|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
45-387 |
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: 546.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQDIELGSMQVMNKTRRIMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNE--NCSSPSWQA 122
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 123 QHEPRTFGVYLNNTGYRTAFFGKYLNEY----NGTYIPPGWKEWVAMVKNSRFYNYTLCrNGVREKHGFEYPKDYLTDLI 198
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 199 TNDSINYFRMSKKIypHRPVLMVISHAAPHGPEDAAPQYTTAFPNAS-QHITPSYNYAPNPDKHWIMRYTGPMkPIHMEF 277
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLN-PTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 278 TNMLQRKRLQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYIRGPNVEAGGI 357
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 1040678789 358 NPHIVLNIDLAPTILDIAGMDVPPDMDGKS 387
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
45-417 |
1.90e-88 |
|
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: 290.58 E-value: 1.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQDIE-LGSMQ-VMNKT---RRIMEQGgTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENcSSPS 119
Cdd:cd16031 2 RPNIIFILTDDHRYDaLGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 WQaqhepRTFGVYLNNTGYRTAFFGKYLNEYNGTYIPPGWKEWVAMVKNSRFYNYTLCRNGVREKHgfeypKDYLTDLIT 199
Cdd:cd16031 80 SQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTDIIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 200 NDSINYFRMSKKiypHRPVLMVISHAAPHGPEDAAPQYTTAFPNAsqHITP-----SYNYAPNPD--KHWIMRYTGPMK- 271
Cdd:cd16031 150 DKALDFLKERDK---DKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEpetfdDDDYAGRPEwaREQRNRIRGVLDg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 272 PIHMEFT---NMlqRKRLQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYIR 348
Cdd:cd16031 225 RFDTPEKyqrYM--KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLIIR 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 349 GP-NVEAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLDtdrmmnrfqlNKKGKVWRDSFLVE 417
Cdd:cd16031 302 DPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
45-417 |
1.12e-71 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 243.63 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQDI-ELGSM-QVMNKT---RRIMEQGgTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSSPs 119
Cdd:COG3119 23 RPNILFILADDLGYgDLGCYgNPLIKTpniDRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 wqAQHEPRTFGVYLNNTGYRTAFFGKYLNeyngtyippgwkewvamvknsrfynytlcrngvrekhgfeypkdYLTDLIT 199
Cdd:COG3119 101 --LPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLLT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 200 NDSINYfrMSKKIYPHRPVLMVISHAAPHGPEDAAPQYTTAFPNasQHITPSYNYAPNPDKHWIMRYtgpmkpihmeftn 279
Cdd:COG3119 135 DKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 280 mLQRKRLQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYIRGPN-VEAGGIN 358
Cdd:COG3119 198 -ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVS 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1040678789 359 PHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLDtdrmmnrfqlnKKGKVWRDSFLVE 417
Cdd:COG3119 277 DALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLT-----------GEKAEWRDYLYWE 324
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
551-677 |
7.65e-61 |
|
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: 203.73 E-value: 7.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 551 RNRFARALSMETGGDLYAVDLDNEH-----RNLSLRLST-----ADEDEEFSGAEPTTiSQSNSLSVPSSIKVTHRCSIL 620
Cdd:pfam12548 6 RTRQKRSLSVEFEGEVYDIDLEEEYqplepRNLLKRHARddgeeGEEGEESSGTGSKR-DSSNSVGPPASVKVTHRCYIL 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1040678789 621 ANETVKCDVGLYKSLQAWKDHKLHIDHEIETLQTKIKNLREVRGHLKKARPEECDCN 677
Cdd:pfam12548 85 ANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCN 141
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
46-387 |
6.98e-51 |
|
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: 179.17 E-value: 6.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQ---DIE-LGSMQVmnKT---RRIMEQGgTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENcssP 118
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 119 SWQAQHEPrTFGVYLNNTGYRTAFFGKylneyngtyippgwkeWvamvknsrfynytlcrngvrekHgfeypkdyltdli 198
Cdd:cd16022 75 GGLPPDEP-TLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 199 tNDSINYFRMSKKiypHRPVLMVISHAAPHGPedaapqyttafpnasqhitpsYNYApnpdkhwimrytgpmkpiHMeft 278
Cdd:cd16022 103 -DEAIDFIERRDK---DKPFFLYVSFNAPHPP---------------------FAYY------------------AM--- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 279 nmlqrkrlqtLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYIRGPNV-EAGGI 357
Cdd:cd16022 137 ----------VSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKiPAGQV 206
|
330 340 350
....*....|....*....|....*....|
gi 1040678789 358 NPHIVLNIDLAPTILDIAGMDVPPDMDGKS 387
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-396 |
1.04e-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: 181.61 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDD---QDieLGSMQVMN-KT---RRIMEQGgTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNnencss 117
Cdd:cd16034 1 KPNILFIFADQhraQA--LGCAGDDPvKTpnlDRLAKEG-VVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 118 pSWQAQHEPRTFGVYLNNTGYRTAFFGK--------YLNEYNGTYIPP----GWKEWVAMVKNSRFYNYTLCRNGVREKH 185
Cdd:cd16034 72 -DVPLPPDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 186 GFEYPKDYLTDLItndsINYfrMSKKIYPHRPVLMVISHAAPHGPEDAAPQ-YTTAFPNASQHitpsynYAPNPDKhwim 264
Cdd:cd16034 151 IKGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLL------LRPNVPE---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 265 rytgpmkpihmeftNMLQRKRLQTLL--------SVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVkGKSMP 336
Cdd:cd16034 215 --------------DKKEEAGLREDLrgyyamitALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVP 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040678789 337 YEFDIRVPFYIRGPNV-EAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLDTDR 396
Cdd:cd16034 280 YEESIRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGK 340
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-392 |
1.24e-47 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 176.19 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDqdieLGSMQV---MNK---TRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSS 117
Cdd:cd16144 1 PNIVLILVDD----LGWADLgcyGSKfyeTPNIdrLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 118 PSWQA-----------QHEPRTFGVYLNNTGYRTAFFGKY-LNEYNGTYipP---GWKEWVAMVKNSRFYNYTLCRNGVR 182
Cdd:cd16144 77 PPDNTklipppsttrlPLEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 183 EKHGFEYPKDYLTDLITNDSINYFRMSKKiyphRPVLMVISHAAPHGPEDAAPQYTTAFPNAsqhitpsynYAPNPDKHW 262
Cdd:cd16144 155 PDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKYEKK---------KKGLRKGQK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 263 IMRYTGpmkpihmeftnMLQrkrlqtllSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLV-------KGKSM 335
Cdd:cd16144 222 NPVYAA-----------MIE--------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGGKGS 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 336 PYEFDIRVPFYIRGPNV-EAGGINPHIVLNIDLAPTILDIAGMDVPP--DMDGKSILKLL 392
Cdd:cd16144 283 LYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLL 342
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
46-400 |
1.31e-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: 171.54 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQDIELGSmqVMN---KTRRIME--QGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTN-NENCSSPS 119
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 WQaqhepRTFGVYLNNTGYRTAFFGKYlnEYNGTYIPPGWKEWVAMVKNSRfynytlcrNGVREKHGFEypkDYLTDLIT 199
Cdd:cd16027 79 GV-----KTLPELLREAGYYTGLIGKT--HYNPDAVFPFDDEMRGPDDGGR--------NAWDYASNAA---DFLNRAKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 200 ND----SINYFrmskkiYPHRPVLMVISHAAPHGPEDAAPqyttafpnasqhitPSYnYAPNPdkhwIMRYTgpmkpiHM 275
Cdd:cd16027 141 GQpfflWFGFH------DPHRPYPPGDGEEPGYDPEKVKV--------------PPY-LPDTP----EVRED------LA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 276 EFTNMLQRkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHGYhigqfGLVKGKSMPYEFDIRVPFYIRGPN-VEA 354
Cdd:cd16027 190 DYYDEIER--------LDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKP 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1040678789 355 GGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLDTDRMMNR 400
Cdd:cd16027 257 GSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
46-377 |
3.65e-44 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 162.21 E-value: 3.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQ---DIELGSMqVMNKTRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNEncsspsW 120
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLYGY-PRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 121 QAQHEPRTFGVYLNNTGYRTAFFGKYLNEYNGTYIPPGWkewvamvKNSRFYNYTLCRNGVREK---HGFEYPKDYLTDL 197
Cdd:pfam00884 74 GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNL-------GFDKFFGRNTGSDLYADPpdvPYNCSGGGVSDEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 198 ITNDSINYfrmskKIYPHRPVLMVISHAAPHGPEDAAPQYTTAFPnasqhitpsyNYAPNPDKHWIMRytgpmkpihmef 277
Cdd:pfam00884 147 LLDEALEF-----LDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYA----------TFKPSSCSEEQLL------------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 278 tnmlqRKRLQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFG--LVKGKSM-PYEFDIRVPFYIRGPNVEA 354
Cdd:pfam00884 200 -----NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKA 274
|
330 340
....*....|....*....|....
gi 1040678789 355 -GGINPHIVLNIDLAPTILDIAGM 377
Cdd:pfam00884 275 kGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-393 |
4.05e-42 |
|
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: 158.55 E-value: 4.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQ--DIeLGSM-QVMNKTRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNenCSSPS 119
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 wqaqhEPRTFGVYLNNTGYRTAFFGKylneyngtyippgwkeWvamvknsrfynytlcrngvrekHGFEYPKDYLTDLit 199
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 200 ndSINYFRMSKKiypHRPVLMVISHAAPH---------GPEDAAPQYTT--------AFP-NASQHItpsynyapnPDkh 261
Cdd:cd16152 113 --AIDYLDNRQK---DKPFFLFLSYLEPHhqndrdryvAPEGSAERFANfwvppdlaALPgDWAEEL---------PD-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 262 wimrYTGpmkpihmeftnMLQRkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHigqFGLVKG--KSMPYEF 339
Cdd:cd16152 177 ----YLG-----------CCER--------LDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1040678789 340 DIRVPFYIRGPNVEAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLD 393
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVD 284
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-392 |
7.69e-41 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 155.83 E-value: 7.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQDI-ELGSM-QVMNKTRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKyaHNHNTY--TNNENCSSPS 119
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTGHTRvrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 WQAqhEPRTFGVYLNNTGYRTAFFGKY-LNEYNGTYIPP--GWKEWVAMVKNSR---FYNYTLCRNGVRE-----KHGFE 188
Cdd:cd16145 79 LPP--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGYLDQVHahnYYPEYLWRNGEKVplpnnVIPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 189 YP--------KDYLTDLITNDSINYFRMSKKiyphRPVLMVISHAAPHGPedaapqyttafpnasqHITPSYNYAPNPDK 260
Cdd:cd16145 157 DEgnnaggggGTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAP----------------LQVPDDGPYKYKPK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 261 HWIMRYTGPMKPIHMEFTNMLQRkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHI-------GQF-----G 328
Cdd:cd16145 217 DPGIYAYLPWPQPEKAYAAMVTR--------LDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngP 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040678789 329 LVKGK-SMpYEFDIRVPFYIRGPN-VEAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLL 392
Cdd:cd16145 289 LRGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-417 |
1.33e-40 |
|
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: 155.07 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQ--DIELGSMQVMNKTRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSSPSWQ 121
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 122 AQHEPRTFGVYLNNTGYRTAFFGKYlneYNGTYIPP---GWKEWVAmvknsrfynytlcrngvrEKHGFEYpkdYLTDLi 198
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKW---HVGPEETPldyGFDEYLP------------------VETTIEY---FLADR- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 199 TNDSINYFRMSKKiyphrPVLMVISHAAPHGPEDAAPQYTTAFPNASQHITPSYN--YAPNPDKHWIMRytgpMKPIHME 276
Cdd:cd16033 136 AIEMLEELAADDK-----PFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFAddFEDKPYIYRRER----KRWGVDT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 277 FTNMLQRKRLQ------TLLsvDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLV-KGKSMpYEFDIRVPFYIRG 349
Cdd:cd16033 207 EDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKW 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040678789 350 PNV-EAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLdtdrmmnrfqLNKKGKVWRDSFLVE 417
Cdd:cd16033 284 PGViAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLL----------RGEQPEDWRDEVVTE 342
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-393 |
2.75e-38 |
|
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: 147.33 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQ---DIE-LGSMQVmnKTRRI--MEQGGTHFSNAFVTTPM----CCPSRSSMLTGKYAHNhntYTNNEN 114
Cdd:cd16155 2 KPNILFILADDQradTIGaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 115 CSSPSwqaqhEPRTFGVYLNNTGYRTAFFGKYLNEYngtyippgwkewvamvknsrfynytlcrngvrekhgfeypkdyl 194
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 195 tdliTNDSINYFRMSKKiyPHRPVLMVISHAAPHGPEDAAPQYTTAFPnaSQHITPSYNYAP-NPdkhwimrytgpmkpi 273
Cdd:cd16155 108 ----ADAAIEFLEEYKD--GDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLPqHP--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 274 hmeFTNMLQRKRLQTLLS---------------------VDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVkG 332
Cdd:cd16155 165 ---FDNGEGTVRDEQLAPfprtpeavrqhlaeyyamithLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-G 240
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040678789 333 KSMPYEFDIRVPFYIRGPNVEAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLD 393
Cdd:cd16155 241 KQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIR 301
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
46-392 |
4.82e-38 |
|
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: 147.70 E-value: 4.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQ---DIELGSMQVMnKT---RRIMEQGgTHFSNaFVTTPMCCPSRSSMLTGKYAHN---HNTYTNNENCS 116
Cdd:cd16146 1 PNVILILTDDQgygDLGFHGNPIL-KTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHTILGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 117 SpswqaqhEPRTFGVYLNNTGYRTAFFGKYLNEYNGTYIPP--GWKEWV----------AMVKNSRFYNYTLCRNGVREK 184
Cdd:cd16146 78 L-------DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLghggggigqyPDYWGNDYFDDTYYHNGKFVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 185 HgfeypKDYLTDLITNDSINYFRMSKKiyphRPVLMVISHAAPHGPEDAAPQYttafpnasqhitpsynYAPNPDKHWim 264
Cdd:cd16146 151 T-----EGYCTDVFFDEAIDFIEENKD----KPFFAYLATNAPHGPLQVPDKY----------------LDPYKDMGL-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 265 rytgpmKPIHMEFTNMLQRkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIG-----QFGLVKGKSMPYEF 339
Cdd:cd16146 204 ------DDKLAAFYGMIEN--------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEG 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1040678789 340 DIRVPFYIRGPNV-EAGGINPHIVLNIDLAPTILDIAGMDVP--PDMDGKSILKLL 392
Cdd:cd16146 270 GHRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPegIKLDGRSLLPLL 325
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-396 |
1.11e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 144.22 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTD--DQDIeLGSM-QVMNKT---RRIMEqGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSSps 119
Cdd:cd16037 1 PNILIIMSDehNPDA-MGCYgHPVVRTpnlDRLAA-RGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 wqaqhEPRTFGVYLNNTGYRTAFFGK--YLNEyngtyippgwkewvamvknsrfynytlcrngvREKHGFEYpkdylTDL 197
Cdd:cd16037 77 -----DVPSWGHALRAAGYETVLIGKlhFRGE--------------------------------DQRHGFRY-----DRD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 198 ITNDSINYFR--MSKKiyphRPVLMVISHAAPHgpedaapqyttaFPnasqhitpsynyapnpdkhwimrYTGPMkpihm 275
Cdd:cd16037 115 VTEAAVDWLReeAADD----KPWFLFVGFVAPH------------FP-----------------------LIAPQ----- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 276 EFTNMLQRKRLQT---LLS-VDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYIRGPN 351
Cdd:cd16037 151 EFYDLYVRRARAAyygLVEfLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPG 229
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1040678789 352 VEAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLL----DTDR 396
Cdd:cd16037 230 IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAegpdDPDR 278
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
45-392 |
3.24e-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: 136.15 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQ---DIE-LGSMQVmnKTRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNencsSP 118
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGSPLI--KTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVV----GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 119 SWQAQHEP---RTFGVYLNNTGYRTAFFGK--------YL------NEYNGT-----YIPPGWKEWvamvkNSRFYNYTL 176
Cdd:cd16026 75 PGSKGGLPpdeITIAEVLKKAGYRTALVGKwhlghqpeFLptrhgfDEYFGIpysndMWPFPLYRN-----DPPGPLPPL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 177 CRNGVREkhgfEYPKDY--LTDLITNDSINYFRMSKKiyphRPVLMVISHAAPHGPEDAAPqyttAFPNASQHitpsyny 254
Cdd:cd16026 150 MENEEVI----EQPADQssLTQRYTDEAVDFIERNKD----QPFFLYLAHTMPHVPLFASE----KFKGRSGA------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 255 apnpdkhwimrytGPMKPIHMEftnmlqrkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHG--YHIGQFG---- 328
Cdd:cd16026 211 -------------GLYGDVVEE---------------LDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsag 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040678789 329 -LVKGKSMPYEFDIRVPFYIRGPN-VEAGGINPHIVLNIDLAPTILDIAGMDVPPD--MDGKSILKLL 392
Cdd:cd16026 263 pLRGGKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLL 330
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
77-392 |
4.79e-33 |
|
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: 133.92 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 77 GTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNnencSSPswQAQHEPrTFGVYLNNTGYRTAFFGK----------- 145
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARHL-TLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 146 YLNEYNGTY--IPPGWKEWVAMvknsrfynytlcrNGVREKHGfeyPKDYLTDlitnDSINYFRmskkIYPHRPVLMVIS 223
Cdd:cd16028 109 PLDPRLLSYelAMPGFDPVDRL-------------DEYPAEDS---DTAFLTD----RAIEYLD----ERQDEPWFLHLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 224 HAAPHGPEdAAPQYTTAFPNASQhiTPSYNYAPNPD---------KHWIMRYtgPMKPIHMEFTNM-----LQRKRLQT- 288
Cdd:cd16028 165 YIRPHPPF-VAPAPYHALYDPAD--VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMRAt 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 289 ---LLS-VDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFYIRGPNVEA----GGINPH 360
Cdd:cd16028 240 ylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREAdatrGQVVDA 318
|
330 340 350
....*....|....*....|....*....|..
gi 1040678789 361 IVLNIDLAPTILDIAGMDVPPDMDGKSILKLL 392
Cdd:cd16028 319 FTESVDVMPTILDWLGGEIPHQCDGRSLLPLL 350
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-414 |
1.14e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 131.18 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQDIE-LGSM-QVMNKTRRI--MEQGGTHFSNAFvTTPMCCPSRSSMLTGKYahNHNTYTNNencsSPSWQ 121
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKY--NFRNYVVF----GYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 122 AQHeprTFGVYLNNTGYRTAFFGK---YLNEYNGTYIPP-GWKEWVA-------MVKNSRFYNYTLCRNGVREKHgfeYP 190
Cdd:cd16151 74 KQK---TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYCLwqltetgEKYSRPATPTFNIRNGKLLET---TE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 191 KDYLTDLITNDSINYFRMSKK-----IYPhrpvlMVIshaaPHGPedaapqyTTAFPNASQHITPSYNYAPNPDKHWIM- 264
Cdd:cd16151 148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDP-------FVPTPDSPDWDPDDKRKKDDPEYFPDMv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 265 RYTgpmkpihmeftnmlqrkrlqtllsvDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIG-----QFGLVKG-KSMPYE 338
Cdd:cd16151 212 AYM-------------------------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040678789 339 FDIRVPFYIRGP-NVEAGGINPHIVLNIDLAPTILDIAGMDVPPD--MDGKSILKLLdtdrmmnrfqLNKKGKVWRDSF 414
Cdd:cd16151 267 AGTHVPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL----------LGKTGSPRREWI 335
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-402 |
1.14e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 129.25 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQ----DIELGSMQVMNKTRRIMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYtnnENCSSPS-W 120
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 121 QAQHEPRTFGVYLNNTGYRTAFFGKY-LNEYNGTYippgwkewvamvknsrfynytlcrngvrekhgfeYPKDyltDLIT 199
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 200 NDSINYFR-MSKKIYPHRPVLMVISHAAPHgpeDAapqyttafpnasqhitpsyNYAPNPDKHWImrytgpmkpihmEFT 278
Cdd:cd16035 121 AQAVEWLReRGAKNADGKPWFLVVSLVNPH---DI-------------------MFPPDDEERWR------------RFR 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 279 NMLqrkrLQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYIRGPNVEAGGIN 358
Cdd:cd16035 167 NFY----YNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGTGQT 242
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1040678789 359 -PHIVLNIDLAPTILDIAGMDVP------PDMDGKSILKLLdTDRMMNRFQ 402
Cdd:cd16035 243 tDALTSHIDLLPTLLGLAGVDAEarateaPPLPGRDLSPLL-TDADADAVR 292
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
46-397 |
3.19e-32 |
|
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: 131.74 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQDIELGS------MQVMNKTRriMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSSPS 119
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcygnkaMKTPNLDR--LAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 wqaqhepRTFGVYLNNTGYRTAFFGKY-LN--EYNGTYI-PPGWKE--WVAMVknsrfyNY---------TLCRNG--VR 182
Cdd:cd16156 79 -------KTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMR------NYldelteeerRKSRRGltSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 183 EKHGFEYPKDYlTDLITNDSINYFRMSKKiyphRPVLMVISHAAPHGPEDAAPQYTTAFPNASQHITPSY--NYAPNPDK 260
Cdd:cd16156 146 EAEGIKEEFTY-GHRCTNRALDFIEKHKD----EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPLH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 261 HWImrYTGPMK-PIHMEFTnmlqrKRLQTLLS----VDDSVEKVYNMLvdTGELDNTYVIYTADHGYHIGQFGL-VKGKS 334
Cdd:cd16156 221 QRL--WAGAKPhEDGDKGT-----IKHPLYFGcnsfVDYEIGRVLDAA--DEIAEDAWVIYTSDHGDMLGAHKLwAKGPA 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040678789 335 MpYEFDIRVPFYIRGPN-VEAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLDTDRM 397
Cdd:cd16156 292 V-YDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDPEI 354
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
45-393 |
9.29e-31 |
|
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: 126.53 E-value: 9.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQDIELGSM--QVMnKTRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENcsspsW 120
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYggHPA-KTPNIdrLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY-----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 121 QAQHEPR-TFGVYLNNTGYRTAFFGKYL--NEYNGTYIPPGWKEWVAMVKNSRFYNYTLCRNGVREKHG--------FEY 189
Cdd:cd16030 76 RKVAPDAvTLPQYFKENGYTTAGVGKIFhpGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpaweaADV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 190 PKDYLTD-LITNDSINYFRMSKK-----------IYPHRP-----------VLMVISHAAPHGPEDAAPQyttAFPNasq 246
Cdd:cd16030 156 PDEAYPDgKVADEAIEQLRKLKDsdkpfflavgfYKPHLPfvapkkyfdlyPLESIPLPNPFDPIDLPEV---AWND--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 247 hitpsYNYAPNPDKHWIMRYTGPMKPIHMEFtnmlQRKRLQTLLS----VDDSVEKVYNMLVDTGELDNTYVIYTADHGY 322
Cdd:cd16030 230 -----LDDLPKYGDIPALNPGDPKGPLPDEQ----ARELRQAYYAsvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGW 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040678789 323 HIGQFGLVkGKSMPYEFDIRVPFYIRGPNV-EAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLD 393
Cdd:cd16030 301 HLGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLK 371
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
75-396 |
3.59e-30 |
|
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: 122.30 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 75 QGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNnencsSPSWQAQhEPrTFGVYLNNTGYRTAFFGKylneyngty 154
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDN-----AAEFPAD-IP-TFAHYLRAAGYRTALSGK--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 155 ippgwkewvaMvknsRFYnytlcrnGVREKHGFEYpkdyltdlitnDSINYFRMSKKIYPH------RPVLMVISHAAPH 228
Cdd:cd16032 98 ----------M----HFV-------GPDQLHGFDY-----------DEEVAFKAVQKLYDLargedgRPFFLTVSFTHPH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 229 GPEDAAPQYTTAFPNASQHitpSYnYApnpdkhwIMRYtgpmkpihmeftnmlqrkrlqtllsVDDSVEKVYNMLVDTGE 308
Cdd:cd16032 146 DPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTGL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 309 LDNTYVIYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYIRGPNVEAGGINPHIVLNIDLAPTILDIAGMDVPPD---MDG 385
Cdd:cd16032 190 ADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHvppLDG 268
|
330
....*....|.
gi 1040678789 386 KSILKLLDTDR 396
Cdd:cd16032 269 RSLLPLLEGGD 279
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
46-388 |
8.31e-30 |
|
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: 123.04 E-value: 8.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQ---DIEL-GSMQVmnKTRRIME--QGGTHFSNAFVTtPMCCPSRSSMLTGKYAHNHNTYTNNENCSSPS 119
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 WQAQHEPrTFGVYLNNTGYRTAFFGKY-LNEYNGTYIPPG----------------WKEWVAMVKNsrFYNYTLCRNgvr 182
Cdd:cd16029 78 GLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSGGAND--YGNDDLRDN--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 183 EKHGFEYPKDYLTDLITNDSINYFRMSKkiyPHRPVLMVISHAAPHGPEDAAPQYTTAFPNASQHITPsynyapnpdkhw 262
Cdd:cd16029 152 EEPAWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 263 imrytgpmkpihmeftnmLQRKRLQTLLS-VDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFG------LVKGKSM 335
Cdd:cd16029 217 ------------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNT 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1040678789 336 PYEFDIRVPFYIRGP--NVEAGGINPHIVLNIDLAPTILDIAGMDVP--PDMDGKSI 388
Cdd:cd16029 279 LWEGGVRVPAFVWSPllPPKRGTVSDGLMHVTDWLPTLLSLAGGDPDdlPPLDGVDQ 335
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
45-393 |
4.02e-29 |
|
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: 121.01 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDD---QDIE-LGS---MQVMNKtrriMEQGGTHFSNaFVTTPMCCPSRSSMLTGKYAH-NHNTYTNNENCS 116
Cdd:cd16025 2 RPNILLILADDlgfSDLGcFGGeipTPNLDA----LAAEGLRFTN-FHTTALCSPTRAALLTGRNHHqVGMGTMAELATG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 117 SPSWQAQHEPR--TFGVYLNNTGYRTAFFGKYlneYNGtyiPPGWkewvamvknsrfynytlcrngvrekhgfeypkdYL 194
Cdd:cd16025 77 KPGYEGYLPDSaaTIAEVLKDAGYHTYMSGKW---HLG---PDDY---------------------------------YS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 195 TDLITNDSINYFRMSKKiyPHRPVLMVISHAAPHGP-----EDAA---------------------------PQYTTAFP 242
Cdd:cd16025 118 TDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAPlqapkEWIDkykgkydagwdalreerlerqkelgliPADTKLTP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 243 NASQhiTPSYNYAPNPDKHWIMRYtgpmkpihME-FTNMLQRkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHG 321
Cdd:cd16025 196 RPPG--VPAWDSLSPEEKKLEARR--------MEvYAAMVEH--------MDQQIGRLIDYLKELGELDNTLIIFLSDNG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 322 --YHIG--QFG---LVKGKSMPYEFDIRVPFYIRGPNV--EAGGINPHIVLNIDLAPTILDIAGMDVP--------PDMD 384
Cdd:cd16025 258 asAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELAGVEYPktvngvpqLPLD 337
|
....*....
gi 1040678789 385 GKSILKLLD 393
Cdd:cd16025 338 GVSLLPTLD 346
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
45-392 |
1.90e-28 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 120.54 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQDIE-LGSM---QVMNKTRRIMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSspsW 120
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 121 QAQHE-PRTFgvylNNTGYRTAFFGKY-------LNEYNGTYIPPGWkewvamVKNSRfynytlcrngVREKHGFEYPKD 192
Cdd:PRK13759 83 NYKNTlPQEF----RDAGYYTQCIGKMhvfpqrnLLGFHNVLLHDGY------LHSGR----------NEDKSQFDFVSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 193 YL-------------------------------------TDLITNDSINYFRMSKkiyPHRPVLMVISHAAPHGPEDAaP 235
Cdd:PRK13759 143 YLawlrekapgkdpdltdigwdcnswvarpwdleerlhpTNWVGSESIEFLRRRD---PTKPFFLKMSFARPHSPYDP-P 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 236 QYttAFPnasqhitpSYNYAPNPDKH---WimRYTGPMKP-------IHMEFTNMLQRKRLQTLLS----VDDSVEKVYN 301
Cdd:PRK13759 219 KR--YFD--------MYKDADIPDPHigdW--EYAEDQDPeggsidaLRGNLGEEYARRARAAYYGlithIDHQIGRFLQ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 302 MLVDTGELDNTYVIYTADHGYHIGQFGLVKgKSMPYEFDIRVPFYIRGP----NVEAGGINPHIVLNIDLAPTILDIAGM 377
Cdd:PRK13759 287 ALKEFGLLDNTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGG 365
|
410
....*....|....*
gi 1040678789 378 DVPPDMDGKSILKLL 392
Cdd:PRK13759 366 TIPDDVDGRSLKNLI 380
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-430 |
2.03e-28 |
|
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: 118.84 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDqdIELGSMQVMNKTRRI-------MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYahNHNTYTNNENCSSP 118
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY--PWRSRLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 119 SWQAQHEPR-TFGVYLNNTGYRTAFFGKY---LNEY--NGTYIPPGWKEWVAMvkNSRFynytlcRNGVREkHGFEY--- 189
Cdd:cd16143 77 SPPLIEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKDVDY--SKPI------KGGPLD-HGFDYyfg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 190 -PKDYLTDLITNDSINYFRMSKKiyPHRPVLMVISHAAPHGPedaapqyttafpnasqhITPS--YNYAPNPDKHwimry 266
Cdd:cd16143 148 iPASEVLPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGPY----- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 267 tGPMkpIHMeftnmlqrkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHG---YHIGQFGLVKG----------K 333
Cdd:cd16143 204 -GDF--VYE----------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGhdpsgplrgmK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 334 SMPYEFDIRVPFYIRGPN-VEAGGINPHIVLNIDLAPTILDIAGMDVPPD--MDGKSILKLLdtdrmmnrfqLNKKGKVW 410
Cdd:cd16143 265 ADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL----------LGPKKQEV 334
|
410 420
....*....|....*....|
gi 1040678789 411 RDSfLVERGKLLHKVLNDGK 430
Cdd:cd16143 335 RES-LVHHSGNGSFAIRKGD 353
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-390 |
2.08e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 115.72 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTD----DQ-DIELGSMQVMNKTRRIMEQGgTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYtnnencsspSW 120
Cdd:cd16148 1 MNVILIVIDslraDHlGCYGYDRVTTPNLDRLAAEG-VVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW---------GG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 121 QAQHEPRTFGVYLNNTGYRTAFFGkylneyNGTYIPPGWkeWVamvkNSRFYNYTLCRNGVREKHGFEYPKDyltDLITN 200
Cdd:cd16148 71 PLEPDDPTLAEILRKAGYYTAAVS------SNPHLFGGP--GF----DRGFDTFEDFRGQEGDPGEEGDERA---ERVTD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 201 DSINYFrmsKKIYPHRPVLMVISHAAPHGPedaapqyttafpnasqhitpsYNYApnpdkhwimryTGpmkpIHMeftnm 280
Cdd:cd16148 136 RALEWL---DRNADDDPFFLFLHYFDPHEP---------------------YLYD-----------AE----VRY----- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 281 lqrkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVKGKSMP-YEFDIRVPFYIRGPNVEAGGINP 359
Cdd:cd16148 172 -----------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEPGKRVD 240
|
330 340 350
....*....|....*....|....*....|.
gi 1040678789 360 HIVLNIDLAPTILDIAGMDVPPDMDGKSILK 390
Cdd:cd16148 241 ALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-389 |
1.74e-24 |
|
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: 103.86 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQ---------DIELgSMQVMNKtrriMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHN-----TYTN 111
Cdd:cd16149 1 PNILFILTDDQgpwalgcygNSEA-VTPNLDR----LAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGihdwiVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 112 NENCSSPSWQAQHEPrTFGVYLNNTGYRTAFFGKylneyngtyippgwkeWvamvknsrfynytlcrngvrekHGFEYPK 191
Cdd:cd16149 76 HGKTKKPEGYLEGQT-TLPEVLQDAGYRCGLSGK----------------W----------------------HLGDDAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 192 DYLTDLITNDsinyfrmskkiyphRPVLMVISHAAPHGPEdaapQYTTAfpnasqhitpsynyapnpdkhwimrytgpmk 271
Cdd:cd16149 117 DFLRRRAEAE--------------KPFFLSVNYTAPHSPW----GYFAA------------------------------- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 272 pihmeftnmlqrkrlqtLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGlVKGK-------SMpYEFDIRVP 344
Cdd:cd16149 148 -----------------VTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1040678789 345 FYIRGPN-VEAGGINPHIVLNIDLAPTILDIAGMDVPPDMD--GKSIL 389
Cdd:cd16149 209 FIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-393 |
6.33e-24 |
|
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: 105.78 E-value: 6.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 77 GTHFSNAFVTTPMCCPSRSSMLTGKYAH--NHNTYTNnencsspsWQAQHEPRTFGvYLNNTGYRTAFFGKylneyNGTY 154
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYPHvnGHRTLHH--------LLRPDEPNLLK-TLKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 155 IPPGWKEwvamvknsrfyNYTLCrngvrekhgfeypkDYLTdliTNDSINYFRmskKIYPHRPVLMVISHAAPHGPedaa 234
Cdd:cd16150 102 PGEFAAE-----------AYCDS--------------DEAC---VRTAIDWLR---NRRPDKPFCLYLPLIFPHPP---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 235 pqYTTAFPNASqhitpSYNYAPNPDkhwimryTGPMKPIHMEFTNMLQRKRLQTLLSVDDS----VEKVY-NM------- 302
Cdd:cd16150 147 --YGVEEPWFS-----MIDREKLPP-------RRPPGLRAKGKPSMLEGIEKQGLDRWSEErwreLRATYlGMvsrldhq 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 303 -------LVDTGELDNTYVIYTADHGYHIGQFGLV-KGKSMPYEFDIRVPFYIRGPNVEAGGINPHIVLNIDLAPTILDI 374
Cdd:cd16150 213 fgrlleaLKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDL 292
|
330
....*....|....*....
gi 1040678789 375 AGMDVPPDMDGKSILKLLD 393
Cdd:cd16150 293 AGIPLSHTHFGRSLLPVLA 311
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-390 |
2.04e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 101.30 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQ---------DIELG---SMQVMNKTRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYt 110
Cdd:cd16153 1 KPNILWIITDDQrvdslscynNAHTGkseSRLGYVESPNIdaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 111 NNENcsspSWQA-QHEPRTFGVYLNNTGYRTAFFGkylneyngtyippgwkewvamvknsrfynytlcrngvreKHGFEY 189
Cdd:cd16153 80 GFEA----AHPAlDHGLPTFPEVLKKAGYQTASFG---------------------------------------KSHLEA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 190 PKDYLTDLITNDSINYFRMSKKIYPHRPVLMVISHAAPHgpedaapqyttafpnasqhiTPSYnyapnPDKHWIMRYTgp 269
Cdd:cd16153 117 FQRYLKNANQSYKSFWGKIAKGADSDKPFFVRLSFLQPH--------------------TPVL-----PPKEFRDRFD-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 270 mkpiHMEFTNMlqrkrlqtllsVDDSVEKVYNMLVDTGEL---DNTYVIYTADHGYHIGQFGLVkGKSMPYEFDIRVPFY 346
Cdd:cd16153 170 ----YYAFCAY-----------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVPLI 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1040678789 347 IRGPNVE---AGGINPHIVLNIDLAPTILDIAGMDV--PPDMDGKSILK 390
Cdd:cd16153 234 VVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDLFE 282
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
45-392 |
6.45e-23 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 103.28 E-value: 6.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQ---DI--------ELGSM-QVMNKtrrimeqgGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYtnN 112
Cdd:cd16160 1 KPNIVLFFADDMgygDLasyghptqERGPIdDMAAE--------GIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 113 ENCSSPSWQAQHEPR---TFGVYLNNTGYRTAFFGKY---LNEYN----------------GTYIPPG-------WKEWV 163
Cdd:cd16160 71 GTRVFLPWDIGGLPKtevTMAEALKEAGYTTGMVGKWhlgINENNhsdgahlpshhgfdfvGTNLPFTnswacddTGRHV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 164 AmvknsrFYNYTLCrngvrekhgFEYPKD----------YLTDLITNDSINYFRMSKkiypHRPVLMVISHAAPHgpeda 233
Cdd:cd16160 151 D------FPDRSAC---------FLYYNDtiveqpiqheHLTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTH----- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 234 APQYTTAfpnasqhitpsynyapnpdkhwimrytgpmkpihmEFTNMLQRKRL-QTLLSVDDSVEKVYNMLVDTGELDNT 312
Cdd:cd16160 207 TPLFASK-----------------------------------RFKGKSKRGRYgDNINEMSWAVGEVLDTLVDTGLDQNT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 313 YVIYTADHGYHI------GQFGLVKG-KSMPYEFDIRVPFYIRGPNVEAGGINPHIVLNIDLAPTILDIAGMDVPPD--M 383
Cdd:cd16160 252 LVFFLSDHGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriY 331
|
....*....
gi 1040678789 384 DGKSILKLL 392
Cdd:cd16160 332 DGLSITDLL 340
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-392 |
8.02e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 98.58 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQDIE------LGS-MQVMNKTRRIMEQGGThFSNAFVTtPMCCPSRSSMLTGKYAHNHNTYTNNENCSSP 118
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSdLPVTPTLDSLANSGIV-FDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 119 SwqaqHE-PRTFGVYLNNTGYRTAFFGKYL--NEYNGTYIPPGWKEWVAMVKN--SRFYNYTLCRNGVREKHgfeypKDY 193
Cdd:cd16154 79 E----ETlLQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-----TEY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 194 LTDLITNDSINYFRMSkkiypHRPVLMVISHAAPHGPedaapqyttaFpnasqHITPSYNYAPNPdkhwimryTGPMKPI 273
Cdd:cd16154 150 ATTKLTNLAIDWIDQQ-----TKPWFLWLAYNAPHTP----------F-----HLPPAELHSRSL--------LGDSADI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 274 HMEftnmlqrKR---LQTLLSVDDSVEKVYNMLvDTGELDNTYVIYTADHGYHiGQ-----FGLVKGKSMPYEFDIRVPF 345
Cdd:cd16154 202 EAN-------PRpyyLAAIEAMDTEIGRLLASI-DEEERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVPL 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1040678789 346 YIRGPNVEAGGINPHIVLNI-DLAPTILDIAGMDVPPDMDGKSILKLL 392
Cdd:cd16154 273 IVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLL 320
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
46-392 |
8.73e-21 |
|
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: 95.30 E-value: 8.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQDIEL----GSMQVMNKTRRIMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSS--PS 119
Cdd:cd16171 1 PNVVMVMSDSFDGRLtfrpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPnyPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 WQaqheprtfgVYLNNTGYRTAFFGKyLNEYNGTYIPPGWKE-WvamvknSRFYNYTLCRNGvrekhgfeYPKdylTDLI 198
Cdd:cd16171 81 WM---------DRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEG--------RPT---VNLV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 199 TNDSINyfRMSKKIYPhrpvlmvISHAAPHGPEDAAPQYTTAF--------PnasqHITPSYNYAPNpdkhwimryTGPM 270
Cdd:cd16171 134 GDRSTV--RVMLKDWQ-------NTDKAVHWIRKEAPNLTQPFalylglnlP----HPYPSPSMGEN---------FGSI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 271 KPIHMEFTNMLQRkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVKGKSMpYEFDIRVPFYIRGP 350
Cdd:cd16171 192 RNIRAFYYAMCAE--------TDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGP 262
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1040678789 351 NVEAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLL 392
Cdd:cd16171 263 GIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
46-375 |
1.32e-18 |
|
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: 86.32 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDD---QDIELGSMQVMNKTR-RIMEQGGTHFsNAFVTTPMC--CPSRSSMLTGKYAHNHNTYTNNENCSSPS 119
Cdd:cd00016 1 KHVVLIVLDGlgaDDLGKAGNPAPTTPNlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 WQAQHEP---RTFGVYLNNTGYRTAFFGKYlneyngtyippgwkewvamvknsrfynytlcrngvrekhgfeypkdyltd 196
Cdd:cd00016 80 SRAAGKDedgPTIPELLKQAGYRTGVIGLL-------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 197 litnDSINYFRMSKkiyphrPVLMVISHAAPHGPedaapqyttafpnasqhitpSYNYAPNPDkhwimrytgpmkpihmE 276
Cdd:cd00016 110 ----KAIDETSKEK------PFVLFLHFDGPDGP--------------------GHAYGPNTP----------------E 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 277 FTNMLQRkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHG---YHIGQFGLVKGKSMPYEFDIRVPFYIRGPNVE 353
Cdd:cd00016 144 YYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVK 215
|
330 340
....*....|....*....|..
gi 1040678789 354 AGGINPHIVLNIDLAPTILDIA 375
Cdd:cd00016 216 KGGVKHELISQYDIAPTLADLL 237
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
764-813 |
1.34e-17 |
|
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: 86.06 E-value: 1.34e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1040678789 764 CTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDINTDPYQLVNAVNTL 813
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
46-392 |
3.29e-15 |
|
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 79.41 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQDI-ELG-----SMQVMNKTRriMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSSpS 119
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 WQAQHEPRTFGVYLNNTGYRTAFFGKY---LNEyNGTYIPPgwkewvamvkNSRFYNYTlcrnGVREKHGFEyPKDYLTD 196
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT----------HQGFDHYL----GIPYSHDQG-PCQNLTC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 197 LITNDSInyFRMSKKIYPHRPVLM--VISHAAPHGPeDAAPQYTTAfpnASQHIT-------PSYNYAPNPDKHWiMRYT 267
Cdd:cd16158 143 FPPNIPC--FGGCDQGEVPCPLFYneSIVQQPVDLL-TLEERYAKF---AKDFIAdnakegkPFFLYYASHHTHY-PQFA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 268 GpmkpihMEFTNMLQRKRL-QTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHI------GQFGLVK-GKSMPYEF 339
Cdd:cd16158 216 G------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTYEG 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1040678789 340 DIRVPFYIRGPNVEAGGINPHIVLNIDLAPTILDIAGMDVPP-DMDGKSILKLL 392
Cdd:cd16158 290 GVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPIL 343
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
45-436 |
1.06e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 78.54 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILtddqdIElgSMQ--VMNKT----------RRIMEQGgTHFSNAFVTTPMCCPSRSSMLTGKY-AHNHNTYTN 111
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 112 NencsspswqAQHEPRTFGVYLNNTGYRTAFFgkylneYNGtyippgwkewvamvkNSRFYNytlcRNGVREKHGFE--Y 189
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 190 PKDYLTDLITN-----D------SINYFRMSKKiyphrPVLMVISHAAPHGPedaapqYTtaFPNASQHITpsynyapnp 258
Cdd:COG1368 352 DREDFDDPFDGgwgvsDedlfdkALEELEKLKK-----PFFAFLITLSNHGP------YT--LPEEDKKIP--------- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 259 dkhwimrytgpmkpihmEFTNMLQRKRLQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGyhigqfGLVKGKSmPYE 338
Cdd:COG1368 410 -----------------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 339 FDI---RVPFYIRGPNVEAGGINPHIVLNIDLAPTILDIAGMDVPPD-MDGKSilkLLDTDRmmNRFQLNKKGKVWRDSF 414
Cdd:COG1368 466 NPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRD---LLSPDT--DPFAFRNGGFITDDYV 540
|
410 420
....*....|....*....|..
gi 1040678789 415 LVERGKLLHKVLNDGKDMAEEE 436
Cdd:COG1368 541 YVLKTGELTEEDKELEEEALAY 562
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
45-400 |
1.30e-14 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 77.51 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQDI-ELGSMQVMNK-TRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKY----------AHNHNTYT 110
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLpirngfyttnAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 111 NNENCSSPSWQAQHEPRtfgvYLNNTGYRTAFFGKYLNEYNGTYIP--PGWKEW-------VAMVKNSRFYNYTLCRNgv 181
Cdd:cd16157 81 PQNIVGGIPDSEILLPE----LLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWfgapnchFGPYDNKAYPNIPVYRD-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 182 rEKHGFEYPKDYLTDLITNDS--INYFR------MSKKIYPHRPVLMVISHAAPHgpedaAPQYttafpnASQHitpsyn 253
Cdd:cd16157 155 -WEMIGRYYEEFKIDKKTGESnlTQIYLqealefIEKQHDAQKPFFLYWAPDATH-----APVY------ASKP------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 254 yapnpdkhwimrytgpmkpihmeFTNMLQRKRL-QTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHG---YHIGQFG- 328
Cdd:cd16157 217 -----------------------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGg 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 329 ----LVKGKSMPYEFDIRVPFYIRGP-NVEAGGINpHIVLNI-DLAPTILDIAGMDVPPD--MDGKSILKLLDTDRMMNR 400
Cdd:cd16157 274 sngpFLCGKQTTFEGGMREPAIAWWPgHIKPGQVS-HQLGSLmDLFTTSLALAGLPIPSDraIDGIDLLPVLLNGKEKDR 352
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-382 |
1.38e-14 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 76.80 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILILTDDQDI-ELGS----MQVMNKTRRI--MEQGGTHFSNAFVTtPMCCPSRSSMLTGKYAhnhntytNNENCSSP 118
Cdd:cd16142 1 PNILVILGDDIGWgDLGCygggIGRGAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTGLTTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 119 SWQAQ-----HEPRTFGVYLNNTGYRTAFFGK-YLNEYNGTYipP---GWKEWvamvknsrfynytlcrngvrekHGFEY 189
Cdd:cd16142 73 GLPGSpgglpPWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEF----------------------YGNLY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 190 pkDYLTDLITNDSINYfrMSKKIYPHRPVLMVISHAAPHGPEDAAPQYttafpnasQHITPS-YNYApnpdkhwimrytg 268
Cdd:cd16142 129 --HTIDEEIVDKAIDF--IKRNAKADKPFFLYVNFTKMHFPTLPSPEF--------EGKSSGkGKYA------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 269 pmkpihmeftnmlqrkrlQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHG-----YHIGQFGLVKG-KSMPYEFDIR 342
Cdd:cd16142 184 ------------------DSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWEGGVR 245
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1040678789 343 VPFYIRGPN-VEAGGINPHIVLNIDLAPTILDIAGMDVPPD 382
Cdd:cd16142 246 VPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
45-392 |
2.27e-14 |
|
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: 77.33 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDDQDI-ELGSMQvmNKTRR-----IMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYA-----HNHNTYTNNE 113
Cdd:cd16159 1 KPNIVLFMADDLGIgDVGCFG--NDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirsgmASSHGMRVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 114 NCSSPSWQAQHEpRTFGVYLNNTGYRTAFFGKY----------------LN-----------------------EYNGTY 154
Cdd:cd16159 79 FTASSGGLPPNE-TTFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEYDLSF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 155 IPPGWKE--------------------------------------WVAMVKNSRFYNYTLCRNG-VREKhgfeyPKDY-- 193
Cdd:cd16159 158 DPLFPLLtafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHeVVEQ-----PMSLen 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 194 LTDLITNDSINYFRMSKkiypHRPVLMVISHAAPHGPEDAAPQyttaFPNASQHitpsynyapnpdkhwimrytGPMKPI 273
Cdd:cd16159 233 LTQRLTKEAISFLERNK----ERPFLLVMSFLHVHTALFTSKK----FKGRSKH--------------------GRYGDN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 274 HMEftnmlqrkrlqtllsVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHI-----------GQFGLVKGKSMP-YEFDI 341
Cdd:cd16159 285 VEE---------------MDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEGGI 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040678789 342 RVPFYIRGPnveaGGINPHIVL-----NIDLAPTILDIAGMDVPPD--MDGKSILKLL 392
Cdd:cd16159 350 RVPTIVRWP----GVIPPGSVIdeptsLMDIFPTVAALAGAPLPSDriIDGRDLMPLL 403
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
46-376 |
2.74e-14 |
|
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: 74.64 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 46 PNIILIL-----TDDQDIELGSMQVMNKTRRIMEQGgTHFSNAFVTTPMCCPSRS--SMLTGkyahnhnTYTNNENCSSP 118
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 119 SWQAQHEPRTFGVYLNNTGYRTAFFgkylneYNGtyippgwkewvamvkNSRFYNytlcRNGVREKHGFE--YPKDYLTD 196
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 197 LITNDSINY------FRMSKKIY---PHRPVLMVISHAAPHGPedaapqyttafpnasqhitpsYNYAPNPDKhwimryt 267
Cdd:cd16015 128 DEKETNGWGvsdeslFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 268 gpmKPIHMEFTNMLQRKRLQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVKGKSMPYEFdiRVPFYI 347
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 1040678789 348 RGPNVEAGGINPHIVLNIDLAPTILDIAG 376
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
45-392 |
3.72e-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: 75.58 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 45 RPNIILILTDD---QDIELGSMQVMNKTRRI--MEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAhNHNTYTNNENCSSPS 119
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLG-LRNGVGHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 120 wqaqheprtfGVYLNNT---------GYRTAFFGKYLNEYNGTYIPpgwkewvamvkNSRFYNYTLcrnGVREKHGFEYP 190
Cdd:cd16161 80 ----------GLPLNETtlaevlrqaGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 191 KDYL---TDLITNDSinyfrmSKKiyphRPVLMVISHAAPHGPEDAAPQyttaFPNASQHITPsynyapnpdkhwimryT 267
Cdd:cd16161 136 DRYAqfaTDFIQRAS------AKD----RPFFLYAALAHVHVPLANLPR----FQSPTSGRGP----------------Y 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 268 GpmkpihmeftnmlqrkrlQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTAD---------------HGYHIGQFGLVKG 332
Cdd:cd16161 186 G------------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVA 247
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040678789 333 KSMPYEFDIRVPFYIRGPN-VEAGGINPHIVLNIDLAPTILDIAGMDVPPD--MDGKSILKLL 392
Cdd:cd16161 248 KASTWEGGHREPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
286-372 |
2.07e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 51.83 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 286 LQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGY-----------HIGQFGlvkgksmPYEfdIRVPFYIRGPNVEA 354
Cdd:COG3083 430 RNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS-------RYQ--LQVPLVIHWPGTPP 500
|
90
....*....|....*...
gi 1040678789 355 GGINpHIVLNIDLAPTIL 372
Cdd:COG3083 501 QVIS-KLTSHLDIVPTLM 517
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
292-389 |
2.18e-06 |
|
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: 51.65 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 292 VDDSVEKVYNMLVdtgELDNTYVIyTADHG-----YHIGQFGLVKGKSMPyefdiRVPFYIRGPNV-----EAGGInphi 361
Cdd:cd16010 412 VDECLGRIVEAVL---ENGGTLLI-TADHGnaeemIDPETGGPHTAHTTN-----PVPFIIVDPGLkrkllKDGGL---- 478
|
90 100
....*....|....*....|....*...
gi 1040678789 362 vlnIDLAPTILDIAGMDVPPDMDGKSIL 389
Cdd:cd16010 479 ---ADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
70-376 |
3.88e-06 |
|
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: 49.51 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 70 RRIMEQGgTHFS---NAFVT-TpmcCPSRSSMLTGKYAHNH----NTY---TNNENCSSPSWQAQH---EPRTFGVYLNN 135
Cdd:cd16018 26 KRLAEEG-VRAKyvkPVFPTlT---FPNHYSIVTGLYPESHgivgNYFydpKTNEEFSDSDWVWDPwwiGGEPIWVTAEK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 136 TGYRTA-FFgkylneyngtyippgWkeWVAMVKNSRFYNYTLCRNGVREKHGFEYPKDYLTDLItndsINYFRMSkkiyp 214
Cdd:cd16018 102 AGLKTAsYF---------------W--PGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTI----LEWLDLE----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 215 hRPVLMVIshaaphgpedaapqyttafpnasqhitpsynYAPNPD--KHwimRYtGPMKPihmEFTNMLQRkrlqtllsV 292
Cdd:cd16018 156 -RPDLILL-------------------------------YFEEPDsaGH---KY-GPDSP---EVNEALKR--------V 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 293 DDSVEKVYNMLVDTGELDNTYVIYTADHGY-----HiGQFglvkgksmPYEFDIRVPFYIRGPNVEAGGINPHIvLNIDL 367
Cdd:cd16018 189 DRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF-RNVDI 258
|
....*....
gi 1040678789 368 APTILDIAG 376
Cdd:cd16018 259 YPLMCNLLG 267
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
345-394 |
5.50e-06 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 50.29 E-value: 5.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1040678789 345 FYIRGPNVEAGGINPHIVLnIDLAPTILDIAGMDVPPDMDGKSILKLLDT 394
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFAR 470
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
292-390 |
2.03e-05 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 48.56 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 292 VDDSVEKVYNMLVdtgELDNTYVIyTADHG-------YHIGQfglvkgksmPY-----EfdiRVPFYI--RGPNVEAGGI 357
Cdd:PRK05434 417 VDECLGRVVDAVL---KVGGTLLI-TADHGnaeqmidPETGQ---------PHtahttN---PVPFILvgGKALRLEGGK 480
|
90 100 110
....*....|....*....|....*....|...
gi 1040678789 358 nphivLNiDLAPTILDIAGMDVPPDMDGKSILK 390
Cdd:PRK05434 481 -----LA-DIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
343-390 |
4.93e-05 |
|
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: 46.97 E-value: 4.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1040678789 343 VPFYIRGPN----VEAGGInphivLnIDLAPTILDIAGMDVPPDMDGKSILK 390
Cdd:COG0696 465 VPFILVGGDkgvkLREDGR-----L-ADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
286-371 |
1.07e-03 |
|
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293744 Cd Length: 294 Bit Score: 42.19 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 286 LQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHG-----YHigqfglvkGKSMPYEfdIRVPFY-----IRGPNVEAG 355
Cdd:cd16020 182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGmtdwgSH--------GDGSPDE--TETPFIawgagIKHPTPGRG 251
|
90 100
....*....|....*....|....*.
gi 1040678789 356 GINP----------HIVLNIDLAPTI 371
Cdd:cd16020 252 PSFSanwgglrlprHDLDQADLAPLM 277
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
292-402 |
4.68e-03 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 40.79 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 292 VDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQF-GLVKGK---SMPYEFdIRVPFYIR--GPN-VEAGGINPH-IVL 363
Cdd:pfam02995 313 LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLrRTSQGMleeRLPLMS-IRYPPWFRetYPQaVENLELNANrLTT 391
|
90 100 110
....*....|....*....|....*....|....*....
gi 1040678789 364 NIDLAPTILDIAGMDVPPDMDGKSILKLLDTDRMMNRFQ 402
Cdd:pfam02995 392 PFDLHATLKDILHLGELSDKELQDRMKALDCPRGISLFL 430
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
288-378 |
7.09e-03 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 39.53 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040678789 288 TLLSVDDSVEKVYNMLVDTGEldNTYVIYTADHGYHIGQFGlVKGKSMPYEFD--IRVPFYI--------RGPNVEAGGI 357
Cdd:cd16017 191 SILYTDYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRAN 267
|
90 100
....*....|....*....|.
gi 1040678789 358 NPHIVLNIDLAPTILDIAGMD 378
Cdd:cd16017 268 KDRPFSHDNLFHTLLGLLGIK 288
|
|
| |
