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Conserved domains on  [gi|2567119174|gb|WMD15580|]
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LTA synthase family protein [Anaerostipes hadrus]

Protein Classification

LTA synthase family protein( domain architecture ID 10887838)

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

CATH:  3.40.720.10|3.30.1120.80
SCOP:  3001353

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 464-758 1.13e-87

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: 279.57  E-value: 1.13e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 464 PNVVVIMNETFSDLNVVNKIKtNKEVMPFINSL-SENTIKGHMLVSVFGGGTSNSEYEFLTGNSvsSLPLNGNAYTQFVK 542
Cdd:cd16015     1 PNVIVILLESFSDPYIDKDVG-GEDLTPNLNKLaKEGLYFGNFYSPGFGGGTANGEFEVLTGLP--PLPLGSGSYTLYKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 543 HKVPSLASQLKQQGYDTLAFHPYKAHGWNRDTVYPLIGFDNFLDETSMNPNGEKFRGWY-SDAEDYNKIIDIFNKKKAgQ 621
Cdd:cd16015    78 NPLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGvSDESLFDQALEELEELKK-K 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 622 PLFLFNVTIQNHGGYLIADKNFKEEIKIKDEKatDTANRYLSLIHESDRAFEKIINYFKNQK--EPTIVVMFGDHQPKLE 699
Cdd:cd16015   157 PFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDK--TELENYLNAIHYTDKALGEFIEKLKKSGlyENTIIVIYGDHLPSLG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2567119174 700 DSFYELLYgkslnslslkELQKKYTVPFIIWANYDIDAKSDVENVSANYLSSLMLQQTN 758
Cdd:cd16015   235 SDYDETDE----------DPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
 
Name Accession Description Interval E-value
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 464-758 1.13e-87

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: 279.57  E-value: 1.13e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 464 PNVVVIMNETFSDLNVVNKIKtNKEVMPFINSL-SENTIKGHMLVSVFGGGTSNSEYEFLTGNSvsSLPLNGNAYTQFVK 542
Cdd:cd16015     1 PNVIVILLESFSDPYIDKDVG-GEDLTPNLNKLaKEGLYFGNFYSPGFGGGTANGEFEVLTGLP--PLPLGSGSYTLYKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 543 HKVPSLASQLKQQGYDTLAFHPYKAHGWNRDTVYPLIGFDNFLDETSMNPNGEKFRGWY-SDAEDYNKIIDIFNKKKAgQ 621
Cdd:cd16015    78 NPLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGvSDESLFDQALEELEELKK-K 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 622 PLFLFNVTIQNHGGYLIADKNFKEEIKIKDEKatDTANRYLSLIHESDRAFEKIINYFKNQK--EPTIVVMFGDHQPKLE 699
Cdd:cd16015   157 PFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDK--TELENYLNAIHYTDKALGEFIEKLKKSGlyENTIIVIYGDHLPSLG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2567119174 700 DSFYELLYgkslnslslkELQKKYTVPFIIWANYDIDAKSDVENVSANYLSSLMLQQTN 758
Cdd:cd16015   235 SDYDETDE----------DPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 256-811 9.68e-85

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 281.54  E-value: 9.68e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 256 KVFYNPISVMNKLAFGMnILWYYILFFILLLIFNRVKWALLVGDVFLYAAAIGNYFVLAFRGTPITPADIYALGTAMDVA 335
Cdd:COG1368    29 QAFLYGLRFILYLLLLL-LLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVADILYYRFFGDRLNFSDLDYLGDTGEVL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 336 DHYVLSYDKPAIVATVVLLGLCVFA---CKLDTYKIFHWKKRLVALLITAIVTVGSSFFLTRVDFLSkkgvavNFWQQKR 412
Cdd:COG1368   108 GSLLSSYDLLLLLDLLLLLLLLLLLyrlLKKLRKSLPWRKRLALLLLLLALLLLGIRLGEDRPLNLS------DAFSRNN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 413 GYLKNG--YILSFLMNIQYTivSQPDGYSPEAVDKIADKYQVTQGT--NKKLKQKPNVVVIMNETFSDlNVVNKIKTNKE 488
Cdd:COG1368   182 FVNELGlnGPYSFYDALRNN--KAPATYSEEEALEIKKYLKSNRPTpnPFGPAKKPNVVVILLESFSD-FFIGALGNGKD 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 489 VMPFINSLSENTIK-GHMLVSvfGGGTSNSEYEFLTGnsVSSLPlNGNAYTQFVKHKVPSLASQLKQQGYDTLAFHPYKA 567
Cdd:COG1368   259 VTPFLDSLAKESLYfGNFYSQ--GGRTSRGEFAVLTG--LPPLP-GGSPYKRPGQNNFPSLPSILKKQGYETSFFHGGDG 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 568 HGWNRDTVYPLIGFDNFLDETSMNPNGEkfRGW-YSDAEDYNKIIDIFNKKKagQPLFLFNVTIQNHGGYLIADKNFKee 646
Cdd:COG1368   334 SFWNRDSFYKNLGFDEFYDREDFDDPFD--GGWgVSDEDLFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEEDKK-- 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 647 ikiKDEKATDTANRYLSLIHESDRAFEKIINYFKNQK--EPTIVVMFGDHQPKLEDSFYELLYgkslnslslkelQKKYT 724
Cdd:COG1368   408 ---IPDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGwyDNTIFVIYGDHGPRSPGKTDYENP------------LERYR 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 725 VPFIIWANYDIDAKSDVENVSANYLSSLMLQQTNLKMSRYNEF---LLNMRNEVPALNANGYVDKDG----KNHELSENN 797
Cdd:COG1368   473 VPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFgrdLLSPDTDPFAFRNGGFITDDYvyvlKTGELTEED 552

                         570
                  ....*....|....*.
gi 2567119174 798 E--YTKLITQYQYLQY 811
Cdd:COG1368   553 KelEEEALAYLQLSDY 568
Sulfatase pfam00884
Sulfatase;
464-759 7.23e-38

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 143.72  E-value: 7.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 464 PNVVVIMNETFSDLNVvNKIKTNKEVMPFINSLSENtikGHMLVSVFGGG--TSNSEYEFLTGnsvsSLPLNGNAYT--- 538
Cdd:pfam00884   1 PNVVLVLGESLRAPDL-GLYGYPRPTTPFLDRLAEE---GLLFSNFYSGGtlTAPSRFALLTG----LPPHNFGSYVstp 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 539 QFVKHKVPSLASQLKQQGYDTLAFHPYKAHGWNRDTVyPLIGFDNFLD--ETSMNPNGEKFRGW------YSDAEDYNKI 610
Cdd:pfam00884  73 VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSP-CNLGFDKFFGrnTGSDLYADPPDVPYncsgggVSDEALLDEA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 611 IDIfnKKKAGQPLFLFNVTIQNHGGYLIADKNFKEEIKIKDEKATDTA--NRYLSLIHESDRAFEKIINYFK--NQKEPT 686
Cdd:pfam00884 152 LEF--LDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCSEEQllNSYDNTLLYTDDAIGRVLDKLEenGLLDNT 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567119174 687 IVVMFGDHQPKLEDSFYELLYGKSLNSlslkeLQKKYTVPFIIWANYDIDAKSDVEN-VSANYLSSLMLQQTNL 759
Cdd:pfam00884 230 LVVYTSDHGESLGEGGGYLHGGKYDNA-----PEGGYRVPLLIWSPGGKAKGQKSEAlVSHVDLFPTILDLAGI 298
 
Name Accession Description Interval E-value
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 464-758 1.13e-87

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: 279.57  E-value: 1.13e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 464 PNVVVIMNETFSDLNVVNKIKtNKEVMPFINSL-SENTIKGHMLVSVFGGGTSNSEYEFLTGNSvsSLPLNGNAYTQFVK 542
Cdd:cd16015     1 PNVIVILLESFSDPYIDKDVG-GEDLTPNLNKLaKEGLYFGNFYSPGFGGGTANGEFEVLTGLP--PLPLGSGSYTLYKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 543 HKVPSLASQLKQQGYDTLAFHPYKAHGWNRDTVYPLIGFDNFLDETSMNPNGEKFRGWY-SDAEDYNKIIDIFNKKKAgQ 621
Cdd:cd16015    78 NPLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGvSDESLFDQALEELEELKK-K 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 622 PLFLFNVTIQNHGGYLIADKNFKEEIKIKDEKatDTANRYLSLIHESDRAFEKIINYFKNQK--EPTIVVMFGDHQPKLE 699
Cdd:cd16015   157 PFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDK--TELENYLNAIHYTDKALGEFIEKLKKSGlyENTIIVIYGDHLPSLG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2567119174 700 DSFYELLYgkslnslslkELQKKYTVPFIIWANYDIDAKSDVENVSANYLSSLMLQQTN 758
Cdd:cd16015   235 SDYDETDE----------DPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 256-811 9.68e-85

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 281.54  E-value: 9.68e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 256 KVFYNPISVMNKLAFGMnILWYYILFFILLLIFNRVKWALLVGDVFLYAAAIGNYFVLAFRGTPITPADIYALGTAMDVA 335
Cdd:COG1368    29 QAFLYGLRFILYLLLLL-LLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVADILYYRFFGDRLNFSDLDYLGDTGEVL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 336 DHYVLSYDKPAIVATVVLLGLCVFA---CKLDTYKIFHWKKRLVALLITAIVTVGSSFFLTRVDFLSkkgvavNFWQQKR 412
Cdd:COG1368   108 GSLLSSYDLLLLLDLLLLLLLLLLLyrlLKKLRKSLPWRKRLALLLLLLALLLLGIRLGEDRPLNLS------DAFSRNN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 413 GYLKNG--YILSFLMNIQYTivSQPDGYSPEAVDKIADKYQVTQGT--NKKLKQKPNVVVIMNETFSDlNVVNKIKTNKE 488
Cdd:COG1368   182 FVNELGlnGPYSFYDALRNN--KAPATYSEEEALEIKKYLKSNRPTpnPFGPAKKPNVVVILLESFSD-FFIGALGNGKD 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 489 VMPFINSLSENTIK-GHMLVSvfGGGTSNSEYEFLTGnsVSSLPlNGNAYTQFVKHKVPSLASQLKQQGYDTLAFHPYKA 567
Cdd:COG1368   259 VTPFLDSLAKESLYfGNFYSQ--GGRTSRGEFAVLTG--LPPLP-GGSPYKRPGQNNFPSLPSILKKQGYETSFFHGGDG 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 568 HGWNRDTVYPLIGFDNFLDETSMNPNGEkfRGW-YSDAEDYNKIIDIFNKKKagQPLFLFNVTIQNHGGYLIADKNFKee 646
Cdd:COG1368   334 SFWNRDSFYKNLGFDEFYDREDFDDPFD--GGWgVSDEDLFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEEDKK-- 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 647 ikiKDEKATDTANRYLSLIHESDRAFEKIINYFKNQK--EPTIVVMFGDHQPKLEDSFYELLYgkslnslslkelQKKYT 724
Cdd:COG1368   408 ---IPDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGwyDNTIFVIYGDHGPRSPGKTDYENP------------LERYR 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 725 VPFIIWANYDIDAKSDVENVSANYLSSLMLQQTNLKMSRYNEF---LLNMRNEVPALNANGYVDKDG----KNHELSENN 797
Cdd:COG1368   473 VPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFgrdLLSPDTDPFAFRNGGFITDDYvyvlKTGELTEED 552

                         570
                  ....*....|....*.
gi 2567119174 798 E--YTKLITQYQYLQY 811
Cdd:COG1368   553 KelEEEALAYLQLSDY 568
Sulfatase pfam00884
Sulfatase;
464-759 7.23e-38

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 143.72  E-value: 7.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 464 PNVVVIMNETFSDLNVvNKIKTNKEVMPFINSLSENtikGHMLVSVFGGG--TSNSEYEFLTGnsvsSLPLNGNAYT--- 538
Cdd:pfam00884   1 PNVVLVLGESLRAPDL-GLYGYPRPTTPFLDRLAEE---GLLFSNFYSGGtlTAPSRFALLTG----LPPHNFGSYVstp 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 539 QFVKHKVPSLASQLKQQGYDTLAFHPYKAHGWNRDTVyPLIGFDNFLD--ETSMNPNGEKFRGW------YSDAEDYNKI 610
Cdd:pfam00884  73 VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSP-CNLGFDKFFGrnTGSDLYADPPDVPYncsgggVSDEALLDEA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 611 IDIfnKKKAGQPLFLFNVTIQNHGGYLIADKNFKEEIKIKDEKATDTA--NRYLSLIHESDRAFEKIINYFK--NQKEPT 686
Cdd:pfam00884 152 LEF--LDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCSEEQllNSYDNTLLYTDDAIGRVLDKLEenGLLDNT 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567119174 687 IVVMFGDHQPKLEDSFYELLYGKSLNSlslkeLQKKYTVPFIIWANYDIDAKSDVEN-VSANYLSSLMLQQTNL 759
Cdd:pfam00884 230 LVVYTSDHGESLGEGGGYLHGGKYDNA-----PEGGYRVPLLIWSPGGKAKGQKSEAlVSHVDLFPTILDLAGI 298
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 464-730 1.33e-11

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: 66.03  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 464 PNVVVIMNETF-SDLnvVNKIKTNKEVMPFINSLSENTIkghmlvsVF------GGGTSNSEYEFLTGnsvsSLPLNGNA 536
Cdd:cd16148     1 MNVILIVIDSLrADH--LGCYGYDRVTTPNLDRLAAEGV-------VFdnhysgSNPTLPSRFSLFTG----LYPFYHGV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 537 YTQFVKHKVPSLASQLKQQGYDTLAF----HPYKAHGWNRdtvypliGFDNFLDETSMNPNGEKFrGWYSDAEDYNKIID 612
Cdd:cd16148    68 WGGPLEPDDPTLAEILRKAGYYTAAVssnpHLFGGPGFDR-------GFDTFEDFRGQEGDPGEE-GDERAERVTDRALE 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 613 IFNKKKAGQPLFLFNVTIQNHGGYliadknfkeeikikdekatdtanRYLSLIHESDRAFEKIINYFKNQK--EPTIVVM 690
Cdd:cd16148   140 WLDRNADDDPFFLFLHYFDPHEPY-----------------------LYDAEVRYVDEQIGRLLDKLKELGllEDTLVIV 196

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2567119174 691 FGDHQpkleDSFYEL-LYGKSLNSLSlKELQKkytVPFIIW 730
Cdd:cd16148   197 TSDHG----EEFGEHgLYWGHGSNLY-DEQLH---VPLIIR 229
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
 458-694 1.19e-07

Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 55.30  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 458 KKLKQKPNVVVIMNET--FSDLNvvnkiktnKEVMPFINSLSENTI--KGHMlvsvfggGTSNSeyeflTGNSVSSL--P 531
Cdd:COG3083   239 SDPAKPPNILLIVVDSlrADMLD--------PEVMPNLYAFAQRSLrfTNHY-------SSGNS-----TRAGLFGLfyG 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 532 LNGNAYTQFVKHKVPS-LASQLKQQGYDtlaFHPYKAHGWNrdtvYPLigFDN--FLDETSMNPNGEKfRGWYSDAEDYN 608
Cdd:COG3083   299 LPGNYWDSILAERTPPvLIDALQQQGYQ---FGLFSSAGFN----SPL--FRQtiFSDVSLPRLHTPG-GPAQRDRQITA 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 609 KIIDIFNKKKAGQPLFLF--------NVTIQNHGGYLIADKNFKEEIKIKDEKATDTANRYLSLIHESDRAFEKIINYFK 680
Cdd:COG3083   369 QWLQWLDQRDSDRPWFSYlfldaphaYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLE 448

                         250
                  ....*....|....*.
gi 2567119174 681 NQK--EPTIVVMFGDH 694
Cdd:COG3083   449 QRGllENTIVIITADH 464
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 534-694 7.37e-07

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: 52.13  E-value: 7.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 534 GNAYTQFVKH-KVPSLASQLKQQGYDTLAFHpyKAHGwNRDTVYPligfdnFLDETSMNPNGEKFRGWYSDaedynKIID 612
Cdd:cd16027    68 GLRSRGFPLPdGVKTLPELLREAGYYTGLIG--KTHY-NPDAVFP------FDDEMRGPDDGGRNAWDYAS-----NAAD 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 613 IFNKKKAGQPLFL---FNVTiqnHGGYliaDKNFKEEIKIKDEKAT-------------DTAnRYLSLIHESDRAFEKII 676
Cdd:cd16027   134 FLNRAKKGQPFFLwfgFHDP---HRPY---PPGDGEEPGYDPEKVKvppylpdtpevreDLA-DYYDEIERLDQQVGEIL 206

                         170       180
                  ....*....|....*....|
gi 2567119174 677 NYFKNQKEP--TIVVMFGDH 694
Cdd:cd16027   207 DELEEDGLLdnTIVIFTSDH 226
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 542-694 1.78e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 51.03  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 542 KHKVPSLASQLKQQGYDT-------LAFHPYKAHGWNRDTV---YPLiGFDNFLdetSMNPNGEKFRGWYSD-------- 603
Cdd:cd16034    76 PPDAPTIADVLKDAGYRTgyigkwhLDGPERNDGRADDYTPppeRRH-GFDYWK---GYECNHDHNNPHYYDddgkriyi 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 604 ---AEDY--NKIID-IFNKKKAGQPLFLFnVTIQN-HGGYLIA---------------DKNFKEEIKIKDEKATDTANrY 661
Cdd:cd16034   152 kgySPDAetDLAIEyLENQADKDKPFALV-LSWNPpHDPYTTApeeyldmydpkklllRPNVPEDKKEEAGLREDLRG-Y 229

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2567119174 662 LSLIHESDRAFEKIINYFK--NQKEPTIVVMFGDH 694
Cdd:cd16034   230 YAMITALDDNIGRLLDALKelGLLENTIVVFTSDH 264
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 464-706 1.12e-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: 48.74  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 464 PNVVVIMNETF--SDLNVVN---KIKTnkevmPFINSLSENTIK---GHMLVSVfgggTSNSEYEFLTGNSV--SSLP-- 531
Cdd:cd16143     1 PNIVIILADDLgyGDISCYNpdsKIPT-----PNIDRLAAEGMRftdAHSPSSV----CTPSRYGLLTGRYPwrSRLKgg 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 532 -LNGNAYTQFVKHKVpSLASQLKQQGYDTLAF------------HPYKAHG-------WNRDTVY-PL-IGFDNFLdets 589
Cdd:cd16143    72 vLGGFSPPLIEPDRV-TLAKMLKQAGYRTAMVgkwhlgldwkkkDGKKAATgtgkdvdYSKPIKGgPLdHGFDYYF---- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 590 MNPNGEKFRGWYSDAEDYnkiidIFNKKKAGQPLFLFNVTIQNHGGYLIAdknfkEEIKIKdekatDTANRYLSLIHESD 669
Cdd:cd16143   147 GIPASEVLPTLTDKAVEF-----IDQHAKKDKPFFLYFALPAPHTPIVPS-----PEFQGK-----SGAGPYGDFVYELD 211

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2567119174 670 RAFEKIINYFKNQK--EPTIVVMFGDHQPKLEDSFYELL 706
Cdd:cd16143   212 WVVGRILDALKELGlaENTLVIFTSDNGPSPYADYKELE 250
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 463-760 2.56e-04

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: 43.77  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 463 KPNVVVIMNET-----FSdlnvVN--KIKTNkevmPFINSLSENTIkghmlvsVFGGGTSNSeyeFLTGNSVSSL--PLN 533
Cdd:cd16017     2 PKNVVLVIGESarrdhMS----LYgyPRDTT----PFLSKLKKNLI-------VFDNVISCG---TSTAVSLPCMlsFAN 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 534 GNAYTQFvkHKVPSLASQLKQQGYDTLafhpykahgW--NRDTVYpliGFDNFLDETSMNPNGEKFRGWYSDAEDY-NKI 610
Cdd:cd16017    64 RENYDRA--YYQENLIDLAKKAGYKTY---------WisNQGGCG---GYDTRISAIAKIETVFTNKGSCNSSNCYdEAL 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 611 IDIFNK--KKAGQPLFLFNVTIQNHGGYliaDKNFKEEIK---------IKDEKATDTANRYLSLIHESDRAFEKIINYF 679
Cdd:cd16017   130 LPLLDEalADSSKKKLIVLHLMGSHGPY---YDRYPEEFAkftpdcdneLQSCSKEELINAYDNSILYTDYVLSQIIERL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 680 KNQKEPTIVVMFGDHQpklEDSFYELLYGKSLNSLSlkelQKKYTVPFIIWANYDIDAKSDVEN--------VSANYLSS 751
Cdd:cd16017   207 KKKDKDAALIYFSDHG---ESLGENGLYLHGAPYAP----KEQYHVPFIIWSSDSYKQRYPVERlrankdrpFSHDNLFH 279


                  ....*....
gi 2567119174 752 LMLQQTNLK 760
Cdd:cd16017   280 TLLGLLGIK 288
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 464-567 2.86e-03

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 40.10  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567119174 464 PNVVVIMNETFSDLNVvNKIKTNKEVMPFINSLSENTIKGHMLVSVFGGGTSNSEYEFLTGnsvsSLPLNGNAYT----- 538
Cdd:cd00016     1 KHVVLIVLDGLGADDL-GKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTG----AYPTLHGYTGngsad 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2567119174 539 -----QFVKHK--VPSLASQLKQQGYDTLAFHPYKA 567
Cdd:cd00016    76 pelpsRAAGKDedGPTIPELLKQAGYRTGVIGLLKA 111
 
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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