|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
4-469 |
0e+00 |
|
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: 835.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKNIST 83
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 84 MGRYFKDAGYHTCYIGKWHLDGHDYFGTGECPPEWDADYWFDGANYLSELTEKEISLWRNGLNSvedLQANHIDETFTWA 163
Cdd:cd16156 81 IGQRLSDNGIHTAYIGKWHLDGGDYFGNGICPQGWDPDYWYDMRNYLDELTEEERRKSRRGLTS---LEAEGIKEEFTYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 164 HRISNRAVDFLQQParADEPFLMVISYDEPHHPFTCPVEYLEKYTDFYYELGEKAEDDLANKPEHHRLWAQAMPSPVGDD 243
Cdd:cd16156 158 HRCTNRALDFIEKH--KDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAYDDLENKPLHQRLWAGAKPHEDGDK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 244 GLYHHPLYFACNDFVDDQIGRVINALtPEQRENTWVIYTSDHGEMMGAHKLISKGAAMYDDITRIPLIIRSPQGERR--Q 321
Cdd:cd16156 236 GTIKHPLYFGCNSFVDYEIGRVLDAA-DEIAEDAWVIYTSDHGDMLGAHKLWAKGPAVYDEITNIPLIIRGKGGEKAgtV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 322 VDTPVSHIDLLPTMMALADIEKPEILPGENILAVKEP------RGVLVEFNRYEIEHDSFGGFIPVRCWVTDDFKLVLNL 395
Cdd:cd16156 315 TDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDpeipenRGVFVEFGRYEVDHDGFGGFQPVRCVVDGRYKLVINL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446751221 396 FTSDELYDRRNDPNEMHNLIDDIHFADVRSKMHDALLDYMDKIRDPFRSYQWNLRPWRKDAQPRWMGAFRPRPQ 469
Cdd:cd16156 395 LSTDELYDLEKDPYEMHNLIDDPDYADVRDQLHDELLDYMNETRDPFRGYYWECRPWRKDARRPSWDYTGYTRQ 468
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-440 |
1.09e-105 |
|
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: 321.09 E-value: 1.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTN-------NVA 76
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNvenagaySRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 77 PGKNISTMGRYFKDAGYHTCYIGKWHLdghdyfGTGECPpewdADYWFDganylseltekeislwrnGLNSVEdlqanhi 156
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHV------GPEETP----LDYGFD------------------EYLPVE------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 157 dETFTwaHRISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEKYTDFYYELGEKAEDDLANKPEHHRLWAqAM 236
Cdd:cd16033 126 -TTIE--YFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYRRER-KR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 237 PSPVGDDGLYHHPL---YFACNDFVDDQIGRVINALTPE-QRENTWVIYTSDHGEMMGAHKLISKGAAMYDDITRIPLII 312
Cdd:cd16033 202 WGVDTEDEEDWKEIiahYWGYITLIDDAIGRILDALEELgLADDTLVIFTSDHGDALGAHRLWDKGPFMYEETYRIPLII 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 313 RSPQGER--RQVDTPVSHIDLLPTMMALADIEKPEILPGENILAVKE-------PRGVLVEFNRYEiehdsFGGFIpvRC 383
Cdd:cd16033 282 KWPGVIAagQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRgeqpedwRDEVVTEYNGHE-----FYLPQ--RM 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446751221 384 WVTDDFKLVLNLFTSDELYDRRNDPNEMHNLIDDIHFADVRSKMHDALLDYMDKIRD 440
Cdd:cd16033 355 VRTDRYKYVFNGFDIDELYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETGD 411
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-441 |
4.97e-105 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 318.75 E-value: 4.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 1 MKRPNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKN 80
Cdd:COG3119 21 AKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 81 IS----TMGRYFKDAGYHTCYIGKWHLDGHDYFGtgecppewdadywfdganylseltekeislwrnglnsvedlqanhi 156
Cdd:COG3119 101 LPpdepTLAELLKEAGYRTALFGKWHLYLTDLLT---------------------------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 157 detftwahrisNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEKYTDFYYELGEkaedDLANKPEHHRLWAQAM 236
Cdd:COG3119 135 -----------DKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPP----NLAPRDLTEEELRRAR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 237 pspvgddglyhhPLYFACNDFVDDQIGRVINALtpE---QRENTWVIYTSDHGEMMGAHKLI-SKGaAMYDDITRIPLII 312
Cdd:COG3119 200 ------------AAYAAMIEEVDDQVGRLLDAL--EelgLADNTIVVFTSDNGPSLGEHGLRgGKG-TLYEGGIRVPLIV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 313 RSPQG--ERRQVDTPVSHIDLLPTMMALADIEKPEILPGENILAV------KEPRGVLVEFNRYeiehdsfggfIPVRCW 384
Cdd:COG3119 265 RWPGKikAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLltgekaEWRDYLYWEYPRG----------GGNRAI 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446751221 385 VTDDFKLVLNLFTSD--ELYDRRNDPNEMHNLIDDihFADVRSKMHDALLDYMDKIRDP 441
Cdd:COG3119 335 RTGRWKLIRYYDDDGpwELYDLKNDPGETNNLAAD--YPEVVAELRALLEAWLKELGDP 391
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-414 |
4.83e-86 |
|
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: 270.21 E-value: 4.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKNIS 82
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPPDAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 83 TMGRYFKDAGYHTCYIGKWHLDGHDyfgtGECPPEWDA----------DYWFDGANYlseltekeislwRNGLNS--VED 150
Cdd:cd16034 81 TIADVLKDAGYRTGYIGKWHLDGPE----RNDGRADDYtppperrhgfDYWKGYECN------------HDHNNPhyYDD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 151 LQANHIDETFTWAHrISNRAVDFLQQPARADEPFLMVISYDEPHHPFT-CPVEYLEKYTDfyyELGEKAEDDLANKPEHH 229
Cdd:cd16034 145 DGKRIYIKGYSPDA-ETDLAIEYLENQADKDKPFALVLSWNPPHDPYTtAPEEYLDMYDP---KKLLLRPNVPEDKKEEA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 230 RLWAQAmpspvgddglyhhPLYFACNDFVDDQIGRVINALTPE-QRENTWVIYTSDHGEMMGAHKLISKGAAmYDDITRI 308
Cdd:cd16034 221 GLREDL-------------RGYYAMITALDDNIGRLLDALKELgLLENTIVVFTSDHGDMLGSHGLMNKQVP-YEESIRV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 309 PLIIRSP--QGERRQVDTPVSHIDLLPTMMALADIEKPEILPGENILAV------KEPRGVLVEFNRYEIEHdSFGGFIP 380
Cdd:cd16034 287 PFIIRYPgkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLllggkdDEPDSVLLQCFVPFGGG-SARDGGE 365
|
410 420 430
....*....|....*....|....*....|....*.
gi 446751221 381 VRCWVTDDFKLVLNLftSDE--LYDRRNDPNEMHNL 414
Cdd:cd16034 366 WRGVRTDRYTYVRDK--NGPwlLFDNEKDPYQLNNL 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
4-435 |
3.12e-83 |
|
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: 262.06 E-value: 3.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYsGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPW---TNNVAPGKN 80
Cdd:cd16027 1 PNILWIIADDLSPDLGGYG-GNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHglrSRGFPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 81 ISTMGRYFKDAGYHTCYIGKWHLdghdyfgtgecPPEWDADYWFDGanylseltekeislwrnglnsvedlqaNHIDETF 160
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKTHY-----------NPDAVFPFDDEM---------------------------RGPDDGG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 161 TWAHRISNRAVDFLQQPArADEPFLMVISYDEPHHPFTcpveylekyTDFYYELGEKAEDD-----LANKPEHHRLWAQa 235
Cdd:cd16027 122 RNAWDYASNAADFLNRAK-KGQPFFLWFGFHDPHRPYP---------PGDGEEPGYDPEKVkvppyLPDTPEVREDLAD- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 236 mpspvgddglYhhplYFACNDFvDDQIGRVINALtpEQR---ENTWVIYTSDHGEMMGAHKliskgAAMYDDITRIPLII 312
Cdd:cd16027 191 ----------Y----YDEIERL-DQQVGEILDEL--EEDgllDNTIVIFTSDHGMPFPRAK-----GTLYDSGLRVPLIV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 313 RSPQGER--RQVDTPVSHIDLLPTMMALADIEKPEILPGENILAV-----KEPRG-VLVEFNRYEIEHDsfggfiPVRCW 384
Cdd:cd16027 249 RWPGKIKpgSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLlkgekDPGRDyVFAERDRHDETYD------PIRSV 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446751221 385 VTDDFKLVLNlFTSDELYDRRNDPNEMHNLIDDIHFADVRSKMHDALLDYM 435
Cdd:cd16027 323 RTGRYKYIRN-YMPEELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWM 372
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
4-351 |
7.36e-83 |
|
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: 256.21 E-value: 7.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPG---KN 80
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGglpPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 81 ISTMGRYFKDAGYHTCYIGKWHldghdyfgtgecppewdadywfdganylseltekeislwrnglnsvedlqanhidetf 160
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGKWH---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 161 twahrisNRAVDFLQQPARaDEPFLMVISYDEPHHPFTcpveylekytdfyyelgekaeddlankpehhrlwaqampspv 240
Cdd:cd16022 103 -------DEAIDFIERRDK-DKPFFLYVSFNAPHPPFA------------------------------------------ 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 241 gddglyhhplYFACNDFVDDQIGRVINALTPE-QRENTWVIYTSDHGEMMGAHKLISKGAAMYDDITRIPLIIRSPQG-- 317
Cdd:cd16022 133 ----------YYAMVSAIDDQIGRILDALEELgLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKip 202
|
330 340 350
....*....|....*....|....*....|....
gi 446751221 318 ERRQVDTPVSHIDLLPTMMALADIEKPEILPGEN 351
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
2-431 |
5.71e-82 |
|
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: 260.54 E-value: 5.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 2 KRPNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNvAPGKNI 81
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNN-GPLFDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 82 STMG--RYFKDAGYHTCYIGKWHLDGHDyfgtGECPPEWdaDYWFDGANYLSELTEKeislwrNGLNSVEDLQANHIDEt 159
Cdd:cd16031 80 SQPTypKLLRKAGYQTAFIGKWHLGSGG----DLPPPGF--DYWVSFPGQGSYYDPE------FIENGKRVGQKGYVTD- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 160 ftwahRISNRAVDFLQQpARADEPFLMVISYDEPHHPFTCPVEYLEKYTDFYYELGEKA-EDDLANKPEhhrlWA-QAMP 237
Cdd:cd16031 147 -----IITDKALDFLKE-RDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFdDDDYAGRPE----WArEQRN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 238 SPVGDDGLYHHPL---------YFACNDFVDDQIGRVINALtpEQR---ENTWVIYTSDHGEMMGAHKLISKgAAMYDDI 305
Cdd:cd16031 217 RIRGVLDGRFDTPekyqrymkdYLRTVTGVDDNVGRILDYL--EEQglaDNTIIIYTSDNGFFLGEHGLFDK-RLMYEES 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 306 TRIPLIIRSPQGER--RQVDTPVSHIDLLPTMMALADIEKPEILPGENIL-------AVKEPRGVLVEFNRYEIEHD--- 373
Cdd:cd16031 294 IRVPLIIRDPRLIKagTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLpllegekPVDWRKEFYYEYYEEPNFHNvpt 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 374 SFGgfipVRcwvTDDFKLV--LNLFTSDELYDRRNDPNEMHNLIDDIHFADVRSKMHDAL 431
Cdd:cd16031 374 HEG----VR---TERYKYIyyYGVWDEEELYDLKKDPLELNNLANDPEYAEVLKELRKRL 426
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-409 |
3.06e-79 |
|
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: 250.15 E-value: 3.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKNIST 83
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 84 MGRYFKDAGYHTCYIGKWHLDGHDYFGtgecppewdadywfdGANYlseltekeislwrnglnsvedlqanhiDEtftwa 163
Cdd:cd16037 81 WGHALRAAGYETVLIGKLHFRGEDQRH---------------GFRY---------------------------DR----- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 164 hRISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEKYTdfyyelgekaeddlankpehHRLWAQampspvgdd 243
Cdd:cd16037 114 -DVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLYV--------------------RRARAA--------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 244 glyhhplYFACNDFVDDQIGRVINAL-TPEQRENTWVIYTSDHGEMMGAHKLISKGaAMYDDITRIPLIIRSP---QGER 319
Cdd:cd16037 164 -------YYGLVEFLDENIGRVLDALeELGLLDNTLIIYTSDHGDMLGERGLWGKS-TMYEESVRVPMIISGPgipAGKR 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 320 rqVDTPVSHIDLLPTMMALADIEKPEILPGENILAVKE-----PRGVLVEFNRyeieHDSFGGFIPVRcwvTDDFKLVLN 394
Cdd:cd16037 236 --VKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEgpddpDRVVFSEYHA----HGSPSGAFMLR---KGRWKYIYY 306
|
410
....*....|....*
gi 446751221 395 LFTSDELYDRRNDPN 409
Cdd:cd16037 307 VGYPPQLFDLENDPE 321
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
2-417 |
4.56e-75 |
|
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: 242.86 E-value: 4.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 2 KRPNFLFIMTDtQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNN-----VA 76
Cdd:cd16030 1 KKPNVLFIAVD-DLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNsyfrkVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 77 PgkNISTMGRYFKDAGYHTCYIGK-WHldgHDYFGTGECPPEWDADYW---FDGANYLSELTEKEISLWRNGLNSVEdlQ 152
Cdd:cd16030 80 P--DAVTLPQYFKENGYTTAGVGKiFH---PGIPDGDDDPASWDEPPNppgPEKYPPGKLCPGKKGGKGGGGGPAWE--A 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 153 ANHIDETFTwAHRISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEKYTDFYYELG---------EKAEDDLA 223
Cdd:cd16030 153 ADVPDEAYP-DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPLPnpfdpidlpEVAWNDLD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 224 NKPEHHRLWAQAMPSPVG--DDGLY----HHplYFACNDFVDDQIGRVINALtpEQ---RENTWVIYTSDHGEMMGAHKL 294
Cdd:cd16030 232 DLPKYGDIPALNPGDPKGplPDEQArelrQA--YYASVSYVDAQVGRVLDAL--EElglADNTIVVLWSDHGWHLGEHGH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 295 ISKgAAMYDDITRIPLIIRSP--QGERRQVDTPVSHIDLLPTMMALADIEKPEILPGENIL------AVKEPRGVLVEFN 366
Cdd:cd16030 308 WGK-HTLFEEATRVPLIIRAPgvTKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVpllknpSAKWKDAAFSQYP 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446751221 367 RYEIEHDSfggfipVRcwvTDDFKLV----LNLFTSDELYDRRNDPNEMHNLIDD 417
Cdd:cd16030 387 RPSIMGYS------IR---TERYRYTewvdFDKVGAEELYDHKNDPNEWKNLAND 432
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-435 |
1.64e-74 |
|
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: 239.44 E-value: 1.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGCYsGKPLN-TQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKNI 81
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCY-GQPLDlTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIPLPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 82 STMGRYFKDAGYHTCYIGKWHLDGHdyfgtgecppewDADYwfdganylseltekeislwrnglnsvedlqanhidetft 161
Cdd:cd16152 80 KTLAHYFRDAGYETGYVGKWHLAGY------------RVDA--------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 162 wahrISNRAVDFLQQPArADEPFLMVISYDEPHHP-----FTCPVEYLEKYTDFYyelgekAEDDLANKPEHhrlWAQAM 236
Cdd:cd16152 109 ----LTDFAIDYLDNRQ-KDKPFFLFLSYLEPHHQndrdrYVAPEGSAERFANFW------VPPDLAALPGD---WAEEL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 237 PSpvgddglyhhplYFACNDFVDDQIGRVINALTpEQ--RENTWVIYTSDHG----EMMGAHKliskgAAMYDDITRIPL 310
Cdd:cd16152 175 PD------------YLGCCERLDENVGRIRDALK-ELglYDNTIIVFTSDHGchfrTRNAEYK-----RSCHESSIRVPL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 311 IIRSPQGER-RQVDTPVSHIDLLPTMMALADIEKPEILPGENILAvkeprgvLVEFNRYEIEHDSF---GGFIPVRCWVT 386
Cdd:cd16152 237 VIYGPGFNGgGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLP-------LVDGKVEDWRNEVFiqiSESQVGRAIRT 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446751221 387 DDFKLVL-------------NLFTSDELYDRRNDPNEMHNLIDDIHFADVRSKMHDALLDYM 435
Cdd:cd16152 310 DRWKYSVaapdkdgwkdsgsDVYVEDYLYDLEADPYELVNLIGRPEYREVAAELRERLLARM 371
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
4-341 |
3.47e-73 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 233.47 E-value: 3.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNN-VAPGKNIS 82
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTpVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 83 TMGRYFKDAGYHTCYIGKWHLDGHDYFGtgecPPEWDADYWFDGANYLSELTEKEISLWRNGLNSVEDlqanhidetftw 162
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWHLGWYNNQS----PCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSD------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 163 aHRISNRAVDFLQQParaDEPFLMVISYDEPHHPFTCPVEYLEKYTDFYyelgekaeddlankpehhrlwaqampsPVGD 242
Cdd:pfam00884 145 -EALLDEALEFLDNN---DKPFFLVLHTLGSHGPPYYPDRYPEKYATFK---------------------------PSSC 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 243 DGLYHHPLYFACNDFVDDQIGRVINAL-TPEQRENTWVIYTSDHGEMM---GAHKLISKGAAMYDDITRIPLIIRSPQGE 318
Cdd:pfam00884 194 SEEQLLNSYDNTLLYTDDAIGRVLDKLeENGLLDNTLVVYTSDHGESLgegGGYLHGGKYDNAPEGGYRVPLLIWSPGGK 273
|
330 340
....*....|....*....|....*
gi 446751221 319 RRQ--VDTPVSHIDLLPTMMALADI 341
Cdd:pfam00884 274 AKGqkSEALVSHVDLFPTILDLAGI 298
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-434 |
2.60e-68 |
|
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: 224.73 E-value: 2.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTG-------IYANQSG------- 69
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGqyparlgITDVIPGrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 70 -----PWTNNVAPGKNIsTMGRYFKDAGYHTCYIGKWHLDGHDYF------------GTGECPPEWDADYWFDGANYLSE 132
Cdd:cd16144 81 tklipPPSTTRLPLEEV-TIAEALKDAGYATAHFGKWHLGGEGGYgpedqgfdvnigGTGNGGPPSYYFPPGKPNPDLED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 133 LTEKEislwrnglnsvedlqanHIDEtftwahRISNRAVDFLQQpaRADEPFLMVISYDEPHHPFTCPVEYLEKYtdfyy 212
Cdd:cd16144 160 GPEGE-----------------YLTD------RLTDEAIDFIEQ--NKDKPFFLYLSHYAVHTPIQARPELIEKY----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 213 elgekaeddlankpehhrlwaQAMPSPVGDDGlyHHPLYFACNDFVDDQIGRVINAL-TPEQRENTWVIYTSDHGEMMGA 291
Cdd:cd16144 210 ---------------------EKKKKGLRKGQ--KNPVYAAMIESLDESVGRILDALeELGLADNTLVIFTSDNGGLSTR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 292 HKLIS--------KGAaMYDDITRIPLIIRSP--QGERRQVDTPVSHIDLLPTMMALADIEKPE--ILPGENILAV-KEP 358
Cdd:cd16144 267 GGPPTsnaplrggKGS-LYEGGIRVPLIVRWPgvIKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLlKGG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 359 RGVLVE---FNRYEIEHDSFGGfiP---VRCwvtDDFKLVLNLFT-SDELYDRRNDPNEMHNLIDDihFADVRSKMHDAL 431
Cdd:cd16144 346 EADLPRralFWHFPHYHGQGGR--PasaIRK---GDWKLIEFYEDgRVELYNLKNDIGETNNLAAE--MPEKAAELKKKL 418
|
...
gi 446751221 432 LDY 434
Cdd:cd16144 419 DAW 421
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-432 |
6.65e-65 |
|
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: 214.35 E-value: 6.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 2 KRPNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAY----TCSPVCTPARAGLFTGIYANQsgpWTNNVAP 77
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYnmggWSGAVCVPSRAMLMTGRTLFH---APEGGKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 78 GKNIS--TMGRYFKDAGYHTCYIGKWHLDghdyfgtgecppewdadywfdganylseltekeislwrnglnsvedlqanh 155
Cdd:cd16155 78 AIPSDdkTWPETFKKAGYRTFATGKWHNG--------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 156 idetftwahrISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEKYtdfyyelgekaeddlanKPEHHRLWAQA 235
Cdd:cd16155 107 ----------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMY-----------------PPETIPLPENF 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 236 MPS--------PVGDDGLYHHPL-----------YFACNDFVDDQIGRVINAL-TPEQRENTWVIYTSDHGEMMGAHKLI 295
Cdd:cd16155 160 LPQhpfdngegTVRDEQLAPFPRtpeavrqhlaeYYAMITHLDAQIGRILDALeASGELDNTIIVFTSDHGLAVGSHGLM 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 296 SKgAAMYDDITRIPLIIRSP---QGERRqvDTPVSHIDLLPTMMALADIEKPEILPGENILAV-----KEPRGVLvefnr 367
Cdd:cd16155 240 GK-QNLYEHSMRVPLIISGPgipKGKRR--DALVYLQDVFPTLCELAGIEIPESVEGKSLLPVirgekKAVRDTL----- 311
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446751221 368 yeiehdsFGGFI----PVRcwvTDDFKLVLNLFTSD--ELYDRRNDPNEMHNLIDDIHFADVRSKMHDALL 432
Cdd:cd16155 312 -------YGAYRdgqrAIR---DDRWKLIIYVPGVKrtQLFDLKKDPDELNNLADEPEYQERLKKLLAELK 372
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
4-439 |
1.25e-61 |
|
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: 207.02 E-value: 1.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTcSPVCTPARAGLFTGIYANQSGPWtnNVAPG----- 78
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHV-SPVCAPTRAALLTGRYPFRTGVW--HTILGrermr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 79 KNISTMGRYFKDAGYHTCYIGKWHL-DGHDYF---------------GTGECPPEWDADYWFDganylseltekeiSLWR 142
Cdd:cd16146 78 LDETTLAEVFKDAGYRTGIFGKWHLgDNYPYRpqdrgfdevlghgggGIGQYPDYWGNDYFDD-------------TYYH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 143 NGLNSVEDlqaNHIDETFTwahrisNRAVDFLQQpaRADEPFLMVISYDEPHHPFTCPveylEKYTDFYYELGEKaeDDL 222
Cdd:cd16146 145 NGKFVKTE---GYCTDVFF------DEAIDFIEE--NKDKPFFAYLATNAPHGPLQVP----DKYLDPYKDMGLD--DKL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 223 ANkpehhrlwaqampspvgddglyhhplYFACNDFVDDQIGRVINALtpEQR---ENTWVIYTSDHGEMMGAHKLI---- 295
Cdd:cd16146 208 AA--------------------------FYGMIENIDDNVGRLLAKL--KELgleENTIVIFMSDNGPAGGVPKRFnagm 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 296 --SKGAAmYDDITRIPLIIRSPQG--ERRQVDTPVSHIDLLPTMMALADIEKPEILP--GENILAV-------KEPRGVL 362
Cdd:cd16146 260 rgKKGSV-YEGGHRVPFFIRWPGKilAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKldGRSLLPLlkgesdpWPERTLF 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446751221 363 VEFNRYEIEHDSFGGFIpVRcwvTDDFKLVLNLFTSDELYDRRNDPNEMHNLIDDihFADVRSKMHDALLDYMDKIR 439
Cdd:cd16146 339 THSGRWPPPPKKKRNAA-VR---TGRWRLVSPKGFQPELYDIENDPGEENDVADE--HPEVVKRLKAAYEAWWDDVK 409
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
1-435 |
9.55e-61 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 206.83 E-value: 9.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 1 MKRPNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGiyanQSgPWT------NN 74
Cdd:PRK13759 4 TKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTG----LS-QWHhgrvgyGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 75 VAPGKNISTMGRYFKDAGYHTCYIGKWHL---------------DGHDYFGTGECPPEWD--ADY--WF--DGANYLSEL 133
Cdd:PRK13759 79 VVPWNYKNTLPQEFRDAGYYTQCIGKMHVfpqrnllgfhnvllhDGYLHSGRNEDKSQFDfvSDYlaWLreKAPGKDPDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 134 TEkeislwrNGLNSvEDLQAN--HIDETFTWAHRISNRAVDFLQQPARaDEPFLMVISYDEPHHPFTCPVEYLEKYTDfy 211
Cdd:PRK13759 159 TD-------IGWDC-NSWVARpwDLEERLHPTNWVGSESIEFLRRRDP-TKPFFLKMSFARPHSPYDPPKRYFDMYKD-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 212 YELGEKAEDDLANKPEHHRLWAQ--AMPSPVGDDGLYH-HPLYFACNDFVDDQIGRVINALTPE-QRENTWVIYTSDHGE 287
Cdd:PRK13759 228 ADIPDPHIGDWEYAEDQDPEGGSidALRGNLGEEYARRaRAAYYGLITHIDHQIGRFLQALKEFgLLDNTIILFVSDHGD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 288 MMGAHKLISKGAAmYDDITRIPLIIRSP----QGERRQV-DTPVSHIDLLPTMMALADIEKPEILPGENILAVKEprGVL 362
Cdd:PRK13759 308 MLGDHYLFRKGYP-YEGSAHIPFIIYDPggllAGNRGTViDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIF--GQY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 363 VEFNRY-EIEH----DSFGgfipvrcWVTDD-FKLVLNLFT-SDELYDRRNDPNEMHNLIDDIHFADVRSKMHDALLDYM 435
Cdd:PRK13759 385 EGWRPYlHGEHalgySSDN-------YLTDGkWKYIWFSQTgEEQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVDHL 457
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-369 |
1.25e-60 |
|
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: 201.28 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMV--GCYSGKPLNTQNidSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSG-------PWTNN 74
Cdd:cd16035 1 PNILLILTDQERYPPPwpAGWAALNLPARE--RLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGvtdtlgsPMQPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 75 VAPGknISTMGRYFKDAGYHTCYIGKWHLDGHDYFGTGecppewdadywFDGanylseltekeislwrnglnsvedlqan 154
Cdd:cd16035 79 LSPD--VPTLGHMLRAAGYYTAYKGKWHLSGAAGGGYK-----------RDP---------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 155 hidetftwahRISNRAVDFLQQPAR---ADEPFLMVISYDEPHhpftcpveylekytdfyyelgekaeDDLANKPEHHRL 231
Cdd:cd16035 118 ----------GIAAQAVEWLRERGAknaDGKPWFLVVSLVNPH-------------------------DIMFPPDDEERW 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 232 WaqampspvgddglYHHPLYFACNDFVDDQIGRVINALTPE-QRENTWVIYTSDHGEMMGAHKLISKGAAMYDDITRIPL 310
Cdd:cd16035 163 R-------------RFRNFYYNLIRDVDRQIGRVLDALDASgLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPL 229
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446751221 311 IIRSPQ--GERRQVDTPVSHIDLLPTMMALADIEKPEI------LPGENILAV------KEPR-GVLVEFNRYE 369
Cdd:cd16035 230 IISHPDlfGTGQTTDALTSHIDLLPTLLGLAGVDAEARateappLPGRDLSPLltdadaDAVRdGILFTYDRYK 303
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-435 |
1.67e-58 |
|
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: 199.00 E-value: 1.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYsGKPLN-TQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSG---------PWTN 73
Cdd:cd16150 1 PNIVIFVADQLRADSLGHL-GNPAAvTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGhrtlhhllrPDEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 74 NvapgknistMGRYFKDAGYHTCYIGKWHLdghdyfgtgecppeWDADYWFDganylseltekeislwrnglnSVEDLqa 153
Cdd:cd16150 80 N---------LLKTLKDAGYHVAWAGKNDD--------------LPGEFAAE---------------------AYCDS-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 154 nhiDETFTwahrisNRAVDFLQQPaRADEPFLMVISYDEPHHPFTCPVEYLEKYT------DFYYELGEKAEDDLANKPE 227
Cdd:cd16150 114 ---DEACV------RTAIDWLRNR-RPDKPFCLYLPLIFPHPPYGVEEPWFSMIDreklppRRPPGLRAKGKPSMLEGIE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 228 HHRLWAqampspVGDDGLYH-HPLYFACNDFVDDQIGRVINALTPE-QRENTWVIYTSDHGEMMGAHKLISKG-AAMYDD 304
Cdd:cd16150 184 KQGLDR------WSEERWRElRATYLGMVSRLDHQFGRLLEALKETgLYDDTAVFFFSDHGDYTGDYGLVEKWpNTFEDC 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 305 ITRIPLIIRSPQG-ERRQVDTPVSHIDLLPTMMALADIEKPEILPGENILAV-----KEPR-GVLVE--FNRYEIEHDSF 375
Cdd:cd16150 258 LTRVPLIIKPPGGpAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVlagetEEHRdAVFSEggRLHGEEQAMEG 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446751221 376 GGFIPVRCW------------------VTDDFKLVLNLFTSDELYDRRNDPNEMHNLIDDIHFADVRSKMHDALLDYM 435
Cdd:cd16150 338 GHGPYDLKWprllqqeeppehtkavmiRTRRYKYVYRLYEPDELYDLEADPLELHNLIGDPAYAEIIAEMKQRLLRWM 415
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
4-441 |
2.24e-55 |
|
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: 191.70 E-value: 2.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKNIST 83
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDARHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 84 MGRYFKDAGYHTCYIGKWH----LDGHDYFGtgecPPEWDADYWFDGANYLSELTEkeislwrnglnsvedLQANHIDET 159
Cdd:cd16028 81 LALELRKAGYDPALFGYTDtspdPRGLAPLD----PRLLSYELAMPGFDPVDRLDE---------------YPAEDSDTA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 160 FtwahrISNRAVDFLQqpARADEPFLMVISYDEPHHPFTCPVEYLEKYTDFYYELGEKAEDDLANKpEHHRLWAQAMPSP 239
Cdd:cd16028 142 F-----LTDRAIEYLD--ERQDEPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPPIRAESLAAEA-AQHPLLAAFLERI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 240 VGDDGLYHHPLYFACNDF---------------VDDQIGRVINAL-TPEQRENTWVIYTSDHGEMMGAHKLISKGAaMYD 303
Cdd:cd16028 214 ESLSFSPGAANAADLDDEevaqmratylgliaeVDDHLGRLFDYLkETGQWDDTLIVFTSDHGEQLGDHWLWGKDG-FFD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 304 DITRIPLIIRSPQGER-----RQVDTPVSHIDLLPTMMALADIEKPEILPGENILAVKepRGVLVEFNRYEI--EHDSFG 376
Cdd:cd16028 293 QAYRVPLIVRDPRREAdatrgQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLL--AGAQPSDWRDAVhyEYDFRD 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446751221 377 GFIP------------VRCWV--TDDFKLVLNLFTSDELYDRRNDPNEMHNLIDDIHFADVRSKMHDALLDYMDKIRDP 441
Cdd:cd16028 371 VSTRrpqealglspdeCSLAVirDERWKYVHFAALPPLLFDLKNDPGELRDLAADPAYAAVVLRYAQKLLSWRMRHADR 449
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
3-418 |
2.35e-55 |
|
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: 190.07 E-value: 2.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGcYSGKPLnTQNIdsLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPG---K 79
Cdd:cd16147 1 RPNIVLILTDDQDVELGS-MDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGgypK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 80 NI------STMGRYFKDAGYHTCYIGKwHLDGHDYFGTGE-CPPEWDadYWF---DGANYlseltekeiSLWRNGLNSVE 149
Cdd:cd16147 77 FWqnglerSTLPVWLQEAGYRTAYAGK-YLNGYGVPGGVSyVPPGWD--EWDglvGNSTY---------YNYTLSNGGNG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 150 DLQANHIDETFTwaHRISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEKYTDFYYE-LGEKAEDDLANKPEh 228
Cdd:cd16147 145 KHGVSYPGDYLT--DVIANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPpRPPPNNPDVSDKPH- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 229 hrlWAQAMPSPVGDDGlyhhplyfACNDF-----------VDDQIGRVINAL-TPEQRENTWVIYTSDHGEMMGAHKL-I 295
Cdd:cd16147 222 ---WLRRLPPLNPTQI--------AYIDElyrkrlrtlqsVDDLVERLVNTLeATGQLDNTYIIYTSDNGYHLGQHRLpP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 296 SKGAAmYD-DItRIPLIIRSPQGERRQVDT-PVSHIDLLPTMMALADIEKPEILPGENILAVKeprgvlveFNRYeiehd 373
Cdd:cd16147 291 GKRTP-YEeDI-RVPLLVRGPGIPAGVTVDqLVSNIDLAPTILDLAGAPPPSDMDGRSCGDSN--------NNTY----- 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446751221 374 sfggfipvRCWVTDDFKLVLNLFTSD----ELYDRRNDPNEMHNLIDDI 418
Cdd:cd16147 356 --------KCVRTVDDTYNLLYFEWCtgfrELYDLTTDPYQLTNLAGDL 396
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
4-409 |
6.84e-54 |
|
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: 183.93 E-value: 6.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKNIST 83
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 84 MGRYFKDAGYHTCYIGKWH------LDGHDYfgtgecppewdadywfdganylseltekeislwrnglnsvedlqanhiD 157
Cdd:cd16032 81 FAHYLRAAGYRTALSGKMHfvgpdqLHGFDY------------------------------------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 158 ETFTWahrisnRAVDFLQQPARADE--PFLMVISYDEPHHPFTCPVEYLekytDFYYELGEKAeddlankpehhrlwaqa 235
Cdd:cd16032 113 EEVAF------KAVQKLYDLARGEDgrPFFLTVSFTHPHDPYVIPQEYW----DLYVRRARRA----------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 236 mpspvgddglyhhplYFACNDFVDDQIGRVINALT-PEQRENTWVIYTSDHGEMMGAHKLISKgAAMYDDITRIPLIIRS 314
Cdd:cd16032 166 ---------------YYGMVSYVDDKVGQLLDTLErTGLADDTIVIFTSDHGDMLGERGLWYK-MSFFEGSARVPLIISA 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 315 PQG-ERRQVDTPVSHIDLLPTMMALADIEKPEILP---GENILAVKEprGVLVEFNRYEI-EHDSFGGFIPVRCWVTDDF 389
Cdd:cd16032 230 PGRfAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpldGRSLLPLLE--GGDSGGEDEVIsEYLAEGAVAPCVMIRRGRW 307
|
410 420
....*....|....*....|
gi 446751221 390 KLVLNLFTSDELYDRRNDPN 409
Cdd:cd16032 308 KFIYCPGDPDQLFDLEADPL 327
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-354 |
1.22e-52 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 178.90 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWtnNVAPGKNIST 83
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW--GGPLEPDDPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 84 MGRYFKDAGYHT-CYIGKWHLDGHDYFGTGecppeWDADYWFDGanylseltekeislwrnglnsvedLQANHIDETFTW 162
Cdd:cd16148 79 LAEILRKAGYYTaAVSSNPHLFGGPGFDRG-----FDTFEDFRG------------------------QEGDPGEEGDER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 163 AHRISNRAVDFLQQpARADEPFLMVISYDEPHHPFtcpveylekytdfyyelgekaeddlankpehhrlwaqampspvgd 242
Cdd:cd16148 130 AERVTDRALEWLDR-NADDDPFFLFLHYFDPHEPY--------------------------------------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 243 dglyhhpLYFACNDFVDDQIGRVINALtpEQR---ENTWVIYTSDHGEMMGAHKLISK-GAAMYDDITRIPLIIRSPQGE 318
Cdd:cd16148 164 -------LYDAEVRYVDEQIGRLLDKL--KELgllEDTLVIVTSDHGEEFGEHGLYWGhGSNLYDEQLHVPLIIRWPGKE 234
|
330 340 350
....*....|....*....|....*....|....*..
gi 446751221 319 RRQ-VDTPVSHIDLLPTMMALADIEKPEILPGENILA 354
Cdd:cd16148 235 PGKrVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-349 |
1.32e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 170.50 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSG------PWTNNVAP 77
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGihdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 78 G-----KNISTMGRYFKDAGYHTCYIGKWHLdghdyfGTgecppewdadywfdganylseltekeislwrnglnsvedlq 152
Cdd:cd16149 81 KpegylEGQTTLPEVLQDAGYRCGLSGKWHL------GD----------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 153 anhidetftwahrisnRAVDFLQQPARADEPFLMVISYDEPHHPftcpveylekytdfyyelgekaeddlankpehhrlW 232
Cdd:cd16149 114 ----------------DAADFLRRRAEAEKPFFLSVNYTAPHSP-----------------------------------W 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 233 AqampspvgddglyhhplYFACNDFVDDQIGRVINAL-TPEQRENTWVIYTSDHGEMMGAHKLISKGAA-----MYDDIT 306
Cdd:cd16149 143 G-----------------YFAAVTGVDRNVGRLLDELeELGLTENTLVIFTSDNGFNMGHHGIWGKGNGtfplnMYDNSV 205
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446751221 307 RIPLIIRSPQGER--RQVDTPVSHIDLLPTMMALADIEKPE--ILPG 349
Cdd:cd16149 206 KVPFIIRWPGVVPagRVVDSLVSAYDFFPTLLELAGVDPPAdpRLPG 252
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
3-415 |
2.13e-49 |
|
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: 174.29 E-value: 2.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKNIS 82
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 83 ------TMGRYFKDAGYHTCYIGKWHLDGHDYFgtgeCPPEWDADYWFdGANY------LSELTEKEISLWRNGLNSVED 150
Cdd:cd16026 81 lppdeiTIAEVLKKAGYRTALVGKWHLGHQPEF----LPTRHGFDEYF-GIPYsndmwpFPLYRNDPPGPLPPLMENEEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 151 LQANHIDETFTwaHRISNRAVDFLQqpARADEPFLMVISYDEPHHPFTCPVEYLEKytdfyyelgekaeddlankpehhr 230
Cdd:cd16026 156 IEQPADQSSLT--QRYTDEAVDFIE--RNKDQPFFLYLAHTMPHVPLFASEKFKGR------------------------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 231 lwaqampspvGDDGLYhhplyfacNDFV---DDQIGRVINAL-TPEQRENTWVIYTSDHG---EMMGAH----KLISKGA 299
Cdd:cd16026 208 ----------SGAGLY--------GDVVeelDWSVGRILDALkELGLEENTLVIFTSDNGpwlEYGGHGgsagPLRGGKG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 300 AMYDDITRIPLIIRSP----QGerRQVDTPVSHIDLLPTMMALADIEKPE--ILPGENILAV-----KEPRGVLVEFNRY 368
Cdd:cd16026 270 TTWEGGVRVPFIAWWPgvipAG--TVSDELASTMDLLPTLAALAGAPLPEdrVIDGKDISPLllggsKSPPHPFFYYYDG 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446751221 369 eiehdsfGGFIPVRcwvTDDFKLVLN---------------LFTSDELYDRRNDPNEMHNLI 415
Cdd:cd16026 348 -------GDLQAVR---SGRWKLHLPttyrtgtdpggldptKLEPPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-415 |
2.34e-47 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 168.53 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDtqatNM----VGCYSGK-PLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYA----NQSGPWTNN 74
Cdd:cd16143 1 PNIVIILAD----DLgygdISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPwrsrLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 75 VAP--GKNISTMGRYFKDAGYHTCYIGKWHLdGHDYFGTGECPPewdADYWFDGANYLSELtekeislwRNGLNSVE-D- 150
Cdd:cd16143 77 SPPliEPDRVTLAKMLKQAGYRTAMVGKWHL-GLDWKKKDGKKA---ATGTGKDVDYSKPI--------KGGPLDHGfDy 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 151 ---LQANHIDETFTwahrisNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEK-----YTDFYYELgekaeddl 222
Cdd:cd16143 145 yfgIPASEVLPTLT------DKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGKsgagpYGDFVYEL-------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 223 ankpehhrlwaqampspvgddglyhhplyfacndfvDDQIGRVINAL-TPEQRENTWVIYTSDHG--EMMGAHKLISKG- 298
Cdd:cd16143 211 ------------------------------------DWVVGRILDALkELGLAENTLVIFTSDNGpsPYADYKELEKFGh 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 299 ----------AAMYDDITRIPLIIRSPQGER--RQVDTPVSHIDLLPTMMALADIEKPE--------ILP---GENilAV 355
Cdd:cd16143 255 dpsgplrgmkADIYEGGHRVPFIVRWPGKIPagSVSDQLVSLTDLFATLAAIVGQKLPDnaaedsfsFLPallGPK--KQ 332
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 356 KEPRGVLVEFNRYE----------IEHDSFGGFipvrcwvTDDFKLVLNLFTSDELYDRRNDPNEMHNLI 415
Cdd:cd16143 333 EVRESLVHHSGNGSfairkgdwklIDGTGSGGF-------SYPRGKEKLGLPPGQLYNLSTDPGESNNLY 395
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-414 |
8.63e-46 |
|
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: 165.08 E-value: 8.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKN--- 80
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDplp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 81 --ISTMGRYFKDAGYHTCYIGKWHLDGhdyFGTGECPPEWDADYWF------DGANYLSELtekeisLWRNG-------- 144
Cdd:cd16145 81 pdDVTLAEVLKKAGYATAAFGKWGLGG---PGTPGHPTKQGFDYFYgyldqvHAHNYYPEY------LWRNGekvplpnn 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 145 LNSVEDLQANHIDETFTWAH-RISNRAVDFLQQpaRADEPFLMVISYDEPHHPFTCPVEYLEKYtdFYYELGEKAEDDLa 223
Cdd:cd16145 152 VIPPLDEGNNAGGGGGTYSHdLFTDEALDFIRE--NKDKPFFLYLAYTLPHAPLQVPDDGPYKY--KPKDPGIYAYLPW- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 224 nkPEHHRLWAqAMPSpvgddglyhhplyfacndFVDDQIGRVINALTpEQ--RENTWVIYTSDHgemmGAHKLISKGAA- 300
Cdd:cd16145 227 --PQPEKAYA-AMVT------------------RLDRDVGRILALLK-ELgiDENTLVVFTSDN----GPHSEGGSEHDp 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 301 ---------------MYDDITRIPLIIRSPQ--GERRQVDTPVSHIDLLPTMMALADIEKPE------ILP---GENILA 354
Cdd:cd16145 281 dffdsngplrgykrsLYEGGIRVPFIARWPGkiPAGSVSDHPSAFWDFMPTLADLAGAEPPEdidgisLLPtllGKPQQQ 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446751221 355 VKEPrgvLVeFNRYEiehdsFGGFIPVRcwvTDDFKLV-LNLFTSD-ELYDRRNDPNEMHNL 414
Cdd:cd16145 361 QHDY---LY-WEFYE-----GGGAQAVR---MGGWKAVrHGKKDGPfELYDLSTDPGETNNL 410
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
2-414 |
9.68e-46 |
|
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: 164.54 E-value: 9.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 2 KRPNFLFIMTDTQATNMVGCYsGKPLNTQNIDSLAAEGIRFNSAYTcSPVCTPARAGLFTGIYANQSG----PWTNNVAP 77
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCF-GGEIPTPNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHHQVGmgtmAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 78 G------KNISTMGRYFKDAGYHTCYIGKWHLDGHDYfgtgecppewdadywfdganYLSELtekeislwrnglnsvedl 151
Cdd:cd16025 79 GyegylpDSAATIAEVLKDAGYHTYMSGKWHLGPDDY--------------------YSTDD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 152 qanhidetftwahrISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEKYTDFY---------------YELG- 215
Cdd:cd16025 121 --------------LTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKYdagwdalreerlerqKELGl 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 216 -------------EKAEDDLAnkPEHHRLWAQAMpspvgddglyhhPLYFACNDFVDDQIGRVINALtpE---QRENTWV 279
Cdd:cd16025 187 ipadtkltprppgVPAWDSLS--PEEKKLEARRM------------EVYAAMVEHMDQQIGRLIDYL--KelgELDNTLI 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 280 IYTSDHG---EMMGAH---------KLiskgaAMYDDITRIPLIIRSPQGERRQ---VDTPVSHIDLLPTMMALADIEKP 344
Cdd:cd16025 251 IFLSDNGasaEPGWANasntpfrlyKQ-----ASHEGGIRTPLIVSWPKGIKAKggiRHQFAHVIDIAPTILELAGVEYP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 345 EILPGEnilAVKEPRGV-LVEFNRYEIEHDS--------FGGfipvRCWVTDDFKLVLNL-----FTSDELYDRRNDPNE 410
Cdd:cd16025 326 KTVNGV---PQLPLDGVsLLPTLDGAAAPSRrrtqyfelFGN----RAIRKGGWKAVALHpppgwGDQWELYDLAKDPSE 398
|
....
gi 446751221 411 MHNL 414
Cdd:cd16025 399 THDL 402
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-414 |
3.83e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 148.52 E-value: 3.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTcSPVCTPARAGLFTGIYANQSGpWTNNVAPGKNIsT 83
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRNY-VVFGYLDPKQK-T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 84 MGRYFKDAGYHTCYIGKWHLDGhdYFGTGECPPE--WDaDYwfdganYLSELTEKEISLWRNGLNSVEDLQANHIDETFT 161
Cdd:cd16151 78 FGHLLKDAGYATAIAGKWQLGG--GRGDGDYPHEfgFD-EY------CLWQLTETGEKYSRPATPTFNIRNGKLLETTEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 162 W--AHRISNRAVDFLQQpaRADEPFL----MVIsydePHHPFT-CPveyLEKYTDfyyelgeKAEDDLANKPEHHRlwaq 234
Cdd:cd16151 149 DygPDLFADFLIDFIER--NKDQPFFayypMVL----VHDPFVpTP---DSPDWD-------PDDKRKKDDPEYFP---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 235 AMpspvgddglyhhplyfacNDFVDDQIGRVINALTPE-QRENTWVIYTSDHG------EMMGAHKLISKGAAMYDDITR 307
Cdd:cd16151 209 DM------------------VAYMDKLVGKLVDKLEELgLRENTIIIFTGDNGthrpitSRTNGREVRGGKGKTTDAGTH 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 308 IPLIIRSPqG---ERRQVDTPVSHIDLLPTMMALADIEKPEILPGENILAVKEPRGVLVEFNRYEI-EHDSFGGFIPVRC 383
Cdd:cd16151 271 VPLIVNWP-GlipAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIyWYYRNPHKKFGSR 349
|
410 420 430
....*....|....*....|....*....|..
gi 446751221 384 WV-TDDFKlvlnLFTSDELYDRRNDPNEMHNL 414
Cdd:cd16151 350 FVrTKRYK----LYADGRFFDLREDPLEKNPL 377
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-354 |
5.12e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 126.72 E-value: 5.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGCY-------SGKPLN---TQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSG--- 69
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYnnahtgkSESRLGyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGvyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 70 -PWTNNVAPGKNIsTMGRYFKDAGYHTCYIGKwhlDGHDYFgtgecppewdadywfdgANYLSeltekeislwrnglnsv 148
Cdd:cd16153 81 fEAAHPALDHGLP-TFPEVLKKAGYQTASFGK---SHLEAF-----------------QRYLK----------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 149 edlQANHIDETFtwahrisnraVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEKYtdfyyelgekaeddlankpeh 228
Cdd:cd16153 123 ---NANQSYKSF----------WGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEFRDRF--------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 229 hrlwaqampspvgddglyhhpLYFACNDFVDDQIGRVINALT----PEQRENTWVIYTSDHGEMMGAHKLISKGAAMYDD 304
Cdd:cd16153 169 ---------------------DYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHGWHLGEQGILAKFTFWPQS 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446751221 305 iTRIPLIIRS------PQGERRqvDTPVSHIDLLPTMMALA--DIEKPEILPGENILA 354
Cdd:cd16153 228 -HRVPLIVVSsdklkaPAGKVR--HDFVEFVDLAPTLLAAAgvDVDAPDYLDGRDLFE 282
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
4-414 |
6.84e-33 |
|
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: 129.21 E-value: 6.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTcSPVCTPARAGLFTGIYANQSGPWTNNVAPG----- 78
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHTGMQHGVILAGepygl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 79 -KNISTMGRYFKDAGYHTCYIGKWHL--------------DGHD-YFGTGEcppewdaDYWfdganylselTEKEISLWR 142
Cdd:cd16029 80 pLNETLLPQYLKELGYATHLVGKWHLgfytweytptnrgfDSFYgYYGGAE-------DYY----------THTSGGAND 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 143 NGLNSVEDLQANHIDETFTWA-HRISNRAVDFLQQpARADEPFLMVISYDEPHHPFTCPVEYLEKYTDFYyelgekaedd 221
Cdd:cd16029 143 YGNDDLRDNEEPAWDYNGTYStDLFTDRAVDIIEN-HDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKF---------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 222 lANKPEHHRLWAQAMPSPVgddglyhhplyfacndfvDDQIGRVINALtpEQR---ENTWVIYTSDHGemmGAHKLISKG 298
Cdd:cd16029 212 -AHIKDEDRRTYAAMVSAL------------------DESVGNVVDAL--KAKgmlDNTLIVFTSDNG---GPTGGGDGG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 299 ---------AAMYDDITRIPLIIRSP--QGERRQVDTPVSHI-DLLPTMMALADIEKPEILP--GENI-LAVKEPRgvlv 363
Cdd:cd16029 268 snyplrggkNTLWEGGVRVPAFVWSPllPPKRGTVSDGLMHVtDWLPTLLSLAGGDPDDLPPldGVDQwDALSGGA---- 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446751221 364 EFNRYEIEH--DSFGGFIPVRCWVTDDFKLVlnlfTSDELYDRRNDPNEMHNL 414
Cdd:cd16029 344 PSPRTEILLniDDITRTTGGAAIRVGDWKLI----VGKPLFNIENDPCERNDL 392
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
3-447 |
4.57e-30 |
|
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: 123.17 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNV------- 75
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGmrvilft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 76 -APG---KNISTMGRYFKDAGYHTCYIGKWHL----------------DGHDYF-GT-----GECPPEWDADYWFDGANY 129
Cdd:cd16159 81 aSSGglpPNETTFAEVLKQQGYSTALIGKWHLglhcesrndfchhplnHGFDYFyGLpltnlKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 130 LSELTE---------------KEISlWRNG-----------------------LNSVedLQANH-------IDETFTwaH 164
Cdd:cd16159 161 FPLLTAfvlitaltiflllylGAVS-KRFFvfllilsllfislfflllitnryFNCI--LMRNHevveqpmSLENLT--Q 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 165 RISNRAVDFLQQpaRADEPFLMVISYDEPHHPFtcpveylekytdfyyelgeKAEDDLANKPEHhrlwaqampspvgddG 244
Cdd:cd16159 236 RLTKEAISFLER--NKERPFLLVMSFLHVHTAL-------------------FTSKKFKGRSKH---------------G 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 245 LYhhplyfacNDFV---DDQIGRVINAL-TPEQRENTWVIYTSDHG----------EMMGAHKLISKGAAM--YDDITRI 308
Cdd:cd16159 280 RY--------GDNVeemDWSVGQILDALdELGLKDNTFVYFTSDNGghleeisvggEYGGGNGGIYGGKKMggWEGGIRV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 309 PLIIRSPQGER--RQVDTPVSHIDLLPTMMALADIEKPE--ILPGENILAV---KEPR----------GVLVEFNRYeie 371
Cdd:cd16159 352 PTIVRWPGVIPpgSVIDEPTSLMDIFPTVAALAGAPLPSdrIIDGRDLMPLltgQEKRspheflfhycGAELHAVRY--- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 372 HDSFGG-----------FIPV-----RCWVTDDFKLVLNLFTSDELYDRRNDPNEMHNL-IDDIHFADVRSKMHDALLDY 434
Cdd:cd16159 429 RPRDGGavwkahyftpnFYPGtegccGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLdPTDEPYQEIIKKILEAVAEH 508
|
570
....*....|...
gi 446751221 435 MDKIRDPFRSYQW 447
Cdd:cd16159 509 QSSIEPVESQLSF 521
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-344 |
9.32e-30 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 119.95 E-value: 9.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLN---TQNIDSLAAEGIRFNSAYTcSPVCTPARAGLFTGIYANQSGpwTNNVAPGKN 80
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTG--LTTVGLPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 81 IS-------TMGRYFKDAGYHTCYIGKWHLDGHDYFgtgeCPPEWDADYWFDGANYlseltekeislwrnglnsvedlqa 153
Cdd:cd16142 78 PGglppwepTLAELLKDAGYATAQFGKWHLGDEDGR----LPTDHGFDEFYGNLYH------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 154 nHIDEtftwahRISNRAVDFLQQPARADEPFLMVISYDEPHHPfTCPveylekytdfyyelgekaEDDLANKPEHHRLWA 233
Cdd:cd16142 130 -TIDE------EIVDKAIDFIKRNAKADKPFFLYVNFTKMHFP-TLP------------------SPEFEGKSSGKGKYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 234 qampspvgdDGLYHHplyfacndfvDDQIGRVINALTPE-QRENTWVIYTSDHGEMM------------GAhklisKGAA 300
Cdd:cd16142 184 ---------DSMVEL----------DDHVGQILDALDELgIADNTIVIFTTDNGPEQdvwpdggytpfrGE-----KGTT 239
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446751221 301 MYDDItRIPLIIRSP---QGERRQVDTpVSHIDLLPTMMALADIEKP 344
Cdd:cd16142 240 WEGGV-RVPAIVRWPgkiKPGRVSNEI-VSHLDWFPTLAALAGAPDP 284
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-410 |
1.12e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 119.76 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQ---ATNMVGCYSGKPlNTQNIDSLAAEGIRFNSAYTcSPVCTPARAGLFTGIYANQSG-PWTNNVAPGK 79
Cdd:cd16154 1 PNILLIIADDQgldSSAQYSLSSDLP-VTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGKYGFRTGvLAVPDELLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 80 NISTMGRYFKDA---GYHTCYIGKWHLDGHDYfgTGECPPEWdaDYWFDGANylselteKEISLWRNGLNSVEDLQANHI 156
Cdd:cd16154 79 EETLLQLLIKDAttaGYSSAVIGKWHLGGNDN--SPNNPGGI--PYYAGILG-------GGVQDYYNWNLTNNGQTTNST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 157 DETFTwahRISNRAVDFLQQparADEPFLMVISYDEPHHPFTCPVEYLEKYTDfyyeLGEKAeDDLANKpehhrlwaqam 236
Cdd:cd16154 148 EYATT---KLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLPPAELHSRSL----LGDSA-DIEANP----------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 237 pspvgddglyhHPLYFACNDFVDDQIGRVINALTPEQRENTWVIYTSDHGEMMGA-HKLISKGAA---MYDDITRIPLII 312
Cdd:cd16154 206 -----------RPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGTPGQVvDLPYTRNHAkgsLYEGGINVPLIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 313 rSPQGERRQV---DTPVSHIDLLPTMMALADIEKPEI---------LPGENIlavkEPRgvlvEFNRYEIEHDSFGGFIP 380
Cdd:cd16154 275 -SGAGVERANereSALVNATDLYATIAELAGVDAAEIhdsvsfkplLSDVNA----STR----QYNYTEYESPTTTGWAT 345
|
410 420 430
....*....|....*....|....*....|
gi 446751221 381 VRcwvtDDFKLVLNLFTSDELYDRRNDPNE 410
Cdd:cd16154 346 RN----QYYKLIESENGQEELYDLINDPSE 371
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
3-375 |
3.81e-23 |
|
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: 101.01 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGcYSGKPLN--TQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPwTNNVAPGK- 79
Cdd:cd16161 1 KPNFLLLFADDLGWGDLG-ANWAPNAilTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 80 -----NISTMGRYFKDAGYHTCYIGKWHLDGHDYFgtgeCPPEWDADYWFdganylseltekeislwrnGLNSVEDLqan 154
Cdd:cd16161 79 gglplNETTLAEVLRQAGYATGMIGKWHLGQREAY----LPNSRGFDYYF-------------------GIPFSHDS--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 155 hidetfTWAHRISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPveylekytdfyyelgekaedDLANKPEHHRlwaq 234
Cdd:cd16161 133 ------SLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANL--------------------PRFQSPTSGR---- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 235 ampSPVGdDGLYHhplyfacndfVDDQIGRVINALTPEQ-RENTWVIYTSD---------------HGEMMGAHKLISKG 298
Cdd:cd16161 183 ---GPYG-DALQE----------MDDLVGQIMDAVKHAGlKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAK 248
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446751221 299 AAMYDDITRIPLIIRSPQ--GERRQVDTPVSHIDLLPTMMALADIEkpeiLPGENILAVKEPRGVLveFNRYEIEHDSF 375
Cdd:cd16161 249 ASTWEGGHREPAIVYWPGriPANSTSAALVSTLDIFPTVVALAGAS----LPPGRIYDGKDLSPVL--FGGSKTGHRCL 321
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
3-414 |
4.69e-23 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 101.35 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGCYsGKPlnTQN---IDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSG---------P 70
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASY-GHP--TQErgpIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGmyggtrvflP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 71 WTNNVAPgKNISTMGRYFKDAGYHTCYIGKWHL----------------DGHDYFGTgECP--PEWDADYW---FDGANy 129
Cdd:cd16160 78 WDIGGLP-KTEVTMAEALKEAGYTTGMVGKWHLginennhsdgahlpshHGFDFVGT-NLPftNSWACDDTgrhVDFPD- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 130 lseltEKEISLWRNGLNSVEDLQANHIDETFTwahrisNRAVDFLQQpaRADEPFLMVISYDEPHHPFTCPVEYLEK--- 206
Cdd:cd16160 155 -----RSACFLYYNDTIVEQPIQHEHLTETLV------GDAKSFIED--NQENPFFLYFSFPQTHTPLFASKRFKGKskr 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 207 --YTDFYYELGekaeddlankpehhrlWAqampspvgddglyhhplyfacndfvddqIGRVINALTPEQ-RENTWVIYTS 283
Cdd:cd16160 222 grYGDNINEMS----------------WA----------------------------VGEVLDTLVDTGlDQNTLVFFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 284 DHGEMM-----GAHKLISKG--AAMYDDITRIPLIIRSPQGERRQVDTP-VSHIDLLPTMMALADIEKPE--ILPGENIL 353
Cdd:cd16160 258 DHGPHVeycleGGSTGGLKGgkGNSWEGGIRVPFIAYWPGTIKPRVSHEvVSTMDIFPTFVDLAGGTLPTdrIYDGLSIT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 354 AV------KEPRGVL---------VEFNRYEI----EHDSFGGFIPVRCwvtDDFKLVLNLFTSDE-------------L 401
Cdd:cd16160 338 DLllgeadSPHDDILyyccsrlmaVRYGSYKIhfktQPLPSQESLDPNC---DGGGPLSDYIVCYDcedecvtkhnpplI 414
|
490
....*....|...
gi 446751221 402 YDRRNDPNEMHNL 414
Cdd:cd16160 415 FDVEKDPGEQYPL 427
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
2-366 |
2.95e-22 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 100.11 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 2 KRPNFLFIMTDTQATNMVGCYS-GKPLnTQNIDSLAAEGIRFNSAYtcSPVCTPARA--GLFTGIYANQSGPWTNNVApG 78
Cdd:COG1368 233 KKPNVVVILLESFSDFFIGALGnGKDV-TPFLDSLAKESLYFGNFY--SQGGRTSRGefAVLTGLPPLPGGSPYKRPG-Q 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 79 KNISTMGRYFKDAGYHTCYIgkwHldGHD-YFgtgecppeWDADYWFDGANY-----LSELTEKEISLWrnGLNsvedlq 152
Cdd:COG1368 309 NNFPSLPSILKKQGYETSFF---H--GGDgSF--------WNRDSFYKNLGFdefydREDFDDPFDGGW--GVS------ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 153 anhiDETFTwahrisNRAVDFLQQparADEPFL-MVISYdEPHHPFTCPVEYlekytdfyYELGEKAEDDLANkpehhrl 231
Cdd:COG1368 368 ----DEDLF------DKALEELEK---LKKPFFaFLITL-SNHGPYTLPEED--------KKIPDYGKTTLNN------- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 232 waqampspvgddglYHHPLYFAcndfvDDQIGRVINALtpEQR---ENTWVIYTSDHGEMMGAHKLISKGAAMYdditRI 308
Cdd:COG1368 419 --------------YLNAVRYA-----DQALGEFIEKL--KKSgwyDNTIFVIYGDHGPRSPGKTDYENPLERY----RV 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 309 PLIIRSPQGER-RQVDTPVSHIDLLPTMMALADIEKPEILP-GENILAVKEPRGVLVEFN 366
Cdd:COG1368 474 PLLIYSPGLKKpKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRDLLSPDTDPFAFRNGG 533
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
4-353 |
7.79e-22 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 96.84 E-value: 7.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGKNIST 83
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 84 MGRYFKDAGYHTCYIGKwhLDghdyFGTGECPPEWDADYWFDGANYLseLTEKEislwRNGLNSVEDLQANHIDETfTWA 163
Cdd:cd16171 81 WMDRLEKHGYHTQKYGK--LD----YTSGHHSVSNRVEAWTRDVPFL--LRQEG----RPTVNLVGDRSTVRVMLK-DWQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 164 hrISNRAVDFLQQPA-RADEPFLMVISYDEPHhPFtcPVEYL-------EKYTDFYYELGekAEDDlankpehhrlwaqA 235
Cdd:cd16171 148 --NTDKAVHWIRKEApNLTQPFALYLGLNLPH-PY--PSPSMgenfgsiRNIRAFYYAMC--AETD-------------A 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 236 MpspvgddglyhhplyfacndfvddqIGRVINAL-TPEQRENTWVIYTSDHGEMMGAHKLISKgAAMYDDITRIPLIIRS 314
Cdd:cd16171 208 M-------------------------LGEIISALkDTGLLDKTYVFFTSDHGELAMEHRQFYK-MSMYEGSSHVPLLIMG 261
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446751221 315 PQ-GERRQVDTPVSHIDLLPTMMALADIEKPEILPGENIL 353
Cdd:cd16171 262 PGiKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLL 301
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
4-346 |
1.60e-21 |
|
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: 97.13 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNVAPGK---- 79
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSrggl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 80 --NISTMGRYFKDAGYHTCYIGKWHL----DG---------HDYFGT----GECPPEWDADYWFDGANY-LSELTEKEIS 139
Cdd:cd16158 82 plNETTIAEVLKTVGYQTAMVGKWHLgvglNGtylpthqgfDHYLGIpyshDQGPCQNLTCFPPNIPCFgGCDQGEVPCP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 140 LWRNglNSVEDLQANHIDetftWAHRISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYLEkytdfyyelgekae 219
Cdd:cd16158 162 LFYN--ESIVQQPVDLLT----LEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAG-------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 220 ddlankpehhrlwaQAMPSPVGDdglyhhplyfACNDFvDDQIGRVINALTPEQ-RENTWVIYTSDHG-EMM-----GAH 292
Cdd:cd16158 222 --------------RSSRGPFGD----------ALAEL-DGSVGELLQTLKENGiDNNTLVFFTSDNGpSTMrksrgGNA 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 293 KLISKG-AAMYDDITRIPLIIRSPQgerrQVDTPVSH-----IDLLPTMMALADIEKPEI 346
Cdd:cd16158 277 GLLKCGkGTTYEGGVREPAIAYWPG----RIKPGVTHelastLDILPTIAKLAGAPLPNV 332
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
4-340 |
1.32e-19 |
|
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: 88.89 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARA--GLFTGIYANQSGPWTNNVAPGKNI 81
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 82 STMGRYFKDAGYHTCYIgkwhldgHDYfgtgecppewDADYW----------FDGANYLSELTEKEISLWRNGLNsvedl 151
Cdd:cd16015 81 PSLPSILKEQGYETIFI-------HGG----------DASFYnrdsvypnlgFDEFYDLEDFPDDEKETNGWGVS----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 152 qanhiDETFTwahrisNRAVDFLQQpaRADEP-FLMVISYDEpHHPFTcpveYLEKYTDFYyeLGEKAEDDLANKpehhr 230
Cdd:cd16015 139 -----DESLF------DQALEELEE--LKKKPfFIFLVTMSN-HGPYD----LPEEKKDEP--LKVEEDKTELEN----- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 231 lwaqampspvgddglyhhplYFACNDFVDDQIGRVINALtpEQR---ENTWVIYTSDHGEMMGAHKLISKgaAMYDDITR 307
Cdd:cd16015 194 --------------------YLNAIHYTDKALGEFIEKL--KKSglyENTIIVIYGDHLPSLGSDYDETD--EDPLDLYR 249
|
330 340 350
....*....|....*....|....*....|....
gi 446751221 308 IPLIIRSPQGER-RQVDTPVSHIDLLPTMMALAD 340
Cdd:cd16015 250 TPLLIYSPGLKKpKKIDRVGSQIDIAPTLLDLLG 283
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
3-355 |
2.49e-15 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 78.28 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 3 RPNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNvAPGKNIS 82
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTN-AHARNAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 83 T----MG----------RYFKDAGYHTCYIGKWHLdGHDyfgTGECPPEWDADYWFDGAN-YLSELTEKE---ISLWRNG 144
Cdd:cd16157 80 TpqniVGgipdseillpELLKKAGYRNKIVGKWHL-GHR---PQYHPLKHGFDEWFGAPNcHFGPYDNKAypnIPVYRDW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 145 L---NSVEDLQANHIDETFTWAHRISNRAVDFLQQPARADEPFLMVISYDEPHHPFTCPVEYL-----EKYTDFYYELge 216
Cdd:cd16157 156 EmigRYYEEFKIDKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLgtsqrGLYGDAVMEL-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 217 kaeddlankpehhrlwaqampspvgddglyhhplyfacndfvDDQIGRVINALTPEQ-RENTWVIYTSDHGEMMGAHKLI 295
Cdd:cd16157 234 ------------------------------------------DSSVGKILESLKSLGiENNTFVFFSSDNGAALISAPEQ 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446751221 296 --SKGAAM------YDDITRIPLIIRSP-QGERRQVDTPVSHI-DLLPTMMALADIEKPE--ILPGENILAV 355
Cdd:cd16157 272 ggSNGPFLcgkqttFEGGMREPAIAWWPgHIKPGQVSHQLGSLmDLFTTSLALAGLPIPSdrAIDGIDLLPV 343
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
145-336 |
3.03e-15 |
|
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: 78.41 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 145 LNSVEDLQANHIDETFTWAHRISNRAVDFLQQPArADEPFLMVISYDEPHhPFTCPVEYLEKYTDFYYELGEKAEDDLAN 224
Cdd:COG3083 345 FSDVSLPRLHTPGGPAQRDRQITAQWLQWLDQRD-SDRPWFSYLFLDAPH-AYSFPADYPKPFQPSEDCNYLALDNESDP 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 225 KPEHHRlwaqampspvgddglYHHPLYFacndfVDDQIGRVINALtpEQR---ENTWVIYTSDHGEMMGAHKLISKGAAM 301
Cdd:COG3083 423 TPFKNR---------------YRNAVHY-----VDSQIGRVLDTL--EQRgllENTIVIITADHGEEFNENGQNYWGHNS 480
|
170 180 190
....*....|....*....|....*....|....*..
gi 446751221 302 Y--DDITRIPLIIRSPQGERRQVDTPVSHIDLLPTMM 336
Cdd:COG3083 481 NfsRYQLQVPLVIHWPGTPPQVISKLTSHLDIVPTLM 517
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
2-342 |
3.79e-11 |
|
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: 63.80 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 2 KRPNFLFIMTDT-QATNMvGCYsGKPLNTQ-NIDSLAAEGIRFNSAYTCSPVCTPARAGLFTGIYANQSGPWTNNvapgK 79
Cdd:cd16017 1 KPKNVVLVIGESaRRDHM-SLY-GYPRDTTpFLSKLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAYYQ----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 80 NISTMgryFKDAGYHTcyigkWHLDGHDYFGTGecppewdadywfdgANYLSELTEKEISLWRNGLNSVEdlqaNHIDET 159
Cdd:cd16017 75 NLIDL---AKKAGYKT-----YWISNQGGCGGY--------------DTRISAIAKIETVFTNKGSCNSS----NCYDEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 160 FtwahrisnraVDFLQQ-PARADEPFLMVIsydepH----HPftcpvEYLEKYtdfyyelgekaeddlankPEHHRLWAQ 234
Cdd:cd16017 129 L----------LPLLDEaLADSSKKKLIVL-----HlmgsHG-----PYYDRY------------------PEEFAKFTP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 235 AMPSPVGDDG------------LYhhplyfacNDFVddqIGRVINALTpEQRENTWVIYTSDHGEMMGAHKLISKGA-AM 301
Cdd:cd16017 171 DCDNELQSCSkeelinaydnsiLY--------TDYV---LSQIIERLK-KKDKDAALIYFSDHGESLGENGLYLHGApYA 238
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446751221 302 YDDITRIPLIIRSPQGERRQ---------VDTPVSHIDLLPTMMALADIE 342
Cdd:cd16017 239 PKEQYHVPFIIWSSDSYKQRypverlranKDRPFSHDNLFHTLLGLLGIK 288
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
4-339 |
6.10e-11 |
|
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: 62.44 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 4 PNFLFIMTDTQATNMVGCYSGKPLNTQNIDSLAAEGIRFNsAYTCSPVC--TPARAGLFTGIYANQSGPWTNNVApgkni 81
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 82 stmgryfkdagyhtcyigkwhldghdyfgtGECPPEWDADYWFDGANYLSELTEKEISlwrnglnsvedlqanhidetFT 161
Cdd:cd00016 75 ------------------------------DPELPSRAAGKDEDGPTIPELLKQAGYR--------------------TG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 162 WAHrisnrAVDFLQQPARADePFLMVISYDEPHHPFtcpveylekytdfyyelgekaeddlankpeHHRLWaqampspvg 241
Cdd:cd00016 105 VIG-----LLKAIDETSKEK-PFVLFLHFDGPDGPG------------------------------HAYGP--------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 242 ddglyHHPLYFACNDFVDDQIGRVINALtPEQR--ENTWVIYTSDHGEMMGAH---KLISKGAAMYDDITRIPLIIRSPQ 316
Cdd:cd00016 140 -----NTPEYYDAVEEIDERIGKVLDAL-KKAGdaDDTVIIVTADHGGIDKGHggdPKADGKADKSHTGMRVPFIAYGPG 213
|
330 340
....*....|....*....|....
gi 446751221 317 GERRQV-DTPVSHIDLLPTMMALA 339
Cdd:cd00016 214 VKKGGVkHELISQYDIAPTLADLL 237
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
385-440 |
1.84e-08 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 52.25 E-value: 1.84e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446751221 385 VTDDFKLVLNLFTSD--ELYDRRNDPNEMHNLIDDIHFADVRSKMHDALLDYMDKIRD 440
Cdd:pfam16347 46 RTERYKLIHFYNDIDewELYDLQKDPKEMNNVYGDPEYAEVQAELKEELEELRKQYKD 103
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
250-354 |
4.78e-06 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 49.08 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 250 LYfacNDFVddqIGRVINAL-TPEQRENTWVIYTSDHGEMMGAHKLISKGA--AMYDDI-TRIPLII-RSPQGE------ 318
Cdd:COG2194 419 LY---TDYV---LSQVIDLLkAKQDRYDTAMLYVSDHGESLGENGLYLHGTpyAIAPDEqTHVPMIMwLSDGYAqrygid 492
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446751221 319 ----RRQVDTPVSHIDLLPTMMALADIEKPEILPGENILA 354
Cdd:COG2194 493 faclKARADKPYSHDNLFHTLLGLLDVRTSVYDPELDILA 532
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
258-353 |
3.52e-05 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 46.25 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 258 VDDQIGRVINALtpeQRENTWVIYTSDHG--EMMgahkliskgaamYDDIT----------RIPLIIRSPQGERRQVDTP 325
Cdd:cd16010 412 VDECLGRIVEAV---LENGGTLLITADHGnaEEM------------IDPETggphtahttnPVPFIIVDPGLKRKLLKDG 476
|
90 100
....*....|....*....|....*....
gi 446751221 326 V-ShiDLLPTMMALADIEKPEILPGENIL 353
Cdd:cd16010 477 GlA--DVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
258-353 |
2.27e-03 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 40.47 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446751221 258 VDDQIGRVINALtpeQRENTWVIYTSDHG--EMMgahkliskgaamYDDIT----------RIPLIIrspqgerrqVDTP 325
Cdd:PRK05434 417 VDECLGRVVDAV---LKVGGTLLITADHGnaEQM------------IDPETgqphtahttnPVPFIL---------VGGK 472
|
90 100 110
....*....|....*....|....*....|....
gi 446751221 326 VSHI------DLLPTMMALADIEKPEILPGENIL 353
Cdd:PRK05434 473 ALRLeggklaDIAPTILDLLGLEQPAEMTGKSLI 506
|
|
| |
