|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
41-383 |
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: 549.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQDVELGSLQVMNKTRKIMEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNE--NCSSPSWQA 118
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 119 QHEPRSFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWVGLIKNSRFYNYTVCrNGNKEKHGADYAKDYFTDLI 194
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 195 TNDSINYFRTSKRMfpHRPVMMVISHAAPHGPEDSAPQYSELFPNAS-QHITPSYNYAPNMDKHWIMQYTGPMkPIHMEF 273
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLN-PTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 274 TNYLHRKRLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFVRGPNVEPGAR 353
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350
....*....|....*....|....*....|
gi 51467917 354 NNHVVLNIDLAPTILDIAGLDTPPDMDGKS 383
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
41-413 |
4.68e-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: 4.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQ--DVeLGSLQ-VMNKT---RKIMEDGgTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNENcSSP 114
Cdd:cd16031 2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQaqhepRSFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWVGLIKNSRFYNYTVCRNGNKEKHgadyaKDYFTDLI 194
Cdd:cd16031 79 ASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTDII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 195 TNDSINYFRTSKrmfPHRPVMMVISHAAPHGPEDSAPQYSELFPNAsqHITPSYNYAPN-------------MDKHWIMQ 261
Cdd:cd16031 149 TDKALDFLKERD---KDKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEPETFDDDdyagrpewareqrNRIRGVLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 262 YTgpmKPIHMEFTNYLhRKRLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPF 341
Cdd:cd16031 224 GR---FDTPEKYQRYM-KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPL 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51467917 342 FVRGP-NVEPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEqektgnrfkpNRKPKVWRDTFLVE 413
Cdd:cd16031 299 IIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
41-413 |
4.19e-75 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 253.65 E-value: 4.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQDVelGSLQVMNKTR-------KIMEDGgTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNENCSS 113
Cdd:COG3119 23 RPNILFILADDLGY--GDLGCYGNPLiktpnidRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 114 PswqAQHEPRSFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewvgliknsrfynytvcrngnkekhgadyakdYFTDL 193
Cdd:COG3119 100 G---LPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 194 ITNDSINYFRTSKRmfPHRPVMMVISHAAPHGPEDSAPQYSELFPNasQHITPSYNYAPNMDKHWIMQYtgpmkpihmef 273
Cdd:COG3119 133 LTDKAIDFLERQAD--KDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR----------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 274 tnyLHRKRLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFVRGPN-VEPGA 352
Cdd:COG3119 198 ---ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGS 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51467917 353 RNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEKtgnrfkpnrkpKVWRDTFLVE 413
Cdd:COG3119 275 VSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEK-----------AEWRDYLYWE 324
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
533-678 |
2.84e-66 |
|
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: 219.52 E-value: 2.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 533 RPRFVHTRPARSLSVEFEGEIYDVDLqADDKTPLEPRPISKRHYEpEPGFDSDFGLESDDGseEMQSDDTNAVGYPNSLK 612
Cdd:pfam12548 1 KPRFVRTRQKRSLSVEFEGEVYDIDL-EEEYQPLEPRNLLKRHAR-DDGEEGEEGEESSGT--GSKRDSSNSVGPPASVK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51467917 613 VTHKCFILINDTVRCEREIYQSSRAWKDHKNFVDHEIEQLQDKMKKLREVRGHLKRRRPDECDCSK 678
Cdd:pfam12548 77 VTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
42-383 |
6.57e-54 |
|
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: 188.03 E-value: 6.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQ---DVE-LGSLQVmnKT---RKIMEDGgTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNENcssP 114
Cdd:cd16022 1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQAQHEPrSFAVYLNNTGYRTAFFGKylneyngsyippgwreWvgliknsrfynytvcrngnkekHgadyakdyftdli 194
Cdd:cd16022 75 GGLPPDEP-TLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 195 tNDSINYFRTSKrmfPHRPVMMVISHAAPHGPedsapqyselfpnasqhitpsYNYAPNMDkhwimqytgpmkpihmeft 274
Cdd:cd16022 103 -DEAIDFIERRD---KDKPFFLYVSFNAPHPP---------------------FAYYAMVS------------------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 275 nylhrkrlqtlmSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFVRGPNV-EPGAR 353
Cdd:cd16022 139 ------------AIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKiPAGQV 206
|
330 340 350
....*....|....*....|....*....|
gi 51467917 354 NNHVVLNIDLAPTILDIAGLDTPPDMDGKS 383
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-393 |
6.37e-52 |
|
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: 188.16 E-value: 6.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTD-----------DQDVELGSLqvmnktRKIMEDgGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNne 109
Cdd:cd16034 1 KPNILFIFADqhraqalgcagDDPVKTPNL------DRLAKE-GVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 110 ncsspSWQAQHEPRSFAVYLNNTGYRTAFFGK--------YLNEYNGSYIPP----GWREWVGLIKNSRFYNYTVCRNGN 177
Cdd:cd16034 72 -----DVPLPPDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 178 KEKHGADYAKDYFTDLItndsINYFRtsKRMFPHRPVMMVISHAAPHGPEDSAPQ-YSELFPNASQHitpsynYAPNMDk 256
Cdd:cd16034 147 KRIYIKGYSPDAETDLA----IEYLE--NQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLL------LRPNVP- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 257 hWIMQYTgpmKPIHMEFTNYL-HRKrlqtlmSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDF 335
Cdd:cd16034 214 -EDKKEE---AGLREDLRGYYaMIT------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPYEE 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 51467917 336 DIRVPFFVRGPNVEPGARNNHVVLN-IDLAPTILDIAGLDTPPDMDGKSILKLLEQEKT 393
Cdd:cd16034 283 SIRVPFIIRYPGKIKAGRVVDLLINtVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKD 341
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
42-396 |
1.02e-51 |
|
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: 186.56 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDVELGSlqVMN---KTRKIME--DGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTN-NENCSSPS 115
Cdd:cd16027 1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 116 WQaqhepRSFAVYLNNTGYRTAFFGKYlnEYNGSYIPPGWrewvgliknsrFYNYTVCRNGNKEKHGADYAKDYFTDLIT 195
Cdd:cd16027 79 GV-----KTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 196 ND----SINYFRtskrmfPHRPVMMVISHAAPHGPEDsapqyselfpnasqhITPSYNYAPNmdkhwimqytgpmKPIHM 271
Cdd:cd16027 141 GQpfflWFGFHD------PHRPYPPGDGEEPGYDPEK---------------VKVPPYLPDT-------------PEVRE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 272 EFTNYLhrkrlQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYhigqfGLVKGKSMPYDFDIRVPFFVRGPN-VEP 350
Cdd:cd16027 187 DLADYY-----DEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKP 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 51467917 351 GARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEKTGNR 396
Cdd:cd16027 257 GSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
42-406 |
1.28e-49 |
|
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: 181.97 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDD---QDVelgSLQvMNKtrkIME--------DGGTSFTNAFVTTPMCCPSRSSMLTGKY--------VHNH 102
Cdd:cd16144 1 PNIVLILVDDlgwADL---GCY-GSK---FYEtpnidrlaKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdVIPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 103 NTYTNNENCSSPSWQAQHEPRS---FAVYLNNTGYRTAFFGKY-LNEYNGSYipP---GWREWVGLIKNSRFYNYTVCRN 175
Cdd:cd16144 74 RRGPPDNTKLIPPPSTTRLPLEevtIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 176 GNKEKHGADYAKDYFTDLITNDSINYFRTSKRmfphRPVMMVISHAAPHGPEDSAPQYSELFpnasqhitpsYNYAPNMD 255
Cdd:cd16144 152 KPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKY----------EKKKKGLR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 256 KHWIMQYTGPMkpihmeftnylhrkrlqtLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLV-------KG 328
Cdd:cd16144 218 KGQKNPVYAAM------------------IESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 329 KSMPYDFDIRVPFFVRGPNV-EPGARNNHVVLNIDLAPTILDIAGLDTPP--DMDGKSILKLLeqekTGNRFKPNRKPKV 405
Cdd:cd16144 280 KGSLYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLL----KGGEADLPRRALF 355
|
.
gi 51467917 406 W 406
Cdd:cd16144 356 W 356
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
42-373 |
1.64e-48 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 174.92 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQ-DVELGSLQ-VMNKTRKI--MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNEncsspsWQ 117
Cdd:pfam00884 1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 118 AQHEPRSFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWVGLIKNSRFYNYTVCRNGNKEKHGadyakdYFTDLIT 195
Cdd:pfam00884 75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 196 NDSINYFRTskrmfPHRPVMMVISHAAPHGPedsaPQYSELFPNASQHITPSYNYApnmdkhwimqytgpmkpihmeftN 275
Cdd:pfam00884 149 DEALEFLDN-----NDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSE-----------------------E 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 276 YLHRKRLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFVRGPNVEPGA 352
Cdd:pfam00884 197 QLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAKG 276
|
330 340
....*....|....*....|..
gi 51467917 353 RNNHVVLN-IDLAPTILDIAGL 373
Cdd:pfam00884 277 QKSEALVShVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-413 |
4.05e-46 |
|
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: 171.63 E-value: 4.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDV----ELGSLQVmnKTRKI--MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNENCSSPS 115
Cdd:cd16033 1 PNILFIMTDQQRYdtlgCYGNPIV--KTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 116 WQAQHEPRSFAVYLNNTGYRTAFFGKylneyngsyippgwreW-VGLIKNSRFYNYtvcrngnKEKHGADYAKDYFtdlI 194
Cdd:cd16033 79 RGLPPGVETFSEDLREAGYRNGYVGK----------------WhVGPEETPLDYGF-------DEYLPVETTIEYF---L 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 195 TNDSINYFRTSKRmfPHRPVMMVISHAAPHGPEDSAPQYSELFPNASqhITPSYNYAPNM-DKHWImQYTGPMKPIHMEF 273
Cdd:cd16033 133 ADRAIEMLEELAA--DDKPFFLRVNFWGPHDPYIPPEPYLDMYDPED--IPLPESFADDFeDKPYI-YRRERKRWGVDTE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 274 TNYLHRKRLQ------TLMsvDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLV-KGKSMpYDFDIRVPFFVRGP 346
Cdd:cd16033 208 DEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKWP 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51467917 347 NV-EPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEKTGNrfkpnrkpkvWRDTFLVE 413
Cdd:cd16033 285 GViAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-397 |
7.12e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 156.55 E-value: 7.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDVEL----GSLQVmnKT---RKIMEDGgTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNENCSSp 114
Cdd:cd16037 1 PNILIIMSDEHNPDAmgcyGHPVV--RTpnlDRLAARG-TRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 swqaqhEPRSFAVYLNNTGYRTAFFGK--YlneyngsyippgwrewvgliknsrfynytvcrNGNKEKHGADYakdyfTD 192
Cdd:cd16037 77 ------DVPSWGHALRAAGYETVLIGKlhF--------------------------------RGEDQRHGFRY-----DR 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 193 LITNDSINYFRtsKRMFPHRPVMMVISHAAPHgpedsapqyselFPnasqhitpsynyapnmdkhwimqYTGPMkpihmE 272
Cdd:cd16037 114 DVTEAAVDWLR--EEAADDKPWFLFVGFVAPH------------FP-----------------------LIAPQ-----E 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 273 FTNYLHRKRLQT---LMS-VDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFVRGPNV 348
Cdd:cd16037 152 FYDLYVRRARAAyygLVEfLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGI 230
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 51467917 349 EPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEKTGNRF 397
Cdd:cd16037 231 PAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPDDPDRV 279
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-396 |
4.35e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 152.72 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQDVE----LGSLQVmnKTRKI--MEDGGTSFTNAFVTTPM----CCPSRSSMLTGKYVHNhntYTNNEN 110
Cdd:cd16155 2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 111 CSSPSwqaqhEPRSFAVYLNNTGYRTAFFGKYLNEYngsyippgwrewvgliknsrfynytvcrngnkekhgADYAKDYF 190
Cdd:cd16155 77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF------------------------------------ADAAIEFL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 191 TDLITNDsinyfrtskrmfphRPVMMVISHAAPHGPEDSAPQYSELFPnaSQHITPSYNYAPnmdKHwimQYTGPMKPIH 270
Cdd:cd16155 116 EEYKDGD--------------KPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLP---QH---PFDNGEGTVR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 271 MEF------TNYLHRKRLQ----TLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVP 340
Cdd:cd16155 174 DEQlapfprTPEAVRQHLAeyyaMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-GKQNLYEHSMRVP 252
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 51467917 341 FFVRGPNVEPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEKTGNR 396
Cdd:cd16155 253 LIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVR 308
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
42-406 |
2.64e-39 |
|
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: 151.59 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDV-ELGSL-QVMNKTRKI--MEDGGTSFTNAFVTTPMCCPSRSSMLTGKyvHNHNTY--TNNENCSSPS 115
Cdd:cd16145 1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTGHTRvrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 116 WQAqhEPRSFAVYLNNTGYRTAFFGKY-LNEYNGSYIPP--GWREWVG--------------LIKNSR--FYNYTVCRNG 176
Cdd:cd16145 79 LPP--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGyldqvhahnyypeyLWRNGEkvPLPNNVIPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 177 NKEKHGADYAKDYFTDLITNDSINYFRT--SKRMFPHRPVmmVISHAAPHGPEDSAPQYSELFPnasqhitPSYNYAPnm 254
Cdd:cd16145 157 DEGNNAGGGGGTYSHDLFTDEALDFIREnkDKPFFLYLAY--TLPHAPLQVPDDGPYKYKPKDP-------GIYAYLP-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 255 dkhWIMQytgpmkpihmeftnylhRKRLQTLMS-VDDSVEKVYNALVDTGELDNTYIIYTADHGYHI-------GQF--- 323
Cdd:cd16145 226 ---WPQP-----------------EKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfds 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 324 --GLVKGK-SMpYDFDIRVPFFVRGPN-VEPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLeqekTGNRFKP 399
Cdd:cd16145 286 ngPLRGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL----LGKPQQQ 360
|
....*..
gi 51467917 400 NRKPKVW 406
Cdd:cd16145 361 QHDYLYW 367
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
42-393 |
4.55e-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: 4.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDVelGSLQVMN----KT---RKIMEDGgTSFTNaFVTTPMCCPSRSSMLTGKYVHN---HNTYTNNENC 111
Cdd:cd16146 1 PNVILILTDDQGY--GDLGFHGnpilKTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRtgvWHTILGRERM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 112 SSpswqaqhEPRSFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWVGL-----------IKNSRFYNyTVCRNGNK 178
Cdd:cd16146 77 RL-------DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdyWGNDYFDD-TYYHNGKF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 179 EKHgadyaKDYFTDLITNDSINYFRTSKrmfpHRPVMMVISHAAPHGPEDSAPQYSELFPNASQHITPSYNYApnMdkhw 258
Cdd:cd16146 149 VKT-----EGYCTDVFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG--M---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 259 imqytgpmkpihmeFTNylhrkrlqtlmsVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIG-----QFGLVKGKSMPY 333
Cdd:cd16146 214 --------------IEN------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVY 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51467917 334 DFDIRVPFFVRGPNVEPGARNNHVVL-NIDLAPTILDIAGLDTP--PDMDGKSILKLLEQEKT 393
Cdd:cd16146 268 EGGHRVPFFIRWPGKILAGKDVDTLTaHIDLLPTLLDLCGVKLPegIKLDGRSLLPLLKGESD 330
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-396 |
1.56e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 145.45 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQ--DVeLGSL-QVMNKTRKI--MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNenCSSPS 115
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 116 wqaqhEPRSFAVYLNNTGYRTAFFGKylneyngsyippgwreWvgliknsrfynytvcrngnkekHGADYAKDYFTDLit 195
Cdd:cd16152 78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 196 ndSINYFRTSKRmfpHRPVMMVISHAAPH---------GPEDSAPQyselFPNasqhitpsyNYAP----NMDKHWIMQY 262
Cdd:cd16152 113 --AIDYLDNRQK---DKPFFLFLSYLEPHhqndrdryvAPEGSAER----FAN---------FWVPpdlaALPGDWAEEL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 263 TGpmkpihmeftnYL---HRkrlqtlmsVDDSVEKVYNALVDTGELDNTYIIYTADHGYHigqFGLVKG--KSMPYDFDI 337
Cdd:cd16152 175 PD-----------YLgccER--------LDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHESSI 232
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 51467917 338 RVPFFVRGPNVEPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEKTGNR 396
Cdd:cd16152 233 RVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWR 291
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
41-389 |
1.17e-36 |
|
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: 144.25 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQDVELGSL--QVMnKTRKImeD----GGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNencssp 114
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYggHPA-KTPNI--DrlaaRGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQAQHEPR--SFAVYLNNTGYRTAFFGKYLNEYNGSYI--PPGWREWVGLIKNSRFYNYTVCRNGNKEKHG-------- 182
Cdd:cd16030 73 SYFRKVAPDavTLPQYFKENGYTTAGVGKIFHPGIPDGDddPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpawea 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 183 ADYAKDYFTD-LITNDSINYFRTSKRMfpHRPVMMVISHAAPHGPEdSAPQ-YSELFPNASQHITPS------------- 247
Cdd:cd16030 153 ADVPDEAYPDgKVADEAIEQLRKLKDS--DKPFFLAVGFYKPHLPF-VAPKkYFDLYPLESIPLPNPfdpidlpevawnd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 248 YNYAPNMDKHWIMQYTGPMKPIhmefTNYLHRKRLQT-LMSV---DDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQF 323
Cdd:cd16030 230 LDDLPKYGDIPALNPGDPKGPL----PDEQARELRQAyYASVsyvDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEH 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51467917 324 GLVkGKSMPYDFDIRVPFFVRGPNV-EPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLE 389
Cdd:cd16030 306 GHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLK 371
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-390 |
5.62e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 136.18 E-value: 5.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQ----DVELGSLQVMNKTRKIMEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYtnnENCSSPS-W 116
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 117 QAQHEPRSFAVYLNNTGYRTAFFGKY-LNEYNGSYippgwrewvgliknsrfynytvcrngnkekhgadYAKDyftDLIT 195
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 196 NDSINYFRTSKRMFPHR-PVMMVISHAAPHgpeDSapqyseLFPnasqhitpsynyaPNMDKHWImqytgpmkpihmEFT 274
Cdd:cd16035 121 AQAVEWLRERGAKNADGkPWFLVVSLVNPH---DI------MFP-------------PDDEERWR------------RFR 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 275 NY---LHRKrlqtlmsVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFVRGPNVEPG 351
Cdd:cd16035 167 NFyynLIRD-------VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGT 239
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 51467917 352 ARN-NHVVLNIDLAPTILDIAGLDTP------PDMDGKSILKLLEQ 390
Cdd:cd16035 240 GQTtDALTSHIDLLPTLLGLAGVDAEarateaPPLPGRDLSPLLTD 285
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-386 |
7.37e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 134.60 E-value: 7.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTD----DQdvelgsLQVMNKTRKIM------EDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYtnnenc 111
Cdd:cd16148 1 MNVILIVIDslraDH------LGCYGYDRVTTpnldrlAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 112 sspSWQAQHEPRSFAVYLNNTGYRTAFFGkylneyNGSYIPPGWrewvGLiknSRFYNYTVCRNGNKEKHGADyaKDYFT 191
Cdd:cd16148 69 ---GGPLEPDDPTLAEILRKAGYYTAAVS------SNPHLFGGP----GF---DRGFDTFEDFRGQEGDPGEE--GDERA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 192 DLITNDSINYFrtsKRMFPHRPVMMVISHAAPHGPedsapqyselfpnasqhitpsYNYApNMdkhwimqytgpmkpIHM 271
Cdd:cd16148 131 ERVTDRALEWL---DRNADDDPFFLFLHYFDPHEP---------------------YLYD-AE--------------VRY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 272 eftnylhrkrlqtlmsVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVKGKSMP-YDFDIRVPFFVRGPNVEP 350
Cdd:cd16148 172 ----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEP 235
|
330 340 350
....*....|....*....|....*....|....*.
gi 51467917 351 GARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILK 386
Cdd:cd16148 236 GKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
41-392 |
8.25e-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: 135.00 E-value: 8.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQ---DVE-LGSlqVMNKTRKI--MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNencsSP 114
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGS--PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVV----GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQAQHEPRS---FAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWVGL----------IKNSRFYNYTVCRNGNKE 179
Cdd:cd16026 75 PGSKGGLPPDeitIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIpysndmwpfpLYRNDPPGPLPPLMENEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 180 KHGADYAKDYFTDLITNDSINYFRTSKrmfpHRPVMMVISHAAPHGPEDSapqySELFPNASQHitpsynyapnmdkhwi 259
Cdd:cd16026 155 VIEQPADQSSLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVPLFA----SEKFKGRSGA---------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 260 mqytGPMKpihmeftnylhrkrlQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHG--YHIGQFG-----LVKGKSMP 332
Cdd:cd16026 211 ----GLYG---------------DVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGGKGTT 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51467917 333 YDFDIRVPFFVRGPN-VEPGARNNHVVLNIDLAPTILDIAGLDTPPD--MDGKSILKLLEQEK 392
Cdd:cd16026 272 WEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLLLGGS 334
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
42-393 |
1.05e-31 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 128.86 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDqdVELGSLQVMNKTRKI-------MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYvhNHNTYTNNENCSSP 114
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY--PWRSRLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQAQHEPR-SFAVYLNNTGYRTAFFGKY---LNEY--NGSYIPPGWREWVgliknsrfyNYTV-CRNGNKEkHGADYak 187
Cdd:cd16143 77 SPPLIEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKDV---------DYSKpIKGGPLD-HGFDY-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 188 dYFT-------DLITNDSINYFRTSKRmfPHRPVMMVISHAAPHGPedsapqyselfpnasqhITPS--YNYAPNMDKH- 257
Cdd:cd16143 145 -YFGipasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGPYg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 258 -WIMQytgpmkpihmeftnylhrkrlqtlmsVDDSVEKVYNALVDTGELDNTYIIYTADHG---YHIGQFGLVKGKSMPY 333
Cdd:cd16143 205 dFVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGHDPSG 258
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51467917 334 DF-----DI-----RVPFFVRGPN-VEPGARNNHVVLNIDLAPTILDIAGLDTPPD--MDGKSILKLLEQEKT 393
Cdd:cd16143 259 PLrgmkaDIyegghRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPALLGPKK 331
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-392 |
1.59e-31 |
|
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: 127.72 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDVE-LGSL-QVMNKTRKI--MEDGGTSFTNAFvTTPMCCPSRSSMLTGKYvhNHNTYTNNencsSPSWQ 117
Cdd:cd16151 1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKY--NFRNYVVF----GYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 118 AQHeprSFAVYLNNTGYRTAFFGK---YLNEYNGSYIPP-GWREWV-------GLIKNSRFYNYTVCRNGNKEKHGADya 186
Cdd:cd16151 74 KQK---TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLETTEG-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 187 kDYFTDLITNDSINYFRTSKR--MFPHRPvmMVISHaAPHGPedsapqyselFPNASQHITPSYNYAPNMDKHWIMQytg 264
Cdd:cd16151 149 -DYGPDLFADFLIDFIERNKDqpFFAYYP--MVLVH-DPFVP----------TPDSPDWDPDDKRKKDDPEYFPDMV--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 265 pmkpihmeftNYLhrkrlqtlmsvDDSVEKVYNALVDTGELDNTYIIYTADHGYHIG-----QFGLVKG-KSMPYDFDIR 338
Cdd:cd16151 212 ----------AYM-----------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTDAGTH 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 51467917 339 VPFFVRGP-NVEPGARNNHVVLNIDLAPTILDIAGLDTPPD--MDGKSILKLLEQEK 392
Cdd:cd16151 271 VPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQLLGKT 327
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
42-391 |
2.24e-31 |
|
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: 129.04 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQD---VELGSLQVMnKTRKI--MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNnenCSSPSW 116
Cdd:cd16156 1 KQFIFIMTDTQRwdmVGCYGNKAM-KTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN---CMALGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 117 QAQHEPRsfavYLNNTGYRTAFFGKY-LN--EYNGSYI-PPGWREwvgliknSRFY---NY---------TVCRNGNKEK 180
Cdd:cd16156 77 NVKTIGQ----RLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDP-------DYWYdmrNYldelteeerRKSRRGLTSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 181 HGADYAKDY-FTDLITNDSINYFRTSKrmfpHRPVMMVISHAAPHGPEDSAPQYSELFPNASQHITPSYN----YAPNMD 255
Cdd:cd16156 146 EAEGIKEEFtYGHRCTNRALDFIEKHK----DEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAYddleNKPLHQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 256 KHWIMQYTGPMKPihmEFTnYLHRKRLQTLMSVDDSVEKVYNALvdTGELDNTYIIYTADHGYHIGQFGL-VKGKSMpYD 334
Cdd:cd16156 222 RLWAGAKPHEDGD---KGT-IKHPLYFGCNSFVDYEIGRVLDAA--DEIAEDAWVIYTSDHGDMLGAHKLwAKGPAV-YD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 51467917 335 FDIRVPFFVRGPN-VEPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQE 391
Cdd:cd16156 295 EITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDP 352
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
73-408 |
3.44e-31 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 128.15 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 73 GTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNnencSSPswQAQHEPrSFAVYLNNTGYRTAFFGK----------- 141
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARHL-TLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 142 YLNEYNGSY--IPPGWREWVglikNSRFYnytvcrngnKEKHgADYAkdYFTDlitnDSINYFRTSKRmfphRPVMMVIS 219
Cdd:cd16028 109 PLDPRLLSYelAMPGFDPVD----RLDEY---------PAED-SDTA--FLTD----RAIEYLDERQD----EPWFLHLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 220 HAAPHGPE-DSAPqYSELFPNASqhiTPSYNYAPNMD---------KHWIMQYtgPMKPIHMEFTNY-----LHRKRLQT 284
Cdd:cd16028 165 YIRPHPPFvAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 285 ----LMS-VDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFVRGPNVEPGARNNHVVL 359
Cdd:cd16028 239 tylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREADATRGQVVD 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 51467917 360 N----IDLAPTILDIAGLDTPPDMDGKSILKLLEqektgnrfkpNRKPKVWRD 408
Cdd:cd16028 318 AftesVDVMPTILDWLGGEIPHQCDGRSLLPLLA----------GAQPSDWRD 360
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
42-389 |
9.03e-31 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 124.23 E-value: 9.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDdqdvELGS----------LQVMNKTRkiMEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNnenc 111
Cdd:cd16032 1 PNILLIMAD----QLTAaalpaygntvVKTPNLDR--LAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDN---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 112 sSPSWQAQhEPrSFAVYLNNTGYRTAFFGKYlneyngsyippgwrewvgliknsRFYnytvcrnGNKEKHGADYakDyft 191
Cdd:cd16032 71 -AAEFPAD-IP-TFAHYLRAAGYRTALSGKM-----------------------HFV-------GPDQLHGFDY--D--- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 192 DLITNDSINYFRTSKRMFPHRPVMMVISHAAPHGPEDSAPQYSELFPNASQHitpSYnYApnmdkhwIMQYtgpmkpihm 271
Cdd:cd16032 113 EEVAFKAVQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQEYWDLYVRRARR---AY-YG-------MVSY--------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 272 eftnylhrkrlqtlmsVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFVRGPNVEPG 351
Cdd:cd16032 173 ----------------VDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAP 235
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 51467917 352 ARNNHVVLNIDLAPTILDIAGLDTPPD---MDGKSILKLLE 389
Cdd:cd16032 236 RRVAEPVSLVDLLPTLVDLAGGGTAPHvppLDGRSLLPLLE 276
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
41-396 |
1.06e-30 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 127.48 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQDVE-LGSL---QVMNKTRKIMEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNENCSspsW 116
Cdd:PRK13759 6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 117 QAQHE-PRSFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWVGLiKNSRFYNYTVCRNGNKEKHGADYAKDY------ 189
Cdd:PRK13759 83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 190 --------FTDL-----------------------ITNDSINYFRtskRMFPHRPVMMVISHAAPHGPEDSAPQYSELFP 238
Cdd:PRK13759 150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 239 NASQHITPSYNYAPNMDKH-WIMQYTGPMKPIHMEftnYLHRKRLQTLMS---VDDSVEKVYNALVDTGELDNTYIIYTA 314
Cdd:PRK13759 227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEE---YARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 315 DHGYHIGQFGLVKgKSMPYDFDIRVPFFVRGP----NVEPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQ 390
Cdd:PRK13759 304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPggllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382
|
....*.
gi 51467917 391 EKTGNR 396
Cdd:PRK13759 383 QYEGWR 388
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
41-392 |
3.33e-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: 121.40 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDqdveLG-----------------SLQvmnktrkimeDGGTSFTNaFVTTPMCCPSRSSMLTGKYVH-NH 102
Cdd:cd16025 2 RPNILLILADD----LGfsdlgcfggeiptpnldALA----------AEGLRFTN-FHTTALCSPTRAALLTGRNHHqVG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 103 NTYTNNENCSSPSWQAQHEPRS--FAVYLNNTGYRTAFFGKylneyngsyippgwreWvgliknsrfynytvcrngnkek 180
Cdd:cd16025 67 MGTMAELATGKPGYEGYLPDSAatIAEVLKDAGYHTYMSGK----------------W---------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 181 H--GADYakdYFTDLITNDSINYFRTSKRmfPHRPVMMVISHAAPHGP-----EDSA---PQYSE--------------- 235
Cdd:cd16025 109 HlgPDDY---YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAPlqapkEWIDkykGKYDAgwdalreerlerqke 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 236 --LFPNASQhITPsynyAPNMDKHWimqytgpmkpihmeftNYL---HRKRLQTLMSV--------DDSVEKVYNALVDT 302
Cdd:cd16025 184 lgLIPADTK-LTP----RPPGVPAW----------------DSLspeEKKLEARRMEVyaamvehmDQQIGRLIDYLKEL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 303 GELDNTYIIYTADHG--YHIG--QFG---LVKGKSMPYDFDIRVPFFVRGPNV--EPGARNNHVVLNIDLAPTILDIAGL 373
Cdd:cd16025 243 GELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELAGV 322
|
410 420
....*....|....*....|....*..
gi 51467917 374 DTP--------PDMDGKSILKLLEQEK 392
Cdd:cd16025 323 EYPktvngvpqLPLDGVSLLPTLDGAA 349
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-386 |
8.08e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 114.39 E-value: 8.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQDVElgSLQVMNKTRKIMEDG----------------GTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNT 104
Cdd:cd16153 1 KPNILWIITDDQRVD--SLSCYNNAHTGKSESrlgyvespnidalaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 105 YtNNENcsspSWQA-QHEPRSFAVYLNNTGYRTAFFGKylneyngsyipPGWREWVGLIKNSrfyNYTVCRNGNKEKHGA 183
Cdd:cd16153 79 Y-GFEA----AHPAlDHGLPTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 184 DYAKDYFTdlitndSINYfrtskrMFPHRPVMMvishaaphgPEdsapQYSELFpnasqhitpsYNYApnmdkhwimqyt 263
Cdd:cd16153 140 DSDKPFFV------RLSF------LQPHTPVLP---------PK----EFRDRF----------DYYA------------ 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 264 gpmkpihmeFTNYlhrkrlqtlmsVDDSVEKVYNALVDTGEL---DNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVP 340
Cdd:cd16153 173 ---------FCAY-----------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVP 231
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 51467917 341 FFVRGPNVEP---GARNNHVVLNIDLAPTILDIAGLD--TPPDMDGKSILK 386
Cdd:cd16153 232 LIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRDLFE 282
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-385 |
1.15e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 113.10 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDV----ELGSLQVMNKTRKIMEDGGTSFTNAFVTTPMCCPSRSSMLTGKY-----VHNHNTYTNNENCS 112
Cdd:cd16149 1 PNILFILTDDQGPwalgCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgIHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 113 SPSWQAQHEPrSFAVYLNNTGYRTAFFGKylneyngsyippgwreWvgliknsrfynytvcrngnkekHGADYAKDYFTD 192
Cdd:cd16149 81 KPEGYLEGQT-TLPEVLQDAGYRCGLSGK----------------W----------------------HLGDDAADFLRR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 193 LITNDsinyfrtskrmfphRPVMMVISHAAPHGPedsapqyselfpnasqhitpsynyapnmdkhWimQYtgpmkpihme 272
Cdd:cd16149 122 RAEAE--------------KPFFLSVNYTAPHSP-------------------------------W--GY---------- 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 273 ftnylhrkrLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGlVKGK-------SMpYDFDIRVPFFVRG 345
Cdd:cd16149 145 ---------FAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVPFIIRW 213
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 51467917 346 PN-VEPGARNNHVVLNIDLAPTILDIAGLDTPPDMD--GKSIL 385
Cdd:cd16149 214 PGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
42-396 |
4.54e-27 |
|
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: 114.95 E-value: 4.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQ---DVEL-GSLQVmnKT---RKIMEDGgTSFTNAFVTtPMCCPSRSSMLTGKYVHNHNTYTNNENCSSP 114
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQI--KTpnlDALAADG-VILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQAQHEPrSFAVYLNNTGYRTAFFGKY-LNEYNGSYIPPG----------------WREWVGliknsRFYNYTVCRNGN 177
Cdd:cd16029 77 YGLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTNrgfdsfygyyggaedyYTHTSG-----GANDYGNDDLRD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 178 KEKHGADYAKDYFTDLITNDSINYFR---TSKRMFphrpvmMVISHAAPHGPEDSAPQYSELFPNASQHITpsynyapnm 254
Cdd:cd16029 151 NEEPAWDYNGTYSTDLFTDRAVDIIEnhdPSKPLF------LYLAFQAVHAPLQVPPEYADPYEDKFAHIK--------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 255 dkhwimqytgpmkpihmeftNYLHRKRLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFG------LVKG 328
Cdd:cd16029 216 --------------------DEDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGG 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51467917 329 KSMPYDFDIRVPFFVRGPNVEP--GARNN---HVVlniDLAPTILDIAGLDTP--PDMDGKSILKLLEQEKTGNR 396
Cdd:cd16029 276 KNTLWEGGVRVPAFVWSPLLPPkrGTVSDglmHVT---DWLPTLLSLAGGDPDdlPPLDGVDQWDALSGGAPSPR 347
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
41-388 |
7.64e-26 |
|
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: 112.14 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDqdVELGSLQVM-NKTRKI-----MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYtnNENCSSP 114
Cdd:cd16160 1 KPNIVLFFADD--MGYGDLASYgHPTQERgpiddMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRVFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQAQHEPRS---FAVYLNNTGYRTAFFGKY---LNEYN---GSYIPP--GWrEWVGliKNSRFYNYTVCRNGNKEKHGA 183
Cdd:cd16160 77 PWDIGGLPKTevtMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLPShhGF-DFVG--TNLPFTNSWACDDTGRHVDFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 184 DYAK----------------DYFTDLITNDSINYFRTSKrmfpHRPVMMVISHAAPHgpedsAPQY-SELFPNASQHitp 246
Cdd:cd16160 154 DRSAcflyyndtiveqpiqhEHLTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTH-----TPLFaSKRFKGKSKR--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 247 sYNYAPNMDKhwimqytgpmkpihmeftnylhrkrlqtlMSVddSVEKVYNALVDTGELDNTYIIYTADHGYHI------ 320
Cdd:cd16160 222 -GRYGDNINE-----------------------------MSW--AVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeycleg 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51467917 321 GQFGLVKG-KSMPYDFDIRVPFFVRGPNVEPGARNNHVVLNIDLAPTILDIAGLDTPPD--MDGKSILKLL 388
Cdd:cd16160 270 GSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDLL 340
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-392 |
1.01e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 111.56 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDVElgSLQVMN----KT---RKIMEDGgTSFTNAFVTTPMCCPSRSSMLTGKY--VHNHNTYTNnencs 112
Cdd:cd16150 1 PNIVIFVADQLRAD--SLGHLGnpaaVTpnlDALAAEG-VRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHH----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 113 spsWQAQHEPrSFAVYLNNTGYRTAFFGKylneyNGSYIPPGWREWVGLiknsrfynytvcrngnkekhgADYAkdyftd 192
Cdd:cd16150 73 ---LLRPDEP-NLLKTLKDAGYHVAWAGK-----NDDLPGEFAAEAYCD---------------------SDEA------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 193 lITNDSINYFRTSKrmfPHRPVMMVISHAAPHGP-EDSAPQYS--------ELFPNASQHITPSyNYAPNMDKHWIMQYT 263
Cdd:cd16150 117 -CVRTAIDWLRNRR---PDKPFCLYLPLIFPHPPyGVEEPWFSmidreklpPRRPPGLRAKGKP-SMLEGIEKQGLDRWS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 264 GpmkpihmEFTNYLHRKRLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLV-KGKSMPYDFDIRVPFF 342
Cdd:cd16150 192 E-------ERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLI 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 51467917 343 VRGPNVEPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEK 392
Cdd:cd16150 265 IKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAGET 314
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-397 |
6.18e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 105.12 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDVE------LGSLQVMNKTRKIMEDGGTSFTNAFVTtPMCCPSRSSMLTGKYVHNHNTYTNNENCSSPS 115
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 116 wqaqHE-PRSFAVYLNNTGYRTAFFGKYL--NEYNGSYIPPGWREWVGLIKN--SRFYNYTVCRNGNKEKHgadyaKDYF 190
Cdd:cd16154 80 ----ETlLQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-----TEYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 191 TDLITNDSINYFRTSkrmfpHRPVMMVISHAAPHGPedsapqyselFpnasqHITPSYNYAPNMdkhwimqyTGPMKPIH 270
Cdd:cd16154 151 TTKLTNLAIDWIDQQ-----TKPWFLWLAYNAPHTP----------F-----HLPPAELHSRSL--------LGDSADIE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 271 MEFTNYLhrkrLQTLMSVDDSVEKVYNALvDTGELDNTYIIYTADHGYHiGQ-----FGLVKGKSMPYDFDIRVPFFVRG 345
Cdd:cd16154 203 ANPRPYY----LAAIEAMDTEIGRLLASI-DEEERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVPLIVSG 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 51467917 346 PNVE-PGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEKTGNRF 397
Cdd:cd16154 277 AGVErANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQ 329
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
42-404 |
1.43e-22 |
|
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: 101.08 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDVELgSLQVMNKTRKI-----MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNENCSS--P 114
Cdd:cd16171 1 PNVVMVMSDSFDGRL-TFRPGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPnyP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQaqheprsfaVYLNNTGYRTAFFGKyLNEYNGSYIPPGWRE-WvgliknSRFYNYTVCRNGNKEkhgadyakdyfTDL 193
Cdd:cd16171 80 TWM---------DRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRPT-----------VNL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 194 ITNdsinyfRTSKRmfphrpVMMV---ISHAAPHGPEDSAPQYSELF--------PnasqHITPSYNYAPNMdkhwimqy 262
Cdd:cd16171 133 VGD------RSTVR------VMLKdwqNTDKAVHWIRKEAPNLTQPFalylglnlP----HPYPSPSMGENF-------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 263 tGPMKPIHMeftnYLHRKRLQTlmsvDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFF 342
Cdd:cd16171 189 -GSIRNIRA----FYYAMCAET----DAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLL 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51467917 343 VRGPNVEPGARNNHVVLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQekTGNRFKPNRKPK 404
Cdd:cd16171 259 IMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSE--SSIKESPSRVPH 318
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
42-378 |
3.89e-18 |
|
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: 87.59 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDV-ELGS----LQVMNKTRKI--MEDGGTSFTNAFVTtPMCCPSRSSMLTGKYVhnhntytNNENCSSP 114
Cdd:cd16142 1 PNILVILGDDIGWgDLGCygggIGRGAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTGLTTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQAQ-----HEPRSFAVYLNNTGYRTAFFGK-YLNEYNGSYipP---GWREWVGliknsrFYNYTVcrngnkEKHGADY 185
Cdd:cd16142 73 GLPGSpgglpPWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEEIVDK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 186 AKDYFTDLITND-----SINYFRTSKRMFPHrpvmmvishaaphgpedsaPQYselfpnasQHITPS-YNYApnmdkhwi 259
Cdd:cd16142 139 AIDFIKRNAKADkpfflYVNFTKMHFPTLPS-------------------PEF--------EGKSSGkGKYA-------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 260 mqytgpmkpihmeftnylhrkrlQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHG-----YHIGQFGLVKG-KSMPY 333
Cdd:cd16142 184 -----------------------DSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTW 240
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 51467917 334 DFDIRVPFFVRGPN-VEPGARNNHVVLNIDLAPTILDIAGLDTPPD 378
Cdd:cd16142 241 EGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
770-819 |
1.06e-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: 86.45 E-value: 1.06e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 51467917 770 CTSSNNNTYWCLRTVNETHNTLFCEFATGFLEYFDLNSDPYQLTNAVYTV 819
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
41-396 |
7.12e-17 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 84.83 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDQDV-ELGSLQVMNK-TRKI--MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNE---NCSS 113
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 114 PSWQAQHEPRS---FAVYLNNTGYRTAFFGKYLNEYNGSYIP--PGWREW-------VGLIKNSRFYNYTVCRNgnkEKH 181
Cdd:cd16157 81 PQNIVGGIPDSeilLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWfgapnchFGPYDNKAYPNIPVYRD---WEM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 182 GADYAKDYFTDLITNDS--INYFRT------SKRMFPHRPVMMVISHAAPHgpedsAPQY-SELFPNASQhitpsynyap 252
Cdd:cd16157 158 IGRYYEEFKIDKKTGESnlTQIYLQealefiEKQHDAQKPFFLYWAPDATH-----APVYaSKPFLGTSQ---------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 253 nmdkhwimqytgpmkpihmeftnylhRKRL-QTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHG---YHIGQFG---- 324
Cdd:cd16157 223 --------------------------RGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsng 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51467917 325 -LVKGKSMPYDFDIRVPFFVRGP-NVEPGARNNHVVLNIDLAPTILDIAGLDTPPD--MDGKSILKLLEQEKTGNR 396
Cdd:cd16157 277 pFLCGKQTTFEGGMREPAIAWWPgHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVLLNGKEKDR 352
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
41-431 |
1.87e-16 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 83.93 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMtddqdVElgSLQ--VMNKT----------RKIMEDGgTSFTNAFVTTPMCCPSRSSMLTGKY-VHNHNTYTN 107
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 108 NencsspswqAQHEPRSFAVYLNNTGYRTAFFgkylneYNGsyippgwrewvglikNSRFYNytvcRNGNKEKHGAD--Y 185
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 186 AKDYFTDLITN-----D------SINYFRTSKRmfphrPVMMVISHAAPHGPedsapqYSelFPNASQHITpsynyapnm 254
Cdd:COG1368 352 DREDFDDPFDGgwgvsDedlfdkALEELEKLKK-----PFFAFLITLSNHGP------YT--LPEEDKKIP--------- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 255 dkhwimqytgpmkpihmEFTNYLHRKRLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGyhigqfGLVKGKSmPYD 334
Cdd:COG1368 410 -----------------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 335 FDI---RVPFFVRGPNVEPGARNNHVVLNIDLAPTILDIAGLDTPPD-MDGKSIlklleqektgnrFKPNRKPKVWRDTF 410
Cdd:COG1368 466 NPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDL------------LSPDTDPFAFRNGG 533
|
410 420
....*....|....*....|.
gi 51467917 411 LVERGKILRKKEDSASSLNTQ 431
Cdd:COG1368 534 FITDDYVYVLKTGELTEEDKE 554
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
42-371 |
4.16e-16 |
|
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: 79.00 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDVELGSLQVMNKTR----KIMEDGGTSFtNAFVTTPMC--CPSRSSMLTGKYVHNHNTYTNNENCSSPS 115
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTtpnlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 116 WQAQHEP---RSFAVYLNNTGYRTAFFGkylneyngsyippgwrewvgliknsrfynytvcrngnkekhgadyAKDYFtd 192
Cdd:cd00016 80 SRAAGKDedgPTIPELLKQAGYRTGVIG---------------------------------------------LLKAI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 193 litndsinyfrtsKRMFPHRPVMMVISHAAPHGPEdsapqyselfpNASQHITPSYnyaPNMDKHWimqytgpmkpihme 272
Cdd:cd00016 113 -------------DETSKEKPFVLFLHFDGPDGPG-----------HAYGPNTPEY---YDAVEEI-------------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 273 ftnylhrkrlqtlmsvDDSVEKVYNALVDTGELDNTYIIYTADHG---YHIGQFGLVKGKSMPYDFDIRVPFFVRGPNVE 349
Cdd:cd00016 152 ----------------DERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVK 215
|
330 340
....*....|....*....|..
gi 51467917 350 PGARNNHVVLNIDLAPTILDIA 371
Cdd:cd00016 216 KGGVKHELISQYDIAPTLADLL 237
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
41-400 |
2.25e-15 |
|
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: 79.44 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDD---QDVELGSLQVMNKTRKI--MEDGGTSFTNAFVTTPMCCPSRSSMLTGKYvHNHNTYTNNENCSSPS 115
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRL-GLRNGVGHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 116 WQAQHEPrSFAVYLNNTGYRTAFFGKYLNEYNGSYIPpgwrewvglikNSRFYNYTVCRNGNKEKHGADYAKDYFTDLIT 195
Cdd:cd16161 80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYFGIPFSHDSSLADRYAQFATDFIQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 196 NDSinyfrTSKRmfphrPVMMVISHAAPHGPEDSAPqyseLFPNASQHITPsynyapnmdkhwimqyTGpmkpihmeftn 275
Cdd:cd16161 148 RAS-----AKDR-----PFFLYAALAHVHVPLANLP----RFQSPTSGRGP----------------YG----------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 276 ylhrkrlQTLMSVDDSVEKVYNALVDTGELDNTYIIYTAD---------------HGYHIGQFGLVKGKSMPYDFDIRVP 340
Cdd:cd16161 187 -------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHREP 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51467917 341 FFVRGPN-VEPGARNNHVVLNIDLAPTILDIAGLDTPPD--MDGKSILKLLEQE-KTGNR--FKPN 400
Cdd:cd16161 260 AIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVLFGGsKTGHRclFHPN 325
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
42-372 |
3.50e-15 |
|
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: 77.34 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIM-----TDDQDVELGSLQVMNKTRKIMEDGgTSFTNAFVTTPMCCPSRS--SMLTGkyvhnhnTYTNNENCSSP 114
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 115 SWQAQHEPRSFAVYLNNTGYRTAFFgkylneYNGsyippgwrewvglikNSRFYNytvcRNGNKEKHGAD--YAKDYFTD 192
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 193 LITNDSINY------FRTSKRMF---PHRPVMMVISHAAPHGPedsapqyselfpnasqhitpsYNYAPNMDKhwimqyt 263
Cdd:cd16015 128 DEKETNGWGvsdeslFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 264 gpmKPIHMEFTNYLHRKRLQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFdiRVPFFV 343
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*....
gi 51467917 344 RGPNVEPGARNNHVVLNIDLAPTILDIAG 372
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
41-393 |
1.70e-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: 77.71 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 41 RPNIILIMTDDqdveLG----------SLQVMNKTRKIMEdgGTSFTNAFVTTPMCCPSRSSMLTGKY------VHNHNt 104
Cdd:cd16159 1 KPNIVLFMADD----LGigdvgcfgndTIRTPNIDRLAKE--GVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 105 YTNNENCSSPSWQAQHEpRSFAVYLNNTGYRTAFFGKY----------------LN-----------------------E 145
Cdd:cd16159 74 MRVILFTASSGGLPPNE-TTFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 146 YNGSYIPP------------------------GWRE--------------WVGLIKNSRFYNYTVCRNGNKEKHGADYak 187
Cdd:cd16159 153 YDLSFDPLfplltafvlitaltiflllylgavSKRFfvfllilsllfislFFLLLITNRYFNCILMRNHEVVEQPMSL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 188 DYFTDLITNDSINYFRTSKRmfphRPVMMVISHAAPHGPEDSAPqyseLFPNASQHitpsYNYAPNmdkhwimqytgpmk 267
Cdd:cd16159 231 ENLTQRLTKEAISFLERNKE----RPFLLVMSFLHVHTALFTSK----KFKGRSKH----GRYGDN-------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 268 pihmeftnylhrkrlqtLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHI-----------GQFGLVKGKSMP-YDF 335
Cdd:cd16159 285 -----------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEG 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51467917 336 DIRVPFFVRGPNV-EPGARNNHVVLNIDLAPTILDIAGLDTPPD--MDGKSILKLLEQEKT 393
Cdd:cd16159 348 GIRVPTIVRWPGViPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTGQEK 408
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
42-393 |
5.42e-14 |
|
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: 75.94 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 42 PNIILIMTDDQDV-ELG-----SLQVMNKTRkiMEDGGTSFTNAFVTTPMCCPSRSSMLTGKYVHNHNTYTNNENCSSpS 115
Cdd:cd16158 2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 116 WQAQHEPRSFAVYLNNTGYRTAFFGKY---LNEyNGSYIPPgwrewvglikNSRFYNYtvcrngnkekHGADYAKDY--- 189
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT----------HQGFDHY----------LGIPYSHDQgpc 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 190 --FTDLITNDSInyFRTSKRMFPHRPVMM--VISHAAPHGPeDSAPQYSELfpnASQHIT-------PSYNYAPNMDKHW 258
Cdd:cd16158 138 qnLTCFPPNIPC--FGGCDQGEVPCPLFYneSIVQQPVDLL-TLEERYAKF---AKDFIAdnakegkPFFLYYASHHTHY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 259 iMQYTGpmkpihMEFTNYLHRKRL-QTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYHI------GQFGLVK-GKS 330
Cdd:cd16158 212 -PQFAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKG 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51467917 331 MPYDFDIRVPFFVRGPN-VEPGaRNNHVVLNIDLAPTILDIAGLDTPP-DMDGKSILKLL-EQEKT 393
Cdd:cd16158 285 TTYEGGVREPAIAYWPGrIKPG-VTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILfEQGKS 349
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
288-385 |
3.24e-08 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 57.43 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 288 VDDSVEKVYNALVdtgELDNTYIIyTADHG-----YHIGQFGLVKGKSMPydfdiRVPFFVRGPNVEPGARNNHVVLNId 362
Cdd:cd16010 412 VDECLGRIVEAVL---ENGGTLLI-TADHGnaeemIDPETGGPHTAHTTN-----PVPFIIVDPGLKRKLLKDGGLADV- 481
|
90 100
....*....|....*....|...
gi 51467917 363 lAPTILDIAGLDTPPDMDGKSIL 385
Cdd:cd16010 482 -APTILDLLGIEKPKEMTGKSLI 503
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
341-390 |
2.60e-07 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 54.52 E-value: 2.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 51467917 341 FFVRGPNVEPGARNNHVVLnIDLAPTILDIAGLDTPPDMDGKSILKLLEQ 390
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFAR 470
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
288-386 |
3.48e-07 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 54.34 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 288 VDDSVEKVYNALVdtgELDNTYIIyTADHG-------YHIGQfglvkgksmPY------DfdirVPFFVRGPnvePGARN 354
Cdd:PRK05434 417 VDECLGRVVDAVL---KVGGTLLI-TADHGnaeqmidPETGQ---------PHtahttnP----VPFILVGG---KALRL 476
|
90 100 110
....*....|....*....|....*....|..
gi 51467917 355 NHVVLNiDLAPTILDIAGLDTPPDMDGKSILK 386
Cdd:PRK05434 477 EGGKLA-DIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
282-377 |
3.66e-07 |
|
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: 54.14 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 282 LQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGYhigQFGLVKGKSMPY-----DFDIRVPFFVRGPNVEPGaRNNH 356
Cdd:COG3083 430 RNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGE---EFNENGQNYWGHnsnfsRYQLQVPLVIHWPGTPPQ-VISK 505
|
90 100
....*....|....*....|..
gi 51467917 357 VVLNIDLAPTIL-DIAGLDTPP 377
Cdd:COG3083 506 LTSHLDIVPTLMqRLLGVQNPA 527
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
66-372 |
7.20e-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: 48.74 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 66 RKIMEDGGTSF--TNAFVT-TpmcCPSRSSMLTGKYVHNH----NTY---TNNENCSSPSWQAQH-----EPrsFAVYLN 130
Cdd:cd16018 26 KRLAEEGVRAKyvKPVFPTlT---FPNHYSIVTGLYPESHgivgNYFydpKTNEEFSDSDWVWDPwwiggEP--IWVTAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 131 NTGYRTA-FFgkylneyngsyippgwreWVGLIKNSRFYNYTVCRNGNkekhgadYAKDYFTDLITNDSINYFRTSKRMF 209
Cdd:cd16018 101 KAGLKTAsYF------------------WPGSEVAIIGYNPTPIPLGG-------YWQPYNDSFPFEERVDTILEWLDLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 210 phRPVMMVISHAAPhgpeDSApqyselfpnasQHitpsyNYAPNmdkhwimqytgpmkpihmeftnylHRKRLQTLMSVD 289
Cdd:cd16018 156 --RPDLILLYFEEP----DSA-----------GH-----KYGPD------------------------SPEVNEALKRVD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 290 DSVEKVYNALVDTGELDNTYIIYTADHGY-----HiGQFglvkgksmPYDFDIRVPFFVRGPNVepgaRNNHVV---LNI 361
Cdd:cd16018 190 RRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAF----KKGKKLgpfRNV 256
|
330
....*....|.
gi 51467917 362 DLAPTILDIAG 372
Cdd:cd16018 257 DIYPLMCNLLG 267
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
288-386 |
1.21e-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: 49.28 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 288 VDDSVEKVYNALVDTGeldNTYIIyTADHGyhigqfglvKGKSMpYDFDI----------RVPFFVRGPNVEPGARNNHV 357
Cdd:COG0696 418 VDECLGRVVDAVLAAG---GTLLI-TADHG---------NAEQM-IDPDTggphtahttnPVPFILVGGDKGVKLREDGR 483
|
90 100
....*....|....*....|....*....
gi 51467917 358 VlnIDLAPTILDIAGLDTPPDMDGKSILK 386
Cdd:COG0696 484 L--ADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
288-400 |
8.28e-04 |
|
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: 43.10 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 288 VDDSVEKVYNALVDTGELDNTYIIYTADHGYHIGQF-GLVKGK---SMPYDFdIRVPFFVR--GP----NVEpgARNNHV 357
Cdd:pfam02995 313 LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLrRTSQGMleeRLPLMS-IRYPPWFRetYPqaveNLE--LNANRL 389
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 51467917 358 VLNIDLAPTILDIAGLDTPPDMDGKSILKLLEQEKTGNRFKPN 400
Cdd:pfam02995 390 TTPFDLHATLKDILHLGELSDKELQDRMKALDCPRGISLFLPI 432
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
289-374 |
1.81e-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: 41.45 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 289 DDSVEKVYNALVDTGEldNTYIIYTADHGYHIGQFGlVKGKSMPYDFD--IRVPFFV--------RGPNVEPGARNNHVV 358
Cdd:cd16017 196 DYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRANKDRPF 272
|
90
....*....|....*.
gi 51467917 359 LNIDLAPTILDIAGLD 374
Cdd:cd16017 273 SHDNLFHTLLGLLGIK 288
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
282-367 |
5.83e-03 |
|
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293744 Cd Length: 294 Bit Score: 39.88 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51467917 282 LQTLMSVDDSVEKVYNALVDTGELDNTYIIYTADHGyhIGQFGLVKGKSmpyDFDIRVPFF-----VRGPNVEPGARNN- 355
Cdd:cd16020 182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHG--MTDWGSHGDGS---PDETETPFIawgagIKHPTPGRGPSFSa 256
|
90 100
....*....|....*....|.
gi 51467917 356 ---------HVVLNIDLAPTI 367
Cdd:cd16020 257 nwgglrlprHDLDQADLAPLM 277
|
|
| |
