|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
1-322 |
3.67e-170 |
|
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: 496.69 E-value: 3.67e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 1 MNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQAMHEPRTFAVYLNNTGYRTAFF 78
Cdd:cd16147 22 MPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQNGLERSTLPVWLQEAGYRTAYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 79 GKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLITNESINYFKMSKRMypHRPVM 154
Cdd:cd16147 102 GKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVIANKALDFLRRAAAD--DKPFF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 155 MVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEFTNILQRKRLQTLMSVDDSVER 233
Cdd:cd16147 179 LVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAYIDELYRKRLRTLQSVDDLVER 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 234 LYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLD 313
Cdd:cd16147 258 LVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAP 337
|
....*....
gi 2319158891 314 TPPDVDGKS 322
Cdd:cd16147 338 PPSDMDGRS 346
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
12-352 |
1.67e-79 |
|
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: 262.46 E-value: 1.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcSSPSWQamhepRTFAVYLNNTGYRTAFFGKYLNEYNGSYIP 91
Cdd:cd16031 38 GVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFDASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 92 PGWREWLGLIKNSRFYNYTVCRNGIKEKHgfdyaKDYFTDLITNESINYFKmsKRMyPHRPVMMVISHAAPHGPEDSAPQ 171
Cdd:cd16031 112 PGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTDIITDKALDFLK--ERD-KDKPFCLSLSFKAPHRPFTPAPR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 172 FSKLYPNAsqHITPSYNYAPN-------------MDKHWIMQYtgpmlPIHMEFTniLQR--KR-LQTLMSVDDSVERLY 235
Cdd:cd16031 184 HRGLYEDV--TIPEPETFDDDdyagrpewareqrNRIRGVLDG-----RFDTPEK--YQRymKDyLRTVTGVDDNVGRIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 236 NMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDT 314
Cdd:cd16031 255 DYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPI 333
|
330 340 350
....*....|....*....|....*....|....*...
gi 2319158891 315 PPDVDGKSVLKLLDpekpgnrfrtNKKAKIWRDTFLVE 352
Cdd:cd16031 334 PEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
472-617 |
1.31e-69 |
|
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: 225.69 E-value: 1.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 472 KPRFVHTRQTRSLSVEFEGEIYDINLEEEEelQVLQPRNIAKRH--DEGHKGPRDLQASSGGnrgrMLADSSNAVGPPTT 549
Cdd:pfam12548 1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEEY--QPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPAS 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2319158891 550 VRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSK 617
Cdd:pfam12548 75 VKVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
12-352 |
5.31e-68 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 230.54 E-value: 5.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsSPSWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyip 91
Cdd:COG3119 59 GVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--YNGGLPPDEP-TLAELLKEAGYRTALFGKWHL-------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 92 pgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDLITNESINYfkMSKRMYPHRPVMMVISHAAPHGPEDSAPQ 171
Cdd:COG3119 128 ------------------------------------YLTDLLTDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 172 FSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmeftniLQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIY 251
Cdd:COG3119 170 YLDKYDG--KDIPLPPNLAPRDLTEEELRR--------------ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 252 TADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLdpe 330
Cdd:COG3119 234 TSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL--- 310
|
330 340
....*....|....*....|..
gi 2319158891 331 kpgnrfrTNKKAKiWRDTFLVE 352
Cdd:COG3119 311 -------TGEKAE-WRDYLYWE 324
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-338 |
8.08e-50 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 180.46 E-value: 8.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTnneNCSSPSwqamHEPRTFAVYLNNTGYRTAFFGK--------YLN 83
Cdd:cd16034 37 GVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG---NDVPLP----PDAPTIADVLKDAGYRTGYIGKwhldgperNDG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 84 EYNGSYIPP----GWREWLGLIKNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLItnesINYfkMSKRMYPHRPVMMVISH 159
Cdd:cd16034 110 RADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIYIKGYSPDAETDLA----IEY--LENQADKDKPFALVLSW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 160 AAPHGPEDSAPQ-FSKLYPNASQHITPsyNYAPNMD-----KHWIMQYtgpmlpihmeFTNILqrkrlqtlmSVDDSVER 233
Cdd:cd16034 184 NPPHDPYTTAPEeYLDMYDPKKLLLRP--NVPEDKKeeaglREDLRGY----------YAMIT---------ALDDNIGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 234 LYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGL 312
Cdd:cd16034 243 LLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPYEESIRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGL 321
|
330 340
....*....|....*....|....*.
gi 2319158891 313 DTPPDVDGKSVLKLLDPEKPGNRFRT 338
Cdd:cd16034 322 PIPDTVEGRDLSPLLLGGKDDEPDSV 347
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
12-322 |
1.44e-47 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 168.77 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsspSWQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyip 91
Cdd:cd16022 36 GVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN----GGGLPPDEPTLAELLKEAGYRTALIGK----------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 92 pgwreWlgliknsrfynytvcrngikekHgfdyakdyftdlitNESINYFKmskRMYPHRPVMMVISHAAPHGPedsapq 171
Cdd:cd16022 101 -----W----------------------H--------------DEAIDFIE---RRDKDKPFFLYVSFNAPHPP------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 172 fsklypnasqhitpsYNYAPNMDkhwimqytgpmlpihmeftnilqrkrlqtlmSVDDSVERLYNMLVETGELENTYIIY 251
Cdd:cd16022 131 ---------------FAYYAMVS-------------------------------AIDDQIGRILDALEELGLLDNTLIVF 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2319158891 252 TADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKS 322
Cdd:cd16022 165 TSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
12-335 |
3.11e-44 |
|
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: 163.83 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTN-NENCSSPSWQamhepRTFAVYLNNTGYRTAFFGKYlnEYNGSYI 90
Cdd:cd16027 35 GVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPDGV-----KTLPELLREAGYYTGLIGKT--HYNPDAV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 91 PPGWrewlgliknsrFYNYTVCRNGIKEKHGFDYAKDYFTDLITNE----SINYFkmskrmYPHRPVMMVISHAAPHGPE 166
Cdd:cd16027 108 FPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKKGQpfflWFGFH------DPHRPYPPGDGEEPGYDPE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 167 DsapqfsklypnasqhITPSYNYA--PNMDKHWIMQYTgpmlpihmeftnilqrkrlqTLMSVDDSVERLYNMLVETGEL 244
Cdd:cd16027 171 K---------------VKVPPYLPdtPEVREDLADYYD--------------------EIERLDQQVGEILDELEEDGLL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 245 ENTYIIYTADHGYhigqfGLVKGKSMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSV 323
Cdd:cd16027 216 DNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSF 290
|
330
....*....|..
gi 2319158891 324 LKLLDPEKPGNR 335
Cdd:cd16027 291 LPLLKGEKDPGR 302
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-352 |
9.96e-44 |
|
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: 163.55 E-value: 9.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyip 91
Cdd:cd16033 36 GVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRGLPPGVETFSEDLREAGYRNGYVGK----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 92 pgWRewlgliknsrfynytVCRNGIKEKHGFDY------AKDYFTDLITNESINYFKMSKRmyphrPVMMVISHAAPHGP 165
Cdd:cd16033 105 --WH---------------VGPEETPLDYGFDEylpvetTIEYFLADRAIEMLEELAADDK-----PFFLRVNFWGPHDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 166 EDSAPQFSKLYPNASqhITPSYNYAPNM-DKHWImQYTGPMLPIHMEFTNILQRKRLQ------TLMsvDDSVERLYNML 238
Cdd:cd16033 163 YIPPEPYLDMYDPED--IPLPESFADDFeDKPYI-YRRERKRWGVDTEDEEDWKEIIAhywgyiTLI--DDAIGRILDAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 239 VETGELENTYIIYTADHGYHIGQFGLV-KGKSMpYDFDIRVPFFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPP 316
Cdd:cd16033 238 EELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKWPgVIAAGQVVDEFVSLLDLAPTILDLAGVDVPP 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 2319158891 317 DVDGKSVLKLLDPEKPGNrfrtnkkakiWRDTFLVE 352
Cdd:cd16033 317 KVDGRSLLPLLRGEQPED----------WRDEVVTE 342
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-335 |
8.83e-43 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 161.17 E-value: 8.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYT----------NNENCSSPSWQAM-HEPRTFAVYLNNTGYRTAFFGK 80
Cdd:cd16144 36 GMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipgrrgppdNTKLIPPPSTTRLpLEEVTIAEALKDAGYATAHFGK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 81 Y-LNEYNGSYipP---GWREWLGLIKNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPVMMV 156
Cdd:cd16144 116 WhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPGKPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 157 ISHAAPHGPEDSAPQFSKLYpnasqhitpsYNYAPNMDKHWIMQYTGPMLpihmeftnilqrkrlqtlMSVDDSVERLYN 236
Cdd:cd16144 190 LSHYAVHTPIQARPELIEKY----------EKKKKGLRKGQKNPVYAAMI------------------ESLDESVGRILD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 237 MLVETGELENTYIIYTADHGYHIGQFGLV-------KGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILD 308
Cdd:cd16144 242 ALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGGKGSLYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLE 321
|
330 340 350
....*....|....*....|....*....|
gi 2319158891 309 IAGLDTPP--DVDGKSVLKLL-DPEKPGNR 335
Cdd:cd16144 322 LAGGPLPPpqHLDGVSLVPLLkGGEADLPR 351
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
8-312 |
2.06e-42 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 156.43 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 8 MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNG 87
Cdd:pfam00884 32 LAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 88 SYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLITNESINYfkmskRMYPHRPVMMVISHAAPHGP 165
Cdd:pfam00884 106 NQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALLDEALEF-----LDNNDKPFFLVLHTLGSHGP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 166 edsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftnilqRKRLQTLMSVDDSVERLYNMLVETGELE 245
Cdd:pfam00884 175 ----PYYPDRYPEKYATFKPSSCSEEQLL-----------------------NSYDNTLLYTDDAIGRVLDKLEENGLLD 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2319158891 246 NTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGPSVEP-GSIVPQIVLNIDLAPTILDIAGL 312
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAkGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-336 |
1.26e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 146.15 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpswqamhEPRTFAVYLNNTGYRTAFFGK--YLNEyngsy 89
Cdd:cd16037 36 GTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRGE----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 90 ippgwrewlgliknsrfynytvcrngiKEKHGFDYakdyfTDLITNESINYFKmsKRMYPHRPVMMVISHAAPHGPEDSA 169
Cdd:cd16037 104 ---------------------------DQRHGFRY-----DRDVTEAAVDWLR--EEAADDKPWFLFVGFVAPHFPLIAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 170 PQFSKLYpnasqhitpsynyapnmdkhwimqytgpmlpihmeftnilqRKRLQT----LMS-VDDSVERLYNMLVETGEL 244
Cdd:cd16037 150 QEFYDLY-----------------------------------------VRRARAayygLVEfLDENIGRVLDALEELGLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 245 ENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVL 324
Cdd:cd16037 189 DNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLL 267
|
330
....*....|..
gi 2319158891 325 KLLDPEKPGNRF 336
Cdd:cd16037 268 PLAEGPDDPDRV 279
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-335 |
1.42e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 135.82 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPSwqamhEPRTFAVYLNNTGYRTAFFGKylneyngsyip 91
Cdd:cd16152 37 GVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA-----DEKTLAHYFRDAGYETGYVGK----------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 92 pgwreWlgliknsrfynytvcrngikekHGFDYAKDYFTDLitneSINYfkMSKRMyPHRPVMMVISHAAPH-------- 163
Cdd:cd16152 99 -----W----------------------HLAGYRVDALTDF----AIDY--LDNRQ-KDKPFFLFLSYLEPHhqndrdry 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 164 -GPEDSAPQFSKLYP---------NASQHItPSYnyapnmdkhwimqytgpmlpihmeftnilqrkrLQTLMSVDDSVER 233
Cdd:cd16152 145 vAPEGSAERFANFWVppdlaalpgDWAEEL-PDY---------------------------------LGCCERLDENVGR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 234 LYNMLVETGELENTYIIYTADHGYHigqFGLVKG--KSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAG 311
Cdd:cd16152 191 IRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAG 267
|
330 340
....*....|....*....|....
gi 2319158891 312 LDTPPDVDGKSVLKLLDPEKPGNR 335
Cdd:cd16152 268 IDVPEEMQGRSLLPLVDGKVEDWR 291
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
10-328 |
8.31e-34 |
|
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: 132.70 E-value: 8.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 10 HGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPSWQamhePrTFAVYLNNTGYRTAFFGKYlneyngsy 89
Cdd:cd16032 34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPADI----P-TFAHYLRAAGYRTALSGKM-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 90 ippgwrewlgliknsRFYnytvcrnGIKEKHGFDY-------AKDYFTDLitnesinyfkmsKRMYPHRPVMMVISHAAP 162
Cdd:cd16032 99 ---------------HFV-------GPDQLHGFDYdeevafkAVQKLYDL------------ARGEDGRPFFLTVSFTHP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 163 HGPEDSAPQFSKLYPNASQHitpSYnYApnmdkhwIMQYtgpmlpihmeftnilqrkrlqtlmsVDDSVERLYNMLVETG 242
Cdd:cd16032 145 HDPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 243 ELENTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDV---D 319
Cdd:cd16032 189 LADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVpplD 267
|
....*....
gi 2319158891 320 GKSVLKLLD 328
Cdd:cd16032 268 GRSLLPLLE 276
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-335 |
9.74e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 133.46 E-value: 9.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPM----CCPSRSSMLTGKYVHNhnvYTNNENCSSPSwqamhEPRTFAVYLNNTGYRTAFFGKYLNEYng 87
Cdd:cd16155 38 GTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGKAAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 88 syippgwrewlgliknsrfynytvcrngikekhgfdyakdyftdliTNESINYFKmsKRMYPHRPVMMVISHAAPHGPED 167
Cdd:cd16155 108 ----------------------------------------------ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 168 SAPQFSKLYPnaSQHITPSYNYAPnmdKHwimQYTGPMLPIHMEFT--------NIlqRKRLQ----TLMSVDDSVERLY 235
Cdd:cd16155 140 APPEYLDMYP--PETIPLPENFLP---QH---PFDNGEGTVRDEQLapfprtpeAV--RQHLAeyyaMITHLDAQIGRIL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 236 NMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTP 315
Cdd:cd16155 210 DALEASGELDNTIIVFTSDHGLAVGSHGLM-GKQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIP 288
|
330 340
....*....|....*....|
gi 2319158891 316 PDVDGKSVLKLLDPEKPGNR 335
Cdd:cd16155 289 ESVEGKSLLPVIRGEKKAVR 308
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
12-349 |
1.44e-33 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 134.69 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNnencSSPswQAMHEPrTFAVYLNNTGYRTAFFGK----------- 80
Cdd:cd16028 36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARHL-TLALELRKAGYDPALFGYtdtspdprgla 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 81 YLNEYNGSY--IPPGWREwlgliknsrfynytVCR-NGIKEKHGfDYAkdYFTDlitnESINYFkmskRMYPHRPVMMVI 157
Cdd:cd16028 109 PLDPRLLSYelAMPGFDP--------------VDRlDEYPAEDS-DTA--FLTD----RAIEYL----DERQDEPWFLHL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 158 SHAAPHGP-EDSAPqFSKLYPNASqhiTPSYNYAPNMD---------KHWIMQYtgPMLPIHMEFTNI-----LQRKRLQ 222
Cdd:cd16028 164 SYIRPHPPfVAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 223 T----LMS-VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVE----PGSIV 293
Cdd:cd16028 238 AtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREadatRGQVV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2319158891 294 PQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNrfrtNKKAKIWRDTF 349
Cdd:cd16028 317 DAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSD----WRDAVHYEYDF 368
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
19-351 |
3.41e-33 |
|
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: 132.67 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 19 FVTTPMCCPSRSSMLTGKYVHNHNVYTnnencSSPSWQAMH-EPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWR 95
Cdd:cd16146 42 FHVSPVCAPTRAALLTGRYPFRTGVWH-----TILGRERMRlDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 96 EWLGL-----------IKNSRFYNyTVCRNGIKEKHgfdyaKDYFTDLITNESINYFKMSKrmypHRPVMMVISHAAPHG 164
Cdd:cd16146 117 EVLGHggggigqypdyWGNDYFDD-TYYHNGKFVKT-----EGYCTDVFFDEAIDFIEENK----DKPFFAYLATNAPHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 165 PEDSAPQFSKLYPNASQHITPSYNYApnmdkhwimqytgpMLpihmefTNIlqrkrlqtlmsvDDSVERLYNMLVETGEL 244
Cdd:cd16146 187 PLQVPDKYLDPYKDMGLDDKLAAFYG--------------MI------ENI------------DDNVGRLLAKLKELGLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 245 ENTYIIYTADHGYHIG-----QFGLVKGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPDV 318
Cdd:cd16146 235 ENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEGGHRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPEGI 314
|
330 340 350
....*....|....*....|....*....|....*
gi 2319158891 319 --DGKSVLKLLdpekpgnrfrTNKKAKiWRDTFLV 351
Cdd:cd16146 315 klDGRSLLPLL----------KGESDP-WPERTLF 338
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
12-335 |
4.17e-33 |
|
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: 133.08 E-value: 4.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNencsSPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYI- 90
Cdd:cd16030 37 GVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN----SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 91 -PPGWREWLGLIKNSRFYNYTVCRNGIKEKHG--------FDYAKDYFTD-LITNESINYFKMSKRMypHRPVMMVISHA 160
Cdd:cd16030 113 dPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpaweaADVPDEAYPDgKVADEAIEQLRKLKDS--DKPFFLAVGFY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 161 APHGPEdSAPQ-FSKLYPNASQHITPSYN------YAPNmDKHWIMQYTGPMLPIHMEFTNIL----QRKRLQT-LMSV- 227
Cdd:cd16030 191 KPHLPF-VAPKkYFDLYPLESIPLPNPFDpidlpeVAWN-DLDDLPKYGDIPALNPGDPKGPLpdeqARELRQAyYASVs 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 228 --DDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAP 304
Cdd:cd16030 269 yvDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYP 347
|
330 340 350
....*....|....*....|....*....|..
gi 2319158891 305 TILDIAGLDTPPDVDGKSVLKLL-DPEKPGNR 335
Cdd:cd16030 348 TLAELAGLPAPPCLEGKSLVPLLkNPSAKWKD 379
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-325 |
5.10e-33 |
|
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: 128.43 E-value: 5.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVytnnencsspsWQAMHEPR--TFAVYLNNTGYRTAFFGkylneyNGSY 89
Cdd:cd16148 36 GVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV-----------WGGPLEPDdpTLAEILRKAGYYTAAVS------SNPH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 90 IPPGWREWLGliknsrfYNYTVCRNGIKEKHGFDyaKDYFTDLITNESINYFKmskRMYPHRPVMMVISHAAPHGPEdsa 169
Cdd:cd16148 99 LFGGPGFDRG-------FDTFEDFRGQEGDPGEE--GDERAERVTDRALEWLD---RNADDDPFFLFLHYFDPHEPY--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 170 pqfskLYPNAsqhitpsynyapnmdkhwimqytgpmlpIHMeftnilqrkrlqtlmsVDDSVERLYNMLVETGELENTYI 249
Cdd:cd16148 164 -----LYDAE----------------------------VRY----------------VDEQIGRLLDKLKELGLLEDTLV 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2319158891 250 IYTADHGYHIGQFGLVKGKSMP-YDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLK 325
Cdd:cd16148 195 IVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-327 |
1.01e-32 |
|
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: 131.56 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAmhEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYI 90
Cdd:cd16145 36 GMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLPP--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 91 PP--GWREWLG--------------LIKNSR--FYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKRmyphRP 152
Cdd:cd16145 114 PTkqGFDYFYGyldqvhahnyypeyLWRNGEkvPLPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENKD----KP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 153 VMMVISHAAPHGPEDsAPQFSklyPNASQHITPSYNYAPNMDKhwimqytgpmlpihmeftnilQRKRLQTLMS-VDDSV 231
Cdd:cd16145 190 FFLYLAYTLPHAPLQ-VPDDG---PYKYKPKDPGIYAYLPWPQ---------------------PEKAYAAMVTrLDRDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 232 ERLYNMLVETGELENTYIIYTADHGYHI-------GQF-----GLVKGK-SMpYDFDIRVPFFIRGPS-VEPGSIVPQIV 297
Cdd:cd16145 245 GRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngPLRGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPS 323
|
330 340 350
....*....|....*....|....*....|
gi 2319158891 298 LNIDLAPTILDIAGLDTPPDVDGKSVLKLL 327
Cdd:cd16145 324 AFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
12-335 |
3.82e-29 |
|
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: 121.72 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSwqamhepRTFAVYLNNTGYRTAFFGKY-LN--EYNGS 88
Cdd:cd16156 36 GVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNV-------KTIGQRLSDNGIHTAYIGKWhLDggDYFGN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 89 YI-PPGWRE--WLGL-----------IKNSRFYNYTVCRNGIKEKhgFDYAKDyftdlITNESINYFkmskRMYPHRPVM 154
Cdd:cd16156 109 GIcPQGWDPdyWYDMrnyldelteeeRRKSRRGLTSLEAEGIKEE--FTYGHR-----CTNRALDFI----EKHKDEDFF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 155 MVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNyaPNMDKHWIMQ--YTGPMLPIHMEFTNILQRKRLQTLMSVDDSVE 232
Cdd:cd16156 178 LVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAY--DDLENKPLHQrlWAGAKPHEDGDKGTIKHPLYFGCNSFVDYEIG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 233 RLYNMLVETgeLENTYIIYTADHGYHIGQFGL-VKGKSMpYDFDIRVPFFIRGPSVEPGSIVPQI-VLNIDLAPTILDIA 310
Cdd:cd16156 256 RVLDAADEI--AEDAWVIYTSDHGDMLGAHKLwAKGPAV-YDEITNIPLIIRGKGGEKAGTVTDTpVSHIDLAPTILDYA 332
|
330 340
....*....|....*....|....*.
gi 2319158891 311 GLDTPPDVDGKSVLKLL-DPEKPGNR 335
Cdd:cd16156 333 GIPQPKVLEGESILATIeDPEIPENR 358
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
11-336 |
4.38e-27 |
|
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: 114.58 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 11 GGATFINAFVTTPMCCPSRSSMLTGKY-----VHNHNVYTNNENCSSPSwqamhEPrTFAVYLNNTGYRTAFFGKYLNEY 85
Cdd:cd16026 36 EGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSKGGLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 86 NGSYIPP--GWREWLGL----------IKNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKrmypHRPV 153
Cdd:cd16026 110 QPEFLPTrhGFDEYFGIpysndmwpfpLYRNDPPGPLPPLMENEEVIEQPADQSSLTQRYTDEAVDFIERNK----DQPF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 154 MMVISHAAPHGPedsapqfskLYPNasqhitpsynyapnmdkhwimqytgpmlpihMEFTNILQRKRL-QTLMSVDDSVE 232
Cdd:cd16026 186 FLYLAHTMPHVP---------LFAS-------------------------------EKFKGRSGAGLYgDVVEELDWSVG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 233 RLYNMLVETGELENTYIIYTADHG--YHIGQFG-----LVKGKSMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAP 304
Cdd:cd16026 226 RILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGGKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLP 305
|
330 340 350
....*....|....*....|....*....|....*.
gi 2319158891 305 TILDIAGLDTPPDV--DGKSVLKLL--DPEKPGNRF 336
Cdd:cd16026 306 TLAALAGAPLPEDRviDGKDISPLLlgGSKSPPHPF 341
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
1-335 |
2.14e-26 |
|
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: 112.29 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 1 MNKTRKI-------MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWqaMHEPR-TFAVYLNNTG 72
Cdd:cd16143 19 YNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL--IEPDRvTLAKMLKQAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 73 YRTAFFGKY---LNEY--NGSYIPPGWRE---WLGLIKNSRFYnytvcrngikekHGFDYakdYFT-------DLITNES 137
Cdd:cd16143 97 YRTAMVGKWhlgLDWKkkDGKKAATGTGKdvdYSKPIKGGPLD------------HGFDY---YFGipasevlPTLTDKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 138 INYFKMSKRmyPHRPVMMVISHAAPHGPedsapqfsklypnasqhITPS--YNYAPNMDKH--WIMQytgpmlpihmeft 213
Cdd:cd16143 162 VEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGPYgdFVYE------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 214 nilqrkrlqtlmsVDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFGLVKGKSMPYDF-----DI-----RVPF 280
Cdd:cd16143 210 -------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGHDPSGPLrgmkaDIyegghRVPF 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2319158891 281 FIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLK-LLDPEKPGNR 335
Cdd:cd16143 277 IVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPaLLGPKKQEVR 335
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
10-326 |
6.03e-26 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 111.00 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 10 HGGATFiNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSS-PSWQAMHEPR--TFAVYLNNTGYRTAFFGKYlneYN 86
Cdd:cd16025 35 AEGLRF-TNFHTTALCSPTRAALLTGRNHHQVGMGTMAELATGkPGYEGYLPDSaaTIAEVLKDAGYHTYMSGKW---HL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 87 GsyiPPGWrewlgliknsrfynytvcrngikekhgfdyakdYFTDLITNESINYFKMSKRmyPHRPVMMVISHAAPHGPe 166
Cdd:cd16025 111 G---PDDY---------------------------------YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 167 dsapqfsklypnasQHitpsynyAPnmdKHWIMQYTG---------------------------PMLPIHMEFT--NIL- 216
Cdd:cd16025 152 --------------LQ-------AP---KEWIDKYKGkydagwdalreerlerqkelglipadtKLTPRPPGVPawDSLs 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 217 --QRKRLQTLMSV--------DDSVERLYNMLVETGELENTYIIYTADHG--YHIG--QFG---LVKGKSMPYDFDIRVP 279
Cdd:cd16025 208 peEKKLEARRMEVyaamvehmDQQIGRLIDYLKELGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTP 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2319158891 280 FFIRGPSV--EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKL 326
Cdd:cd16025 288 LIVSWPKGikAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGVPQLPL 336
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-324 |
1.23e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 106.94 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNV-----YTNNENCSSP-SWQAMHEprTFAVYLNNTGYRTAFFGKylney 85
Cdd:cd16149 36 GVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTKKPeGYLEGQT--TLPEVLQDAGYRCGLSGK----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 86 ngsyippgwreW-LGliknsrfynytvcrngikekhgfDYAKDYFTDLITNEsinyfkmskrmyphRPVMMVISHAAPHG 164
Cdd:cd16149 109 -----------WhLG-----------------------DDAADFLRRRAEAE--------------KPFFLSVNYTAPHS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 165 PedsapqfsklypnasqhitpsynyapnmdkhWimQYtgpmlpihmeftnilqrkrLQTLMSVDDSVERLYNMLVETGEL 244
Cdd:cd16149 141 P-------------------------------W--GY-------------------FAAVTGVDRNVGRLLDELEELGLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 245 ENTYIIYTADHGYHIGQFGlVKGK-------SMpYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPP 316
Cdd:cd16149 169 ENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVPFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPA 246
|
330
....*....|
gi 2319158891 317 DVD--GKSVL 324
Cdd:cd16149 247 DPRlpGRSFA 256
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-313 |
1.33e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 108.06 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 5 RKIMEHGgATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtnnENCSSPS-WQAMHEPRTFAVYLNNTGYRTAFFGKY-L 82
Cdd:cd16035 30 ERLAANG-LSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqPLLSPDVPTLGHMLRAAGYYTAYKGKWhL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 83 NEYNGSYippgwrewlgliknsrfynytvcrngikekhgfdYAKDyftDLITNESINY-FKMSKRMYPHRPVMMVISHAA 161
Cdd:cd16035 106 SGAAGGG----------------------------------YKRD---PGIAAQAVEWlRERGAKNADGKPWFLVVSLVN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 162 PH----GPEDSapqfsklypnasqhitPSYNYAPNMdkhwimqYtgpmlpihmeftnilqrkrLQTLMSVDDSVERLYNM 237
Cdd:cd16035 149 PHdimfPPDDE----------------ERWRRFRNF-------Y-------------------YNLIRDVDRQIGRVLDA 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2319158891 238 LVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEP-GSIVPQIVLNIDLAPTILDIAGLD 313
Cdd:cd16035 187 LDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGtGQTTDALTSHIDLLPTLLGLAGVD 263
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
12-335 |
4.94e-25 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 109.76 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsWQAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYI 90
Cdd:PRK13759 42 GYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---WNYKNTlPQEFR----DAGYYTQCIGKM------HVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 91 PPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY--------------FTDL-----------------------I 133
Cdd:PRK13759 109 PQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlrekapgkdpdLTDIgwdcnswvarpwdleerlhptnwV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 134 TNESINYFKmskRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEF 212
Cdd:PRK13759 186 GSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEEY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 213 TNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----VE 288
Cdd:PRK13759 263 ARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGN 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2319158891 289 PGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 335
Cdd:PRK13759 342 RGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFGQYEGWR 388
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-335 |
1.06e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 104.62 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKY--VHNHNVYTNnencsspsWQAMHEPrTFAVYLNNTGYRTAFFGKylneyNGSY 89
Cdd:cd16150 36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHH--------LLRPDEP-NLLKTLKDAGYHVAWAGK-----NDDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 90 IPPGWREwlgliknsrfyNYTVCrngikekhgfDYAkdyftdlITNESINYFKmskRMYPHRPVMMVISHAAPHGP-EDS 168
Cdd:cd16150 102 PGEFAAE-----------AYCDS----------DEA-------CVRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 169 APQFSKLYPNASQHITPSynyapnmdKHWIMQYtgPMLPIHMEFTNiLQR---KRLQTL--------MSVDDSVERLYNM 237
Cdd:cd16150 151 EPWFSMIDREKLPPRRPP--------GLRAKGK--PSMLEGIEKQG-LDRwseERWRELratylgmvSRLDHQFGRLLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 238 LVETGELENTYIIYTADHGYHIGQFGLV-KGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPP 316
Cdd:cd16150 220 LKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSH 299
|
330 340
....*....|....*....|
gi 2319158891 317 DVDGKSVLKLL-DPEKPGNR 335
Cdd:cd16150 300 THFGRSLLPVLaGETEEHRD 319
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
21-323 |
1.35e-23 |
|
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: 103.78 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 21 TTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAMHEPrTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPPGwR---- 95
Cdd:cd16029 44 VQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTN-Rgfds 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 96 ---EWLGLI-----KNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKrmyPHRPVMMVISHAAPHGPED 167
Cdd:cd16029 122 fygYYGGAEdyythTSGGANDYGNDDLRDNEEPAWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 168 SAPQFSKLYPNASQHITPsynyapnmdkhwimqytgpmlpihmeftniLQRKRLQTLMS-VDDSVERLYNMLVETGELEN 246
Cdd:cd16029 199 VPPEYADPYEDKFAHIKD------------------------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 247 TYIIYTADHGYHIGQFG------LVKGKSMPYDFDIRVPFFIRGPSVEP--GSIVPQIVLNIDLAPTILDIAGLDTP--P 316
Cdd:cd16029 249 TLIVFTSDNGGPTGGGDggsnypLRGGKNTLWEGGVRVPAFVWSPLLPPkrGTVSDGLMHVTDWLPTLLSLAGGDPDdlP 328
|
....*..
gi 2319158891 317 DVDGKSV 323
Cdd:cd16029 329 PLDGVDQ 335
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
11-327 |
9.15e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 101.14 E-value: 9.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 11 GGATFINAFvTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPswqamheprTFAVYLNNTGYRTAFFGK---YLNEYNG 87
Cdd:cd16151 35 EGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK---------TFGHLLKDAGYATAIAGKwqlGGGRGDG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 88 SYIPP-GWREWL-------GLIKNSRFYNYTVCRNGIKEKhgfDYAKDYFTDLITNESINYFKMSKR-----MYPhrpvm 154
Cdd:cd16151 105 DYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTEGDYGPDLFADFLIDFIERNKDqpffaYYP----- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 155 MVIshaaPHGPEDSAPQFSKLYPnasqhitPSYNYAPNMDKHWIM-QYTgpmlpihmeftnilqrkrlqtlmsvDDSVER 233
Cdd:cd16151 177 MVL----VHDPFVPTPDSPDWDP-------DDKRKKDDPEYFPDMvAYM-------------------------DKLVGK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 234 LYNMLVETGELENTYIIYTADHGYHIG-----QFGLVKG-KSMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTI 306
Cdd:cd16151 221 LVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTDAGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTL 300
|
330 340
....*....|....*....|...
gi 2319158891 307 LDIAGLDTPPD--VDGKSVLKLL 327
Cdd:cd16151 301 AELAGAPLPEDypLDGRSFAPQL 323
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-325 |
2.92e-20 |
|
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: 91.67 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtNNENcsspSWQAMHE-PRTFAVYLNNTGYRTAFFGKylneyngsyi 90
Cdd:cd16153 47 GVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY-GFEA----AHPALDHgLPTFPEVLKKAGYQTASFGK---------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 91 pPGWREWLGLIKNSrfyNYTVCRNGIKEKHGFDYAKdyftdlitnesinyfkmskrmyphrPVMMVISHAAPHGPedsap 170
Cdd:cd16153 112 -SHLEAFQRYLKNA---NQSYKSFWGKIAKGADSDK-------------------------PFFVRLSFLQPHTP----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 171 qfsklypnasqhITPSYNYAPNMDKHWIMQYtgpmlpihmeftnilqrkrlqtlmsVDDSVERLYNMLVETGEL---ENT 247
Cdd:cd16153 158 ------------VLPPKEFRDRFDYYAFCAY-------------------------GDAQVGRAVEAFKAYSLKqdrDYT 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 248 YIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVEP---GSIVPQIVLNIDLAPTILDIAGLD--TPPDVDGKS 322
Cdd:cd16153 201 IVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVPLIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRD 279
|
...
gi 2319158891 323 VLK 325
Cdd:cd16153 280 LFE 282
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
12-332 |
1.39e-19 |
|
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: 92.49 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtnNENCSSPSWQAMHEPR---TFAVYLNNTGYRTAFFGKY---LNEY 85
Cdd:cd16160 37 GIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRVFLPWDIGGLPKtevTMAEALKEAGYTTGMVGKWhlgINEN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 86 N---GSYIPpgwrewlgliknsrfynytvcrngikEKHGFDYA---------------------KD------YFTDLITN 135
Cdd:cd16160 115 NhsdGAHLP--------------------------SHHGFDFVgtnlpftnswacddtgrhvdfPDrsacflYYNDTIVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 136 ESINYFKMSKRMYP----------HRPVMMVISHAAPHGPEDSAPQFSklypNASQHitpsYNYAPNMDKhwimqytgpm 205
Cdd:cd16160 169 QPIQHEHLTETLVGdaksfiednqENPFFLYFSFPQTHTPLFASKRFK----GKSKR----GRYGDNINE---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 206 lpihmeftnilqrkrlqtlMSVddSVERLYNMLVETGELENTYIIYTADHGYHI------GQFGLVKG-KSMPYDFDIRV 278
Cdd:cd16160 231 -------------------MSW--AVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeyclegGSTGGLKGgKGNSWEGGIRV 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2319158891 279 PFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLLDPEKP 332
Cdd:cd16160 290 PFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDLLLGEAD 345
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
706-755 |
1.25e-18 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 88.76 E-value: 1.25e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2319158891 706 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 755
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-338 |
4.31e-18 |
|
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: 87.02 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSwqamHE-PRTFAVYLNNTGYRTAFFGKYL--NEYNGS 88
Cdd:cd16154 38 GIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE----ETlLQLLIKDATTAGYSSAVIGKWHlgGNDNSP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 89 YIPPGWREWLGLIKN--SRFYNYTVCRNGIKEKHGfDYAKDYFTDL----ITNESINYFkmskrmyphrpvmMVISHAAP 162
Cdd:cd16154 113 NNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST-EYATTKLTNLaidwIDQQTKPWF-------------LWLAYNAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 163 HGPedsapqFsKLYPNA--SQHITPSYnyapnmdkhwimqytgpmlpihmefTNILQRKR---LQTLMSVDDSVERLYNM 237
Cdd:cd16154 179 HTP------F-HLPPAElhSRSLLGDS-------------------------ADIEANPRpyyLAAIEAMDTEIGRLLAS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 238 LVETgELENTYIIYTADHGYHiGQ-----FGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNI-DLAPTILDIAG 311
Cdd:cd16154 227 IDEE-ERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNAtDLYATIAELAG 304
|
330 340
....*....|....*....|....*..
gi 2319158891 312 LDTPPDVDGKSVLKLLDPEKPGNRFRT 338
Cdd:cd16154 305 VDAAEIHDSVSFKPLLSDVNASTRQYN 331
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
8-327 |
9.14e-17 |
|
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: 82.97 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 8 MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtNNENCSSPSWQamheprTFAVYLNNTGYRTAFFGKyLNEYNG 87
Cdd:cd16171 32 MKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNYP------TWMDRLEKHGYHTQKYGK-LDYTSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 88 SYIPPGWRE-WlgliknSRFYNYTVCRNGIKEkhgfdyakdyfTDLITNESinyfkmskrmypHRPVMMvishaaphgpe 166
Cdd:cd16171 104 HHSVSNRVEaW------TRDVPFLLRQEGRPT-----------VNLVGDRS------------TVRVML----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 167 dsapqfsKLYPNASQHITPSYNYAPNMDKHWIMqYTGPMLP-------IHMEFTNILQRKRLQTLM--SVDDSVERLYNM 237
Cdd:cd16171 144 -------KDWQNTDKAVHWIRKEAPNLTQPFAL-YLGLNLPhpypspsMGENFGSIRNIRAFYYAMcaETDAMLGEIISA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 238 LVETGELENTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPD 317
Cdd:cd16171 216 LKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294
|
330
....*....|
gi 2319158891 318 VDGKSVLKLL 327
Cdd:cd16171 295 LSGYSLLPLL 304
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
57-360 |
9.55e-17 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 84.32 E-value: 9.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 57 AMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--YAKDYFTDLIT 134
Cdd:COG1368 307 GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefYDREDFDDPFD 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 135 N-----------ESINYFKMSKRmyphrPVMMVISHAAPHGPedsapqfsklypnasqhitpsynYAPNMDKHWIMQYTG 203
Cdd:COG1368 362 GgwgvsdedlfdKALEELEKLKK-----PFFAFLITLSNHGP-----------------------YTLPEEDKKIPDYGK 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 204 PMLpihmeftnilqRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGyhigqfGLVKGKSmPYDFDI---RVPF 280
Cdd:COG1368 414 TTL-----------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLeryRVPL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 281 FIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVD-GKSvlkLLDPEKPGNRFR-----TNKKAKIWRDTFLVERG 354
Cdd:COG1368 476 LIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRD---LLSPDTDPFAFRnggfiTDDYVYVLKTGELTEED 552
|
....*.
gi 2319158891 355 KFLRKK 360
Cdd:COG1368 553 KELEEE 558
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
31-311 |
2.71e-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: 76.95 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 31 SMLTGkyvhnhnVYTNNENCSSPSWQAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNyt 110
Cdd:cd16015 57 EVLTG-------LPPLPLGSGSYTLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 111 vcRNGIKEKHGFD--YAKDYFTDLITNESINY------FKMSKRMY---PHRPVMMVISHAAPHGPedsapqfsklypna 179
Cdd:cd16015 107 --RDSVYPNLGFDefYDLEDFPDDEKETNGWGvsdeslFDQALEELeelKKKPFFIFLVTMSNHGP-------------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 180 sqhitpsYNYAPNMDKhwimqytgpmLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHI 259
Cdd:cd16015 171 -------YDLPEEKKD----------EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2319158891 260 GQFGLVKGKSMPYDFdiRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAG 311
Cdd:cd16015 234 GSDYDETDEDPLDLY--RTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
8-335 |
1.54e-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: 77.10 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 8 MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpSWQAMHEPRTFAVYLNNTGYRTAFFGKY---LNE 84
Cdd:cd16158 33 LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-RGGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 85 yNGSYIPP--GWREWLGL---------IKNSRFYNYTVCRNGIKEkhGFDYAKDYFTDLITNESINYFKMSKRM--YPHR 151
Cdd:cd16158 112 -NGTYLPThqGFDHYLGIpyshdqgpcQNLTCFPPNIPCFGGCDQ--GEVPCPLFYNESIVQQPVDLLTLEERYakFAKD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 152 pvmmVISHAAphgpEDSAPQFskLYpNASQHItpsynYAPnmdkhwimQYTGpmlpihMEFTNILQRKRL-QTLMSVDDS 230
Cdd:cd16158 189 ----FIADNA----KEGKPFF--LY-YASHHT-----HYP--------QFAG------QKFAGRSSRGPFgDALAELDGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 231 VERLYNMLVETGELENTYIIYTADHGYHI------GQFGLVK-GKSMPYDFDIRVPFFIRGPS-VEPGsIVPQIVLNIDL 302
Cdd:cd16158 239 VGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTYEGGVREPAIAYWPGrIKPG-VTHELASTLDI 317
|
330 340 350
....*....|....*....|....*....|....
gi 2319158891 303 APTILDIAGLDTPP-DVDGKSVLKLLDPEKPGNR 335
Cdd:cd16158 318 LPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPR 351
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-317 |
2.93e-14 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 75.26 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 12 GATFINAFVTtPMCCPSRSSMLTGKYVhnhnvytNNENCSSPSWQ-AMH----EPRTFAVYLNNTGYRTAFFGK-YLNEY 85
Cdd:cd16142 39 GLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTGLTTVGLPgSPGglppWEPTLAELLKDAGYATAQFGKwHLGDE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 86 NGSYipP---GWREWLGliknsrFYNYTVcrngikEKHGFDYAKDYFTDLITNE-----SINYFKMSKRMYPHrpvmmvi 157
Cdd:cd16142 111 DGRL--PtdhGFDEFYG------NLYHTI------DEEIVDKAIDFIKRNAKADkpfflYVNFTKMHFPTLPS------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 158 shaaphgpEDSAPQFSKLYPNASqhitpsynyapnmdkhwimqytgpmlpihmeftnilqrkrlqTLMSVDDSVERLYNM 237
Cdd:cd16142 170 --------PEFEGKSSGKGKYAD------------------------------------------SMVELDDHVGQILDA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 238 LVETGELENTYIIYTADHG-----YHIGQFGLVKG-KSMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIA 310
Cdd:cd16142 200 LDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALA 279
|
....*..
gi 2319158891 311 GLDTPPD 317
Cdd:cd16142 280 GAPDPKD 286
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
8-327 |
2.35e-13 |
|
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: 73.27 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 8 MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE---NCSSPSWQAMHEPRT---FAVYLNNTGYRTAFFGKY 81
Cdd:cd16157 33 MAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharNAYTPQNIVGGIPDSeilLPELLKKAGYRNKIVGKW 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 82 LNEYNGSYIP--PGWREWLG-------LIKNSRFYNYTVCRNgikEKHGFDYAKDYFTDLITNESiNYfkmsKRMYPHRP 152
Cdd:cd16157 113 HLGHRPQYHPlkHGFDEWFGapnchfgPYDNKAYPNIPVYRD---WEMIGRYYEEFKIDKKTGES-NL----TQIYLQEA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 153 VMMVISHAAPHgpedsAPQFSKLYPNASQhiTPSYNYAPnmdkhwimqytgpmlpihmeFTNILQRKRL-QTLMSVDDSV 231
Cdd:cd16157 185 LEFIEKQHDAQ-----KPFFLYWAPDATH--APVYASKP--------------------FLGTSQRGLYgDAVMELDSSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 232 ERLYNMLVETGELENTYIIYTADHG---YHIGQFG-----LVKGKSMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDL 302
Cdd:cd16157 238 GKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngpFLCGKQTTFEGGMREPAIAWWPGhIKPGQVSHQLGSLMDL 317
|
330 340
....*....|....*....|....*..
gi 2319158891 303 APTILDIAGLDTPPD--VDGKSVLKLL 327
Cdd:cd16157 318 FTTSLALAGLPIPSDraIDGIDLLPVL 344
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
22-327 |
8.16e-13 |
|
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: 71.55 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 22 TPMCCPSRSSMLTGKY------VHNHNVYTNNENCSS---PSWQAmheprTFAVYLNNTGYRTAFFGKY----------- 81
Cdd:cd16159 47 APLCTPSRAAFLTGRYpirsgmASSHGMRVILFTASSgglPPNET-----TFAEVLKQQGYSTALIGKWhlglhcesrnd 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 82 -----LN-----------------------EYNGSYIPP------------------------GWRE------------- 96
Cdd:cd16159 122 fchhpLNhgfdyfyglpltnlkdcgdgsngEYDLSFDPLfplltafvlitaltiflllylgavSKRFfvfllilsllfis 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 97 -WLGLIKNSRFYNYTVCRNG-IKEKhgfDYAKDYFTDLITNESINYFKMSKRmyphRPVMMVISHAAPHGPEDSAPQFSk 174
Cdd:cd16159 202 lFFLLLITNRYFNCILMRNHeVVEQ---PMSLENLTQRLTKEAISFLERNKE----RPFLLVMSFLHVHTALFTSKKFK- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 175 lypNASQHitpsYNYAPNmdkhwimqytgpmlpihmeftnilqrkrlqtLMSVDDSVERLYNMLVETGELENTYIIYTAD 254
Cdd:cd16159 274 ---GRSKH----GRYGDN-------------------------------VEEMDWSVGQILDALDELGLKDNTFVYFTSD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 255 HGYHI-----------GQFGLVKGKSMP-YDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VD 319
Cdd:cd16159 316 NGGHLeeisvggeyggGNGGIYGGKKMGgWEGGIRVPTIVRWPGViPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriID 395
|
....*...
gi 2319158891 320 GKSVLKLL 327
Cdd:cd16159 396 GRDLMPLL 403
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
8-310 |
8.45e-12 |
|
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: 65.90 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 8 MEHGGATFiNAFVTTPMC--CPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAMHEP---RTFAVYLNNTGYRTAFFG--K 80
Cdd:cd00016 32 LASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELPSRAAGKDedgPTIPELLKQAGYRTGVIGllK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 81 YLNEyngsyippgwrewlgliknsrfynytvcrnGIKEKHGFDYakdyftdlitnesINYfkmskrmyphrpvmmvishA 160
Cdd:cd00016 111 AIDE------------------------------TSKEKPFVLF-------------LHF-------------------D 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 161 APHGPEDSAPQFSKLYPNASQHItpsynyapnmdkhwimqytgpmlpihmeftnilqrkrlqtlmsvDDSVERLYNMLVE 240
Cdd:cd00016 129 GPDGPGHAYGPNTPEYYDAVEEI--------------------------------------------DERIGKVLDALKK 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2319158891 241 TGELENTYIIYTADHG---YHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIA 310
Cdd:cd00016 165 AGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
8-327 |
9.73e-12 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 67.49 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 8 MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVyTNNENCSSPSWQAMHEPrTFAVYLNNTGYRTAFFGKYLNEYNG 87
Cdd:cd16161 34 LAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVGGLPLNET-TLAEVLRQAGYATGMIGKWHLGQRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 88 SYIPpgwrewlglikNSRFYNYTVcrnGIKEKHGFDYAKDYF---TDLITNESINyfkmskrmypHRPVMMVISHAAPHG 164
Cdd:cd16161 112 AYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaTDFIQRASAK----------DRPFFLYAALAHVHV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 165 PEDSAPQFsklyPNASQHITPsynyapnmdkhwimqyTGpmlpihmeftnilqrkrlQTLMSVDDSVERLYNMLVETGEL 244
Cdd:cd16161 168 PLANLPRF----QSPTSGRGP----------------YG------------------DALQEMDDLVGQIMDAVKHAGLK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 245 ENTYIIYTAD---------------HGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILD 308
Cdd:cd16161 210 DNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGrIPANSTSAALVSTLDIFPTVVA 289
|
330 340
....*....|....*....|.
gi 2319158891 309 IAGLDTPPD--VDGKSVLKLL 327
Cdd:cd16161 290 LAGASLPPGriYDGKDLSPVL 310
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
222-311 |
1.64e-07 |
|
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: 53.36 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 222 QTLMSVDDSVERLYNMLVETGELENTYIIYTADHGY-----HiGQFglvkgksmPYDFDIRVPFFIRGPSVEPGSIVPQI 296
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF 253
|
90
....*....|....*
gi 2319158891 297 vLNIDLAPTILDIAG 311
Cdd:cd16018 254 -RNVDIYPLMCNLLG 267
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
280-328 |
2.64e-06 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 50.67 E-value: 2.64e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2319158891 280 FFIRGPSVEPGSIVPQIVLnIDLAPTILDIAGLDTPPDVDGKSVLKLLD 328
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
167-316 |
7.70e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 49.52 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 167 DSAPQFSKLYPNASQhitPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELEN 246
Cdd:COG3083 379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2319158891 247 TYIIYTADHGYhigQFGLVKGKSMPY-----DFDIRVPFFIRGPSVEPGSIvPQIVLNIDLAPTIL-DIAGLDTPP 316
Cdd:COG3083 456 TIVIITADHGE---EFNENGQNYWGHnsnfsRYQLQVPLVIHWPGTPPQVI-SKLTSHLDIVPTLMqRLLGVQNPA 527
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
227-325 |
2.01e-03 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 41.63 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 227 VDDSVERLYNMLVETGeleNTYIIyTADHG-------YHIGQfglvkgksmPY------DfdirVPFFIRGPSV---EPG 290
Cdd:PRK05434 417 VDECLGRVVDAVLKVG---GTLLI-TADHGnaeqmidPETGQ---------PHtahttnP----VPFILVGGKAlrlEGG 479
|
90 100 110
....*....|....*....|....*....|....*
gi 2319158891 291 SIvpqivlnIDLAPTILDIAGLDTPPDVDGKSVLK 325
Cdd:PRK05434 480 KL-------ADIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
228-313 |
4.34e-03 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 39.91 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 228 DDSVERLYNMLVETGEleNTYIIYTADHGYHIGQFGlVKGKSMPYDFD--IRVPFFI--------RGPSVEPGSIVPQIV 297
Cdd:cd16017 196 DYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRANKDRPF 272
|
90
....*....|....*.
gi 2319158891 298 LNIDLAPTILDIAGLD 313
Cdd:cd16017 273 SHDNLFHTLLGLLGIK 288
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
221-306 |
4.87e-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: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319158891 221 LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGyhIGQFGLVKGKSmpyDFDIRVPFF-----IRGPSVEPGSI--- 292
Cdd:cd16020 182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHG--MTDWGSHGDGS---PDETETPFIawgagIKHPTPGRGPSfsa 256
|
90 100
....*....|....*....|.
gi 2319158891 293 ------VPQIVLN-IDLAPTI 306
Cdd:cd16020 257 nwgglrLPRHDLDqADLAPLM 277
|
|
| |
