSYVPPGWKEWVGLLKN--SRFYNYTLCRNGVKEKHgsdysTDYL 225
Cdd:cd16154 80 ----ETLlQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-----TEYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 226 TDLITNDSVSFFRTSkkmypHRPVLMVISHAAPHGPedsapqysrlFpnasqHITPSYNYAPNPdkhwimryTGPMKPIH 305
Cdd:cd16154 151 TTKLTNLAIDWIDQQ-----TKPWFLWLAYNAPHTP----------F-----HLPPAELHSRSL--------LGDSADIE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 306 MEftnmlqrkRLQTLMSVDDSMETIYDMLVET---GELDNTYILYTADHGYHiGQ-----FGLVKGKSMPYEFDIRVPFY 377
Cdd:cd16154 203 AN--------PRPYYLAAIEAMDTEIGRLLASideEERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVPLI 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 357588455 378 VRGPNVEAGSLNPHIVLNI-DLAPTILDIAGLDIPADMDGKSILKLLDSERPVNRFH 433
Cdd:cd16154 274 VSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQY 330
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
76-421 |
2.49e-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: 98.22 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQDV------------ELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYt 141
Cdd:cd16153 1 KPNILWIITDDQRVdslscynnahtgKSESRLGYVESPNIdaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 142 NNENcsspSWQAQHESR-TFAVYLNSTGYRTAFFGKylneyngsyvpPGWKEWVGLLKNSrfyNYTLCRNGVKEKHGSDY 220
Cdd:cd16153 80 GFEA----AHPALDHGLpTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGADS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 221 STDYLTdlitndSVSFfrtskkMYPHRPVLmvishaaphgpedsapqysrlfpnasqhitpsynyapnPDKHWIMRYTgp 300
Cdd:cd16153 142 DKPFFV------RLSF------LQPHTPVL--------------------------------------PPKEFRDRFD-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 301 mkpiHMEFTNMlqrkrlqtlmsVDDSMETIYDMLVETGEL---DNTYILYTADHGYHIGQFGLVkGKSMPYEFDIRVPFY 377
Cdd:cd16153 170 ----YYAFCAY-----------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVPLI 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 357588455 378 VRGPNVE---AGSLNPHIVLNIDLAPTILDIAGLDI--PADMDGKSILK 421
Cdd:cd16153 234 VVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDLFE 282
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
77-423 |
7.41e-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: 92.60 E-value: 7.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQDVEL----GSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYtNNENCSSPSWQ 152
Cdd:cd16171 1 PNVVMVMSDSFDGRLtfrpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 153 aqhesrTFAVYLNSTGYRTAFFGKyLNEYNGSYVPPGWKE-WvgllknSRFYNYTLCRNGVKekhgsdystdyLTDLITN 231
Cdd:cd16171 80 ------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRP-----------TVNLVGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 232 DSVSffRTSKKMYPhrpvlmvISHAAPHGPEDSAPQYSRLF--------PnasqHITPSYNYAPNpdkhwimryTGPMKP 303
Cdd:cd16171 136 RSTV--RVMLKDWQ-------NTDKAVHWIRKEAPNLTQPFalylglnlP----HPYPSPSMGEN---------FGSIRN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 304 IHMEFTNMLQRkrlqtlmsVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYVRGPNV 383
Cdd:cd16171 194 IRAFYYAMCAE--------TDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGPGI 264
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 357588455 384 EAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLL 423
Cdd:cd16171 265 KAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
108-427 |
2.90e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 91.53 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 108 GAHFINAFVTTPMCCPSRSSILTGKY--VHNHNTYTNNENCSSPSwqaqhesrtFAVYLNSTGYRTAFFGKylneyNGSY 185
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHHLLRPDEPN---------LLKTLKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 186 VPPGWKEwvgllknsrfynytlcrngvkekhgsDYST-DYLTdliTNDSVSFFRTSKkmyPHRPVLMVISHAAPHGP-ED 263
Cdd:cd16150 102 PGEFAAE--------------------------AYCDsDEAC---VRTAIDWLRNRR---PDKPFCLYLPLIFPHPPyGV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 264 SAPQYSRLFPNAS-QHITPSYNYAPNPDKHWIMRYTGpMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYDMLVETGELDN 342
Cdd:cd16150 150 EEPWFSMIDREKLpPRRPPGLRAKGKPSMLEGIEKQG-LDRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 343 TYILYTADHGYHIGQFGLV-KGKSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILK 421
Cdd:cd16150 229 TAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLP 308
|
....*.
gi 357588455 422 LLDSER 427
Cdd:cd16150 309 VLAGET 314
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
787-836 |
7.87e-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: 86.84 E-value: 7.87e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 357588455 787 CTSANNNTYWCLRTINETHNFLFCEFATGFIEYFDLSTDPYQLMNAVNTL 836
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
76-432 |
4.24e-17 |
|
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: 85.42 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDqdveLGSMQVM---NKTRR-----IMEQGGAHFINAFVTTPMCCPSRSSILTGKY------VHNHNtYT 141
Cdd:cd16159 1 KPNIVLFMADD----LGIGDVGcfgNDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHG-MR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 142 NNENCSSPSWQAQHESrTFAVYLNSTGYRTAFFGKY----------------LN-----------------------EYN 182
Cdd:cd16159 76 VILFTASSGGLPPNET-TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 183 GSYVPPGWKE--------------------------------------WVGLLKNSRFYNYTLCRNG-VKEKhgsDYSTD 223
Cdd:cd16159 155 LSFDPLFPLLtafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHeVVEQ---PMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 224 YLTDLITNDSVSFFRTSKkmypHRPVLMVISHAAPHGPEDSAPqysrLFPNASQHitpsYNYAPNpdkhwimrytgpmkp 303
Cdd:cd16159 232 NLTQRLTKEAISFLERNK----ERPFLLVMSFLHVHTALFTSK----KFKGRSKH----GRYGDN--------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 304 ihmeftnmlqrkrlqtLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHI-----------GQFGLVKGKSMP-YEFD 371
Cdd:cd16159 285 ----------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEGG 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357588455 372 IRVPFYVRGPNV-EAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLLD--SERPVNRF 432
Cdd:cd16159 349 IRVPTIVRWPGViPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTgqEKRSPHEF 414
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
77-413 |
6.99e-17 |
|
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: 83.35 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDqdveLGSMQV--------M-NKTRRI--MEQGGAHFINAFVTtPMCCPSRSSILTGKYVhnhntytNNEN 145
Cdd:cd16142 1 PNILVILGDD----IGWGDLgcygggigRgAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 146 CSSPSWQAQ-----HESRTFAVYLNSTGYRTAFFGK-YLNEYNGSYvpP---GWKEWVGllknsrFYNYTLcrngvkEKH 216
Cdd:cd16142 69 LTTVGLPGSpgglpPWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 217 GSDYSTDYLTDLITNDSvSFFrtskkMYpHRPVLMvishaapHgpedsapqysrlFPNasqhitpsynyapNPDKHWIMR 296
Cdd:cd16142 135 IVDKAIDFIKRNAKADK-PFF-----LY-VNFTKM-------H------------FPT-------------LPSPEFEGK 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 297 YTGpmkpihmeftnmlQRKRLQTLMSVDDSMETIYDMLVETGELDNTYILYTADHG-----YHIGQFGLVKG-KSMPYEF 370
Cdd:cd16142 176 SSG-------------KGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWEG 242
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 357588455 371 DIRVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPAD 413
Cdd:cd16142 243 GVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
76-433 |
2.64e-15 |
|
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: 79.43 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDDQDV-ELGSMQVMNK-TRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpSW 151
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARN-AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 152 QAQH-------ESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVP--PGWKEW-------VGLLKNSRFYNYTLCRNG-VKE 214
Cdd:cd16157 80 TPQNivggipdSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWfgapnchFGPYDNKAYPNIPVYRDWeMIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 215 KHGSDYSTDY------LTDLITNDSVSFFrtSKKMYPHRPVLMVISHAAPHgpedsAPQYsrlfpnASQHitpsynyapn 288
Cdd:cd16157 160 RYYEEFKIDKktgesnLTQIYLQEALEFI--EKQHDAQKPFFLYWAPDATH-----APVY------ASKP---------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 289 pdkhwimrytgpmkpihmeFTNMLQRKRL-QTLMSVDDSMETIYDMLVETGELDNTYILYTADHG---YHIGQFG----- 359
Cdd:cd16157 217 -------------------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngp 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357588455 360 LVKGKSMPYEFDIRVPFYVRGP-NVEAGSLNpHIVLNI-DLAPTILDIAGLDIPAD--MDGKSILKLLDSERPVNRFH 433
Cdd:cd16157 278 FLCGKQTTFEGGMREPAIAWWPgHIKPGQVS-HQLGSLmDLFTTSLALAGLPIPSDraIDGIDLLPVLLNGKEKDRPI 354
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
76-423 |
5.20e-14 |
|
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: 74.81 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLTDD---QDVELGSMQVMNKTRRI--MEQGGAHFINAFVTTPMCCPSRSSILTGKYvHNHNTYTNNENCSSPS 150
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRL-GLRNGVGHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 WQAQHESrTFAVYLNSTGYRTAFFGKYLNEYNGSYVPpgwkewvgllkNSRFYNYTLcrnGVKEKHGSDYSTDYL---TD 227
Cdd:cd16161 80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaTD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 228 LITNDSVSffrtskkmypHRPVLMVISHAAPHGPEDSAPqysrLFPNASQHITPsynyapnpdkhwimryTGpmkpihme 307
Cdd:cd16161 145 FIQRASAK----------DRPFFLYAALAHVHVPLANLP----RFQSPTSGRGP----------------YG-------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 308 ftnmlqrkrlQTLMSVDDSMETIYDMLVETGELDNTYILYTAD---------------HGYHIGQFGLVKGKSMPYEFDI 372
Cdd:cd16161 187 ----------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGH 256
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 357588455 373 RVPFYVRGPN-VEAGSLNPHIVLNIDLAPTILDIAGLDIPAD--MDGKSILKLL 423
Cdd:cd16161 257 REPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
77-406 |
1.88e-13 |
|
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: 70.91 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDD---QDVELGSMQVMNKTR-RIMEQGGAHFiNAFVTTPMC--CPSRSSILTGKYVHNHNTYTNNENCSSPS 150
Cdd:cd00016 1 KHVVLIVLDGlgaDDLGKAGNPAPTTPNlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 WQAQHES---RTFAVYLNSTGYRTAffgkylneyngsyvppgwkeWVGLLknsrfynytlcrngvkekhgsdystDYLtd 227
Cdd:cd00016 80 SRAAGKDedgPTIPELLKQAGYRTG--------------------VIGLL-------------------------KAI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 228 litndsvsffrtsKKMYPHRPVLMVISHAAPHGPedsapqysrlfpnasqhitpSYNYAPNPDkhwimrytgpmkpihmE 307
Cdd:cd00016 113 -------------DETSKEKPFVLFLHFDGPDGP--------------------GHAYGPNTP----------------E 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 308 FTNMLQRkrlqtlmsVDDSMETIYDMLVETGELDNTYILYTADHG---YHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVE 384
Cdd:cd00016 144 YYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVK 215
|
330 340
....*....|....*....|..
gi 357588455 385 AGSLNPHIVLNIDLAPTILDIA 406
Cdd:cd00016 216 KGGVKHELISQYDIAPTLADLL 237
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
77-423 |
3.91e-13 |
|
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: 72.86 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVLTDDQDV-ELG-----SMQVMNKTRriMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSpS 150
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 151 WQAQHESRTFAVYLNSTGYRTAFFGKY---LNEyNGSYVPPgwkewvgllknsrfynytlcRNGVKEKHGSDYSTDY--- 224
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT--------------------HQGFDHYLGIPYSHDQgpc 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 225 --LTDLITNDSVsfFRTSKKMYPHRPVLM--VISHAAPHGPeDSAPQY----SRLFPNASQHITPSYNYAPNPDKHWiMR 296
Cdd:cd16158 138 qnLTCFPPNIPC--FGGCDQGEVPCPLFYneSIVQQPVDLL-TLEERYakfaKDFIADNAKEGKPFFLYYASHHTHY-PQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 297 YTGpmkpihMEFTNMLQRKRL-QTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHI------GQFGLVK-GKSMPY 368
Cdd:cd16158 214 FAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTY 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 357588455 369 EFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIP-ADMDGKSILKLL 423
Cdd:cd16158 288 EGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPnVTLDGVDMSPIL 343
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
76-434 |
1.10e-10 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 65.06 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 76 RPNIILVLtddqdVElgSMQ--VMNKT----------RRIMEQGgAHFINAFVTTPMCCPSRSSILTGKY-VHNHNTYTN 142
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 143 NencsspswqAQHESRTFAVYLNSTGYRTAFFgkylneYNGsyvppgwkewvgllkNSRFYNytlcRNGVKEKHGSD--Y 220
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 221 STDYLTDLITN-----DSvSFFRTSKKMYPhrpvlmvishaaphgpEDSAPQYSRLFpNASQHiTPsYNYaPNPDKHWIm 295
Cdd:COG1368 352 DREDFDDPFDGgwgvsDE-DLFDKALEELE----------------KLKKPFFAFLI-TLSNH-GP-YTL-PEEDKKIP- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 296 rytgpmkpihmEFTNMLQRKRLQTLMSVDDSMETIYDMLVETGELDNTYILYTADHGyhigqfGLVKGKSmPYEFDI--- 372
Cdd:COG1368 410 -----------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLery 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357588455 373 RVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPAD-MDGKSILKLLDSERPVNRFHL 434
Cdd:COG1368 472 RVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDLLSPDTDPFAFRNGGF 534
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
77-407 |
1.37e-10 |
|
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: 63.09 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 77 PNIILVL-----TDDQDVELGSMQVMNKTRRIMEQGgAHFINAFVTTPMCCPSRS--SILTGkyvhnhnTYTNNENCSSP 149
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 150 SWQAQHESRTFAVYLNSTGYRTAFFgkylneYNGsyvppgwkewvgllkNSRFYNytlcRNGVKEKHGSD--YSTDYLTD 227
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 228 LITNDSV------SFFRTSKKMY---PHRPVLMVISHAAPHGPedsapqysrlfpnasqhitpsYNYAPNPDKhwimryt 298
Cdd:cd16015 128 DEKETNGwgvsdeSLFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 299 gpmKPIHMEFTNMLQRKRLQTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVKGKSMPYEFdiRVPFYV 378
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 357588455 379 RGPNVEAGSLNPHIVLNIDLAPTILDIAG 407
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
323-420 |
8.30e-07 |
|
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: 52.80 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 323 VDDSMETIYDMLVETGeldntYILY-TADHG-----YHIGQFGLVKGKSMPyefdiRVPFYVRGPNV-----EAGSLnph 391
Cdd:cd16010 412 VDECLGRIVEAVLENG-----GTLLiTADHGnaeemIDPETGGPHTAHTTN-----PVPFIIVDPGLkrkllKDGGL--- 478
|
90 100
....*....|....*....|....*....
gi 357588455 392 ivlnIDLAPTILDIAGLDIPADMDGKSIL 420
Cdd:cd16010 479 ----ADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
374-421 |
1.63e-06 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 51.64 E-value: 1.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 357588455 374 VPF-YVRGPNV--EAGSLNphivlniDLAPTILDIAGLDIPADMDGKSILK 421
Cdd:PRK05434 464 VPFiLVGGKALrlEGGKLA-------DIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
374-421 |
3.31e-06 |
|
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: 50.82 E-value: 3.31e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 357588455 374 VPFYVRGPNvEAGSLNPHIVLnIDLAPTILDIAGLDIPADMDGKSILK 421
Cdd:COG0696 465 VPFILVGGD-KGVKLREDGRL-ADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
376-424 |
1.43e-05 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 48.75 E-value: 1.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 357588455 376 FYVRGPNVEAGSLNPHIVLnIDLAPTILDIAGLDIPADMDGKSILKLLD 424
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
101-407 |
2.97e-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: 46.81 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 101 RRIMEQGgAHF---INAFVT-TpmcCPSRSSILTGKYVHNH----NTY---TNNENCSSPSWQAQH---ESRTFAVYLNS 166
Cdd:cd16018 26 KRLAEEG-VRAkyvKPVFPTlT---FPNHYSIVTGLYPESHgivgNYFydpKTNEEFSDSDWVWDPwwiGGEPIWVTAEK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 167 TGYRTA-FFgkylneyngsyvppgwkeWVGLLKNSRFYNYTLCRNGvkekhgsDYSTDYLTDLITNDSVSFFRTSKKMYp 245
Cdd:cd16018 102 AGLKTAsYF------------------WPGSEVAIIGYNPTPIPLG-------GYWQPYNDSFPFEERVDTILEWLDLE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 246 hRPVLMVISHAAPhgpeDSApqysrlfpnasQHitpsyNYAPNpdkhwimrytgpmkpiHMEFTNMLQRkrlqtlmsVDD 325
Cdd:cd16018 156 -RPDLILLYFEEP----DSA-----------GH-----KYGPD----------------SPEVNEALKR--------VDR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 326 SMETIYDMLVETGELDNTYILYTADHGY-----HiGQFglvkgksmPYEFDIRVPFYVRGP----NVEAGSLNphivlNI 396
Cdd:cd16018 191 RLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPafkkGKKLGPFR-----NV 256
|
330
....*....|.
gi 357588455 397 DLAPTILDIAG 407
Cdd:cd16018 257 DIYPLMCNLLG 267
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
317-403 |
7.93e-05 |
|
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: 46.44 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 317 LQTLMSVDDSMETIYDMLVETGELDNTYILYTADHGY-----------HIGQFGlvkgksmPYEfdIRVPFYVRGPNVEA 385
Cdd:COG3083 430 RNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS-------RYQ--LQVPLVIHWPGTPP 500
|
90
....*....|....*...
gi 357588455 386 GSLNpHIVLNIDLAPTIL 403
Cdd:COG3083 501 QVIS-KLTSHLDIVPTLM 517
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
324-419 |
5.96e-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: 42.55 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357588455 324 DDSMETIYDMLVETGELDNTYILYTADHGY-----HigqfglvkGKSMPYEfdIRVPFYVRGPNVEAGSLNPH------- 391
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHGMtdagnH--------GGSSPGE--TSVPLLFISPKFSSKPSNADgelsyye 246
|
90 100
....*....|....*....|....*...
gi 357588455 392 IVLNIDLAPTILDIAGLDIPADMDGKSI 419
Cdd:cd16024 247 TVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
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