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Conserved domains on  [gi|488288901|ref|WP_002360109|]
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MULTISPECIES: LTA synthase family protein [Enterococcus]

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 ...
19-629 9.24e-134

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


:

Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 405.58  E-value: 9.24e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  19 WAKTILaYYLDFSLGVKGSLQ---REILWFNPVATTLLLFGFSLY---FKKHKTFMLSLTLLNVLNTLILYLNIIFYREF 92
Cdd:COG1368   10 SLRLVF-LLFNFDLSLGEILQaflYGLRFILYLLLLLLLLLLLLLpllFRRPKLRWIYLLLVLLLLLLLLVADILYYRFF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  93 TDFITIQSVFGFSKVSEGISgdllALMRVHDVFYWLDTLVLLVLVFYSFKQRRnhQVFVTKPINRRLAISISCLSVLLFS 172
Cdd:COG1368   89 GDRLNFSDLDYLGDTGEVLG----SLLSSYDLLLLLDLLLLLLLLLLLYRLLK--KLRKSLPWRKRLALLLLLLALLLLG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 173 VNLFlseTDRPQLLQRIFDRNYIVKYLGLD-AFTAIDGVKtamSNEVRAEASSNELPEIMKFTKQNNLPLNPQyaGIAKG 251
Cdd:COG1368  163 IRLG---EDRPLNLSDAFSRNNFVNELGLNgPYSFYDALR---NNKAPATYSEEEALEIKKYLKSNRPTPNPF--GPAKK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 252 KNVFVIHLESFQQFLINMKVQGQEVTPFLNQLYQNkaTISFDNFFHEVGqgKTSDAENMLETGTFGLPQGSlFTQLGSDN 331
Cdd:COG1368  235 PNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKE--SLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGS-PYKRPGQN 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 332 TFEAAPAVLGQKGYTTAVFHGNVGSFWNRDHVYKNLGYQYFFDRSYFsKDDKMLGYGILDKQLLRESASELEHLQQPFYA 411
Cdd:COG1368  310 NFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDF-DDPFDGGWGVSDEDLFDKALEELEKLKKPFFA 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 412 KFLTVTNHTPYYTDDQNFPFPKlnTGNSIVDDYVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVIYGDHFGISDANNKDLc 491
Cdd:COG1368  389 FLITLSNHGPYTLPEEDKKIPD--YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYE- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 492 kafnrdpktwtnyDNAQLQRVPLMFYMPGYTQGKIMHEYGGEIDVLPTLYHLLGVDDKNYIHFGTDLLSPQYKQvVPFRN 571
Cdd:COG1368  466 -------------NPLERYRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDP-FAFRN 531
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488288901 572 GDFVTprfsylGGEIYNNQGKKLDQVPADLKAEvtkdndwVKKSLSLSDKLNQENLLR 629
Cdd:COG1368  532 GGFIT------DDYVYVLKTGELTEEDKELEEE-------ALAYLQLSDYLYGNDLLR 576
 
Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
19-629 9.24e-134

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 405.58  E-value: 9.24e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  19 WAKTILaYYLDFSLGVKGSLQ---REILWFNPVATTLLLFGFSLY---FKKHKTFMLSLTLLNVLNTLILYLNIIFYREF 92
Cdd:COG1368   10 SLRLVF-LLFNFDLSLGEILQaflYGLRFILYLLLLLLLLLLLLLpllFRRPKLRWIYLLLVLLLLLLLLVADILYYRFF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  93 TDFITIQSVFGFSKVSEGISgdllALMRVHDVFYWLDTLVLLVLVFYSFKQRRnhQVFVTKPINRRLAISISCLSVLLFS 172
Cdd:COG1368   89 GDRLNFSDLDYLGDTGEVLG----SLLSSYDLLLLLDLLLLLLLLLLLYRLLK--KLRKSLPWRKRLALLLLLLALLLLG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 173 VNLFlseTDRPQLLQRIFDRNYIVKYLGLD-AFTAIDGVKtamSNEVRAEASSNELPEIMKFTKQNNLPLNPQyaGIAKG 251
Cdd:COG1368  163 IRLG---EDRPLNLSDAFSRNNFVNELGLNgPYSFYDALR---NNKAPATYSEEEALEIKKYLKSNRPTPNPF--GPAKK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 252 KNVFVIHLESFQQFLINMKVQGQEVTPFLNQLYQNkaTISFDNFFHEVGqgKTSDAENMLETGTFGLPQGSlFTQLGSDN 331
Cdd:COG1368  235 PNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKE--SLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGS-PYKRPGQN 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 332 TFEAAPAVLGQKGYTTAVFHGNVGSFWNRDHVYKNLGYQYFFDRSYFsKDDKMLGYGILDKQLLRESASELEHLQQPFYA 411
Cdd:COG1368  310 NFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDF-DDPFDGGWGVSDEDLFDKALEELEKLKKPFFA 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 412 KFLTVTNHTPYYTDDQNFPFPKlnTGNSIVDDYVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVIYGDHFGISDANNKDLc 491
Cdd:COG1368  389 FLITLSNHGPYTLPEEDKKIPD--YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYE- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 492 kafnrdpktwtnyDNAQLQRVPLMFYMPGYTQGKIMHEYGGEIDVLPTLYHLLGVDDKNYIHFGTDLLSPQYKQvVPFRN 571
Cdd:COG1368  466 -------------NPLERYRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDP-FAFRN 531
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488288901 572 GDFVTprfsylGGEIYNNQGKKLDQVPADLKAEvtkdndwVKKSLSLSDKLNQENLLR 629
Cdd:COG1368  532 GGFIT------DDYVYVLKTGELTEEDKELEEE-------ALAYLQLSDYLYGNDLLR 576
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
252-545 1.34e-72

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: 236.43  E-value: 1.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 252 KNVFVIHLESFQQFLINMKVQGQEVTPFLNQLYQNkaTISFDNFFHEVGQGKTSDAENMLETGTFGLPQGSLFTQLGSDN 331
Cdd:cd16015    1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKE--GLYFGNFYSPGFGGGTANGEFEVLTGLPPLPLGSGSYTLYKLN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 332 TFEAAPAVLGQKGYTTAVFHGNVGSFWNRDHVYKNLGYQYFFDRSYFSKDDKML-GYGILDKQLLRESASELEHLQ-QPF 409
Cdd:cd16015   79 PLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETnGWGVSDESLFDQALEELEELKkKPF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 410 YAKFLTVTNHTPYYTDDQNFPFP-KLNTGNSIVDDYVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVIYGDHFGISDANNK 488
Cdd:cd16015  159 FIFLVTMSNHGPYDLPEEKKDEPlKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488288901 489 DlckafnrdpktwTNYDNAQLQRVPLMFYMPGYTQGKIMHEYGGEIDVLPTLYHLLG 545
Cdd:cd16015  239 E------------TDEDPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
Sulfatase pfam00884
Sulfatase;
252-546 1.24e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 139.48  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  252 KNVFVIHLESFQQFliNMKVQG--QEVTPFLNQLYQNkaTISFDNFFheVGQGKTSDAENMLETGTFGLPQGSLFTQL-G 328
Cdd:pfam00884   1 PNVVLVLGESLRAP--DLGLYGypRPTTPFLDRLAEE--GLLFSNFY--SGGTLTAPSRFALLTGLPPHNFGSYVSTPvG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  329 SDNTFEAAPAVLGQKGYTTAVFHGNVGSFWNRDHVyKNLGYQYFFDRSYFSKDDKM--------LGYGILDKQLLRESAS 400
Cdd:pfam00884  75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSP-CNLGFDKFFGRNTGSDLYADppdvpyncSGGGVSDEALLDEALE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  401 ELEHLQQPFYAKFLTVTNHTPYYTDDQ-----NFPFPKLNTGNSIVDDYVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVI 475
Cdd:pfam00884 154 FLDNNDKPFFLVLHTLGSHGPPYYPDRypekyATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVY 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288901  476 YGDHFGISDANNKDLckafnRDPKTWTNYDnaQLQRVPLMFYMPG-YTQGKIMHEYGGEIDVLPTLYHLLGV 546
Cdd:pfam00884 234 TSDHGESLGEGGGYL-----HGGKYDNAPE--GGYRVPLLIWSPGgKAKGQKSEALVSHVDLFPTILDLAGI 298
PRK12363 PRK12363
phosphoglycerol transferase I; Provisional
242-562 1.56e-08

phosphoglycerol transferase I; Provisional


Pssm-ID: 171438  Cd Length: 703  Bit Score: 57.99  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 242 NPQYAgIAKGKNVFVIHLESFQQFLINMKVQgQEVTPFLNQLyqnkATISFD--NFFHEVGQGKTsdAENMLETgTFGLP 319
Cdd:PRK12363 148 VPQQP-LQKRKNIVWIYGESLERTYFDEDVF-PGLMPNLTRL----ATEAVDvrNLASTEGSGWT--IAGMVAS-MCGVP 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 320 qgsLFTQLGSDNT------FEAAPAVLG----QKGYTTAVFHGNVGSFWNRDHVYKNLGYQYFFDRSYFSKDDKML---- 385
Cdd:PRK12363 219 ---LTTAQGDENSmdrmghFLPEARCLGdylkDQGYTNHYVGGADASFAGKGKFLSSHGFDEVHDVNYFLHDKGVApkhf 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 386 -GYGILDKQLLRESASELEHLQ---QPFYAKFLTVTNHTP--YYTDDQNFPFPKLNTGNSIVDDYVRTAHYLdqsLEQFF 459
Cdd:PRK12363 296 sAWGVHDDVLLDDAYDEFETLSragQPFMLTTLTMDTHHPagHLPSACKGQRYDSPLGDIGMLHAIKCSDRL---IGQLV 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 460 HYLQTTSLYNHSIFVIYGDHFGISDANNKDLCKafnrdpktwtnydnaQLQRVPLMFYMPGYTQGKIMHEYGGEIDVLPT 539
Cdd:PRK12363 373 DRIRNSRYGKNTIIVIASDHLAMPNDLSDVLTK---------------QKRENLLLFLGKDIAPQQVVTRAGTTLDSGAT 437
                        330       340
                 ....*....|....*....|...
gi 488288901 540 LYHLLGVDDKNYiHFGTDLLSPQ 562
Cdd:PRK12363 438 LLQLLEPGMRTL-GFGRSLLADD 459
 
Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
19-629 9.24e-134

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 405.58  E-value: 9.24e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  19 WAKTILaYYLDFSLGVKGSLQ---REILWFNPVATTLLLFGFSLY---FKKHKTFMLSLTLLNVLNTLILYLNIIFYREF 92
Cdd:COG1368   10 SLRLVF-LLFNFDLSLGEILQaflYGLRFILYLLLLLLLLLLLLLpllFRRPKLRWIYLLLVLLLLLLLLVADILYYRFF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  93 TDFITIQSVFGFSKVSEGISgdllALMRVHDVFYWLDTLVLLVLVFYSFKQRRnhQVFVTKPINRRLAISISCLSVLLFS 172
Cdd:COG1368   89 GDRLNFSDLDYLGDTGEVLG----SLLSSYDLLLLLDLLLLLLLLLLLYRLLK--KLRKSLPWRKRLALLLLLLALLLLG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 173 VNLFlseTDRPQLLQRIFDRNYIVKYLGLD-AFTAIDGVKtamSNEVRAEASSNELPEIMKFTKQNNLPLNPQyaGIAKG 251
Cdd:COG1368  163 IRLG---EDRPLNLSDAFSRNNFVNELGLNgPYSFYDALR---NNKAPATYSEEEALEIKKYLKSNRPTPNPF--GPAKK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 252 KNVFVIHLESFQQFLINMKVQGQEVTPFLNQLYQNkaTISFDNFFHEVGqgKTSDAENMLETGTFGLPQGSlFTQLGSDN 331
Cdd:COG1368  235 PNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKE--SLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGS-PYKRPGQN 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 332 TFEAAPAVLGQKGYTTAVFHGNVGSFWNRDHVYKNLGYQYFFDRSYFsKDDKMLGYGILDKQLLRESASELEHLQQPFYA 411
Cdd:COG1368  310 NFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDF-DDPFDGGWGVSDEDLFDKALEELEKLKKPFFA 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 412 KFLTVTNHTPYYTDDQNFPFPKlnTGNSIVDDYVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVIYGDHFGISDANNKDLc 491
Cdd:COG1368  389 FLITLSNHGPYTLPEEDKKIPD--YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYE- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 492 kafnrdpktwtnyDNAQLQRVPLMFYMPGYTQGKIMHEYGGEIDVLPTLYHLLGVDDKNYIHFGTDLLSPQYKQvVPFRN 571
Cdd:COG1368  466 -------------NPLERYRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDP-FAFRN 531
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488288901 572 GDFVTprfsylGGEIYNNQGKKLDQVPADLKAEvtkdndwVKKSLSLSDKLNQENLLR 629
Cdd:COG1368  532 GGFIT------DDYVYVLKTGELTEEDKELEEE-------ALAYLQLSDYLYGNDLLR 576
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
252-545 1.34e-72

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: 236.43  E-value: 1.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 252 KNVFVIHLESFQQFLINMKVQGQEVTPFLNQLYQNkaTISFDNFFHEVGQGKTSDAENMLETGTFGLPQGSLFTQLGSDN 331
Cdd:cd16015    1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKE--GLYFGNFYSPGFGGGTANGEFEVLTGLPPLPLGSGSYTLYKLN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 332 TFEAAPAVLGQKGYTTAVFHGNVGSFWNRDHVYKNLGYQYFFDRSYFSKDDKML-GYGILDKQLLRESASELEHLQ-QPF 409
Cdd:cd16015   79 PLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETnGWGVSDESLFDQALEELEELKkKPF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 410 YAKFLTVTNHTPYYTDDQNFPFP-KLNTGNSIVDDYVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVIYGDHFGISDANNK 488
Cdd:cd16015  159 FIFLVTMSNHGPYDLPEEKKDEPlKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488288901 489 DlckafnrdpktwTNYDNAQLQRVPLMFYMPGYTQGKIMHEYGGEIDVLPTLYHLLG 545
Cdd:cd16015  239 E------------TDEDPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
Sulfatase pfam00884
Sulfatase;
252-546 1.24e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 139.48  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  252 KNVFVIHLESFQQFliNMKVQG--QEVTPFLNQLYQNkaTISFDNFFheVGQGKTSDAENMLETGTFGLPQGSLFTQL-G 328
Cdd:pfam00884   1 PNVVLVLGESLRAP--DLGLYGypRPTTPFLDRLAEE--GLLFSNFY--SGGTLTAPSRFALLTGLPPHNFGSYVSTPvG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  329 SDNTFEAAPAVLGQKGYTTAVFHGNVGSFWNRDHVyKNLGYQYFFDRSYFSKDDKM--------LGYGILDKQLLRESAS 400
Cdd:pfam00884  75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSP-CNLGFDKFFGRNTGSDLYADppdvpyncSGGGVSDEALLDEALE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901  401 ELEHLQQPFYAKFLTVTNHTPYYTDDQ-----NFPFPKLNTGNSIVDDYVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVI 475
Cdd:pfam00884 154 FLDNNDKPFFLVLHTLGSHGPPYYPDRypekyATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVY 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288901  476 YGDHFGISDANNKDLckafnRDPKTWTNYDnaQLQRVPLMFYMPG-YTQGKIMHEYGGEIDVLPTLYHLLGV 546
Cdd:pfam00884 234 TSDHGESLGEGGGYL-----HGGKYDNAPE--GGYRVPLLIWSPGgKAKGQKSEALVSHVDLFPTILDLAGI 298
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
252-560 9.93e-17

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: 80.67  E-value: 9.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 252 KNVFVIHLESFQQFLINMKVQGQEVTPFLNQLYQNkaTISFDNFFhevgqgkTSDAENM-----LETGTFGLPQGSLFTQ 326
Cdd:cd16148    1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAE--GVVFDNHY-------SGSNPTLpsrfsLFTGLYPFYHGVWGGP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 327 LGSDNTFeaAPAVLGQKGYTTAVFHGNVGSFWNR------DHVYKNLGYQYFFDRSYFSKDDKMLGYGIldkQLLRESAS 400
Cdd:cd16148   72 LEPDDPT--LAEILRKAGYYTAAVSSNPHLFGGPgfdrgfDTFEDFRGQEGDPGEEGDERAERVTDRAL---EWLDRNAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 401 ElehlqQPFyakFLTV---TNHTPYytddqnfpfpklntgnsivdDYVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVIYG 477
Cdd:cd16148  147 D-----DPF---FLFLhyfDPHEPY--------------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTS 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 478 DH---FGISDANNKDlckafnrdpktWTNYDNAQLqRVPLMFYMPGYTQGKIMHEYGGEIDVLPTLYHLLGVDDKNYIHf 554
Cdd:cd16148  199 DHgeeFGEHGLYWGH-----------GSNLYDEQL-HVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSD- 265

                 ....*.
gi 488288901 555 GTDLLS 560
Cdd:cd16148  266 GRSLLP 271
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
252-544 5.58e-14

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: 72.07  E-value: 5.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 252 KNVFVIHLESFQQFLINMKVQGQEVTPFLNQLYQNKATisfDNFFHEVGQGKTSDAENMLETGTFGLPQGS--------- 322
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGAT---FNFRSVSPPTSSAPNHAALLTGAYPTLHGYtgngsadpe 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 323 -LFTQLGSDNTFEAAPAVLGQKGYTTAVFHgnvgsfwNRDHVYKNLGYQYFFdrSYFskddkmlgygildkqllresase 401
Cdd:cd00016   78 lPSRAAGKDEDGPTIPELLKQAGYRTGVIG-------LLKAIDETSKEKPFV--LFL----------------------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 402 leHLQQPFYAKFLTVTNHTPYYtddqnfpfpklntgnsivdDYVRtahYLDQSLEQFFHYLQTTSLYNHSIFVIYGDHFG 481
Cdd:cd00016  126 --HFDGPDGPGHAYGPNTPEYY-------------------DAVE---EIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288901 482 IsdannkdlCKAFNRDPKTWTNYDNAQLQ-RVPLMFYMPGYTQGKIMHEYGGEIDVLPTLYHLL 544
Cdd:cd00016  182 I--------DKGHGGDPKADGKADKSHTGmRVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
PRK12363 PRK12363
phosphoglycerol transferase I; Provisional
242-562 1.56e-08

phosphoglycerol transferase I; Provisional


Pssm-ID: 171438  Cd Length: 703  Bit Score: 57.99  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 242 NPQYAgIAKGKNVFVIHLESFQQFLINMKVQgQEVTPFLNQLyqnkATISFD--NFFHEVGQGKTsdAENMLETgTFGLP 319
Cdd:PRK12363 148 VPQQP-LQKRKNIVWIYGESLERTYFDEDVF-PGLMPNLTRL----ATEAVDvrNLASTEGSGWT--IAGMVAS-MCGVP 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 320 qgsLFTQLGSDNT------FEAAPAVLG----QKGYTTAVFHGNVGSFWNRDHVYKNLGYQYFFDRSYFSKDDKML---- 385
Cdd:PRK12363 219 ---LTTAQGDENSmdrmghFLPEARCLGdylkDQGYTNHYVGGADASFAGKGKFLSSHGFDEVHDVNYFLHDKGVApkhf 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 386 -GYGILDKQLLRESASELEHLQ---QPFYAKFLTVTNHTP--YYTDDQNFPFPKLNTGNSIVDDYVRTAHYLdqsLEQFF 459
Cdd:PRK12363 296 sAWGVHDDVLLDDAYDEFETLSragQPFMLTTLTMDTHHPagHLPSACKGQRYDSPLGDIGMLHAIKCSDRL---IGQLV 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 460 HYLQTTSLYNHSIFVIYGDHFGISDANNKDLCKafnrdpktwtnydnaQLQRVPLMFYMPGYTQGKIMHEYGGEIDVLPT 539
Cdd:PRK12363 373 DRIRNSRYGKNTIIVIASDHLAMPNDLSDVLTK---------------QKRENLLLFLGKDIAPQQVVTRAGTTLDSGAT 437
                        330       340
                 ....*....|....*....|...
gi 488288901 540 LYHLLGVDDKNYiHFGTDLLSPQ 562
Cdd:PRK12363 438 LLQLLEPGMRTL-GFGRSLLADD 459
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
337-559 3.15e-08

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 56.43  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 337 PAVLGQKGYTTAVFhGNvgsfWnrdHVYKNlgyQYFFDRSyfskddkmlgygildKQLLRESASElehlQQPFYAKFLTV 416
Cdd:COG3119  109 AELLKEAGYRTALF-GK----W---HLYLT---DLLTDKA---------------IDFLERQADK----DKPFFLYLAFN 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 417 TNHTPYYT--------DDQNFPFPKLNTGNSIVDDYVRTA--------HYLDQSLEQFFHYLQTTSLYNHSIFVIYGDHF 480
Cdd:COG3119  159 APHAPYQApeeyldkyDGKDIPLPPNLAPRDLTEEELRRAraayaamiEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 481 GISDANNKDLCKafnrdpktWTNYDNAQlqRVPLMFYMPGYTQ-GKIMHEYGGEIDVLPTLYHLLGVDDKNYIHfGTDLL 559
Cdd:COG3119  239 PSLGEHGLRGGK--------GTLYEGGI--RVPLIVRWPGKIKaGSVSDALVSLIDLLPTLLDLAGVPIPEDLD-GRSLL 307
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
337-575 4.71e-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: 52.51  E-value: 4.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 337 PAVLGQKGYTTavfhGNVGsfwnRDHVYKNLGYQYFFDRSYFSKDDKMLGYGILDKQLLRESASElehlQQPFYAKFLTV 416
Cdd:cd16027   84 PELLREAGYYT----GLIG----KTHYNPDAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKK----GQPFFLWFGFH 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 417 TNHTPYYTDDQNFPFPKLNtgNSIVDDY------VR--TAHY------LDQSLEQFFHYLQTTSLYNHSIFVIYGDHfGI 482
Cdd:cd16027  152 DPHRPYPPGDGEEPGYDPE--KVKVPPYlpdtpeVRedLADYydeierLDQQVGEILDELEEDGLLDNTIVIFTSDH-GM 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 483 sdannkdlckAFNRDpKtWTNYDNAqlQRVPLMFYMPGYTQGK------IMHeyggeIDVLPTLYHLLGVDDKNYIHfGT 556
Cdd:cd16027  229 ----------PFPRA-K-GTLYDSG--LRVPLIVRWPGKIKPGsvsdalVSF-----IDLAPTLLDLAGIEPPEYLQ-GR 288
                        250
                 ....*....|....*....
gi 488288901 557 DLLSPQYKQVVPFRngDFV 575
Cdd:cd16027  289 SFLPLLKGEKDPGR--DYV 305
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
444-548 5.01e-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: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 42.58  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288901 444 YVRTAHYLDQSLEQFFHYLQTTSLYNHSIFVIYGDHfGisdannkDLCKAFNRDPKTWTNYDNAQlqRVPLMFYMPGY-T 522
Cdd:cd16035  169 YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDH-G-------EMGGAHGLRGKGFNAYEEAL--HVPLIISHPDLfG 238
                         90       100
                 ....*....|....*....|....*.
gi 488288901 523 QGKIMHEYGGEIDVLPTLYHLLGVDD 548
Cdd:cd16035  239 TGQTTDALTSHIDLLPTLLGLAGVDA 264
 
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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