|
Name |
Accession |
Description |
Interval |
E-value |
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
19-671 |
1.04e-58 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 207.58 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 19 TFFMSLLFVFNRIGFILYTGYYKhalknpvFDEIIKTLFNGARYdnrvVSSLAILFIIIGLLGLLAPKHQTKMLNIVAYF 98
Cdd:COG1368 1 FFLLFLLLLSLRLVFLLFNFDLS-------LGEILQAFLYGLRF----ILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 99 SIAIILFLNIANIVYYGIYGNVFDENLLEFLhEDTLTILKMSGEYPIFSSFSLFVILGVLISFIYFklqnalFKPKNVYQ 178
Cdd:COG1368 70 VLLLLLLLLVADILYYRFFGDRLNFSDLDYL-GDTGEVLGSLLSSYDLLLLLDLLLLLLLLLLLYR------LLKKLRKS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 179 ATKPLKTFILFALFSLTqMFYINAQLSFvgaSLDLSIEPAKDPFLMKITPGAFRNLYLLARNYRqshnlKFSDFAKETPL 258
Cdd:COG1368 143 LPWRKRLALLLLLLALL-LLGIRLGEDR---PLNLSDAFSRNNFVNELGLNGPYSFYDALRNNK-----APATYSEEEAL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 259 EVAknyfhlkenpsnNLYELLSQTSHNHSNQTIQHVFYIVSESLSSWHFDPKFDAIGLTSALQDLVKkeHAHMLSAFIES 338
Cdd:COG1368 214 EIK------------KYLKSNRPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAK--ESLYFGNFYSQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 339 APRTVKSLDVQITGLPYINDNNLVNSGViLPSFPmAIGNITKTLGYKNNFYYGGSGIWNKLTSFTKKQGFHALYFNNHll 418
Cdd:COG1368 280 GGRTSRGEFAVLTGLPPLPGGSPYKRPG-QNNFP-SLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDRED-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 419 efvknkpYPKPIESNWGVHDNILFDYILENTNPNEK-TFSMVMTLSNHAiknvnlkAFGVPLEKiqqfvEKTPKSENLPD 497
Cdd:COG1368 356 -------FDDPFDGGWGVSDEDLFDKALEELEKLKKpFFAFLITLSNHG-------PYTLPEED-----KKIPDYGKTTL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 498 ANSLGHIYWYDKVIVSFIKKASQK--FPNSLFIITGDHFDRSYEYAKNDLYIIK-SVPLILFAPTL-KPKKISQVGSHLD 573
Cdd:COG1368 417 NNYLNAVRYADQALGEFIEKLKKSgwYDNTIFVIYGDHGPRSPGKTDYENPLERyRVPLLIYSPGLkKPKVIDTVGSQID 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 574 IAPTIIELVAPEGFQFVSFGKPLFSnnttnpPSHPNYALGYEAIATKDYFYnpslglrYLNENPKEPEDKQnDKIEASKF 653
Cdd:COG1368 497 IAPTLLDLLGIDYPSYYAFGRDLLS------PDTDPFAFRNGGFITDDYVY-------VLKTGELTEEDKE-LEEEALAY 562
|
650
....*....|....*...
gi 1151269616 654 YQqleslkaLSYYLLYHG 671
Cdd:COG1368 563 LQ-------LSDYLYGND 573
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
292-581 |
2.20e-45 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 163.75 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 292 QHVFYIVSESLSSWHFDPKFDAIGLTSALQDLVkkEHAHMLSAFIESAPRTVKSLDVQITGLPYINDNNLVNSGVILPSF 371
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLA--EEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 372 PMAIGNITKTLGYKNNFYYGGSGIWNKLTSFtKKQGFHALYFNNHLLEFVKNKPYPKPIESNWGVHDNILFDYILENTNP 451
Cdd:pfam00884 79 EPSLPDLLKRAGYNTGAIGKWHLGWYNNQSP-CNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 452 NEK-TFSMVMTLSNHAiknvnlkafgvPLEKIQQFVEKTPKSENLPD------ANSLGHIYWYDKVIVSFIKKA--SQKF 522
Cdd:pfam00884 158 NDKpFFLVLHTLGSHG-----------PPYYPDRYPEKYATFKPSSCseeqllNSYDNTLLYTDDAIGRVLDKLeeNGLL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 523 PNSLFIITGDHFDRSYEyAKNDLYIIKS---------VPLILFAPTLKPK--KISQVGSHLDIAPTIIEL 581
Cdd:pfam00884 227 DNTLVVYTSDHGESLGE-GGGYLHGGKYdnapeggyrVPLLIWSPGGKAKgqKSEALVSHVDLFPTILDL 295
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
292-581 |
2.30e-39 |
|
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: 146.29 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 292 QHVFYIVSESLSSWHFDPKFDAIGLTSALQDLVKKEHA--HMLSAfiESAPRTVKSLDVQITGLPYINDNNLVNSGVILP 369
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYfgNFYSP--GFGGGTANGEFEVLTGLPPLPLGSGSYTLYKLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 370 SFPmAIGNITKTLGYKNNFYYGGSGIWNKLTSFTKKQGFHALYFNNHLlefvknkPYPKPIESNWGVHDNILFDYILE-- 447
Cdd:cd16015 79 PLP-SLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDF-------PDDEKETNGWGVSDESLFDQALEel 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 448 NTNPNEKTFSMVMTLSNHAiknvnlkAFGVPLEKIQQFVEKTPKSENLpdANSLGHIYWYDKVIVSFIKKASQK--FPNS 525
Cdd:cd16015 151 EELKKKPFFIFLVTMSNHG-------PYDLPEEKKDEPLKVEEDKTEL--ENYLNAIHYTDKALGEFIEKLKKSglYENT 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 526 LFIITGDH---FDRSYEYAKNDLYIIKSVPLILFAPTLK-PKKISQVGSHLDIAPTIIEL 581
Cdd:cd16015 222 IIVIYGDHlpsLGSDYDETDEDPLDLYRTPLLIYSPGLKkPKKIDRVGSQIDIAPTLLDL 281
|
|
| PRK12363 |
PRK12363 |
phosphoglycerol transferase I; Provisional |
237-606 |
2.01e-09 |
|
phosphoglycerol transferase I; Provisional
Pssm-ID: 171438 Cd Length: 703 Bit Score: 60.69 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 237 LARNYRQSHN-LKFSDFAKetpleVAKNYfhlkENPsnnlyellsqtshNHSNQTIQHVFYIVSESLSSWHFDPKFdAIG 315
Cdd:PRK12363 123 LYRDGKRLYYqLRPVDFAT-----VAPEY----QVP-------------QQPLQKRKNIVWIYGESLERTYFDEDV-FPG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 316 LTSALQDLVKKEHAHMLSAFIESAPRTVKSLDVQITGLPYI----NDNNLVNSGVILPSfPMAIGNITKTLGYKNNFYYG 391
Cdd:PRK12363 180 LMPNLTRLATEAVDVRNLASTEGSGWTIAGMVASMCGVPLTtaqgDENSMDRMGHFLPE-ARCLGDYLKDQGYTNHYVGG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 392 GSGIWNKLTSFTKKQGFHALYFNNHlleFVKNKPYPKPIESNWGVHDNILFDYI---LENTNPNEKTFsMVMTLSnhaiK 468
Cdd:PRK12363 259 ADASFAGKGKFLSSHGFDEVHDVNY---FLHDKGVAPKHFSAWGVHDDVLLDDAydeFETLSRAGQPF-MLTTLT----M 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 469 NVNLKAFGVPLekiqqfVEKTPKSEN-LPDANSLGHIYWYDKVIVSFIKK--ASQKFPNSLFIITGDHF----DRSYEYA 541
Cdd:PRK12363 331 DTHHPAGHLPS------ACKGQRYDSpLGDIGMLHAIKCSDRLIGQLVDRirNSRYGKNTIIVIASDHLampnDLSDVLT 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151269616 542 KNdlyiiKSVPLILF-APTLKPKKIS-QVGSHLDIAPTIIELVAPEGFQFvSFGKPLFSNNTtnPPS 606
Cdd:PRK12363 405 KQ-----KRENLLLFlGKDIAPQQVVtRAGTTLDSGATLLQLLEPGMRTL-GFGRSLLADDA--PPS 463
|
|
| exo_archaeo |
TIGR04178 |
exosortase/archaeosortase family protein; This model represents the most conserved region of ... |
67-166 |
1.69e-03 |
|
exosortase/archaeosortase family protein; This model represents the most conserved region of the multitransmembrane protein family of exosortases and archaeosortases. The region includes nearly invariant motifs at the ends of three predicted transmembrane helices on the extracytoplasmic face: a Cys (often Cys-Xaa-Gly), Asn-Xaa-Xaa-Arg, and His. This model is much broader than the bacterial exosortase model (TIGR02602), and has in intended scope similar to (or broader than) pfam09721.
Pssm-ID: 275031 [Multi-domain] Cd Length: 97 Bit Score: 38.36 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 67 VSSLAILFIIIGLLGLLAPKHQTKMLNIVAyFSIAIILFLNIANIVYYGIYGNVFDENLLEFLHEdtltilkmsgeypiF 146
Cdd:TIGR04178 10 LRSLILLLALGLLFAYLFPRSLRRKLLLLL-LGVPIIYLANILRIVLLILLGYYFGPEAFEFAHD--------------I 74
|
90 100
....*....|....*....|
gi 1151269616 147 SSFSLFVILGVLISFIYFKL 166
Cdd:TIGR04178 75 LGWLLFLLVALLLLLLVLWL 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
19-671 |
1.04e-58 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 207.58 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 19 TFFMSLLFVFNRIGFILYTGYYKhalknpvFDEIIKTLFNGARYdnrvVSSLAILFIIIGLLGLLAPKHQTKMLNIVAYF 98
Cdd:COG1368 1 FFLLFLLLLSLRLVFLLFNFDLS-------LGEILQAFLYGLRF----ILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 99 SIAIILFLNIANIVYYGIYGNVFDENLLEFLhEDTLTILKMSGEYPIFSSFSLFVILGVLISFIYFklqnalFKPKNVYQ 178
Cdd:COG1368 70 VLLLLLLLLVADILYYRFFGDRLNFSDLDYL-GDTGEVLGSLLSSYDLLLLLDLLLLLLLLLLLYR------LLKKLRKS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 179 ATKPLKTFILFALFSLTqMFYINAQLSFvgaSLDLSIEPAKDPFLMKITPGAFRNLYLLARNYRqshnlKFSDFAKETPL 258
Cdd:COG1368 143 LPWRKRLALLLLLLALL-LLGIRLGEDR---PLNLSDAFSRNNFVNELGLNGPYSFYDALRNNK-----APATYSEEEAL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 259 EVAknyfhlkenpsnNLYELLSQTSHNHSNQTIQHVFYIVSESLSSWHFDPKFDAIGLTSALQDLVKkeHAHMLSAFIES 338
Cdd:COG1368 214 EIK------------KYLKSNRPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAK--ESLYFGNFYSQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 339 APRTVKSLDVQITGLPYINDNNLVNSGViLPSFPmAIGNITKTLGYKNNFYYGGSGIWNKLTSFTKKQGFHALYFNNHll 418
Cdd:COG1368 280 GGRTSRGEFAVLTGLPPLPGGSPYKRPG-QNNFP-SLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDRED-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 419 efvknkpYPKPIESNWGVHDNILFDYILENTNPNEK-TFSMVMTLSNHAiknvnlkAFGVPLEKiqqfvEKTPKSENLPD 497
Cdd:COG1368 356 -------FDDPFDGGWGVSDEDLFDKALEELEKLKKpFFAFLITLSNHG-------PYTLPEED-----KKIPDYGKTTL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 498 ANSLGHIYWYDKVIVSFIKKASQK--FPNSLFIITGDHFDRSYEYAKNDLYIIK-SVPLILFAPTL-KPKKISQVGSHLD 573
Cdd:COG1368 417 NNYLNAVRYADQALGEFIEKLKKSgwYDNTIFVIYGDHGPRSPGKTDYENPLERyRVPLLIYSPGLkKPKVIDTVGSQID 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 574 IAPTIIELVAPEGFQFVSFGKPLFSnnttnpPSHPNYALGYEAIATKDYFYnpslglrYLNENPKEPEDKQnDKIEASKF 653
Cdd:COG1368 497 IAPTLLDLLGIDYPSYYAFGRDLLS------PDTDPFAFRNGGFITDDYVY-------VLKTGELTEEDKE-LEEEALAY 562
|
650
....*....|....*...
gi 1151269616 654 YQqleslkaLSYYLLYHG 671
Cdd:COG1368 563 LQ-------LSDYLYGND 573
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
292-581 |
2.20e-45 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 163.75 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 292 QHVFYIVSESLSSWHFDPKFDAIGLTSALQDLVkkEHAHMLSAFIESAPRTVKSLDVQITGLPYINDNNLVNSGVILPSF 371
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLA--EEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 372 PMAIGNITKTLGYKNNFYYGGSGIWNKLTSFtKKQGFHALYFNNHLLEFVKNKPYPKPIESNWGVHDNILFDYILENTNP 451
Cdd:pfam00884 79 EPSLPDLLKRAGYNTGAIGKWHLGWYNNQSP-CNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 452 NEK-TFSMVMTLSNHAiknvnlkafgvPLEKIQQFVEKTPKSENLPD------ANSLGHIYWYDKVIVSFIKKA--SQKF 522
Cdd:pfam00884 158 NDKpFFLVLHTLGSHG-----------PPYYPDRYPEKYATFKPSSCseeqllNSYDNTLLYTDDAIGRVLDKLeeNGLL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 523 PNSLFIITGDHFDRSYEyAKNDLYIIKS---------VPLILFAPTLKPK--KISQVGSHLDIAPTIIEL 581
Cdd:pfam00884 227 DNTLVVYTSDHGESLGE-GGGYLHGGKYdnapeggyrVPLLIWSPGGKAKgqKSEALVSHVDLFPTILDL 295
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
292-581 |
2.30e-39 |
|
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: 146.29 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 292 QHVFYIVSESLSSWHFDPKFDAIGLTSALQDLVKKEHA--HMLSAfiESAPRTVKSLDVQITGLPYINDNNLVNSGVILP 369
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYfgNFYSP--GFGGGTANGEFEVLTGLPPLPLGSGSYTLYKLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 370 SFPmAIGNITKTLGYKNNFYYGGSGIWNKLTSFTKKQGFHALYFNNHLlefvknkPYPKPIESNWGVHDNILFDYILE-- 447
Cdd:cd16015 79 PLP-SLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDF-------PDDEKETNGWGVSDESLFDQALEel 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 448 NTNPNEKTFSMVMTLSNHAiknvnlkAFGVPLEKIQQFVEKTPKSENLpdANSLGHIYWYDKVIVSFIKKASQK--FPNS 525
Cdd:cd16015 151 EELKKKPFFIFLVTMSNHG-------PYDLPEEKKDEPLKVEEDKTEL--ENYLNAIHYTDKALGEFIEKLKKSglYENT 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 526 LFIITGDH---FDRSYEYAKNDLYIIKSVPLILFAPTLK-PKKISQVGSHLDIAPTIIEL 581
Cdd:cd16015 222 IIVIYGDHlpsLGSDYDETDEDPLDLYRTPLLIYSPGLKkPKKIDRVGSQIDIAPTLLDL 281
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
524-663 |
1.25e-09 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 60.66 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 524 NSLFIITGDH----FDRSYEYAKNDLY--IIKsVPLILFAP-TLKPKKIS-QVGSHLDIAPTIIELV---APEGFQFVSF 592
Cdd:COG3119 228 NTIVVFTSDNgpslGEHGLRGGKGTLYegGIR-VPLIVRWPgKIKAGSVSdALVSLIDLLPTLLDLAgvpIPEDLDGRSL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 593 gKPLFSNNTTNPP----SHPNYALGYEAIATKDYFYnpslgLRYLNENPkEPE--DKQNDKIE----ASKFYQQLESLKA 662
Cdd:COG3119 307 -LPLLTGEKAEWRdylyWEYPRGGGNRAIRTGRWKL-----IRYYDDDG-PWElyDLKNDPGEtnnlAADYPEVVAELRA 379
|
.
gi 1151269616 663 L 663
Cdd:COG3119 380 L 380
|
|
| PRK12363 |
PRK12363 |
phosphoglycerol transferase I; Provisional |
237-606 |
2.01e-09 |
|
phosphoglycerol transferase I; Provisional
Pssm-ID: 171438 Cd Length: 703 Bit Score: 60.69 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 237 LARNYRQSHN-LKFSDFAKetpleVAKNYfhlkENPsnnlyellsqtshNHSNQTIQHVFYIVSESLSSWHFDPKFdAIG 315
Cdd:PRK12363 123 LYRDGKRLYYqLRPVDFAT-----VAPEY----QVP-------------QQPLQKRKNIVWIYGESLERTYFDEDV-FPG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 316 LTSALQDLVKKEHAHMLSAFIESAPRTVKSLDVQITGLPYI----NDNNLVNSGVILPSfPMAIGNITKTLGYKNNFYYG 391
Cdd:PRK12363 180 LMPNLTRLATEAVDVRNLASTEGSGWTIAGMVASMCGVPLTtaqgDENSMDRMGHFLPE-ARCLGDYLKDQGYTNHYVGG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 392 GSGIWNKLTSFTKKQGFHALYFNNHlleFVKNKPYPKPIESNWGVHDNILFDYI---LENTNPNEKTFsMVMTLSnhaiK 468
Cdd:PRK12363 259 ADASFAGKGKFLSSHGFDEVHDVNY---FLHDKGVAPKHFSAWGVHDDVLLDDAydeFETLSRAGQPF-MLTTLT----M 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 469 NVNLKAFGVPLekiqqfVEKTPKSEN-LPDANSLGHIYWYDKVIVSFIKK--ASQKFPNSLFIITGDHF----DRSYEYA 541
Cdd:PRK12363 331 DTHHPAGHLPS------ACKGQRYDSpLGDIGMLHAIKCSDRLIGQLVDRirNSRYGKNTIIVIASDHLampnDLSDVLT 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151269616 542 KNdlyiiKSVPLILF-APTLKPKKIS-QVGSHLDIAPTIIELVAPEGFQFvSFGKPLFSNNTtnPPS 606
Cdd:PRK12363 405 KQ-----KRENLLLFlGKDIAPQQVVtRAGTTLDSGATLLQLLEPGMRTL-GFGRSLLADDA--PPS 463
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
494-631 |
4.19e-06 |
|
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: 49.43 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 494 NLPD--------ANSLGHIYWYDKVIVSFIK--KASQKFPNSLFIITGDH---FDRS----YEYAkndlyiIKsVPLILF 556
Cdd:cd16027 177 YLPDtpevredlADYYDEIERLDQQVGEILDelEEDGLLDNTIVIFTSDHgmpFPRAkgtlYDSG------LR-VPLIVR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 557 AP-TLKPKKISQ--VgSHLDIAPTIIELV---APEGFQfvsfGKPLFSNNTTNPPSHPNYALGyeAIATKDYFYNPSLGL 630
Cdd:cd16027 250 WPgKIKPGSVSDalV-SFIDLAPTLLDLAgiePPEYLQ----GRSFLPLLKGEKDPGRDYVFA--ERDRHDETYDPIRSV 322
|
.
gi 1151269616 631 R 631
Cdd:cd16027 323 R 323
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
524-598 |
7.86e-06 |
|
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: 47.93 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 524 NSLFIITGDH----FDRSYeYAKN--DLY--IIKsVPLILFAPTLKP-KKISQVGSHLDIAPTIIELV---APEGFQfvs 591
Cdd:cd16148 191 DTLVIVTSDHgeefGEHGL-YWGHgsNLYdeQLH-VPLIIRWPGKEPgKRVDALVSHIDIAPTLLDLLgvePPDYSD--- 265
|
....*..
gi 1151269616 592 fGKPLFS 598
Cdd:cd16148 266 -GRSLLP 271
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
551-662 |
1.17e-04 |
|
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: 45.21 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 551 VPLILFAPTLKPK--KISQVGSHLDIAPTIIELV---APEGFQFVSFgKPLFSNNT-------------TNPPSHPNYAl 612
Cdd:cd16031 296 VPLIIRDPRLIKAgtVVDALVLNIDFAPTILDLAgvpIPEDMQGRSL-LPLLEGEKpvdwrkefyyeyyEEPNFHNVPT- 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1151269616 613 gYEAIATKDYFYnpslgLRYLNENPKEpE--DKQNDKIEA------SKFYQQLESLKA 662
Cdd:cd16031 374 -HEGVRTERYKY-----IYYYGVWDEE-ElyDLKKDPLELnnlandPEYAEVLKELRK 424
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
551-649 |
3.10e-04 |
|
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: 43.72 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 551 VPLILFAP--TLKPKKISQVGSHLDIAPTIIELV---APEGFQFVSFgKPLFSNNTTNPP-----SHPNYALGYEAIATK 620
Cdd:cd16030 320 VPLIIRAPgvTKPGKVTDALVELVDIYPTLAELAglpAPPCLEGKSL-VPLLKNPSAKWKdaafsQYPRPSIMGYSIRTE 398
|
90 100 110
....*....|....*....|....*....|..
gi 1151269616 621 DYFYNpslglRYLNENPKEPE---DKQNDKIE 649
Cdd:cd16030 399 RYRYT-----EWVDFDKVGAEelyDHKNDPNE 425
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
524-588 |
4.82e-04 |
|
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: 42.04 E-value: 4.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151269616 524 NSLFIITGDH----FDRSYEYAKNDLY--IIKsVPLILFAPTLKP--KKISQVGSHLDIAPTIIELV---APEGFQ 588
Cdd:cd16022 159 NTLIVFTSDHgdmlGDHGLRGKKGSLYegGIR-VPFIVRWPGKIPagQVSDALVSLLDLLPTLLDLAgiePPEGLD 233
|
|
| PRK03776 |
PRK03776 |
phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase; |
371-533 |
5.46e-04 |
|
phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase;
Pssm-ID: 179648 Cd Length: 762 Bit Score: 43.17 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 371 FPMAI--GNITKTLGYKNNFYYGGSGIWNKLTSFTKKQGFHALYFNNHLLEFVKNKPYpkpiESNWGVHDNILFDYI--- 445
Cdd:PRK03776 240 FPQNIclGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDHLYGSEELKSVVADPHY----RNDWGFYDDTVLDEAwkk 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 446 LENTNPNEKTFSM-VMTLSNHAIK-----NVNLKAFGVPLEKIQQFVEKTPKSENlpdanslghiywydkvIVSFIKK-- 517
Cdd:PRK03776 316 FEELSRSGQRFSLfTLTVDTHHPDgfisrTCNRKSYDFDGKPNQSFSAVSCSQEN----------------IAALINKik 379
|
170
....*....|....*.
gi 1151269616 518 ASQKFPNSLFIITGDH 533
Cdd:PRK03776 380 ASPWFKNTVIVVSSDH 395
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
524-581 |
5.51e-04 |
|
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: 42.57 E-value: 5.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 524 NSLFIITGDH----------FDRS-YEYAKndlyiikSVPLILFAPTL-KPKKISQVGSHLDIAPTIIEL 581
Cdd:cd16032 192 DTIVIFTSDHgdmlgerglwYKMSfFEGSA-------RVPLIISAPGRfAPRRVAEPVSLVDLLPTLVDL 254
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
517-580 |
9.39e-04 |
|
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: 42.20 E-value: 9.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151269616 517 KASQKFPNSLFIITGDHfdrSYEYAKNDL-----------YIIkSVPLILFAPTLKPKKISQVGSHLDIAPTIIE 580
Cdd:COG3083 448 EQRGLLENTIVIITADH---GEEFNENGQnywghnsnfsrYQL-QVPLVIHWPGTPPQVISKLTSHLDIVPTLMQ 518
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
517-663 |
1.25e-03 |
|
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: 41.78 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 517 KASQKFPNSLFIITGDH---FDRSYEYAKNDLY--IIKsVPLILFAPTLKP-KKISQVGSHLDIAPTIIELV---APEGF 587
Cdd:cd16155 213 EASGELDNTIIVFTSDHglaVGSHGLMGKQNLYehSMR-VPLIISGPGIPKgKRRDALVYLQDVFPTLCELAgieIPESV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 588 QFVSFgKPLFSNNTTNPpsHPNYALGY----EAIATKDY---FYNPSLG---LRYLNENPKEpedkQNDKIEASKFYQQL 657
Cdd:cd16155 292 EGKSL-LPVIRGEKKAV--RDTLYGAYrdgqRAIRDDRWkliIYVPGVKrtqLFDLKKDPDE----LNNLADEPEYQERL 364
|
....*.
gi 1151269616 658 ESLKAL 663
Cdd:cd16155 365 KKLLAE 370
|
|
| exo_archaeo |
TIGR04178 |
exosortase/archaeosortase family protein; This model represents the most conserved region of ... |
67-166 |
1.69e-03 |
|
exosortase/archaeosortase family protein; This model represents the most conserved region of the multitransmembrane protein family of exosortases and archaeosortases. The region includes nearly invariant motifs at the ends of three predicted transmembrane helices on the extracytoplasmic face: a Cys (often Cys-Xaa-Gly), Asn-Xaa-Xaa-Arg, and His. This model is much broader than the bacterial exosortase model (TIGR02602), and has in intended scope similar to (or broader than) pfam09721.
Pssm-ID: 275031 [Multi-domain] Cd Length: 97 Bit Score: 38.36 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 67 VSSLAILFIIIGLLGLLAPKHQTKMLNIVAyFSIAIILFLNIANIVYYGIYGNVFDENLLEFLHEdtltilkmsgeypiF 146
Cdd:TIGR04178 10 LRSLILLLALGLLFAYLFPRSLRRKLLLLL-LGVPIIYLANILRIVLLILLGYYFGPEAFEFAHD--------------I 74
|
90 100
....*....|....*....|
gi 1151269616 147 SSFSLFVILGVLISFIYFKL 166
Cdd:TIGR04178 75 LGWLLFLLVALLLLLLVLWL 94
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
389-581 |
2.51e-03 |
|
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: 40.10 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 389 YYGGSGIWNKLTSFTKKQGFHALYFNNHLLEFVKNKPYpkpiesNWGVhdnILFDYILENTNPNEKTFSMVMTLSNHAI- 467
Cdd:cd00016 64 TLHGYTGNGSADPELPSRAAGKDEDGPTIPELLKQAGY------RTGV---IGLLKAIDETSKEKPFVLFLHFDGPDGPg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 468 --KNVNLKAFGVPLEKIQQFVEKtpksenlpdanslghiywydkvIVSFIKKASQKfPNSLFIITGDHFDRSYE---YAK 542
Cdd:cd00016 135 haYGPNTPEYYDAVEEIDERIGK----------------------VLDALKKAGDA-DDTVIIVTADHGGIDKGhggDPK 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1151269616 543 NDLYIIKS-----VPLILFAPTLK-PKKISQVGSHLDIAPTIIEL 581
Cdd:cd00016 192 ADGKADKShtgmrVPFIAYGPGVKkGGVKHELISQYDIAPTLADL 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
551-662 |
3.95e-03 |
|
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: 40.23 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 551 VPLILFAP--TLKPKKISQVGSHLDIAPTIIEL---VAPEGFQF--VSFgKPLFSNNTTNPPSH-----------PNYAL 612
Cdd:cd16146 273 VPFFIRWPgkILAGKDVDTLTAHIDLLPTLLDLcgvKLPEGIKLdgRSL-LPLLKGESDPWPERtlfthsgrwppPPKKK 351
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1151269616 613 GYEAIATKDYfynpslglRYLNENPKEPE--DKQNDKIE----ASKFYQQLESLKA 662
Cdd:cd16146 352 RNAAVRTGRW--------RLVSPKGFQPElyDIENDPGEendvADEHPEVVKRLKA 399
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
524-598 |
8.59e-03 |
|
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: 38.68 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151269616 524 NSLFIITGDHFD---RSYEYAKNDLYIiKS--VPLILFAP-TLKPKKISQVGSHLDIAPTIIELV---APEGFQfvsfGK 594
Cdd:cd16037 190 NTLIIYTSDHGDmlgERGLWGKSTMYE-ESvrVPMIISGPgIPAGKRVKTPVSLVDLAPTILEAAgapPPPDLD----GR 264
|
....
gi 1151269616 595 PLFS 598
Cdd:cd16037 265 SLLP 268
|
|
| |
