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Conserved domains on  [gi|1092675703|ref|WP_070609423|]
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LTA synthase family protein [Pseudomonas sp. HMSC16B01]

Protein Classification

LTA synthase family protein( domain architecture ID 11443228)

LTA (lipoteichoic acid) synthase family protein belonging to the alkaline phosphatase (AlkP) superfamily; similar to LTA synthase which catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, an important cell wall polymer

EC:  2.7.8.-
Gene Ontology:  GO:0070395
PubMed:  26716576|29070681
SCOP:  3001353

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
56-525 1.63e-56

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 203.35  E-value: 1.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703  56 RRSLWFALPVMLLWCLSLIGNAELVGAVGRMPEPSDLKYLLDPQFVSSSTQGGGLahLPLALGLGGATLLCVLLWR---- 131
Cdd:COG1368    61 KLRWIYLLLVLLLLLLLLVADILYYRFFGDRLNFSDLDYLGDTGEVLGSLLSSYD--LLLLLDLLLLLLLLLLLYRllkk 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 132 -----RRGPRLPRYAYALPAAFLAAHVGLQY-LRPSDADQWQQY------NLPHKLLASALSSGQ---------LAVEDW 190
Cdd:COG1368   139 lrkslPWRKRLALLLLLLALLLLGIRLGEDRpLNLSDAFSRNNFvnelglNGPYSFYDALRNNKApatyseeeaLEIKKY 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 191 LADDRPDTPPdvaglnqldlsgtpllAGGGRARNVLIVAMEGIPGAYIAANraainsSYHEAPMPRLSGWAERAMTTPDY 270
Cdd:COG1368   219 LKSNRPTPNP----------------FGPAKKPNVVVILLESFSDFFIGAL------GNGKDVTPFLDSLAKESLYFGNF 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 271 VLHSHQTIRGLYAMLCGDYskldsGTPKGVELLNNPARARECLPAQLRQHGFSTHFLQGAGLRFMAKDKVMPQMGFDKTL 350
Cdd:COG1368   277 YSQGGRTSRGEFAVLTGLP-----PLPGGSPYKRPGQNNFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFY 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 351 GRDWFRNTSylEFPWGMDDKAFFEGAAtyvKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYPSAKQ------AAVAYL 424
Cdd:COG1368   352 DREDFDDPF--DGGWGVSDEDLFDKAL---EELEKLKKPFFAFLITLSNHGPYTLPEEDKKIPDYGKTtlnnylNAVRYA 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 425 DDAIDAFLADLEKQGVLRDTLVVLTSDESHGVDQVRLASAWGFN-----LVLAPEQAAlPPIKSGVYGHVDLAASVLDYF 499
Cdd:COG1368   427 DQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLERyrvplLIYSPGLKK-PKVIDTVGSQIDIAPTLLDLL 505
                         490       500
                  ....*....|....*....|....*..
gi 1092675703 500 GYRVPAGIS-GRSLFRDYASGREMMSY 525
Cdd:COG1368   506 GIDYPSYYAfGRDLLSPDTDPFAFRNG 532
 
Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
56-525 1.63e-56

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 203.35  E-value: 1.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703  56 RRSLWFALPVMLLWCLSLIGNAELVGAVGRMPEPSDLKYLLDPQFVSSSTQGGGLahLPLALGLGGATLLCVLLWR---- 131
Cdd:COG1368    61 KLRWIYLLLVLLLLLLLLVADILYYRFFGDRLNFSDLDYLGDTGEVLGSLLSSYD--LLLLLDLLLLLLLLLLLYRllkk 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 132 -----RRGPRLPRYAYALPAAFLAAHVGLQY-LRPSDADQWQQY------NLPHKLLASALSSGQ---------LAVEDW 190
Cdd:COG1368   139 lrkslPWRKRLALLLLLLALLLLGIRLGEDRpLNLSDAFSRNNFvnelglNGPYSFYDALRNNKApatyseeeaLEIKKY 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 191 LADDRPDTPPdvaglnqldlsgtpllAGGGRARNVLIVAMEGIPGAYIAANraainsSYHEAPMPRLSGWAERAMTTPDY 270
Cdd:COG1368   219 LKSNRPTPNP----------------FGPAKKPNVVVILLESFSDFFIGAL------GNGKDVTPFLDSLAKESLYFGNF 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 271 VLHSHQTIRGLYAMLCGDYskldsGTPKGVELLNNPARARECLPAQLRQHGFSTHFLQGAGLRFMAKDKVMPQMGFDKTL 350
Cdd:COG1368   277 YSQGGRTSRGEFAVLTGLP-----PLPGGSPYKRPGQNNFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFY 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 351 GRDWFRNTSylEFPWGMDDKAFFEGAAtyvKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYPSAKQ------AAVAYL 424
Cdd:COG1368   352 DREDFDDPF--DGGWGVSDEDLFDKAL---EELEKLKKPFFAFLITLSNHGPYTLPEEDKKIPDYGKTtlnnylNAVRYA 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 425 DDAIDAFLADLEKQGVLRDTLVVLTSDESHGVDQVRLASAWGFN-----LVLAPEQAAlPPIKSGVYGHVDLAASVLDYF 499
Cdd:COG1368   427 DQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLERyrvplLIYSPGLKK-PKVIDTVGSQIDIAPTLLDLL 505
                         490       500
                  ....*....|....*....|....*..
gi 1092675703 500 GYRVPAGIS-GRSLFRDYASGREMMSY 525
Cdd:COG1368   506 GIDYPSYYAfGRDLLSPDTDPFAFRNG 532
Sulfatase pfam00884
Sulfatase;
223-501 1.86e-45

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 164.90  E-value: 1.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 223 RNVLIVAMEGIPGAYIAANraainsSYHEAPMPRLSGWAERAMTTPDYVLHSHQTIRGLYAMLCGDYSKLDSGTpkgVEL 302
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLY------GYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY---VST 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 303 LNNPARARECLPAQLRQHGFSTHFLQGAGLRFMAKDKVmPQMGFDKTLGR----DWFRNTSYLEF---PWGMDDKAFFEG 375
Cdd:pfam00884  72 PVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSP-CNLGFDKFFGRntgsDLYADPPDVPYncsGGGVSDEALLDE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 376 AatyVKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYP-------------SAKQAAVAYLDDAIDAFLADLEKQGVLR 442
Cdd:pfam00884 151 A---LEFLDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqllNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092675703 443 DTLVVLTSD--ESHGVDQVRLASAWGFN----------LVLAPEQAALPPIKSGVYGHVDLAASVLDYFGY 501
Cdd:pfam00884 228 NTLVVYTSDhgESLGEGGGYLHGGKYDNapeggyrvplLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
223-500 1.03e-44

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: 162.08  E-value: 1.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 223 RNVLIVAMEGIPGAYIaanraaINSSYHEAPMPRLSGWAERAMTTPDYVLHS--HQTIRGLYAMLCGDYSKLDSGTPKGV 300
Cdd:cd16015     1 PNVIVILLESFSDPYI------DKDVGGEDLTPNLNKLAKEGLYFGNFYSPGfgGGTANGEFEVLTGLPPLPLGSGSYTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 301 ELLNNPararECLPAQLRQHGFSTHFLQGAGLRFMAKDKVMPQMGFDKTLGRDWFRNTSYLEFPWGMDDKAFFEGAATYV 380
Cdd:cd16015    75 YKLNPL----PSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDESLFDQALEEL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 381 KQLrqQKKPWMLTLLTVGTHQPYSAPADYLARYPSAKQ---------AAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:cd16015   151 EEL--KKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEdktelenylNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGD 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1092675703 452 ESHGVDQVRLASAWGFN-------LVLAPEQAAlPPIKSGVYGHVDLAASVLDYFG 500
Cdd:cd16015   229 HLPSLGSDYDETDEDPLdlyrtplLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLLG 283
PRK12363 PRK12363
phosphoglycerol transferase I; Provisional
277-451 4.58e-12

phosphoglycerol transferase I; Provisional


Pssm-ID: 171438  Cd Length: 703  Bit Score: 69.55  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 277 TIRGLYAMLCGDYSKLDSGTPKGVELLNNPARARECLPAQLRQHGFSTHFLQGAGLRFMAKDKVMPQMGFDKTLGRDWFR 356
Cdd:PRK12363  206 TIAGMVASMCGVPLTTAQGDENSMDRMGHFLPEARCLGDYLKDQGYTNHYVGGADASFAGKGKFLSSHGFDEVHDVNYFL 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 357 NTSYLE----FPWGMDDKAFFEGAATYVKQLRQQKKPWMLTLLTVGTHQpysaPADYL------ARYPSAKQ-----AAV 421
Cdd:PRK12363  286 HDKGVApkhfSAWGVHDDVLLDDAYDEFETLSRAGQPFMLTTLTMDTHH----PAGHLpsackgQRYDSPLGdigmlHAI 361
                         170       180       190
                  ....*....|....*....|....*....|
gi 1092675703 422 AYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:PRK12363  362 KCSDRLIGQLVDRIRNSRYGKNTIIVIASD 391
 
Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
56-525 1.63e-56

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 203.35  E-value: 1.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703  56 RRSLWFALPVMLLWCLSLIGNAELVGAVGRMPEPSDLKYLLDPQFVSSSTQGGGLahLPLALGLGGATLLCVLLWR---- 131
Cdd:COG1368    61 KLRWIYLLLVLLLLLLLLVADILYYRFFGDRLNFSDLDYLGDTGEVLGSLLSSYD--LLLLLDLLLLLLLLLLLYRllkk 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 132 -----RRGPRLPRYAYALPAAFLAAHVGLQY-LRPSDADQWQQY------NLPHKLLASALSSGQ---------LAVEDW 190
Cdd:COG1368   139 lrkslPWRKRLALLLLLLALLLLGIRLGEDRpLNLSDAFSRNNFvnelglNGPYSFYDALRNNKApatyseeeaLEIKKY 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 191 LADDRPDTPPdvaglnqldlsgtpllAGGGRARNVLIVAMEGIPGAYIAANraainsSYHEAPMPRLSGWAERAMTTPDY 270
Cdd:COG1368   219 LKSNRPTPNP----------------FGPAKKPNVVVILLESFSDFFIGAL------GNGKDVTPFLDSLAKESLYFGNF 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 271 VLHSHQTIRGLYAMLCGDYskldsGTPKGVELLNNPARARECLPAQLRQHGFSTHFLQGAGLRFMAKDKVMPQMGFDKTL 350
Cdd:COG1368   277 YSQGGRTSRGEFAVLTGLP-----PLPGGSPYKRPGQNNFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFY 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 351 GRDWFRNTSylEFPWGMDDKAFFEGAAtyvKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYPSAKQ------AAVAYL 424
Cdd:COG1368   352 DREDFDDPF--DGGWGVSDEDLFDKAL---EELEKLKKPFFAFLITLSNHGPYTLPEEDKKIPDYGKTtlnnylNAVRYA 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 425 DDAIDAFLADLEKQGVLRDTLVVLTSDESHGVDQVRLASAWGFN-----LVLAPEQAAlPPIKSGVYGHVDLAASVLDYF 499
Cdd:COG1368   427 DQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLERyrvplLIYSPGLKK-PKVIDTVGSQIDIAPTLLDLL 505
                         490       500
                  ....*....|....*....|....*..
gi 1092675703 500 GYRVPAGIS-GRSLFRDYASGREMMSY 525
Cdd:COG1368   506 GIDYPSYYAfGRDLLSPDTDPFAFRNG 532
Sulfatase pfam00884
Sulfatase;
223-501 1.86e-45

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 164.90  E-value: 1.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 223 RNVLIVAMEGIPGAYIAANraainsSYHEAPMPRLSGWAERAMTTPDYVLHSHQTIRGLYAMLCGDYSKLDSGTpkgVEL 302
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLY------GYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY---VST 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 303 LNNPARARECLPAQLRQHGFSTHFLQGAGLRFMAKDKVmPQMGFDKTLGR----DWFRNTSYLEF---PWGMDDKAFFEG 375
Cdd:pfam00884  72 PVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSP-CNLGFDKFFGRntgsDLYADPPDVPYncsGGGVSDEALLDE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 376 AatyVKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYP-------------SAKQAAVAYLDDAIDAFLADLEKQGVLR 442
Cdd:pfam00884 151 A---LEFLDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqllNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092675703 443 DTLVVLTSD--ESHGVDQVRLASAWGFN----------LVLAPEQAALPPIKSGVYGHVDLAASVLDYFGY 501
Cdd:pfam00884 228 NTLVVYTSDhgESLGEGGGYLHGGKYDNapeggyrvplLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
223-500 1.03e-44

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: 162.08  E-value: 1.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 223 RNVLIVAMEGIPGAYIaanraaINSSYHEAPMPRLSGWAERAMTTPDYVLHS--HQTIRGLYAMLCGDYSKLDSGTPKGV 300
Cdd:cd16015     1 PNVIVILLESFSDPYI------DKDVGGEDLTPNLNKLAKEGLYFGNFYSPGfgGGTANGEFEVLTGLPPLPLGSGSYTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 301 ELLNNPararECLPAQLRQHGFSTHFLQGAGLRFMAKDKVMPQMGFDKTLGRDWFRNTSYLEFPWGMDDKAFFEGAATYV 380
Cdd:cd16015    75 YKLNPL----PSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDESLFDQALEEL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 381 KQLrqQKKPWMLTLLTVGTHQPYSAPADYLARYPSAKQ---------AAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:cd16015   151 EEL--KKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEdktelenylNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGD 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1092675703 452 ESHGVDQVRLASAWGFN-------LVLAPEQAAlPPIKSGVYGHVDLAASVLDYFG 500
Cdd:cd16015   229 HLPSLGSDYDETDEDPLdlyrtplLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLLG 283
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
249-513 3.91e-19

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: 87.99  E-value: 3.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 249 YHEAPMPRLSGWAERAMTTPDYVLHSHQTIRGLYAMLCGDYskldsGTPKGVELLNNPARaRECLPAQLRQHGFSTHFLQ 328
Cdd:cd16148    21 YDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLY-----PFYHGVWGGPLEPD-DPTLAEILRKAGYYTAAVS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 329 GAGLRFmakdkvmPQMGFDKTL-GRDWFRNTSYLEFPWG-MDDKAFFEGAATYVKQlRQQKKPWMLTLLTVGTHQPYsap 406
Cdd:cd16148    95 SNPHLF-------GGPGFDRGFdTFEDFRGQEGDPGEEGdERAERVTDRALEWLDR-NADDDPFFLFLHYFDPHEPY--- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 407 adylaRYpsakQAAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD--ES---HGVdqvrlasAWGFNLVLAPEQAALPPI 481
Cdd:cd16148   164 -----LY----DAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDhgEEfgeHGL-------YWGHGSNLYDEQLHVPLI 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1092675703 482 ksgVYG--------------HVDLAASVLDYFGYRVPAGISGRSLF 513
Cdd:cd16148   228 ---IRWpgkepgkrvdalvsHIDIAPTLLDLLGVEPPDYSDGRSLL 270
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
349-536 1.16e-16

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: 81.82  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 349 TLGRDWFRNTsylEFPWGMD-DKAFFEGAATYVKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYPSAKQAA----VAY 423
Cdd:cd16037    94 LIGKLHFRGE---DQRHGFRyDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLYVRRARAAyyglVEF 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 424 LDDAIDAFLADLEKQGVLRDTLVVLTSDesHGvDQVRLASAWGFNL-----VLAPEQAALPPIKSGVY-----GHVDLAA 493
Cdd:cd16037   171 LDENIGRVLDALEELGLLDNTLIIYTSD--HG-DMLGERGLWGKSTmyeesVRVPMIISGPGIPAGKRvktpvSLVDLAP 247
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1092675703 494 SVLDYFGYRVPAGISGRSLF----RDYASGREMMS--YTNG------MLRHHDGK 536
Cdd:cd16037   248 TILEAAGAPPPPDLDGRSLLplaeGPDDPDRVVFSeyHAHGspsgafMLRKGRWK 302
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
365-534 2.11e-14

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 75.69  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 365 WGMD-DKAFFEGAATYVKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYPSAKQ------------------------A 419
Cdd:COG3119   125 WHLYlTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIplppnlaprdlteeelrraraayaA 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 420 AVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD--ESHGVDQVRLA--SAW--GFN---LVLAPEQaalppIKSG-VY--- 486
Cdd:COG3119   205 MIEEVDDQVGRLLDALEELGLADNTIVVFTSDngPSLGEHGLRGGkgTLYegGIRvplIVRWPGK-----IKAGsVSdal 279
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1092675703 487 -GHVDLAASVLDYFGYRVPAGISGRSL----------FRDYASGREMMSYTNGMLRHHD 534
Cdd:COG3119   280 vSLIDLLPTLLDLAGVPIPEDLDGRSLlplltgekaeWRDYLYWEYPRGGGNRAIRTGR 338
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
272-526 2.51e-13

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: 72.16  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 272 LHSHQTirGLYAMLCGDYSkldsgTPKGVEllnnparareCLPAQLRQHGFSTHFlqgAGLRFMAKDKVMPqmgfdktlg 351
Cdd:cd16027    59 LYPHQN--GAHGLRSRGFP-----LPDGVK----------TLPELLREAGYYTGL---IGKTHYNPDAVFP--------- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 352 rdwFRNTSYLEFPWGMDDKAFFEGAATYVKQlRQQKKPWMLTLLTVGTHQPYSAPADYLARYPSAK-------------- 417
Cdd:cd16027   110 ---FDDEMRGPDDGGRNAWDYASNAADFLNR-AKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKvkvppylpdtpevr 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 418 ------QAAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSDesHGVDQVRlASAWGFN-------LVLAPEQaalppIKSG 484
Cdd:cd16027   186 edladyYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSD--HGMPFPR-AKGTLYDsglrvplIVRWPGK-----IKPG 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1092675703 485 VY-----GHVDLAASVLDYFGYRVPAGISGRSLF----------RDYA-SGREMMSYT 526
Cdd:cd16027   258 SVsdalvSFIDLAPTLLDLAGIEPPEYLQGRSFLpllkgekdpgRDYVfAERDRHDET 315
PRK12363 PRK12363
phosphoglycerol transferase I; Provisional
277-451 4.58e-12

phosphoglycerol transferase I; Provisional


Pssm-ID: 171438  Cd Length: 703  Bit Score: 69.55  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 277 TIRGLYAMLCGDYSKLDSGTPKGVELLNNPARARECLPAQLRQHGFSTHFLQGAGLRFMAKDKVMPQMGFDKTLGRDWFR 356
Cdd:PRK12363  206 TIAGMVASMCGVPLTTAQGDENSMDRMGHFLPEARCLGDYLKDQGYTNHYVGGADASFAGKGKFLSSHGFDEVHDVNYFL 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 357 NTSYLE----FPWGMDDKAFFEGAATYVKQLRQQKKPWMLTLLTVGTHQpysaPADYL------ARYPSAKQ-----AAV 421
Cdd:PRK12363  286 HDKGVApkhfSAWGVHDDVLLDDAYDEFETLSRAGQPFMLTTLTMDTHH----PAGHLpsackgQRYDSPLGdigmlHAI 361
                         170       180       190
                  ....*....|....*....|....*....|
gi 1092675703 422 AYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:PRK12363  362 KCSDRLIGQLVDRIRNSRYGKNTIIVIASD 391
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
384-511 3.36e-09

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: 57.83  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 384 RQQKKPWMLTLltvgthqPYSAPADYLARYpsakqAAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSDesHG--VDQVRL 461
Cdd:cd16022   112 RDKDKPFFLYV-------SFNAPHPPFAYY-----AMVSAIDDQIGRILDALEELGLLDNTLIVFTSD--HGdmLGDHGL 177
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1092675703 462 ASAWGFN---------LVLAPEQAALPPIKSGVYGHVDLAASVLDYFGYRVPAGISGRS 511
Cdd:cd16022   178 RGKKGSLyeggirvpfIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
376-511 6.59e-09

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: 58.72  E-value: 6.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 376 AATYVKQLRQQKKPWMLTLLTVGTHQPY-SAP-------------------------ADYLARYPSAKQAAVAYL----- 424
Cdd:cd16147   163 ALDFLRRAAADDKPFFLVVAPPAPHGPFtPAPryanlfpnvtapprpppnnpdvsdkPHWLRRLPPLNPTQIAYIdelyr 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 425 ---------DDAIDAFLADLEKQGVLRDTLVVLTSDesHGVdqvrlasAWG-FNLVLAPEQA-----------ALPPIKS 483
Cdd:cd16147   243 krlrtlqsvDDLVERLVNTLEATGQLDNTYIIYTSD--NGY-------HLGqHRLPPGKRTPyeedirvpllvRGPGIPA 313
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1092675703 484 G-----VYGHVDLAASVLDYFGYRVPAGISGRS 511
Cdd:cd16147   314 GvtvdqLVSNIDLAPTILDLAGAPPPSDMDGRS 346
PRK03776 PRK03776
phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase;
312-451 7.06e-09

phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase;


Pssm-ID: 179648  Cd Length: 762  Bit Score: 59.34  E-value: 7.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 312 CLPAQLRQHGFSTHFLQGAGLRFMAKDKVMPQMGFD--------KTLGRDW-FRNTsylefpWGMDDKAFFEGAATYVKQ 382
Cdd:PRK03776  245 CLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDhlygseelKSVVADPhYRND------WGFYDDTVLDEAWKKFEE 318
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092675703 383 LRQQKKPWMLTLLTVGTHQP--YSAPADYLARYPSAKQ-----AAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:PRK03776  319 LSRSGQRFSLFTLTVDTHHPdgFISRTCNRKSYDFDGKpnqsfSAVSCSQENIAALINKIKASPWFKNTVIVVSSD 394
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
311-512 1.08e-08

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: 57.96  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 311 ECLPAQLRQHGFST------HfLQGAGLRFMAKDKVMP----QMGFDKTLG---RDWFRNTSY------LEFPWGMDDKA 371
Cdd:cd16034    80 PTIADVLKDAGYRTgyigkwH-LDGPERNDGRADDYTPpperRHGFDYWKGyecNHDHNNPHYydddgkRIYIKGYSPDA 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 372 FFEGAATYVKQLRQQKKPWMLtLLTVGT-HQPY-SAPADYLARYPSAKQ------------------------AAVAYLD 425
Cdd:cd16034   159 ETDLAIEYLENQADKDKPFAL-VLSWNPpHDPYtTAPEEYLDMYDPKKLllrpnvpedkkeeaglredlrgyyAMITALD 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 426 DAIDAFLADLEKQGVLRDTLVVLTSD-----ESHGVD--QVRLASAWGFNLVLA-PEQAALPPIKSGVYGHVDLAASVLD 497
Cdd:cd16034   238 DNIGRLLDALKELGLLENTIVVFTSDhgdmlGSHGLMnkQVPYEESIRVPFIIRyPGKIKAGRVVDLLINTVDIMPTLLG 317
                         250
                  ....*....|....*
gi 1092675703 498 YFGYRVPAGISGRSL 512
Cdd:cd16034   318 LCGLPIPDTVEGRDL 332
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
387-455 3.53e-08

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: 56.05  E-value: 3.53e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092675703 387 KKPWMLTLLTVGTHQPYSAPADYLARY-PSAKQA---AVAYLDDAIDAFLADLEKQGVLRDTLVVLTSDesHG 455
Cdd:cd16032   132 GRPFFLTVSFTHPHDPYVIPQEYWDLYvRRARRAyygMVSYVDDKVGQLLDTLERTGLADDTIVIFTSD--HG 202
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
374-512 6.73e-08

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: 55.69  E-value: 6.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 374 EGAATYVKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYPSAK-----------------------------------Q 418
Cdd:cd16033   134 DRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDiplpesfaddfedkpyiyrrerkrwgvdtedeedwK 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 419 AAVA-------YLDDAIDAFLADLEKQGVLRDTLVVLTSDesHGvDQvrLASAWGFN--LVLAPEQAALP-----PIKSG 484
Cdd:cd16033   214 EIIAhywgyitLIDDAIGRILDALEELGLADDTLVIFTSD--HG-DA--LGAHRLWDkgPFMYEETYRIPliikwPGVIA 288
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1092675703 485 VYGHV-------DLAASVLDYFGYRVPAGISGRSL 512
Cdd:cd16033   289 AGQVVdefvsllDLAPTILDLAGVDVPPKVDGRSL 323
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
282-451 3.12e-07

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: 53.36  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 282 YAMLCGDYSkLDSGTPKGVELLNNPAR---ARECLPAQLRQHGFST------HFlqgaGLRFMAKDKVMPQMGFDKTLgr 352
Cdd:cd16143    55 YGLLTGRYP-WRSRLKGGVLGGFSPPLiepDRVTLAKMLKQAGYRTamvgkwHL----GLDWKKKDGKKAATGTGKDV-- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 353 DWFRNT----------SYLEFPWGMDDKAFFEGAATYVKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARY-PSAKQAAV 421
Cdd:cd16143   128 DYSKPIkggpldhgfdYYFGIPASEVLPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGKSgAGPYGDFV 207
                         170       180       190
                  ....*....|....*....|....*....|
gi 1092675703 422 AYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:cd16143   208 YELDWVVGRILDALKELGLAENTLVIFTSD 237
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
343-451 3.47e-07

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: 53.32  E-value: 3.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 343 QMGFDKTLG----------RDWFRNTSYLEFPWGMDDKAFF---EGAATYVKQlrQQKKPWMLTLLTVGTHQPYSAPADY 409
Cdd:cd16144   128 DQGFDVNIGgtgnggppsyYFPPGKPNPDLEDGPEGEYLTDrltDEAIDFIEQ--NKDKPFFLYLSHYAVHTPIQARPEL 205
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1092675703 410 LARY-----------PSAKQAA-VAYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:cd16144   206 IEKYekkkkglrkgqKNPVYAAmIESLDESVGRILDALEELGLADNTLVIFTSD 259
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
375-455 3.77e-06

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: 48.96  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 375 GAATYVKQLrQQKKPWMLTLLTVGTHQPYSAPADYLARYPsakqAAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSDESH 454
Cdd:cd00016   107 GLLKAIDET-SKEKPFVLFLHFDGPDGPGHAYGPNTPEYY----DAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181

                  .
gi 1092675703 455 G 455
Cdd:cd00016   182 I 182
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
372-512 5.15e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 49.49  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 372 FFEGAATYVKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYPSAK---------------------------------- 417
Cdd:cd16155   107 FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETiplpenflpqhpfdngegtvrdeqlapfprtpea 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 418 --------QAAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSDE-----SHGV--DQvrlasawgfNL----VLAPEQAAL 478
Cdd:cd16155   187 vrqhlaeyYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHglavgSHGLmgKQ---------NLyehsMRVPLIISG 257
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1092675703 479 PPIKSG------VYgHVDLAASVLDYFGYRVPAGISGRSL 512
Cdd:cd16155   258 PGIPKGkrrdalVY-LQDVFPTLCELAGIEIPESVEGKSL 296
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
421-512 1.08e-05

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: 48.79  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 421 VAYLDDAIDAFLADLEKQGVLRDTLVVLTSDesHGvDQvrLASAW-----GFN--------LVLAPEQAALPPIKSGVYG 487
Cdd:cd16028   244 IAEVDDHLGRLFDYLKETGQWDDTLIVFTSD--HG-EQ--LGDHWlwgkdGFFdqayrvplIVRDPRREADATRGQVVDA 318
                          90       100
                  ....*....|....*....|....*...
gi 1092675703 488 ---HVDLAASVLDYFGYRVPAGISGRSL 512
Cdd:cd16028   319 fteSVDVMPTILDWLGGEIPHQCDGRSL 346
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
372-451 1.59e-05

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: 47.93  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 372 FFEGAATYVKQlrQQKKPWMLTLLTVGTHQPYSAPADYLARYP----SAKQAA----VAYLDDAIDAFLADLEKQGVLRD 443
Cdd:cd16146   159 FFDEAIDFIEE--NKDKPFFAYLATNAPHGPLQVPDKYLDPYKdmglDDKLAAfygmIENIDDNVGRLLAKLKELGLEEN 236

                  ....*...
gi 1092675703 444 TLVVLTSD 451
Cdd:cd16146   237 TIVIFMSD 244
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
337-451 4.53e-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: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 46.37  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 337 KDKVMPQ-MGFDktlgrDWFRNTSYLefpwgmDDKAFFEGAATYVKQLRQQKKPWMLTLLTVGTHQPYSAPADYLARYPS 415
Cdd:cd16142   110 EDGRLPTdHGFD-----EFYGNLYHT------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSG 178
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1092675703 416 AKQ--AAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:cd16142   179 KGKyaDSMVELDDHVGQILDALDELGIADNTIVIFTTD 216
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
376-455 4.89e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 45.69  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 376 AATYVKQLRQQKKPWMLTLLTVGTHQPYSapadYLArypsakqaAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSDesHG 455
Cdd:cd16149   115 AADFLRRRAEAEKPFFLSVNYTAPHSPWG----YFA--------AVTGVDRNVGRLLDELEELGLTENTLVIFTSD--NG 180
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
313-451 5.50e-05

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: 46.31  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 313 LPAQLRQHGFST------HFLQgaglrfmaKDKVMPQM-GFDktlgrdwfrntSYLEFPWGMDDK---AFFEGAATYVKQ 382
Cdd:cd16161    88 LAEVLRQAGYATgmigkwHLGQ--------REAYLPNSrGFD-----------YYFGIPFSHDSSladRYAQFATDFIQR 148
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092675703 383 LRQQKKPWMLTLLTVGTH--QPYSAPADYLARYPSAKQAAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:cd16161   149 ASAKDRPFFLYAALAHVHvpLANLPRFQSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSD 219
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
280-451 7.98e-05

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: 45.62  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 280 GLYAMLCGDYSK-LDSGTPKGVeLLNNPArarecLPAQLRQHGFSTHfLQG---AGlrfMAKDKVMP-QMGFDKTLG--- 351
Cdd:cd16029    58 GRYPIHTGMQHGvILAGEPYGL-PLNETL-----LPQYLKELGYATH-LVGkwhLG---FYTWEYTPtNRGFDSFYGyyg 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 352 ---------RDWFRNTSYLEFpwGMDDKAFFEGAATY---------VKQLRQ--QKKPWMLTLLTVGTHQPYSAPADYLA 411
Cdd:cd16029   128 gaedyythtSGGANDYGNDDL--RDNEEPAWDYNGTYstdlftdraVDIIENhdPSKPLFLYLAFQAVHAPLQVPPEYAD 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1092675703 412 RYPSAK-----------QAAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:cd16029   206 PYEDKFahikdedrrtyAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSD 256
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
386-513 4.80e-04

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: 42.75  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 386 QKKPWMLTLLTVGTHQPYSAPADYLARYpsAKQAAVAYLDD----AIDAFLADLEKQGvlRD-TLVVLTSDesHGV---D 457
Cdd:cd16153   141 SDKPFFVRLSFLQPHTPVLPPKEFRDRF--DYYAFCAYGDAqvgrAVEAFKAYSLKQD--RDyTIVYVTGD--HGWhlgE 214
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092675703 458 QVRLA-------SAWGFNLVLAPEQAALPPIKsgVYG----HVDLAASVLDYFGYRV--PAGISGRSLF 513
Cdd:cd16153   215 QGILAkftfwpqSHRVPLIVVSSDKLKAPAGK--VRHdfveFVDLAPTLLAAAGVDVdaPDYLDGRDLF 281
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
384-451 7.27e-04

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: 42.55  E-value: 7.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092675703 384 RQQKKPWMLTLLTVGTHQPYSAPADYLARypSAKQA---AVAYLDDAIDAFLADLEKQGVLRDTLVVLTSD 451
Cdd:cd16026   179 RNKDQPFFLYLAHTMPHVPLFASEKFKGR--SGAGLygdVVEELDWSVGRILDALKELGLEENTLVIFTSD 247
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
297-455 1.12e-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: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 41.81  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 297 PKGVELLNNPARAReclpaqLRQHG--FSTHF-------------LQGaglRFMAKDKV---------------MPQMGf 346
Cdd:cd16035    18 PAGWAALNLPARER------LAANGlsFENHYtaacmcspsrstlYTG---LHPQQTGVtdtlgspmqpllspdVPTLG- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 347 dktlgrDWFRNTSY----------LEFPWG--MDDKAFFEGAATYVKQLRQQK---KPWMLTLLTVGTHQPYSAPAD--- 408
Cdd:cd16035    88 ------HMLRAAGYytaykgkwhlSGAAGGgyKRDPGIAAQAVEWLRERGAKNadgKPWFLVVSLVNPHDIMFPPDDeer 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1092675703 409 --YLARYPSAKQAAVaylDDAIDAFLADLEKQGVLRDTLVVLTSDesHG 455
Cdd:cd16035   162 wrRFRNFYYNLIRDV---DRQIGRVLDALDASGLADNTIVVFTSD--HG 205
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
419-455 3.73e-03

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 40.50  E-value: 3.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1092675703 419 AAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSDesHG 455
Cdd:COG1524   209 AALREVDAALGRLLDALKARGLYEGTLVIVTAD--HG 243
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
372-451 4.23e-03

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: 40.27  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 372 FFEGAATYVKqlRQQKKPWMLTLLTVGTHQPYSAPADYLARY---------------PSAKQAA-VAYLDDAIDAFLADL 435
Cdd:cd16145   174 FTDEALDFIR--ENKDKPFFLYLAYTLPHAPLQVPDDGPYKYkpkdpgiyaylpwpqPEKAYAAmVTRLDRDVGRILALL 251
                          90
                  ....*....|....*.
gi 1092675703 436 EKQGVLRDTLVVLTSD 451
Cdd:cd16145   252 KELGIDENTLVVFTSD 267
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
394-459 5.38e-03

SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 39.82  E-value: 5.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675703 394 LLTVGthqpYSAPaDYL-ARY-PSAK--QAAVAYLDDAIDAFLADLEKQGVLRDTLVVLTSDesHGVDQV 459
Cdd:cd16016   209 LLAVS----FSAT-DYIgHAFgPNSVemEDTYLRLDRDLARLLDALDKKVGKGNYLVFLTAD--HGAADN 271
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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