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Conserved domains on  [gi|926120082|emb|CUD62510|]
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glycerol phosphate lipoteichoic acid synthase [Staphylococcus aureus]

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 ...
13-619 2.61e-153

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


:

Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 454.50  E-value: 2.61e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  13 FFLLTVITITLKTYFsYYVDFSLGVKGLVQNLILLMN-------PYSLVALVLSVFLFFKGKKAFWFMFIGGFLLTFLLY 85
Cdd:COG1368    1 FFLLFLLLLSLRLVF-LLFNFDLSLGEILQAFLYGLRfilylllLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  86 ANVVYFRFFSDFLTFSTLNQVGNVESMGGAVsasFKWYDFVYFIDTLVYLFILIF----KTKWLDTKAFSKKFVPVVMAA 161
Cdd:COG1368   80 ADILYYRFFGDRLNFSDLDYLGDTGEVLGSL---LSSYDLLLLLDLLLLLLLLLLlyrlLKKLRKSLPWRKRLALLLLLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 162 SVALFFLNLAFaetDRPELLTRTFDHKYLVKYLGP-YNFTVYDGVKtieNNQQKALASEDDLTKVLNYTKQRQTEPNPey 240
Cdd:COG1368  157 ALLLLGIRLGE---DRPLNLSDAFSRNNFVNELGLnGPYSFYDALR---NNKAPATYSEEEALEIKKYLKSNRPTPNP-- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 241 YGVAKKKNIIKIHLESFQTFLINKKVNGKEVTPFLNKLssgKEQFTYFPNFFHQTGqgKTSDSEFTMDNSLYGLPQGSAF 320
Cdd:COG1368  229 FGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSL---AKESLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGSPY 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 321 SLKGDNTYQSLPAILdQKQGYKSDVMHGDYKTFWNRDQVYKHFGIDKFYDATYYDMSDKNVvnLGLKDKIFFKDSANYQA 400
Cdd:COG1368  304 KRPGQNNFPSLPSIL-KKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDFDDPFDGG--WGVSDEDLFDKALEELE 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 401 KMKSPFYSHLITLTNHYPFTLDEKDATIekSNTGDATVDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGDHYGIS 480
Cdd:COG1368  381 KLKKPFFAFLITLSNHGPYTLPEEDKKI--PDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 481 ENHNNAMEKLlgekitpakftDLNRTGFWIKIPG-KSGGINNEYAGQVDVMPTILHLAGIDTKNYLMFGTDLFSKGHNQv 559
Cdd:COG1368  459 PGKTDYENPL-----------ERYRVPLLIYSPGlKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDP- 526
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 560 VPFRNGDFITKDYKYVngkiysNKNNELITTQpadfEKNKKQVEKDLEMSDNVLNGDLFR 619
Cdd:COG1368  527 FAFRNGGFITDDYVYV------LKTGELTEED----KELEEEALAYLQLSDYLYGNDLLR 576
 
Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
13-619 2.61e-153

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 454.50  E-value: 2.61e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  13 FFLLTVITITLKTYFsYYVDFSLGVKGLVQNLILLMN-------PYSLVALVLSVFLFFKGKKAFWFMFIGGFLLTFLLY 85
Cdd:COG1368    1 FFLLFLLLLSLRLVF-LLFNFDLSLGEILQAFLYGLRfilylllLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  86 ANVVYFRFFSDFLTFSTLNQVGNVESMGGAVsasFKWYDFVYFIDTLVYLFILIF----KTKWLDTKAFSKKFVPVVMAA 161
Cdd:COG1368   80 ADILYYRFFGDRLNFSDLDYLGDTGEVLGSL---LSSYDLLLLLDLLLLLLLLLLlyrlLKKLRKSLPWRKRLALLLLLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 162 SVALFFLNLAFaetDRPELLTRTFDHKYLVKYLGP-YNFTVYDGVKtieNNQQKALASEDDLTKVLNYTKQRQTEPNPey 240
Cdd:COG1368  157 ALLLLGIRLGE---DRPLNLSDAFSRNNFVNELGLnGPYSFYDALR---NNKAPATYSEEEALEIKKYLKSNRPTPNP-- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 241 YGVAKKKNIIKIHLESFQTFLINKKVNGKEVTPFLNKLssgKEQFTYFPNFFHQTGqgKTSDSEFTMDNSLYGLPQGSAF 320
Cdd:COG1368  229 FGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSL---AKESLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGSPY 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 321 SLKGDNTYQSLPAILdQKQGYKSDVMHGDYKTFWNRDQVYKHFGIDKFYDATYYDMSDKNVvnLGLKDKIFFKDSANYQA 400
Cdd:COG1368  304 KRPGQNNFPSLPSIL-KKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDFDDPFDGG--WGVSDEDLFDKALEELE 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 401 KMKSPFYSHLITLTNHYPFTLDEKDATIekSNTGDATVDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGDHYGIS 480
Cdd:COG1368  381 KLKKPFFAFLITLSNHGPYTLPEEDKKI--PDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 481 ENHNNAMEKLlgekitpakftDLNRTGFWIKIPG-KSGGINNEYAGQVDVMPTILHLAGIDTKNYLMFGTDLFSKGHNQv 559
Cdd:COG1368  459 PGKTDYENPL-----------ERYRVPLLIYSPGlKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDP- 526
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 560 VPFRNGDFITKDYKYVngkiysNKNNELITTQpadfEKNKKQVEKDLEMSDNVLNGDLFR 619
Cdd:COG1368  527 FAFRNGGFITDDYVYV------LKTGELTEED----KELEEEALAYLQLSDYLYGNDLLR 576
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
247-538 2.06e-74

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: 240.28  E-value: 2.06e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 247 KNIIKIHLESFQTFLINKKVNGKEVTPFLNKLssgKEQFTYFPNFFHQTGQGKTSDSEFTMDNSLYGLPQGSAF-SLKGD 325
Cdd:cd16015    1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKL---AKEGLYFGNFYSPGFGGGTANGEFEVLTGLPPLPLGSGSyTLYKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 326 NTYQSLPAILdQKQGYKSDVMHGDYKTFWNRDQVYKHFGIDKFYDATYYDMSDKNVVNLGLKDKIFFKDSAN-YQAKMKS 404
Cdd:cd16015   78 NPLPSLPSIL-KEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDESLFDQALEeLEELKKK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 405 PFYSHLITLTNHYPFTLDEKDATIEKSNTGDAT-VDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGDHYGISENH 483
Cdd:cd16015  157 PFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTeLENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 926120082 484 NNamekllgekITPAKFTDLNRTGFWIKIPG-KSGGINNEYAGQVDVMPTILHLAG 538
Cdd:cd16015  237 YD---------ETDEDPLDLYRTPLLIYSPGlKKPKKIDRVGSQIDIAPTLLDLLG 283
Sulfatase pfam00884
Sulfatase;
247-539 1.62e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 138.71  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  247 KNIIKIHLESFQTFLINKKVNGKEVTPFLNKLSsgkEQFTYFPNFFhqTGQGKTSDSEFTMDNSLYGLPQGSAFSLKGD- 325
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLA---EEGLLFSNFY--SGGTLTAPSRFALLTGLPPHNFGSYVSTPVGl 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  326 -NTYQSLPAILdQKQGYKSDVMHGDYKTFWNRDQVYKHfGIDKFYD-----ATYYDMSD--KNVVNLGLKDKIFFKDSAN 397
Cdd:pfam00884  76 pRTEPSLPDLL-KRAGYNTGAIGKWHLGWYNNQSPCNL-GFDKFFGrntgsDLYADPPDvpYNCSGGGVSDEALLDEALE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  398 YQAKMKSPFYSHLITLTNHYPFTLDEKDATIEK-----SNTGDATVDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMI 472
Cdd:pfam00884 154 FLDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVY 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 926120082  473 YGDHYGISENHNNAmekLLGEKiTPAKFTDLNRTGFWIKIPG--KSGGINNEYAGQVDVMPTILHLAGI 539
Cdd:pfam00884 234 TSDHGESLGEGGGY---LHGGK-YDNAPEGGYRVPLLIWSPGgkAKGQKSEALVSHVDLFPTILDLAGI 298
PRK12363 PRK12363
phosphoglycerol transferase I; Provisional
53-553 1.74e-08

phosphoglycerol transferase I; Provisional


Pssm-ID: 171438  Cd Length: 703  Bit Score: 57.61  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  53 LVALVLSVFLFFKGKKAFWFMfiGGFLLTFLLYANVVYF--RFFSDFLTFSTLNQVGnvESMGGAVSASFKWYDFVYFID 130
Cdd:PRK12363   6 LLSLLLLLWLLVASPRLAWLK--AGLLSLFLLLLSAWGLvdRLSGDGVNAATLYHLR--ADMDGAGVSDFSGYIAVFIGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 131 TLVYLfILIFKTKwldtkafSKKFVP-----VVMAASVALFFLNLAFAETDRpelltrtfDHKYLVKYLGPYNFTvydgv 205
Cdd:PRK12363  82 ILLSL-SPLFAFR-------VRRFRRprgggALFAGFVFMLVVTIAQSPLYR--------DGKRLYYQLRPVDFA----- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 206 ktiennqqkalaseddlTKVLNYTkqrqtepNPEYyGVAKKKNIIKIHLESFQTFLINKKVNgKEVTPFLNKLSSGKEQF 285
Cdd:PRK12363 141 -----------------TVAPEYQ-------VPQQ-PLQKRKNIVWIYGESLERTYFDEDVF-PGLMPNLTRLATEAVDV 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 286 TyfpNFFHQTGQGKTSDSeftMDNSLYGLP----QGSAFSLkgDNTYQSLPA---ILD--QKQGYKSDVMHGDYKTFWNR 356
Cdd:PRK12363 195 R---NLASTEGSGWTIAG---MVASMCGVPlttaQGDENSM--DRMGHFLPEarcLGDylKDQGYTNHYVGGADASFAGK 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 357 DQVYKHFGIDKFYDATYYD----MSDKNVVNLGLKDKIFFKDSAN-YQ--AKMKSPFYSHLITLTNHYP--FTLDEKDAT 427
Cdd:PRK12363 267 GKFLSSHGFDEVHDVNYFLhdkgVAPKHFSAWGVHDDVLLDDAYDeFEtlSRAGQPFMLTTLTMDTHHPagHLPSACKGQ 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 428 IEKSNTGDATVDGYIQTARYLdeaLEEYINDLKKKGLYDNSVIMIYGDHYgisenhnnAMEKLLGEKITPAKFTDLNrtg 507
Cdd:PRK12363 347 RYDSPLGDIGMLHAIKCSDRL---IGQLVDRIRNSRYGKNTIIVIASDHL--------AMPNDLSDVLTKQKRENLL--- 412
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 926120082 508 FWIKIPGKSGGINNEYAGQVDVMPTILHLAGIDTKNyLMFGTDLFS 553
Cdd:PRK12363 413 LFLGKDIAPQQVVTRAGTTLDSGATLLQLLEPGMRT-LGFGRSLLA 457
 
Name Accession Description Interval E-value
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
13-619 2.61e-153

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 454.50  E-value: 2.61e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  13 FFLLTVITITLKTYFsYYVDFSLGVKGLVQNLILLMN-------PYSLVALVLSVFLFFKGKKAFWFMFIGGFLLTFLLY 85
Cdd:COG1368    1 FFLLFLLLLSLRLVF-LLFNFDLSLGEILQAFLYGLRfilylllLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  86 ANVVYFRFFSDFLTFSTLNQVGNVESMGGAVsasFKWYDFVYFIDTLVYLFILIF----KTKWLDTKAFSKKFVPVVMAA 161
Cdd:COG1368   80 ADILYYRFFGDRLNFSDLDYLGDTGEVLGSL---LSSYDLLLLLDLLLLLLLLLLlyrlLKKLRKSLPWRKRLALLLLLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 162 SVALFFLNLAFaetDRPELLTRTFDHKYLVKYLGP-YNFTVYDGVKtieNNQQKALASEDDLTKVLNYTKQRQTEPNPey 240
Cdd:COG1368  157 ALLLLGIRLGE---DRPLNLSDAFSRNNFVNELGLnGPYSFYDALR---NNKAPATYSEEEALEIKKYLKSNRPTPNP-- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 241 YGVAKKKNIIKIHLESFQTFLINKKVNGKEVTPFLNKLssgKEQFTYFPNFFHQTGqgKTSDSEFTMDNSLYGLPQGSAF 320
Cdd:COG1368  229 FGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSL---AKESLYFGNFYSQGG--RTSRGEFAVLTGLPPLPGGSPY 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 321 SLKGDNTYQSLPAILdQKQGYKSDVMHGDYKTFWNRDQVYKHFGIDKFYDATYYDMSDKNVvnLGLKDKIFFKDSANYQA 400
Cdd:COG1368  304 KRPGQNNFPSLPSIL-KKQGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDFDDPFDGG--WGVSDEDLFDKALEELE 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 401 KMKSPFYSHLITLTNHYPFTLDEKDATIekSNTGDATVDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGDHYGIS 480
Cdd:COG1368  381 KLKKPFFAFLITLSNHGPYTLPEEDKKI--PDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 481 ENHNNAMEKLlgekitpakftDLNRTGFWIKIPG-KSGGINNEYAGQVDVMPTILHLAGIDTKNYLMFGTDLFSKGHNQv 559
Cdd:COG1368  459 PGKTDYENPL-----------ERYRVPLLIYSPGlKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDP- 526
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 560 VPFRNGDFITKDYKYVngkiysNKNNELITTQpadfEKNKKQVEKDLEMSDNVLNGDLFR 619
Cdd:COG1368  527 FAFRNGGFITDDYVYV------LKTGELTEED----KELEEEALAYLQLSDYLYGNDLLR 576
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
247-538 2.06e-74

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: 240.28  E-value: 2.06e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 247 KNIIKIHLESFQTFLINKKVNGKEVTPFLNKLssgKEQFTYFPNFFHQTGQGKTSDSEFTMDNSLYGLPQGSAF-SLKGD 325
Cdd:cd16015    1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKL---AKEGLYFGNFYSPGFGGGTANGEFEVLTGLPPLPLGSGSyTLYKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 326 NTYQSLPAILdQKQGYKSDVMHGDYKTFWNRDQVYKHFGIDKFYDATYYDMSDKNVVNLGLKDKIFFKDSAN-YQAKMKS 404
Cdd:cd16015   78 NPLPSLPSIL-KEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDESLFDQALEeLEELKKK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 405 PFYSHLITLTNHYPFTLDEKDATIEKSNTGDAT-VDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGDHYGISENH 483
Cdd:cd16015  157 PFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTeLENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 926120082 484 NNamekllgekITPAKFTDLNRTGFWIKIPG-KSGGINNEYAGQVDVMPTILHLAG 538
Cdd:cd16015  237 YD---------ETDEDPLDLYRTPLLIYSPGlKKPKKIDRVGSQIDIAPTLLDLLG 283
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
247-537 2.01e-42

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: 153.35  E-value: 2.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 247 KNIIKIHLESFQTFLINKKVNGKEVTPFLNKLssgKEQFTYFpNFFHQTGQGKTSDSEFTMDNSLYGLPQGSAF------ 320
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRL---ASEGATF-NFRSVSPPTSSAPNHAALLTGAYPTLHGYTGngsadp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 321 -----SLKGDNTYQSLPAILDQKqGYKSDVMHgdyktfwnrdqvykhfgidkfydatyydmsdknvvnlglkdkifFKDS 395
Cdd:cd00016   77 elpsrAAGKDEDGPTIPELLKQA-GYRTGVIG--------------------------------------------LLKA 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 396 ANYQAKmKSPFYSHLITLTNHYPFTLDekdatieksntgDATVDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGD 475
Cdd:cd00016  112 IDETSK-EKPFVLFLHFDGPDGPGHAY------------GPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTAD 178
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 926120082 476 HYGISENHNNAMEKllgeKITPAKFTDLNRTGFWIKIPG-KSGGINNEYAGQVDVMPTILHLA 537
Cdd:cd00016  179 HGGIDKGHGGDPKA----DGKADKSHTGMRVPFIAYGPGvKKGGVKHELISQYDIAPTLADLL 237
Sulfatase pfam00884
Sulfatase;
247-539 1.62e-36

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 138.71  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  247 KNIIKIHLESFQTFLINKKVNGKEVTPFLNKLSsgkEQFTYFPNFFhqTGQGKTSDSEFTMDNSLYGLPQGSAFSLKGD- 325
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLA---EEGLLFSNFY--SGGTLTAPSRFALLTGLPPHNFGSYVSTPVGl 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  326 -NTYQSLPAILdQKQGYKSDVMHGDYKTFWNRDQVYKHfGIDKFYD-----ATYYDMSD--KNVVNLGLKDKIFFKDSAN 397
Cdd:pfam00884  76 pRTEPSLPDLL-KRAGYNTGAIGKWHLGWYNNQSPCNL-GFDKFFGrntgsDLYADPPDvpYNCSGGGVSDEALLDEALE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  398 YQAKMKSPFYSHLITLTNHYPFTLDEKDATIEK-----SNTGDATVDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMI 472
Cdd:pfam00884 154 FLDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVY 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 926120082  473 YGDHYGISENHNNAmekLLGEKiTPAKFTDLNRTGFWIKIPG--KSGGINNEYAGQVDVMPTILHLAGI 539
Cdd:pfam00884 234 TSDHGESLGEGGGY---LHGGK-YDNAPEGGYRVPLLIWSPGgkAKGQKSEALVSHVDLFPTILDLAGI 298
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
267-553 1.11e-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: 77.59  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 267 NGKEVTPFLNKLSsgkEQFTYFPNffHQTGQGKTSDSEFTMdnsLYGLP----QGSAFSLKGDNTyqSLPAILdQKQGYK 342
Cdd:cd16148   21 YDRVTTPNLDRLA---AEGVVFDN--HYSGSNPTLPSRFSL---FTGLYpfyhGVWGGPLEPDDP--TLAEIL-RKAGYY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 343 ----SDVMHGDYKTFWNRDQVYKHFGIDKFYDATY-YDMSDKNVVNLGLKdkiFFKDSANyqakmKSPFYSHLITLTNHY 417
Cdd:cd16148   90 taavSSNPHLFGGPGFDRGFDTFEDFRGQEGDPGEeGDERAERVTDRALE---WLDRNAD-----DDPFFLFLHYFDPHE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 418 PFtldekdatieksntgdatvdGYIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGDH-YGISENHNNAMEkllgekit 496
Cdd:cd16148  162 PY--------------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHgEEFGEHGLYWGH-------- 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 926120082 497 PAKFTD-LNRTGFWIKIPGKSGGINNEY-AGQVDVMPTILHLAGIDTKNYLMfGTDLFS 553
Cdd:cd16148  214 GSNLYDeQLHVPLIIRWPGKEPGKRVDAlVSHIDIAPTLLDLLGVEPPDYSD-GRSLLP 271
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
329-575 2.95e-13

N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.


Pssm-ID: 293751 [Multi-domain]  Cd Length: 373  Bit Score: 71.77  E-value: 2.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 329 QSLPAILdQKQGYKsdvmhgdykTFWNRDQVYKHFGIDKFYDATYYDMSDKNVVNLGLKDKIFFKDsanyQAKMKSPFYS 408
Cdd:cd16027   81 KTLPELL-REAGYY---------TGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWDYASNAADFLN----RAKKGQPFFL 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 409 HL-ITLTnHYPFTLDEKDATIEKSNtgDATVDGYI--------QTARY------LDEALEEYINDLKKKGLYDNSVIMIY 473
Cdd:cd16027  147 WFgFHDP-HRPYPPGDGEEPGYDPE--KVKVPPYLpdtpevreDLADYydeierLDQQVGEILDELEEDGLLDNTIVIFT 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 474 GDHyGISenhnnamekLLGEKITPakfTDL-NRTGFWIKIPG--KSGGINNEYAGQVDVMPTILHLAGIDTKNYlMFGTD 550
Cdd:cd16027  224 SDH-GMP---------FPRAKGTL---YDSgLRVPLIVRWPGkiKPGSVSDALVSFIDLAPTLLDLAGIEPPEY-LQGRS 289
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 926120082 551 LFSKGHNQVVPFRN------------GDFI----TKDYKYV 575
Cdd:cd16027  290 FLPLLKGEKDPGRDyvfaerdrhdetYDPIrsvrTGRYKYI 330
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
399-575 5.67e-09

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 58.35  E-value: 5.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 399 QAKMKSPFYSHLITLTNHYPFTLDE--------KDATIEKSNTGDATVDGYIQTAR--------YLDEALEEYINDLKKK 462
Cdd:COG3119  144 QADKDKPFFLYLAFNAPHAPYQAPEeyldkydgKDIPLPPNLAPRDLTEEELRRARaayaamieEVDDQVGRLLDALEEL 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 463 GLYDNSVIMIYGDHYGISENHNnamekLLGEKITPakFTDLNRTGFWIKIPG--KSGGINNEYAGQVDVMPTILHLAGID 540
Cdd:COG3119  224 GLADNTIVVFTSDNGPSLGEHG-----LRGGKGTL--YEGGIRVPLIVRWPGkiKAGSVSDALVSLIDLLPTLLDLAGVP 296
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 926120082 541 TKNYlMFGTDLFS--KGHNQVV--------PFRNGDF--ITKDYKYV 575
Cdd:COG3119  297 IPED-LDGRSLLPllTGEKAEWrdylyweyPRGGGNRaiRTGRWKLI 342
PRK12363 PRK12363
phosphoglycerol transferase I; Provisional
53-553 1.74e-08

phosphoglycerol transferase I; Provisional


Pssm-ID: 171438  Cd Length: 703  Bit Score: 57.61  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  53 LVALVLSVFLFFKGKKAFWFMfiGGFLLTFLLYANVVYF--RFFSDFLTFSTLNQVGnvESMGGAVSASFKWYDFVYFID 130
Cdd:PRK12363   6 LLSLLLLLWLLVASPRLAWLK--AGLLSLFLLLLSAWGLvdRLSGDGVNAATLYHLR--ADMDGAGVSDFSGYIAVFIGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 131 TLVYLfILIFKTKwldtkafSKKFVP-----VVMAASVALFFLNLAFAETDRpelltrtfDHKYLVKYLGPYNFTvydgv 205
Cdd:PRK12363  82 ILLSL-SPLFAFR-------VRRFRRprgggALFAGFVFMLVVTIAQSPLYR--------DGKRLYYQLRPVDFA----- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 206 ktiennqqkalaseddlTKVLNYTkqrqtepNPEYyGVAKKKNIIKIHLESFQTFLINKKVNgKEVTPFLNKLSSGKEQF 285
Cdd:PRK12363 141 -----------------TVAPEYQ-------VPQQ-PLQKRKNIVWIYGESLERTYFDEDVF-PGLMPNLTRLATEAVDV 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 286 TyfpNFFHQTGQGKTSDSeftMDNSLYGLP----QGSAFSLkgDNTYQSLPA---ILD--QKQGYKSDVMHGDYKTFWNR 356
Cdd:PRK12363 195 R---NLASTEGSGWTIAG---MVASMCGVPlttaQGDENSM--DRMGHFLPEarcLGDylKDQGYTNHYVGGADASFAGK 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 357 DQVYKHFGIDKFYDATYYD----MSDKNVVNLGLKDKIFFKDSAN-YQ--AKMKSPFYSHLITLTNHYP--FTLDEKDAT 427
Cdd:PRK12363 267 GKFLSSHGFDEVHDVNYFLhdkgVAPKHFSAWGVHDDVLLDDAYDeFEtlSRAGQPFMLTTLTMDTHHPagHLPSACKGQ 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 428 IEKSNTGDATVDGYIQTARYLdeaLEEYINDLKKKGLYDNSVIMIYGDHYgisenhnnAMEKLLGEKITPAKFTDLNrtg 507
Cdd:PRK12363 347 RYDSPLGDIGMLHAIKCSDRL---IGQLVDRIRNSRYGKNTIIVIASDHL--------AMPNDLSDVLTKQKRENLL--- 412
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 926120082 508 FWIKIPGKSGGINNEYAGQVDVMPTILHLAGIDTKNyLMFGTDLFS 553
Cdd:PRK12363 413 LFLGKDIAPQQVVTRAGTTLDSGATLLQLLEPGMRT-LGFGRSLLA 457
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
440-575 3.17e-08

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


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 56.08  E-value: 3.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 440 GYIQtarYLDEALEEYINDLKKKGLYDNSVIMI---YGDHYGIsenHNnameklLGEKiTPAKFTDLNRTGFWIKIPGKS 516
Cdd:cd16033  221 GYIT---LIDDAIGRILDALEELGLADDTLVIFtsdHGDALGA---HR------LWDK-GPFMYEETYRIPLIIKWPGVI 287
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 926120082 517 --GGINNEYAGQVDVMPTILHLAGIDTKNY-----LM----------FGTDLFSKGHNQVVPFRNGDFITKDYKYV 575
Cdd:cd16033  288 aaGQVVDEFVSLLDLAPTILDLAGVDVPPKvdgrsLLpllrgeqpedWRDEVVTEYNGHEFYLPQRMVRTDRYKYV 363
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
447-551 9.18e-08

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 54.93  E-value: 9.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 447 YLDEALEEYINDLKKKGLYDNSVIMIYGDH------YGISENHNNAMEKllgekitpakftDLNRTGFWIKIPGKS-GGI 519
Cdd:cd16150  208 RLDHQFGRLLEALKETGLYDDTAVFFFSDHgdytgdYGLVEKWPNTFED------------CLTRVPLIIKPPGGPaGGV 275
                         90       100       110
                 ....*....|....*....|....*....|..
gi 926120082 520 NNEYAGQVDVMPTILHLAGIDTKnYLMFGTDL 551
Cdd:cd16150  276 SDALVELVDIPPTLLDLAGIPLS-HTHFGRSL 306
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
447-545 5.44e-07

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: 50.90  E-value: 5.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 447 YLDEALEEYINDLKKKGLYDNSVIMIYGDHYGISENHNnamekLLGEKITPakFTDLNRTGFWIKIPG--KSGGINNEYA 524
Cdd:cd16022  139 AIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHG-----LRGKKGSL--YEGGIRVPFIVRWPGkiPAGQVSDALV 211
                         90       100
                 ....*....|....*....|.
gi 926120082 525 GQVDVMPTILHLAGIDTKNYL 545
Cdd:cd16022  212 SLLDLLPTLLDLAGIEPPEGL 232
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
448-575 1.80e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 50.69  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 448 LDEALEEYINDLKKKGLYDNSVIMIYGDH----------YGISeNHNNAMekllgekitpakftdlnRTGFWIKIPGKSG 517
Cdd:cd16152  184 LDENVGRIRDALKELGLYDNTIIVFTSDHgchfrtrnaeYKRS-CHESSI-----------------RVPLVIYGPGFNG 245
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 926120082 518 GIN-NEYAGQVDVMPTILHLAGIDTKNYlMFGTDLFSKGHNQVVPFRNGDFI------------TKDYKYV 575
Cdd:cd16152  246 GGRvEELVSLIDLPPTLLDAAGIDVPEE-MQGRSLLPLVDGKVEDWRNEVFIqisesqvgrairTDRWKYS 315
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
384-540 2.48e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 49.54  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 384 LGLKDKIFFKDsanyQAKMKSPFYSHLITLTNHYPFtldekdatieksntgdatvdGYIQTARYLDEALEEYINDLKKKG 463
Cdd:cd16149  111 LGDDAADFLRR----RAEAEKPFFLSVNYTAPHSPW--------------------GYFAAVTGVDRNVGRLLDELEELG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 464 LYDNSVIMIYGDHyGISENHNNAMEKllGEKITPAKFTDLN-RTGFWIKIPG--KSGGINNEYAGQVDVMPTILHLAGID 540
Cdd:cd16149  167 LTENTLVIFTSDN-GFNMGHHGIWGK--GNGTFPLNMYDNSvKVPFIIRWPGvvPAGRVVDSLVSAYDFFPTLLELAGVD 243
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
442-545 6.28e-06

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 49.09  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 442 IQTARYLDEALEEYINDLKKKGLYDNSVImIY----GDHYGiseNHNnamekLLGEKITPAKFtDLnRTGFWIKIPG-KS 516
Cdd:cd16147  245 LRTLQSVDDLVERLVNTLEATGQLDNTYI-IYtsdnGYHLG---QHR-----LPPGKRTPYEE-DI-RVPLLVRGPGiPA 313
                         90       100
                 ....*....|....*....|....*....
gi 926120082 517 GGINNEYAGQVDVMPTILHLAGIDTKNYL 545
Cdd:cd16147  314 GVTVDQLVSNIDLAPTILDLAGAPPPSDM 342
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
448-575 8.62e-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: 48.33  E-value: 8.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 448 LDEALEEYINDLKKKGLYDNSVIMIYGDHyGIsenhnnamekLLGEKitpakftDLNRTGFW----IKIP--------GK 515
Cdd:cd16034  236 LDDNIGRLLDALKELGLLENTIVVFTSDH-GD----------MLGSH-------GLMNKQVPyeesIRVPfiirypgkIK 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 516 SGGINNEYAGQVDVMPTILHLAGIDTKNYlMFGTDL--------FSKGHNQ----VVPFRNGDF---------ITKDYKY 574
Cdd:cd16034  298 AGRVVDLLINTVDIMPTLLGLCGLPIPDT-VEGRDLsplllggkDDEPDSVllqcFVPFGGGSArdggewrgvRTDRYTY 376

                 .
gi 926120082 575 V 575
Cdd:cd16034  377 V 377
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
337-587 1.54e-05

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


Pssm-ID: 293765 [Multi-domain]  Cd Length: 409  Bit Score: 47.54  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 337 QKQGYKSDVMHGDYKTfwnrDQVYKHFGIDKFYDATYYDmsDKNVVNLGLKDKIFFKDSANY-QAKMKSPFYSHLITLTN 415
Cdd:cd16146  111 QDRGFDEVLGHGGGGI----GQYPDYWGNDYFDDTYYHN--GKFVKTEGYCTDVFFDEAIDFiEENKDKPFFAYLATNAP 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 416 HYPFTLDEKDAT--IEKS-NTGDATVDGYIQTaryLDEALEEYINDLKKKGLYDNSVIMIYGD--HYGISENHNNAmeKL 490
Cdd:cd16146  185 HGPLQVPDKYLDpyKDMGlDDKLAAFYGMIEN---IDDNVGRLLAKLKELGLEENTIVIFMSDngPAGGVPKRFNA--GM 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 491 LGEKITPakftDLN--RTGFWIKIPGK--SGGINNEYAGQVDVMPTILHLAGIDT-----------KNYLMFGTD----- 550
Cdd:cd16146  260 RGKKGSV----YEGghRVPFFIRWPGKilAGKDVDTLTAHIDLLPTLLDLCGVKLpegikldgrslLPLLKGESDpwper 335
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 926120082 551 -LFSKGHNQVVP---FRNGDFITKDYKYVNGKiysNKNNEL 587
Cdd:cd16146  336 tLFTHSGRWPPPpkkKRNAAVRTGRWRLVSPK---GFQPEL 373
EcfT cd16914
T component of ECF-type transporters; The transmembrane component (T component) of the energy ...
10-165 6.09e-05

T component of ECF-type transporters; The transmembrane component (T component) of the energy coupling-factor (ECF)-type transporter is a transmembrane protein important for vitamin uptake in prokaryotes. In addition to the T component, energy-coupling factor (ECF) transporters contain an energy-coupling module that consists of two ATP-binding proteins (known as the A and A' components) and a substrate-binding (S) component. ECF transporters comprise a subgroup of ATP-binding cassette (ABC) transporters that do not make use of water-soluble substrate binding proteins or domains, but instead employ integral membrane proteins for substrate binding, the S component, in contrast to classical ABC importers. The T component links the S component to the ATP-binding subcomplex that is composed of the A and A' components.


Pssm-ID: 410987  Cd Length: 233  Bit Score: 44.84  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082  10 LFAFFLLTVITITLKTYFSYYVdfslgvkglvqNLILLMnpySLVALVLSVFLFFKGKKAFWFMFIGGFLLTFLLYANVV 89
Cdd:cd16914    7 LLLLLLLLILVLLLPSLLLLLL-----------LLLLLL---LLLLLAGLPLRLLRLLKRLLFLLLFLLLILLLLPLGGG 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 926120082  90 YFRFFSDFLTFSTlnqvgnvESMGGAVSASFKwydfvyFIDTLVYLFILIFKTKWLD-TKAFSKKFVP--VVMAASVAL 165
Cdd:cd16914   73 GGVFGLGGLGITL-------EGLLYALLLALR------LLAIVLAALLLLLTTPPSElLAALRRLGVPpkLALLLSLAL 138
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
456-540 1.58e-04

Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; 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: 293749 [Multi-domain]  Cd Length: 402  Bit Score: 44.36  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 456 INDLKKKGLYDNSVIMIYGDHyGISENHNNAMeklLGEkiTPAKFTDLN------RTGFWIKIPG---KSGGINNEYAGQ 526
Cdd:cd16025  236 IDYLKELGELDNTLIIFLSDN-GASAEPGWAN---ASN--TPFRLYKQAsheggiRTPLIVSWPKgikAKGGIRHQFAHV 309
                         90
                 ....*....|....
gi 926120082 527 VDVMPTILHLAGID 540
Cdd:cd16025  310 IDIAPTILELAGVE 323
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
459-545 1.68e-04

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: 44.49  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 459 LKKKGLYDNSVIMIYGDHyGISenhnnameklLGEKITPAKFTDL---NRTGFWIKIPG--KSGGINNEYAGQVDVMPTI 533
Cdd:cd16030  281 LEELGLADNTIVVLWSDH-GWH----------LGEHGHWGKHTLFeeaTRVPLIIRAPGvtKPGKVTDALVELVDIYPTL 349
                         90
                 ....*....|..
gi 926120082 534 LHLAGIDTKNYL 545
Cdd:cd16030  350 AELAGLPAPPCL 361
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
403-542 3.33e-04

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: 43.69  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 403 KSPFYSHLITLTNHYPftLDEKDATIEKSNTGDATVDGYIQTARY------LDEALEEYINDLKKKGLYDNSVIMIYGDH 476
Cdd:cd16144  183 DKPFFLYLSHYAVHTP--IQARPELIEKYEKKKKGLRKGQKNPVYaamiesLDESVGRILDALEELGLADNTLVIFTSDN 260
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 926120082 477 YGISENHNNA--MEKLLGEKIT--------PakftdlnrtgFWIKIPG--KSGGINNEYAGQVDVMPTILHLAGIDTK 542
Cdd:cd16144  261 GGLSTRGGPPtsNAPLRGGKGSlyeggirvP----------LIVRWPGviKPGSVSDVPVIGTDLYPTFLELAGGPLP 328
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
364-558 3.47e-04

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


Pssm-ID: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 43.29  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 364 GIDKFYDATYYDMsDKNVVNLGLKdkiFFKDsanyQAKMKSPFYSHLITLTNHYPFTLDEKDATIEKSNT--GDATVDGY 441
Cdd:cd16142  119 GFDEFYGNLYHTI-DEEIVDKAID---FIKR----NAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSGKGkyADSMVELD 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 442 IQTARYLDEaleeyindLKKKGLYDNSVIMIYGDhygisenhNNA-MEKLLGEKITP---AKFTDL---NRTGFWIKIPG 514
Cdd:cd16142  191 DHVGQILDA--------LDELGIADNTIVIFTTD--------NGPeQDVWPDGGYTPfrgEKGTTWeggVRVPAIVRWPG 254
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 926120082 515 --KSGGINNEYAGQVDVMPTILHLAGIDTKNYLMFGTDLFSKGHNQ 558
Cdd:cd16142  255 kiKPGRVSNEIVSHLDWFPTLAALAGAPDPKDKLLGKDRHIDGVDQ 300
MFS_MelB_like cd17332
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major ...
7-107 1.40e-03

Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major Facilitator Superfamily; This family is composed of Salmonella enterica Na+/melibiose symporter MelB, Major Facilitator Superfamily domain-containing proteins, MFSD2 and MFSD12, and other sugar transporters. MelB catalyzes the electrogenic symport of galactosides with Na+, Li+ or H+. The MFSD2 subfamily is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. MelB-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340890 [Multi-domain]  Cd Length: 424  Bit Score: 41.44  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082   7 KISLFAFFLLTVITITLkTYFSYYVDFSLGVKglvQNLILLMNPYSLVALVLSVFLFFK----GKKAFWF----MFIGGF 78
Cdd:cd17332  225 ILLLAYLLYFLAFNIVN-TVLVYYFKYVLGGR---AELVLLLLLILSGALLALLPWPPLkkrfGKKKAFFigllLAILGL 300
                         90       100
                 ....*....|....*....|....*....
gi 926120082  79 LLTFLLYANVVYFrffsdFLTFSTLNQVG 107
Cdd:cd17332  301 LLLFFLPPGNLVL-----ILVLAVLAGIG 324
DUF229 pfam02995
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ...
431-476 1.44e-03

Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.


Pssm-ID: 397236  Cd Length: 496  Bit Score: 41.56  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 926120082  431 SNTGdatVDGYIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGDH 476
Cdd:pfam02995 299 SNSL---SHDDFNYASALDEDFLKYLKKLHKRGLLDNTIVIFMSDH 341
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
399-540 2.03e-03

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


Pssm-ID: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 41.03  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 399 QAKMKSPFYSHLITLTNHYPFTLDEKdaTIEKSNT---GDATVDgyiqtaryLDEALEEYINDLKKKGLYDNSVIMIYGD 475
Cdd:cd16143  168 HAKKDKPFFLYFALPAPHTPIVPSPE--FQGKSGAgpyGDFVYE--------LDWVVGRILDALKELGLAENTLVIFTSD 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 476 H---------YGISENHNNAMeKLLGEKitpakfTDL----NRTGFWIKIPGK--SGGINNEYAGQVDVMPTILHLAGID 540
Cdd:cd16143  238 NgpspyadykELEKFGHDPSG-PLRGMK------ADIyeggHRVPFIVRWPGKipAGSVSDQLVSLTDLFATLAAIVGQK 310
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
447-553 2.61e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 40.05  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 447 YLD----EALEEYInDLKKKGLYDNSVIMIYGDHyGISenhnnameklLGEKITPAKFTDL---NRTGFWIKIPGKS--- 516
Cdd:cd16153  176 YGDaqvgRAVEAFK-AYSLKQDRDYTIVYVTGDH-GWH----------LGEQGILAKFTFWpqsHRVPLIVVSSDKLkap 243
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 926120082 517 -GGINNEYAGQVDVMPTILHLAGIDTKNY-LMFGTDLFS 553
Cdd:cd16153  244 aGKVRHDFVEFVDLAPTLLAAAGVDVDAPdYLDGRDLFE 282
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
439-541 4.39e-03

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: 39.87  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 439 DGYIQTAR--------YLDEALEEYINDLKKKGLYDNSVIMIYGDHyGisenhnnameKLLGE-----KITPakFTDLNR 505
Cdd:cd16032  156 DLYVRRARrayygmvsYVDDKVGQLLDTLERTGLADDTIVIFTSDH-G----------DMLGErglwyKMSF--FEGSAR 222
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 926120082 506 TGFWIKIPGK-SGGINNEYAGQVDVMPTILHLAGIDT 541
Cdd:cd16032  223 VPLIISAPGRfAPRRVAEPVSLVDLLPTLVDLAGGGT 259
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
416-540 4.51e-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: 39.45  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 416 HYPFTLDEKDatieksntgdatVDGYIQTAR--------YLDEALEEYINDLKKKGLYDNSVImIYG-DHygiSENhnna 486
Cdd:cd16037  143 HFPLIAPQEF------------YDLYVRRARaayyglveFLDENIGRVLDALEELGLLDNTLI-IYTsDH---GDM---- 202
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926120082 487 meklLGEKitpakftdlnrtGFW---------------IKIPG-KSGGINNEYAGQVDVMPTILHLAGID 540
Cdd:cd16037  203 ----LGER------------GLWgkstmyeesvrvpmiISGPGiPAGKRVKTPVSLVDLAPTILEAAGAP 256
ALP_like cd16021
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ...
441-476 6.64e-03

uncharacterized Alkaline phosphatase subfamily; 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.


Pssm-ID: 293745  Cd Length: 278  Bit Score: 39.04  E-value: 6.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 926120082 441 YIQTARYLDEALEEYINDLKKKGLYDNSVIMIYGDH 476
Cdd:cd16021  178 YLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDH 213
 
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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