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Conserved domains on  [gi|489818936|ref|WP_003722749|]
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MULTISPECIES: lipoteichoic acid synthase LtaS [Listeria]

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 ...
18-625 1.27e-159

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


:

Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 471.06  E-value: 1.27e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  18 FFVLAVILYWLKTYIaYQLEFKLGIENLMQQI---LLFINPLSGAIFFMGLALFA----KGRRSFIWIIVIDFLMSFILY 90
Cdd:COG1368    1 FFLLFLLLLSLRLVF-LLFNFDLSLGEILQAFlygLRFILYLLLLLLLLLLLLLPllfrRPKLRWIYLLLVLLLLLLLLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  91 ANIVYYRFFSDFITLPNLNakQMQNMGDMGSSitaLLSWHDIIYFADIIILIALLAFRFV---KPNKTARIRARKVVGVL 167
Cdd:COG1368   80 ADILYYRFFGDRLNFSDLD--YLGDTGEVLGS---LLSSYDLLLLLDLLLLLLLLLLLYRllkKLRKSLPWRKRLALLLL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 168 TLGIAMFFGNLGlaeIDRPQLLTRTFDRNYIVKYLG-MTNYQIYDAVKSTESstqRALADSSDVTEVLNYTKSKYAAPNP 246
Cdd:COG1368  155 LLALLLLGIRLG---EDRPLNLSDAFSRNNFVNELGlNGPYSFYDALRNNKA---PATYSEEEALEIKKYLKSNRPTPNP 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 247 eyFGKAKGKNVIYIHLESFQQFLVNYKLNGEEVTPFINSFFKdqNTLSFTNFFHQTGqgKTADSEMLLENSLYGLPQGSA 326
Cdd:COG1368  229 --FGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAK--ESLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGSP 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 327 FTTKGQNTYESASAILGQQGYTSAVFHGNYKSFWNRDEIYKQFGYDNFFDASYYDmnEADVSNYGLKDKPFFKESEEYLS 406
Cdd:COG1368  303 YKRPGQNNFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDFD--DPFDGGWGVSDEDLFDKALEELE 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 407 SLQQPFYTKFITLTNHFPYPIDEKDASIAPatTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHYGIS 486
Cdd:COG1368  381 KLKKPFFAFLITLSNHGPYTLPEEDKKIPD--YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 487 DNHEEAMTKIlgkdyntfenaQAQRVPLMIHVPGV-QGGVQEQYGGQVDLLPTLLHLLGVDNKEYLQFGTDLLSKDHKQL 565
Cdd:COG1368  459 PGKTDYENPL-----------ERYRVPLLIYSPGLkKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDPF 527
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 566 vPFRNGDYITPTYsmiggnMYNQQTGEPiateTKEMKETKEKVAKELELSDSVLQGDLLR 625
Cdd:COG1368  528 -AFRNGGFITDDY------VYVLKTGEL----TEEDKELEEEALAYLQLSDYLYGNDLLR 576
 
Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
18-625 1.27e-159

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 471.06  E-value: 1.27e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  18 FFVLAVILYWLKTYIaYQLEFKLGIENLMQQI---LLFINPLSGAIFFMGLALFA----KGRRSFIWIIVIDFLMSFILY 90
Cdd:COG1368    1 FFLLFLLLLSLRLVF-LLFNFDLSLGEILQAFlygLRFILYLLLLLLLLLLLLLPllfrRPKLRWIYLLLVLLLLLLLLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  91 ANIVYYRFFSDFITLPNLNakQMQNMGDMGSSitaLLSWHDIIYFADIIILIALLAFRFV---KPNKTARIRARKVVGVL 167
Cdd:COG1368   80 ADILYYRFFGDRLNFSDLD--YLGDTGEVLGS---LLSSYDLLLLLDLLLLLLLLLLLYRllkKLRKSLPWRKRLALLLL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 168 TLGIAMFFGNLGlaeIDRPQLLTRTFDRNYIVKYLG-MTNYQIYDAVKSTESstqRALADSSDVTEVLNYTKSKYAAPNP 246
Cdd:COG1368  155 LLALLLLGIRLG---EDRPLNLSDAFSRNNFVNELGlNGPYSFYDALRNNKA---PATYSEEEALEIKKYLKSNRPTPNP 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 247 eyFGKAKGKNVIYIHLESFQQFLVNYKLNGEEVTPFINSFFKdqNTLSFTNFFHQTGqgKTADSEMLLENSLYGLPQGSA 326
Cdd:COG1368  229 --FGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAK--ESLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGSP 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 327 FTTKGQNTYESASAILGQQGYTSAVFHGNYKSFWNRDEIYKQFGYDNFFDASYYDmnEADVSNYGLKDKPFFKESEEYLS 406
Cdd:COG1368  303 YKRPGQNNFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDFD--DPFDGGWGVSDEDLFDKALEELE 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 407 SLQQPFYTKFITLTNHFPYPIDEKDASIAPatTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHYGIS 486
Cdd:COG1368  381 KLKKPFFAFLITLSNHGPYTLPEEDKKIPD--YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 487 DNHEEAMTKIlgkdyntfenaQAQRVPLMIHVPGV-QGGVQEQYGGQVDLLPTLLHLLGVDNKEYLQFGTDLLSKDHKQL 565
Cdd:COG1368  459 PGKTDYENPL-----------ERYRVPLLIYSPGLkKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDPF 527
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 566 vPFRNGDYITPTYsmiggnMYNQQTGEPiateTKEMKETKEKVAKELELSDSVLQGDLLR 625
Cdd:COG1368  528 -AFRNGGFITDDY------VYVLKTGEL----TEEDKELEEEALAYLQLSDYLYGNDLLR 576
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
255-534 3.37e-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: 234.50  E-value: 3.37e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 255 KNVIYIHLESFQQFLVNYKLNGEEVTPFINSFFKdqNTLSFTNFFHQTGQGKTADSEMLLENSLYGLPQGSAFTT-KGQN 333
Cdd:cd16015    1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAK--EGLYFGNFYSPGFGGGTANGEFEVLTGLPPLPLGSGSYTlYKLN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 334 TYESASAILGQQGYTSAVFHGNYKSFWNRDEIYKQFGYDNFFDASYYDMNEADVSNYGLKDKPFFKESEEYLSSLQ-QPF 412
Cdd:cd16015   79 PLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDESLFDQALEELEELKkKPF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 413 YTKFITLTNHFPYPIDEKDASI-APATTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHYGISDNHEe 491
Cdd:cd16015  159 FIFLVTMSNHGPYDLPEEKKDEpLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDY- 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489818936 492 amtkilgkDYNTFENAQAQRVPLMIHVPG-VQGGVQEQYGGQVD 534
Cdd:cd16015  238 --------DETDEDPLDLYRTPLLIYSPGlKKPKKIDRVGSQID 273
Sulfatase pfam00884
Sulfatase;
255-534 6.79e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 136.78  E-value: 6.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  255 KNVIYIHLESFQQFLVNYKLNGEEVTPFINSffKDQNTLSFTNFFhqTGQGKTADSEMLLENSLYGLPQGSAFTTKGQ-- 332
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDR--LAEEGLLFSNFY--SGGTLTAPSRFALLTGLPPHNFGSYVSTPVGlp 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  333 NTYESASAILGQQGYTSAVFHGNYKSFWNRDEIYKQfGYDNFFD-----ASYYDMNEADV--SNYGLKDKPFFKESEEYL 405
Cdd:pfam00884  77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNL-GFDKFFGrntgsDLYADPPDVPYncSGGGVSDEALLDEALEFL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  406 SSLQQPFYTKFITLTNHFPYPIDEKDA-----SIAPATTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYG 480
Cdd:pfam00884 156 DNNDKPFFLVLHTLGSHGPPYYPDRYPekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTS 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489818936  481 DHYGISDnhEEAMTKILGKDYNTFEnaQAQRVPLMIHVPGV--QGGVQEQYGGQVD 534
Cdd:pfam00884 236 DHGESLG--EGGGYLHGGKYDNAPE--GGYRVPLLIWSPGGkaKGQKSEALVSHVD 287
PRK12363 PRK12363
phosphoglycerol transferase I; Provisional
241-500 7.07e-10

phosphoglycerol transferase I; Provisional


Pssm-ID: 171438  Cd Length: 703  Bit Score: 62.23  E-value: 7.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 241 YAAPNPEY----FGKAKGKNVIYIHLESFQQFLVNyklngEEV----TPFINSFFKDqnTLSFTNFFHQTGQGKTADSem 312
Cdd:PRK12363 139 FATVAPEYqvpqQPLQKRKNIVWIYGESLERTYFD-----EDVfpglMPNLTRLATE--AVDVRNLASTEGSGWTIAG-- 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 313 lLENSLYGLP----QGSAFTTKGQNTYESASAILG----QQGYTSAVFHGNYKSFWNRDEIYKQFGYDNFFDASYYDMN- 383
Cdd:PRK12363 210 -MVASMCGVPlttaQGDENSMDRMGHFLPEARCLGdylkDQGYTNHYVGGADASFAGKGKFLSSHGFDEVHDVNYFLHDk 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 384 ---EADVSNYGLKDKPFFK---ESEEYLSSLQQPFYTKFITLTNHFP---YPIdEKDASIAPATTGDSSVDTYFQTARYL 454
Cdd:PRK12363 289 gvaPKHFSAWGVHDDVLLDdayDEFETLSRAGQPFMLTTLTMDTHHPaghLPS-ACKGQRYDSPLGDIGMLHAIKCSDRL 367
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489818936 455 desVKSFVDYLKKSGLYDNSVIIMYGDHYGISDNHEEAMTK--------ILGKD 500
Cdd:PRK12363 368 ---IGQLVDRIRNSRYGKNTIIVIASDHLAMPNDLSDVLTKqkrenlllFLGKD 418
 
Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
18-625 1.27e-159

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 471.06  E-value: 1.27e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  18 FFVLAVILYWLKTYIaYQLEFKLGIENLMQQI---LLFINPLSGAIFFMGLALFA----KGRRSFIWIIVIDFLMSFILY 90
Cdd:COG1368    1 FFLLFLLLLSLRLVF-LLFNFDLSLGEILQAFlygLRFILYLLLLLLLLLLLLLPllfrRPKLRWIYLLLVLLLLLLLLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  91 ANIVYYRFFSDFITLPNLNakQMQNMGDMGSSitaLLSWHDIIYFADIIILIALLAFRFV---KPNKTARIRARKVVGVL 167
Cdd:COG1368   80 ADILYYRFFGDRLNFSDLD--YLGDTGEVLGS---LLSSYDLLLLLDLLLLLLLLLLLYRllkKLRKSLPWRKRLALLLL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 168 TLGIAMFFGNLGlaeIDRPQLLTRTFDRNYIVKYLG-MTNYQIYDAVKSTESstqRALADSSDVTEVLNYTKSKYAAPNP 246
Cdd:COG1368  155 LLALLLLGIRLG---EDRPLNLSDAFSRNNFVNELGlNGPYSFYDALRNNKA---PATYSEEEALEIKKYLKSNRPTPNP 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 247 eyFGKAKGKNVIYIHLESFQQFLVNYKLNGEEVTPFINSFFKdqNTLSFTNFFHQTGqgKTADSEMLLENSLYGLPQGSA 326
Cdd:COG1368  229 --FGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAK--ESLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGSP 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 327 FTTKGQNTYESASAILGQQGYTSAVFHGNYKSFWNRDEIYKQFGYDNFFDASYYDmnEADVSNYGLKDKPFFKESEEYLS 406
Cdd:COG1368  303 YKRPGQNNFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDFD--DPFDGGWGVSDEDLFDKALEELE 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 407 SLQQPFYTKFITLTNHFPYPIDEKDASIAPatTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHYGIS 486
Cdd:COG1368  381 KLKKPFFAFLITLSNHGPYTLPEEDKKIPD--YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 487 DNHEEAMTKIlgkdyntfenaQAQRVPLMIHVPGV-QGGVQEQYGGQVDLLPTLLHLLGVDNKEYLQFGTDLLSKDHKQL 565
Cdd:COG1368  459 PGKTDYENPL-----------ERYRVPLLIYSPGLkKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDPF 527
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 566 vPFRNGDYITPTYsmiggnMYNQQTGEPiateTKEMKETKEKVAKELELSDSVLQGDLLR 625
Cdd:COG1368  528 -AFRNGGFITDDY------VYVLKTGEL----TEEDKELEEEALAYLQLSDYLYGNDLLR 576
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
255-534 3.37e-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: 234.50  E-value: 3.37e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 255 KNVIYIHLESFQQFLVNYKLNGEEVTPFINSFFKdqNTLSFTNFFHQTGQGKTADSEMLLENSLYGLPQGSAFTT-KGQN 333
Cdd:cd16015    1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAK--EGLYFGNFYSPGFGGGTANGEFEVLTGLPPLPLGSGSYTlYKLN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 334 TYESASAILGQQGYTSAVFHGNYKSFWNRDEIYKQFGYDNFFDASYYDMNEADVSNYGLKDKPFFKESEEYLSSLQ-QPF 412
Cdd:cd16015   79 PLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDESLFDQALEELEELKkKPF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 413 YTKFITLTNHFPYPIDEKDASI-APATTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHYGISDNHEe 491
Cdd:cd16015  159 FIFLVTMSNHGPYDLPEEKKDEpLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDY- 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489818936 492 amtkilgkDYNTFENAQAQRVPLMIHVPG-VQGGVQEQYGGQVD 534
Cdd:cd16015  238 --------DETDEDPLDLYRTPLLIYSPGlKKPKKIDRVGSQID 273
Sulfatase pfam00884
Sulfatase;
255-534 6.79e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 136.78  E-value: 6.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  255 KNVIYIHLESFQQFLVNYKLNGEEVTPFINSffKDQNTLSFTNFFhqTGQGKTADSEMLLENSLYGLPQGSAFTTKGQ-- 332
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDR--LAEEGLLFSNFY--SGGTLTAPSRFALLTGLPPHNFGSYVSTPVGlp 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  333 NTYESASAILGQQGYTSAVFHGNYKSFWNRDEIYKQfGYDNFFD-----ASYYDMNEADV--SNYGLKDKPFFKESEEYL 405
Cdd:pfam00884  77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNL-GFDKFFGrntgsDLYADPPDVPYncSGGGVSDEALLDEALEFL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936  406 SSLQQPFYTKFITLTNHFPYPIDEKDA-----SIAPATTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYG 480
Cdd:pfam00884 156 DNNDKPFFLVLHTLGSHGPPYYPDRYPekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTS 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489818936  481 DHYGISDnhEEAMTKILGKDYNTFEnaQAQRVPLMIHVPGV--QGGVQEQYGGQVD 534
Cdd:pfam00884 236 DHGESLG--EGGGYLHGGKYDNAPE--GGYRVPLLIWSPGGkaKGQKSEALVSHVD 287
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
255-534 8.34e-20

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: 89.02  E-value: 8.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 255 KNVIYIHLESFQQFLVNYKLNGEEVTPFINSffKDQNTLSFtNFFHQTGQGKTADSEMLLENSLYGLPQGSAFTtkgqnt 334
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKR--LASEGATF-NFRSVSPPTSSAPNHAALLTGAYPTLHGYTGN------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 335 yesaSAILGQQGYTSAVFHGNYKSFWnrdEIYKQFGYDnffdasyydmneadVSNYGLKDkpFFKESeeylsSLQQPFYT 414
Cdd:cd00016   72 ----GSADPELPSRAAGKDEDGPTIP---ELLKQAGYR--------------TGVIGLLK--AIDET-----SKEKPFVL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 415 KFITLTNHFPypidekdasiapATTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHYGISDNHEEAMT 494
Cdd:cd00016  124 FLHFDGPDGP------------GHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPK 191
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 489818936 495 KILGKDYNTFENaqaqRVPLMIHVPGVQ-GGVQEQYGGQVD 534
Cdd:cd00016  192 ADGKADKSHTGM----RVPFIAYGPGVKkGGVKHELISQYD 228
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
255-524 3.83e-15

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: 76.05  E-value: 3.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 255 KNVIYIHLESFQQFLVNYKLNGEEVTPFINSFFKDqnTLSFTNffHQTGQGKT--ADSEMLLenSLYGLPQGSaFTTKGQ 332
Cdd:cd16148    1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAE--GVVFDN--HYSGSNPTlpSRFSLFT--GLYPFYHGV-WGGPLE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 333 NTYESASAILGQQGYTSAVFHGNYksfwnrdEIYKQFGYDNFFDasYYDMNEADVSNYGLKDKPF----FKESEEYLSSL 408
Cdd:cd16148   74 PDDPTLAEILRKAGYYTAAVSSNP-------HLFGGPGFDRGFD--TFEDFRGQEGDPGEEGDERaervTDRALEWLDRN 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 409 Q--QPFYTkFI-TLTNHFPYpidEKDASIapattgdssvdtyfqtaRYLDESVKSFVDYLKKSGLYDNSVIIMYGDH-YG 484
Cdd:cd16148  145 AddDPFFL-FLhYFDPHEPY---LYDAEV-----------------RYVDEQIGRLLDKLKELGLLEDTLVIVTSDHgEE 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489818936 485 ISDNHeeamtkILGKDYNTFENAQAqRVPLMIHVPGVQGG 524
Cdd:cd16148  204 FGEHG------LYWGHGSNLYDEQL-HVPLIIRWPGKEPG 236
PRK12363 PRK12363
phosphoglycerol transferase I; Provisional
241-500 7.07e-10

phosphoglycerol transferase I; Provisional


Pssm-ID: 171438  Cd Length: 703  Bit Score: 62.23  E-value: 7.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 241 YAAPNPEY----FGKAKGKNVIYIHLESFQQFLVNyklngEEV----TPFINSFFKDqnTLSFTNFFHQTGQGKTADSem 312
Cdd:PRK12363 139 FATVAPEYqvpqQPLQKRKNIVWIYGESLERTYFD-----EDVfpglMPNLTRLATE--AVDVRNLASTEGSGWTIAG-- 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 313 lLENSLYGLP----QGSAFTTKGQNTYESASAILG----QQGYTSAVFHGNYKSFWNRDEIYKQFGYDNFFDASYYDMN- 383
Cdd:PRK12363 210 -MVASMCGVPlttaQGDENSMDRMGHFLPEARCLGdylkDQGYTNHYVGGADASFAGKGKFLSSHGFDEVHDVNYFLHDk 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 384 ---EADVSNYGLKDKPFFK---ESEEYLSSLQQPFYTKFITLTNHFP---YPIdEKDASIAPATTGDSSVDTYFQTARYL 454
Cdd:PRK12363 289 gvaPKHFSAWGVHDDVLLDdayDEFETLSRAGQPFMLTTLTMDTHHPaghLPS-ACKGQRYDSPLGDIGMLHAIKCSDRL 367
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489818936 455 desVKSFVDYLKKSGLYDNSVIIMYGDHYGISDNHEEAMTK--------ILGKD 500
Cdd:PRK12363 368 ---IGQLVDRIRNSRYGKNTIIVIASDHLAMPNDLSDVLTKqkrenlllFLGKD 418
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
319-521 5.50e-08

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: 55.21  E-value: 5.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 319 YGLPQGSAFTTKGQNTYesaSAILGQQGYTSAVF---HGNYKSFWNRDEIYKQFGYDNFFDASYYDmNEADVSNYGLKDK 395
Cdd:cd16027   67 HGLRSRGFPLPDGVKTL---PELLREAGYYTGLIgktHYNPDAVFPFDDEMRGPDDGGRNAWDYAS-NAADFLNRAKKGQ 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 396 PFFkeseeylssLQ-QPFYTkfitltnHFPYPIDEKDASIAPAttgdSSV-------DT---------YFQTARYLDESV 458
Cdd:cd16027  143 PFF---------LWfGFHDP-------HRPYPPGDGEEPGYDP----EKVkvppylpDTpevredladYYDEIERLDQQV 202
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489818936 459 KSFVDYLKKSGLYDNSVIIMYGDH-------------YGIsdnheeamtkilgkdyntfenaqaqRVPLMIHVPGV 521
Cdd:cd16027  203 GEILDELEEDGLLDNTIVIFTSDHgmpfprakgtlydSGL-------------------------RVPLIVRWPGK 253
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
393-534 7.08e-08

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 55.27  E-value: 7.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 393 KDKPFFkeseeyLS-SLQQPfytkfitltnHFPY--------PIDEKDASIAPATTGDSSVDTYFQTAR--------YLD 455
Cdd:COG3119  147 KDKPFF------LYlAFNAP----------HAPYqapeeyldKYDGKDIPLPPNLAPRDLTEEELRRARaayaamieEVD 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 456 ESVKSFVDYLKKSGLYDNSVIIMYGDHyGIsdnHEEAMTKILGKdYNTFENaqAQRVPLMIHVPGV--QGGVQEQYGGQV 533
Cdd:COG3119  211 DQVGRLLDALEELGLADNTIVVFTSDN-GP---SLGEHGLRGGK-GTLYEG--GIRVPLIVRWPGKikAGSVSDALVSLI 283

                 .
gi 489818936 534 D 534
Cdd:COG3119  284 D 284
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
221-527 9.79e-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: 51.83  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 221 QRALADSSDVTEV-LNYTKSKYaapnpEYFGKAKGKNVIYIHLESfqqflVNYKLNGEEVTPFINSFfkDQNTLSFTNff 299
Cdd:COG3083  215 QQRLEEQGNPEASsLNYPLHPL-----QFSDPAKPPNILLIVVDS-----LRADMLDPEVMPNLYAF--AQRSLRFTN-- 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 300 HQTGqGKTADSEMLlenSL-YGLP-----------QGSAFTTkgqntyesasaILGQQGY-----TSAVFH--------- 353
Cdd:COG3083  281 HYSS-GNSTRAGLF---GLfYGLPgnywdsilaerTPPVLID-----------ALQQQGYqfglfSSAGFNsplfrqtif 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 354 --------GNYKSFWNRDE-IYKQFgyDNFFDAsyydmneadvsnyGLKDKPFFkeSEEYLSSLQQpfYTKFITLTNHFP 424
Cdd:COG3083  346 sdvslprlHTPGGPAQRDRqITAQW--LQWLDQ-------------RDSDRPWF--SYLFLDAPHA--YSFPADYPKPFQ 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 425 YPIDEKDASIAPATTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHyGISDNHEEAMTKILGKDYNtf 504
Cdd:COG3083  407 PSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADH-GEEFNENGQNYWGHNSNFS-- 483
                        330       340
                 ....*....|....*....|...
gi 489818936 505 eNAQAQrVPLMIHVPGVQGGVQE 527
Cdd:COG3083  484 -RYQLQ-VPLVIHWPGTPPQVIS 504
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
447-521 5.05e-06

unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.


Pssm-ID: 293755 [Multi-domain]  Cd Length: 429  Bit Score: 49.45  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 447 YFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDH------YGISDN---HEEAMtkilgkdyntfenaqaqRVPLMIH 517
Cdd:cd16031  239 YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNgfflgeHGLFDKrlmYEESI-----------------RVPLIIR 301

                 ....
gi 489818936 518 VPGV 521
Cdd:cd16031  302 DPRL 305
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
446-534 6.66e-06

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: 47.82  E-value: 6.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 446 TYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHYGISDNHeeamtKILGKDYNTFEnaQAQRVPLMIHVPGV--QG 523
Cdd:cd16022  132 AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDH-----GLRGKKGSLYE--GGIRVPFIVRWPGKipAG 204
                         90
                 ....*....|.
gi 489818936 524 GVQEQYGGQVD 534
Cdd:cd16022  205 QVSDALVSLLD 215
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
447-527 7.38e-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: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 48.36  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 447 YFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHyGisdnhEEAMT-KILGKDYNTFEnaQAQRVPLMIHVPGVQGGV 525
Cdd:cd16035  169 YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDH-G-----EMGGAhGLRGKGFNAYE--EALHVPLIISHPDLFGTG 240

                 ..
gi 489818936 526 QE 527
Cdd:cd16035  241 QT 242
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
447-582 1.05e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 47.99  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 447 YFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHygisDNHeeAMTKilGKDY--NTFENAQaqRVPLMIHVPGVQGG 524
Cdd:cd16152  177 YLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCH--FRTR--NAEYkrSCHESSI--RVPLVIYGPGFNGG 246
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489818936 525 VQ-EQYGGQVDLLPTLLHLLGVDNKEYLQfGTDLLSKDHKQLVPFRNGDYITPTYSMIG 582
Cdd:cd16152  247 GRvEELVSLIDLPPTLLDAAGIDVPEEMQ-GRSLLPLVDGKVEDWRNEVFIQISESQVG 304
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
460-522 2.14e-05

iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.


Pssm-ID: 293754 [Multi-domain]  Cd Length: 435  Bit Score: 47.18  E-value: 2.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818936 460 SFVDY--------LKKSGLYDNSVIIMYGDH-YGISDNHEeamtkiLGKdYNTFEnaQAQRVPLMIHVPGVQ 522
Cdd:cd16030  268 SYVDAqvgrvldaLEELGLADNTIVVLWSDHgWHLGEHGH------WGK-HTLFE--EATRVPLIIRAPGVT 330
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
340-534 6.78e-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: 45.65  E-value: 6.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 340 AILGQQGYTSAVF---H---GNYK--------SFWNRDEIYK-------QFGYDNFF--DASYYDMNeadvsnyglkdkp 396
Cdd:cd16143   90 KMLKQAGYRTAMVgkwHlglDWKKkdgkkaatGTGKDVDYSKpikggplDHGFDYYFgiPASEVLPT------------- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 397 FFKESEEYL---SSLQQPFYTKFITLTNHFPY-PidekdasiAPATTGDSSVDTYFQTARYLDESVKSFVDYLKKSGLYD 472
Cdd:cd16143  157 LTDKAVEFIdqhAKKDKPFFLYFALPAPHTPIvP--------SPEFQGKSGAGPYGDFVYELDWVVGRILDALKELGLAE 228
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489818936 473 NSVIIMYGDHyGISDNHEEAMTKILGKDYN---------TFENaqAQRVPLMIHVPG--VQGGVQEQYGGQVD 534
Cdd:cd16143  229 NTLVIFTSDN-GPSPYADYKELEKFGHDPSgplrgmkadIYEG--GHRVPFIVRWPGkiPAGSVSDQLVSLTD 298
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
393-526 7.64e-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: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 45.61  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 393 KDKPFFkeseeylssLQQPFYTKfitltnHfpYPIDEKDASIAPATTGDSSVDTYFQTARY------LDESVKSFVDYLK 466
Cdd:cd16144  182 KDKPFF---------LYLSHYAV------H--TPIQARPELIEKYEKKKKGLRKGQKNPVYaamiesLDESVGRILDALE 244
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489818936 467 KSGLYDNSVIIMYGDHYGISDNHEEAMT-KIL--GKdYNTFENaqAQRVPLMIHVPGV-QGGVQ 526
Cdd:cd16144  245 ELGLADNTLVIFTSDNGGLSTRGGPPTSnAPLrgGK-GSLYEG--GIRVPLIVRWPGViKPGSV 305
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
454-534 1.10e-04

Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.


Pssm-ID: 293752 [Multi-domain]  Cd Length: 449  Bit Score: 44.94  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 454 LDESVKSFVDYLKKSGLYDNSVII-------MYGDHYgisdnheeamtkILGKDynTFeNAQAQRVPLMIHVPGVQGGVQ 526
Cdd:cd16028  247 VDDHLGRLFDYLKETGQWDDTLIVftsdhgeQLGDHW------------LWGKD--GF-FDQAYRVPLIVRDPRREADAT 311

                 ....*...
gi 489818936 527 EqyGGQVD 534
Cdd:cd16028  312 R--GQVVD 317
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
352-488 1.45e-04

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: 44.46  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 352 FHGNYKSFWNRDEIYKQFGYDNFFdasyYDMNEADVSNYGL------------------KDKPFFkeseEYLSsLQQPfy 413
Cdd:cd16029  125 YYGGAEDYYTHTSGGANDYGNDDL----RDNEEPAWDYNGTystdlftdravdiienhdPSKPLF----LYLA-FQAV-- 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 414 tkfitltnHFPypIDEKDASIAPATTGDSSVD-----TYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMygdhygISDN 488
Cdd:cd16029  194 --------HAP--LQVPPEYADPYEDKFAHIKdedrrTYAAMVSALDESVGNVVDALKAKGMLDNTLIVF------TSDN 257
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
453-534 1.53e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 44.52  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 453 YLDESVKSFVDYLKKSGLYDNSVIIM---YGDHYGISDNHEeamtkilgKDYNTFEnaQAQRVPLMIHVPGV--QGGVQE 527
Cdd:cd16033  225 LIDDAIGRILDALEELGLADDTLVIFtsdHGDALGAHRLWD--------KGPFMYE--ETYRIPLIIKWPGViaAGQVVD 294

                 ....*..
gi 489818936 528 QYGGQVD 534
Cdd:cd16033  295 EFVSLLD 301
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
446-524 2.82e-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: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 43.76  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 446 TYFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDH------YGISDnheeamtkilgKDYNTFENAQAqRVPLMIHVP 519
Cdd:cd16150  201 TYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHgdytgdYGLVE-----------KWPNTFEDCLT-RVPLIIKPP 268

                 ....*
gi 489818936 520 GVQGG 524
Cdd:cd16150  269 GGPAG 273
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
447-524 4.42e-04

choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.


Pssm-ID: 293756 [Multi-domain]  Cd Length: 327  Bit Score: 42.95  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 447 YFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHyGisdnheeamtKILGK-----DYNTFEnaQAQRVPLMIHVPGV 521
Cdd:cd16032  166 YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDH-G----------DMLGErglwyKMSFFE--GSARVPLIISAPGR 232

                 ...
gi 489818936 522 QGG 524
Cdd:cd16032  233 FAP 235
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
364-524 7.18e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 42.17  E-value: 7.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 364 EIYKQFGYDNFF----DASYYDMNEADVSNYGLKDKPFFKeseeYLS--------SLQQPFYTKF----ITLTNHFP--Y 425
Cdd:cd16155   88 ETFKKAGYRTFAtgkwHNGFADAAIEFLEEYKDGDKPFFM----YVAftaphdprQAPPEYLDMYppetIPLPENFLpqH 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 426 PIDEKDASIA-------PATTGDSSVDT--YFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHyGIsdnheeAMTK- 495
Cdd:cd16155  164 PFDNGEGTVRdeqlapfPRTPEAVRQHLaeYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDH-GL------AVGSh 236
                        170       180       190
                 ....*....|....*....|....*....|
gi 489818936 496 -ILGKDyNTFEnaQAQRVPLMIHVPGVQGG 524
Cdd:cd16155  237 gLMGKQ-NLYE--HSMRVPLIISGPGIPKG 263
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
339-521 9.66e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 42.17  E-value: 9.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 339 SAILGQQGYTSAVF--------HGNYKSFWNR----------DEIYKQFGYDNFFDASYYDMN-------------EADV 387
Cdd:cd16034   83 ADVLKDAGYRTGYIgkwhldgpERNDGRADDYtppperrhgfDYWKGYECNHDHNNPHYYDDDgkriyikgyspdaETDL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 388 -----SNYGLKDKPFFKeseeYLS---------SLQQPFYTKFITLTNHFP--YPIDEKD-ASIAPATTGdssvdtYFQT 450
Cdd:cd16034  163 aieylENQADKDKPFAL----VLSwnpphdpytTAPEEYLDMYDPKKLLLRpnVPEDKKEeAGLREDLRG------YYAM 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 451 ARYLDESVKSFVDYLKKSGLYDNSVIIMYGDH------YGiSDN----HEEAMtkilgkdyntfenaqaqRVPLMIHVPG 520
Cdd:cd16034  233 ITALDDNIGRLLDALKELGLLENTIVVFTSDHgdmlgsHG-LMNkqvpYEESI-----------------RVPFIIRYPG 294

                 .
gi 489818936 521 V 521
Cdd:cd16034  295 K 295
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
447-521 1.08e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 41.46  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 447 YFQTARYLDESVKSFVDYLKKSGLYDNSVIIMYGDHyGISDNHEeamtKILGKD-----YNTFENaqAQRVPLMIHVPGV 521
Cdd:cd16149  144 YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDN-GFNMGHH----GIWGKGngtfpLNMYDN--SVKVPFIIRWPGV 216
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
341-524 2.68e-03

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 40.22  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 341 ILGQQGYTSAV-----FHGNyksfwnrdeiykqfGYDNFFDasyYDMNEAD-----VSNYGLKDKPFFkeseeYLSSLQQ 410
Cdd:cd16037   84 ALRAAGYETVLigklhFRGE--------------DQRHGFR---YDRDVTEaavdwLREEAADDKPWF-----LFVGFVA 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818936 411 PfytkfitltnHFPYpidekdasIAPAttgdSSVDTYFQTAR--------YLDESVKSFVDYLKKSGLYDNSVIIMYGDH 482
Cdd:cd16037  142 P----------HFPL--------IAPQ----EFYDLYVRRARaayyglveFLDENIGRVLDALEELGLLDNTLIIYTSDH 199
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489818936 483 ygiSDNheeamtkiLGKDY-----NTFEnaQAQRVPLMIHVPGVQGG 524
Cdd:cd16037  200 ---GDM--------LGERGlwgksTMYE--ESVRVPMIISGPGIPAG 233
 
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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