|
Name |
Accession |
Description |
Interval |
E-value |
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
1-592 |
7.94e-107 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 333.16 E-value: 7.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 1 MFEGGFLFdtsaILYTNLLYIFLMLIPLHYKenVIYQKITKGIFVTTNLIVIIMNLMDTVYFQYTHRRTTASVFSEFKNE 80
Cdd:COG1368 30 AFLYGLRF----ILYLLLLLLLLLLLLLPLL--FRRPKLRWIYLLLVLLLLLLLLVADILYYRFFGDRLNFSDLDYLGDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 81 GNLGGIIGTEllNHWYLTLFAIAFGYALFKLYRKPKPVKVermPVYYTVHLLTLGLGVYLCIGGMRGGFTGMVRPITISN 160
Cdd:COG1368 104 GEVLGSLLSS--YDLLLLLDLLLLLLLLLLLYRLLKKLRK---SLPWRKRLALLLLLLALLLLGIRLGEDRPLNLSDAFS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 161 ANKYVDRpmetgIVLNTPFSIFRTFGKTSFaiPQYFDKEKMEALYTPV----HMPADSVQFRPLNVVVFILESFSKESSG 236
Cdd:COG1368 179 RNNFVNE-----LGLNGPYSFYDALRNNKA--PATYSEEEALEIKKYLksnrPTPNPFGPAKKPNVVVILLESFSDFFIG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 237 FLneeldnGTYKGYMPFLDSLMAEGLTFKYSFSNGMKSIDGMPSVLSGIPMFIEPFFLTPSSLNTVSSIGGELGKKGYYT 316
Cdd:COG1368 252 AL------GNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGSPYKRPGQNNFPSLPSILKKQGYET 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 317 AFFHGADNGSMGFEAFARTAGYTNYFGRTEYneanpgNKDFDGHWGIWDEKFFQFFGNTLSGFQQPFAAALFSLSSHHPF 396
Cdd:COG1368 326 SFFHGGDGSFWNRDSFYKNLGFDEFYDREDF------DDPFDGGWGVSDEDLFDKALEELEKLKKPFFAFLITLSNHGPY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 397 AVPAEYEGVFPKGNKAIR---QCIGYTDHALKLFFEKVSKEPWYKNTLFVFTADHTN-SPERPEYETESGLFSVPVVFYQ 472
Cdd:COG1368 400 TLPEEDKKIPDYGKTTLNnylNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPrSPGKTDYENPLERYRVPLLIYS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 473 PGsNLKGFRKDVIAQQIDIMPTVLGYLGYD-KPFVSFGCDLLNtPAEDTYAVNYingiYQFFKGDYLlqfdgrnavamYA 551
Cdd:COG1368 480 PG-LKKPKVIDTVGSQIDIAPTLLDLLGIDyPSYYAFGRDLLS-PDTDPFAFRN----GGFITDDYV-----------YV 542
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1763932513 552 FKTDKLlehnllgqIDVQQSMEDELKAIIQQYMIRMNNDEL 592
Cdd:COG1368 543 LKTGEL--------TEEDKELEEEALAYLQLSDYLYGNDLL 575
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
221-500 |
6.07e-61 |
|
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: 203.68 E-value: 6.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 221 NVVVFILESFSKESSGFlneeldNGTYKGYMPFLDSLMAEGLTFKYSFSNGM--KSIDGMPSVLSGIPM-FIEPFFLTPS 297
Cdd:cd16015 2 NVIVILLESFSDPYIDK------DVGGEDLTPNLNKLAKEGLYFGNFYSPGFggGTANGEFEVLTGLPPlPLGSGSYTLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 298 SLNTVSSIGGELGKKGYYTAFFHGADNGSMGFEAFARTAGYTNYFGRTEYNEANPgnkdFDGHWGIWDEKFFQFFGNTLS 377
Cdd:cd16015 76 KLNPLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEK----ETNGWGVSDESLFDQALEELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 378 GFQ-QPFAAALFSLSSHHPFAVPAEYEGVFPKGNKAIR------QCIGYTDHALKLFFEKVSKEPWYKNTLFVFTADHT- 449
Cdd:cd16015 152 ELKkKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTelenylNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLp 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1763932513 450 --NSPERPEYETESGLFSVPVVFYQPGsNLKGFRKDVIAQQIDIMPTVLGYLG 500
Cdd:cd16015 232 slGSDYDETDEDPLDLYRTPLLIYSPG-LKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
221-501 |
7.31e-33 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 127.92 E-value: 7.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 221 NVVVFILESFSKESSGFLNEELDNgtykgyMPFLDSLMAEGLTFKYSFSNGMKSIDGMPSVLSGIPM--FIEPFFLTPSS 298
Cdd:pfam00884 2 NVVLVLGESLRAPDLGLYGYPRPT------TPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPhnFGSYVSTPVGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 299 LNTVSSIGGELGKKGYYTAFFHGADNG--------SMGFEAFARTAGYTNYFGRTEYNEANPGNkdfdghWGIWDEKFFQ 370
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGwynnqspcNLGFDKFFGRNTGSDLYADPPDVPYNCSG------GGVSDEALLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 371 FFGNTLSGFQQPFAAALFSLSSHHPFAVPAEYEGVFPKGNKAIR----------QCIGYTDHALKLFFEKVSKEPWYKNT 440
Cdd:pfam00884 150 EALEFLDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCseeqllnsydNTLLYTDDAIGRVLDKLEENGLLDNT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1763932513 441 LFVFTADH--------TNSPERPEYETESGLFSVPVVFYQPGSNLKGFRKDVIAQQIDIMPTVLGYLGY 501
Cdd:pfam00884 230 LVVYTSDHgeslgeggGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
220-513 |
1.07e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 101.09 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 220 LNVVVFILESFSKEssgFLNEEldnGTYKGYMPFLDSLMAEGLTFKYSFSNGMKSIDGMPSVLSGIPMF---IEPFFLTP 296
Cdd:cd16148 1 MNVILIVIDSLRAD---HLGCY---GYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFyhgVWGGPLEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 297 SslntVSSIGGELGKKGYYTAFFHGADNGSMGFEaFARTAGYTNYFGRTE----YNEANPGNKDFDghwgiwdeKFFQFF 372
Cdd:cd16148 75 D----DPTLAEILRKAGYYTAAVSSNPHLFGGPG-FDRGFDTFEDFRGQEgdpgEEGDERAERVTD--------RALEWL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 373 GNTLSGfqQPFAAALFSLSSHHPFAvpaeYEGvfpkgnkAIRqcigYTDHALKLFFEKVSKEPWYKNTLFVFTADH-TNS 451
Cdd:cd16148 142 DRNADD--DPFFLFLHYFDPHEPYL----YDA-------EVR----YVDEQIGRLLDKLKELGLLEDTLVIVTSDHgEEF 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1763932513 452 PERPEYETESGLFS-----VPVVFYQPGSnLKGFRKDVIAQQIDIMPTVLGYLGYDKPFVSFGCDLL 513
Cdd:cd16148 205 GEHGLYWGHGSNLYdeqlhVPLIIRWPGK-EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLL 270
|
|
| PRK12363 |
PRK12363 |
phosphoglycerol transferase I; Provisional |
143-523 |
1.10e-14 |
|
phosphoglycerol transferase I; Provisional
Pssm-ID: 171438 Cd Length: 703 Bit Score: 77.25 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 143 GGMRGGFTGM-VRPITISNANKYVDRpmetgivlntpfsIFRTFGKTSFAipqyfdkeKMEALYTPVHMPADsvqfRPLN 221
Cdd:PRK12363 104 GALFAGFVFMlVVTIAQSPLYRDGKR-------------LYYQLRPVDFA--------TVAPEYQVPQQPLQ----KRKN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 222 VVVFILESFSKEssgFLNEEldngTYKGYMPFLDSLMAEGLTFKysfsnGMKSIDGMPSVLSGI--PMFIEPFFLTPSSL 299
Cdd:PRK12363 159 IVWIYGESLERT---YFDED----VFPGLMPNLTRLATEAVDVR-----NLASTEGSGWTIAGMvaSMCGVPLTTAQGDE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 300 NTVSS----------IGGELGKKGYYTAFFHGADNGSMGFEAFARTAGY-----TNYFgrteYNEANPGNKDFDGhWGIW 364
Cdd:PRK12363 227 NSMDRmghflpearcLGDYLKDQGYTNHYVGGADASFAGKGKFLSSHGFdevhdVNYF----LHDKGVAPKHFSA-WGVH 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 365 DEKF----FQFFgNTLSGFQQPFAAALFSLSSHHPFA-VPAEYEGVFPK---GNKAIRQCIGYTDHALKLFFEKVSKEPW 436
Cdd:PRK12363 302 DDVLlddaYDEF-ETLSRAGQPFMLTTLTMDTHHPAGhLPSACKGQRYDsplGDIGMLHAIKCSDRLIGQLVDRIRNSRY 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 437 YKNTLFVFTADHTNSPERPEYetesglfsvpVVFYQPGSNLKGF-RKDVIAQQI--------DIMPTVLGYLGYDKPFVS 507
Cdd:PRK12363 381 GKNTIIVIASDHLAMPNDLSD----------VLTKQKRENLLLFlGKDIAPQQVvtragttlDSGATLLQLLEPGMRTLG 450
|
410
....*....|....*.
gi 1763932513 508 FGCDLLNTPAEDTYAV 523
Cdd:PRK12363 451 FGRSLLADDAPPSASV 466
|
|
| PRK03776 |
PRK03776 |
phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase; |
211-448 |
3.09e-14 |
|
phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase;
Pssm-ID: 179648 Cd Length: 762 Bit Score: 75.91 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 211 PADSVQFRPLNVVVFILESFskESSGFlneelDNGTYKGYMPFLDSLMAEGLtfkySFSNGMK------SIDGMPSVLSG 284
Cdd:PRK03776 153 PAKTIPNPKLNLVYIYGESL--ERTYF-----DNEAFPGLTPELGALKNEGL----DFSHTQQlpgtdyTIAGMVASQCG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 285 IPMFiEPFFLTPSSlnTVSS-------IGGELGKKGYYTAFFHGADNGSMGFEAFARTAGYTNYFGRTEYNE--ANPGNK 355
Cdd:PRK03776 222 IPLF-APFEGNASA--SVSSffpqnicLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDHLYGSEELKSvvADPHYR 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 356 DfdgHWGIWD----EKFFQFFgNTLSGFQQPFAaaLFSLS--SHHP--FaVPA-------EYEGvfpKGNKAIRQCIGYT 420
Cdd:PRK03776 299 N---DWGFYDdtvlDEAWKKF-EELSRSGQRFS--LFTLTvdTHHPdgF-ISRtcnrksyDFDG---KPNQSFSAVSCSQ 368
|
250 260
....*....|....*....|....*...
gi 1763932513 421 DHALKlFFEKVSKEPWYKNTLFVFTADH 448
Cdd:PRK03776 369 ENIAA-LINKIKASPWFKNTVIVVSSDH 395
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
251-584 |
1.01e-12 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 69.91 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 251 MPFLDSLMAEGLTF--------------------KYSFSNGMksidgmPSVLSGIPMFIEPFFLTpsslntvssIGGELG 310
Cdd:COG3119 49 TPNIDRLAAEGVRFtnayvtspvcspsraslltgRYPHRTGV------TDNGEGYNGGLPPDEPT---------LAELLK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 311 KKGYYTAFFhgadnGSMGFEAFARTAGYTNYFGRTEYNEANPgnkdfdghwgiwdekFFQFFGntlsgFQQPfaaalfsl 390
Cdd:COG3119 114 EAGYRTALF-----GKWHLYLTDLLTDKAIDFLERQADKDKP---------------FFLYLA-----FNAP-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 391 ssHHPFAVPAEYEGVF--------------PKGNKAIRQ-------CIGYTDHALKLFFEKVSKEPWYKNTLFVFTADHt 449
Cdd:COG3119 161 --HAPYQAPEEYLDKYdgkdiplppnlaprDLTEEELRRaraayaaMIEEVDDQVGRLLDALEELGLADNTIVVFTSDN- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 450 nSPERPE----------YEtesGLFSVPVVFYQPGSNLKGFRKDVIAQQIDIMPTVLGYLGYDKPFVSFGCDLL-----N 514
Cdd:COG3119 238 -GPSLGEhglrggkgtlYE---GGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLplltgE 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1763932513 515 TPAEDTYAVNYINGIYQFF---KGDYLL--QFDGRNAVAMYAFKTDKLLEHNLLGQI-DVQQSMEDELKAIIQQYM 584
Cdd:COG3119 314 KAEWRDYLYWEYPRGGGNRairTGRWKLirYYDDDGPWELYDLKNDPGETNNLAADYpEVVAELRALLEAWLKELG 389
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
221-504 |
6.28e-10 |
|
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: 61.37 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 221 NVVVFILESFSKESSGFlneeldnGTYKGYMPFLDSLMAEGLTFKYSFSNGMKS-------IDGMPSVLSGIPMFIEPFF 293
Cdd:cd16027 2 NILWIIADDLSPDLGGY-------GGNVVKTPNLDRLAAEGVRFTNAFTTAPVCspsrsalLTGLYPHQNGAHGLRSRGF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 294 LTPSSLNTVSSIggeLGKKGYYTAFfhgadngsmgfeafartAGYTNYFGRTEYNEANPGNKDFDGHWGIWD--EKFFQF 371
Cdd:cd16027 75 PLPDGVKTLPEL---LREAGYYTGL-----------------IGKTHYNPDAVFPFDDEMRGPDDGGRNAWDyaSNAADF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 372 FGNTLSGfqQPFAAALFSLSSHHPFAVPAEYEGVFPKG----------NKAIRQ-------CIGYTDHALKLFFEKVSKE 434
Cdd:cd16027 135 LNRAKKG--QPFFLWFGFHDPHRPYPPGDGEEPGYDPEkvkvppylpdTPEVREdladyydEIERLDQQVGEILDELEED 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1763932513 435 PWYKNTLFVFTADH--------TNSperpeyeTESGLfSVPVVFYQPGSNLKGFRKDVIAQQIDIMPTVLGYLGYDKP 504
Cdd:cd16027 213 GLLDNTIVIFTSDHgmpfprakGTL-------YDSGL-RVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPP 282
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
252-512 |
4.85e-09 |
|
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: 58.73 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 252 PFLDSLMAEGLTFKYSFSNgmksidgMP-------SVLSGI-----PMFIEPFFLTPSSLntvsSIGGELGKKGYYTAFF 319
Cdd:cd16034 28 PNLDRLAKEGVVFTNAVSN-------YPvcspyraSLLTGQypltnGVFGNDVPLPPDAP----TIADVLKDAGYRTGYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 320 -------HGADNGSM-----------GFEAFaRTAGYTNYFGRTEYNEANPGNKDFDGHWGIWD-EKFFQFFGNTLSGfQ 380
Cdd:cd16034 97 gkwhldgPERNDGRAddytppperrhGFDYW-KGYECNHDHNNPHYYDDDGKRIYIKGYSPDAEtDLAIEYLENQADK-D 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 381 QPFAAALfslsSHHP-----FAVPAEYEGVFPKGNKAIRQCI---------------GY------TDHALKLFFEKVSKE 434
Cdd:cd16034 175 KPFALVL----SWNPphdpyTTAPEEYLDMYDPKKLLLRPNVpedkkeeaglredlrGYyamitaLDDNIGRLLDALKEL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 435 PWYKNTLFVFTADH-----------TNSPerpeYEtESglFSVPVVFYQPGSNLKGFRKDVIAQQIDIMPTVLGYLGYDK 503
Cdd:cd16034 251 GLLENTIVVFTSDHgdmlgshglmnKQVP----YE-ES--IRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPI 323
|
....*....
gi 1763932513 504 PFVSFGCDL 512
Cdd:cd16034 324 PDTVEGRDL 332
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
221-496 |
7.17e-09 |
|
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: 56.66 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 221 NVVVFILESFSkessgflneeLDNGTYKGYM----PFLDSLMAEGLTFKYSFSNGMksidgmpsvlsgipmfiepfflTP 296
Cdd:cd00016 2 HVVLIVLDGLG----------ADDLGKAGNPapttPNLKRLASEGATFNFRSVSPP----------------------TS 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 297 SSLNTVSSIGGELgkKGYYTAFFHGADNGSMGFEAFARTAGYTNYFGRteyneanpgNKDFDGHWGIWdeKFFQFFGNTL 376
Cdd:cd00016 50 SAPNHAALLTGAY--PTLHGYTGNGSADPELPSRAAGKDEDGPTIPEL---------LKQAGYRTGVI--GLLKAIDETS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 377 SGfqQPFAAALFSLSSHHPFAVPAEYEGVFPKGNKAIRQCIGytdhalKLFfEKVSKEPWYKNTLFVFTADHTNSPERPE 456
Cdd:cd00016 117 KE--KPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIG------KVL-DALKKAGDADDTVIIVTADHGGIDKGHG 187
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1763932513 457 YETESGLF--------SVPVVFYQPGSNlKGFRKDVIAQQIDIMPTVL 496
Cdd:cd00016 188 GDPKADGKadkshtgmRVPFIAYGPGVK-KGGVKHELISQYDIAPTLA 234
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
251-504 |
4.64e-08 |
|
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: 53.98 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 251 MPFLDSLMAEGLTFKYSFSN---------GMksIDGMPSVLSGIPMFIEPFFLTPSSLNTvssIGGELGKKGYYTAFFhg 321
Cdd:cd16022 26 TPNLDRLAAEGVRFTNAYVAspvcspsraSL--LTGRYPHRHGVRGNVGNGGGLPPDEPT---LAELLKEAGYRTALI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 322 adnGSMGFEAfartagytnyfgrTEYNEANPGNKDFdghwgiwdekFFQFfgntlsGFQQPfaaalfslssHHPFAvpae 401
Cdd:cd16022 99 ---GKWHDEA-------------IDFIERRDKDKPF----------FLYV------SFNAP----------HPPFA---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 402 YEGvfpkgnkairqCIGYTDHALKLFFEKVSKEPWYKNTLFVFTADHtnSPERPE----------YEtesGLFSVPVVFY 471
Cdd:cd16022 133 YYA-----------MVSAIDDQIGRILDALEELGLLDNTLIVFTSDH--GDMLGDhglrgkkgslYE---GGIRVPFIVR 196
|
250 260 270
....*....|....*....|....*....|...
gi 1763932513 472 QPGSNLKGFRKDVIAQQIDIMPTVLGYLGYDKP 504
Cdd:cd16022 197 WPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPP 229
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
416-514 |
2.52e-05 |
|
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: 46.84 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 416 CIGYTDHALKLFFEKVSKEPWYKNTLFVFTADHTnsperpEYETESGL-------FS-----VPVVFyQPGSNLKGFRKD 483
Cdd:cd16150 205 MVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHG------DYTGDYGLvekwpntFEdcltrVPLII-KPPGGPAGGVSD 277
|
90 100 110
....*....|....*....|....*....|.
gi 1763932513 484 VIAQQIDIMPTVLGYLGYDKPFVSFGCDLLN 514
Cdd:cd16150 278 ALVELVDIPPTLLDLAGIPLSHTHFGRSLLP 308
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
244-587 |
3.27e-05 |
|
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: 46.45 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 244 NGTYKGYMPFLDSLMAEGLTFKYSFSNgmksidgMP-------SVLSGipmfiepffLTPSSlntvssiGGELGKKGYYT 316
Cdd:cd16033 19 YGNPIVKTPNIDRLAAEGVRFTNAYTP-------SPvccparaSLLTG---------LYPHE-------HGVLNNVENAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 317 AFFHGADngsMGFEAFART---AGYTNYF------GrteyNEANPGNKDFDGHWGIwdEKFFQFFG--------NTLSGF 379
Cdd:cd16033 76 AYSRGLP---PGVETFSEDlreAGYRNGYvgkwhvG----PEETPLDYGFDEYLPV--ETTIEYFLadraiemlEELAAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 380 QQPFAAALFSLSSHHPFAVPAEY------EGVFPKGN------------------------------KAIRQCIGYT--- 420
Cdd:cd16033 147 DKPFFLRVNFWGPHDPYIPPEPYldmydpEDIPLPESfaddfedkpyiyrrerkrwgvdtedeedwkEIIAHYWGYItli 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 421 DHALKLFFEKVSKEPWYKNTLFVFTADHTnsperpEYETESGLF-----------SVPVVFYQPGSNLKGFRKDVIAQQI 489
Cdd:cd16033 227 DDAIGRILDALEELGLADDTLVIFTSDHG------DALGAHRLWdkgpfmyeetyRIPLIIKWPGVIAAGQVVDEFVSLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 490 DIMPTVLGYLGYDKPFVSFG---CDLLNTPAED---TYAVNYINGiYQF-------FKGDYLLQFDGRNAVAMYAFKTDK 556
Cdd:cd16033 301 DLAPTILDLAGVDVPPKVDGrslLPLLRGEQPEdwrDEVVTEYNG-HEFylpqrmvRTDRYKYVFNGFDIDELYDLESDP 379
|
410 420 430
....*....|....*....|....*....|.
gi 1763932513 557 LLEHNLLGqidvqqsmEDELKAIIQQYMIRM 587
Cdd:cd16033 380 YELNNLID--------DPEYEEILREMRTRL 402
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
244-557 |
4.72e-05 |
|
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: 46.04 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 244 NGTYKGYMPFLDSLMAEGLTF--------------------KYSFSNGMKSidgmpSVLSGI-PMFIEPFFLTpsslntv 302
Cdd:cd16143 20 NPDSKIPTPNIDRLAAEGMRFtdahspssvctpsryglltgRYPWRSRLKG-----GVLGGFsPPLIEPDRVT------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 303 ssIGGELGKKGYYTAFF---H-GADNG-SMGFEAFARTAGYTNYFGRTEyneanPGNKD--FDGHWGI--------WDEK 367
Cdd:cd16143 88 --LAKMLKQAGYRTAMVgkwHlGLDWKkKDGKKAATGTGKDVDYSKPIK-----GGPLDhgFDYYFGIpasevlptLTDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 368 FFQFFGNtLSGFQQPFAAALFSLSSHHPFAVPAEYEGVfPKGNK---AIRQcigyTDHALKLFFEKVSKEPWYKNTLFVF 444
Cdd:cd16143 161 AVEFIDQ-HAKKDKPFFLYFALPAPHTPIVPSPEFQGK-SGAGPygdFVYE----LDWVVGRILDALKELGLAENTLVIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 445 TADHTNSPERPEYETES------------------GLFSVPVVFYQPGSNLKGFRKDVIAQQIDIMPTVLGYLGYDKPF- 505
Cdd:cd16143 235 TSDNGPSPYADYKELEKfghdpsgplrgmkadiyeGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDn 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 506 -----VSFGCDLLN---TPAEDTYAVNYINGIYQFFKGDYLLQFDGRNAVAMYAFKTDKL 557
Cdd:cd16143 315 aaedsFSFLPALLGpkkQEVRESLVHHSGNGSFAIRKGDWKLIDGTGSGGFSYPRGKEKL 374
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
218-502 |
8.33e-05 |
|
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: 44.92 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 218 RPLNVVVFILESFSKESSGFLNEELDNgtykgyMPFLDSLMAEGLTFKYSFSNGMKSIDGMPSVLSGIPmfIEPFFLTPS 297
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDT------TPFLSKLKKNLIVFDNVISCGTSTAVSLPCMLSFAN--RENYDRAYY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 298 SLNTVSsiggeLGKK-GYYTAFFhgaDN-GSMGfeafartaGYTNYFGRTEYNEANPGNKDFDGHWGIWDEKFFQFFGNT 375
Cdd:cd16017 73 QENLID-----LAKKaGYKTYWI---SNqGGCG--------GYDTRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 376 LSGFQQPFAAALFSLSSHHPFA--VPAEYEGVFPKGNKAIRQC------------IGYTDHALKLFFEKVSKEPwyKNTL 441
Cdd:cd16017 137 LADSSKKKLIVLHLMGSHGPYYdrYPEEFAKFTPDCDNELQSCskeelinaydnsILYTDYVLSQIIERLKKKD--KDAA 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1763932513 442 FVFTADHTNS-----------PERPEYETEsglfsVPVVFY-------QPGSNLKGFRKDVIAQQIDIMPTVLGYLGYD 502
Cdd:cd16017 215 LIYFSDHGESlgenglylhgaPYAPKEQYH-----VPFIIWssdsykqRYPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
437-504 |
1.78e-04 |
|
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: 44.17 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 437 YKNTLFVFTADHTnsperpEYETESGL----------FSVPVVFYQPGSNLKGFRKDVIA---QQIDIMPTVLGYLGYDK 503
Cdd:cd16028 264 WDDTLIVFTSDHG------EQLGDHWLwgkdgffdqaYRVPLIVRDPRREADATRGQVVDaftESVDVMPTILDWLGGEI 337
|
.
gi 1763932513 504 P 504
Cdd:cd16028 338 P 338
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
252-504 |
2.97e-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: 43.67 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 252 PFLDSLMAEGLTFKYSF-SNgmkSIdGMPS---VLSG-------IPMFIEPFFltPSSLNTVSSIggeLGKKGYYTAFF- 319
Cdd:cd16031 29 PNIDRLAKEGVRFDNAFvTT---SI-CAPSrasILTGqyshrhgVTDNNGPLF--DASQPTYPKL---LRKAGYQTAFIg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 320 --H-GADNGSM--GFEAFARTAGYTNYFgrTEYNEANPGNKDFDGH-------WGIwdekffQFFGNTLSgfQQPFAAAL 387
Cdd:cd16031 100 kwHlGSGGDLPppGFDYWVSFPGQGSYY--DPEFIENGKRVGQKGYvtdiitdKAL------DFLKERDK--DKPFCLSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 388 FSLSSHHPFaVPAE-----YEGV-FPKGN-----------KAIRQCIGYTDHALKLFFEKVSKEPWY------------- 437
Cdd:cd16031 170 SFKAPHRPF-TPAPrhrglYEDVtIPEPEtfddddyagrpEWAREQRNRIRGVLDGRFDTPEKYQRYmkdylrtvtgvdd 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 438 ---------------KNTLFVFTADHTNsperpeYETESGLFS----------VPVVFYQPGSNLKGFRKDVIAQQIDIM 492
Cdd:cd16031 249 nvgrildyleeqglaDNTIIIYTSDNGF------FLGEHGLFDkrlmyeesirVPLIIRDPRLIKAGTVVDALVLNIDFA 322
|
330
....*....|..
gi 1763932513 493 PTVLGYLGYDKP 504
Cdd:cd16031 323 PTILDLAGVPIP 334
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
417-496 |
5.41e-04 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 42.73 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 417 IGYTDHALKLFFEKVSKEPWYKNTLFVFTADH-----TNSPERPEYETEsGLFSVPVVFYQPGSNLKGFRKDVIAQQI-- 489
Cdd:PRK13759 274 ITHIDHQIGRFLQALKEFGLLDNTIILFVSDHgdmlgDHYLFRKGYPYE-GSAHIPFIIYDPGGLLAGNRGTVIDQVVel 352
|
....*...
gi 1763932513 490 -DIMPTVL 496
Cdd:PRK13759 353 rDIMPTLL 360
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
421-495 |
5.10e-03 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 39.09 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763932513 421 DHALKLFFEKVSKEPWYKNTLFVFTADH--TN-------SPErpeyETesglfSVPVVFYQPGSNLKGFRKDV------I 485
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHgmTDagnhggsSPG----ET-----SVPLLFISPKFSSKPSNADGelsyyeT 247
|
90
....*....|
gi 1763932513 486 AQQIDIMPTV 495
Cdd:cd16024 248 VQQVDLAPTL 257
|
|
| |
